HEADER MEMBRANE PROTEIN 16-MAY-22 8CU7 TITLE CRYSTAL STRUCTURE OF A2AAR-STAR2-BRIL IN COMPLEX WITH A NOVEL A2A TITLE 2 ANTAGONIST, LJ-4517 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, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, A2A ADENOSINE RECEPTOR, LCP, S277A MUTANT, NUCLEOSIDE, KEYWDS 2 ANTAGONIST, MOLECULAR DYNAMICS, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.SHIRIAEVA,D.-J.PARK,G.KIM,Y.LEE,X.HOU,D.B.JARHAD,G.KIM,J.YU, AUTHOR 2 Y.E.HYUN,W.KIM,Z.-G.GAO,K.A.JACOBSON,G.W.HAN,R.C.STEVENS,L.S.JEONG, AUTHOR 3 S.CHOI,V.CHEREZOV REVDAT 2 21-SEP-22 8CU7 1 JRNL REVDAT 1 31-AUG-22 8CU7 0 JRNL AUTH A.SHIRIAEVA,D.PARK,G.KIM,Y.LEE,X.HOU,D.B.JARHAD,G.KIM,J.YU, JRNL AUTH 2 Y.E.HYUN,W.KIM,Z.G.GAO,K.A.JACOBSON,G.W.HAN,R.C.STEVENS, JRNL AUTH 3 L.S.JEONG,S.CHOI,V.CHEREZOV JRNL TITL GPCR AGONIST-TO-ANTAGONIST CONVERSION: ENABLING THE DESIGN JRNL TITL 2 OF NUCLEOSIDE FUNCTIONAL SWITCHES FOR THE A 2A ADENOSINE JRNL TITL 3 RECEPTOR. JRNL REF J.MED.CHEM. V. 65 11648 2022 JRNL REFN ISSN 0022-2623 JRNL PMID 35977382 JRNL DOI 10.1021/ACS.JMEDCHEM.2C00462 REMARK 2 REMARK 2 RESOLUTION. 2.05 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 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) : 2.05 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.89 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 87.3 REMARK 3 NUMBER OF REFLECTIONS : 28215 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.179 REMARK 3 R VALUE (WORKING SET) : 0.177 REMARK 3 FREE R VALUE : 0.211 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 1445 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 44.8900 - 4.4100 0.99 3234 168 0.1890 0.1964 REMARK 3 2 4.4000 - 3.5000 1.00 3111 178 0.1567 0.2089 REMARK 3 3 3.5000 - 3.0500 1.00 3035 168 0.1725 0.2047 REMARK 3 4 3.0500 - 2.7800 0.99 3035 153 0.1687 0.2048 REMARK 3 5 2.7800 - 2.5800 0.97 2954 156 0.1664 0.2137 REMARK 3 6 2.5800 - 2.4200 0.93 2814 168 0.1679 0.2027 REMARK 3 7 2.4200 - 2.3000 0.91 2739 147 0.1832 0.2161 REMARK 3 8 2.3000 - 2.2000 0.85 2589 137 0.2046 0.2509 REMARK 3 9 2.2000 - 2.1200 0.70 2132 116 0.2223 0.2523 REMARK 3 10 2.1200 - 2.0500 0.37 1127 54 0.2552 0.2975 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 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) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 20.560 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.27 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID -3 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): -23.7803 -5.0201 20.8540 REMARK 3 T TENSOR REMARK 3 T11: 0.1079 T22: 0.1329 REMARK 3 T33: 0.0938 T12: -0.0105 REMARK 3 T13: -0.0124 T23: 0.0199 REMARK 3 L TENSOR REMARK 3 L11: 0.4411 L22: 0.6448 REMARK 3 L33: 0.8872 L12: 0.0121 REMARK 3 L13: 0.0043 L23: 0.3808 REMARK 3 S TENSOR REMARK 3 S11: -0.0214 S12: -0.0907 S13: -0.0108 REMARK 3 S21: -0.0022 S22: 0.0379 S23: -0.0384 REMARK 3 S31: 0.0794 S32: -0.1609 S33: -0.0503 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.0371 -54.4855 19.9117 REMARK 3 T TENSOR REMARK 3 T11: 0.3545 T22: 0.2097 REMARK 3 T33: 0.7008 T12: 0.1078 REMARK 3 T13: -0.0709 T23: -0.0308 REMARK 3 L TENSOR REMARK 3 L11: 0.1937 L22: 0.1720 REMARK 3 L33: 0.1885 L12: -0.0610 REMARK 3 L13: -0.1066 L23: -0.1369 REMARK 3 S TENSOR REMARK 3 S11: 0.1805 S12: -0.2170 S13: 0.3488 REMARK 3 S21: -0.3107 S22: -0.0735 S23: -0.1371 REMARK 3 S31: 0.1018 S32: 0.0547 S33: 0.2461 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 308 ) REMARK 3 ORIGIN FOR THE GROUP (A): -18.1815 -10.9122 10.7377 REMARK 3 T TENSOR REMARK 3 T11: 0.1550 T22: 0.1458 REMARK 3 T33: 0.1218 T12: 0.0004 REMARK 3 T13: -0.0076 T23: -0.0032 REMARK 3 L TENSOR REMARK 3 L11: 0.2287 L22: 0.4191 REMARK 3 L33: 0.6256 L12: -0.0237 REMARK 3 L13: 0.1451 L23: -0.1750 REMARK 3 S TENSOR REMARK 3 S11: -0.0486 S12: 0.0641 S13: -0.0602 REMARK 3 S21: -0.2679 S22: 0.0919 S23: -0.1169 REMARK 3 S31: 0.1163 S32: 0.0346 S33: -0.0073 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 8CU7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-22. REMARK 100 THE DEPOSITION ID IS D_1000265463. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 06-DEC-18 REMARK 200 TEMPERATURE (KELVIN) : 123 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 28215 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.050 REMARK 200 RESOLUTION RANGE LOW (A) : 44.900 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 92.6 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : 0.15000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 12.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.11 REMARK 200 COMPLETENESS FOR SHELL (%) : 64.4 REMARK 200 DATA REDUNDANCY IN SHELL : 1.60 REMARK 200 R MERGE FOR SHELL (I) : 0.41700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: PDB ENTRY 4EIY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.03 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES, PH 5.3, 0.05 M SODIUM REMARK 280 THIOCYANATE, 30% PEG400, 2% 2,2,2-TRIFLUOROETHANOL, LIPIDIC REMARK 280 CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.43650 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 70.43650 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 19.72800 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.79000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.72800 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.79000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.43650 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.72800 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.79000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.43650 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.72800 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.79000 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 300 REMARK: THE AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN. 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 14630 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21190 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 77.0 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 MET A -24 REMARK 465 LYS A -23 REMARK 465 THR A -22 REMARK 465 ILE A -21 REMARK 465 ILE A -20 REMARK 465 ALA A -19 REMARK 465 LEU A -18 REMARK 465 SER A -17 REMARK 465 TYR A -16 REMARK 465 ILE A -15 REMARK 465 PHE A -14 REMARK 465 CYS A -13 REMARK 465 LEU A -12 REMARK 465 VAL A -11 REMARK 465 PHE A -10 REMARK 465 ALA A -9 REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 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 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 HIS A 317 REMARK 465 HIS 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 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 LYS A1042 CG CD CE NZ REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 1393 O HOH A 1412 2.09 REMARK 500 O HOH A 1436 O HOH A 1452 2.18 REMARK 500 OD1 ASP A 1074 O HOH A 1301 2.19 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -51.03 -122.28 REMARK 500 TYR A1101 -58.83 -136.82 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 1205 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 1220 REMARK 610 OLA A 1221 REMARK 610 OLC A 1222 REMARK 610 OLC A 1223 REMARK 610 OLA A 1224 REMARK 610 OLA A 1225 REMARK 610 OLA A 1226 REMARK 610 OLA A 1227 REMARK 610 OLA A 1228 REMARK 610 OLA A 1229 REMARK 610 OLA A 1230 REMARK 610 OLA A 1232 REMARK 610 OLA A 1233 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A1203 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 126.6 REMARK 620 3 HOH A1318 O 64.9 69.4 REMARK 620 4 HOH A1350 O 101.6 122.6 166.5 REMARK 620 5 HOH A1387 O 90.4 66.6 94.2 86.2 REMARK 620 6 HOH A1393 O 81.5 120.6 85.0 92.7 171.4 REMARK 620 N 1 2 3 4 5 DBREF 8CU7 A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 8CU7 A 1001 1105 UNP P0ABE7 C562_ECOLX 23 127 DBREF 8CU7 A 219 316 UNP P29274 AA2AR_HUMAN 219 316 SEQADV 8CU7 MET A -24 UNP P29274 EXPRESSION TAG SEQADV 8CU7 LYS A -23 UNP P29274 EXPRESSION TAG SEQADV 8CU7 THR A -22 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ILE A -21 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ILE A -20 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ALA A -19 UNP P29274 EXPRESSION TAG SEQADV 8CU7 LEU A -18 UNP P29274 EXPRESSION TAG SEQADV 8CU7 SER A -17 UNP P29274 EXPRESSION TAG SEQADV 8CU7 TYR A -16 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ILE A -15 UNP P29274 EXPRESSION TAG SEQADV 8CU7 PHE A -14 UNP P29274 EXPRESSION TAG SEQADV 8CU7 CYS A -13 UNP P29274 EXPRESSION TAG SEQADV 8CU7 LEU A -12 UNP P29274 EXPRESSION TAG SEQADV 8CU7 VAL A -11 UNP P29274 EXPRESSION TAG SEQADV 8CU7 PHE A -10 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 8CU7 TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 8CU7 LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 8CU7 GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 8CU7 ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 8CU7 PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 8CU7 LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 8CU7 ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 8CU7 ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 8CU7 ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 8CU7 ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 8CU7 ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 8CU7 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 8CU7 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 8CU7 LEU A 1106 UNP P0ABE7 ENGINEERED MUTATION SEQADV 8CU7 ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 8CU7 ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 8CU7 ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 8CU7 HIS A 317 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 318 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 8CU7 HIS A 326 UNP P29274 EXPRESSION TAG SEQRES 1 A 447 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 447 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO SEQRES 3 A 447 PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU LEU SEQRES 4 A 447 ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL SEQRES 5 A 447 CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL SEQRES 6 A 447 THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE SEQRES 7 A 447 LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SEQRES 8 A 447 SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE SEQRES 9 A 447 ILE ALA CYS PHE VAL LEU VAL LEU ALA GLN SER SER ILE SEQRES 10 A 447 PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA SEQRES 11 A 447 ILE ALA ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY SEQRES 12 A 447 THR ARG ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SEQRES 13 A 447 SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN SEQRES 14 A 447 ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SER GLN SEQRES 15 A 447 GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP SEQRES 16 A 447 VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE SEQRES 17 A 447 ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL SEQRES 18 A 447 TYR LEU ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA SEQRES 19 A 447 ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU SEQRES 20 A 447 LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS SEQRES 21 A 447 ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA SEQRES 22 A 447 GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO SEQRES 23 A 447 ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP SEQRES 24 A 447 ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA SEQRES 25 A 447 ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU SEQRES 26 A 447 GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR SEQRES 27 A 447 LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS SEQRES 28 A 447 ALA ALA LYS SER ALA ALA ILE ILE ALA GLY LEU PHE ALA SEQRES 29 A 447 LEU CYS TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR SEQRES 30 A 447 PHE PHE CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU SEQRES 31 A 447 MET TYR LEU ALA ILE VAL LEU ALA HIS THR ASN SER VAL SEQRES 32 A 447 VAL ASN PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE SEQRES 33 A 447 ARG GLN THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU SEQRES 34 A 447 ARG GLN GLN GLU PRO PHE LYS ALA HIS HIS HIS HIS HIS SEQRES 35 A 447 HIS HIS HIS HIS HIS HET PEG A1201 7 HET LJX A1202 28 HET NA A1203 1 HET OLC A1204 25 HET OLA A1205 18 HET OLC A1206 25 HET OLA A1207 20 HET OLA A1208 20 HET CLR A1209 28 HET CLR A1210 28 HET CLR A1211 28 HET OLA A1212 20 HET OLA A1213 14 HET OLA A1214 9 HET OLA A1215 17 HET OLA A1216 12 HET OLA A1217 15 HET OLA A1218 11 HET OLA A1219 11 HET OLA A1220 12 HET OLA A1221 15 HET OLC A1222 15 HET OLC A1223 10 HET OLA A1224 19 HET OLA A1225 15 HET OLA A1226 11 HET OLA A1227 10 HET OLA A1228 13 HET OLA A1229 9 HET OLA A1230 7 HET OLA A1231 20 HET OLA A1232 13 HET OLA A1233 18 HET ETF A1234 6 HET PEG A1235 7 HET PEG A1236 7 HET PEG A1237 7 HET OLC A1238 25 HET OLC A1239 25 HET OLC A1240 25 HETNAM PEG DI(HYDROXYETHYL)ETHER HETNAM LJX (2R,3R,4R)-2-[(8P)-6-AMINO-2-(HEX-1-YN-1-YL)-8- HETNAM 2 LJX (THIOPHEN-2-YL)-9H-PURIN-9-YL]OXOLANE-3,4-DIOL HETNAM NA SODIUM ION HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETNAM CLR CHOLESTEROL HETNAM ETF TRIFLUOROETHANOL HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 PEG 4(C4 H10 O3) FORMUL 3 LJX C19 H21 N5 O3 S FORMUL 4 NA NA 1+ FORMUL 5 OLC 7(C21 H40 O4) FORMUL 6 OLA 23(C18 H34 O2) FORMUL 10 CLR 3(C27 H46 O) FORMUL 35 ETF C2 H3 F3 O FORMUL 42 HOH *177(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 THR A 68 1 11 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ARG A 111 VAL A 116 1 6 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLN A 157 1 8 HELIX 10 AB1 LEU A 167 VAL A 172 1 6 HELIX 11 AB2 PRO A 173 PHE A 180 1 8 HELIX 12 AB3 VAL A 186 LYS A 1019 1 42 HELIX 13 AB4 ASN A 1022 GLN A 1041 1 20 HELIX 14 AB5 PRO A 1056 GLU A 1081 1 26 HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11 HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9 HELIX 17 AB8 TYR A 1101 CYS A 259 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 VAL A 307 1 16 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 A1203 1555 1555 2.50 LINK OG SER A 91 NA NA A1203 1555 1555 2.53 LINK NA NA A1203 O HOH A1318 1555 1555 2.27 LINK NA NA A1203 O HOH A1350 1555 1555 2.63 LINK NA NA A1203 O HOH A1387 1555 1555 2.63 LINK NA NA A1203 O HOH A1393 1555 1555 2.16 CRYST1 39.456 179.580 140.873 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 0.025345 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005569 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007099 0.00000 ATOM 1 N ASP A -3 -22.288 28.593 4.282 1.00103.45 N ANISOU 1 N ASP A -3 15056 11614 12638 442 30 302 N ATOM 2 CA ASP A -3 -22.793 27.462 3.454 1.00104.71 C ANISOU 2 CA ASP A -3 15195 11839 12753 454 5 332 C ATOM 3 C ASP A -3 -21.995 27.322 2.160 1.00105.71 C ANISOU 3 C ASP A -3 15393 11933 12837 364 67 357 C ATOM 4 O ASP A -3 -22.448 27.730 1.090 1.00103.76 O ANISOU 4 O ASP A -3 15237 11662 12526 391 45 389 O ATOM 5 CB ASP A -3 -24.278 27.653 3.136 1.00104.15 C ANISOU 5 CB ASP A -3 15141 11799 12631 576 -89 352 C ATOM 6 CG ASP A -3 -24.798 26.632 2.142 1.00102.28 C ANISOU 6 CG ASP A -3 14896 11624 12343 584 -116 381 C ATOM 7 OD1 ASP A -3 -24.755 25.422 2.451 1.00104.86 O ANISOU 7 OD1 ASP A -3 15132 12020 12691 563 -113 375 O ATOM 8 OD2 ASP A -3 -25.254 27.039 1.052 1.00 90.74 O ANISOU 8 OD2 ASP A -3 13519 10139 10818 612 -141 410 O ATOM 9 N ASP A -2 -20.794 26.753 2.271 1.00106.13 N ANISOU 9 N ASP A -2 15404 11990 12930 258 144 337 N ATOM 10 CA ASP A -2 -19.985 26.406 1.112 1.00101.18 C ANISOU 10 CA ASP A -2 14821 11352 12269 169 208 352 C ATOM 11 C ASP A -2 -19.915 24.906 0.868 1.00 96.31 C ANISOU 11 C ASP A -2 14127 10812 11653 140 215 353 C ATOM 12 O ASP A -2 -19.355 24.487 -0.151 1.00 87.44 O ANISOU 12 O ASP A -2 13035 9691 10498 75 262 363 O ATOM 13 CB ASP A -2 -18.562 26.963 1.269 1.00108.73 C ANISOU 13 CB ASP A -2 15789 12257 13266 63 299 323 C ATOM 14 CG ASP A -2 -18.515 28.476 1.174 1.00120.03 C ANISOU 14 CG ASP A -2 17323 13602 14681 74 304 329 C ATOM 15 OD1 ASP A -2 -19.290 29.047 0.377 1.00110.92 O ANISOU 15 OD1 ASP A -2 16266 12417 13461 133 262 365 O ATOM 16 OD2 ASP A -2 -17.705 29.095 1.896 1.00132.68 O ANISOU 16 OD2 ASP A -2 18909 15167 16336 25 348 296 O ATOM 17 N GLY A -1 -20.464 24.091 1.771 1.00 96.83 N ANISOU 17 N GLY A -1 14097 10940 11755 186 171 341 N ATOM 18 CA GLY A -1 -20.546 22.663 1.575 1.00 85.16 C ANISOU 18 CA GLY A -1 12550 9534 10274 168 168 346 C ATOM 19 C GLY A -1 -21.932 22.243 1.119 1.00 75.29 C ANISOU 19 C GLY A -1 11304 8334 8969 260 83 378 C ATOM 20 O GLY A -1 -22.905 22.980 1.266 1.00 77.67 O ANISOU 20 O GLY A -1 11634 8628 9248 351 17 387 O ATOM 21 N ALA A 0 -22.009 21.038 0.562 1.00 62.36 N ANISOU 21 N ALA A 0 9630 6753 7310 236 83 389 N ATOM 22 CA ALA A 0 -23.268 20.554 0.020 1.00 58.86 C ANISOU 22 CA ALA A 0 9183 6368 6812 312 4 415 C ATOM 23 C ALA A 0 -24.342 20.538 1.108 1.00 59.28 C ANISOU 23 C ALA A 0 9164 6471 6887 410 -74 407 C ATOM 24 O ALA A 0 -24.032 20.403 2.296 1.00 56.21 O ANISOU 24 O ALA A 0 8710 6090 6558 406 -62 382 O ATOM 25 CB ALA A 0 -23.094 19.152 -0.562 1.00 56.61 C ANISOU 25 CB ALA A 0 8855 6142 6512 261 21 421 C ATOM 26 N PRO A 1 -25.612 20.680 0.734 1.00 58.97 N ANISOU 26 N PRO A 1 9131 6472 6803 501 -155 421 N ATOM 27 CA PRO A 1 -26.694 20.584 1.724 1.00 52.59 C ANISOU 27 CA PRO A 1 8237 5731 6013 596 -230 406 C ATOM 28 C PRO A 1 -26.603 19.282 2.501 1.00 45.27 C ANISOU 28 C PRO A 1 7200 4879 5120 572 -227 395 C ATOM 29 O PRO A 1 -26.424 18.210 1.905 1.00 40.53 O ANISOU 29 O PRO A 1 6577 4320 4501 519 -211 406 O ATOM 30 CB PRO A 1 -27.966 20.636 0.865 1.00 51.40 C ANISOU 30 CB PRO A 1 8098 5628 5802 673 -307 420 C ATOM 31 CG PRO A 1 -27.559 21.372 -0.363 1.00 50.31 C ANISOU 31 CG PRO A 1 8086 5410 5618 642 -278 443 C ATOM 32 CD PRO A 1 -26.124 20.999 -0.612 1.00 50.84 C ANISOU 32 CD PRO A 1 8183 5431 5704 523 -182 446 C ATOM 33 N PRO A 2 -26.718 19.328 3.833 1.00 44.72 N ANISOU 33 N PRO A 2 7033 4849 5108 597 -236 358 N ATOM 34 CA PRO A 2 -26.538 18.096 4.621 1.00 40.53 C ANISOU 34 CA PRO A 2 6357 4417 4625 547 -219 325 C ATOM 35 C PRO A 2 -27.470 16.963 4.227 1.00 37.17 C ANISOU 35 C PRO A 2 5859 4096 4167 564 -267 332 C ATOM 36 O PRO A 2 -27.097 15.793 4.379 1.00 33.49 O ANISOU 36 O PRO A 2 5314 3687 3724 498 -239 320 O ATOM 37 CB PRO A 2 -26.802 18.562 6.059 1.00 41.80 C ANISOU 37 CB PRO A 2 6439 4607 4838 594 -237 286 C ATOM 38 CG PRO A 2 -26.493 20.011 6.052 1.00 45.74 C ANISOU 38 CG PRO A 2 7048 4994 5336 624 -227 291 C ATOM 39 CD PRO A 2 -26.897 20.508 4.698 1.00 47.95 C ANISOU 39 CD PRO A 2 7460 5213 5545 660 -254 338 C ATOM 40 N ILE A 3 -28.673 17.265 3.734 1.00 30.86 N ANISOU 40 N ILE A 3 5083 3324 3316 652 -342 347 N ATOM 41 CA ILE A 3 -29.621 16.197 3.425 1.00 36.36 C ANISOU 41 CA ILE A 3 5701 4128 3986 666 -391 346 C ATOM 42 C ILE A 3 -29.080 15.291 2.328 1.00 34.19 C ANISOU 42 C ILE A 3 5465 3847 3680 587 -356 369 C ATOM 43 O ILE A 3 -29.437 14.108 2.258 1.00 32.35 O ANISOU 43 O ILE A 3 5149 3699 3445 558 -368 359 O ATOM 44 CB ILE A 3 -30.991 16.786 3.034 1.00 37.92 C ANISOU 44 CB ILE A 3 5921 4355 4133 780 -481 354 C ATOM 45 CG1 ILE A 3 -32.061 15.691 3.072 1.00 47.61 C ANISOU 45 CG1 ILE A 3 7029 5713 5348 795 -533 335 C ATOM 46 CG2 ILE A 3 -30.925 17.404 1.648 1.00 41.98 C ANISOU 46 CG2 ILE A 3 6560 4797 4595 781 -482 384 C ATOM 47 CD1 ILE A 3 -33.459 16.181 2.755 1.00 56.43 C ANISOU 47 CD1 ILE A 3 8121 6882 6437 889 -611 321 C ATOM 48 N MET A 4 -28.225 15.821 1.451 1.00 31.32 N ANISOU 48 N MET A 4 5229 3383 3290 549 -311 398 N ATOM 49 CA MET A 4 -27.681 15.005 0.371 1.00 28.82 C ANISOU 49 CA MET A 4 4954 3058 2940 474 -273 416 C ATOM 50 C MET A 4 -26.782 13.905 0.921 1.00 29.15 C ANISOU 50 C MET A 4 4903 3133 3039 382 -210 389 C ATOM 51 O MET A 4 -26.973 12.721 0.614 1.00 25.05 O ANISOU 51 O MET A 4 4327 2680 2511 347 -215 383 O ATOM 52 CB MET A 4 -26.921 15.887 -0.617 1.00 30.52 C ANISOU 52 CB MET A 4 5313 3162 3121 444 -227 443 C ATOM 53 CG MET A 4 -27.810 16.872 -1.361 1.00 32.81 C ANISOU 53 CG MET A 4 5665 3435 3365 518 -283 453 C ATOM 54 SD MET A 4 -26.926 17.840 -2.598 1.00 37.87 S ANISOU 54 SD MET A 4 6453 3965 3971 467 -222 472 S ATOM 55 CE MET A 4 -26.493 16.570 -3.784 1.00 28.99 C ANISOU 55 CE MET A 4 5334 2872 2808 384 -185 480 C ATOM 56 N GLY A 5 -25.799 14.276 1.745 1.00 29.71 N ANISOU 56 N GLY A 5 4958 3159 3170 343 -153 369 N ATOM 57 CA GLY A 5 -24.962 13.270 2.375 1.00 28.64 C ANISOU 57 CA GLY A 5 4732 3059 3093 267 -101 339 C ATOM 58 C GLY A 5 -25.736 12.399 3.345 1.00 30.81 C ANISOU 58 C GLY A 5 4872 3439 3397 292 -144 316 C ATOM 59 O GLY A 5 -25.466 11.201 3.469 1.00 23.57 O ANISOU 59 O GLY A 5 3887 2571 2500 240 -125 302 O ATOM 60 N SER A 6 -26.708 12.988 4.047 1.00 24.19 N ANISOU 60 N SER A 6 3998 2635 2559 371 -201 308 N ATOM 61 CA SER A 6 -27.557 12.197 4.933 1.00 28.45 C ANISOU 61 CA SER A 6 4413 3279 3118 394 -241 286 C ATOM 62 C SER A 6 -28.330 11.142 4.154 1.00 23.53 C ANISOU 62 C SER A 6 3764 2725 2453 386 -276 296 C ATOM 63 O SER A 6 -28.518 10.020 4.635 1.00 20.84 O ANISOU 63 O SER A 6 3330 2455 2132 352 -276 279 O ATOM 64 CB SER A 6 -28.524 13.108 5.692 1.00 28.34 C ANISOU 64 CB SER A 6 4372 3290 3105 485 -295 274 C ATOM 65 OG SER A 6 -27.829 13.986 6.561 1.00 40.35 O ANISOU 65 OG SER A 6 5906 4756 4670 489 -264 257 O ATOM 66 N SER A 7 -28.792 11.485 2.948 1.00 21.90 N ANISOU 66 N SER A 7 3642 2495 2185 415 -307 322 N ATOM 67 CA SER A 7 -29.579 10.541 2.161 1.00 24.76 C ANISOU 67 CA SER A 7 3982 2924 2503 411 -346 328 C ATOM 68 C SER A 7 -28.764 9.305 1.802 1.00 18.98 C ANISOU 68 C SER A 7 3233 2194 1783 317 -293 325 C ATOM 69 O SER A 7 -29.282 8.183 1.824 1.00 18.81 O ANISOU 69 O SER A 7 3140 2248 1760 293 -311 312 O ATOM 70 CB SER A 7 -30.100 11.221 0.895 1.00 26.03 C ANISOU 70 CB SER A 7 4249 3050 2590 461 -389 357 C ATOM 71 OG SER A 7 -30.994 12.273 1.216 1.00 39.35 O ANISOU 71 OG SER A 7 5944 4743 4265 560 -449 357 O ATOM 72 N VAL A 8 -27.489 9.492 1.459 1.00 16.31 N ANISOU 72 N VAL A 8 2964 1775 1459 261 -225 333 N ATOM 73 CA VAL A 8 -26.633 8.355 1.137 1.00 19.11 C ANISOU 73 CA VAL A 8 3303 2128 1829 177 -171 324 C ATOM 74 C VAL A 8 -26.404 7.501 2.377 1.00 20.16 C ANISOU 74 C VAL A 8 3322 2312 2026 148 -156 296 C ATOM 75 O VAL A 8 -26.535 6.273 2.340 1.00 17.60 O ANISOU 75 O VAL A 8 2943 2037 1707 110 -156 286 O ATOM 76 CB VAL A 8 -25.305 8.843 0.532 1.00 19.82 C ANISOU 76 CB VAL A 8 3487 2124 1922 127 -99 333 C ATOM 77 CG1 VAL A 8 -24.356 7.674 0.315 1.00 24.84 C ANISOU 77 CG1 VAL A 8 4094 2761 2582 45 -41 316 C ATOM 78 CG2 VAL A 8 -25.558 9.577 -0.773 1.00 23.44 C ANISOU 78 CG2 VAL A 8 4069 2531 2305 149 -112 366 C ATOM 79 N TYR A 9 -26.060 8.140 3.496 1.00 19.82 N ANISOU 79 N TYR A 9 3246 2254 2031 166 -143 282 N ATOM 80 CA TYR A 9 -25.850 7.403 4.737 1.00 16.50 C ANISOU 80 CA TYR A 9 2724 1879 1666 144 -132 257 C ATOM 81 C TYR A 9 -27.107 6.640 5.137 1.00 15.00 C ANISOU 81 C TYR A 9 2451 1784 1462 167 -186 252 C ATOM 82 O TYR A 9 -27.050 5.446 5.453 1.00 14.49 O ANISOU 82 O TYR A 9 2328 1763 1417 124 -177 241 O ATOM 83 CB TYR A 9 -25.424 8.369 5.845 1.00 21.63 C ANISOU 83 CB TYR A 9 3358 2501 2359 170 -119 242 C ATOM 84 CG TYR A 9 -25.566 7.810 7.245 1.00 18.89 C ANISOU 84 CG TYR A 9 2907 2215 2054 170 -127 219 C ATOM 85 CD1 TYR A 9 -24.701 6.833 7.715 1.00 19.34 C ANISOU 85 CD1 TYR A 9 2919 2277 2151 114 -90 204 C ATOM 86 CD2 TYR A 9 -26.561 8.269 8.098 1.00 17.86 C ANISOU 86 CD2 TYR A 9 2728 2137 1923 230 -172 211 C ATOM 87 CE1 TYR A 9 -24.828 6.321 8.992 1.00 17.50 C ANISOU 87 CE1 TYR A 9 2603 2097 1950 116 -99 187 C ATOM 88 CE2 TYR A 9 -26.696 7.763 9.377 1.00 16.25 C ANISOU 88 CE2 TYR A 9 2435 1989 1750 227 -176 191 C ATOM 89 CZ TYR A 9 -25.826 6.792 9.819 1.00 18.46 C ANISOU 89 CZ TYR A 9 2680 2270 2065 169 -140 182 C ATOM 90 OH TYR A 9 -25.956 6.284 11.091 1.00 22.57 O ANISOU 90 OH TYR A 9 3123 2843 2610 167 -145 166 O ATOM 91 N ILE A 10 -28.258 7.313 5.113 1.00 16.14 N ANISOU 91 N ILE A 10 2593 1963 1575 235 -243 257 N ATOM 92 CA ILE A 10 -29.498 6.673 5.540 1.00 15.00 C ANISOU 92 CA ILE A 10 2363 1917 1421 257 -292 245 C ATOM 93 C ILE A 10 -29.866 5.529 4.604 1.00 16.79 C ANISOU 93 C ILE A 10 2587 2179 1614 215 -303 250 C ATOM 94 O ILE A 10 -30.304 4.462 5.051 1.00 13.41 O ANISOU 94 O ILE A 10 2082 1816 1197 183 -310 236 O ATOM 95 CB ILE A 10 -30.627 7.716 5.635 1.00 18.15 C ANISOU 95 CB ILE A 10 2759 2345 1793 345 -351 243 C ATOM 96 CG1 ILE A 10 -30.356 8.680 6.796 1.00 22.23 C ANISOU 96 CG1 ILE A 10 3259 2840 2349 384 -340 229 C ATOM 97 CG2 ILE A 10 -31.974 7.022 5.803 1.00 21.98 C ANISOU 97 CG2 ILE A 10 3156 2937 2258 363 -402 227 C ATOM 98 CD1 ILE A 10 -31.304 9.870 6.849 1.00 26.03 C ANISOU 98 CD1 ILE A 10 3753 3330 2806 479 -393 226 C ATOM 99 N THR A 11 -29.709 5.728 3.293 1.00 15.57 N ANISOU 99 N THR A 11 2519 1981 1415 212 -305 268 N ATOM 100 CA THR A 11 -30.045 4.664 2.352 1.00 15.96 C ANISOU 100 CA THR A 11 2572 2063 1430 172 -317 269 C ATOM 101 C THR A 11 -29.173 3.435 2.585 1.00 13.56 C ANISOU 101 C THR A 11 2239 1751 1163 92 -264 259 C ATOM 102 O THR A 11 -29.662 2.300 2.547 1.00 15.15 O ANISOU 102 O THR A 11 2390 2007 1361 56 -277 248 O ATOM 103 CB THR A 11 -29.902 5.164 0.912 1.00 18.28 C ANISOU 103 CB THR A 11 2975 2304 1665 182 -322 292 C ATOM 104 OG1 THR A 11 -30.798 6.259 0.692 1.00 19.10 O ANISOU 104 OG1 THR A 11 3109 2417 1732 266 -381 302 O ATOM 105 CG2 THR A 11 -30.225 4.055 -0.080 1.00 21.93 C ANISOU 105 CG2 THR A 11 3443 2801 2090 139 -335 289 C ATOM 106 N VAL A 12 -27.879 3.642 2.837 1.00 14.82 N ANISOU 106 N VAL A 12 2429 1842 1361 62 -205 260 N ATOM 107 CA VAL A 12 -26.984 2.518 3.094 1.00 14.91 C ANISOU 107 CA VAL A 12 2413 1842 1411 -4 -158 247 C ATOM 108 C VAL A 12 -27.355 1.824 4.399 1.00 13.03 C ANISOU 108 C VAL A 12 2078 1661 1210 -10 -170 232 C ATOM 109 O VAL A 12 -27.350 0.590 4.482 1.00 14.04 O ANISOU 109 O VAL A 12 2171 1814 1348 -56 -162 224 O ATOM 110 CB VAL A 12 -25.521 2.997 3.102 1.00 17.75 C ANISOU 110 CB VAL A 12 2820 2122 1804 -28 -96 244 C ATOM 111 CG1 VAL A 12 -24.597 1.887 3.584 1.00 18.12 C ANISOU 111 CG1 VAL A 12 2824 2162 1898 -82 -54 225 C ATOM 112 CG2 VAL A 12 -25.112 3.469 1.715 1.00 19.80 C ANISOU 112 CG2 VAL A 12 3180 2324 2019 -39 -74 259 C ATOM 113 N GLU A 13 -27.672 2.600 5.439 1.00 12.73 N ANISOU 113 N GLU A 13 2002 1644 1193 35 -186 229 N ATOM 114 CA GLU A 13 -28.078 2.006 6.709 1.00 12.56 C ANISOU 114 CA GLU A 13 1893 1681 1200 30 -196 216 C ATOM 115 C GLU A 13 -29.313 1.132 6.536 1.00 12.45 C ANISOU 115 C GLU A 13 1831 1745 1156 18 -234 213 C ATOM 116 O GLU A 13 -29.399 0.043 7.116 1.00 12.06 O ANISOU 116 O GLU A 13 1732 1728 1124 -25 -226 206 O ATOM 117 CB GLU A 13 -28.353 3.100 7.739 1.00 13.88 C ANISOU 117 CB GLU A 13 2031 1861 1383 86 -210 210 C ATOM 118 CG GLU A 13 -27.115 3.805 8.270 1.00 15.91 C ANISOU 118 CG GLU A 13 2314 2050 1679 87 -170 205 C ATOM 119 CD GLU A 13 -26.473 3.064 9.426 1.00 18.30 C ANISOU 119 CD GLU A 13 2562 2364 2026 55 -145 192 C ATOM 120 OE1 GLU A 13 -26.110 1.882 9.253 1.00 18.56 O ANISOU 120 OE1 GLU A 13 2586 2398 2067 5 -128 193 O ATOM 121 OE2 GLU A 13 -26.341 3.661 10.516 1.00 17.84 O ANISOU 121 OE2 GLU A 13 2474 2312 1992 82 -145 181 O ATOM 122 N LEU A 14 -30.287 1.597 5.751 1.00 13.82 N ANISOU 122 N LEU A 14 2019 1948 1285 55 -278 216 N ATOM 123 CA LEU A 14 -31.507 0.823 5.561 1.00 13.42 C ANISOU 123 CA LEU A 14 1915 1978 1206 43 -318 206 C ATOM 124 C LEU A 14 -31.232 -0.453 4.779 1.00 13.09 C ANISOU 124 C LEU A 14 1893 1926 1154 -26 -301 206 C ATOM 125 O LEU A 14 -31.814 -1.504 5.070 1.00 15.45 O ANISOU 125 O LEU A 14 2138 2279 1455 -68 -308 194 O ATOM 126 CB LEU A 14 -32.561 1.676 4.856 1.00 17.06 C ANISOU 126 CB LEU A 14 2388 2474 1621 107 -375 206 C ATOM 127 CG LEU A 14 -33.097 2.846 5.688 1.00 16.62 C ANISOU 127 CG LEU A 14 2300 2443 1574 181 -400 199 C ATOM 128 CD1 LEU A 14 -34.021 3.722 4.856 1.00 28.63 C ANISOU 128 CD1 LEU A 14 3847 3985 3047 253 -460 199 C ATOM 129 CD2 LEU A 14 -33.810 2.339 6.933 1.00 23.36 C ANISOU 129 CD2 LEU A 14 3048 3378 2449 171 -405 177 C ATOM 130 N ALA A 15 -30.347 -0.383 3.783 1.00 12.81 N ANISOU 130 N ALA A 15 1938 1822 1108 -42 -275 216 N ATOM 131 CA ALA A 15 -29.931 -1.594 3.083 1.00 15.04 C ANISOU 131 CA ALA A 15 2242 2086 1385 -107 -252 212 C ATOM 132 C ALA A 15 -29.292 -2.589 4.043 1.00 15.17 C ANISOU 132 C ALA A 15 2218 2093 1451 -155 -215 204 C ATOM 133 O ALA A 15 -29.566 -3.794 3.978 1.00 14.45 O ANISOU 133 O ALA A 15 2105 2026 1360 -204 -215 196 O ATOM 134 CB ALA A 15 -28.962 -1.237 1.956 1.00 14.13 C ANISOU 134 CB ALA A 15 2220 1897 1253 -114 -220 221 C ATOM 135 N ILE A 16 -28.438 -2.106 4.946 1.00 12.88 N ANISOU 135 N ILE A 16 1923 1768 1204 -140 -185 207 N ATOM 136 CA ILE A 16 -27.805 -3.001 5.910 1.00 13.40 C ANISOU 136 CA ILE A 16 1954 1824 1314 -176 -156 201 C ATOM 137 C ILE A 16 -28.845 -3.586 6.853 1.00 13.47 C ANISOU 137 C ILE A 16 1890 1904 1322 -186 -182 198 C ATOM 138 O ILE A 16 -28.777 -4.766 7.220 1.00 14.28 O ANISOU 138 O ILE A 16 1974 2012 1438 -233 -170 195 O ATOM 139 CB ILE A 16 -26.697 -2.255 6.675 1.00 15.85 C ANISOU 139 CB ILE A 16 2270 2086 1667 -153 -125 201 C ATOM 140 CG1 ILE A 16 -25.559 -1.901 5.718 1.00 16.33 C ANISOU 140 CG1 ILE A 16 2399 2074 1731 -162 -87 199 C ATOM 141 CG2 ILE A 16 -26.178 -3.098 7.836 1.00 15.50 C ANISOU 141 CG2 ILE A 16 2185 2042 1664 -177 -107 195 C ATOM 142 CD1 ILE A 16 -24.613 -0.862 6.258 1.00 19.38 C ANISOU 142 CD1 ILE A 16 2797 2417 2152 -136 -60 195 C ATOM 143 N ALA A 17 -29.830 -2.779 7.254 1.00 15.39 N ANISOU 143 N ALA A 17 2095 2203 1548 -142 -216 197 N ATOM 144 CA ALA A 17 -30.850 -3.260 8.179 1.00 16.31 C ANISOU 144 CA ALA A 17 2139 2396 1663 -154 -235 190 C ATOM 145 C ALA A 17 -31.627 -4.428 7.582 1.00 15.18 C ANISOU 145 C ALA A 17 1980 2292 1495 -208 -249 182 C ATOM 146 O ALA A 17 -31.829 -5.454 8.241 1.00 16.09 O ANISOU 146 O ALA A 17 2063 2430 1621 -257 -237 180 O ATOM 147 CB ALA A 17 -31.796 -2.120 8.555 1.00 11.55 C ANISOU 147 CB ALA A 17 1496 1849 1044 -91 -269 183 C ATOM 148 N AVAL A 18 -32.088 -4.276 6.338 0.50 15.97 N ANISOU 148 N AVAL A 18 2108 2401 1559 -201 -275 178 N ATOM 149 N BVAL A 18 -32.060 -4.300 6.325 0.50 15.95 N ANISOU 149 N BVAL A 18 2107 2397 1557 -202 -274 178 N ATOM 150 CA AVAL A 18 -32.831 -5.348 5.679 0.50 17.17 C ANISOU 150 CA AVAL A 18 2247 2590 1685 -254 -292 165 C ATOM 151 CA BVAL A 18 -32.851 -5.367 5.717 0.50 17.16 C ANISOU 151 CA BVAL A 18 2244 2592 1685 -255 -292 165 C ATOM 152 C AVAL A 18 -31.986 -6.613 5.624 0.50 16.75 C ANISOU 152 C AVAL A 18 2227 2484 1655 -320 -253 168 C ATOM 153 C BVAL A 18 -32.011 -6.629 5.547 0.50 16.75 C ANISOU 153 C BVAL A 18 2229 2485 1653 -321 -254 167 C ATOM 154 O AVAL A 18 -32.447 -7.709 5.964 0.50 16.68 O ANISOU 154 O AVAL A 18 2187 2502 1647 -376 -250 160 O ATOM 155 O BVAL A 18 -32.505 -7.747 5.736 0.50 16.86 O ANISOU 155 O BVAL A 18 2215 2525 1665 -378 -254 158 O ATOM 156 CB AVAL A 18 -33.271 -4.912 4.269 0.50 18.54 C ANISOU 156 CB AVAL A 18 2459 2772 1814 -230 -327 160 C ATOM 157 CB BVAL A 18 -33.455 -4.901 4.377 0.50 18.76 C ANISOU 157 CB BVAL A 18 2475 2813 1841 -229 -332 158 C ATOM 158 CG1AVAL A 18 -33.967 -6.060 3.552 0.50 16.85 C ANISOU 158 CG1AVAL A 18 2234 2595 1574 -290 -344 142 C ATOM 159 CG1BVAL A 18 -34.382 -3.715 4.594 0.50 18.36 C ANISOU 159 CG1BVAL A 18 2384 2820 1771 -157 -376 153 C ATOM 160 CG2AVAL A 18 -34.177 -3.691 4.339 0.50 18.00 C ANISOU 160 CG2AVAL A 18 2360 2758 1723 -157 -373 156 C ATOM 161 CG2BVAL A 18 -32.369 -4.544 3.378 0.50 19.68 C ANISOU 161 CG2BVAL A 18 2681 2846 1949 -218 -310 172 C ATOM 162 N LEU A 19 -30.732 -6.476 5.193 1.00 14.70 N ANISOU 162 N LEU A 19 2029 2144 1411 -314 -222 176 N ATOM 163 CA LEU A 19 -29.871 -7.643 5.042 1.00 16.80 C ANISOU 163 CA LEU A 19 2328 2355 1698 -367 -187 174 C ATOM 164 C LEU A 19 -29.587 -8.294 6.390 1.00 17.15 C ANISOU 164 C LEU A 19 2339 2395 1780 -389 -168 180 C ATOM 165 O LEU A 19 -29.534 -9.525 6.491 1.00 16.39 O ANISOU 165 O LEU A 19 2249 2285 1692 -441 -156 176 O ATOM 166 CB LEU A 19 -28.568 -7.240 4.350 1.00 15.83 C ANISOU 166 CB LEU A 19 2271 2155 1587 -352 -155 176 C ATOM 167 CG LEU A 19 -28.685 -6.843 2.875 1.00 16.41 C ANISOU 167 CG LEU A 19 2398 2219 1617 -344 -166 172 C ATOM 168 CD1 LEU A 19 -27.366 -6.275 2.365 1.00 18.24 C ANISOU 168 CD1 LEU A 19 2691 2378 1863 -329 -125 175 C ATOM 169 CD2 LEU A 19 -29.118 -8.029 2.024 1.00 22.79 C ANISOU 169 CD2 LEU A 19 3222 3039 2400 -398 -174 157 C ATOM 170 N ALA A 20 -29.409 -7.486 7.437 1.00 13.93 N ANISOU 170 N ALA A 20 1902 1997 1392 -348 -165 188 N ATOM 171 CA ALA A 20 -29.162 -8.044 8.761 1.00 16.55 C ANISOU 171 CA ALA A 20 2207 2329 1753 -363 -150 195 C ATOM 172 C ALA A 20 -30.353 -8.859 9.244 1.00 17.42 C ANISOU 172 C ALA A 20 2272 2503 1844 -408 -165 194 C ATOM 173 O ALA A 20 -30.184 -9.936 9.826 1.00 16.13 O ANISOU 173 O ALA A 20 2113 2323 1692 -453 -149 200 O ATOM 174 CB ALA A 20 -28.847 -6.924 9.751 1.00 13.75 C ANISOU 174 CB ALA A 20 1828 1980 1416 -309 -148 201 C ATOM 175 N ILE A 21 -31.568 -8.362 9.010 1.00 16.75 N ANISOU 175 N ILE A 21 2144 2491 1728 -398 -194 184 N ATOM 176 CA ILE A 21 -32.763 -9.066 9.466 1.00 15.33 C ANISOU 176 CA ILE A 21 1912 2382 1531 -445 -205 176 C ATOM 177 C ILE A 21 -32.960 -10.350 8.671 1.00 18.39 C ANISOU 177 C ILE A 21 2325 2754 1906 -515 -202 168 C ATOM 178 O ILE A 21 -33.187 -11.424 9.240 1.00 17.22 O ANISOU 178 O ILE A 21 2170 2609 1762 -576 -187 170 O ATOM 179 CB ILE A 21 -33.993 -8.146 9.366 1.00 14.67 C ANISOU 179 CB ILE A 21 1767 2386 1419 -408 -240 160 C ATOM 180 CG1 ILE A 21 -33.857 -6.974 10.343 1.00 13.82 C ANISOU 180 CG1 ILE A 21 1632 2293 1324 -343 -240 165 C ATOM 181 CG2 ILE A 21 -35.271 -8.934 9.638 1.00 19.66 C ANISOU 181 CG2 ILE A 21 2340 3099 2033 -467 -249 143 C ATOM 182 CD1 ILE A 21 -34.788 -5.820 10.045 1.00 17.00 C ANISOU 182 CD1 ILE A 21 1994 2760 1705 -282 -278 149 C ATOM 183 N LEU A 22 -32.870 -10.260 7.342 1.00 18.54 N ANISOU 183 N LEU A 22 2381 2755 1910 -510 -216 157 N ATOM 184 CA LEU A 22 -33.105 -11.426 6.498 1.00 16.55 C ANISOU 184 CA LEU A 22 2155 2491 1644 -576 -217 144 C ATOM 185 C LEU A 22 -32.145 -12.558 6.836 1.00 18.15 C ANISOU 185 C LEU A 22 2404 2616 1875 -618 -181 154 C ATOM 186 O LEU A 22 -32.565 -13.697 7.070 1.00 19.29 O ANISOU 186 O LEU A 22 2548 2765 2019 -684 -174 149 O ATOM 187 CB LEU A 22 -32.972 -11.041 5.023 1.00 20.18 C ANISOU 187 CB LEU A 22 2656 2934 2077 -554 -235 132 C ATOM 188 CG LEU A 22 -34.118 -10.238 4.403 1.00 25.64 C ANISOU 188 CG LEU A 22 3309 3704 2729 -523 -282 117 C ATOM 189 CD1 LEU A 22 -33.789 -9.878 2.962 1.00 26.09 C ANISOU 189 CD1 LEU A 22 3427 3730 2756 -500 -296 112 C ATOM 190 CD2 LEU A 22 -35.418 -11.018 4.472 1.00 28.60 C ANISOU 190 CD2 LEU A 22 3625 4157 3085 -581 -304 93 C ATOM 191 N GLY A 23 -30.845 -12.267 6.858 1.00 15.90 N ANISOU 191 N GLY A 23 2164 2260 1618 -581 -158 165 N ATOM 192 CA GLY A 23 -29.869 -13.326 7.043 1.00 15.54 C ANISOU 192 CA GLY A 23 2166 2139 1600 -611 -130 169 C ATOM 193 C GLY A 23 -29.949 -13.964 8.413 1.00 18.37 C ANISOU 193 C GLY A 23 2507 2499 1976 -635 -119 186 C ATOM 194 O GLY A 23 -29.830 -15.185 8.548 1.00 21.03 O ANISOU 194 O GLY A 23 2874 2797 2319 -686 -107 188 O ATOM 195 N ASN A 24 -30.158 -13.154 9.449 1.00 15.32 N ANISOU 195 N ASN A 24 2076 2153 1592 -600 -123 199 N ATOM 196 CA ASN A 24 -30.158 -13.690 10.802 1.00 15.96 C ANISOU 196 CA ASN A 24 2147 2234 1683 -619 -111 217 C ATOM 197 C ASN A 24 -31.495 -14.314 11.174 1.00 18.85 C ANISOU 197 C ASN A 24 2477 2665 2022 -683 -115 215 C ATOM 198 O ASN A 24 -31.536 -15.206 12.027 1.00 18.44 O ANISOU 198 O ASN A 24 2439 2597 1971 -726 -100 231 O ATOM 199 CB ASN A 24 -29.760 -12.593 11.784 1.00 17.89 C ANISOU 199 CB ASN A 24 2363 2494 1941 -556 -111 228 C ATOM 200 CG ASN A 24 -28.288 -12.266 11.696 1.00 16.59 C ANISOU 200 CG ASN A 24 2237 2256 1811 -509 -100 229 C ATOM 201 OD1 ASN A 24 -27.449 -13.026 12.176 1.00 17.00 O ANISOU 201 OD1 ASN A 24 2323 2252 1885 -515 -87 237 O ATOM 202 ND2 ASN A 24 -27.962 -11.148 11.057 1.00 16.70 N ANISOU 202 ND2 ASN A 24 2247 2269 1828 -461 -104 219 N ATOM 203 N VAL A 25 -32.590 -13.883 10.546 1.00 17.67 N ANISOU 203 N VAL A 25 2282 2588 1846 -691 -136 196 N ATOM 204 CA VAL A 25 -33.835 -14.633 10.676 1.00 20.85 C ANISOU 204 CA VAL A 25 2648 3050 2224 -765 -138 184 C ATOM 205 C VAL A 25 -33.664 -16.022 10.076 1.00 21.33 C ANISOU 205 C VAL A 25 2765 3053 2286 -836 -126 180 C ATOM 206 O VAL A 25 -34.170 -17.016 10.608 1.00 19.03 O ANISOU 206 O VAL A 25 2477 2766 1988 -908 -111 184 O ATOM 207 CB VAL A 25 -34.999 -13.864 10.023 1.00 22.27 C ANISOU 207 CB VAL A 25 2763 3322 2377 -752 -169 157 C ATOM 208 CG1 VAL A 25 -36.191 -14.787 9.796 1.00 21.30 C ANISOU 208 CG1 VAL A 25 2607 3254 2232 -838 -173 134 C ATOM 209 CG2 VAL A 25 -35.402 -12.678 10.892 1.00 20.96 C ANISOU 209 CG2 VAL A 25 2534 3221 2208 -693 -177 158 C ATOM 210 N LEU A 26 -32.923 -16.113 8.970 1.00 22.71 N ANISOU 210 N LEU A 26 2989 3169 2469 -818 -131 171 N ATOM 211 CA LEU A 26 -32.643 -17.410 8.363 1.00 18.92 C ANISOU 211 CA LEU A 26 2569 2625 1994 -878 -119 163 C ATOM 212 C LEU A 26 -31.848 -18.301 9.310 1.00 19.03 C ANISOU 212 C LEU A 26 2633 2564 2032 -894 -94 188 C ATOM 213 O LEU A 26 -32.119 -19.503 9.419 1.00 21.97 O ANISOU 213 O LEU A 26 3039 2907 2401 -964 -82 188 O ATOM 214 CB LEU A 26 -31.889 -17.207 7.048 1.00 22.07 C ANISOU 214 CB LEU A 26 3012 2977 2396 -845 -125 146 C ATOM 215 CG LEU A 26 -31.606 -18.439 6.190 1.00 28.01 C ANISOU 215 CG LEU A 26 3826 3667 3150 -899 -116 129 C ATOM 216 CD1 LEU A 26 -32.897 -19.029 5.643 1.00 31.22 C ANISOU 216 CD1 LEU A 26 4207 4129 3524 -973 -132 103 C ATOM 217 CD2 LEU A 26 -30.654 -18.075 5.061 1.00 29.80 C ANISOU 217 CD2 LEU A 26 4096 3845 3381 -854 -113 115 C ATOM 218 N VAL A 27 -30.861 -17.732 10.006 1.00 18.98 N ANISOU 218 N VAL A 27 2637 2524 2050 -829 -87 208 N ATOM 219 CA VAL A 27 -30.085 -18.514 10.965 1.00 22.92 C ANISOU 219 CA VAL A 27 3184 2956 2570 -833 -70 232 C ATOM 220 C VAL A 27 -30.995 -19.066 12.056 1.00 19.33 C ANISOU 220 C VAL A 27 2713 2538 2094 -892 -61 251 C ATOM 221 O VAL A 27 -30.944 -20.255 12.388 1.00 21.46 O ANISOU 221 O VAL A 27 3035 2755 2363 -946 -48 263 O ATOM 222 CB VAL A 27 -28.947 -17.663 11.559 1.00 18.41 C ANISOU 222 CB VAL A 27 2611 2357 2025 -751 -69 245 C ATOM 223 CG1 VAL A 27 -28.367 -18.335 12.797 1.00 19.97 C ANISOU 223 CG1 VAL A 27 2845 2508 2235 -749 -60 272 C ATOM 224 CG2 VAL A 27 -27.859 -17.434 10.518 1.00 19.24 C ANISOU 224 CG2 VAL A 27 2748 2406 2155 -708 -67 226 C ATOM 225 N CYS A 28 -31.839 -18.207 12.633 1.00 20.67 N ANISOU 225 N CYS A 28 2813 2797 2245 -884 -66 252 N ATOM 226 CA CYS A 28 -32.737 -18.655 13.693 1.00 24.93 C ANISOU 226 CA CYS A 28 3331 3382 2760 -943 -51 266 C ATOM 227 C CYS A 28 -33.721 -19.695 13.174 1.00 24.94 C ANISOU 227 C CYS A 28 3337 3398 2743 -1041 -43 250 C ATOM 228 O CYS A 28 -34.024 -20.676 13.864 1.00 25.47 O ANISOU 228 O CYS A 28 3436 3444 2797 -1110 -21 267 O ATOM 229 CB CYS A 28 -33.483 -17.461 14.286 1.00 24.02 C ANISOU 229 CB CYS A 28 3132 3367 2629 -910 -57 261 C ATOM 230 SG CYS A 28 -32.424 -16.261 15.123 1.00 22.76 S ANISOU 230 SG CYS A 28 2966 3193 2489 -806 -63 279 S ATOM 231 N TRP A 29 -34.222 -19.500 11.953 1.00 26.71 N ANISOU 231 N TRP A 29 3534 3655 2961 -1051 -61 217 N ATOM 232 CA TRP A 29 -35.159 -20.455 11.373 1.00 27.34 C ANISOU 232 CA TRP A 29 3613 3754 3023 -1146 -57 193 C ATOM 233 C TRP A 29 -34.491 -21.807 11.160 1.00 31.94 C ANISOU 233 C TRP A 29 4291 4227 3619 -1192 -42 203 C ATOM 234 O TRP A 29 -35.109 -22.855 11.378 1.00 28.07 O ANISOU 234 O TRP A 29 3822 3728 3116 -1282 -24 202 O ATOM 235 CB TRP A 29 -35.709 -19.891 10.060 1.00 30.52 C ANISOU 235 CB TRP A 29 3970 4212 3415 -1132 -88 154 C ATOM 236 CG TRP A 29 -36.979 -20.530 9.562 1.00 48.16 C ANISOU 236 CG TRP A 29 6166 6506 5625 -1224 -92 120 C ATOM 237 CD1 TRP A 29 -37.203 -21.038 8.314 1.00 54.16 C ANISOU 237 CD1 TRP A 29 6945 7256 6378 -1260 -109 87 C ATOM 238 CD2 TRP A 29 -38.200 -20.714 10.293 1.00 54.48 C ANISOU 238 CD2 TRP A 29 6901 7391 6406 -1292 -79 110 C ATOM 239 NE1 TRP A 29 -38.483 -21.527 8.223 1.00 57.09 N ANISOU 239 NE1 TRP A 29 7264 7700 6728 -1347 -110 56 N ATOM 240 CE2 TRP A 29 -39.115 -21.343 9.425 1.00 64.10 C ANISOU 240 CE2 TRP A 29 8097 8648 7609 -1370 -90 68 C ATOM 241 CE3 TRP A 29 -38.606 -20.411 11.596 1.00 53.02 C ANISOU 241 CE3 TRP A 29 6674 7257 6214 -1298 -57 128 C ATOM 242 CZ2 TRP A 29 -40.411 -21.675 9.818 1.00 71.21 C ANISOU 242 CZ2 TRP A 29 8934 9633 8492 -1436 -77 43 C ATOM 243 CZ3 TRP A 29 -39.893 -20.743 11.984 1.00 58.62 C ANISOU 243 CZ3 TRP A 29 7318 8054 6902 -1382 -42 105 C ATOM 244 CH2 TRP A 29 -40.779 -21.368 11.098 1.00 59.84 C ANISOU 244 CH2 TRP A 29 7453 8239 7045 -1434 -51 61 C ATOM 245 N ALA A 30 -33.215 -21.802 10.766 1.00 25.80 N ANISOU 245 N ALA A 30 3571 3365 2868 -1131 -46 210 N ATOM 246 CA ALA A 30 -32.511 -23.055 10.506 1.00 25.24 C ANISOU 246 CA ALA A 30 3591 3187 2812 -1162 -35 214 C ATOM 247 C ALA A 30 -32.307 -23.860 11.785 1.00 29.99 C ANISOU 247 C ALA A 30 4240 3740 3415 -1178 -15 249 C ATOM 248 O ALA A 30 -32.491 -25.082 11.787 1.00 27.57 O ANISOU 248 O ALA A 30 3984 3384 3106 -1215 -5 242 O ATOM 249 CB ALA A 30 -31.165 -22.775 9.837 1.00 25.04 C ANISOU 249 CB ALA A 30 3605 3092 2816 -1082 -42 208 C ATOM 250 N VAL A 31 -31.911 -23.203 12.877 1.00 28.56 N ANISOU 250 N VAL A 31 4046 3570 3236 -1136 -13 282 N ATOM 251 CA VAL A 31 -31.697 -23.930 14.125 1.00 26.07 C ANISOU 251 CA VAL A 31 3777 3211 2916 -1135 0 313 C ATOM 252 C VAL A 31 -33.020 -24.461 14.664 1.00 30.78 C ANISOU 252 C VAL A 31 4349 3865 3480 -1209 19 308 C ATOM 253 O VAL A 31 -33.084 -25.569 15.208 1.00 27.61 O ANISOU 253 O VAL A 31 4007 3412 3073 -1238 33 320 O ATOM 254 CB VAL A 31 -30.985 -23.035 15.157 1.00 28.96 C ANISOU 254 CB VAL A 31 4134 3584 3287 -1073 -4 347 C ATOM 255 CG1 VAL A 31 -30.753 -23.794 16.458 1.00 30.12 C ANISOU 255 CG1 VAL A 31 4336 3687 3423 -1071 6 380 C ATOM 256 CG2 VAL A 31 -29.664 -22.530 14.600 1.00 22.97 C ANISOU 256 CG2 VAL A 31 3388 2774 2565 -979 -22 336 C ATOM 257 N TRP A 32 -34.095 -23.683 14.525 1.00 34.18 N ANISOU 257 N TRP A 32 4693 4404 3891 -1241 20 290 N ATOM 258 CA TRP A 32 -35.399 -24.126 15.005 1.00 34.59 C ANISOU 258 CA TRP A 32 4710 4520 3913 -1313 40 279 C ATOM 259 C TRP A 32 -35.898 -25.347 14.241 1.00 36.58 C ANISOU 259 C TRP A 32 4999 4737 4163 -1376 46 251 C ATOM 260 O TRP A 32 -36.563 -26.210 14.824 1.00 36.03 O ANISOU 260 O TRP A 32 4949 4666 4076 -1433 69 252 O ATOM 261 CB TRP A 32 -36.408 -22.981 14.895 1.00 38.14 C ANISOU 261 CB TRP A 32 5047 5098 4345 -1325 34 257 C ATOM 262 CG TRP A 32 -37.820 -23.351 15.263 1.00 43.14 C ANISOU 262 CG TRP A 32 5629 5811 4950 -1398 55 233 C ATOM 263 CD1 TRP A 32 -38.728 -24.010 14.482 1.00 42.67 C ANISOU 263 CD1 TRP A 32 5553 5777 4883 -1462 56 195 C ATOM 264 CD2 TRP A 32 -38.490 -23.065 16.498 1.00 50.02 C ANISOU 264 CD2 TRP A 32 6459 6750 5798 -1414 79 243 C ATOM 265 NE1 TRP A 32 -39.914 -24.159 15.157 1.00 47.29 N ANISOU 265 NE1 TRP A 32 6086 6440 5442 -1517 81 179 N ATOM 266 CE2 TRP A 32 -39.796 -23.587 16.396 1.00 49.77 C ANISOU 266 CE2 TRP A 32 6383 6781 5745 -1489 96 207 C ATOM 267 CE3 TRP A 32 -38.112 -22.422 17.681 1.00 54.16 C ANISOU 267 CE3 TRP A 32 6976 7288 6313 -1372 89 275 C ATOM 268 CZ2 TRP A 32 -40.723 -23.486 17.431 1.00 50.65 C ANISOU 268 CZ2 TRP A 32 6446 6968 5830 -1524 125 202 C ATOM 269 CZ3 TRP A 32 -39.035 -22.323 18.708 1.00 61.77 C ANISOU 269 CZ3 TRP A 32 7894 8327 7248 -1406 116 271 C ATOM 270 CH2 TRP A 32 -40.325 -22.852 18.576 1.00 56.39 C ANISOU 270 CH2 TRP A 32 7170 7706 6548 -1482 135 234 C ATOM 271 N LEU A 33 -35.591 -25.441 12.947 1.00 35.66 N ANISOU 271 N LEU A 33 4895 4592 4062 -1369 28 225 N ATOM 272 CA LEU A 33 -36.109 -26.520 12.115 1.00 38.96 C ANISOU 272 CA LEU A 33 5341 4985 4476 -1428 32 193 C ATOM 273 C LEU A 33 -35.253 -27.781 12.173 1.00 37.11 C ANISOU 273 C LEU A 33 5213 4628 4258 -1421 40 208 C ATOM 274 O LEU A 33 -35.796 -28.890 12.225 1.00 42.42 O ANISOU 274 O LEU A 33 5921 5275 4921 -1481 57 198 O ATOM 275 CB LEU A 33 -36.225 -26.056 10.659 1.00 38.96 C ANISOU 275 CB LEU A 33 5306 5017 4479 -1426 7 155 C ATOM 276 CG LEU A 33 -37.398 -25.146 10.288 1.00 46.92 C ANISOU 276 CG LEU A 33 6208 6153 5466 -1453 -8 125 C ATOM 277 CD1 LEU A 33 -37.355 -24.828 8.800 1.00 52.60 C ANISOU 277 CD1 LEU A 33 6914 6885 6186 -1446 -38 90 C ATOM 278 CD2 LEU A 33 -38.730 -25.781 10.659 1.00 51.21 C ANISOU 278 CD2 LEU A 33 6714 6756 5986 -1530 12 104 C ATOM 279 N ASN A 34 -33.929 -27.644 12.155 1.00 34.19 N ANISOU 279 N ASN A 34 4893 4182 3916 -1349 29 227 N ATOM 280 CA ASN A 34 -33.022 -28.781 12.030 1.00 33.55 C ANISOU 280 CA ASN A 34 4906 3985 3855 -1330 32 233 C ATOM 281 C ASN A 34 -32.510 -29.181 13.410 1.00 37.42 C ANISOU 281 C ASN A 34 5449 4424 4345 -1306 41 277 C ATOM 282 O ASN A 34 -31.779 -28.420 14.054 1.00 34.43 O ANISOU 282 O ASN A 34 5063 4044 3976 -1244 32 303 O ATOM 283 CB ASN A 34 -31.861 -28.439 11.098 1.00 33.79 C ANISOU 283 CB ASN A 34 4958 3965 3915 -1264 14 220 C ATOM 284 CG ASN A 34 -31.024 -29.650 10.743 1.00 36.42 C ANISOU 284 CG ASN A 34 5379 4187 4270 -1248 16 214 C ATOM 285 OD1 ASN A 34 -31.131 -30.701 11.377 1.00 39.54 O ANISOU 285 OD1 ASN A 34 5830 4532 4661 -1273 27 230 O ATOM 286 ND2 ASN A 34 -30.179 -29.509 9.728 1.00 35.39 N ANISOU 286 ND2 ASN A 34 5265 4019 4164 -1205 6 190 N ATOM 287 N SER A 35 -32.876 -30.390 13.849 1.00 35.47 N ANISOU 287 N SER A 35 5258 4132 4086 -1354 58 284 N ATOM 288 CA SER A 35 -32.411 -30.883 15.139 1.00 38.56 C ANISOU 288 CA SER A 35 5711 4468 4471 -1335 65 327 C ATOM 289 C SER A 35 -30.911 -31.138 15.137 1.00 35.00 C ANISOU 289 C SER A 35 5328 3918 4053 -1252 45 343 C ATOM 290 O SER A 35 -30.281 -31.101 16.199 1.00 38.38 O ANISOU 290 O SER A 35 5790 4312 4479 -1208 40 379 O ATOM 291 CB SER A 35 -33.160 -32.162 15.515 1.00 41.88 C ANISOU 291 CB SER A 35 6185 4859 4871 -1411 88 330 C ATOM 292 OG SER A 35 -32.937 -33.178 14.553 1.00 43.71 O ANISOU 292 OG SER A 35 6470 5018 5118 -1426 85 305 O ATOM 293 N ASN A 36 -30.321 -31.389 13.965 1.00 31.66 N ANISOU 293 N ASN A 36 4923 3449 3657 -1228 34 313 N ATOM 294 CA ASN A 36 -28.873 -31.546 13.883 1.00 33.36 C ANISOU 294 CA ASN A 36 5192 3578 3907 -1145 16 319 C ATOM 295 C ASN A 36 -28.133 -30.249 14.181 1.00 39.07 C ANISOU 295 C ASN A 36 5870 4332 4645 -1075 0 332 C ATOM 296 O ASN A 36 -26.928 -30.286 14.454 1.00 36.89 O ANISOU 296 O ASN A 36 5632 3989 4393 -1003 -15 343 O ATOM 297 CB ASN A 36 -28.471 -32.058 12.499 1.00 38.48 C ANISOU 297 CB ASN A 36 5863 4178 4580 -1139 12 277 C ATOM 298 CG ASN A 36 -28.997 -33.450 12.219 1.00 42.26 C ANISOU 298 CG ASN A 36 6399 4607 5049 -1200 24 265 C ATOM 299 OD1 ASN A 36 -29.208 -34.242 13.137 1.00 42.39 O ANISOU 299 OD1 ASN A 36 6468 4588 5051 -1223 32 294 O ATOM 300 ND2 ASN A 36 -29.211 -33.757 10.946 1.00 41.80 N ANISOU 300 ND2 ASN A 36 6337 4548 4998 -1226 27 223 N ATOM 301 N LEU A 37 -28.818 -29.109 14.128 1.00 32.80 N ANISOU 301 N LEU A 37 4993 3634 3835 -1093 4 328 N ATOM 302 CA LEU A 37 -28.235 -27.824 14.486 1.00 32.42 C ANISOU 302 CA LEU A 37 4900 3622 3796 -1034 -8 342 C ATOM 303 C LEU A 37 -28.553 -27.416 15.917 1.00 31.40 C ANISOU 303 C LEU A 37 4756 3534 3641 -1035 -5 381 C ATOM 304 O LEU A 37 -28.087 -26.364 16.365 1.00 28.63 O ANISOU 304 O LEU A 37 4370 3214 3295 -986 -15 396 O ATOM 305 CB LEU A 37 -28.727 -26.737 13.523 1.00 28.42 C ANISOU 305 CB LEU A 37 4315 3196 3288 -1047 -9 314 C ATOM 306 CG LEU A 37 -28.237 -26.841 12.077 1.00 30.71 C ANISOU 306 CG LEU A 37 4616 3451 3602 -1034 -15 275 C ATOM 307 CD1 LEU A 37 -28.931 -25.812 11.202 1.00 30.03 C ANISOU 307 CD1 LEU A 37 4457 3451 3502 -1057 -17 251 C ATOM 308 CD2 LEU A 37 -26.728 -26.670 12.005 1.00 31.34 C ANISOU 308 CD2 LEU A 37 4731 3459 3720 -953 -25 275 C ATOM 309 N GLN A 38 -29.323 -28.221 16.647 1.00 31.36 N ANISOU 309 N GLN A 38 4778 3530 3607 -1089 11 397 N ATOM 310 CA GLN A 38 -29.757 -27.869 17.998 1.00 35.90 C ANISOU 310 CA GLN A 38 5338 4152 4150 -1098 20 431 C ATOM 311 C GLN A 38 -28.743 -28.416 18.996 1.00 35.52 C ANISOU 311 C GLN A 38 5371 4021 4104 -1044 7 468 C ATOM 312 O GLN A 38 -28.847 -29.547 19.472 1.00 37.21 O ANISOU 312 O GLN A 38 5655 4178 4304 -1070 15 483 O ATOM 313 CB GLN A 38 -31.161 -28.397 18.259 1.00 36.19 C ANISOU 313 CB GLN A 38 5359 4239 4152 -1189 48 425 C ATOM 314 CG GLN A 38 -32.226 -27.699 17.427 1.00 37.86 C ANISOU 314 CG GLN A 38 5479 4549 4357 -1236 55 389 C ATOM 315 CD GLN A 38 -33.591 -28.340 17.566 1.00 43.15 C ANISOU 315 CD GLN A 38 6133 5265 4997 -1329 82 375 C ATOM 316 OE1 GLN A 38 -33.775 -29.273 18.346 1.00 42.82 O ANISOU 316 OE1 GLN A 38 6150 5182 4937 -1362 99 395 O ATOM 317 NE2 GLN A 38 -34.557 -27.843 16.804 1.00 40.60 N ANISOU 317 NE2 GLN A 38 5731 5028 4668 -1371 85 339 N ATOM 318 N ASN A 39 -27.746 -27.592 19.309 1.00 32.80 N ANISOU 318 N ASN A 39 5018 3669 3776 -968 -15 481 N ATOM 319 CA ASN A 39 -26.747 -27.901 20.319 1.00 31.51 C ANISOU 319 CA ASN A 39 4920 3440 3612 -906 -36 515 C ATOM 320 C ASN A 39 -26.383 -26.612 21.042 1.00 33.19 C ANISOU 320 C ASN A 39 5086 3708 3817 -856 -49 533 C ATOM 321 O ASN A 39 -26.773 -25.514 20.633 1.00 28.30 O ANISOU 321 O ASN A 39 4387 3166 3200 -864 -43 518 O ATOM 322 CB ASN A 39 -25.503 -28.553 19.703 1.00 29.51 C ANISOU 322 CB ASN A 39 4728 3084 3401 -846 -60 503 C ATOM 323 CG ASN A 39 -24.973 -27.782 18.510 1.00 31.17 C ANISOU 323 CG ASN A 39 4889 3303 3650 -815 -68 467 C ATOM 324 OD1 ASN A 39 -24.417 -26.695 18.656 1.00 30.11 O ANISOU 324 OD1 ASN A 39 4715 3197 3528 -766 -81 470 O ATOM 325 ND2 ASN A 39 -25.141 -28.345 17.319 1.00 33.74 N ANISOU 325 ND2 ASN A 39 5221 3604 3995 -844 -57 432 N ATOM 326 N VAL A 40 -25.617 -26.753 22.127 1.00 28.96 N ANISOU 326 N VAL A 40 4601 3131 3270 -802 -70 566 N ATOM 327 CA VAL A 40 -25.304 -25.603 22.971 1.00 27.10 C ANISOU 327 CA VAL A 40 4328 2950 3020 -756 -85 585 C ATOM 328 C VAL A 40 -24.555 -24.541 22.179 1.00 26.85 C ANISOU 328 C VAL A 40 4232 2938 3033 -693 -103 552 C ATOM 329 O VAL A 40 -24.849 -23.344 22.286 1.00 24.29 O ANISOU 329 O VAL A 40 3820 2702 2708 -675 -98 536 O ATOM 330 CB VAL A 40 -24.501 -26.050 24.206 1.00 32.04 C ANISOU 330 CB VAL A 40 5027 3520 3626 -698 -113 621 C ATOM 331 CG1 VAL A 40 -23.990 -24.835 24.963 1.00 32.23 C ANISOU 331 CG1 VAL A 40 5011 3596 3640 -636 -136 632 C ATOM 332 CG2 VAL A 40 -25.362 -26.923 25.103 1.00 32.27 C ANISOU 332 CG2 VAL A 40 5102 3552 3608 -756 -88 646 C ATOM 333 N THR A 41 -23.567 -24.956 21.384 1.00 23.55 N ANISOU 333 N THR A 41 3842 2446 2662 -645 -121 528 N ATOM 334 CA THR A 41 -22.813 -23.991 20.594 1.00 23.90 C ANISOU 334 CA THR A 41 3812 2514 2755 -578 -131 482 C ATOM 335 C THR A 41 -23.746 -23.116 19.767 1.00 25.58 C ANISOU 335 C THR A 41 3942 2813 2966 -622 -105 457 C ATOM 336 O THR A 41 -23.584 -21.891 19.719 1.00 24.07 O ANISOU 336 O THR A 41 3675 2684 2788 -579 -108 437 O ATOM 337 CB THR A 41 -21.817 -24.715 19.687 1.00 30.21 C ANISOU 337 CB THR A 41 4654 3225 3601 -541 -143 454 C ATOM 338 OG1 THR A 41 -21.114 -25.709 20.441 1.00 30.59 O ANISOU 338 OG1 THR A 41 4791 3187 3647 -506 -169 480 O ATOM 339 CG2 THR A 41 -20.814 -23.733 19.106 1.00 26.21 C ANISOU 339 CG2 THR A 41 4078 2737 3143 -464 -153 409 C ATOM 340 N ASN A 42 -24.741 -23.725 19.124 1.00 22.88 N ANISOU 340 N ASN A 42 3613 2473 2605 -708 -82 457 N ATOM 341 CA ASN A 42 -25.629 -22.983 18.241 1.00 24.14 C ANISOU 341 CA ASN A 42 3698 2711 2762 -746 -65 430 C ATOM 342 C ASN A 42 -26.700 -22.196 18.985 1.00 22.56 C ANISOU 342 C ASN A 42 3436 2611 2524 -776 -53 443 C ATOM 343 O ASN A 42 -27.337 -21.328 18.378 1.00 22.46 O ANISOU 343 O ASN A 42 3350 2672 2510 -784 -47 419 O ATOM 344 CB ASN A 42 -26.287 -23.935 17.244 1.00 23.21 C ANISOU 344 CB ASN A 42 3614 2564 2640 -826 -49 418 C ATOM 345 CG ASN A 42 -25.333 -24.378 16.152 1.00 28.34 C ANISOU 345 CG ASN A 42 4299 3138 3332 -792 -57 387 C ATOM 346 OD1 ASN A 42 -24.258 -23.801 15.979 1.00 26.82 O ANISOU 346 OD1 ASN A 42 4088 2931 3174 -711 -71 369 O ATOM 347 ND2 ASN A 42 -25.724 -25.400 15.405 1.00 25.89 N ANISOU 347 ND2 ASN A 42 4036 2784 3019 -853 -47 376 N ATOM 348 N TYR A 43 -26.917 -22.464 20.273 1.00 21.90 N ANISOU 348 N TYR A 43 3382 2533 2406 -790 -50 480 N ATOM 349 CA TYR A 43 -27.817 -21.610 21.040 1.00 23.12 C ANISOU 349 CA TYR A 43 3471 2787 2526 -807 -37 487 C ATOM 350 C TYR A 43 -27.201 -20.235 21.250 1.00 22.26 C ANISOU 350 C TYR A 43 3298 2723 2438 -718 -55 469 C ATOM 351 O TYR A 43 -27.911 -19.223 21.239 1.00 18.66 O ANISOU 351 O TYR A 43 2765 2354 1971 -718 -48 452 O ATOM 352 CB TYR A 43 -28.163 -22.268 22.375 1.00 25.55 C ANISOU 352 CB TYR A 43 3834 3087 2786 -847 -25 531 C ATOM 353 CG TYR A 43 -28.863 -23.603 22.226 1.00 33.06 C ANISOU 353 CG TYR A 43 4841 4000 3721 -929 -3 537 C ATOM 354 CD1 TYR A 43 -29.658 -23.874 21.117 1.00 37.10 C ANISOU 354 CD1 TYR A 43 5321 4533 4244 -986 11 503 C ATOM 355 CD2 TYR A 43 -28.723 -24.596 23.186 1.00 32.60 C ANISOU 355 CD2 TYR A 43 4860 3886 3640 -935 -1 565 C ATOM 356 CE1 TYR A 43 -30.294 -25.091 20.974 1.00 39.84 C ANISOU 356 CE1 TYR A 43 5709 4848 4581 -1049 29 497 C ATOM 357 CE2 TYR A 43 -29.355 -25.815 23.049 1.00 38.65 C ANISOU 357 CE2 TYR A 43 5671 4618 4398 -999 19 561 C ATOM 358 CZ TYR A 43 -30.141 -26.057 21.942 1.00 41.53 C ANISOU 358 CZ TYR A 43 6001 5005 4775 -1057 34 526 C ATOM 359 OH TYR A 43 -30.773 -27.271 21.803 1.00 47.59 O ANISOU 359 OH TYR A 43 6813 5738 5532 -1122 53 520 O ATOM 360 N PHE A 44 -25.878 -20.174 21.420 1.00 19.79 N ANISOU 360 N PHE A 44 3013 2350 2155 -642 -80 467 N ATOM 361 CA PHE A 44 -25.204 -18.882 21.460 1.00 16.88 C ANISOU 361 CA PHE A 44 2584 2016 1814 -562 -95 443 C ATOM 362 C PHE A 44 -25.164 -18.233 20.083 1.00 17.17 C ANISOU 362 C PHE A 44 2573 2066 1885 -552 -91 405 C ATOM 363 O PHE A 44 -25.137 -17.002 19.981 1.00 17.23 O ANISOU 363 O PHE A 44 2519 2126 1903 -512 -93 384 O ATOM 364 CB PHE A 44 -23.791 -19.044 22.019 1.00 18.52 C ANISOU 364 CB PHE A 44 2831 2160 2047 -488 -123 446 C ATOM 365 CG PHE A 44 -23.760 -19.475 23.457 1.00 19.86 C ANISOU 365 CG PHE A 44 3047 2323 2178 -484 -133 483 C ATOM 366 CD1 PHE A 44 -24.074 -18.582 24.468 1.00 23.28 C ANISOU 366 CD1 PHE A 44 3438 2827 2582 -466 -134 489 C ATOM 367 CD2 PHE A 44 -23.418 -20.772 23.798 1.00 20.97 C ANISOU 367 CD2 PHE A 44 3278 2383 2306 -496 -144 513 C ATOM 368 CE1 PHE A 44 -24.049 -18.976 25.792 1.00 28.21 C ANISOU 368 CE1 PHE A 44 4110 3447 3163 -463 -143 525 C ATOM 369 CE2 PHE A 44 -23.391 -21.171 25.120 1.00 30.61 C ANISOU 369 CE2 PHE A 44 4552 3594 3484 -492 -155 552 C ATOM 370 CZ PHE A 44 -23.708 -20.273 26.117 1.00 22.81 C ANISOU 370 CZ PHE A 44 3521 2683 2464 -477 -154 558 C ATOM 371 N VAL A 45 -25.158 -19.037 19.018 1.00 16.44 N ANISOU 371 N VAL A 45 2514 1925 1806 -586 -84 394 N ATOM 372 CA VAL A 45 -25.277 -18.488 17.670 1.00 17.23 C ANISOU 372 CA VAL A 45 2577 2043 1927 -586 -78 361 C ATOM 373 C VAL A 45 -26.623 -17.797 17.497 1.00 16.36 C ANISOU 373 C VAL A 45 2404 2024 1786 -625 -69 356 C ATOM 374 O VAL A 45 -26.710 -16.714 16.904 1.00 15.91 O ANISOU 374 O VAL A 45 2296 2010 1739 -594 -72 334 O ATOM 375 CB VAL A 45 -25.073 -19.600 16.624 1.00 20.60 C ANISOU 375 CB VAL A 45 3057 2400 2368 -621 -73 350 C ATOM 376 CG1 VAL A 45 -25.514 -19.133 15.246 1.00 21.34 C ANISOU 376 CG1 VAL A 45 3117 2525 2466 -639 -65 320 C ATOM 377 CG2 VAL A 45 -23.617 -20.035 16.598 1.00 25.21 C ANISOU 377 CG2 VAL A 45 3687 2901 2992 -563 -84 341 C ATOM 378 N VAL A 46 -27.693 -18.407 18.011 1.00 17.73 N ANISOU 378 N VAL A 46 2583 2230 1923 -693 -57 375 N ATOM 379 CA VAL A 46 -29.011 -17.789 17.920 1.00 18.29 C ANISOU 379 CA VAL A 46 2587 2397 1966 -729 -49 365 C ATOM 380 C VAL A 46 -29.056 -16.504 18.736 1.00 17.80 C ANISOU 380 C VAL A 46 2468 2399 1898 -673 -54 364 C ATOM 381 O VAL A 46 -29.599 -15.487 18.287 1.00 15.11 O ANISOU 381 O VAL A 46 2064 2121 1555 -654 -59 341 O ATOM 382 CB VAL A 46 -30.098 -18.782 18.367 1.00 18.60 C ANISOU 382 CB VAL A 46 2643 2457 1968 -822 -29 382 C ATOM 383 CG1 VAL A 46 -31.445 -18.078 18.480 1.00 27.79 C ANISOU 383 CG1 VAL A 46 3724 3731 3103 -852 -21 367 C ATOM 384 CG2 VAL A 46 -30.178 -19.944 17.394 1.00 21.81 C ANISOU 384 CG2 VAL A 46 3101 2805 2382 -881 -24 375 C ATOM 385 N SER A 47 -28.493 -16.525 19.946 1.00 17.32 N ANISOU 385 N SER A 47 2429 2321 1831 -645 -57 386 N ATOM 386 CA SER A 47 -28.412 -15.301 20.736 1.00 15.29 C ANISOU 386 CA SER A 47 2121 2117 1570 -587 -63 380 C ATOM 387 C SER A 47 -27.645 -14.223 19.983 1.00 16.72 C ANISOU 387 C SER A 47 2275 2288 1791 -518 -78 353 C ATOM 388 O SER A 47 -28.031 -13.049 19.994 1.00 15.64 O ANISOU 388 O SER A 47 2082 2210 1652 -486 -81 336 O ATOM 389 CB SER A 47 -27.756 -15.590 22.087 1.00 20.37 C ANISOU 389 CB SER A 47 2805 2735 2202 -564 -68 406 C ATOM 390 OG SER A 47 -27.707 -14.424 22.894 1.00 21.06 O ANISOU 390 OG SER A 47 2845 2876 2283 -512 -74 398 O ATOM 391 N LEU A 48 -26.557 -14.610 19.316 1.00 16.90 N ANISOU 391 N LEU A 48 2339 2234 1848 -496 -85 346 N ATOM 392 CA LEU A 48 -25.811 -13.662 18.497 1.00 15.51 C ANISOU 392 CA LEU A 48 2143 2044 1708 -442 -91 319 C ATOM 393 C LEU A 48 -26.659 -13.155 17.337 1.00 15.36 C ANISOU 393 C LEU A 48 2091 2065 1681 -462 -87 302 C ATOM 394 O LEU A 48 -26.647 -11.958 17.025 1.00 15.82 O ANISOU 394 O LEU A 48 2112 2151 1746 -421 -92 285 O ATOM 395 CB LEU A 48 -24.531 -14.331 17.990 1.00 17.07 C ANISOU 395 CB LEU A 48 2389 2154 1942 -423 -93 312 C ATOM 396 CG LEU A 48 -23.471 -13.491 17.281 1.00 19.50 C ANISOU 396 CG LEU A 48 2684 2435 2290 -370 -93 283 C ATOM 397 CD1 LEU A 48 -23.009 -12.332 18.144 1.00 20.68 C ANISOU 397 CD1 LEU A 48 2796 2611 2449 -315 -102 275 C ATOM 398 CD2 LEU A 48 -22.286 -14.375 16.914 1.00 21.05 C ANISOU 398 CD2 LEU A 48 2926 2551 2520 -357 -93 273 C ATOM 399 N ALA A 49 -27.412 -14.048 16.690 1.00 12.77 N ANISOU 399 N ALA A 49 1778 1738 1335 -523 -81 304 N ATOM 400 CA ALA A 49 -28.264 -13.627 15.583 1.00 15.89 C ANISOU 400 CA ALA A 49 2143 2177 1719 -541 -84 285 C ATOM 401 C ALA A 49 -29.393 -12.725 16.068 1.00 16.45 C ANISOU 401 C ALA A 49 2148 2340 1762 -535 -89 281 C ATOM 402 O ALA A 49 -29.783 -11.779 15.374 1.00 14.03 O ANISOU 402 O ALA A 49 1808 2071 1454 -507 -101 263 O ATOM 403 CB ALA A 49 -28.827 -14.850 14.859 1.00 19.69 C ANISOU 403 CB ALA A 49 2654 2642 2187 -613 -78 285 C ATOM 404 N ALA A 50 -29.933 -13.002 17.257 1.00 15.64 N ANISOU 404 N ALA A 50 2029 2275 1638 -559 -82 296 N ATOM 405 CA ALA A 50 -30.973 -12.143 17.812 1.00 14.50 C ANISOU 405 CA ALA A 50 1817 2222 1468 -550 -84 287 C ATOM 406 C ALA A 50 -30.464 -10.722 18.005 1.00 15.50 C ANISOU 406 C ALA A 50 1919 2358 1612 -468 -96 275 C ATOM 407 O ALA A 50 -31.170 -9.753 17.702 1.00 13.83 O ANISOU 407 O ALA A 50 1658 2204 1392 -441 -107 257 O ATOM 408 CB ALA A 50 -31.470 -12.715 19.140 1.00 20.62 C ANISOU 408 CB ALA A 50 2589 3030 2216 -590 -66 306 C ATOM 409 N ALA A 51 -29.241 -10.577 18.517 1.00 16.79 N ANISOU 409 N ALA A 51 2115 2465 1800 -428 -95 284 N ATOM 410 CA ALA A 51 -28.658 -9.250 18.667 1.00 14.79 C ANISOU 410 CA ALA A 51 1842 2212 1566 -358 -104 269 C ATOM 411 C ALA A 51 -28.532 -8.552 17.321 1.00 15.25 C ANISOU 411 C ALA A 51 1901 2254 1640 -333 -112 252 C ATOM 412 O ALA A 51 -28.761 -7.342 17.217 1.00 15.96 O ANISOU 412 O ALA A 51 1962 2373 1730 -288 -121 237 O ATOM 413 CB ALA A 51 -27.294 -9.351 19.346 1.00 15.59 C ANISOU 413 CB ALA A 51 1977 2252 1693 -326 -104 276 C ATOM 414 N ASP A 52 -28.167 -9.299 16.275 1.00 13.41 N ANISOU 414 N ASP A 52 1707 1970 1417 -362 -108 253 N ATOM 415 CA ASP A 52 -28.012 -8.687 14.960 1.00 14.47 C ANISOU 415 CA ASP A 52 1852 2086 1560 -342 -113 238 C ATOM 416 C ASP A 52 -29.359 -8.338 14.337 1.00 14.05 C ANISOU 416 C ASP A 52 1763 2100 1475 -352 -129 229 C ATOM 417 O ASP A 52 -29.467 -7.332 13.628 1.00 14.82 O ANISOU 417 O ASP A 52 1856 2205 1569 -313 -141 218 O ATOM 418 CB ASP A 52 -27.211 -9.616 14.047 1.00 15.87 C ANISOU 418 CB ASP A 52 2081 2194 1754 -369 -102 237 C ATOM 419 CG ASP A 52 -25.751 -9.723 14.463 1.00 21.46 C ANISOU 419 CG ASP A 52 2819 2836 2500 -342 -91 236 C ATOM 420 OD1 ASP A 52 -25.218 -8.741 15.023 1.00 22.21 O ANISOU 420 OD1 ASP A 52 2896 2931 2611 -296 -92 230 O ATOM 421 OD2 ASP A 52 -25.134 -10.784 14.235 1.00 24.73 O ANISOU 421 OD2 ASP A 52 3270 3197 2928 -366 -83 238 O ATOM 422 N ILE A 53 -30.394 -9.144 14.588 1.00 15.79 N ANISOU 422 N ILE A 53 1959 2369 1669 -404 -130 232 N ATOM 423 CA ILE A 53 -31.739 -8.762 14.165 1.00 14.53 C ANISOU 423 CA ILE A 53 1750 2289 1481 -410 -148 217 C ATOM 424 C ILE A 53 -32.135 -7.437 14.805 1.00 15.76 C ANISOU 424 C ILE A 53 1859 2497 1633 -349 -160 207 C ATOM 425 O ILE A 53 -32.695 -6.552 14.144 1.00 15.78 O ANISOU 425 O ILE A 53 1839 2532 1624 -310 -182 192 O ATOM 426 CB ILE A 53 -32.749 -9.875 14.504 1.00 17.59 C ANISOU 426 CB ILE A 53 2112 2724 1846 -484 -141 217 C ATOM 427 CG1 ILE A 53 -32.462 -11.127 13.671 1.00 16.26 C ANISOU 427 CG1 ILE A 53 1995 2501 1680 -544 -134 222 C ATOM 428 CG2 ILE A 53 -34.175 -9.391 14.261 1.00 20.93 C ANISOU 428 CG2 ILE A 53 2467 3245 2242 -485 -161 194 C ATOM 429 CD1 ILE A 53 -33.237 -12.354 14.116 1.00 19.52 C ANISOU 429 CD1 ILE A 53 2400 2941 2075 -627 -120 226 C ATOM 430 N LEU A 54 -31.851 -7.278 16.101 1.00 14.30 N ANISOU 430 N LEU A 54 1661 2320 1454 -335 -147 215 N ATOM 431 CA LEU A 54 -32.185 -6.039 16.791 1.00 15.11 C ANISOU 431 CA LEU A 54 1719 2468 1552 -276 -156 202 C ATOM 432 C LEU A 54 -31.344 -4.863 16.311 1.00 16.22 C ANISOU 432 C LEU A 54 1887 2558 1716 -210 -165 196 C ATOM 433 O LEU A 54 -31.769 -3.714 16.462 1.00 13.44 O ANISOU 433 O LEU A 54 1506 2240 1359 -157 -180 181 O ATOM 434 CB LEU A 54 -32.021 -6.218 18.301 1.00 15.15 C ANISOU 434 CB LEU A 54 1712 2491 1555 -282 -139 210 C ATOM 435 CG LEU A 54 -33.026 -7.165 18.963 1.00 17.19 C ANISOU 435 CG LEU A 54 1937 2811 1782 -347 -124 214 C ATOM 436 CD1 LEU A 54 -32.718 -7.328 20.443 1.00 19.72 C ANISOU 436 CD1 LEU A 54 2260 3138 2094 -350 -106 227 C ATOM 437 CD2 LEU A 54 -34.448 -6.665 18.767 1.00 18.90 C ANISOU 437 CD2 LEU A 54 2083 3124 1976 -343 -136 187 C ATOM 438 N VAL A 55 -30.162 -5.112 15.744 1.00 15.26 N ANISOU 438 N VAL A 55 1822 2357 1620 -214 -155 205 N ATOM 439 CA VAL A 55 -29.408 -4.019 15.138 1.00 12.82 C ANISOU 439 CA VAL A 55 1543 1999 1330 -163 -159 198 C ATOM 440 C VAL A 55 -30.183 -3.439 13.961 1.00 12.28 C ANISOU 440 C VAL A 55 1475 1952 1240 -144 -180 191 C ATOM 441 O VAL A 55 -30.284 -2.215 13.806 1.00 14.50 O ANISOU 441 O VAL A 55 1755 2234 1519 -89 -194 183 O ATOM 442 CB VAL A 55 -28.005 -4.496 14.716 1.00 13.42 C ANISOU 442 CB VAL A 55 1673 1991 1436 -178 -139 204 C ATOM 443 CG1 VAL A 55 -27.375 -3.506 13.747 1.00 14.42 C ANISOU 443 CG1 VAL A 55 1834 2069 1575 -144 -136 197 C ATOM 444 CG2 VAL A 55 -27.117 -4.669 15.938 1.00 15.51 C ANISOU 444 CG2 VAL A 55 1935 2233 1724 -171 -126 206 C ATOM 445 N GLY A 56 -30.763 -4.304 13.129 1.00 12.29 N ANISOU 445 N GLY A 56 1479 1969 1221 -188 -187 193 N ATOM 446 CA GLY A 56 -31.517 -3.813 11.989 1.00 16.67 C ANISOU 446 CA GLY A 56 2035 2548 1750 -169 -215 184 C ATOM 447 C GLY A 56 -32.850 -3.211 12.387 1.00 13.80 C ANISOU 447 C GLY A 56 1607 2273 1363 -137 -243 169 C ATOM 448 O GLY A 56 -33.291 -2.218 11.803 1.00 15.70 O ANISOU 448 O GLY A 56 1849 2528 1590 -84 -270 160 O ATOM 449 N VAL A 57 -33.501 -3.792 13.395 1.00 16.85 N ANISOU 449 N VAL A 57 1938 2720 1744 -168 -235 164 N ATOM 450 CA VAL A 57 -34.842 -3.356 13.767 1.00 14.56 C ANISOU 450 CA VAL A 57 1575 2525 1432 -146 -258 141 C ATOM 451 C VAL A 57 -34.801 -2.089 14.616 1.00 16.90 C ANISOU 451 C VAL A 57 1849 2834 1737 -75 -262 132 C ATOM 452 O VAL A 57 -35.667 -1.219 14.483 1.00 16.09 O ANISOU 452 O VAL A 57 1709 2785 1621 -21 -291 111 O ATOM 453 CB VAL A 57 -35.584 -4.494 14.492 1.00 19.36 C ANISOU 453 CB VAL A 57 2133 3195 2028 -218 -241 137 C ATOM 454 CG1 VAL A 57 -36.902 -3.992 15.067 1.00 25.28 C ANISOU 454 CG1 VAL A 57 2796 4050 2758 -195 -256 108 C ATOM 455 CG2 VAL A 57 -35.823 -5.662 13.545 1.00 22.00 C ANISOU 455 CG2 VAL A 57 2485 3523 2351 -287 -243 139 C ATOM 456 N LEU A 58 -33.813 -1.962 15.506 1.00 14.80 N ANISOU 456 N LEU A 58 1607 2522 1494 -70 -236 143 N ATOM 457 CA LEU A 58 -33.785 -0.867 16.471 1.00 14.87 C ANISOU 457 CA LEU A 58 1593 2546 1510 -10 -237 130 C ATOM 458 C LEU A 58 -32.528 -0.014 16.384 1.00 14.46 C ANISOU 458 C LEU A 58 1600 2408 1486 31 -230 137 C ATOM 459 O LEU A 58 -32.628 1.217 16.304 1.00 13.05 O ANISOU 459 O LEU A 58 1425 2224 1310 95 -247 124 O ATOM 460 CB LEU A 58 -33.932 -1.425 17.898 1.00 16.71 C ANISOU 460 CB LEU A 58 1786 2823 1739 -43 -213 129 C ATOM 461 CG LEU A 58 -35.296 -2.008 18.279 1.00 18.52 C ANISOU 461 CG LEU A 58 1945 3153 1940 -79 -213 114 C ATOM 462 CD1 LEU A 58 -35.267 -2.539 19.704 1.00 20.15 C ANISOU 462 CD1 LEU A 58 2130 3389 2138 -114 -182 118 C ATOM 463 CD2 LEU A 58 -36.401 -0.975 18.122 1.00 23.80 C ANISOU 463 CD2 LEU A 58 2555 3893 2594 -17 -242 81 C ATOM 464 N ALA A 59 -31.340 -0.624 16.403 1.00 12.21 N ANISOU 464 N ALA A 59 1360 2056 1224 -5 -206 154 N ATOM 465 CA ALA A 59 -30.117 0.169 16.505 1.00 13.95 C ANISOU 465 CA ALA A 59 1623 2203 1474 28 -195 154 C ATOM 466 C ALA A 59 -29.924 1.064 15.287 1.00 13.45 C ANISOU 466 C ALA A 59 1607 2093 1412 62 -207 154 C ATOM 467 O ALA A 59 -29.490 2.215 15.416 1.00 13.51 O ANISOU 467 O ALA A 59 1635 2066 1433 109 -207 145 O ATOM 468 CB ALA A 59 -28.904 -0.744 16.685 1.00 15.34 C ANISOU 468 CB ALA A 59 1831 2321 1674 -16 -170 167 C ATOM 469 N ILE A 60 -30.226 0.558 14.096 1.00 14.66 N ANISOU 469 N ILE A 60 1782 2240 1548 38 -215 163 N ATOM 470 CA ILE A 60 -29.988 1.319 12.871 1.00 14.77 C ANISOU 470 CA ILE A 60 1852 2204 1555 65 -224 168 C ATOM 471 C ILE A 60 -31.007 2.452 12.775 1.00 13.37 C ANISOU 471 C ILE A 60 1657 2066 1355 131 -259 157 C ATOM 472 O ILE A 60 -30.620 3.600 12.513 1.00 13.84 O ANISOU 472 O ILE A 60 1761 2078 1421 178 -262 156 O ATOM 473 CB ILE A 60 -30.010 0.403 11.638 1.00 13.66 C ANISOU 473 CB ILE A 60 1743 2049 1397 19 -223 179 C ATOM 474 CG1 ILE A 60 -28.674 -0.346 11.550 1.00 15.29 C ANISOU 474 CG1 ILE A 60 1987 2189 1633 -27 -185 186 C ATOM 475 CG2 ILE A 60 -30.276 1.209 10.373 1.00 16.92 C ANISOU 475 CG2 ILE A 60 2205 2440 1784 55 -245 184 C ATOM 476 CD1 ILE A 60 -28.603 -1.403 10.470 1.00 15.80 C ANISOU 476 CD1 ILE A 60 2081 2238 1685 -77 -180 194 C ATOM 477 N PRO A 61 -32.301 2.200 12.975 1.00 14.06 N ANISOU 477 N PRO A 61 1684 2240 1418 139 -287 145 N ATOM 478 CA PRO A 61 -33.237 3.332 13.085 1.00 17.17 C ANISOU 478 CA PRO A 61 2052 2676 1796 213 -322 128 C ATOM 479 C PRO A 61 -32.825 4.345 14.140 1.00 15.75 C ANISOU 479 C PRO A 61 1869 2477 1639 260 -312 115 C ATOM 480 O PRO A 61 -32.951 5.555 13.912 1.00 16.44 O ANISOU 480 O PRO A 61 1983 2540 1723 326 -332 108 O ATOM 481 CB PRO A 61 -34.566 2.646 13.424 1.00 17.79 C ANISOU 481 CB PRO A 61 2046 2860 1852 197 -341 110 C ATOM 482 CG PRO A 61 -34.455 1.306 12.787 1.00 18.32 C ANISOU 482 CG PRO A 61 2123 2925 1913 120 -329 124 C ATOM 483 CD PRO A 61 -33.008 0.907 12.922 1.00 15.44 C ANISOU 483 CD PRO A 61 1815 2476 1577 81 -289 145 C ATOM 484 N PHE A 62 -32.325 3.887 15.292 1.00 15.29 N ANISOU 484 N PHE A 62 1783 2427 1602 228 -282 112 N ATOM 485 CA PHE A 62 -31.808 4.815 16.293 1.00 14.10 C ANISOU 485 CA PHE A 62 1632 2253 1472 267 -271 97 C ATOM 486 C PHE A 62 -30.643 5.626 15.737 1.00 17.78 C ANISOU 486 C PHE A 62 2177 2619 1961 282 -259 105 C ATOM 487 O PHE A 62 -30.585 6.849 15.910 1.00 15.61 O ANISOU 487 O PHE A 62 1922 2315 1692 338 -267 92 O ATOM 488 CB PHE A 62 -31.375 4.055 17.553 1.00 14.26 C ANISOU 488 CB PHE A 62 1618 2295 1506 225 -244 95 C ATOM 489 CG PHE A 62 -32.516 3.469 18.350 1.00 13.81 C ANISOU 489 CG PHE A 62 1485 2337 1424 212 -249 83 C ATOM 490 CD1 PHE A 62 -33.839 3.727 18.019 1.00 18.47 C ANISOU 490 CD1 PHE A 62 2030 2999 1990 242 -276 67 C ATOM 491 CD2 PHE A 62 -32.256 2.662 19.448 1.00 14.27 C ANISOU 491 CD2 PHE A 62 1519 2420 1484 168 -225 87 C ATOM 492 CE1 PHE A 62 -34.872 3.184 18.760 1.00 18.10 C ANISOU 492 CE1 PHE A 62 1908 3048 1922 222 -274 51 C ATOM 493 CE2 PHE A 62 -33.287 2.118 20.193 1.00 17.66 C ANISOU 493 CE2 PHE A 62 1883 2938 1887 147 -221 76 C ATOM 494 CZ PHE A 62 -34.595 2.380 19.849 1.00 20.49 C ANISOU 494 CZ PHE A 62 2191 3370 2223 171 -243 57 C ATOM 495 N ALA A 63 -29.697 4.958 15.069 1.00 14.95 N ANISOU 495 N ALA A 63 1862 2203 1614 230 -235 124 N ATOM 496 CA ALA A 63 -28.556 5.672 14.503 1.00 15.81 C ANISOU 496 CA ALA A 63 2043 2221 1745 234 -215 129 C ATOM 497 C ALA A 63 -29.003 6.693 13.462 1.00 15.54 C ANISOU 497 C ALA A 63 2061 2156 1688 282 -238 135 C ATOM 498 O ALA A 63 -28.505 7.823 13.434 1.00 16.20 O ANISOU 498 O ALA A 63 2191 2180 1784 315 -232 130 O ATOM 499 CB ALA A 63 -27.567 4.683 13.888 1.00 14.64 C ANISOU 499 CB ALA A 63 1925 2027 1611 170 -185 143 C ATOM 500 N ILE A 64 -29.935 6.310 12.589 1.00 17.09 N ANISOU 500 N ILE A 64 2255 2391 1850 286 -267 146 N ATOM 501 CA ILE A 64 -30.470 7.261 11.620 1.00 15.95 C ANISOU 501 CA ILE A 64 2161 2223 1675 340 -298 153 C ATOM 502 C ILE A 64 -31.062 8.465 12.339 1.00 19.66 C ANISOU 502 C ILE A 64 2613 2709 2147 418 -324 133 C ATOM 503 O ILE A 64 -30.833 9.617 11.952 1.00 17.10 O ANISOU 503 O ILE A 64 2355 2321 1820 463 -330 136 O ATOM 504 CB ILE A 64 -31.510 6.570 10.717 1.00 16.12 C ANISOU 504 CB ILE A 64 2166 2302 1658 336 -333 161 C ATOM 505 CG1 ILE A 64 -30.820 5.549 9.811 1.00 14.53 C ANISOU 505 CG1 ILE A 64 2003 2066 1453 265 -307 179 C ATOM 506 CG2 ILE A 64 -32.272 7.604 9.893 1.00 21.67 C ANISOU 506 CG2 ILE A 64 2910 2997 2325 410 -379 164 C ATOM 507 CD1 ILE A 64 -31.773 4.600 9.118 1.00 17.35 C ANISOU 507 CD1 ILE A 64 2329 2487 1776 243 -335 181 C ATOM 508 N THR A 65 -31.819 8.216 13.406 1.00 16.43 N ANISOU 508 N THR A 65 2120 2383 1741 432 -336 111 N ATOM 509 CA THR A 65 -32.426 9.306 14.160 1.00 20.91 C ANISOU 509 CA THR A 65 2662 2973 2310 507 -358 85 C ATOM 510 C THR A 65 -31.361 10.203 14.781 1.00 21.43 C ANISOU 510 C THR A 65 2772 2963 2409 517 -330 77 C ATOM 511 O THR A 65 -31.479 11.434 14.748 1.00 17.61 O ANISOU 511 O THR A 65 2328 2439 1924 581 -347 67 O ATOM 512 CB THR A 65 -33.345 8.730 15.237 1.00 21.46 C ANISOU 512 CB THR A 65 2628 3151 2375 506 -365 60 C ATOM 513 OG1 THR A 65 -34.388 7.968 14.616 1.00 25.98 O ANISOU 513 OG1 THR A 65 3158 3796 2919 495 -392 62 O ATOM 514 CG2 THR A 65 -33.956 9.833 16.077 1.00 25.05 C ANISOU 514 CG2 THR A 65 3052 3634 2832 585 -385 27 C ATOM 515 N ILE A 66 -30.311 9.601 15.346 1.00 18.45 N ANISOU 515 N ILE A 66 2389 2563 2060 456 -289 79 N ATOM 516 CA ILE A 66 -29.236 10.377 15.961 1.00 19.17 C ANISOU 516 CA ILE A 66 2513 2587 2185 457 -262 65 C ATOM 517 C ILE A 66 -28.584 11.298 14.939 1.00 19.98 C ANISOU 517 C ILE A 66 2712 2589 2289 468 -254 79 C ATOM 518 O ILE A 66 -28.201 12.429 15.259 1.00 22.02 O ANISOU 518 O ILE A 66 3010 2793 2565 500 -249 63 O ATOM 519 CB ILE A 66 -28.194 9.437 16.599 1.00 23.17 C ANISOU 519 CB ILE A 66 2996 3090 2719 388 -225 65 C ATOM 520 CG1 ILE A 66 -28.783 8.684 17.796 1.00 28.49 C ANISOU 520 CG1 ILE A 66 3585 3853 3386 381 -231 51 C ATOM 521 CG2 ILE A 66 -26.954 10.221 17.007 1.00 29.59 C ANISOU 521 CG2 ILE A 66 3847 3827 3568 383 -198 48 C ATOM 522 CD1 ILE A 66 -29.231 9.570 18.925 1.00 42.53 C ANISOU 522 CD1 ILE A 66 5330 5664 5166 436 -242 19 C ATOM 523 N SER A 67 -28.434 10.828 13.697 1.00 18.60 N ANISOU 523 N SER A 67 2583 2386 2097 436 -250 107 N ATOM 524 CA SER A 67 -27.702 11.602 12.699 1.00 21.25 C ANISOU 524 CA SER A 67 3019 2624 2432 432 -232 123 C ATOM 525 C SER A 67 -28.389 12.917 12.363 1.00 22.02 C ANISOU 525 C SER A 67 3170 2690 2506 511 -267 124 C ATOM 526 O SER A 67 -27.750 13.801 11.783 1.00 21.40 O ANISOU 526 O SER A 67 3182 2519 2429 513 -249 134 O ATOM 527 CB SER A 67 -27.514 10.783 11.419 1.00 19.70 C ANISOU 527 CB SER A 67 2860 2412 2212 384 -222 152 C ATOM 528 OG SER A 67 -28.716 10.713 10.670 1.00 21.65 O ANISOU 528 OG SER A 67 3110 2703 2414 425 -269 166 O ATOM 529 N THR A 68 -29.670 13.075 12.710 1.00 26.23 N ANISOU 529 N THR A 68 3652 3295 3018 576 -315 112 N ATOM 530 CA THR A 68 -30.375 14.314 12.402 1.00 25.25 C ANISOU 530 CA THR A 68 3578 3142 2872 663 -355 110 C ATOM 531 C THR A 68 -30.145 15.397 13.448 1.00 23.50 C ANISOU 531 C THR A 68 3359 2889 2680 705 -349 79 C ATOM 532 O THR A 68 -30.358 16.577 13.151 1.00 27.23 O ANISOU 532 O THR A 68 3902 3302 3143 769 -370 79 O ATOM 533 CB THR A 68 -31.883 14.066 12.271 1.00 28.28 C ANISOU 533 CB THR A 68 3901 3622 3222 724 -413 103 C ATOM 534 OG1 THR A 68 -32.453 13.830 13.565 1.00 22.44 O ANISOU 534 OG1 THR A 68 3057 2969 2499 740 -418 67 O ATOM 535 CG2 THR A 68 -32.161 12.871 11.371 1.00 28.43 C ANISOU 535 CG2 THR A 68 3903 3685 3214 675 -420 126 C ATOM 536 N GLY A 69 -29.717 15.034 14.654 1.00 25.22 N ANISOU 536 N GLY A 69 3509 3142 2931 673 -322 53 N ATOM 537 CA GLY A 69 -29.542 16.023 15.700 1.00 23.80 C ANISOU 537 CA GLY A 69 3326 2940 2776 712 -319 18 C ATOM 538 C GLY A 69 -30.838 16.617 16.202 1.00 26.14 C ANISOU 538 C GLY A 69 3580 3297 3056 805 -366 -8 C ATOM 539 O GLY A 69 -30.842 17.743 16.708 1.00 28.64 O ANISOU 539 O GLY A 69 3926 3573 3385 860 -373 -34 O ATOM 540 N PHE A 70 -31.941 15.882 16.081 1.00 27.81 N ANISOU 540 N PHE A 70 3721 3606 3241 823 -397 -7 N ATOM 541 CA PHE A 70 -33.247 16.403 16.458 1.00 29.00 C ANISOU 541 CA PHE A 70 3821 3824 3374 914 -443 -36 C ATOM 542 C PHE A 70 -33.288 16.752 17.942 1.00 25.29 C ANISOU 542 C PHE A 70 3290 3393 2926 935 -430 -82 C ATOM 543 O PHE A 70 -32.565 16.178 18.762 1.00 24.12 O ANISOU 543 O PHE A 70 3108 3259 2798 871 -391 -88 O ATOM 544 CB PHE A 70 -34.333 15.375 16.140 1.00 29.47 C ANISOU 544 CB PHE A 70 3800 3993 3405 910 -470 -33 C ATOM 545 CG PHE A 70 -34.389 14.235 17.117 1.00 25.79 C ANISOU 545 CG PHE A 70 3234 3617 2946 847 -442 -47 C ATOM 546 CD1 PHE A 70 -33.323 13.362 17.247 1.00 24.28 C ANISOU 546 CD1 PHE A 70 3052 3401 2774 754 -397 -25 C ATOM 547 CD2 PHE A 70 -35.509 14.036 17.907 1.00 30.82 C ANISOU 547 CD2 PHE A 70 3771 4366 3572 880 -459 -82 C ATOM 548 CE1 PHE A 70 -33.370 12.318 18.148 1.00 25.54 C ANISOU 548 CE1 PHE A 70 3132 3635 2937 700 -374 -34 C ATOM 549 CE2 PHE A 70 -35.564 12.991 18.804 1.00 27.29 C ANISOU 549 CE2 PHE A 70 3243 3997 3127 817 -430 -91 C ATOM 550 CZ PHE A 70 -34.493 12.131 18.926 1.00 28.93 C ANISOU 550 CZ PHE A 70 3470 4170 3350 728 -389 -64 C ATOM 551 N CYS A 71 -34.153 17.704 18.283 1.00 25.09 N ANISOU 551 N CYS A 71 3254 3387 2894 1030 -465 -115 N ATOM 552 CA CYS A 71 -34.341 18.086 19.676 1.00 28.86 C ANISOU 552 CA CYS A 71 3671 3910 3386 1059 -456 -164 C ATOM 553 C CYS A 71 -34.992 16.951 20.452 1.00 27.22 C ANISOU 553 C CYS A 71 3344 3834 3166 1023 -446 -179 C ATOM 554 O CYS A 71 -35.950 16.329 19.986 1.00 25.15 O ANISOU 554 O CYS A 71 3027 3649 2880 1031 -470 -174 O ATOM 555 CB CYS A 71 -35.208 19.341 19.770 1.00 32.89 C ANISOU 555 CB CYS A 71 4194 4412 3889 1176 -498 -199 C ATOM 556 SG CYS A 71 -34.485 20.802 19.012 1.00 34.19 S ANISOU 556 SG CYS A 71 4512 4413 4066 1222 -508 -183 S ATOM 557 N ALA A 72 -34.477 16.690 21.652 1.00 23.60 N ANISOU 557 N ALA A 72 2845 3399 2722 983 -410 -200 N ATOM 558 CA ALA A 72 -34.978 15.583 22.452 1.00 25.34 C ANISOU 558 CA ALA A 72 2966 3735 2927 938 -394 -210 C ATOM 559 C ALA A 72 -34.587 15.785 23.906 1.00 26.21 C ANISOU 559 C ALA A 72 3045 3866 3046 931 -366 -246 C ATOM 560 O ALA A 72 -33.572 16.420 24.208 1.00 27.36 O ANISOU 560 O ALA A 72 3249 3929 3216 926 -351 -252 O ATOM 561 CB ALA A 72 -34.432 14.245 21.945 1.00 26.81 C ANISOU 561 CB ALA A 72 3154 3923 3112 841 -371 -165 C ATOM 562 N ALA A 73 -35.404 15.236 24.801 1.00 28.94 N ANISOU 562 N ALA A 73 3300 4325 3371 927 -358 -272 N ATOM 563 CA ALA A 73 -35.016 15.148 26.201 1.00 25.22 C ANISOU 563 CA ALA A 73 2797 3887 2899 904 -328 -299 C ATOM 564 C ALA A 73 -33.704 14.384 26.306 1.00 21.74 C ANISOU 564 C ALA A 73 2394 3393 2472 817 -299 -264 C ATOM 565 O ALA A 73 -33.526 13.347 25.661 1.00 19.61 O ANISOU 565 O ALA A 73 2126 3125 2199 755 -293 -222 O ATOM 566 CB ALA A 73 -36.111 14.457 27.013 1.00 27.92 C ANISOU 566 CB ALA A 73 3038 4363 3208 896 -317 -323 C ATOM 567 N CYS A 74 -32.777 14.900 27.115 1.00 21.01 N ANISOU 567 N CYS A 74 2331 3254 2397 814 -284 -284 N ATOM 568 CA CYS A 74 -31.408 14.395 27.065 1.00 24.94 C ANISOU 568 CA CYS A 74 2873 3686 2916 744 -264 -257 C ATOM 569 C CYS A 74 -31.342 12.909 27.394 1.00 21.81 C ANISOU 569 C CYS A 74 2435 3351 2500 670 -246 -227 C ATOM 570 O CYS A 74 -30.608 12.158 26.743 1.00 17.57 O ANISOU 570 O CYS A 74 1927 2771 1977 614 -238 -189 O ATOM 571 CB CYS A 74 -30.513 15.190 28.012 1.00 30.09 C ANISOU 571 CB CYS A 74 3550 4294 3587 755 -255 -293 C ATOM 572 SG CYS A 74 -28.763 14.774 27.824 1.00 26.16 S ANISOU 572 SG CYS A 74 3106 3709 3126 680 -236 -270 S ATOM 573 N HIS A 75 -32.101 12.461 28.397 1.00 20.80 N ANISOU 573 N HIS A 75 2242 3322 2340 669 -237 -245 N ATOM 574 CA HIS A 75 -32.027 11.055 28.785 1.00 27.04 C ANISOU 574 CA HIS A 75 3004 4163 3108 596 -218 -216 C ATOM 575 C HIS A 75 -32.722 10.153 27.773 1.00 24.16 C ANISOU 575 C HIS A 75 2621 3827 2733 563 -222 -180 C ATOM 576 O HIS A 75 -32.356 8.981 27.638 1.00 21.77 O ANISOU 576 O HIS A 75 2322 3524 2424 496 -209 -144 O ATOM 577 CB HIS A 75 -32.622 10.859 30.178 1.00 28.29 C ANISOU 577 CB HIS A 75 3106 4416 3228 597 -202 -245 C ATOM 578 CG HIS A 75 -31.792 11.453 31.272 1.00 31.17 C ANISOU 578 CG HIS A 75 3490 4758 3597 613 -197 -275 C ATOM 579 ND1 HIS A 75 -31.879 12.779 31.636 1.00 36.03 N ANISOU 579 ND1 HIS A 75 4111 5355 4222 681 -207 -324 N ATOM 580 CD2 HIS A 75 -30.848 10.904 32.072 1.00 29.97 C ANISOU 580 CD2 HIS A 75 3354 4594 3438 570 -187 -266 C ATOM 581 CE1 HIS A 75 -31.031 13.020 32.619 1.00 34.87 C ANISOU 581 CE1 HIS A 75 3981 5191 4075 675 -202 -346 C ATOM 582 NE2 HIS A 75 -30.392 11.899 32.902 1.00 32.96 N ANISOU 582 NE2 HIS A 75 3745 4956 3823 611 -191 -312 N ATOM 583 N GLY A 76 -33.722 10.671 27.058 1.00 22.96 N ANISOU 583 N GLY A 76 2449 3699 2577 612 -242 -192 N ATOM 584 CA GLY A 76 -34.271 9.921 25.941 1.00 25.23 C ANISOU 584 CA GLY A 76 2728 4002 2858 584 -252 -161 C ATOM 585 C GLY A 76 -33.273 9.793 24.807 1.00 20.09 C ANISOU 585 C GLY A 76 2150 3250 2234 557 -257 -124 C ATOM 586 O GLY A 76 -33.105 8.717 24.230 1.00 16.75 O ANISOU 586 O GLY A 76 1733 2823 1807 496 -249 -89 O ATOM 587 N CYS A 77 -32.596 10.894 24.474 1.00 18.91 N ANISOU 587 N CYS A 77 2059 3014 2110 600 -267 -132 N ATOM 588 CA CYS A 77 -31.498 10.833 23.520 1.00 19.09 C ANISOU 588 CA CYS A 77 2154 2939 2160 568 -262 -101 C ATOM 589 C CYS A 77 -30.437 9.840 23.972 1.00 17.03 C ANISOU 589 C CYS A 77 1900 2661 1910 496 -235 -82 C ATOM 590 O CYS A 77 -29.903 9.071 23.163 1.00 15.75 O ANISOU 590 O CYS A 77 1765 2461 1756 447 -228 -50 O ATOM 591 CB CYS A 77 -30.890 12.222 23.355 1.00 19.90 C ANISOU 591 CB CYS A 77 2318 2956 2288 618 -268 -120 C ATOM 592 SG CYS A 77 -29.469 12.261 22.264 1.00 22.22 S ANISOU 592 SG CYS A 77 2699 3129 2614 573 -252 -89 S ATOM 593 N LEU A 78 -30.128 9.840 25.268 1.00 13.49 N ANISOU 593 N LEU A 78 1426 2240 1459 493 -224 -104 N ATOM 594 CA LEU A 78 -29.110 8.944 25.800 1.00 15.43 C ANISOU 594 CA LEU A 78 1678 2470 1713 435 -206 -89 C ATOM 595 C LEU A 78 -29.477 7.485 25.558 1.00 15.91 C ANISOU 595 C LEU A 78 1717 2574 1752 377 -198 -54 C ATOM 596 O LEU A 78 -28.615 6.669 25.209 1.00 14.12 O ANISOU 596 O LEU A 78 1518 2305 1541 330 -189 -28 O ATOM 597 CB LEU A 78 -28.933 9.224 27.293 1.00 19.05 C ANISOU 597 CB LEU A 78 2111 2965 2161 450 -201 -121 C ATOM 598 CG LEU A 78 -27.748 8.621 28.045 1.00 18.55 C ANISOU 598 CG LEU A 78 2061 2881 2107 410 -191 -117 C ATOM 599 CD1 LEU A 78 -26.418 8.990 27.396 1.00 17.17 C ANISOU 599 CD1 LEU A 78 1936 2610 1979 399 -189 -117 C ATOM 600 CD2 LEU A 78 -27.792 9.097 29.491 1.00 17.15 C ANISOU 600 CD2 LEU A 78 1859 2748 1910 437 -191 -154 C ATOM 601 N PHE A 79 -30.756 7.137 25.721 1.00 15.53 N ANISOU 601 N PHE A 79 1618 2610 1670 380 -201 -56 N ATOM 602 CA PHE A 79 -31.162 5.741 25.589 1.00 16.14 C ANISOU 602 CA PHE A 79 1675 2730 1726 318 -191 -26 C ATOM 603 C PHE A 79 -30.934 5.227 24.172 1.00 14.31 C ANISOU 603 C PHE A 79 1478 2448 1509 289 -196 5 C ATOM 604 O PHE A 79 -30.343 4.159 23.978 1.00 16.33 O ANISOU 604 O PHE A 79 1755 2679 1770 233 -185 32 O ATOM 605 CB PHE A 79 -32.628 5.571 25.985 1.00 19.22 C ANISOU 605 CB PHE A 79 1999 3225 2079 323 -190 -41 C ATOM 606 CG PHE A 79 -33.139 4.173 25.788 1.00 20.08 C ANISOU 606 CG PHE A 79 2087 3377 2166 253 -177 -13 C ATOM 607 CD1 PHE A 79 -32.929 3.203 26.753 1.00 26.26 C ANISOU 607 CD1 PHE A 79 2866 4185 2926 200 -154 2 C ATOM 608 CD2 PHE A 79 -33.813 3.823 24.631 1.00 20.08 C ANISOU 608 CD2 PHE A 79 2078 3389 2164 239 -189 -2 C ATOM 609 CE1 PHE A 79 -33.391 1.913 26.572 1.00 24.15 C ANISOU 609 CE1 PHE A 79 2589 3949 2638 131 -140 29 C ATOM 610 CE2 PHE A 79 -34.276 2.535 24.444 1.00 20.30 C ANISOU 610 CE2 PHE A 79 2088 3452 2172 169 -176 20 C ATOM 611 CZ PHE A 79 -34.064 1.579 25.416 1.00 26.37 C ANISOU 611 CZ PHE A 79 2856 4241 2922 114 -150 36 C ATOM 612 N ILE A 80 -31.407 5.965 23.164 1.00 12.72 N ANISOU 612 N ILE A 80 1287 2232 1314 328 -215 -1 N ATOM 613 CA ILE A 80 -31.246 5.499 21.792 1.00 16.92 C ANISOU 613 CA ILE A 80 1855 2720 1853 301 -221 27 C ATOM 614 C ILE A 80 -29.788 5.548 21.361 1.00 15.94 C ANISOU 614 C ILE A 80 1794 2499 1762 282 -208 40 C ATOM 615 O ILE A 80 -29.391 4.818 20.447 1.00 15.05 O ANISOU 615 O ILE A 80 1712 2350 1656 241 -202 65 O ATOM 616 CB ILE A 80 -32.125 6.308 20.819 1.00 13.97 C ANISOU 616 CB ILE A 80 1483 2354 1470 353 -249 18 C ATOM 617 CG1 ILE A 80 -31.731 7.785 20.820 1.00 15.32 C ANISOU 617 CG1 ILE A 80 1693 2470 1660 419 -259 -2 C ATOM 618 CG2 ILE A 80 -33.595 6.147 21.180 1.00 20.07 C ANISOU 618 CG2 ILE A 80 2181 3234 2212 368 -262 -2 C ATOM 619 CD1 ILE A 80 -32.433 8.599 19.753 1.00 24.54 C ANISOU 619 CD1 ILE A 80 2882 3625 2817 475 -290 -4 C ATOM 620 N ALA A 81 -28.974 6.389 22.000 1.00 15.44 N ANISOU 620 N ALA A 81 1750 2395 1722 309 -202 21 N ATOM 621 CA ALA A 81 -27.547 6.392 21.703 1.00 14.31 C ANISOU 621 CA ALA A 81 1655 2168 1612 285 -186 26 C ATOM 622 C ALA A 81 -26.851 5.171 22.287 1.00 16.92 C ANISOU 622 C ALA A 81 1976 2504 1948 233 -172 39 C ATOM 623 O ALA A 81 -25.927 4.632 21.669 1.00 15.94 O ANISOU 623 O ALA A 81 1883 2326 1846 199 -160 52 O ATOM 624 CB ALA A 81 -26.904 7.670 22.237 1.00 17.46 C ANISOU 624 CB ALA A 81 2073 2525 2035 325 -184 -5 C ATOM 625 N CYS A 82 -27.290 4.707 23.458 1.00 16.31 N ANISOU 625 N CYS A 82 1858 2491 1849 228 -173 35 N ATOM 626 CA CYS A 82 -26.607 3.636 24.170 1.00 15.10 C ANISOU 626 CA CYS A 82 1703 2339 1695 188 -165 47 C ATOM 627 C CYS A 82 -27.136 2.247 23.843 1.00 15.04 C ANISOU 627 C CYS A 82 1690 2359 1665 138 -160 79 C ATOM 628 O CYS A 82 -26.472 1.259 24.176 1.00 12.83 O ANISOU 628 O CYS A 82 1424 2061 1388 103 -154 95 O ATOM 629 CB CYS A 82 -26.718 3.852 25.684 1.00 16.49 C ANISOU 629 CB CYS A 82 1850 2563 1851 207 -167 28 C ATOM 630 SG CYS A 82 -25.791 5.263 26.310 1.00 21.14 S ANISOU 630 SG CYS A 82 2451 3112 2471 255 -172 -15 S ATOM 631 N PHE A 83 -28.306 2.134 23.213 1.00 12.39 N ANISOU 631 N PHE A 83 1334 2066 1307 133 -164 87 N ATOM 632 CA PHE A 83 -28.907 0.815 23.049 1.00 13.38 C ANISOU 632 CA PHE A 83 1449 2226 1409 78 -158 112 C ATOM 633 C PHE A 83 -28.009 -0.110 22.234 1.00 12.99 C ANISOU 633 C PHE A 83 1444 2110 1381 38 -152 134 C ATOM 634 O PHE A 83 -27.926 -1.309 22.520 1.00 10.99 O ANISOU 634 O PHE A 83 1199 1860 1118 -8 -144 155 O ATOM 635 CB PHE A 83 -30.284 0.931 22.401 1.00 14.10 C ANISOU 635 CB PHE A 83 1506 2375 1476 81 -167 108 C ATOM 636 CG PHE A 83 -30.994 -0.383 22.281 1.00 15.05 C ANISOU 636 CG PHE A 83 1610 2536 1571 18 -159 127 C ATOM 637 CD1 PHE A 83 -31.525 -1.001 23.400 1.00 18.06 C ANISOU 637 CD1 PHE A 83 1960 2977 1923 -12 -145 130 C ATOM 638 CD2 PHE A 83 -31.115 -1.010 21.054 1.00 14.70 C ANISOU 638 CD2 PHE A 83 1586 2470 1531 -14 -163 142 C ATOM 639 CE1 PHE A 83 -32.170 -2.217 23.295 1.00 19.44 C ANISOU 639 CE1 PHE A 83 2126 3186 2076 -78 -133 148 C ATOM 640 CE2 PHE A 83 -31.761 -2.224 20.944 1.00 14.91 C ANISOU 640 CE2 PHE A 83 1600 2530 1536 -77 -155 157 C ATOM 641 CZ PHE A 83 -32.287 -2.829 22.066 1.00 15.80 C ANISOU 641 CZ PHE A 83 1683 2699 1622 -111 -139 160 C ATOM 642 N VAL A 84 -27.324 0.425 21.218 1.00 11.93 N ANISOU 642 N VAL A 84 1343 1913 1276 53 -153 130 N ATOM 643 CA VAL A 84 -26.429 -0.412 20.423 1.00 13.22 C ANISOU 643 CA VAL A 84 1547 2016 1461 17 -143 145 C ATOM 644 C VAL A 84 -25.291 -0.948 21.282 1.00 10.92 C ANISOU 644 C VAL A 84 1267 1694 1190 9 -137 145 C ATOM 645 O VAL A 84 -24.748 -2.022 21.004 1.00 10.54 O ANISOU 645 O VAL A 84 1242 1613 1151 -25 -131 160 O ATOM 646 CB VAL A 84 -25.891 0.368 19.206 1.00 13.94 C ANISOU 646 CB VAL A 84 1673 2049 1576 34 -139 138 C ATOM 647 CG1 VAL A 84 -24.882 1.413 19.642 1.00 13.79 C ANISOU 647 CG1 VAL A 84 1664 1988 1588 68 -133 115 C ATOM 648 CG2 VAL A 84 -25.267 -0.587 18.201 1.00 13.98 C ANISOU 648 CG2 VAL A 84 1714 2005 1594 -7 -127 152 C ATOM 649 N LEU A 85 -24.910 -0.218 22.335 1.00 11.09 N ANISOU 649 N LEU A 85 1274 1724 1218 42 -141 126 N ATOM 650 CA LEU A 85 -23.904 -0.737 23.257 1.00 11.88 C ANISOU 650 CA LEU A 85 1380 1804 1330 39 -144 124 C ATOM 651 C LEU A 85 -24.388 -2.022 23.914 1.00 12.10 C ANISOU 651 C LEU A 85 1407 1866 1324 5 -145 151 C ATOM 652 O LEU A 85 -23.599 -2.945 24.152 1.00 10.69 O ANISOU 652 O LEU A 85 1252 1654 1155 -11 -148 162 O ATOM 653 CB LEU A 85 -23.569 0.308 24.321 1.00 14.20 C ANISOU 653 CB LEU A 85 1655 2111 1628 81 -151 95 C ATOM 654 CG LEU A 85 -23.205 1.703 23.812 1.00 15.21 C ANISOU 654 CG LEU A 85 1787 2206 1785 114 -148 66 C ATOM 655 CD1 LEU A 85 -22.909 2.628 24.977 1.00 17.76 C ANISOU 655 CD1 LEU A 85 2092 2545 2110 150 -157 35 C ATOM 656 CD2 LEU A 85 -22.022 1.634 22.870 1.00 17.02 C ANISOU 656 CD2 LEU A 85 2046 2364 2057 99 -136 60 C ATOM 657 N VAL A 86 -25.688 -2.098 24.208 1.00 12.74 N ANISOU 657 N VAL A 86 1463 2012 1366 -7 -143 160 N ATOM 658 CA VAL A 86 -26.262 -3.316 24.771 1.00 12.85 C ANISOU 658 CA VAL A 86 1480 2058 1344 -51 -138 187 C ATOM 659 C VAL A 86 -26.095 -4.472 23.796 1.00 12.53 C ANISOU 659 C VAL A 86 1473 1975 1313 -96 -133 210 C ATOM 660 O VAL A 86 -25.678 -5.573 24.173 1.00 11.07 O ANISOU 660 O VAL A 86 1319 1765 1123 -123 -133 231 O ATOM 661 CB VAL A 86 -27.744 -3.096 25.125 1.00 13.65 C ANISOU 661 CB VAL A 86 1539 2244 1405 -61 -131 185 C ATOM 662 CG1 VAL A 86 -28.352 -4.371 25.682 1.00 15.64 C ANISOU 662 CG1 VAL A 86 1797 2527 1617 -119 -119 212 C ATOM 663 CG2 VAL A 86 -27.900 -1.947 26.109 1.00 11.95 C ANISOU 663 CG2 VAL A 86 1291 2069 1178 -13 -135 158 C ATOM 664 N LEU A 87 -26.416 -4.233 22.522 1.00 10.85 N ANISOU 664 N LEU A 87 1258 1751 1113 -102 -130 205 N ATOM 665 CA LEU A 87 -26.353 -5.298 21.527 1.00 12.00 C ANISOU 665 CA LEU A 87 1434 1860 1264 -146 -125 222 C ATOM 666 C LEU A 87 -24.913 -5.714 21.256 1.00 14.20 C ANISOU 666 C LEU A 87 1752 2061 1581 -139 -125 221 C ATOM 667 O LEU A 87 -24.631 -6.901 21.056 1.00 13.49 O ANISOU 667 O LEU A 87 1695 1939 1494 -172 -122 237 O ATOM 668 CB LEU A 87 -27.034 -4.842 20.237 1.00 12.52 C ANISOU 668 CB LEU A 87 1491 1936 1330 -148 -126 214 C ATOM 669 CG LEU A 87 -28.493 -4.394 20.371 1.00 14.81 C ANISOU 669 CG LEU A 87 1733 2307 1586 -147 -131 208 C ATOM 670 CD1 LEU A 87 -29.062 -3.984 19.015 1.00 17.49 C ANISOU 670 CD1 LEU A 87 2070 2652 1925 -142 -140 200 C ATOM 671 CD2 LEU A 87 -29.340 -5.491 20.992 1.00 11.31 C ANISOU 671 CD2 LEU A 87 1275 1912 1109 -202 -122 224 C ATOM 672 N ALA A 88 -23.988 -4.753 21.237 1.00 13.86 N ANISOU 672 N ALA A 88 1708 1989 1571 -97 -127 198 N ATOM 673 CA ALA A 88 -22.583 -5.101 21.053 1.00 13.85 C ANISOU 673 CA ALA A 88 1732 1923 1609 -88 -125 188 C ATOM 674 C ALA A 88 -22.067 -5.921 22.226 1.00 13.76 C ANISOU 674 C ALA A 88 1732 1906 1591 -86 -138 198 C ATOM 675 O ALA A 88 -21.292 -6.866 22.039 1.00 12.52 O ANISOU 675 O ALA A 88 1603 1702 1452 -95 -141 203 O ATOM 676 CB ALA A 88 -21.743 -3.838 20.877 1.00 11.88 C ANISOU 676 CB ALA A 88 1473 1649 1394 -50 -122 157 C ATOM 677 N GLN A 89 -22.488 -5.580 23.445 1.00 14.61 N ANISOU 677 N GLN A 89 1819 2061 1671 -71 -148 201 N ATOM 678 CA GLN A 89 -22.023 -6.325 24.608 1.00 13.60 C ANISOU 678 CA GLN A 89 1709 1929 1529 -65 -163 214 C ATOM 679 C GLN A 89 -22.575 -7.743 24.602 1.00 14.87 C ANISOU 679 C GLN A 89 1905 2085 1660 -113 -159 250 C ATOM 680 O GLN A 89 -21.856 -8.697 24.923 1.00 14.29 O ANISOU 680 O GLN A 89 1869 1969 1591 -112 -172 263 O ATOM 681 CB GLN A 89 -22.418 -5.602 25.893 1.00 12.06 C ANISOU 681 CB GLN A 89 1488 1790 1302 -41 -171 207 C ATOM 682 CG GLN A 89 -21.577 -6.010 27.079 1.00 17.56 C ANISOU 682 CG GLN A 89 2204 2476 1992 -18 -194 209 C ATOM 683 CD GLN A 89 -20.120 -5.660 26.877 1.00 17.23 C ANISOU 683 CD GLN A 89 2160 2385 2003 20 -208 177 C ATOM 684 OE1 GLN A 89 -19.795 -4.592 26.357 1.00 16.51 O ANISOU 684 OE1 GLN A 89 2041 2286 1945 39 -201 145 O ATOM 685 NE2 GLN A 89 -19.234 -6.570 27.259 1.00 20.29 N ANISOU 685 NE2 GLN A 89 2575 2735 2398 32 -229 183 N ATOM 686 N SER A 90 -23.851 -7.899 24.248 1.00 15.22 N ANISOU 686 N SER A 90 1939 2170 1674 -153 -144 265 N ATOM 687 CA SER A 90 -24.419 -9.234 24.108 1.00 12.76 C ANISOU 687 CA SER A 90 1661 1850 1337 -209 -136 296 C ATOM 688 C SER A 90 -23.631 -10.055 23.096 1.00 12.96 C ANISOU 688 C SER A 90 1724 1801 1397 -219 -137 297 C ATOM 689 O SER A 90 -23.333 -11.231 23.336 1.00 13.94 O ANISOU 689 O SER A 90 1896 1885 1515 -239 -141 319 O ATOM 690 CB SER A 90 -25.887 -9.133 23.695 1.00 17.22 C ANISOU 690 CB SER A 90 2194 2475 1871 -251 -119 300 C ATOM 691 OG SER A 90 -26.469 -10.420 23.560 1.00 16.04 O ANISOU 691 OG SER A 90 2077 2318 1698 -314 -108 327 O ATOM 692 N SER A 91 -23.284 -9.450 21.958 1.00 12.93 N ANISOU 692 N SER A 91 1707 1778 1428 -205 -131 273 N ATOM 693 CA SER A 91 -22.472 -10.145 20.966 1.00 13.92 C ANISOU 693 CA SER A 91 1866 1836 1587 -212 -128 267 C ATOM 694 C SER A 91 -21.148 -10.606 21.565 1.00 13.61 C ANISOU 694 C SER A 91 1851 1746 1574 -176 -144 261 C ATOM 695 O SER A 91 -20.701 -11.730 21.313 1.00 11.34 O ANISOU 695 O SER A 91 1604 1407 1296 -189 -147 270 O ATOM 696 CB SER A 91 -22.229 -9.233 19.761 1.00 14.70 C ANISOU 696 CB SER A 91 1946 1925 1714 -198 -117 240 C ATOM 697 OG SER A 91 -23.453 -8.839 19.156 1.00 14.09 O ANISOU 697 OG SER A 91 1849 1894 1610 -223 -109 245 O ATOM 698 N ILE A 92 -20.509 -9.751 22.365 1.00 14.36 N ANISOU 698 N ILE A 92 1920 1854 1682 -130 -157 243 N ATOM 699 CA ILE A 92 -19.239 -10.117 22.986 1.00 16.85 C ANISOU 699 CA ILE A 92 2250 2130 2023 -90 -179 232 C ATOM 700 C ILE A 92 -19.422 -11.327 23.895 1.00 14.17 C ANISOU 700 C ILE A 92 1956 1778 1648 -101 -196 267 C ATOM 701 O ILE A 92 -18.657 -12.297 23.830 1.00 15.88 O ANISOU 701 O ILE A 92 2211 1940 1882 -90 -210 270 O ATOM 702 CB ILE A 92 -18.655 -8.913 23.748 1.00 14.67 C ANISOU 702 CB ILE A 92 1934 1880 1761 -43 -191 203 C ATOM 703 CG1 ILE A 92 -18.041 -7.925 22.757 1.00 15.11 C ANISOU 703 CG1 ILE A 92 1960 1920 1863 -30 -173 164 C ATOM 704 CG2 ILE A 92 -17.618 -9.367 24.766 1.00 15.03 C ANISOU 704 CG2 ILE A 92 1993 1905 1815 -2 -223 196 C ATOM 705 CD1 ILE A 92 -17.883 -6.529 23.301 1.00 20.94 C ANISOU 705 CD1 ILE A 92 2659 2690 2609 0 -175 137 C ATOM 706 N PHE A 93 -20.440 -11.289 24.758 1.00 13.49 N ANISOU 706 N PHE A 93 1870 1743 1511 -124 -195 294 N ATOM 707 CA PHE A 93 -20.691 -12.420 25.647 1.00 17.89 C ANISOU 707 CA PHE A 93 2482 2289 2028 -143 -206 333 C ATOM 708 C PHE A 93 -20.960 -13.697 24.858 1.00 16.04 C ANISOU 708 C PHE A 93 2297 2005 1792 -190 -195 355 C ATOM 709 O PHE A 93 -20.427 -14.763 25.189 1.00 17.50 O ANISOU 709 O PHE A 93 2539 2135 1974 -184 -212 374 O ATOM 710 CB PHE A 93 -21.865 -12.108 26.579 1.00 18.92 C ANISOU 710 CB PHE A 93 2599 2489 2100 -171 -195 355 C ATOM 711 CG PHE A 93 -21.532 -11.126 27.675 1.00 22.57 C ANISOU 711 CG PHE A 93 3031 2993 2551 -122 -211 338 C ATOM 712 CD1 PHE A 93 -20.358 -11.242 28.404 1.00 28.77 C ANISOU 712 CD1 PHE A 93 3835 3747 3349 -70 -245 330 C ATOM 713 CD2 PHE A 93 -22.395 -10.084 27.972 1.00 18.01 C ANISOU 713 CD2 PHE A 93 2404 2487 1952 -126 -196 326 C ATOM 714 CE1 PHE A 93 -20.052 -10.340 29.407 1.00 31.58 C ANISOU 714 CE1 PHE A 93 4164 4143 3693 -27 -263 310 C ATOM 715 CE2 PHE A 93 -22.095 -9.180 28.972 1.00 19.72 C ANISOU 715 CE2 PHE A 93 2594 2739 2158 -83 -210 307 C ATOM 716 CZ PHE A 93 -20.921 -9.308 29.691 1.00 25.16 C ANISOU 716 CZ PHE A 93 3305 3397 2858 -35 -244 299 C ATOM 717 N SER A 94 -21.790 -13.615 23.816 1.00 13.49 N ANISOU 717 N SER A 94 1956 1698 1470 -236 -169 352 N ATOM 718 CA SER A 94 -22.058 -14.793 22.996 1.00 16.20 C ANISOU 718 CA SER A 94 2345 1995 1815 -284 -158 366 C ATOM 719 C SER A 94 -20.783 -15.313 22.344 1.00 15.83 C ANISOU 719 C SER A 94 2326 1871 1816 -249 -170 347 C ATOM 720 O SER A 94 -20.539 -16.525 22.318 1.00 16.89 O ANISOU 720 O SER A 94 2521 1948 1950 -262 -177 364 O ATOM 721 CB SER A 94 -23.103 -14.469 21.929 1.00 16.75 C ANISOU 721 CB SER A 94 2382 2102 1879 -332 -133 358 C ATOM 722 OG SER A 94 -24.383 -14.273 22.502 1.00 18.84 O ANISOU 722 OG SER A 94 2624 2437 2098 -373 -120 375 O ATOM 723 N LEU A 95 -19.963 -14.411 21.802 1.00 15.88 N ANISOU 723 N LEU A 95 2290 1876 1866 -205 -171 308 N ATOM 724 CA LEU A 95 -18.715 -14.835 21.176 1.00 14.72 C ANISOU 724 CA LEU A 95 2160 1665 1768 -171 -178 281 C ATOM 725 C LEU A 95 -17.796 -15.503 22.187 1.00 16.40 C ANISOU 725 C LEU A 95 2407 1839 1986 -124 -212 288 C ATOM 726 O LEU A 95 -17.175 -16.531 21.890 1.00 19.31 O ANISOU 726 O LEU A 95 2819 2144 2374 -113 -222 286 O ATOM 727 CB LEU A 95 -18.019 -13.636 20.533 1.00 15.96 C ANISOU 727 CB LEU A 95 2262 1835 1966 -139 -167 238 C ATOM 728 CG LEU A 95 -18.712 -13.048 19.302 1.00 18.38 C ANISOU 728 CG LEU A 95 2548 2163 2272 -176 -137 228 C ATOM 729 CD1 LEU A 95 -18.146 -11.676 18.973 1.00 18.10 C ANISOU 729 CD1 LEU A 95 2465 2146 2266 -144 -126 193 C ATOM 730 CD2 LEU A 95 -18.567 -13.980 18.114 1.00 17.45 C ANISOU 730 CD2 LEU A 95 2466 1995 2168 -203 -122 221 C ATOM 731 N LEU A 96 -17.696 -14.934 23.388 1.00 17.81 N ANISOU 731 N LEU A 96 2567 2054 2145 -93 -232 294 N ATOM 732 CA LEU A 96 -16.836 -15.517 24.412 1.00 19.09 C ANISOU 732 CA LEU A 96 2763 2185 2306 -42 -272 301 C ATOM 733 C LEU A 96 -17.349 -16.884 24.844 1.00 18.90 C ANISOU 733 C LEU A 96 2820 2120 2239 -73 -280 349 C ATOM 734 O LEU A 96 -16.560 -17.812 25.054 1.00 18.21 O ANISOU 734 O LEU A 96 2783 1971 2164 -38 -309 353 O ATOM 735 CB LEU A 96 -16.743 -14.570 25.608 1.00 23.36 C ANISOU 735 CB LEU A 96 3269 2780 2826 -8 -291 297 C ATOM 736 CG LEU A 96 -15.806 -14.976 26.749 1.00 29.93 C ANISOU 736 CG LEU A 96 4128 3590 3652 54 -340 298 C ATOM 737 CD1 LEU A 96 -14.397 -15.247 26.240 1.00 26.86 C ANISOU 737 CD1 LEU A 96 3728 3150 3326 109 -361 255 C ATOM 738 CD2 LEU A 96 -15.787 -13.892 27.815 1.00 29.37 C ANISOU 738 CD2 LEU A 96 4016 3582 3561 82 -355 287 C ATOM 739 N ALA A 97 -18.670 -17.027 24.980 1.00 19.33 N ANISOU 739 N ALA A 97 2890 2209 2245 -140 -256 385 N ATOM 740 CA ALA A 97 -19.237 -18.317 25.353 1.00 22.70 C ANISOU 740 CA ALA A 97 3398 2596 2630 -184 -256 432 C ATOM 741 C ALA A 97 -18.933 -19.376 24.301 1.00 20.37 C ANISOU 741 C ALA A 97 3149 2224 2365 -199 -251 426 C ATOM 742 O ALA A 97 -18.662 -20.534 24.636 1.00 19.57 O ANISOU 742 O ALA A 97 3126 2056 2252 -195 -269 452 O ATOM 743 CB ALA A 97 -20.746 -18.188 25.554 1.00 22.99 C ANISOU 743 CB ALA A 97 3427 2692 2614 -261 -222 460 C ATOM 744 N ILE A 98 -18.980 -18.999 23.021 1.00 19.01 N ANISOU 744 N ILE A 98 2934 2058 2230 -216 -226 393 N ATOM 745 CA ILE A 98 -18.718 -19.960 21.953 1.00 19.82 C ANISOU 745 CA ILE A 98 3078 2092 2361 -233 -219 381 C ATOM 746 C ILE A 98 -17.274 -20.438 22.012 1.00 20.06 C ANISOU 746 C ILE A 98 3132 2056 2434 -157 -251 358 C ATOM 747 O ILE A 98 -16.994 -21.634 21.869 1.00 22.00 O ANISOU 747 O ILE A 98 3448 2227 2684 -155 -262 368 O ATOM 748 CB ILE A 98 -19.056 -19.339 20.585 1.00 14.88 C ANISOU 748 CB ILE A 98 2401 1495 1759 -263 -186 349 C ATOM 749 CG1 ILE A 98 -20.571 -19.172 20.444 1.00 18.35 C ANISOU 749 CG1 ILE A 98 2826 1990 2154 -341 -160 372 C ATOM 750 CG2 ILE A 98 -18.494 -20.198 19.457 1.00 23.11 C ANISOU 750 CG2 ILE A 98 3478 2466 2837 -264 -180 325 C ATOM 751 CD1 ILE A 98 -20.991 -18.266 19.295 1.00 17.59 C ANISOU 751 CD1 ILE A 98 2671 1940 2072 -360 -137 342 C ATOM 752 N ALA A 99 -16.334 -19.515 22.224 1.00 18.13 N ANISOU 752 N ALA A 99 2829 1838 2224 -92 -266 322 N ATOM 753 CA ALA A 99 -14.933 -19.903 22.343 1.00 20.71 C ANISOU 753 CA ALA A 99 3163 2112 2593 -14 -300 291 C ATOM 754 C ALA A 99 -14.731 -20.851 23.518 1.00 20.79 C ANISOU 754 C ALA A 99 3249 2079 2571 17 -343 330 C ATOM 755 O ALA A 99 -14.083 -21.896 23.385 1.00 21.60 O ANISOU 755 O ALA A 99 3407 2107 2692 51 -366 326 O ATOM 756 CB ALA A 99 -14.058 -18.658 22.497 1.00 15.86 C ANISOU 756 CB ALA A 99 2466 1544 2016 40 -308 245 C ATOM 757 N ILE A 100 -15.289 -20.503 24.680 1.00 22.44 N ANISOU 757 N ILE A 100 3465 2332 2730 9 -355 366 N ATOM 758 CA ILE A 100 -15.146 -21.351 25.861 1.00 22.99 C ANISOU 758 CA ILE A 100 3614 2363 2757 37 -395 408 C ATOM 759 C ILE A 100 -15.785 -22.712 25.620 1.00 20.85 C ANISOU 759 C ILE A 100 3441 2022 2458 -18 -384 451 C ATOM 760 O ILE A 100 -15.237 -23.750 26.009 1.00 21.22 O ANISOU 760 O ILE A 100 3569 1994 2500 22 -419 469 O ATOM 761 CB ILE A 100 -15.748 -20.648 27.092 1.00 20.20 C ANISOU 761 CB ILE A 100 3249 2079 2348 26 -400 439 C ATOM 762 CG1 ILE A 100 -14.895 -19.430 27.462 1.00 24.51 C ANISOU 762 CG1 ILE A 100 3710 2678 2924 93 -422 392 C ATOM 763 CG2 ILE A 100 -15.857 -21.616 28.263 1.00 24.44 C ANISOU 763 CG2 ILE A 100 3885 2575 2825 35 -432 494 C ATOM 764 CD1 ILE A 100 -15.523 -18.526 28.501 1.00 27.74 C ANISOU 764 CD1 ILE A 100 4092 3165 3284 80 -420 410 C ATOM 765 N ASP A 101 -16.955 -22.730 24.978 1.00 20.40 N ANISOU 765 N ASP A 101 3380 1987 2382 -108 -336 466 N ATOM 766 CA ASP A 101 -17.618 -23.995 24.681 1.00 23.76 C ANISOU 766 CA ASP A 101 3895 2348 2783 -171 -320 501 C ATOM 767 C ASP A 101 -16.735 -24.896 23.824 1.00 25.83 C ANISOU 767 C ASP A 101 4198 2521 3095 -134 -335 473 C ATOM 768 O ASP A 101 -16.629 -26.100 24.083 1.00 24.84 O ANISOU 768 O ASP A 101 4171 2312 2953 -132 -353 502 O ATOM 769 CB ASP A 101 -18.949 -23.731 23.978 1.00 22.82 C ANISOU 769 CB ASP A 101 3745 2281 2645 -271 -268 506 C ATOM 770 CG ASP A 101 -19.632 -25.007 23.534 1.00 29.54 C ANISOU 770 CG ASP A 101 4679 3067 3477 -345 -248 533 C ATOM 771 OD1 ASP A 101 -20.245 -25.680 24.387 1.00 32.01 O ANISOU 771 OD1 ASP A 101 5065 3362 3737 -389 -246 583 O ATOM 772 OD2 ASP A 101 -19.549 -25.341 22.334 1.00 28.26 O ANISOU 772 OD2 ASP A 101 4514 2872 3351 -363 -233 502 O ATOM 773 N ARG A 102 -16.095 -24.333 22.797 1.00 21.58 N ANISOU 773 N ARG A 102 3588 1996 2615 -103 -325 416 N ATOM 774 CA ARG A 102 -15.239 -25.144 21.939 1.00 27.32 C ANISOU 774 CA ARG A 102 4346 2644 3391 -66 -334 382 C ATOM 775 C ARG A 102 -13.982 -25.597 22.670 1.00 25.07 C ANISOU 775 C ARG A 102 4092 2306 3127 36 -390 372 C ATOM 776 O ARG A 102 -13.431 -26.656 22.351 1.00 25.67 O ANISOU 776 O ARG A 102 4232 2297 3225 69 -409 363 O ATOM 777 CB ARG A 102 -14.875 -24.368 20.672 1.00 25.08 C ANISOU 777 CB ARG A 102 3976 2394 3159 -63 -304 322 C ATOM 778 CG ARG A 102 -16.055 -24.078 19.746 1.00 25.24 C ANISOU 778 CG ARG A 102 3974 2454 3161 -157 -255 326 C ATOM 779 CD ARG A 102 -16.668 -25.359 19.183 1.00 32.22 C ANISOU 779 CD ARG A 102 4942 3271 4030 -218 -241 344 C ATOM 780 NE ARG A 102 -17.553 -26.020 20.136 1.00 33.03 N ANISOU 780 NE ARG A 102 5116 3358 4076 -268 -247 404 N ATOM 781 CZ ARG A 102 -17.870 -27.308 20.103 1.00 39.33 C ANISOU 781 CZ ARG A 102 6011 4077 4857 -306 -247 430 C ATOM 782 NH1 ARG A 102 -17.388 -28.117 19.173 1.00 45.70 N ANISOU 782 NH1 ARG A 102 6857 4810 5699 -296 -246 399 N ATOM 783 NH2 ARG A 102 -18.685 -27.800 21.032 1.00 32.47 N ANISOU 783 NH2 ARG A 102 5204 3201 3932 -358 -247 486 N ATOM 784 N TYR A 103 -13.520 -24.823 23.654 1.00 21.61 N ANISOU 784 N TYR A 103 3612 1918 2682 91 -421 371 N ATOM 785 CA TYR A 103 -12.375 -25.256 24.447 1.00 24.18 C ANISOU 785 CA TYR A 103 3968 2199 3020 191 -482 363 C ATOM 786 C TYR A 103 -12.735 -26.435 25.342 1.00 31.15 C ANISOU 786 C TYR A 103 4977 3012 3847 188 -512 428 C ATOM 787 O TYR A 103 -11.962 -27.393 25.457 1.00 28.41 O ANISOU 787 O TYR A 103 4697 2583 3515 253 -555 425 O ATOM 788 CB TYR A 103 -11.842 -24.097 25.289 1.00 26.15 C ANISOU 788 CB TYR A 103 4139 2525 3273 245 -509 344 C ATOM 789 CG TYR A 103 -10.706 -24.503 26.199 1.00 31.48 C ANISOU 789 CG TYR A 103 4842 3166 3955 351 -579 335 C ATOM 790 CD1 TYR A 103 -9.429 -24.710 25.695 1.00 30.37 C ANISOU 790 CD1 TYR A 103 4666 2992 3882 433 -607 272 C ATOM 791 CD2 TYR A 103 -10.911 -24.688 27.559 1.00 35.89 C ANISOU 791 CD2 TYR A 103 5460 3725 4450 371 -620 386 C ATOM 792 CE1 TYR A 103 -8.388 -25.085 26.520 1.00 35.83 C ANISOU 792 CE1 TYR A 103 5377 3656 4581 536 -678 259 C ATOM 793 CE2 TYR A 103 -9.874 -25.064 28.393 1.00 38.53 C ANISOU 793 CE2 TYR A 103 5823 4029 4787 473 -692 378 C ATOM 794 CZ TYR A 103 -8.615 -25.260 27.867 1.00 40.45 C ANISOU 794 CZ TYR A 103 6026 4242 5101 558 -723 313 C ATOM 795 OH TYR A 103 -7.577 -25.635 28.691 1.00 49.27 O ANISOU 795 OH TYR A 103 7166 5333 6222 667 -801 299 O ATOM 796 N ILE A 104 -13.898 -26.379 25.995 1.00 28.05 N ANISOU 796 N ILE A 104 4622 2650 3387 112 -491 487 N ATOM 797 CA ILE A 104 -14.332 -27.503 26.821 1.00 31.51 C ANISOU 797 CA ILE A 104 5189 3019 3764 92 -510 553 C ATOM 798 C ILE A 104 -14.466 -28.759 25.972 1.00 31.01 C ANISOU 798 C ILE A 104 5206 2858 3717 60 -495 557 C ATOM 799 O ILE A 104 -14.114 -29.862 26.406 1.00 35.34 O ANISOU 799 O ILE A 104 5826 3347 4255 93 -517 568 O ATOM 800 CB ILE A 104 -15.652 -27.162 27.538 1.00 31.27 C ANISOU 800 CB ILE A 104 5171 3048 3660 1 -474 607 C ATOM 801 CG1 ILE A 104 -15.470 -25.940 28.440 1.00 30.40 C ANISOU 801 CG1 ILE A 104 4985 3032 3533 40 -491 599 C ATOM 802 CG2 ILE A 104 -16.138 -28.354 28.359 1.00 37.56 C ANISOU 802 CG2 ILE A 104 6074 3798 4400 -32 -472 658 C ATOM 803 CD1 ILE A 104 -16.763 -25.402 29.014 1.00 35.24 C ANISOU 803 CD1 ILE A 104 5585 3722 4083 -48 -448 637 C ATOM 804 N ALA A 105 -14.970 -28.611 24.745 1.00 30.17 N ANISOU 804 N ALA A 105 5056 2766 3641 -6 -445 528 N ATOM 805 CA ALA A 105 -15.190 -29.770 23.888 1.00 31.93 C ANISOU 805 CA ALA A 105 5342 2911 3878 -46 -424 523 C ATOM 806 C ALA A 105 -13.874 -30.435 23.499 1.00 37.36 C ANISOU 806 C ALA A 105 6049 3524 4622 54 -463 478 C ATOM 807 O ALA A 105 -13.795 -31.667 23.415 1.00 39.20 O ANISOU 807 O ALA A 105 6351 3691 4852 56 -465 482 O ATOM 808 CB ALA A 105 -15.968 -29.353 22.642 1.00 31.80 C ANISOU 808 CB ALA A 105 5274 2930 3879 -133 -369 499 C ATOM 809 N ILE A 106 -12.834 -29.641 23.252 1.00 30.73 N ANISOU 809 N ILE A 106 5133 2708 3835 137 -489 427 N ATOM 810 CA ILE A 106 -11.548 -30.193 22.840 1.00 34.67 C ANISOU 810 CA ILE A 106 5639 3142 4394 237 -526 376 C ATOM 811 C ILE A 106 -10.702 -30.608 24.043 1.00 33.96 C ANISOU 811 C ILE A 106 5580 3033 4289 335 -589 387 C ATOM 812 O ILE A 106 -9.951 -31.585 23.958 1.00 34.91 O ANISOU 812 O ILE A 106 5737 3094 4433 397 -615 364 O ATOM 813 CB ILE A 106 -10.795 -29.178 21.956 1.00 34.85 C ANISOU 813 CB ILE A 106 5529 3231 4482 272 -506 297 C ATOM 814 CG1 ILE A 106 -9.586 -29.827 21.276 1.00 37.64 C ANISOU 814 CG1 ILE A 106 5883 3518 4900 357 -528 234 C ATOM 815 CG2 ILE A 106 -10.349 -27.976 22.770 1.00 33.64 C ANISOU 815 CG2 ILE A 106 5286 3166 4329 318 -528 285 C ATOM 816 CD1 ILE A 106 -9.884 -30.377 19.904 1.00 44.21 C ANISOU 816 CD1 ILE A 106 6733 4309 5757 302 -481 205 C ATOM 817 N ALA A 107 -10.816 -29.896 25.168 1.00 33.38 N ANISOU 817 N ALA A 107 5491 3016 4177 350 -614 419 N ATOM 818 CA ALA A 107 -9.945 -30.157 26.310 1.00 34.06 C ANISOU 818 CA ALA A 107 5592 3099 4248 446 -677 421 C ATOM 819 C ALA A 107 -10.451 -31.317 27.158 1.00 36.15 C ANISOU 819 C ALA A 107 5966 3320 4448 418 -681 480 C ATOM 820 O ALA A 107 -9.655 -32.148 27.611 1.00 42.15 O ANISOU 820 O ALA A 107 6770 4034 5212 494 -726 473 O ATOM 821 CB ALA A 107 -9.810 -28.897 27.165 1.00 34.42 C ANISOU 821 CB ALA A 107 5573 3227 4277 476 -703 424 C ATOM 822 N ILE A 108 -11.758 -31.393 27.388 1.00 37.04 N ANISOU 822 N ILE A 108 6122 3449 4504 309 -635 536 N ATOM 823 CA ILE A 108 -12.339 -32.455 28.207 1.00 43.36 C ANISOU 823 CA ILE A 108 7024 4210 5241 271 -630 590 C ATOM 824 C ILE A 108 -13.586 -32.991 27.515 1.00 43.58 C ANISOU 824 C ILE A 108 7087 4220 5251 147 -564 613 C ATOM 825 O ILE A 108 -14.705 -32.795 28.010 1.00 43.37 O ANISOU 825 O ILE A 108 7072 4237 5170 58 -525 656 O ATOM 826 CB ILE A 108 -12.659 -31.953 29.623 1.00 46.24 C ANISOU 826 CB ILE A 108 7398 4631 5539 269 -646 635 C ATOM 827 CG1 ILE A 108 -13.352 -30.590 29.568 1.00 43.93 C ANISOU 827 CG1 ILE A 108 7025 4431 5236 213 -613 638 C ATOM 828 CG2 ILE A 108 -11.383 -31.873 30.451 1.00 52.90 C ANISOU 828 CG2 ILE A 108 8234 5475 6392 395 -720 614 C ATOM 829 CD1 ILE A 108 -13.913 -30.135 30.902 1.00 52.76 C ANISOU 829 CD1 ILE A 108 8155 5610 6282 190 -613 684 C ATOM 830 N PRO A 109 -13.443 -33.682 26.381 1.00 42.55 N ANISOU 830 N PRO A 109 6969 4032 5165 137 -547 581 N ATOM 831 CA PRO A 109 -14.637 -34.173 25.675 1.00 46.03 C ANISOU 831 CA PRO A 109 7435 4464 5591 17 -485 595 C ATOM 832 C PRO A 109 -15.416 -35.219 26.451 1.00 51.45 C ANISOU 832 C PRO A 109 8217 5116 6217 -42 -470 646 C ATOM 833 O PRO A 109 -16.637 -35.318 26.275 1.00 49.32 O ANISOU 833 O PRO A 109 7951 4873 5917 -153 -417 667 O ATOM 834 CB PRO A 109 -14.061 -34.752 24.375 1.00 44.11 C ANISOU 834 CB PRO A 109 7189 4161 5411 43 -481 543 C ATOM 835 CG PRO A 109 -12.640 -35.084 24.700 1.00 41.16 C ANISOU 835 CG PRO A 109 6828 3741 5070 174 -544 516 C ATOM 836 CD PRO A 109 -12.194 -34.052 25.693 1.00 40.00 C ANISOU 836 CD PRO A 109 6634 3656 4909 234 -582 525 C ATOM 837 N LEU A 110 -14.754 -36.003 27.306 1.00 61.48 N ANISOU 837 N LEU A 110 9562 6330 7468 28 -515 665 N ATOM 838 CA LEU A 110 -15.441 -37.097 27.984 1.00 64.58 C ANISOU 838 CA LEU A 110 10057 6677 7805 -28 -500 713 C ATOM 839 C LEU A 110 -16.483 -36.592 28.973 1.00 65.35 C ANISOU 839 C LEU A 110 10153 6842 7836 -105 -469 760 C ATOM 840 O LEU A 110 -17.447 -37.308 29.268 1.00 68.13 O ANISOU 840 O LEU A 110 10565 7176 8143 -192 -431 793 O ATOM 841 CB LEU A 110 -14.427 -37.992 28.697 1.00 69.53 C ANISOU 841 CB LEU A 110 10767 7228 8425 73 -561 722 C ATOM 842 CG LEU A 110 -13.505 -38.801 27.780 1.00 74.07 C ANISOU 842 CG LEU A 110 11362 7723 9060 141 -587 677 C ATOM 843 CD1 LEU A 110 -12.438 -39.519 28.589 1.00 80.45 C ANISOU 843 CD1 LEU A 110 12237 8470 9859 254 -654 683 C ATOM 844 CD2 LEU A 110 -14.304 -39.795 26.948 1.00 71.81 C ANISOU 844 CD2 LEU A 110 11128 7381 8775 50 -538 678 C ATOM 845 N ARG A 111 -16.317 -35.375 29.493 1.00 64.72 N ANISOU 845 N ARG A 111 10003 6841 7748 -75 -483 761 N ATOM 846 CA ARG A 111 -17.268 -34.786 30.429 1.00 68.97 C ANISOU 846 CA ARG A 111 10528 7453 8224 -141 -453 800 C ATOM 847 C ARG A 111 -17.836 -33.474 29.895 1.00 59.89 C ANISOU 847 C ARG A 111 9268 6397 7089 -189 -418 780 C ATOM 848 O ARG A 111 -18.217 -32.593 30.669 1.00 59.06 O ANISOU 848 O ARG A 111 9124 6368 6947 -202 -411 799 O ATOM 849 CB ARG A 111 -16.618 -34.581 31.798 1.00 77.91 C ANISOU 849 CB ARG A 111 11689 8596 9316 -61 -503 825 C ATOM 850 CG ARG A 111 -15.329 -33.773 31.783 1.00 70.59 C ANISOU 850 CG ARG A 111 10700 7689 8432 59 -564 788 C ATOM 851 CD ARG A 111 -14.685 -33.771 33.163 1.00 88.78 C ANISOU 851 CD ARG A 111 13042 9997 10692 138 -618 811 C ATOM 852 NE ARG A 111 -13.450 -32.996 33.207 1.00 97.00 N ANISOU 852 NE ARG A 111 14015 11065 11775 253 -679 768 N ATOM 853 CZ ARG A 111 -12.704 -32.835 34.292 1.00 99.39 C ANISOU 853 CZ ARG A 111 14328 11382 12052 337 -735 772 C ATOM 854 NH1 ARG A 111 -13.037 -33.386 35.448 1.00104.73 N ANISOU 854 NH1 ARG A 111 15088 12045 12658 323 -740 821 N ATOM 855 NH2 ARG A 111 -11.597 -32.103 34.215 1.00100.69 N ANISOU 855 NH2 ARG A 111 14416 11578 12263 437 -788 723 N ATOM 856 N TYR A 112 -17.904 -33.335 28.569 1.00 52.50 N ANISOU 856 N TYR A 112 8284 5458 6206 -214 -396 742 N ATOM 857 CA TYR A 112 -18.482 -32.136 27.972 1.00 50.40 C ANISOU 857 CA TYR A 112 7919 5277 5954 -263 -363 723 C ATOM 858 C TYR A 112 -20.006 -32.172 28.019 1.00 50.06 C ANISOU 858 C TYR A 112 7865 5287 5869 -388 -300 743 C ATOM 859 O TYR A 112 -20.644 -31.210 28.460 1.00 44.35 O ANISOU 859 O TYR A 112 7083 4651 5117 -424 -279 754 O ATOM 860 CB TYR A 112 -17.996 -31.979 26.528 1.00 43.79 C ANISOU 860 CB TYR A 112 7036 4416 5186 -244 -363 673 C ATOM 861 CG TYR A 112 -18.770 -30.950 25.730 1.00 41.43 C ANISOU 861 CG TYR A 112 6647 4195 4898 -313 -321 654 C ATOM 862 CD1 TYR A 112 -18.390 -29.616 25.725 1.00 36.96 C ANISOU 862 CD1 TYR A 112 6005 3689 4348 -272 -336 640 C ATOM 863 CD2 TYR A 112 -19.881 -31.317 24.980 1.00 42.37 C ANISOU 863 CD2 TYR A 112 6757 4329 5011 -416 -269 648 C ATOM 864 CE1 TYR A 112 -19.097 -28.673 24.999 1.00 35.57 C ANISOU 864 CE1 TYR A 112 5751 3584 4181 -333 -300 625 C ATOM 865 CE2 TYR A 112 -20.592 -30.384 24.253 1.00 41.09 C ANISOU 865 CE2 TYR A 112 6512 4244 4858 -474 -235 628 C ATOM 866 CZ TYR A 112 -20.196 -29.064 24.266 1.00 37.61 C ANISOU 866 CZ TYR A 112 6000 3859 4432 -432 -250 618 C ATOM 867 OH TYR A 112 -20.903 -28.134 23.542 1.00 35.62 O ANISOU 867 OH TYR A 112 5667 3680 4185 -487 -218 600 O ATOM 868 N ASN A 113 -20.607 -33.276 27.566 1.00 50.78 N ANISOU 868 N ASN A 113 8008 5329 5956 -455 -270 745 N ATOM 869 CA ASN A 113 -22.064 -33.348 27.513 1.00 52.29 C ANISOU 869 CA ASN A 113 8179 5573 6114 -575 -211 754 C ATOM 870 C ASN A 113 -22.685 -33.280 28.901 1.00 49.05 C ANISOU 870 C ASN A 113 7796 5204 5639 -606 -197 797 C ATOM 871 O ASN A 113 -23.798 -32.766 29.057 1.00 47.78 O ANISOU 871 O ASN A 113 7581 5123 5449 -686 -152 799 O ATOM 872 CB ASN A 113 -22.500 -34.626 26.797 1.00 50.85 C ANISOU 872 CB ASN A 113 8055 5324 5941 -634 -188 744 C ATOM 873 CG ASN A 113 -22.327 -34.538 25.293 1.00 53.22 C ANISOU 873 CG ASN A 113 8307 5614 6299 -637 -182 696 C ATOM 874 OD1 ASN A 113 -22.382 -33.452 24.713 1.00 47.95 O ANISOU 874 OD1 ASN A 113 7552 5013 5655 -636 -176 671 O ATOM 875 ND2 ASN A 113 -22.121 -35.683 24.652 1.00 59.67 N ANISOU 875 ND2 ASN A 113 9187 6349 7137 -642 -184 681 N ATOM 876 N GLY A 114 -21.990 -33.791 29.920 1.00 47.86 N ANISOU 876 N GLY A 114 7724 5000 5460 -544 -234 828 N ATOM 877 CA GLY A 114 -22.492 -33.684 31.278 1.00 53.11 C ANISOU 877 CA GLY A 114 8416 5703 6059 -567 -222 869 C ATOM 878 C GLY A 114 -22.284 -32.325 31.907 1.00 53.53 C ANISOU 878 C GLY A 114 8397 5844 6098 -523 -236 870 C ATOM 879 O GLY A 114 -23.019 -31.963 32.832 1.00 54.24 O ANISOU 879 O GLY A 114 8478 5996 6135 -567 -209 894 O ATOM 880 N LEU A 115 -21.304 -31.565 31.423 1.00 50.76 N ANISOU 880 N LEU A 115 7995 5499 5793 -439 -278 843 N ATOM 881 CA LEU A 115 -20.996 -30.247 31.964 1.00 52.00 C ANISOU 881 CA LEU A 115 8083 5734 5940 -390 -297 840 C ATOM 882 C LEU A 115 -21.728 -29.135 31.224 1.00 50.68 C ANISOU 882 C LEU A 115 7811 5655 5791 -445 -259 814 C ATOM 883 O LEU A 115 -22.261 -28.216 31.857 1.00 48.58 O ANISOU 883 O LEU A 115 7493 5475 5490 -465 -242 821 O ATOM 884 CB LEU A 115 -19.485 -30.008 31.906 1.00 50.68 C ANISOU 884 CB LEU A 115 7916 5527 5814 -265 -367 820 C ATOM 885 CG LEU A 115 -18.977 -28.578 32.106 1.00 54.96 C ANISOU 885 CG LEU A 115 8374 6142 6366 -205 -395 801 C ATOM 886 CD1 LEU A 115 -19.374 -28.039 33.471 1.00 62.40 C ANISOU 886 CD1 LEU A 115 9315 7153 7241 -210 -392 830 C ATOM 887 CD2 LEU A 115 -17.468 -28.537 31.927 1.00 55.12 C ANISOU 887 CD2 LEU A 115 8395 6113 6436 -83 -464 772 C ATOM 888 N VAL A 116 -21.768 -29.201 29.897 1.00 49.11 N ANISOU 888 N VAL A 116 7578 5436 5644 -468 -247 782 N ATOM 889 CA VAL A 116 -22.374 -28.169 29.064 1.00 46.14 C ANISOU 889 CA VAL A 116 7104 5137 5289 -513 -217 754 C ATOM 890 C VAL A 116 -23.703 -28.713 28.558 1.00 45.81 C ANISOU 890 C VAL A 116 7053 5115 5235 -626 -159 750 C ATOM 891 O VAL A 116 -23.735 -29.569 27.665 1.00 48.25 O ANISOU 891 O VAL A 116 7392 5365 5574 -652 -151 733 O ATOM 892 CB VAL A 116 -21.454 -27.766 27.903 1.00 44.51 C ANISOU 892 CB VAL A 116 6863 4901 5149 -456 -245 718 C ATOM 893 CG1 VAL A 116 -22.025 -26.573 27.159 1.00 40.88 C ANISOU 893 CG1 VAL A 116 6304 4525 4705 -495 -218 694 C ATOM 894 CG2 VAL A 116 -20.053 -27.458 28.416 1.00 44.83 C ANISOU 894 CG2 VAL A 116 6919 4908 5206 -338 -308 716 C ATOM 895 N THR A 117 -24.801 -28.217 29.124 1.00 42.23 N ANISOU 895 N THR A 117 6557 4748 4739 -691 -120 759 N ATOM 896 CA THR A 117 -26.142 -28.666 28.783 1.00 42.02 C ANISOU 896 CA THR A 117 6513 4754 4698 -797 -67 750 C ATOM 897 C THR A 117 -26.960 -27.502 28.238 1.00 37.43 C ANISOU 897 C THR A 117 5819 4279 4124 -838 -40 722 C ATOM 898 O THR A 117 -26.629 -26.331 28.441 1.00 34.19 O ANISOU 898 O THR A 117 5352 3925 3715 -791 -55 718 O ATOM 899 CB THR A 117 -26.859 -29.266 30.000 1.00 44.63 C ANISOU 899 CB THR A 117 6896 5093 4969 -847 -40 784 C ATOM 900 OG1 THR A 117 -27.023 -28.259 31.006 1.00 42.33 O ANISOU 900 OG1 THR A 117 6563 4882 4639 -829 -37 797 O ATOM 901 CG2 THR A 117 -26.064 -30.432 30.575 1.00 47.24 C ANISOU 901 CG2 THR A 117 7344 5317 5288 -805 -69 815 C ATOM 902 N GLY A 118 -28.050 -27.844 27.548 1.00 36.58 N ANISOU 902 N GLY A 118 5679 4199 4019 -924 -2 699 N ATOM 903 CA GLY A 118 -28.903 -26.816 26.978 1.00 38.83 C ANISOU 903 CA GLY A 118 5857 4586 4311 -963 21 669 C ATOM 904 C GLY A 118 -29.580 -25.964 28.034 1.00 37.79 C ANISOU 904 C GLY A 118 5675 4551 4134 -978 42 679 C ATOM 905 O GLY A 118 -29.693 -24.745 27.881 1.00 38.04 O ANISOU 905 O GLY A 118 5622 4660 4170 -957 40 663 O ATOM 906 N THR A 119 -30.045 -26.592 29.116 1.00 36.31 N ANISOU 906 N THR A 119 5537 4359 3900 -1014 65 705 N ATOM 907 CA THR A 119 -30.690 -25.837 30.187 1.00 36.68 C ANISOU 907 CA THR A 119 5540 4496 3900 -1028 89 712 C ATOM 908 C THR A 119 -29.723 -24.843 30.818 1.00 34.66 C ANISOU 908 C THR A 119 5274 4257 3637 -937 53 727 C ATOM 909 O THR A 119 -30.098 -23.703 31.114 1.00 36.17 O ANISOU 909 O THR A 119 5388 4543 3813 -929 63 713 O ATOM 910 CB THR A 119 -31.240 -26.793 31.246 1.00 40.03 C ANISOU 910 CB THR A 119 6036 4899 4275 -1081 118 740 C ATOM 911 OG1 THR A 119 -32.273 -27.603 30.671 1.00 45.32 O ANISOU 911 OG1 THR A 119 6703 5569 4949 -1175 155 721 O ATOM 912 CG2 THR A 119 -31.804 -26.019 32.428 1.00 41.23 C ANISOU 912 CG2 THR A 119 6148 5141 4375 -1089 143 748 C ATOM 913 N ARG A 120 -28.472 -25.257 31.035 1.00 34.66 N ANISOU 913 N ARG A 120 5351 4170 3648 -864 10 750 N ATOM 914 CA ARG A 120 -27.477 -24.332 31.566 1.00 38.53 C ANISOU 914 CA ARG A 120 5831 4673 4134 -773 -31 758 C ATOM 915 C ARG A 120 -27.137 -23.243 30.556 1.00 35.24 C ANISOU 915 C ARG A 120 5334 4295 3763 -739 -49 727 C ATOM 916 O ARG A 120 -26.892 -22.095 30.944 1.00 33.35 O ANISOU 916 O ARG A 120 5043 4118 3512 -695 -64 722 O ATOM 917 CB ARG A 120 -26.218 -25.097 31.977 1.00 41.37 C ANISOU 917 CB ARG A 120 6290 4931 4499 -699 -80 785 C ATOM 918 CG ARG A 120 -26.423 -26.018 33.174 1.00 44.55 C ANISOU 918 CG ARG A 120 6778 5301 4848 -717 -69 822 C ATOM 919 CD ARG A 120 -25.199 -26.880 33.449 1.00 44.35 C ANISOU 919 CD ARG A 120 6851 5169 4831 -643 -121 844 C ATOM 920 NE ARG A 120 -25.429 -27.816 34.545 1.00 56.02 N ANISOU 920 NE ARG A 120 8418 6613 6256 -664 -110 882 N ATOM 921 CZ ARG A 120 -24.596 -28.788 34.892 1.00 55.27 C ANISOU 921 CZ ARG A 120 8420 6423 6158 -614 -148 906 C ATOM 922 NH1 ARG A 120 -23.460 -28.992 34.244 1.00 48.34 N ANISOU 922 NH1 ARG A 120 7561 5477 5331 -538 -199 892 N ATOM 923 NH2 ARG A 120 -24.912 -29.579 35.914 1.00 61.96 N ANISOU 923 NH2 ARG A 120 9347 7244 6949 -641 -135 942 N ATOM 924 N ALA A 121 -27.128 -23.575 29.263 1.00 32.05 N ANISOU 924 N ALA A 121 4917 3853 3406 -760 -48 706 N ATOM 925 CA ALA A 121 -26.845 -22.568 28.245 1.00 34.94 C ANISOU 925 CA ALA A 121 5210 4252 3813 -734 -61 678 C ATOM 926 C ALA A 121 -27.927 -21.495 28.212 1.00 28.32 C ANISOU 926 C ALA A 121 4270 3534 2958 -773 -30 656 C ATOM 927 O ALA A 121 -27.621 -20.301 28.113 1.00 28.64 O ANISOU 927 O ALA A 121 4231 3628 3025 -707 -45 623 O ATOM 928 CB ALA A 121 -26.709 -23.233 26.876 1.00 34.23 C ANISOU 928 CB ALA A 121 5134 4100 3773 -755 -61 657 C ATOM 929 N ALA A 122 -29.197 -21.899 28.287 1.00 29.46 N ANISOU 929 N ALA A 122 4393 3722 3077 -855 14 649 N ATOM 930 CA ALA A 122 -30.284 -20.925 28.273 1.00 27.28 C ANISOU 930 CA ALA A 122 4017 3564 2785 -891 43 625 C ATOM 931 C ALA A 122 -30.199 -19.985 29.469 1.00 30.07 C ANISOU 931 C ALA A 122 4345 3984 3098 -850 41 635 C ATOM 932 O ALA A 122 -30.498 -18.791 29.352 1.00 31.08 O ANISOU 932 O ALA A 122 4379 4194 3236 -818 41 601 O ATOM 933 CB ALA A 122 -31.632 -21.644 28.252 1.00 32.41 C ANISOU 933 CB ALA A 122 4653 4246 3416 -985 86 611 C ATOM 934 N GLY A 123 -29.797 -20.505 30.630 1.00 31.32 N ANISOU 934 N GLY A 123 4577 4104 3221 -831 35 666 N ATOM 935 CA GLY A 123 -29.633 -19.645 31.790 1.00 27.36 C ANISOU 935 CA GLY A 123 4057 3661 2677 -787 29 673 C ATOM 936 C GLY A 123 -28.469 -18.685 31.635 1.00 25.41 C ANISOU 936 C GLY A 123 3779 3405 2471 -680 -20 652 C ATOM 937 O GLY A 123 -28.559 -17.517 32.022 1.00 24.36 O ANISOU 937 O GLY A 123 3572 3346 2337 -636 -23 624 O ATOM 938 N ILE A 124 -27.361 -19.162 31.066 1.00 24.77 N ANISOU 938 N ILE A 124 3745 3230 2435 -631 -59 655 N ATOM 939 CA ILE A 124 -26.221 -18.285 30.816 1.00 25.27 C ANISOU 939 CA ILE A 124 3767 3282 2553 -530 -102 622 C ATOM 940 C ILE A 124 -26.607 -17.182 29.840 1.00 23.92 C ANISOU 940 C ILE A 124 3490 3172 2428 -520 -91 573 C ATOM 941 O ILE A 124 -26.265 -16.009 30.036 1.00 22.38 O ANISOU 941 O ILE A 124 3233 3020 2249 -458 -106 542 O ATOM 942 CB ILE A 124 -25.023 -19.107 30.303 1.00 23.98 C ANISOU 942 CB ILE A 124 3670 3010 2431 -486 -140 629 C ATOM 943 CG1 ILE A 124 -24.493 -20.010 31.420 1.00 32.80 C ANISOU 943 CG1 ILE A 124 4894 4068 3501 -470 -164 676 C ATOM 944 CG2 ILE A 124 -23.923 -18.188 29.782 1.00 25.50 C ANISOU 944 CG2 ILE A 124 3804 3196 2689 -396 -174 584 C ATOM 945 CD1 ILE A 124 -23.470 -21.028 30.958 1.00 37.40 C ANISOU 945 CD1 ILE A 124 5553 4539 4118 -435 -199 686 C ATOM 946 N ILE A 125 -27.330 -17.537 28.777 1.00 23.93 N ANISOU 946 N ILE A 125 3472 3173 2445 -580 -67 564 N ATOM 947 CA ILE A 125 -27.745 -16.540 27.794 1.00 24.05 C ANISOU 947 CA ILE A 125 3395 3243 2498 -570 -60 521 C ATOM 948 C ILE A 125 -28.599 -15.463 28.452 1.00 18.67 C ANISOU 948 C ILE A 125 2641 2667 1788 -568 -42 504 C ATOM 949 O ILE A 125 -28.450 -14.270 28.162 1.00 19.00 O ANISOU 949 O ILE A 125 2614 2746 1857 -513 -53 469 O ATOM 950 CB ILE A 125 -28.486 -17.223 26.630 1.00 22.03 C ANISOU 950 CB ILE A 125 3138 2976 2255 -642 -38 517 C ATOM 951 CG1 ILE A 125 -27.500 -18.043 25.791 1.00 19.56 C ANISOU 951 CG1 ILE A 125 2887 2561 1985 -625 -60 521 C ATOM 952 CG2 ILE A 125 -29.207 -16.184 25.776 1.00 20.14 C ANISOU 952 CG2 ILE A 125 2804 2810 2037 -639 -30 476 C ATOM 953 CD1 ILE A 125 -28.162 -19.014 24.831 1.00 26.61 C ANISOU 953 CD1 ILE A 125 3804 3426 2880 -705 -39 523 C ATOM 954 N ALA A 126 -29.507 -15.864 29.345 1.00 21.98 N ANISOU 954 N ALA A 126 3072 3132 2146 -629 -11 526 N ATOM 955 CA ALA A 126 -30.361 -14.888 30.017 1.00 19.06 C ANISOU 955 CA ALA A 126 2630 2867 1746 -628 10 505 C ATOM 956 C ALA A 126 -29.542 -13.949 30.893 1.00 20.09 C ANISOU 956 C ALA A 126 2751 3008 1874 -543 -17 495 C ATOM 957 O ALA A 126 -29.762 -12.731 30.891 1.00 20.39 O ANISOU 957 O ALA A 126 2714 3107 1925 -500 -19 458 O ATOM 958 CB ALA A 126 -31.421 -15.608 30.850 1.00 26.41 C ANISOU 958 CB ALA A 126 3584 3843 2610 -717 54 531 C ATOM 959 N ILE A 127 -28.592 -14.497 31.653 1.00 22.15 N ANISOU 959 N ILE A 127 3089 3208 2119 -515 -40 525 N ATOM 960 CA ILE A 127 -27.744 -13.668 32.506 1.00 21.30 C ANISOU 960 CA ILE A 127 2975 3109 2009 -435 -70 512 C ATOM 961 C ILE A 127 -26.933 -12.690 31.667 1.00 19.82 C ANISOU 961 C ILE A 127 2734 2903 1892 -363 -100 470 C ATOM 962 O ILE A 127 -26.809 -11.507 32.009 1.00 19.94 O ANISOU 962 O ILE A 127 2696 2965 1915 -312 -108 438 O ATOM 963 CB ILE A 127 -26.838 -14.564 33.372 1.00 22.19 C ANISOU 963 CB ILE A 127 3185 3154 2093 -417 -97 552 C ATOM 964 CG1 ILE A 127 -27.677 -15.302 34.419 1.00 26.36 C ANISOU 964 CG1 ILE A 127 3768 3711 2538 -486 -64 593 C ATOM 965 CG2 ILE A 127 -25.741 -13.740 34.030 1.00 26.07 C ANISOU 965 CG2 ILE A 127 3666 3642 2596 -325 -140 530 C ATOM 966 CD1 ILE A 127 -26.986 -16.504 35.027 1.00 27.34 C ANISOU 966 CD1 ILE A 127 4009 3750 2627 -487 -86 644 C ATOM 967 N CYS A 128 -26.368 -13.163 30.555 1.00 19.84 N ANISOU 967 N CYS A 128 2755 2837 1946 -360 -113 469 N ATOM 968 CA CYS A 128 -25.541 -12.292 29.726 1.00 20.21 C ANISOU 968 CA CYS A 128 2759 2862 2057 -298 -135 431 C ATOM 969 C CYS A 128 -26.354 -11.140 29.145 1.00 16.50 C ANISOU 969 C CYS A 128 2208 2458 1601 -297 -117 396 C ATOM 970 O CYS A 128 -25.861 -10.011 29.046 1.00 18.49 O ANISOU 970 O CYS A 128 2420 2722 1885 -240 -132 363 O ATOM 971 CB CYS A 128 -24.879 -13.106 28.616 1.00 18.85 C ANISOU 971 CB CYS A 128 2625 2608 1931 -304 -145 435 C ATOM 972 SG CYS A 128 -23.553 -14.175 29.214 1.00 28.25 S ANISOU 972 SG CYS A 128 3902 3709 3123 -268 -182 461 S ATOM 973 N TRP A 129 -27.605 -11.401 28.760 1.00 17.73 N ANISOU 973 N TRP A 129 2342 2661 1735 -360 -88 402 N ATOM 974 CA TRP A 129 -28.449 -10.323 28.253 1.00 20.08 C ANISOU 974 CA TRP A 129 2561 3025 2041 -352 -76 368 C ATOM 975 C TRP A 129 -28.731 -9.289 29.335 1.00 18.72 C ANISOU 975 C TRP A 129 2348 2922 1842 -315 -74 349 C ATOM 976 O TRP A 129 -28.732 -8.082 29.066 1.00 18.43 O ANISOU 976 O TRP A 129 2261 2912 1831 -266 -82 315 O ATOM 977 CB TRP A 129 -29.752 -10.892 27.695 1.00 20.55 C ANISOU 977 CB TRP A 129 2601 3127 2080 -426 -48 374 C ATOM 978 CG TRP A 129 -29.643 -11.287 26.252 1.00 21.74 C ANISOU 978 CG TRP A 129 2759 3230 2270 -444 -54 369 C ATOM 979 CD1 TRP A 129 -29.499 -12.549 25.753 1.00 19.08 C ANISOU 979 CD1 TRP A 129 2478 2835 1935 -495 -50 393 C ATOM 980 CD2 TRP A 129 -29.659 -10.408 25.120 1.00 20.06 C ANISOU 980 CD2 TRP A 129 2504 3024 2095 -409 -65 339 C ATOM 981 NE1 TRP A 129 -29.430 -12.510 24.381 1.00 21.78 N ANISOU 981 NE1 TRP A 129 2811 3151 2315 -496 -57 377 N ATOM 982 CE2 TRP A 129 -29.523 -11.207 23.968 1.00 17.55 C ANISOU 982 CE2 TRP A 129 2216 2653 1799 -444 -67 345 C ATOM 983 CE3 TRP A 129 -29.772 -9.022 24.971 1.00 18.02 C ANISOU 983 CE3 TRP A 129 2190 2805 1852 -352 -75 307 C ATOM 984 CZ2 TRP A 129 -29.502 -10.667 22.682 1.00 19.56 C ANISOU 984 CZ2 TRP A 129 2448 2899 2085 -424 -76 323 C ATOM 985 CZ3 TRP A 129 -29.752 -8.488 23.695 1.00 16.67 C ANISOU 985 CZ3 TRP A 129 2001 2619 1713 -332 -85 288 C ATOM 986 CH2 TRP A 129 -29.618 -9.308 22.567 1.00 21.98 C ANISOU 986 CH2 TRP A 129 2705 3243 2402 -368 -86 296 C ATOM 987 N VAL A 130 -28.964 -9.740 30.569 1.00 19.83 N ANISOU 987 N VAL A 130 2515 3090 1929 -338 -62 371 N ATOM 988 CA VAL A 130 -29.157 -8.801 31.673 1.00 18.32 C ANISOU 988 CA VAL A 130 2291 2962 1707 -301 -59 350 C ATOM 989 C VAL A 130 -27.899 -7.967 31.879 1.00 20.39 C ANISOU 989 C VAL A 130 2556 3186 2005 -221 -95 329 C ATOM 990 O VAL A 130 -27.961 -6.739 32.014 1.00 17.68 O ANISOU 990 O VAL A 130 2163 2881 1674 -174 -100 291 O ATOM 991 CB VAL A 130 -29.552 -9.554 32.956 1.00 24.71 C ANISOU 991 CB VAL A 130 3142 3801 2445 -345 -38 382 C ATOM 992 CG1 VAL A 130 -29.569 -8.606 34.148 1.00 24.07 C ANISOU 992 CG1 VAL A 130 3035 3780 2331 -301 -39 359 C ATOM 993 CG2 VAL A 130 -30.909 -10.214 32.782 1.00 24.39 C ANISOU 993 CG2 VAL A 130 3084 3812 2370 -431 5 394 C ATOM 994 N LEU A 131 -26.736 -8.624 31.910 1.00 18.90 N ANISOU 994 N LEU A 131 2426 2922 1835 -205 -121 348 N ATOM 995 CA LEU A 131 -25.483 -7.894 32.061 1.00 15.52 C ANISOU 995 CA LEU A 131 1995 2457 1444 -134 -155 322 C ATOM 996 C LEU A 131 -25.245 -6.939 30.899 1.00 18.92 C ANISOU 996 C LEU A 131 2379 2873 1937 -104 -159 286 C ATOM 997 O LEU A 131 -24.674 -5.860 31.091 1.00 19.87 O ANISOU 997 O LEU A 131 2472 2996 2082 -52 -174 251 O ATOM 998 CB LEU A 131 -24.318 -8.875 32.183 1.00 16.80 C ANISOU 998 CB LEU A 131 2222 2543 1618 -122 -184 345 C ATOM 999 CG LEU A 131 -24.319 -9.764 33.427 1.00 23.41 C ANISOU 999 CG LEU A 131 3121 3381 2391 -137 -190 383 C ATOM 1000 CD1 LEU A 131 -23.223 -10.809 33.324 1.00 25.21 C ANISOU 1000 CD1 LEU A 131 3416 3525 2637 -121 -223 406 C ATOM 1001 CD2 LEU A 131 -24.149 -8.925 34.687 1.00 25.31 C ANISOU 1001 CD2 LEU A 131 3347 3673 2597 -94 -204 363 C ATOM 1002 N SER A 132 -25.670 -7.314 29.690 1.00 16.52 N ANISOU 1002 N SER A 132 2071 2550 1656 -139 -145 293 N ATOM 1003 CA SER A 132 -25.481 -6.436 28.539 1.00 14.78 C ANISOU 1003 CA SER A 132 1816 2312 1486 -113 -147 263 C ATOM 1004 C SER A 132 -26.278 -5.148 28.694 1.00 16.96 C ANISOU 1004 C SER A 132 2037 2654 1755 -88 -138 233 C ATOM 1005 O SER A 132 -25.786 -4.061 28.369 1.00 15.94 O ANISOU 1005 O SER A 132 1887 2510 1660 -42 -148 203 O ATOM 1006 CB SER A 132 -25.879 -7.163 27.254 1.00 16.99 C ANISOU 1006 CB SER A 132 2108 2566 1782 -158 -135 278 C ATOM 1007 OG SER A 132 -25.015 -8.259 27.007 1.00 18.49 O ANISOU 1007 OG SER A 132 2350 2686 1988 -171 -144 299 O ATOM 1008 N PHE A 133 -27.514 -5.248 29.188 1.00 18.95 N ANISOU 1008 N PHE A 133 2262 2977 1959 -118 -119 240 N ATOM 1009 CA PHE A 133 -28.295 -4.041 29.435 1.00 19.45 C ANISOU 1009 CA PHE A 133 2270 3107 2013 -87 -113 207 C ATOM 1010 C PHE A 133 -27.658 -3.188 30.527 1.00 21.52 C ANISOU 1010 C PHE A 133 2528 3376 2270 -35 -126 183 C ATOM 1011 O PHE A 133 -27.608 -1.959 30.411 1.00 20.98 O ANISOU 1011 O PHE A 133 2431 3317 2225 13 -133 148 O ATOM 1012 CB PHE A 133 -29.734 -4.408 29.798 1.00 21.74 C ANISOU 1012 CB PHE A 133 2528 3478 2254 -133 -86 213 C ATOM 1013 CG PHE A 133 -30.636 -4.567 28.604 1.00 22.01 C ANISOU 1013 CG PHE A 133 2533 3530 2299 -163 -78 211 C ATOM 1014 CD1 PHE A 133 -31.286 -3.470 28.061 1.00 19.21 C ANISOU 1014 CD1 PHE A 133 2125 3214 1959 -124 -83 177 C ATOM 1015 CD2 PHE A 133 -30.828 -5.807 28.021 1.00 21.03 C ANISOU 1015 CD2 PHE A 133 2437 3382 2171 -226 -69 241 C ATOM 1016 CE1 PHE A 133 -32.113 -3.609 26.962 1.00 20.86 C ANISOU 1016 CE1 PHE A 133 2307 3443 2175 -146 -83 174 C ATOM 1017 CE2 PHE A 133 -31.653 -5.953 26.923 1.00 24.59 C ANISOU 1017 CE2 PHE A 133 2860 3853 2631 -254 -65 235 C ATOM 1018 CZ PHE A 133 -32.296 -4.851 26.391 1.00 24.31 C ANISOU 1018 CZ PHE A 133 2768 3861 2606 -213 -73 201 C ATOM 1019 N ALA A 134 -27.149 -3.821 31.586 1.00 21.66 N ANISOU 1019 N ALA A 134 2582 3388 2258 -42 -131 201 N ATOM 1020 CA ALA A 134 -26.527 -3.062 32.668 1.00 21.86 C ANISOU 1020 CA ALA A 134 2606 3426 2274 6 -147 176 C ATOM 1021 C ALA A 134 -25.260 -2.356 32.196 1.00 18.70 C ANISOU 1021 C ALA A 134 2210 2962 1934 53 -173 149 C ATOM 1022 O ALA A 134 -25.038 -1.185 32.523 1.00 15.82 O ANISOU 1022 O ALA A 134 1820 2609 1583 98 -181 110 O ATOM 1023 CB ALA A 134 -26.216 -3.984 33.847 1.00 23.54 C ANISOU 1023 CB ALA A 134 2866 3643 2437 -11 -153 205 C ATOM 1024 N ILE A 135 -24.414 -3.050 31.433 1.00 16.87 N ANISOU 1024 N ILE A 135 2009 2662 1739 43 -184 166 N ATOM 1025 CA ILE A 135 -23.181 -2.441 30.942 1.00 15.34 C ANISOU 1025 CA ILE A 135 1815 2410 1604 79 -203 137 C ATOM 1026 C ILE A 135 -23.491 -1.383 29.889 1.00 17.90 C ANISOU 1026 C ILE A 135 2109 2726 1964 92 -190 112 C ATOM 1027 O ILE A 135 -22.957 -0.268 29.927 1.00 15.21 O ANISOU 1027 O ILE A 135 1754 2373 1654 129 -197 75 O ATOM 1028 CB ILE A 135 -22.235 -3.520 30.385 1.00 18.00 C ANISOU 1028 CB ILE A 135 2190 2681 1970 65 -214 158 C ATOM 1029 CG1 ILE A 135 -21.703 -4.400 31.518 1.00 27.01 C ANISOU 1029 CG1 ILE A 135 3367 3818 3077 70 -237 177 C ATOM 1030 CG2 ILE A 135 -21.090 -2.876 29.617 1.00 23.82 C ANISOU 1030 CG2 ILE A 135 2917 3362 2771 92 -222 124 C ATOM 1031 CD1 ILE A 135 -21.015 -5.667 31.043 1.00 26.96 C ANISOU 1031 CD1 ILE A 135 3404 3750 3088 54 -248 204 C ATOM 1032 N GLY A 136 -24.355 -1.720 28.930 1.00 16.35 N ANISOU 1032 N GLY A 136 1909 2537 1765 61 -173 132 N ATOM 1033 CA GLY A 136 -24.614 -0.815 27.825 1.00 15.36 C ANISOU 1033 CA GLY A 136 1767 2398 1671 75 -166 114 C ATOM 1034 C GLY A 136 -25.341 0.450 28.232 1.00 16.97 C ANISOU 1034 C GLY A 136 1936 2650 1863 111 -165 84 C ATOM 1035 O GLY A 136 -25.129 1.507 27.631 1.00 17.72 O ANISOU 1035 O GLY A 136 2027 2717 1988 142 -167 60 O ATOM 1036 N LEU A 137 -26.198 0.369 29.250 1.00 14.46 N ANISOU 1036 N LEU A 137 1595 2401 1497 109 -160 85 N ATOM 1037 CA LEU A 137 -26.973 1.516 29.705 1.00 17.34 C ANISOU 1037 CA LEU A 137 1923 2819 1847 147 -157 52 C ATOM 1038 C LEU A 137 -26.381 2.163 30.951 1.00 16.05 C ANISOU 1038 C LEU A 137 1759 2666 1676 182 -167 23 C ATOM 1039 O LEU A 137 -27.062 2.952 31.613 1.00 14.76 O ANISOU 1039 O LEU A 137 1565 2554 1488 211 -163 -5 O ATOM 1040 CB LEU A 137 -28.422 1.104 29.968 1.00 18.67 C ANISOU 1040 CB LEU A 137 2057 3069 1967 122 -140 62 C ATOM 1041 CG LEU A 137 -29.192 0.530 28.773 1.00 16.71 C ANISOU 1041 CG LEU A 137 1800 2825 1723 88 -133 83 C ATOM 1042 CD1 LEU A 137 -30.639 0.256 29.159 1.00 25.09 C ANISOU 1042 CD1 LEU A 137 2815 3978 2739 64 -116 81 C ATOM 1043 CD2 LEU A 137 -29.122 1.459 27.567 1.00 16.54 C ANISOU 1043 CD2 LEU A 137 1780 2765 1742 123 -145 67 C ATOM 1044 N THR A 138 -25.135 1.842 31.289 1.00 14.71 N ANISOU 1044 N THR A 138 1618 2449 1524 183 -181 25 N ATOM 1045 CA THR A 138 -24.489 2.491 32.426 1.00 15.35 C ANISOU 1045 CA THR A 138 1696 2537 1598 217 -196 -8 C ATOM 1046 C THR A 138 -24.572 4.011 32.365 1.00 14.36 C ANISOU 1046 C THR A 138 1551 2409 1496 262 -197 -55 C ATOM 1047 O THR A 138 -24.823 4.628 33.415 1.00 14.91 O ANISOU 1047 O THR A 138 1605 2523 1538 289 -199 -84 O ATOM 1048 CB THR A 138 -23.025 2.034 32.521 1.00 16.64 C ANISOU 1048 CB THR A 138 1888 2643 1792 216 -217 -8 C ATOM 1049 OG1 THR A 138 -22.974 0.688 33.011 1.00 22.26 O ANISOU 1049 OG1 THR A 138 2625 3364 2468 187 -222 31 O ATOM 1050 CG2 THR A 138 -22.230 2.937 33.456 1.00 19.75 C ANISOU 1050 CG2 THR A 138 2275 3036 2194 255 -236 -54 C ATOM 1051 N PRO A 139 -24.390 4.668 31.216 1.00 14.66 N ANISOU 1051 N PRO A 139 1593 2396 1580 272 -194 -64 N ATOM 1052 CA PRO A 139 -24.548 6.132 31.183 1.00 15.42 C ANISOU 1052 CA PRO A 139 1681 2485 1695 316 -195 -106 C ATOM 1053 C PRO A 139 -25.888 6.611 31.708 1.00 16.76 C ANISOU 1053 C PRO A 139 1818 2727 1824 342 -188 -120 C ATOM 1054 O PRO A 139 -25.971 7.723 32.244 1.00 15.66 O ANISOU 1054 O PRO A 139 1670 2596 1686 384 -192 -162 O ATOM 1055 CB PRO A 139 -24.377 6.466 29.696 1.00 15.74 C ANISOU 1055 CB PRO A 139 1741 2461 1778 312 -189 -97 C ATOM 1056 CG PRO A 139 -23.540 5.363 29.159 1.00 14.09 C ANISOU 1056 CG PRO A 139 1553 2212 1588 270 -188 -67 C ATOM 1057 CD PRO A 139 -23.954 4.136 29.914 1.00 15.88 C ANISOU 1057 CD PRO A 139 1771 2493 1771 244 -189 -38 C ATOM 1058 N AMET A 140 -26.943 5.804 31.566 0.50 17.40 N ANISOU 1058 N AMET A 140 1879 2863 1870 317 -177 -91 N ATOM 1059 N BMET A 140 -26.947 5.814 31.570 0.50 17.40 N ANISOU 1059 N BMET A 140 1879 2863 1870 317 -177 -91 N ATOM 1060 CA AMET A 140 -28.250 6.193 32.083 0.50 19.54 C ANISOU 1060 CA AMET A 140 2109 3214 2102 338 -167 -109 C ATOM 1061 CA BMET A 140 -28.247 6.231 32.079 0.50 19.54 C ANISOU 1061 CA BMET A 140 2109 3213 2103 340 -167 -110 C ATOM 1062 C AMET A 140 -28.221 6.358 33.596 0.50 20.26 C ANISOU 1062 C AMET A 140 2188 3356 2154 352 -165 -135 C ATOM 1063 C BMET A 140 -28.304 6.233 33.600 0.50 20.36 C ANISOU 1063 C BMET A 140 2199 3375 2163 347 -163 -131 C ATOM 1064 O AMET A 140 -29.034 7.103 34.155 0.50 19.08 O ANISOU 1064 O AMET A 140 2006 3261 1981 387 -158 -169 O ATOM 1065 O BMET A 140 -29.273 6.750 34.164 0.50 19.04 O ANISOU 1065 O BMET A 140 1995 3274 1964 373 -153 -158 O ATOM 1066 CB AMET A 140 -29.302 5.152 31.692 0.50 20.29 C ANISOU 1066 CB AMET A 140 2181 3362 2167 296 -152 -75 C ATOM 1067 CB BMET A 140 -29.345 5.328 31.516 0.50 20.32 C ANISOU 1067 CB BMET A 140 2183 3360 2176 303 -154 -78 C ATOM 1068 CG AMET A 140 -29.409 4.886 30.196 0.50 20.71 C ANISOU 1068 CG AMET A 140 2247 3373 2251 280 -156 -50 C ATOM 1069 CG BMET A 140 -29.388 5.296 29.996 0.50 20.12 C ANISOU 1069 CG BMET A 140 2172 3285 2187 297 -161 -59 C ATOM 1070 SD AMET A 140 -30.104 6.268 29.271 0.50 18.80 S ANISOU 1070 SD AMET A 140 1989 3121 2032 341 -169 -80 S ATOM 1071 SD BMET A 140 -30.872 4.510 29.346 0.50 25.03 S ANISOU 1071 SD BMET A 140 2755 3977 2780 263 -150 -38 S ATOM 1072 CE AMET A 140 -31.814 6.220 29.805 0.50 25.19 C ANISOU 1072 CE AMET A 140 2728 4049 2793 351 -158 -99 C ATOM 1073 CE BMET A 140 -32.083 5.804 29.603 0.50 25.37 C ANISOU 1073 CE BMET A 140 2744 4087 2810 332 -155 -87 C ATOM 1074 N LEU A 141 -27.299 5.675 34.272 1.00 16.41 N ANISOU 1074 N LEU A 141 1727 2852 1656 328 -171 -120 N ATOM 1075 CA LEU A 141 -27.208 5.721 35.725 1.00 18.20 C ANISOU 1075 CA LEU A 141 1950 3127 1837 337 -172 -140 C ATOM 1076 C LEU A 141 -26.504 6.970 36.237 1.00 20.68 C ANISOU 1076 C LEU A 141 2267 3415 2174 387 -189 -194 C ATOM 1077 O LEU A 141 -26.353 7.116 37.454 1.00 20.46 O ANISOU 1077 O LEU A 141 2239 3425 2109 399 -193 -217 O ATOM 1078 CB LEU A 141 -26.477 4.480 36.249 1.00 18.69 C ANISOU 1078 CB LEU A 141 2046 3179 1875 298 -180 -103 C ATOM 1079 CG LEU A 141 -27.039 3.119 35.833 1.00 24.75 C ANISOU 1079 CG LEU A 141 2823 3962 2620 242 -164 -48 C ATOM 1080 CD1 LEU A 141 -26.425 2.012 36.678 1.00 23.20 C ANISOU 1080 CD1 LEU A 141 2668 3763 2386 214 -173 -16 C ATOM 1081 CD2 LEU A 141 -28.551 3.105 35.941 1.00 27.32 C ANISOU 1081 CD2 LEU A 141 3107 4367 2904 228 -134 -49 C ATOM 1082 N GLY A 142 -26.064 7.862 35.350 1.00 17.57 N ANISOU 1082 N GLY A 142 1882 2957 1838 411 -197 -214 N ATOM 1083 CA GLY A 142 -25.475 9.118 35.774 1.00 17.64 C ANISOU 1083 CA GLY A 142 1896 2936 1871 453 -210 -268 C ATOM 1084 C GLY A 142 -24.174 9.467 35.081 1.00 17.80 C ANISOU 1084 C GLY A 142 1945 2866 1953 448 -223 -276 C ATOM 1085 O GLY A 142 -23.739 10.621 35.124 1.00 19.37 O ANISOU 1085 O GLY A 142 2152 3026 2183 477 -228 -321 O ATOM 1086 N TRP A 143 -23.534 8.489 34.443 1.00 16.05 N ANISOU 1086 N TRP A 143 1739 2608 1750 409 -225 -237 N ATOM 1087 CA TRP A 143 -22.286 8.742 33.724 1.00 14.87 C ANISOU 1087 CA TRP A 143 1611 2377 1660 398 -231 -248 C ATOM 1088 C TRP A 143 -22.614 9.226 32.311 1.00 16.17 C ANISOU 1088 C TRP A 143 1790 2492 1861 398 -216 -235 C ATOM 1089 O TRP A 143 -22.474 8.517 31.314 1.00 14.98 O ANISOU 1089 O TRP A 143 1652 2313 1728 367 -209 -199 O ATOM 1090 CB TRP A 143 -21.416 7.491 33.709 1.00 16.50 C ANISOU 1090 CB TRP A 143 1827 2569 1872 364 -241 -218 C ATOM 1091 CG TRP A 143 -19.987 7.752 33.323 1.00 18.16 C ANISOU 1091 CG TRP A 143 2048 2713 2140 356 -250 -243 C ATOM 1092 CD1 TRP A 143 -19.441 8.948 32.951 1.00 14.38 C ANISOU 1092 CD1 TRP A 143 1574 2183 1707 367 -244 -286 C ATOM 1093 CD2 TRP A 143 -18.923 6.794 33.272 1.00 14.85 C ANISOU 1093 CD2 TRP A 143 1634 2270 1740 334 -264 -232 C ATOM 1094 NE1 TRP A 143 -18.107 8.793 32.673 1.00 16.60 N ANISOU 1094 NE1 TRP A 143 1858 2416 2035 347 -250 -304 N ATOM 1095 CE2 TRP A 143 -17.763 7.481 32.862 1.00 17.04 C ANISOU 1095 CE2 TRP A 143 1909 2489 2075 331 -264 -273 C ATOM 1096 CE3 TRP A 143 -18.840 5.424 33.531 1.00 16.89 C ANISOU 1096 CE3 TRP A 143 1898 2548 1971 317 -276 -192 C ATOM 1097 CZ2 TRP A 143 -16.534 6.843 32.705 1.00 16.43 C ANISOU 1097 CZ2 TRP A 143 1827 2381 2033 315 -276 -280 C ATOM 1098 CZ3 TRP A 143 -17.620 4.792 33.376 1.00 14.72 C ANISOU 1098 CZ3 TRP A 143 1627 2237 1729 307 -292 -196 C ATOM 1099 CH2 TRP A 143 -16.484 5.501 32.965 1.00 15.80 C ANISOU 1099 CH2 TRP A 143 1753 2324 1927 308 -292 -242 C ATOM 1100 N ASN A 144 -23.071 10.475 32.250 1.00 16.07 N ANISOU 1100 N ASN A 144 1780 2470 1857 435 -213 -268 N ATOM 1101 CA ASN A 144 -23.483 11.091 30.998 1.00 17.50 C ANISOU 1101 CA ASN A 144 1982 2605 2063 445 -203 -259 C ATOM 1102 C ASN A 144 -23.182 12.582 31.065 1.00 19.03 C ANISOU 1102 C ASN A 144 2197 2748 2285 480 -204 -307 C ATOM 1103 O ASN A 144 -22.780 13.111 32.103 1.00 18.40 O ANISOU 1103 O ASN A 144 2110 2679 2204 497 -212 -350 O ATOM 1104 CB ASN A 144 -24.969 10.849 30.720 1.00 19.05 C ANISOU 1104 CB ASN A 144 2157 2860 2222 462 -200 -234 C ATOM 1105 CG ASN A 144 -25.859 11.359 31.834 1.00 16.26 C ANISOU 1105 CG ASN A 144 1771 2577 1830 503 -204 -267 C ATOM 1106 OD1 ASN A 144 -25.960 12.563 32.056 1.00 23.50 O ANISOU 1106 OD1 ASN A 144 2695 3475 2757 548 -208 -308 O ATOM 1107 ND2 ASN A 144 -26.514 10.444 32.537 1.00 16.44 N ANISOU 1107 ND2 ASN A 144 1760 2680 1806 487 -199 -250 N ATOM 1108 N ASN A 145 -23.386 13.260 29.936 1.00 17.91 N ANISOU 1108 N ASN A 145 2089 2549 2167 492 -197 -299 N ATOM 1109 CA ASN A 145 -23.165 14.696 29.840 1.00 22.73 C ANISOU 1109 CA ASN A 145 2734 3098 2804 523 -196 -339 C ATOM 1110 C ASN A 145 -24.462 15.493 29.910 1.00 21.87 C ANISOU 1110 C ASN A 145 2622 3017 2670 585 -205 -352 C ATOM 1111 O ASN A 145 -24.468 16.681 29.573 1.00 25.60 O ANISOU 1111 O ASN A 145 3136 3428 3163 618 -206 -376 O ATOM 1112 CB ASN A 145 -22.418 15.032 28.548 1.00 23.48 C ANISOU 1112 CB ASN A 145 2882 3099 2942 495 -181 -325 C ATOM 1113 CG ASN A 145 -21.041 14.400 28.486 1.00 26.41 C ANISOU 1113 CG ASN A 145 3250 3440 3344 438 -170 -326 C ATOM 1114 OD1 ASN A 145 -20.396 14.185 29.512 1.00 32.88 O ANISOU 1114 OD1 ASN A 145 4041 4286 4167 429 -178 -355 O ATOM 1115 ND2 ASN A 145 -20.582 14.102 27.277 1.00 24.97 N ANISOU 1115 ND2 ASN A 145 3098 3204 3185 401 -152 -297 N ATOM 1116 N CYS A 146 -25.562 14.869 30.342 1.00 21.93 N ANISOU 1116 N CYS A 146 2583 3114 2634 602 -211 -339 N ATOM 1117 CA CYS A 146 -26.829 15.586 30.419 1.00 26.24 C ANISOU 1117 CA CYS A 146 3115 3696 3157 666 -221 -357 C ATOM 1118 C CYS A 146 -26.801 16.702 31.454 1.00 29.72 C ANISOU 1118 C CYS A 146 3557 4137 3599 712 -226 -417 C ATOM 1119 O CYS A 146 -27.636 17.611 31.388 1.00 27.96 O ANISOU 1119 O CYS A 146 3339 3915 3371 774 -235 -442 O ATOM 1120 CB CYS A 146 -27.969 14.613 30.730 1.00 26.72 C ANISOU 1120 CB CYS A 146 3118 3863 3173 664 -221 -336 C ATOM 1121 SG CYS A 146 -28.370 13.502 29.357 1.00 25.50 S ANISOU 1121 SG CYS A 146 2963 3711 3016 623 -219 -272 S ATOM 1122 N GLY A 147 -25.864 16.661 32.402 1.00 30.38 N ANISOU 1122 N GLY A 147 3637 4219 3688 687 -223 -445 N ATOM 1123 CA GLY A 147 -25.736 17.743 33.361 1.00 35.62 C ANISOU 1123 CA GLY A 147 4306 4876 4353 727 -228 -507 C ATOM 1124 C GLY A 147 -25.124 19.004 32.786 1.00 35.77 C ANISOU 1124 C GLY A 147 4386 4786 4418 742 -228 -534 C ATOM 1125 O GLY A 147 -25.294 20.081 33.366 1.00 40.68 O ANISOU 1125 O GLY A 147 5022 5393 5043 788 -233 -585 O ATOM 1126 N GLN A 148 -24.420 18.896 31.661 1.00 32.36 N ANISOU 1126 N GLN A 148 3996 4277 4022 702 -219 -501 N ATOM 1127 CA GLN A 148 -23.770 20.033 31.008 1.00 33.87 C ANISOU 1127 CA GLN A 148 4255 4357 4256 703 -212 -520 C ATOM 1128 C GLN A 148 -24.227 20.099 29.557 1.00 33.35 C ANISOU 1128 C GLN A 148 4233 4242 4197 710 -210 -471 C ATOM 1129 O GLN A 148 -23.441 19.865 28.630 1.00 34.39 O ANISOU 1129 O GLN A 148 4400 4311 4354 660 -194 -443 O ATOM 1130 CB GLN A 148 -22.248 19.923 31.093 1.00 44.05 C ANISOU 1130 CB GLN A 148 5556 5595 5584 637 -199 -535 C ATOM 1131 CG GLN A 148 -21.694 19.873 32.512 1.00 53.91 C ANISOU 1131 CG GLN A 148 6765 6891 6826 630 -208 -586 C ATOM 1132 CD GLN A 148 -21.814 18.499 33.146 1.00 66.31 C ANISOU 1132 CD GLN A 148 8276 8558 8360 611 -216 -559 C ATOM 1133 OE1 GLN A 148 -21.881 17.483 32.452 1.00 51.60 O ANISOU 1133 OE1 GLN A 148 6404 6709 6493 582 -211 -506 O ATOM 1134 NE2 GLN A 148 -21.840 18.462 34.474 1.00 68.50 N ANISOU 1134 NE2 GLN A 148 8519 8898 8609 627 -229 -597 N ATOM 1135 N PRO A 149 -25.497 20.419 29.324 1.00 28.81 N ANISOU 1135 N PRO A 149 3655 3696 3595 775 -226 -465 N ATOM 1136 CA PRO A 149 -25.997 20.481 27.947 1.00 29.15 C ANISOU 1136 CA PRO A 149 3741 3697 3637 789 -231 -420 C ATOM 1137 C PRO A 149 -25.405 21.652 27.181 1.00 31.86 C ANISOU 1137 C PRO A 149 4177 3914 4012 793 -223 -426 C ATOM 1138 O PRO A 149 -25.132 22.719 27.737 1.00 36.89 O ANISOU 1138 O PRO A 149 4847 4504 4668 818 -223 -473 O ATOM 1139 CB PRO A 149 -27.510 20.645 28.128 1.00 32.25 C ANISOU 1139 CB PRO A 149 4098 4162 3995 867 -256 -427 C ATOM 1140 CG PRO A 149 -27.654 21.306 29.460 1.00 34.54 C ANISOU 1140 CG PRO A 149 4361 4485 4280 907 -259 -488 C ATOM 1141 CD PRO A 149 -26.537 20.765 30.308 1.00 33.97 C ANISOU 1141 CD PRO A 149 4264 4425 4218 841 -241 -503 C ATOM 1142 N LYS A 150 -25.206 21.438 25.883 1.00 30.30 N ANISOU 1142 N LYS A 150 4030 3662 3821 765 -215 -378 N ATOM 1143 CA LYS A 150 -24.746 22.494 24.982 1.00 35.08 C ANISOU 1143 CA LYS A 150 4735 4145 4448 765 -204 -373 C ATOM 1144 C LYS A 150 -25.941 23.380 24.651 1.00 36.50 C ANISOU 1144 C LYS A 150 4953 4309 4606 859 -236 -374 C ATOM 1145 O LYS A 150 -26.678 23.141 23.692 1.00 32.28 O ANISOU 1145 O LYS A 150 4436 3781 4047 887 -254 -332 O ATOM 1146 CB LYS A 150 -24.121 21.897 23.727 1.00 33.13 C ANISOU 1146 CB LYS A 150 4528 3852 4208 700 -182 -322 C ATOM 1147 CG LYS A 150 -22.822 21.144 23.977 1.00 36.62 C ANISOU 1147 CG LYS A 150 4938 4296 4679 612 -150 -328 C ATOM 1148 CD LYS A 150 -22.319 20.472 22.710 1.00 36.12 C ANISOU 1148 CD LYS A 150 4907 4199 4619 553 -127 -280 C ATOM 1149 CE LYS A 150 -20.986 19.773 22.932 1.00 45.69 C ANISOU 1149 CE LYS A 150 6087 5410 5864 472 -95 -293 C ATOM 1150 NZ LYS A 150 -19.884 20.740 23.198 1.00 53.50 N ANISOU 1150 NZ LYS A 150 7114 6319 6894 437 -68 -338 N ATOM 1151 N GLU A 151 -26.136 24.423 25.463 1.00 37.05 N ANISOU 1151 N GLU A 151 5036 4358 4683 913 -247 -425 N ATOM 1152 CA GLU A 151 -27.301 25.286 25.292 1.00 42.29 C ANISOU 1152 CA GLU A 151 5730 5012 5328 1015 -281 -435 C ATOM 1153 C GLU A 151 -27.225 26.097 24.004 1.00 39.85 C ANISOU 1153 C GLU A 151 5537 4582 5021 1032 -285 -401 C ATOM 1154 O GLU A 151 -28.262 26.392 23.400 1.00 42.25 O ANISOU 1154 O GLU A 151 5865 4889 5300 1110 -321 -383 O ATOM 1155 CB GLU A 151 -27.444 26.220 26.494 1.00 47.23 C ANISOU 1155 CB GLU A 151 6345 5638 5962 1066 -289 -504 C ATOM 1156 CG GLU A 151 -27.803 25.509 27.789 1.00 45.94 C ANISOU 1156 CG GLU A 151 6070 5603 5782 1069 -290 -538 C ATOM 1157 CD GLU A 151 -29.195 24.906 27.759 1.00 50.37 C ANISOU 1157 CD GLU A 151 6559 6275 6305 1127 -317 -525 C ATOM 1158 OE1 GLU A 151 -29.914 25.111 26.758 1.00 53.41 O ANISOU 1158 OE1 GLU A 151 6978 6638 6678 1176 -340 -494 O ATOM 1159 OE2 GLU A 151 -29.571 24.228 28.738 1.00 55.99 O ANISOU 1159 OE2 GLU A 151 7180 7097 6996 1123 -314 -546 O ATOM 1160 N GLY A 152 -26.021 26.472 23.571 1.00 39.01 N ANISOU 1160 N GLY A 152 5508 4372 4944 961 -250 -394 N ATOM 1161 CA GLY A 152 -25.900 27.202 22.319 1.00 38.04 C ANISOU 1161 CA GLY A 152 5506 4130 4817 967 -247 -357 C ATOM 1162 C GLY A 152 -26.419 26.402 21.141 1.00 40.46 C ANISOU 1162 C GLY A 152 5817 4466 5091 967 -261 -293 C ATOM 1163 O GLY A 152 -27.183 26.907 20.314 1.00 40.29 O ANISOU 1163 O GLY A 152 5861 4405 5043 1034 -293 -266 O ATOM 1164 N LYS A 153 -26.010 25.135 21.051 1.00 38.23 N ANISOU 1164 N LYS A 153 5465 4252 4809 894 -241 -271 N ATOM 1165 CA LYS A 153 -26.499 24.272 19.983 1.00 35.92 C ANISOU 1165 CA LYS A 153 5168 3995 4485 889 -254 -215 C ATOM 1166 C LYS A 153 -27.997 24.025 20.121 1.00 37.37 C ANISOU 1166 C LYS A 153 5289 4275 4633 979 -306 -215 C ATOM 1167 O LYS A 153 -28.717 23.957 19.118 1.00 34.86 O ANISOU 1167 O LYS A 153 5005 3957 4285 1018 -335 -178 O ATOM 1168 CB LYS A 153 -25.725 22.953 19.998 1.00 35.53 C ANISOU 1168 CB LYS A 153 5053 3999 4446 793 -221 -199 C ATOM 1169 CG LYS A 153 -25.899 22.102 18.750 1.00 38.28 C ANISOU 1169 CG LYS A 153 5418 4359 4769 765 -221 -143 C ATOM 1170 CD LYS A 153 -25.088 20.810 18.825 1.00 38.39 C ANISOU 1170 CD LYS A 153 5370 4420 4797 675 -188 -133 C ATOM 1171 CE LYS A 153 -23.586 21.070 18.859 1.00 42.05 C ANISOU 1171 CE LYS A 153 5871 4805 5302 595 -137 -149 C ATOM 1172 NZ LYS A 153 -22.794 19.808 18.776 1.00 42.85 N ANISOU 1172 NZ LYS A 153 5918 4947 5417 515 -109 -138 N ATOM 1173 N ALA A 154 -28.486 23.898 21.357 1.00 32.67 N ANISOU 1173 N ALA A 154 4604 3769 4042 1012 -318 -260 N ATOM 1174 CA ALA A 154 -29.910 23.668 21.573 1.00 36.07 C ANISOU 1174 CA ALA A 154 4963 4300 4442 1094 -361 -269 C ATOM 1175 C ALA A 154 -30.736 24.881 21.164 1.00 38.07 C ANISOU 1175 C ALA A 154 5284 4499 4682 1201 -403 -278 C ATOM 1176 O ALA A 154 -31.772 24.739 20.503 1.00 39.53 O ANISOU 1176 O ALA A 154 5458 4724 4837 1262 -444 -259 O ATOM 1177 CB ALA A 154 -30.165 23.318 23.039 1.00 30.86 C ANISOU 1177 CB ALA A 154 4197 3742 3786 1098 -356 -317 C ATOM 1178 N HIS A 155 -30.301 26.083 21.551 1.00 39.13 N ANISOU 1178 N HIS A 155 5488 4540 4838 1229 -396 -311 N ATOM 1179 CA HIS A 155 -31.046 27.284 21.186 1.00 41.09 C ANISOU 1179 CA HIS A 155 5808 4730 5074 1323 -434 -318 C ATOM 1180 C HIS A 155 -31.009 27.522 19.682 1.00 39.62 C ANISOU 1180 C HIS A 155 5729 4460 4867 1319 -446 -258 C ATOM 1181 O HIS A 155 -32.022 27.903 19.084 1.00 44.46 O ANISOU 1181 O HIS A 155 6355 5090 5448 1380 -487 -244 O ATOM 1182 CB HIS A 155 -30.488 28.496 21.930 1.00 42.17 C ANISOU 1182 CB HIS A 155 5997 4786 5240 1321 -415 -361 C ATOM 1183 CG HIS A 155 -30.786 28.494 23.396 1.00 46.30 C ANISOU 1183 CG HIS A 155 6423 5398 5773 1343 -413 -424 C ATOM 1184 ND1 HIS A 155 -32.068 28.401 23.894 1.00 52.86 N ANISOU 1184 ND1 HIS A 155 7165 6341 6579 1407 -445 -448 N ATOM 1185 CD2 HIS A 155 -29.970 28.584 24.473 1.00 49.62 C ANISOU 1185 CD2 HIS A 155 6819 5811 6221 1303 -382 -470 C ATOM 1186 CE1 HIS A 155 -32.029 28.426 25.214 1.00 56.15 C ANISOU 1186 CE1 HIS A 155 7513 6816 7007 1405 -431 -502 C ATOM 1187 NE2 HIS A 155 -30.767 28.537 25.591 1.00 52.51 N ANISOU 1187 NE2 HIS A 155 7089 6285 6575 1346 -395 -516 N ATOM 1188 N ASER A 156 -29.852 27.302 19.051 0.50 39.58 N ANISOU 1188 N ASER A 156 5799 4366 4875 1242 -407 -224 N ATOM 1189 N BSER A 156 -29.851 27.304 19.053 0.50 39.59 N ANISOU 1189 N BSER A 156 5799 4366 4875 1242 -407 -224 N ATOM 1190 CA ASER A 156 -29.753 27.512 17.611 0.50 42.11 C ANISOU 1190 CA ASER A 156 6226 4606 5168 1227 -411 -165 C ATOM 1191 CA BSER A 156 -29.747 27.509 17.613 0.50 42.11 C ANISOU 1191 CA BSER A 156 6226 4606 5168 1227 -411 -165 C ATOM 1192 C ASER A 156 -30.725 26.622 16.850 0.50 42.20 C ANISOU 1192 C ASER A 156 6190 4707 5139 1261 -452 -130 C ATOM 1193 C BSER A 156 -30.723 26.622 16.852 0.50 42.20 C ANISOU 1193 C BSER A 156 6190 4706 5139 1261 -452 -130 C ATOM 1194 O ASER A 156 -31.259 27.031 15.812 0.50 42.43 O ANISOU 1194 O ASER A 156 6283 4705 5132 1291 -480 -96 O ATOM 1195 O BSER A 156 -31.259 27.035 15.817 0.50 42.46 O ANISOU 1195 O BSER A 156 6288 4710 5136 1291 -480 -96 O ATOM 1196 CB ASER A 156 -28.321 27.258 17.138 0.50 41.37 C ANISOU 1196 CB ASER A 156 6197 4428 5095 1114 -350 -139 C ATOM 1197 CB BSER A 156 -28.315 27.243 17.149 0.50 41.38 C ANISOU 1197 CB BSER A 156 6195 4430 5095 1113 -349 -139 C ATOM 1198 OG ASER A 156 -27.992 25.882 17.217 0.50 44.17 O ANISOU 1198 OG ASER A 156 6454 4876 5453 1034 -326 -127 O ATOM 1199 OG BSER A 156 -28.183 27.457 15.755 0.50 42.56 O ANISOU 1199 OG BSER A 156 6460 4497 5215 1100 -349 -83 O ATOM 1200 N GLN A 157 -30.967 25.410 17.343 1.00 39.79 N ANISOU 1200 N GLN A 157 5760 4524 4836 1232 -449 -139 N ATOM 1201 CA GLN A 157 -31.917 24.496 16.727 1.00 39.24 C ANISOU 1201 CA GLN A 157 5629 4550 4730 1254 -485 -113 C ATOM 1202 C GLN A 157 -33.339 24.706 17.223 1.00 38.20 C ANISOU 1202 C GLN A 157 5415 4517 4582 1350 -537 -150 C ATOM 1203 O GLN A 157 -34.247 23.996 16.777 1.00 39.73 O ANISOU 1203 O GLN A 157 5546 4803 4748 1365 -567 -139 O ATOM 1204 CB GLN A 157 -31.499 23.046 16.984 1.00 42.15 C ANISOU 1204 CB GLN A 157 5901 5007 5107 1154 -449 -104 C ATOM 1205 CG GLN A 157 -30.241 22.628 16.242 1.00 46.99 C ANISOU 1205 CG GLN A 157 6579 5546 5729 1049 -400 -64 C ATOM 1206 CD GLN A 157 -29.921 21.156 16.409 1.00 51.10 C ANISOU 1206 CD GLN A 157 7009 6152 6255 963 -372 -53 C ATOM 1207 OE1 GLN A 157 -28.765 20.783 16.605 1.00 61.71 O ANISOU 1207 OE1 GLN A 157 8355 7464 7626 877 -323 -52 O ATOM 1208 NE2 GLN A 157 -30.944 20.309 16.322 1.00 47.86 N ANISOU 1208 NE2 GLN A 157 6517 5850 5819 986 -405 -48 N ATOM 1209 N GLY A 158 -33.555 25.651 18.132 1.00 39.52 N ANISOU 1209 N GLY A 158 5574 4676 4766 1392 -538 -198 N ATOM 1210 CA GLY A 158 -34.891 25.913 18.628 1.00 44.48 C ANISOU 1210 CA GLY A 158 6120 5400 5379 1462 -575 -239 C ATOM 1211 C GLY A 158 -35.445 24.829 19.522 1.00 47.60 C ANISOU 1211 C GLY A 158 6370 5943 5775 1447 -569 -269 C ATOM 1212 O GLY A 158 -36.659 24.604 19.528 1.00 46.44 O ANISOU 1212 O GLY A 158 6146 5894 5606 1483 -597 -288 O ATOM 1213 N CYS A 159 -34.589 24.144 20.277 1.00 40.32 N ANISOU 1213 N CYS A 159 5406 5037 4876 1390 -530 -275 N ATOM 1214 CA CYS A 159 -35.066 23.126 21.199 1.00 41.32 C ANISOU 1214 CA CYS A 159 5399 5301 4999 1366 -519 -301 C ATOM 1215 C CYS A 159 -35.729 23.774 22.413 1.00 48.43 C ANISOU 1215 C CYS A 159 6242 6258 5902 1409 -519 -364 C ATOM 1216 O CYS A 159 -35.503 24.944 22.732 1.00 49.45 O ANISOU 1216 O CYS A 159 6433 6311 6045 1446 -520 -389 O ATOM 1217 CB CYS A 159 -33.919 22.221 21.652 1.00 35.64 C ANISOU 1217 CB CYS A 159 4660 4583 4299 1265 -470 -286 C ATOM 1218 SG CYS A 159 -33.034 21.369 20.318 1.00 34.30 S ANISOU 1218 SG CYS A 159 4553 4353 4126 1168 -449 -215 S ATOM 1219 N GLY A 160 -36.559 22.987 23.097 1.00 47.20 N ANISOU 1219 N GLY A 160 5969 6236 5731 1398 -514 -389 N ATOM 1220 CA GLY A 160 -37.306 23.460 24.242 1.00 49.30 C ANISOU 1220 CA GLY A 160 6171 6570 5991 1433 -512 -448 C ATOM 1221 C GLY A 160 -36.572 23.237 25.551 1.00 50.93 C ANISOU 1221 C GLY A 160 6341 6799 6211 1393 -472 -477 C ATOM 1222 O GLY A 160 -35.395 22.874 25.593 1.00 46.70 O ANISOU 1222 O GLY A 160 5837 6212 5696 1345 -449 -456 O ATOM 1223 N GLU A 161 -37.300 23.465 26.643 1.00 57.72 N ANISOU 1223 N GLU A 161 7134 7740 7059 1415 -466 -529 N ATOM 1224 CA GLU A 161 -36.730 23.312 27.975 1.00 57.41 C ANISOU 1224 CA GLU A 161 7058 7731 7024 1382 -431 -562 C ATOM 1225 C GLU A 161 -36.385 21.854 28.247 1.00 53.91 C ANISOU 1225 C GLU A 161 6549 7364 6571 1305 -402 -537 C ATOM 1226 O GLU A 161 -37.164 20.946 27.945 1.00 57.25 O ANISOU 1226 O GLU A 161 6907 7873 6971 1282 -404 -519 O ATOM 1227 CB GLU A 161 -37.710 23.826 29.031 1.00 74.19 C ANISOU 1227 CB GLU A 161 9124 9933 9130 1422 -431 -622 C ATOM 1228 CG GLU A 161 -37.249 23.618 30.470 1.00 96.56 C ANISOU 1228 CG GLU A 161 11915 12814 11958 1388 -396 -658 C ATOM 1229 CD GLU A 161 -38.081 22.587 31.210 1.00102.19 C ANISOU 1229 CD GLU A 161 12523 13671 12636 1353 -374 -672 C ATOM 1230 OE1 GLU A 161 -39.323 22.725 31.228 1.00108.63 O ANISOU 1230 OE1 GLU A 161 13288 14556 13430 1388 -386 -697 O ATOM 1231 OE2 GLU A 161 -37.495 21.637 31.771 1.00100.75 O ANISOU 1231 OE2 GLU A 161 12307 13530 12443 1289 -344 -659 O ATOM 1232 N GLY A 162 -35.207 21.636 28.828 1.00 52.88 N ANISOU 1232 N GLY A 162 6435 7199 6456 1264 -377 -537 N ATOM 1233 CA GLY A 162 -34.743 20.301 29.133 1.00 50.53 C ANISOU 1233 CA GLY A 162 6088 6962 6150 1185 -350 -509 C ATOM 1234 C GLY A 162 -34.331 19.479 27.935 1.00 41.55 C ANISOU 1234 C GLY A 162 4983 5786 5019 1123 -351 -443 C ATOM 1235 O GLY A 162 -33.924 18.324 28.110 1.00 40.84 O ANISOU 1235 O GLY A 162 4865 5734 4921 1040 -328 -413 O ATOM 1236 N GLN A 163 -34.417 20.029 26.730 1.00 38.39 N ANISOU 1236 N GLN A 163 4646 5310 4630 1160 -378 -420 N ATOM 1237 CA GLN A 163 -34.063 19.311 25.517 1.00 36.86 C ANISOU 1237 CA GLN A 163 4489 5078 4438 1105 -380 -359 C ATOM 1238 C GLN A 163 -32.676 19.718 25.038 1.00 31.21 C ANISOU 1238 C GLN A 163 3872 4233 3753 1062 -363 -335 C ATOM 1239 O GLN A 163 -32.160 20.788 25.368 1.00 35.58 O ANISOU 1239 O GLN A 163 4480 4710 4327 1092 -361 -363 O ATOM 1240 CB GLN A 163 -35.087 19.570 24.409 1.00 33.68 C ANISOU 1240 CB GLN A 163 4094 4683 4021 1171 -422 -346 C ATOM 1241 CG GLN A 163 -36.454 18.974 24.675 1.00 34.16 C ANISOU 1241 CG GLN A 163 4048 4879 4052 1196 -436 -367 C ATOM 1242 CD GLN A 163 -37.355 19.042 23.461 1.00 36.51 C ANISOU 1242 CD GLN A 163 4359 5178 4334 1225 -471 -348 C ATOM 1243 OE1 GLN A 163 -37.125 19.836 22.547 1.00 35.61 O ANISOU 1243 OE1 GLN A 163 4334 4969 4228 1267 -497 -329 O ATOM 1244 NE2 GLN A 163 -38.384 18.204 23.439 1.00 40.64 N ANISOU 1244 NE2 GLN A 163 4798 5809 4834 1200 -472 -353 N ATOM 1245 N VAL A 164 -32.076 18.832 24.245 1.00 26.07 N ANISOU 1245 N VAL A 164 3242 3558 3105 988 -349 -285 N ATOM 1246 CA VAL A 164 -30.777 19.065 23.633 1.00 26.56 C ANISOU 1246 CA VAL A 164 3391 3507 3195 937 -328 -260 C ATOM 1247 C VAL A 164 -30.846 18.592 22.189 1.00 24.71 C ANISOU 1247 C VAL A 164 3196 3241 2949 914 -337 -207 C ATOM 1248 O VAL A 164 -31.713 17.802 21.813 1.00 24.40 O ANISOU 1248 O VAL A 164 3108 3279 2886 917 -354 -189 O ATOM 1249 CB VAL A 164 -29.639 18.332 24.377 1.00 25.60 C ANISOU 1249 CB VAL A 164 3246 3389 3092 853 -292 -261 C ATOM 1250 CG1 VAL A 164 -29.567 18.792 25.821 1.00 28.31 C ANISOU 1250 CG1 VAL A 164 3551 3765 3438 875 -286 -314 C ATOM 1251 CG2 VAL A 164 -29.839 16.821 24.303 1.00 25.70 C ANISOU 1251 CG2 VAL A 164 3197 3482 3085 794 -284 -228 C ATOM 1252 N ALA A 165 -29.926 19.101 21.374 1.00 22.24 N ANISOU 1252 N ALA A 165 2978 2817 2656 890 -323 -186 N ATOM 1253 CA ALA A 165 -29.699 18.531 20.052 1.00 23.21 C ANISOU 1253 CA ALA A 165 3145 2905 2768 848 -320 -135 C ATOM 1254 C ALA A 165 -29.116 17.137 20.240 1.00 25.23 C ANISOU 1254 C ALA A 165 3347 3209 3030 760 -291 -118 C ATOM 1255 O ALA A 165 -28.022 16.986 20.792 1.00 27.34 O ANISOU 1255 O ALA A 165 3616 3448 3326 706 -259 -129 O ATOM 1256 CB ALA A 165 -28.766 19.421 19.237 1.00 29.10 C ANISOU 1256 CB ALA A 165 4006 3520 3531 834 -303 -120 C ATOM 1257 N CYS A 166 -29.850 16.113 19.814 1.00 21.95 N ANISOU 1257 N CYS A 166 2883 2867 2588 747 -305 -94 N ATOM 1258 CA CYS A 166 -29.489 14.735 20.137 1.00 20.74 C ANISOU 1258 CA CYS A 166 2674 2769 2437 673 -283 -80 C ATOM 1259 C CYS A 166 -28.334 14.293 19.248 1.00 23.19 C ANISOU 1259 C CYS A 166 3042 3005 2764 603 -254 -49 C ATOM 1260 O CYS A 166 -28.524 13.963 18.075 1.00 22.90 O ANISOU 1260 O CYS A 166 3039 2950 2710 591 -261 -17 O ATOM 1261 CB CYS A 166 -30.687 13.807 19.979 1.00 23.31 C ANISOU 1261 CB CYS A 166 2931 3195 2730 677 -305 -69 C ATOM 1262 SG CYS A 166 -30.309 12.106 20.421 1.00 23.71 S ANISOU 1262 SG CYS A 166 2923 3306 2781 586 -278 -51 S ATOM 1263 N LEU A 167 -27.132 14.273 19.820 1.00 22.28 N ANISOU 1263 N LEU A 167 2933 2850 2681 558 -222 -63 N ATOM 1264 CA LEU A 167 -25.931 13.828 19.130 1.00 20.38 C ANISOU 1264 CA LEU A 167 2734 2546 2462 490 -190 -44 C ATOM 1265 C LEU A 167 -25.147 12.911 20.055 1.00 18.16 C ANISOU 1265 C LEU A 167 2399 2298 2202 439 -170 -56 C ATOM 1266 O LEU A 167 -24.994 13.202 21.245 1.00 19.33 O ANISOU 1266 O LEU A 167 2512 2471 2361 453 -171 -88 O ATOM 1267 CB LEU A 167 -25.072 15.020 18.692 1.00 24.06 C ANISOU 1267 CB LEU A 167 3283 2906 2952 490 -170 -53 C ATOM 1268 CG LEU A 167 -25.731 15.917 17.641 1.00 24.60 C ANISOU 1268 CG LEU A 167 3426 2924 2996 539 -189 -34 C ATOM 1269 CD1 LEU A 167 -24.993 17.237 17.525 1.00 26.47 C ANISOU 1269 CD1 LEU A 167 3744 3057 3255 545 -170 -50 C ATOM 1270 CD2 LEU A 167 -25.783 15.205 16.294 1.00 24.77 C ANISOU 1270 CD2 LEU A 167 3482 2935 2995 506 -185 9 C ATOM 1271 N PHE A 168 -24.656 11.803 19.494 1.00 16.66 N ANISOU 1271 N PHE A 168 2205 2109 2015 382 -154 -31 N ATOM 1272 CA PHE A 168 -24.016 10.761 20.292 1.00 18.80 C ANISOU 1272 CA PHE A 168 2427 2415 2301 339 -142 -37 C ATOM 1273 C PHE A 168 -22.945 11.337 21.211 1.00 15.99 C ANISOU 1273 C PHE A 168 2068 2028 1981 333 -128 -75 C ATOM 1274 O PHE A 168 -22.977 11.134 22.430 1.00 14.28 O ANISOU 1274 O PHE A 168 1803 1861 1761 343 -138 -95 O ATOM 1275 CB PHE A 168 -23.417 9.699 19.365 1.00 19.91 C ANISOU 1275 CB PHE A 168 2583 2534 2448 282 -123 -10 C ATOM 1276 CG PHE A 168 -22.861 8.505 20.092 1.00 16.42 C ANISOU 1276 CG PHE A 168 2095 2127 2016 245 -117 -12 C ATOM 1277 CD1 PHE A 168 -21.563 8.516 20.581 1.00 18.83 C ANISOU 1277 CD1 PHE A 168 2397 2398 2360 221 -99 -37 C ATOM 1278 CD2 PHE A 168 -23.635 7.373 20.286 1.00 19.31 C ANISOU 1278 CD2 PHE A 168 2423 2558 2354 234 -131 10 C ATOM 1279 CE1 PHE A 168 -21.050 7.421 21.252 1.00 17.52 C ANISOU 1279 CE1 PHE A 168 2194 2261 2201 196 -101 -37 C ATOM 1280 CE2 PHE A 168 -23.128 6.274 20.954 1.00 17.18 C ANISOU 1280 CE2 PHE A 168 2123 2312 2091 202 -127 13 C ATOM 1281 CZ PHE A 168 -21.831 6.298 21.438 1.00 16.92 C ANISOU 1281 CZ PHE A 168 2091 2243 2094 188 -115 -10 C ATOM 1282 N GLU A 169 -21.984 12.064 20.639 1.00 16.19 N ANISOU 1282 N GLU A 169 2144 1971 2035 314 -104 -87 N ATOM 1283 CA GLU A 169 -20.850 12.552 21.419 1.00 19.38 C ANISOU 1283 CA GLU A 169 2542 2344 2477 298 -89 -128 C ATOM 1284 C GLU A 169 -21.211 13.715 22.333 1.00 21.20 C ANISOU 1284 C GLU A 169 2771 2576 2707 347 -104 -163 C ATOM 1285 O GLU A 169 -20.374 14.120 23.147 1.00 19.07 O ANISOU 1285 O GLU A 169 2489 2291 2465 337 -97 -203 O ATOM 1286 CB GLU A 169 -19.709 12.961 20.484 1.00 17.82 C ANISOU 1286 CB GLU A 169 2397 2060 2313 253 -52 -134 C ATOM 1287 CG GLU A 169 -19.046 11.779 19.792 1.00 18.82 C ANISOU 1287 CG GLU A 169 2516 2187 2450 200 -32 -114 C ATOM 1288 CD GLU A 169 -17.840 12.175 18.957 1.00 19.78 C ANISOU 1288 CD GLU A 169 2680 2229 2606 151 12 -129 C ATOM 1289 OE1 GLU A 169 -17.225 13.220 19.246 1.00 24.88 O ANISOU 1289 OE1 GLU A 169 3346 2828 3278 146 28 -164 O ATOM 1290 OE2 GLU A 169 -17.509 11.436 18.007 1.00 19.72 O ANISOU 1290 OE2 GLU A 169 2687 2209 2598 114 33 -108 O ATOM 1291 N ASP A 170 -22.422 14.257 22.229 1.00 18.54 N ANISOU 1291 N ASP A 170 2445 2259 2340 401 -126 -153 N ATOM 1292 CA ASP A 170 -22.860 15.301 23.143 1.00 18.75 C ANISOU 1292 CA ASP A 170 2467 2294 2364 454 -143 -190 C ATOM 1293 C ASP A 170 -23.456 14.758 24.436 1.00 19.36 C ANISOU 1293 C ASP A 170 2471 2466 2418 476 -162 -205 C ATOM 1294 O ASP A 170 -23.468 15.479 25.440 1.00 23.07 O ANISOU 1294 O ASP A 170 2928 2946 2891 507 -170 -245 O ATOM 1295 CB ASP A 170 -23.891 16.207 22.461 1.00 24.65 C ANISOU 1295 CB ASP A 170 3260 3016 3089 513 -160 -178 C ATOM 1296 CG ASP A 170 -23.264 17.145 21.442 1.00 31.20 C ANISOU 1296 CG ASP A 170 4180 3737 3939 500 -140 -173 C ATOM 1297 OD1 ASP A 170 -22.040 17.048 21.214 1.00 33.67 O ANISOU 1297 OD1 ASP A 170 4512 3998 4282 440 -107 -179 O ATOM 1298 OD2 ASP A 170 -23.996 17.981 20.871 1.00 30.29 O ANISOU 1298 OD2 ASP A 170 4116 3587 3805 552 -157 -163 O ATOM 1299 N VAL A 171 -23.946 13.518 24.445 1.00 16.63 N ANISOU 1299 N VAL A 171 2081 2188 2047 458 -168 -175 N ATOM 1300 CA VAL A 171 -24.602 12.948 25.613 1.00 16.23 C ANISOU 1300 CA VAL A 171 1969 2230 1968 473 -182 -184 C ATOM 1301 C VAL A 171 -23.797 11.799 26.215 1.00 15.41 C ANISOU 1301 C VAL A 171 1835 2152 1869 423 -175 -177 C ATOM 1302 O VAL A 171 -23.790 11.627 27.437 1.00 16.62 O ANISOU 1302 O VAL A 171 1952 2355 2007 431 -182 -199 O ATOM 1303 CB VAL A 171 -26.040 12.494 25.272 1.00 17.29 C ANISOU 1303 CB VAL A 171 2075 2433 2064 497 -197 -159 C ATOM 1304 CG1 VAL A 171 -26.875 13.689 24.829 1.00 23.57 C ANISOU 1304 CG1 VAL A 171 2894 3208 2852 561 -213 -172 C ATOM 1305 CG2 VAL A 171 -26.040 11.415 24.201 1.00 15.63 C ANISOU 1305 CG2 VAL A 171 1872 2218 1849 452 -191 -113 C ATOM 1306 N VAL A 172 -23.115 11.010 25.393 1.00 14.29 N ANISOU 1306 N VAL A 172 1709 1976 1744 376 -162 -150 N ATOM 1307 CA VAL A 172 -22.325 9.878 25.868 1.00 14.20 C ANISOU 1307 CA VAL A 172 1675 1982 1739 335 -159 -143 C ATOM 1308 C VAL A 172 -20.911 10.381 26.157 1.00 15.32 C ANISOU 1308 C VAL A 172 1829 2069 1924 320 -150 -180 C ATOM 1309 O VAL A 172 -20.245 10.872 25.234 1.00 15.71 O ANISOU 1309 O VAL A 172 1915 2049 2006 302 -132 -184 O ATOM 1310 CB VAL A 172 -22.298 8.735 24.846 1.00 16.01 C ANISOU 1310 CB VAL A 172 1913 2202 1966 295 -150 -101 C ATOM 1311 CG1 VAL A 172 -21.567 7.532 25.424 1.00 16.93 C ANISOU 1311 CG1 VAL A 172 2008 2337 2086 262 -152 -93 C ATOM 1312 CG2 VAL A 172 -23.710 8.352 24.435 1.00 18.30 C ANISOU 1312 CG2 VAL A 172 2191 2544 2217 306 -159 -70 C ATOM 1313 N PRO A 173 -20.417 10.274 27.393 1.00 16.16 N ANISOU 1313 N PRO A 173 1906 2206 2030 325 -162 -208 N ATOM 1314 CA PRO A 173 -19.060 10.759 27.678 1.00 15.53 C ANISOU 1314 CA PRO A 173 1829 2079 1992 310 -158 -250 C ATOM 1315 C PRO A 173 -18.015 9.900 26.986 1.00 14.97 C ANISOU 1315 C PRO A 173 1760 1975 1953 266 -145 -239 C ATOM 1316 O PRO A 173 -18.149 8.677 26.899 1.00 13.71 O ANISOU 1316 O PRO A 173 1588 1844 1777 251 -151 -205 O ATOM 1317 CB PRO A 173 -18.949 10.652 29.207 1.00 17.10 C ANISOU 1317 CB PRO A 173 1993 2335 2171 330 -181 -279 C ATOM 1318 CG PRO A 173 -20.343 10.409 29.701 1.00 20.27 C ANISOU 1318 CG PRO A 173 2378 2805 2518 358 -191 -256 C ATOM 1319 CD PRO A 173 -21.044 9.697 28.594 1.00 16.15 C ANISOU 1319 CD PRO A 173 1868 2284 1986 341 -181 -205 C ATOM 1320 N MET A 174 -16.958 10.552 26.501 1.00 14.84 N ANISOU 1320 N MET A 174 1760 1895 1983 243 -125 -270 N ATOM 1321 CA MET A 174 -15.950 9.823 25.746 1.00 14.31 C ANISOU 1321 CA MET A 174 1692 1795 1949 201 -107 -266 C ATOM 1322 C MET A 174 -15.010 9.038 26.650 1.00 12.30 C ANISOU 1322 C MET A 174 1395 1570 1709 197 -128 -290 C ATOM 1323 O MET A 174 -14.432 8.042 26.205 1.00 12.83 O ANISOU 1323 O MET A 174 1453 1631 1791 175 -124 -278 O ATOM 1324 CB MET A 174 -15.149 10.780 24.864 1.00 18.41 C ANISOU 1324 CB MET A 174 2243 2239 2512 172 -72 -293 C ATOM 1325 CG MET A 174 -14.402 10.075 23.745 1.00 24.28 C ANISOU 1325 CG MET A 174 2996 2948 3282 128 -43 -281 C ATOM 1326 SD MET A 174 -15.494 9.280 22.543 1.00 26.44 S ANISOU 1326 SD MET A 174 3304 3226 3517 125 -36 -212 S ATOM 1327 CE MET A 174 -16.080 10.707 21.638 1.00 29.03 C ANISOU 1327 CE MET A 174 3698 3496 3836 131 -14 -205 C ATOM 1328 N ASN A 175 -14.846 9.446 27.912 1.00 11.66 N ANISOU 1328 N ASN A 175 1289 1521 1622 221 -153 -327 N ATOM 1329 CA ASN A 175 -14.072 8.611 28.824 1.00 13.89 C ANISOU 1329 CA ASN A 175 1534 1837 1905 226 -182 -344 C ATOM 1330 C ASN A 175 -14.790 7.294 29.091 1.00 12.86 C ANISOU 1330 C ASN A 175 1401 1754 1729 236 -201 -291 C ATOM 1331 O ASN A 175 -14.146 6.247 29.212 1.00 12.25 O ANISOU 1331 O ASN A 175 1311 1684 1659 230 -216 -284 O ATOM 1332 CB ASN A 175 -13.773 9.351 30.131 1.00 13.83 C ANISOU 1332 CB ASN A 175 1505 1857 1895 251 -208 -395 C ATOM 1333 CG ASN A 175 -15.008 9.943 30.783 1.00 18.12 C ANISOU 1333 CG ASN A 175 2059 2437 2390 284 -216 -386 C ATOM 1334 OD1 ASN A 175 -16.138 9.622 30.425 1.00 20.53 O ANISOU 1334 OD1 ASN A 175 2380 2761 2660 292 -209 -339 O ATOM 1335 ND2 ASN A 175 -14.789 10.815 31.758 1.00 20.84 N ANISOU 1335 ND2 ASN A 175 2391 2793 2733 304 -231 -436 N ATOM 1336 N TYR A 176 -16.124 7.318 29.158 1.00 13.05 N ANISOU 1336 N TYR A 176 1440 1811 1707 251 -201 -255 N ATOM 1337 CA TYR A 176 -16.874 6.068 29.205 1.00 13.50 C ANISOU 1337 CA TYR A 176 1500 1907 1722 247 -209 -202 C ATOM 1338 C TYR A 176 -16.616 5.230 27.958 1.00 9.62 C ANISOU 1338 C TYR A 176 1024 1377 1253 215 -191 -172 C ATOM 1339 O TYR A 176 -16.313 4.036 28.049 1.00 12.34 O ANISOU 1339 O TYR A 176 1368 1729 1592 206 -203 -150 O ATOM 1340 CB TYR A 176 -18.375 6.344 29.356 1.00 13.75 C ANISOU 1340 CB TYR A 176 1537 1981 1706 263 -206 -177 C ATOM 1341 CG TYR A 176 -19.219 5.113 29.099 1.00 14.03 C ANISOU 1341 CG TYR A 176 1578 2049 1705 245 -205 -123 C ATOM 1342 CD1 TYR A 176 -19.513 4.220 30.123 1.00 13.34 C ANISOU 1342 CD1 TYR A 176 1482 2012 1574 247 -222 -104 C ATOM 1343 CD2 TYR A 176 -19.700 4.829 27.827 1.00 11.98 C ANISOU 1343 CD2 TYR A 176 1335 1766 1452 224 -185 -92 C ATOM 1344 CE1 TYR A 176 -20.268 3.086 29.887 1.00 15.37 C ANISOU 1344 CE1 TYR A 176 1749 2293 1798 223 -217 -56 C ATOM 1345 CE2 TYR A 176 -20.454 3.699 27.583 1.00 14.22 C ANISOU 1345 CE2 TYR A 176 1622 2077 1703 202 -184 -48 C ATOM 1346 CZ TYR A 176 -20.734 2.829 28.617 1.00 16.12 C ANISOU 1346 CZ TYR A 176 1855 2364 1904 199 -199 -30 C ATOM 1347 OH TYR A 176 -21.486 1.702 28.376 1.00 20.44 O ANISOU 1347 OH TYR A 176 2410 2935 2420 170 -194 12 O ATOM 1348 N MET A 177 -16.736 5.841 26.775 1.00 11.27 N ANISOU 1348 N MET A 177 1255 1544 1485 200 -162 -169 N ATOM 1349 CA MET A 177 -16.613 5.075 25.537 1.00 12.26 C ANISOU 1349 CA MET A 177 1399 1636 1623 169 -143 -140 C ATOM 1350 C MET A 177 -15.227 4.467 25.373 1.00 10.13 C ANISOU 1350 C MET A 177 1117 1336 1396 152 -140 -163 C ATOM 1351 O MET A 177 -15.097 3.371 24.815 1.00 11.72 O ANISOU 1351 O MET A 177 1326 1529 1599 135 -137 -138 O ATOM 1352 CB MET A 177 -16.939 5.962 24.335 1.00 14.71 C ANISOU 1352 CB MET A 177 1741 1904 1944 159 -114 -136 C ATOM 1353 CG MET A 177 -18.418 6.282 24.184 1.00 17.72 C ANISOU 1353 CG MET A 177 2134 2316 2282 178 -119 -106 C ATOM 1354 SD MET A 177 -19.447 4.808 24.015 1.00 15.78 S ANISOU 1354 SD MET A 177 1883 2120 1993 164 -129 -54 S ATOM 1355 CE MET A 177 -18.826 4.117 22.481 1.00 18.48 C ANISOU 1355 CE MET A 177 2255 2406 2361 124 -105 -37 C ATOM 1356 N VAL A 178 -14.184 5.149 25.839 1.00 9.80 N ANISOU 1356 N VAL A 178 1054 1279 1391 157 -143 -215 N ATOM 1357 CA VAL A 178 -12.819 4.678 25.625 1.00 11.63 C ANISOU 1357 CA VAL A 178 1264 1484 1669 142 -139 -247 C ATOM 1358 C VAL A 178 -12.398 3.742 26.752 1.00 12.64 C ANISOU 1358 C VAL A 178 1367 1650 1787 167 -182 -252 C ATOM 1359 O VAL A 178 -12.054 2.581 26.510 1.00 11.57 O ANISOU 1359 O VAL A 178 1231 1510 1656 165 -190 -235 O ATOM 1360 CB VAL A 178 -11.843 5.861 25.492 1.00 11.07 C ANISOU 1360 CB VAL A 178 1180 1378 1647 127 -117 -307 C ATOM 1361 CG1 VAL A 178 -10.405 5.366 25.469 1.00 16.15 C ANISOU 1361 CG1 VAL A 178 1786 2010 2340 116 -118 -351 C ATOM 1362 CG2 VAL A 178 -12.151 6.662 24.232 1.00 16.99 C ANISOU 1362 CG2 VAL A 178 1969 2079 2406 98 -72 -296 C ATOM 1363 N TYR A 179 -12.422 4.234 27.993 1.00 13.36 N ANISOU 1363 N TYR A 179 1440 1776 1861 195 -211 -275 N ATOM 1364 CA TYR A 179 -11.921 3.437 29.111 1.00 15.12 C ANISOU 1364 CA TYR A 179 1643 2032 2069 223 -256 -283 C ATOM 1365 C TYR A 179 -12.870 2.293 29.454 1.00 15.41 C ANISOU 1365 C TYR A 179 1707 2100 2049 232 -274 -222 C ATOM 1366 O TYR A 179 -12.437 1.149 29.637 1.00 14.72 O ANISOU 1366 O TYR A 179 1623 2011 1959 241 -297 -207 O ATOM 1367 CB TYR A 179 -11.712 4.322 30.340 1.00 14.55 C ANISOU 1367 CB TYR A 179 1548 1991 1988 249 -283 -327 C ATOM 1368 CG TYR A 179 -10.562 5.298 30.237 1.00 17.54 C ANISOU 1368 CG TYR A 179 1895 2343 2425 238 -274 -398 C ATOM 1369 CD1 TYR A 179 -9.357 4.931 29.651 1.00 20.90 C ANISOU 1369 CD1 TYR A 179 2294 2741 2906 223 -267 -431 C ATOM 1370 CD2 TYR A 179 -10.680 6.585 30.738 1.00 18.56 C ANISOU 1370 CD2 TYR A 179 2020 2477 2557 242 -270 -436 C ATOM 1371 CE1 TYR A 179 -8.307 5.821 29.565 1.00 21.64 C ANISOU 1371 CE1 TYR A 179 2353 2814 3054 205 -254 -500 C ATOM 1372 CE2 TYR A 179 -9.633 7.482 30.656 1.00 21.60 C ANISOU 1372 CE2 TYR A 179 2376 2835 2995 224 -260 -503 C ATOM 1373 CZ TYR A 179 -8.449 7.095 30.069 1.00 22.83 C ANISOU 1373 CZ TYR A 179 2503 2967 3205 203 -250 -535 C ATOM 1374 OH TYR A 179 -7.404 7.983 29.982 1.00 28.97 O ANISOU 1374 OH TYR A 179 3248 3722 4038 178 -234 -607 O ATOM 1375 N PHE A 180 -14.164 2.586 29.575 1.00 12.52 N ANISOU 1375 N PHE A 180 1359 1760 1638 230 -263 -188 N ATOM 1376 CA PHE A 180 -15.123 1.613 30.093 1.00 14.78 C ANISOU 1376 CA PHE A 180 1666 2084 1865 232 -277 -136 C ATOM 1377 C PHE A 180 -15.631 0.685 28.991 1.00 12.72 C ANISOU 1377 C PHE A 180 1430 1800 1602 202 -255 -89 C ATOM 1378 O PHE A 180 -15.508 -0.540 29.096 1.00 14.16 O ANISOU 1378 O PHE A 180 1630 1979 1770 198 -270 -60 O ATOM 1379 CB PHE A 180 -16.289 2.340 30.772 1.00 14.41 C ANISOU 1379 CB PHE A 180 1619 2085 1771 243 -274 -129 C ATOM 1380 CG PHE A 180 -17.200 1.433 31.555 1.00 14.05 C ANISOU 1380 CG PHE A 180 1589 2087 1660 242 -286 -85 C ATOM 1381 CD1 PHE A 180 -18.253 0.782 30.936 1.00 13.50 C ANISOU 1381 CD1 PHE A 180 1538 2027 1566 214 -265 -37 C ATOM 1382 CD2 PHE A 180 -17.006 1.239 32.914 1.00 18.24 C ANISOU 1382 CD2 PHE A 180 2121 2655 2153 265 -316 -92 C ATOM 1383 CE1 PHE A 180 -19.094 -0.049 31.652 1.00 20.05 C ANISOU 1383 CE1 PHE A 180 2383 2901 2336 203 -269 1 C ATOM 1384 CE2 PHE A 180 -17.845 0.408 33.636 1.00 20.80 C ANISOU 1384 CE2 PHE A 180 2467 3022 2413 258 -321 -49 C ATOM 1385 CZ PHE A 180 -18.890 -0.236 33.005 1.00 16.81 C ANISOU 1385 CZ PHE A 180 1978 2524 1885 224 -295 -3 C ATOM 1386 N ASN A 181 -16.202 1.251 27.927 1.00 11.84 N ANISOU 1386 N ASN A 181 1325 1671 1502 182 -223 -82 N ATOM 1387 CA ASN A 181 -16.768 0.409 26.879 1.00 11.11 C ANISOU 1387 CA ASN A 181 1256 1563 1402 152 -204 -41 C ATOM 1388 C ASN A 181 -15.674 -0.279 26.068 1.00 13.34 C ANISOU 1388 C ASN A 181 1544 1795 1729 139 -198 -50 C ATOM 1389 O ASN A 181 -15.672 -1.507 25.930 1.00 15.64 O ANISOU 1389 O ASN A 181 1854 2079 2011 128 -205 -22 O ATOM 1390 CB ASN A 181 -17.675 1.232 25.967 1.00 14.76 C ANISOU 1390 CB ASN A 181 1725 2023 1859 140 -177 -32 C ATOM 1391 CG ASN A 181 -18.471 0.363 25.013 1.00 15.20 C ANISOU 1391 CG ASN A 181 1802 2076 1896 111 -164 10 C ATOM 1392 OD1 ASN A 181 -18.072 0.146 23.870 1.00 17.18 O ANISOU 1392 OD1 ASN A 181 2069 2285 2174 90 -146 12 O ATOM 1393 ND2 ASN A 181 -19.597 -0.152 25.487 1.00 13.52 N ANISOU 1393 ND2 ASN A 181 1590 1911 1636 104 -171 42 N ATOM 1394 N PHE A 182 -14.730 0.491 25.525 1.00 12.80 N ANISOU 1394 N PHE A 182 1461 1691 1710 137 -181 -92 N ATOM 1395 CA PHE A 182 -13.755 -0.091 24.604 1.00 13.06 C ANISOU 1395 CA PHE A 182 1495 1679 1786 121 -165 -106 C ATOM 1396 C PHE A 182 -12.732 -0.948 25.345 1.00 13.45 C ANISOU 1396 C PHE A 182 1529 1730 1853 144 -198 -125 C ATOM 1397 O PHE A 182 -12.655 -2.162 25.133 1.00 14.99 O ANISOU 1397 O PHE A 182 1741 1912 2043 142 -207 -101 O ATOM 1398 CB PHE A 182 -13.065 1.014 23.799 1.00 12.43 C ANISOU 1398 CB PHE A 182 1407 1565 1752 105 -131 -147 C ATOM 1399 CG PHE A 182 -12.074 0.503 22.783 1.00 15.55 C ANISOU 1399 CG PHE A 182 1800 1918 2190 84 -106 -167 C ATOM 1400 CD1 PHE A 182 -12.354 -0.619 22.020 1.00 15.55 C ANISOU 1400 CD1 PHE A 182 1825 1904 2179 68 -99 -134 C ATOM 1401 CD2 PHE A 182 -10.869 1.157 22.582 1.00 16.62 C ANISOU 1401 CD2 PHE A 182 1908 2029 2377 75 -87 -223 C ATOM 1402 CE1 PHE A 182 -11.449 -1.082 21.078 1.00 17.53 C ANISOU 1402 CE1 PHE A 182 2074 2118 2468 51 -73 -156 C ATOM 1403 CE2 PHE A 182 -9.961 0.699 21.647 1.00 19.32 C ANISOU 1403 CE2 PHE A 182 2243 2338 2759 54 -59 -247 C ATOM 1404 CZ PHE A 182 -10.250 -0.424 20.896 1.00 21.04 C ANISOU 1404 CZ PHE A 182 2487 2544 2964 44 -52 -213 C ATOM 1405 N PHE A 183 -11.934 -0.335 26.222 1.00 14.41 N ANISOU 1405 N PHE A 183 1617 1864 1995 169 -219 -171 N ATOM 1406 CA PHE A 183 -10.856 -1.073 26.877 1.00 14.91 C ANISOU 1406 CA PHE A 183 1659 1928 2078 199 -256 -196 C ATOM 1407 C PHE A 183 -11.406 -2.213 27.728 1.00 16.85 C ANISOU 1407 C PHE A 183 1934 2195 2271 220 -294 -149 C ATOM 1408 O PHE A 183 -11.058 -3.382 27.526 1.00 15.86 O ANISOU 1408 O PHE A 183 1826 2048 2150 227 -307 -134 O ATOM 1409 CB PHE A 183 -10.006 -0.131 27.737 1.00 14.58 C ANISOU 1409 CB PHE A 183 1575 1904 2061 221 -276 -257 C ATOM 1410 CG PHE A 183 -9.136 0.820 26.949 1.00 15.90 C ANISOU 1410 CG PHE A 183 1711 2042 2289 196 -239 -313 C ATOM 1411 CD1 PHE A 183 -9.068 0.759 25.567 1.00 22.16 C ANISOU 1411 CD1 PHE A 183 2516 2795 3108 160 -192 -307 C ATOM 1412 CD2 PHE A 183 -8.376 1.774 27.606 1.00 22.59 C ANISOU 1412 CD2 PHE A 183 2518 2901 3164 206 -251 -373 C ATOM 1413 CE1 PHE A 183 -8.264 1.633 24.859 1.00 20.16 C ANISOU 1413 CE1 PHE A 183 2240 2514 2905 131 -152 -357 C ATOM 1414 CE2 PHE A 183 -7.572 2.647 26.902 1.00 24.94 C ANISOU 1414 CE2 PHE A 183 2790 3171 3517 175 -212 -426 C ATOM 1415 CZ PHE A 183 -7.516 2.575 25.526 1.00 21.28 C ANISOU 1415 CZ PHE A 183 2343 2667 3077 136 -161 -416 C ATOM 1416 N ALA A 184 -12.275 -1.890 28.687 1.00 14.24 N ANISOU 1416 N ALA A 184 1614 1906 1889 229 -309 -127 N ATOM 1417 CA ALA A 184 -12.680 -2.877 29.682 1.00 17.13 C ANISOU 1417 CA ALA A 184 2011 2296 2202 247 -345 -88 C ATOM 1418 C ALA A 184 -13.692 -3.875 29.131 1.00 16.13 C ANISOU 1418 C ALA A 184 1929 2161 2042 216 -327 -26 C ATOM 1419 O ALA A 184 -13.583 -5.076 29.398 1.00 16.06 O ANISOU 1419 O ALA A 184 1953 2137 2014 223 -349 3 O ATOM 1420 CB ALA A 184 -13.255 -2.173 30.911 1.00 17.83 C ANISOU 1420 CB ALA A 184 2095 2437 2243 263 -362 -89 C ATOM 1421 N CYS A 185 -14.679 -3.408 28.364 1.00 12.03 N ANISOU 1421 N CYS A 185 1412 1647 1513 182 -289 -8 N ATOM 1422 CA CYS A 185 -15.798 -4.260 27.984 1.00 14.58 C ANISOU 1422 CA CYS A 185 1770 1973 1796 148 -274 46 C ATOM 1423 C CYS A 185 -15.669 -4.873 26.597 1.00 16.30 C ANISOU 1423 C CYS A 185 2003 2145 2045 120 -249 55 C ATOM 1424 O CYS A 185 -16.396 -5.826 26.298 1.00 15.07 O ANISOU 1424 O CYS A 185 1880 1985 1862 92 -243 96 O ATOM 1425 CB CYS A 185 -17.110 -3.471 28.052 1.00 16.67 C ANISOU 1425 CB CYS A 185 2025 2283 2024 131 -253 61 C ATOM 1426 SG CYS A 185 -17.578 -2.974 29.723 1.00 22.07 S ANISOU 1426 SG CYS A 185 2701 3031 2655 157 -275 58 S ATOM 1427 N VAL A 186 -14.781 -4.359 25.748 1.00 14.13 N ANISOU 1427 N VAL A 186 1707 1838 1825 123 -233 16 N ATOM 1428 CA VAL A 186 -14.638 -4.871 24.388 1.00 16.73 C ANISOU 1428 CA VAL A 186 2051 2124 2180 96 -206 21 C ATOM 1429 C VAL A 186 -13.252 -5.473 24.181 1.00 15.34 C ANISOU 1429 C VAL A 186 1868 1909 2052 116 -216 -12 C ATOM 1430 O VAL A 186 -13.120 -6.670 23.900 1.00 15.48 O ANISOU 1430 O VAL A 186 1913 1899 2069 113 -223 6 O ATOM 1431 CB VAL A 186 -14.908 -3.761 23.354 1.00 12.62 C ANISOU 1431 CB VAL A 186 1520 1598 1676 74 -169 5 C ATOM 1432 CG1 VAL A 186 -14.612 -4.256 21.947 1.00 14.32 C ANISOU 1432 CG1 VAL A 186 1753 1771 1917 47 -140 4 C ATOM 1433 CG2 VAL A 186 -16.349 -3.273 23.455 1.00 18.32 C ANISOU 1433 CG2 VAL A 186 2249 2361 2352 61 -163 37 C ATOM 1434 N ALEU A 187 -12.213 -4.652 24.343 0.60 16.29 N ANISOU 1434 N ALEU A 187 1948 2027 2215 136 -217 -65 N ATOM 1435 N BLEU A 187 -12.211 -4.643 24.296 0.40 16.50 N ANISOU 1435 N BLEU A 187 1974 2052 2242 135 -216 -65 N ATOM 1436 CA ALEU A 187 -10.855 -5.095 24.040 0.60 17.02 C ANISOU 1436 CA ALEU A 187 2019 2087 2359 155 -222 -108 C ATOM 1437 CA BLEU A 187 -10.854 -5.118 24.037 0.40 17.02 C ANISOU 1437 CA BLEU A 187 2020 2087 2360 155 -222 -108 C ATOM 1438 C ALEU A 187 -10.429 -6.253 24.938 0.60 17.63 C ANISOU 1438 C ALEU A 187 2110 2162 2427 195 -271 -98 C ATOM 1439 C BLEU A 187 -10.499 -6.293 24.935 0.40 17.64 C ANISOU 1439 C BLEU A 187 2114 2164 2425 193 -271 -95 C ATOM 1440 O ALEU A 187 -9.910 -7.267 24.459 0.60 17.93 O ANISOU 1440 O ALEU A 187 2162 2165 2485 203 -275 -101 O ATOM 1441 O BLEU A 187 -10.088 -7.356 24.454 0.40 18.07 O ANISOU 1441 O BLEU A 187 2187 2183 2495 199 -275 -92 O ATOM 1442 CB ALEU A 187 -9.892 -3.915 24.183 0.60 18.62 C ANISOU 1442 CB ALEU A 187 2170 2297 2607 165 -215 -170 C ATOM 1443 CB BLEU A 187 -9.841 -3.988 24.234 0.40 18.64 C ANISOU 1443 CB BLEU A 187 2172 2299 2610 167 -218 -171 C ATOM 1444 CG ALEU A 187 -8.441 -4.151 23.773 0.60 19.73 C ANISOU 1444 CG ALEU A 187 2273 2413 2810 178 -211 -229 C ATOM 1445 CG BLEU A 187 -9.527 -3.083 23.043 0.40 18.68 C ANISOU 1445 CG BLEU A 187 2163 2281 2653 131 -164 -202 C ATOM 1446 CD1ALEU A 187 -8.354 -4.631 22.333 0.60 23.23 C ANISOU 1446 CD1ALEU A 187 2735 2819 3275 145 -166 -226 C ATOM 1447 CD1BLEU A 187 -8.380 -2.148 23.394 0.40 21.34 C ANISOU 1447 CD1BLEU A 187 2447 2624 3039 141 -163 -270 C ATOM 1448 CD2ALEU A 187 -7.652 -2.870 23.959 0.60 23.67 C ANISOU 1448 CD2ALEU A 187 2720 2923 3348 175 -198 -290 C ATOM 1449 CD2BLEU A 187 -9.198 -3.879 21.785 0.40 18.53 C ANISOU 1449 CD2BLEU A 187 2159 2225 2657 109 -133 -203 C ATOM 1450 N VAL A 188 -10.632 -6.117 26.250 1.00 15.94 N ANISOU 1450 N VAL A 188 1896 1982 2177 222 -310 -88 N ATOM 1451 CA VAL A 188 -10.231 -7.175 27.176 1.00 17.54 C ANISOU 1451 CA VAL A 188 2121 2180 2362 264 -362 -75 C ATOM 1452 C VAL A 188 -10.928 -8.492 26.856 1.00 16.34 C ANISOU 1452 C VAL A 188 2032 1999 2177 246 -360 -18 C ATOM 1453 O VAL A 188 -10.235 -9.513 26.712 1.00 20.36 O ANISOU 1453 O VAL A 188 2559 2470 2706 272 -382 -22 O ATOM 1454 CB VAL A 188 -10.451 -6.717 28.628 1.00 19.10 C ANISOU 1454 CB VAL A 188 2316 2423 2516 291 -400 -70 C ATOM 1455 CG1 VAL A 188 -10.453 -7.913 29.573 1.00 23.05 C ANISOU 1455 CG1 VAL A 188 2866 2918 2974 324 -449 -33 C ATOM 1456 CG2 VAL A 188 -9.374 -5.719 29.030 1.00 18.09 C ANISOU 1456 CG2 VAL A 188 2127 2315 2432 321 -416 -140 C ATOM 1457 N PRO A 189 -12.257 -8.553 26.724 1.00 19.12 N ANISOU 1457 N PRO A 189 2418 2366 2482 203 -337 33 N ATOM 1458 CA PRO A 189 -12.879 -9.828 26.325 1.00 17.79 C ANISOU 1458 CA PRO A 189 2307 2166 2287 177 -331 81 C ATOM 1459 C PRO A 189 -12.366 -10.366 24.999 1.00 15.37 C ANISOU 1459 C PRO A 189 2003 1809 2027 165 -307 63 C ATOM 1460 O PRO A 189 -12.188 -11.582 24.857 1.00 18.26 O ANISOU 1460 O PRO A 189 2412 2134 2392 171 -321 81 O ATOM 1461 CB PRO A 189 -14.372 -9.479 26.259 1.00 22.01 C ANISOU 1461 CB PRO A 189 2853 2736 2772 127 -302 122 C ATOM 1462 CG PRO A 189 -14.531 -8.354 27.208 1.00 19.67 C ANISOU 1462 CG PRO A 189 2523 2492 2458 145 -312 107 C ATOM 1463 CD PRO A 189 -13.265 -7.551 27.111 1.00 18.55 C ANISOU 1463 CD PRO A 189 2332 2343 2373 181 -320 47 C ATOM 1464 N LEU A 190 -12.131 -9.496 24.015 1.00 14.75 N ANISOU 1464 N LEU A 190 1886 1732 1987 146 -270 28 N ATOM 1465 CA LEU A 190 -11.621 -9.965 22.731 1.00 16.45 C ANISOU 1465 CA LEU A 190 2104 1904 2243 133 -243 7 C ATOM 1466 C LEU A 190 -10.225 -10.554 22.878 1.00 19.19 C ANISOU 1466 C LEU A 190 2435 2220 2636 182 -269 -36 C ATOM 1467 O LEU A 190 -9.885 -11.541 22.214 1.00 18.46 O ANISOU 1467 O LEU A 190 2367 2084 2561 185 -265 -39 O ATOM 1468 CB LEU A 190 -11.618 -8.823 21.717 1.00 15.82 C ANISOU 1468 CB LEU A 190 1991 1832 2188 103 -196 -22 C ATOM 1469 CG LEU A 190 -12.984 -8.400 21.168 1.00 15.72 C ANISOU 1469 CG LEU A 190 1998 1839 2135 55 -168 17 C ATOM 1470 CD1 LEU A 190 -12.843 -7.159 20.305 1.00 19.86 C ANISOU 1470 CD1 LEU A 190 2496 2368 2683 37 -129 -12 C ATOM 1471 CD2 LEU A 190 -13.630 -9.527 20.370 1.00 17.08 C ANISOU 1471 CD2 LEU A 190 2217 1984 2287 22 -156 50 C ATOM 1472 N LEU A 191 -9.401 -9.965 23.748 1.00 16.26 N ANISOU 1472 N LEU A 191 2021 1873 2285 225 -298 -73 N ATOM 1473 CA LEU A 191 -8.081 -10.530 24.005 1.00 20.10 C ANISOU 1473 CA LEU A 191 2484 2338 2814 281 -333 -118 C ATOM 1474 C LEU A 191 -8.191 -11.860 24.736 1.00 20.69 C ANISOU 1474 C LEU A 191 2618 2386 2856 316 -382 -78 C ATOM 1475 O LEU A 191 -7.397 -12.776 24.493 1.00 23.44 O ANISOU 1475 O LEU A 191 2976 2696 3235 353 -401 -99 O ATOM 1476 CB LEU A 191 -7.235 -9.542 24.808 1.00 18.43 C ANISOU 1476 CB LEU A 191 2210 2165 2629 315 -356 -171 C ATOM 1477 CG LEU A 191 -6.847 -8.246 24.088 1.00 22.43 C ANISOU 1477 CG LEU A 191 2658 2686 3178 283 -308 -221 C ATOM 1478 CD1 LEU A 191 -6.147 -7.285 25.042 1.00 26.98 C ANISOU 1478 CD1 LEU A 191 3177 3301 3772 312 -335 -270 C ATOM 1479 CD2 LEU A 191 -5.970 -8.536 22.878 1.00 29.53 C ANISOU 1479 CD2 LEU A 191 3533 3554 4134 275 -271 -268 C ATOM 1480 N LEU A 192 -9.168 -11.987 25.637 1.00 22.74 N ANISOU 1480 N LEU A 192 2922 2665 3053 306 -401 -22 N ATOM 1481 CA LEU A 192 -9.398 -13.269 26.293 1.00 18.83 C ANISOU 1481 CA LEU A 192 2498 2138 2517 328 -441 25 C ATOM 1482 C LEU A 192 -9.808 -14.333 25.283 1.00 20.74 C ANISOU 1482 C LEU A 192 2792 2326 2760 295 -415 52 C ATOM 1483 O LEU A 192 -9.343 -15.477 25.353 1.00 21.98 O ANISOU 1483 O LEU A 192 2995 2434 2924 330 -445 58 O ATOM 1484 CB LEU A 192 -10.462 -13.123 27.382 1.00 17.38 C ANISOU 1484 CB LEU A 192 2351 1991 2261 310 -454 81 C ATOM 1485 CG LEU A 192 -10.081 -12.270 28.595 1.00 25.80 C ANISOU 1485 CG LEU A 192 3381 3107 3313 350 -490 59 C ATOM 1486 CD1 LEU A 192 -11.260 -12.150 29.544 1.00 35.83 C ANISOU 1486 CD1 LEU A 192 4691 4415 4508 322 -491 114 C ATOM 1487 CD2 LEU A 192 -8.869 -12.850 29.314 1.00 32.93 C ANISOU 1487 CD2 LEU A 192 4288 3991 4234 427 -554 32 C ATOM 1488 N MET A 193 -10.684 -13.978 24.339 1.00 18.90 N ANISOU 1488 N MET A 193 2558 2102 2521 230 -362 67 N ATOM 1489 CA MET A 193 -11.045 -14.916 23.279 1.00 22.03 C ANISOU 1489 CA MET A 193 2998 2451 2921 194 -336 83 C ATOM 1490 C MET A 193 -9.810 -15.365 22.512 1.00 19.58 C ANISOU 1490 C MET A 193 2670 2098 2673 232 -336 29 C ATOM 1491 O MET A 193 -9.650 -16.553 22.210 1.00 18.30 O ANISOU 1491 O MET A 193 2558 1880 2515 243 -346 38 O ATOM 1492 CB MET A 193 -12.047 -14.278 22.319 1.00 17.46 C ANISOU 1492 CB MET A 193 2408 1897 2330 126 -283 95 C ATOM 1493 CG MET A 193 -13.416 -14.032 22.900 1.00 24.43 C ANISOU 1493 CG MET A 193 3311 2820 3152 83 -278 147 C ATOM 1494 SD MET A 193 -14.479 -13.237 21.683 1.00 27.86 S ANISOU 1494 SD MET A 193 3723 3284 3577 17 -224 151 S ATOM 1495 CE MET A 193 -15.256 -11.990 22.709 1.00 20.45 C ANISOU 1495 CE MET A 193 2749 2420 2602 15 -228 165 C ATOM 1496 N LEU A 194 -8.935 -14.420 22.169 1.00 20.57 N ANISOU 1496 N LEU A 194 2722 2246 2847 250 -321 -30 N ATOM 1497 CA LEU A 194 -7.696 -14.772 21.487 1.00 24.73 C ANISOU 1497 CA LEU A 194 3218 2742 3435 286 -317 -91 C ATOM 1498 C LEU A 194 -6.928 -15.821 22.280 1.00 21.96 C ANISOU 1498 C LEU A 194 2893 2358 3094 359 -378 -97 C ATOM 1499 O LEU A 194 -6.457 -16.819 21.725 1.00 24.03 O ANISOU 1499 O LEU A 194 3181 2569 3381 382 -382 -113 O ATOM 1500 CB LEU A 194 -6.845 -13.519 21.274 1.00 23.11 C ANISOU 1500 CB LEU A 194 2928 2575 3278 292 -295 -156 C ATOM 1501 CG LEU A 194 -5.500 -13.731 20.576 1.00 28.53 C ANISOU 1501 CG LEU A 194 3566 3242 4032 325 -283 -230 C ATOM 1502 CD1 LEU A 194 -5.703 -14.252 19.161 1.00 32.91 C ANISOU 1502 CD1 LEU A 194 4148 3759 4596 284 -232 -233 C ATOM 1503 CD2 LEU A 194 -4.702 -12.440 20.568 1.00 27.13 C ANISOU 1503 CD2 LEU A 194 3304 3107 3896 324 -262 -292 C ATOM 1504 N GLY A 195 -6.807 -15.614 23.593 1.00 25.43 N ANISOU 1504 N GLY A 195 3329 2823 3509 400 -429 -85 N ATOM 1505 CA GLY A 195 -6.122 -16.590 24.422 1.00 26.76 C ANISOU 1505 CA GLY A 195 3530 2959 3677 476 -495 -85 C ATOM 1506 C GLY A 195 -6.804 -17.944 24.417 1.00 28.24 C ANISOU 1506 C GLY A 195 3821 3086 3825 466 -507 -24 C ATOM 1507 O GLY A 195 -6.140 -18.984 24.409 1.00 23.02 O ANISOU 1507 O GLY A 195 3194 2371 3183 521 -542 -36 O ATOM 1508 N VAL A 196 -8.138 -17.954 24.423 1.00 23.89 N ANISOU 1508 N VAL A 196 3320 2541 3218 396 -479 40 N ATOM 1509 CA VAL A 196 -8.867 -19.219 24.424 1.00 20.32 C ANISOU 1509 CA VAL A 196 2966 2030 2724 372 -484 99 C ATOM 1510 C VAL A 196 -8.628 -19.969 23.119 1.00 23.05 C ANISOU 1510 C VAL A 196 3329 2320 3110 360 -455 74 C ATOM 1511 O VAL A 196 -8.362 -21.176 23.117 1.00 22.52 O ANISOU 1511 O VAL A 196 3328 2185 3045 391 -481 84 O ATOM 1512 CB VAL A 196 -10.367 -18.979 24.670 1.00 21.36 C ANISOU 1512 CB VAL A 196 3133 2192 2792 292 -454 162 C ATOM 1513 CG1 VAL A 196 -11.163 -20.249 24.402 1.00 22.20 C ANISOU 1513 CG1 VAL A 196 3334 2237 2862 249 -445 214 C ATOM 1514 CG2 VAL A 196 -10.601 -18.502 26.094 1.00 20.59 C ANISOU 1514 CG2 VAL A 196 3039 2140 2646 311 -489 191 C ATOM 1515 N TYR A 197 -8.721 -19.266 21.987 1.00 20.04 N ANISOU 1515 N TYR A 197 2892 1964 2759 314 -399 40 N ATOM 1516 CA TYR A 197 -8.506 -19.923 20.704 1.00 26.07 C ANISOU 1516 CA TYR A 197 3670 2679 3555 299 -366 13 C ATOM 1517 C TYR A 197 -7.066 -20.397 20.551 1.00 25.05 C ANISOU 1517 C TYR A 197 3514 2516 3486 380 -393 -50 C ATOM 1518 O TYR A 197 -6.823 -21.437 19.930 1.00 26.10 O ANISOU 1518 O TYR A 197 3692 2588 3638 393 -392 -62 O ATOM 1519 CB TYR A 197 -8.895 -18.987 19.559 1.00 23.62 C ANISOU 1519 CB TYR A 197 3310 2407 3257 235 -303 -8 C ATOM 1520 CG TYR A 197 -10.393 -18.886 19.370 1.00 25.88 C ANISOU 1520 CG TYR A 197 3634 2711 3487 154 -275 50 C ATOM 1521 CD1 TYR A 197 -11.141 -20.008 19.040 1.00 22.25 C ANISOU 1521 CD1 TYR A 197 3252 2204 3000 116 -271 88 C ATOM 1522 CD2 TYR A 197 -11.059 -17.677 19.520 1.00 23.89 C ANISOU 1522 CD2 TYR A 197 3340 2524 3214 117 -254 63 C ATOM 1523 CE1 TYR A 197 -12.507 -19.934 18.872 1.00 26.56 C ANISOU 1523 CE1 TYR A 197 3824 2771 3496 40 -246 134 C ATOM 1524 CE2 TYR A 197 -12.431 -17.591 19.350 1.00 21.48 C ANISOU 1524 CE2 TYR A 197 3062 2241 2859 49 -232 110 C ATOM 1525 CZ TYR A 197 -13.148 -18.725 19.028 1.00 24.44 C ANISOU 1525 CZ TYR A 197 3506 2574 3207 10 -228 145 C ATOM 1526 OH TYR A 197 -14.511 -18.658 18.857 1.00 26.91 O ANISOU 1526 OH TYR A 197 3837 2915 3474 -60 -207 185 O ATOM 1527 N LEU A 198 -6.104 -19.661 21.111 1.00 24.99 N ANISOU 1527 N LEU A 198 3434 2549 3512 436 -418 -97 N ATOM 1528 CA LEU A 198 -4.730 -20.151 21.121 1.00 27.08 C ANISOU 1528 CA LEU A 198 3667 2789 3834 521 -453 -161 C ATOM 1529 C LEU A 198 -4.628 -21.455 21.900 1.00 28.88 C ANISOU 1529 C LEU A 198 3980 2953 4038 583 -518 -126 C ATOM 1530 O LEU A 198 -3.921 -22.382 21.486 1.00 26.55 O ANISOU 1530 O LEU A 198 3705 2603 3779 635 -534 -160 O ATOM 1531 CB LEU A 198 -3.795 -19.095 21.712 1.00 28.13 C ANISOU 1531 CB LEU A 198 3704 2984 4002 565 -473 -216 C ATOM 1532 CG LEU A 198 -3.536 -17.865 20.837 1.00 29.69 C ANISOU 1532 CG LEU A 198 3813 3231 4236 517 -408 -269 C ATOM 1533 CD1 LEU A 198 -2.822 -16.782 21.631 1.00 36.76 C ANISOU 1533 CD1 LEU A 198 4625 4188 5155 548 -431 -312 C ATOM 1534 CD2 LEU A 198 -2.730 -18.242 19.602 1.00 32.03 C ANISOU 1534 CD2 LEU A 198 4078 3502 4591 524 -369 -334 C ATOM 1535 N ARG A 199 -5.337 -21.550 23.027 1.00 27.29 N ANISOU 1535 N ARG A 199 3837 2756 3776 578 -554 -59 N ATOM 1536 CA ARG A 199 -5.348 -22.792 23.790 1.00 27.13 C ANISOU 1536 CA ARG A 199 3915 2669 3723 628 -613 -15 C ATOM 1537 C ARG A 199 -6.099 -23.899 23.057 1.00 27.36 C ANISOU 1537 C ARG A 199 4039 2625 3733 579 -585 25 C ATOM 1538 O ARG A 199 -5.772 -25.079 23.224 1.00 31.02 O ANISOU 1538 O ARG A 199 4578 3011 4196 630 -625 35 O ATOM 1539 CB ARG A 199 -5.970 -22.558 25.166 1.00 32.01 C ANISOU 1539 CB ARG A 199 4575 3315 4273 625 -651 48 C ATOM 1540 CG ARG A 199 -5.118 -21.721 26.110 1.00 40.05 C ANISOU 1540 CG ARG A 199 5520 4393 5304 693 -698 10 C ATOM 1541 CD ARG A 199 -5.735 -21.669 27.503 1.00 54.75 C ANISOU 1541 CD ARG A 199 7439 6273 7089 694 -739 76 C ATOM 1542 NE ARG A 199 -4.780 -21.230 28.517 1.00 67.39 N ANISOU 1542 NE ARG A 199 8994 7913 8697 780 -805 39 N ATOM 1543 CZ ARG A 199 -4.866 -20.106 29.220 1.00 83.93 C ANISOU 1543 CZ ARG A 199 11032 10084 10774 770 -809 31 C ATOM 1544 NH1 ARG A 199 -5.874 -19.262 29.067 1.00 81.64 N ANISOU 1544 NH1 ARG A 199 10723 9839 10456 684 -751 58 N ATOM 1545 NH2 ARG A 199 -3.916 -19.826 30.108 1.00 90.23 N ANISOU 1545 NH2 ARG A 199 11790 10912 11581 853 -875 -8 N ATOM 1546 N ILE A 200 -7.102 -23.547 22.249 1.00 23.98 N ANISOU 1546 N ILE A 200 3609 2216 3288 482 -520 46 N ATOM 1547 CA ILE A 200 -7.848 -24.563 21.509 1.00 24.13 C ANISOU 1547 CA ILE A 200 3710 2168 3288 427 -492 78 C ATOM 1548 C ILE A 200 -6.970 -25.186 20.431 1.00 25.92 C ANISOU 1548 C ILE A 200 3927 2345 3576 465 -481 14 C ATOM 1549 O ILE A 200 -6.883 -26.413 20.310 1.00 28.63 O ANISOU 1549 O ILE A 200 4354 2605 3919 489 -502 25 O ATOM 1550 CB ILE A 200 -9.127 -23.961 20.901 1.00 21.39 C ANISOU 1550 CB ILE A 200 3353 1865 2908 317 -430 109 C ATOM 1551 CG1 ILE A 200 -10.164 -23.691 21.994 1.00 26.95 C ANISOU 1551 CG1 ILE A 200 4091 2604 3544 276 -441 179 C ATOM 1552 CG2 ILE A 200 -9.691 -24.894 19.828 1.00 25.65 C ANISOU 1552 CG2 ILE A 200 3955 2345 3445 261 -395 116 C ATOM 1553 CD1 ILE A 200 -11.422 -22.988 21.495 1.00 23.57 C ANISOU 1553 CD1 ILE A 200 3639 2231 3085 177 -386 203 C ATOM 1554 N PHE A 201 -6.320 -24.349 19.621 1.00 27.38 N ANISOU 1554 N PHE A 201 4014 2576 3812 468 -445 -54 N ATOM 1555 CA PHE A 201 -5.506 -24.873 18.531 1.00 30.41 C ANISOU 1555 CA PHE A 201 4382 2921 4252 498 -425 -120 C ATOM 1556 C PHE A 201 -4.252 -25.564 19.049 1.00 29.77 C ANISOU 1556 C PHE A 201 4299 2799 4212 613 -487 -163 C ATOM 1557 O PHE A 201 -3.811 -26.560 18.468 1.00 36.22 O ANISOU 1557 O PHE A 201 5155 3550 5057 649 -491 -193 O ATOM 1558 CB PHE A 201 -5.142 -23.750 17.562 1.00 33.52 C ANISOU 1558 CB PHE A 201 4673 3379 4685 466 -365 -180 C ATOM 1559 CG PHE A 201 -6.328 -23.153 16.860 1.00 30.91 C ANISOU 1559 CG PHE A 201 4349 3081 4316 361 -307 -144 C ATOM 1560 CD1 PHE A 201 -7.125 -23.931 16.038 1.00 31.42 C ANISOU 1560 CD1 PHE A 201 4482 3098 4356 303 -278 -120 C ATOM 1561 CD2 PHE A 201 -6.645 -21.814 17.019 1.00 30.50 C ANISOU 1561 CD2 PHE A 201 4233 3104 4252 323 -283 -138 C ATOM 1562 CE1 PHE A 201 -8.219 -23.388 15.392 1.00 33.02 C ANISOU 1562 CE1 PHE A 201 4688 3336 4524 212 -231 -91 C ATOM 1563 CE2 PHE A 201 -7.736 -21.265 16.375 1.00 30.71 C ANISOU 1563 CE2 PHE A 201 4266 3159 4243 236 -236 -107 C ATOM 1564 CZ PHE A 201 -8.525 -22.053 15.560 1.00 30.04 C ANISOU 1564 CZ PHE A 201 4246 3034 4134 182 -211 -83 C ATOM 1565 N ALA A 202 -3.666 -25.055 20.135 1.00 30.53 N ANISOU 1565 N ALA A 202 4352 2935 4312 676 -538 -170 N ATOM 1566 CA ALA A 202 -2.536 -25.746 20.747 1.00 36.63 C ANISOU 1566 CA ALA A 202 5130 3672 5118 793 -609 -207 C ATOM 1567 C ALA A 202 -2.955 -27.113 21.271 1.00 38.22 C ANISOU 1567 C ALA A 202 5466 3779 5277 820 -657 -144 C ATOM 1568 O ALA A 202 -2.236 -28.103 21.092 1.00 38.57 O ANISOU 1568 O ALA A 202 5545 3757 5353 896 -690 -177 O ATOM 1569 CB ALA A 202 -1.948 -24.895 21.872 1.00 34.82 C ANISOU 1569 CB ALA A 202 4831 3509 4890 848 -658 -222 C ATOM 1570 N ALA A 203 -4.121 -27.188 21.917 1.00 34.66 N ANISOU 1570 N ALA A 203 5094 3320 4754 757 -658 -56 N ATOM 1571 CA ALA A 203 -4.608 -28.473 22.407 1.00 36.17 C ANISOU 1571 CA ALA A 203 5425 3419 4900 767 -695 9 C ATOM 1572 C ALA A 203 -4.861 -29.438 21.257 1.00 37.29 C ANISOU 1572 C ALA A 203 5626 3482 5059 732 -657 -1 C ATOM 1573 O ALA A 203 -4.505 -30.619 21.337 1.00 36.70 O ANISOU 1573 O ALA A 203 5613 3349 4982 772 -679 2 O ATOM 1574 CB ALA A 203 -5.880 -28.270 23.230 1.00 34.70 C ANISOU 1574 CB ALA A 203 5302 3251 4633 688 -688 100 C ATOM 1575 N ALA A 204 -5.470 -28.953 20.172 1.00 37.56 N ANISOU 1575 N ALA A 204 5620 3551 5100 639 -582 -14 N ATOM 1576 CA ALA A 204 -5.717 -29.814 19.020 1.00 34.00 C ANISOU 1576 CA ALA A 204 5220 3033 4664 602 -544 -30 C ATOM 1577 C ALA A 204 -4.409 -30.276 18.389 1.00 38.50 C ANISOU 1577 C ALA A 204 5754 3568 5305 696 -558 -117 C ATOM 1578 O ALA A 204 -4.273 -31.445 18.010 1.00 34.87 O ANISOU 1578 O ALA A 204 5356 3043 4849 709 -557 -121 O ATOM 1579 CB ALA A 204 -6.578 -29.083 17.992 1.00 32.16 C ANISOU 1579 CB ALA A 204 4942 2857 4422 490 -466 -32 C ATOM 1580 N ARG A 205 -3.439 -29.369 18.258 1.00 38.66 N ANISOU 1580 N ARG A 205 5652 3660 5376 744 -554 -187 N ATOM 1581 CA ARG A 205 -2.133 -29.755 17.733 1.00 47.21 C ANISOU 1581 CA ARG A 205 6680 4731 6525 830 -561 -275 C ATOM 1582 C ARG A 205 -1.512 -30.852 18.586 1.00 42.64 C ANISOU 1582 C ARG A 205 6150 4118 5935 912 -623 -259 C ATOM 1583 O ARG A 205 -0.996 -31.847 18.065 1.00 47.03 O ANISOU 1583 O ARG A 205 6730 4627 6513 947 -620 -291 O ATOM 1584 CB ARG A 205 -1.208 -28.537 17.676 1.00 50.37 C ANISOU 1584 CB ARG A 205 6941 5219 6979 866 -553 -350 C ATOM 1585 CG ARG A 205 0.082 -28.779 16.901 1.00 57.71 C ANISOU 1585 CG ARG A 205 7789 6167 7973 922 -532 -447 C ATOM 1586 CD ARG A 205 1.120 -27.692 17.150 1.00 57.81 C ANISOU 1586 CD ARG A 205 7663 6272 8031 962 -534 -516 C ATOM 1587 NE ARG A 205 1.535 -27.644 18.549 1.00 64.90 N ANISOU 1587 NE ARG A 205 8551 7197 8909 1027 -609 -491 N ATOM 1588 CZ ARG A 205 1.185 -26.703 19.417 1.00 65.48 C ANISOU 1588 CZ ARG A 205 8602 7318 8960 1014 -633 -460 C ATOM 1589 NH1 ARG A 205 0.442 -25.667 19.060 1.00 62.50 N ANISOU 1589 NH1 ARG A 205 8197 6974 8575 933 -584 -446 N ATOM 1590 NH2 ARG A 205 1.598 -26.799 20.678 1.00 74.05 N ANISOU 1590 NH2 ARG A 205 9688 8425 10021 1075 -704 -439 N ATOM 1591 N ARG A 206 -1.559 -30.683 19.908 1.00 46.29 N ANISOU 1591 N ARG A 206 6630 4600 6359 943 -680 -210 N ATOM 1592 CA ARG A 206 -0.938 -31.650 20.805 1.00 42.88 C ANISOU 1592 CA ARG A 206 6245 4139 5910 1023 -744 -195 C ATOM 1593 C ARG A 206 -1.601 -33.016 20.689 1.00 45.12 C ANISOU 1593 C ARG A 206 6660 4328 6154 993 -741 -140 C ATOM 1594 O ARG A 206 -0.919 -34.047 20.680 1.00 45.70 O ANISOU 1594 O ARG A 206 6764 4356 6242 1057 -768 -161 O ATOM 1595 CB ARG A 206 -1.013 -31.137 22.243 1.00 48.01 C ANISOU 1595 CB ARG A 206 6897 4831 6514 1047 -800 -149 C ATOM 1596 CG ARG A 206 -0.316 -32.015 23.264 1.00 64.69 C ANISOU 1596 CG ARG A 206 9054 6922 8604 1133 -871 -137 C ATOM 1597 CD ARG A 206 -0.482 -31.450 24.664 1.00 89.89 C ANISOU 1597 CD ARG A 206 12252 10159 11742 1146 -920 -91 C ATOM 1598 NE ARG A 206 0.265 -32.213 25.656 1.00120.02 N ANISOU 1598 NE ARG A 206 16106 13959 15535 1232 -991 -86 N ATOM 1599 CZ ARG A 206 0.263 -31.954 26.957 1.00133.50 C ANISOU 1599 CZ ARG A 206 17833 15699 17191 1256 -1042 -50 C ATOM 1600 NH1 ARG A 206 -0.446 -30.958 27.463 1.00137.69 N ANISOU 1600 NH1 ARG A 206 18347 16281 17687 1203 -1029 -13 N ATOM 1601 NH2 ARG A 206 0.990 -32.715 27.770 1.00142.89 N ANISOU 1601 NH2 ARG A 206 19063 16868 18362 1337 -1107 -51 N ATOM 1602 N GLN A 207 -2.932 -33.045 20.597 1.00 42.50 N ANISOU 1602 N GLN A 207 6405 3968 5773 893 -707 -71 N ATOM 1603 CA GLN A 207 -3.638 -34.321 20.555 1.00 39.52 C ANISOU 1603 CA GLN A 207 6152 3508 5356 851 -701 -17 C ATOM 1604 C GLN A 207 -3.443 -35.033 19.222 1.00 37.84 C ANISOU 1604 C GLN A 207 5944 3246 5186 841 -658 -68 C ATOM 1605 O GLN A 207 -3.401 -36.267 19.183 1.00 40.85 O ANISOU 1605 O GLN A 207 6406 3556 5559 856 -670 -55 O ATOM 1606 CB GLN A 207 -5.123 -34.099 20.835 1.00 36.44 C ANISOU 1606 CB GLN A 207 5828 3117 4901 738 -671 66 C ATOM 1607 CG GLN A 207 -5.400 -33.575 22.233 1.00 38.49 C ANISOU 1607 CG GLN A 207 6100 3417 5106 745 -712 123 C ATOM 1608 CD GLN A 207 -6.866 -33.283 22.468 1.00 41.40 C ANISOU 1608 CD GLN A 207 6520 3797 5412 628 -675 198 C ATOM 1609 OE1 GLN A 207 -7.739 -33.862 21.820 1.00 41.46 O ANISOU 1609 OE1 GLN A 207 6584 3765 5402 543 -630 221 O ATOM 1610 NE2 GLN A 207 -7.145 -32.376 23.397 1.00 40.63 N ANISOU 1610 NE2 GLN A 207 6398 3760 5280 622 -692 232 N ATOM 1611 N LEU A 208 -3.330 -34.282 18.123 1.00 40.77 N ANISOU 1611 N LEU A 208 6236 3654 5602 813 -607 -126 N ATOM 1612 CA LEU A 208 -3.046 -34.905 16.834 1.00 39.69 C ANISOU 1612 CA LEU A 208 6096 3478 5506 807 -564 -184 C ATOM 1613 C LEU A 208 -1.636 -35.479 16.807 1.00 44.74 C ANISOU 1613 C LEU A 208 6693 4108 6196 921 -596 -251 C ATOM 1614 O LEU A 208 -1.408 -36.552 16.239 1.00 48.20 O ANISOU 1614 O LEU A 208 7178 4485 6649 938 -587 -273 O ATOM 1615 CB LEU A 208 -3.237 -33.895 15.702 1.00 39.28 C ANISOU 1615 CB LEU A 208 5968 3474 5483 748 -501 -233 C ATOM 1616 CG LEU A 208 -4.687 -33.555 15.348 1.00 46.60 C ANISOU 1616 CG LEU A 208 6944 4398 6362 624 -459 -177 C ATOM 1617 CD1 LEU A 208 -4.751 -32.306 14.485 1.00 46.24 C ANISOU 1617 CD1 LEU A 208 6815 4413 6342 581 -410 -223 C ATOM 1618 CD2 LEU A 208 -5.355 -34.726 14.639 1.00 45.01 C ANISOU 1618 CD2 LEU A 208 6833 4128 6142 564 -429 -160 C ATOM 1619 N ALA A1001 -0.679 -34.784 17.431 1.00 43.72 N ANISOU 1619 N ALA A1001 4101 3221 9291 637 342 -674 N ATOM 1620 CA ALA A1001 0.684 -35.300 17.498 1.00 48.43 C ANISOU 1620 CA ALA A1001 4693 3824 9885 648 367 -677 C ATOM 1621 C ALA A1001 0.754 -36.554 18.361 1.00 50.04 C ANISOU 1621 C ALA A1001 4882 4075 10058 646 290 -706 C ATOM 1622 O ALA A1001 1.426 -37.526 18.000 1.00 51.16 O ANISOU 1622 O ALA A1001 5092 4220 10127 685 277 -662 O ATOM 1623 CB ALA A1001 1.632 -34.226 18.034 1.00 41.12 C ANISOU 1623 CB ALA A1001 3650 2892 9082 601 444 -745 C ATOM 1624 N ASP A1002 0.062 -36.552 19.503 1.00 49.48 N ANISOU 1624 N ASP A1002 4721 4041 10037 604 238 -781 N ATOM 1625 CA ASP A1002 0.061 -37.727 20.369 1.00 51.75 C ANISOU 1625 CA ASP A1002 4988 4378 10296 602 160 -813 C ATOM 1626 C ASP A1002 -0.504 -38.944 19.646 1.00 53.95 C ANISOU 1626 C ASP A1002 5401 4653 10445 656 93 -727 C ATOM 1627 O ASP A1002 0.054 -40.043 19.735 1.00 52.41 O ANISOU 1627 O ASP A1002 5243 4478 10194 680 59 -708 O ATOM 1628 CB ASP A1002 -0.737 -37.439 21.640 1.00 50.63 C ANISOU 1628 CB ASP A1002 4735 4277 10226 548 112 -906 C ATOM 1629 CG ASP A1002 -0.067 -36.409 22.528 1.00 57.45 C ANISOU 1629 CG ASP A1002 5464 5152 11211 489 169 -1003 C ATOM 1630 OD1 ASP A1002 1.060 -35.984 22.198 1.00 62.62 O ANISOU 1630 OD1 ASP A1002 6108 5784 11899 490 242 -998 O ATOM 1631 OD2 ASP A1002 -0.665 -36.025 23.555 1.00 62.85 O ANISOU 1631 OD2 ASP A1002 6056 5868 11957 442 141 -1085 O ATOM 1632 N LEU A1003 -1.616 -38.769 18.927 1.00 51.81 N ANISOU 1632 N LEU A1003 5206 4357 10122 673 74 -673 N ATOM 1633 CA LEU A1003 -2.175 -39.870 18.150 1.00 51.25 C ANISOU 1633 CA LEU A1003 5272 4279 9923 722 13 -588 C ATOM 1634 C LEU A1003 -1.138 -40.441 17.192 1.00 51.66 C ANISOU 1634 C LEU A1003 5425 4308 9897 772 50 -519 C ATOM 1635 O LEU A1003 -0.959 -41.661 17.103 1.00 53.52 O ANISOU 1635 O LEU A1003 5730 4557 10048 801 0 -483 O ATOM 1636 CB LEU A1003 -3.408 -39.399 17.378 1.00 51.26 C ANISOU 1636 CB LEU A1003 5340 4251 9886 734 4 -539 C ATOM 1637 CG LEU A1003 -4.726 -39.306 18.148 1.00 55.11 C ANISOU 1637 CG LEU A1003 5771 4762 10404 701 -63 -579 C ATOM 1638 CD1 LEU A1003 -5.796 -38.679 17.271 1.00 56.84 C ANISOU 1638 CD1 LEU A1003 6054 4948 10593 715 -54 -526 C ATOM 1639 CD2 LEU A1003 -5.173 -40.675 18.636 1.00 61.37 C ANISOU 1639 CD2 LEU A1003 6596 5592 11131 710 -165 -573 C ATOM 1640 N GLU A1004 -0.444 -39.567 16.460 1.00 54.63 N ANISOU 1640 N GLU A1004 5811 4647 10297 781 137 -498 N ATOM 1641 CA GLU A1004 0.562 -40.025 15.512 1.00 61.97 C ANISOU 1641 CA GLU A1004 6836 5555 11155 829 176 -433 C ATOM 1642 C GLU A1004 1.761 -40.657 16.206 1.00 62.96 C ANISOU 1642 C GLU A1004 6908 5708 11307 825 180 -468 C ATOM 1643 O GLU A1004 2.475 -41.448 15.580 1.00 63.78 O ANISOU 1643 O GLU A1004 7100 5802 11330 868 186 -412 O ATOM 1644 CB GLU A1004 1.020 -38.860 14.631 1.00 69.43 C ANISOU 1644 CB GLU A1004 7792 6458 12131 837 266 -410 C ATOM 1645 CG GLU A1004 2.000 -39.253 13.533 1.00 79.60 C ANISOU 1645 CG GLU A1004 9185 7720 13339 889 307 -340 C ATOM 1646 CD GLU A1004 1.445 -40.317 12.604 1.00 81.73 C ANISOU 1646 CD GLU A1004 9613 7981 13459 943 253 -259 C ATOM 1647 OE1 GLU A1004 0.209 -40.371 12.429 1.00 80.19 O ANISOU 1647 OE1 GLU A1004 9460 7784 13223 944 204 -241 O ATOM 1648 OE2 GLU A1004 2.245 -41.103 12.053 1.00 75.39 O ANISOU 1648 OE2 GLU A1004 8892 7173 12579 984 258 -214 O ATOM 1649 N ASP A1005 1.997 -40.333 17.479 1.00 55.77 N ANISOU 1649 N ASP A1005 5856 4831 10503 773 178 -559 N ATOM 1650 CA ASP A1005 3.095 -40.958 18.209 1.00 57.73 C ANISOU 1650 CA ASP A1005 6047 5110 10776 768 177 -597 C ATOM 1651 C ASP A1005 2.734 -42.370 18.655 1.00 55.45 C ANISOU 1651 C ASP A1005 5797 4859 10414 786 85 -587 C ATOM 1652 O ASP A1005 3.554 -43.286 18.537 1.00 52.15 O ANISOU 1652 O ASP A1005 5421 4449 9943 817 80 -557 O ATOM 1653 CB ASP A1005 3.482 -40.100 19.415 1.00 50.96 C ANISOU 1653 CB ASP A1005 5026 4280 10055 705 205 -704 C ATOM 1654 CG ASP A1005 4.190 -38.819 19.016 1.00 60.03 C ANISOU 1654 CG ASP A1005 6135 5393 11282 687 303 -713 C ATOM 1655 OD1 ASP A1005 4.932 -38.836 18.011 1.00 64.55 O ANISOU 1655 OD1 ASP A1005 6784 5931 11811 727 354 -646 O ATOM 1656 OD2 ASP A1005 4.007 -37.794 19.707 1.00 62.80 O ANISOU 1656 OD2 ASP A1005 6377 5749 11736 634 328 -787 O ATOM 1657 N ASN A1006 1.518 -42.564 19.171 1.00 53.99 N ANISOU 1657 N ASN A1006 5596 4695 10222 766 11 -611 N ATOM 1658 CA ASN A1006 1.084 -43.908 19.541 1.00 58.54 C ANISOU 1658 CA ASN A1006 6214 5304 10723 783 -82 -596 C ATOM 1659 C ASN A1006 1.098 -44.838 18.335 1.00 54.11 C ANISOU 1659 C ASN A1006 5820 4714 10026 843 -95 -490 C ATOM 1660 O ASN A1006 1.552 -45.985 18.429 1.00 50.89 O ANISOU 1660 O ASN A1006 5456 4324 9555 869 -132 -466 O ATOM 1661 CB ASN A1006 -0.312 -43.856 20.161 1.00 64.24 C ANISOU 1661 CB ASN A1006 6900 6049 11460 754 -157 -632 C ATOM 1662 CG ASN A1006 -0.299 -43.336 21.585 1.00 70.05 C ANISOU 1662 CG ASN A1006 7473 6832 12309 697 -167 -746 C ATOM 1663 OD1 ASN A1006 -0.234 -44.110 22.540 1.00 76.09 O ANISOU 1663 OD1 ASN A1006 8185 7649 13076 687 -229 -793 O ATOM 1664 ND2 ASN A1006 -0.358 -42.019 21.735 1.00 70.48 N ANISOU 1664 ND2 ASN A1006 7450 6872 12457 660 -107 -794 N ATOM 1665 N TRP A1007 0.603 -44.361 17.191 1.00 54.07 N ANISOU 1665 N TRP A1007 5909 4664 9970 866 -65 -427 N ATOM 1666 CA TRP A1007 0.640 -45.161 15.972 1.00 52.16 C ANISOU 1666 CA TRP A1007 5830 4394 9593 922 -71 -330 C ATOM 1667 C TRP A1007 2.070 -45.506 15.578 1.00 52.21 C ANISOU 1667 C TRP A1007 5869 4392 9577 955 -15 -303 C ATOM 1668 O TRP A1007 2.322 -46.593 15.045 1.00 51.57 O ANISOU 1668 O TRP A1007 5899 4308 9388 997 -40 -243 O ATOM 1669 CB TRP A1007 -0.068 -44.408 14.845 1.00 53.98 C ANISOU 1669 CB TRP A1007 6142 4583 9786 938 -40 -278 C ATOM 1670 CG TRP A1007 0.022 -45.062 13.499 1.00 50.16 C ANISOU 1670 CG TRP A1007 5826 4068 9163 996 -35 -185 C ATOM 1671 CD1 TRP A1007 0.819 -44.686 12.458 1.00 54.55 C ANISOU 1671 CD1 TRP A1007 6450 4591 9686 1032 36 -142 C ATOM 1672 CD2 TRP A1007 -0.721 -46.200 13.044 1.00 48.52 C ANISOU 1672 CD2 TRP A1007 5742 3863 8829 1025 -106 -127 C ATOM 1673 NE1 TRP A1007 0.620 -45.518 11.384 1.00 55.14 N ANISOU 1673 NE1 TRP A1007 6684 4648 9619 1082 13 -65 N ATOM 1674 CE2 TRP A1007 -0.320 -46.457 11.719 1.00 53.23 C ANISOU 1674 CE2 TRP A1007 6480 4427 9317 1077 -71 -53 C ATOM 1675 CE3 TRP A1007 -1.684 -47.028 13.629 1.00 47.21 C ANISOU 1675 CE3 TRP A1007 5582 3726 8630 1009 -197 -131 C ATOM 1676 CZ2 TRP A1007 -0.846 -47.508 10.970 1.00 53.44 C ANISOU 1676 CZ2 TRP A1007 6655 4448 9203 1114 -119 14 C ATOM 1677 CZ3 TRP A1007 -2.206 -48.069 12.884 1.00 50.74 C ANISOU 1677 CZ3 TRP A1007 6172 4166 8941 1043 -245 -60 C ATOM 1678 CH2 TRP A1007 -1.786 -48.299 11.569 1.00 51.99 C ANISOU 1678 CH2 TRP A1007 6470 4290 8991 1094 -203 11 C ATOM 1679 N GLU A1008 3.019 -44.603 15.836 1.00 55.30 N ANISOU 1679 N GLU A1008 6166 4779 10068 935 60 -347 N ATOM 1680 CA GLU A1008 4.420 -44.891 15.550 1.00 61.06 C ANISOU 1680 CA GLU A1008 6912 5502 10787 962 114 -326 C ATOM 1681 C GLU A1008 5.015 -45.840 16.583 1.00 53.58 C ANISOU 1681 C GLU A1008 5903 4599 9855 955 74 -364 C ATOM 1682 O GLU A1008 5.839 -46.695 16.242 1.00 56.23 O ANISOU 1682 O GLU A1008 6303 4935 10126 994 81 -321 O ATOM 1683 CB GLU A1008 5.226 -43.593 15.501 1.00 69.53 C ANISOU 1683 CB GLU A1008 7899 6555 11963 939 206 -360 C ATOM 1684 CG GLU A1008 4.979 -42.752 14.260 1.00 79.82 C ANISOU 1684 CG GLU A1008 9281 7811 13237 960 257 -308 C ATOM 1685 CD GLU A1008 5.683 -41.410 14.316 1.00 94.28 C ANISOU 1685 CD GLU A1008 11016 9624 15182 930 344 -347 C ATOM 1686 OE1 GLU A1008 6.669 -41.286 15.073 1.00 96.06 O ANISOU 1686 OE1 GLU A1008 11142 9869 15490 905 375 -398 O ATOM 1687 OE2 GLU A1008 5.246 -40.478 13.608 1.00 98.99 O ANISOU 1687 OE2 GLU A1008 11637 10189 15786 931 380 -327 O ATOM 1688 N THR A1009 4.612 -45.703 17.848 1.00 52.90 N ANISOU 1688 N THR A1009 5693 4555 9854 907 32 -447 N ATOM 1689 CA THR A1009 5.124 -46.593 18.885 1.00 51.05 C ANISOU 1689 CA THR A1009 5393 4371 9634 900 -12 -490 C ATOM 1690 C THR A1009 4.681 -48.031 18.642 1.00 50.28 C ANISOU 1690 C THR A1009 5406 4282 9413 939 -91 -430 C ATOM 1691 O THR A1009 5.463 -48.969 18.831 1.00 47.20 O ANISOU 1691 O THR A1009 5033 3913 8987 964 -102 -414 O ATOM 1692 CB THR A1009 4.660 -46.116 20.261 1.00 49.76 C ANISOU 1692 CB THR A1009 5076 4253 9576 841 -47 -596 C ATOM 1693 OG1 THR A1009 5.202 -44.816 20.527 1.00 56.81 O ANISOU 1693 OG1 THR A1009 5865 5138 10582 802 30 -654 O ATOM 1694 CG2 THR A1009 5.111 -47.084 21.347 1.00 49.57 C ANISOU 1694 CG2 THR A1009 4985 4291 9558 836 -101 -642 C ATOM 1695 N ALEU A1010 3.424 -48.222 18.237 0.50 49.07 N ANISOU 1695 N ALEU A1010 5331 4116 9196 943 -146 -394 N ATOM 1696 N BLEU A1010 3.433 -48.225 18.212 0.50 49.07 N ANISOU 1696 N BLEU A1010 5334 4116 9195 944 -145 -393 N ATOM 1697 CA ALEU A1010 2.930 -49.565 17.954 0.50 47.52 C ANISOU 1697 CA ALEU A1010 5249 3928 8880 976 -222 -334 C ATOM 1698 CA BLEU A1010 2.944 -49.579 17.973 0.50 47.52 C ANISOU 1698 CA BLEU A1010 5248 3928 8880 975 -223 -335 C ATOM 1699 C ALEU A1010 3.726 -50.211 16.828 0.50 47.14 C ANISOU 1699 C ALEU A1010 5338 3847 8725 1032 -182 -248 C ATOM 1700 C BLEU A1010 3.669 -50.233 16.801 0.50 47.15 C ANISOU 1700 C BLEU A1010 5345 3849 8722 1033 -185 -246 C ATOM 1701 O ALEU A1010 4.147 -51.369 16.931 0.50 45.98 O ANISOU 1701 O ALEU A1010 5239 3719 8512 1059 -216 -219 O ATOM 1702 O BLEU A1010 3.985 -51.428 16.850 0.50 46.03 O ANISOU 1702 O BLEU A1010 5261 3724 8506 1060 -224 -213 O ATOM 1703 CB ALEU A1010 1.444 -49.506 17.598 0.50 47.19 C ANISOU 1703 CB ALEU A1010 5269 3873 8789 967 -279 -309 C ATOM 1704 CB BLEU A1010 1.435 -49.553 17.730 0.50 47.23 C ANISOU 1704 CB BLEU A1010 5263 3883 8800 964 -285 -315 C ATOM 1705 CG ALEU A1010 0.762 -50.834 17.256 0.50 46.73 C ANISOU 1705 CG ALEU A1010 5333 3819 8601 994 -362 -245 C ATOM 1706 CG BLEU A1010 0.576 -49.226 18.956 0.50 45.23 C ANISOU 1706 CG BLEU A1010 4883 3670 8633 913 -347 -399 C ATOM 1707 CD1ALEU A1010 0.601 -51.692 18.499 0.50 45.11 C ANISOU 1707 CD1ALEU A1010 5054 3670 8416 973 -449 -293 C ATOM 1708 CD1BLEU A1010 -0.864 -48.963 18.550 0.50 48.09 C ANISOU 1708 CD1BLEU A1010 5297 4014 8960 903 -390 -373 C ATOM 1709 CD2ALEU A1010 -0.583 -50.587 16.590 0.50 47.29 C ANISOU 1709 CD2ALEU A1010 5482 3868 8620 991 -393 -206 C ATOM 1710 CD2BLEU A1010 0.641 -50.352 19.979 0.50 47.29 C ANISOU 1710 CD2BLEU A1010 5102 3985 8881 908 -430 -430 C ATOM 1711 N ASN A1011 3.945 -49.470 15.741 1.00 44.68 N ANISOU 1711 N ASN A1011 5091 3491 8395 1053 -111 -207 N ATOM 1712 CA ASN A1011 4.643 -50.032 14.589 1.00 46.88 C ANISOU 1712 CA ASN A1011 5508 3740 8565 1109 -74 -127 C ATOM 1713 C ASN A1011 6.130 -50.215 14.868 1.00 46.51 C ANISOU 1713 C ASN A1011 5412 3703 8556 1123 -23 -139 C ATOM 1714 O ASN A1011 6.722 -51.219 14.457 1.00 47.96 O ANISOU 1714 O ASN A1011 5686 3886 8650 1165 -27 -88 O ATOM 1715 CB ASN A1011 4.438 -49.138 13.367 1.00 49.27 C ANISOU 1715 CB ASN A1011 5886 3995 8837 1127 -18 -87 C ATOM 1716 CG ASN A1011 2.998 -49.118 12.897 1.00 53.12 C ANISOU 1716 CG ASN A1011 6450 4471 9263 1124 -68 -59 C ATOM 1717 OD1 ASN A1011 2.270 -50.099 13.053 1.00 55.55 O ANISOU 1717 OD1 ASN A1011 6814 4796 9498 1128 -142 -37 O ATOM 1718 ND2 ASN A1011 2.578 -47.999 12.318 1.00 55.94 N ANISOU 1718 ND2 ASN A1011 6806 4800 9649 1117 -28 -58 N ATOM 1719 N ASP A1012 6.751 -49.258 15.559 1.00 48.71 N ANISOU 1719 N ASP A1012 5549 3993 8966 1086 28 -207 N ATOM 1720 CA ASP A1012 8.172 -49.377 15.865 1.00 49.45 C ANISOU 1720 CA ASP A1012 5586 4099 9104 1095 79 -221 C ATOM 1721 C ASP A1012 8.439 -50.589 16.747 1.00 44.16 C ANISOU 1721 C ASP A1012 4890 3476 8415 1101 20 -235 C ATOM 1722 O ASP A1012 9.344 -51.385 16.473 1.00 46.50 O ANISOU 1722 O ASP A1012 5240 3773 8655 1140 36 -193 O ATOM 1723 CB ASP A1012 8.673 -48.100 16.539 1.00 49.79 C ANISOU 1723 CB ASP A1012 5475 4149 9295 1047 139 -299 C ATOM 1724 CG ASP A1012 8.683 -46.911 15.600 1.00 55.81 C ANISOU 1724 CG ASP A1012 6264 4865 10078 1047 209 -278 C ATOM 1725 OD1 ASP A1012 8.364 -47.092 14.406 1.00 59.01 O ANISOU 1725 OD1 ASP A1012 6808 5235 10380 1088 212 -204 O ATOM 1726 OD2 ASP A1012 9.011 -45.795 16.057 1.00 62.61 O ANISOU 1726 OD2 ASP A1012 7008 5725 11056 1005 260 -337 O ATOM 1727 N ASN A1013 7.652 -50.750 17.813 1.00 41.67 N ANISOU 1727 N ASN A1013 4490 3200 8143 1063 -50 -295 N ATOM 1728 CA ASN A1013 7.872 -51.868 18.723 1.00 47.75 C ANISOU 1728 CA ASN A1013 5223 4021 8899 1067 -113 -315 C ATOM 1729 C ASN A1013 7.568 -53.205 18.060 1.00 43.26 C ANISOU 1729 C ASN A1013 4810 3442 8186 1114 -165 -230 C ATOM 1730 O ASN A1013 8.154 -54.228 18.435 1.00 43.89 O ANISOU 1730 O ASN A1013 4895 3551 8230 1137 -191 -218 O ATOM 1731 CB ASN A1013 7.031 -51.684 19.985 1.00 46.03 C ANISOU 1731 CB ASN A1013 4881 3852 8756 1016 -182 -402 C ATOM 1732 CG ASN A1013 7.689 -50.757 20.989 1.00 46.54 C ANISOU 1732 CG ASN A1013 4773 3951 8957 970 -138 -500 C ATOM 1733 OD1 ASN A1013 8.877 -50.890 21.283 1.00 49.11 O ANISOU 1733 OD1 ASN A1013 5047 4297 9315 978 -96 -514 O ATOM 1734 ND2 ASN A1013 6.923 -49.807 21.512 1.00 52.19 N ANISOU 1734 ND2 ASN A1013 5402 4676 9752 921 -147 -567 N ATOM 1735 N LEU A1014 6.663 -53.224 17.078 1.00 42.07 N ANISOU 1735 N LEU A1014 4785 3253 7947 1130 -181 -172 N ATOM 1736 CA LEU A1014 6.455 -54.442 16.303 1.00 41.29 C ANISOU 1736 CA LEU A1014 4847 3141 7700 1175 -218 -88 C ATOM 1737 C LEU A1014 7.719 -54.826 15.547 1.00 45.49 C ANISOU 1737 C LEU A1014 5457 3652 8176 1226 -152 -34 C ATOM 1738 O LEU A1014 8.090 -56.005 15.498 1.00 42.26 O ANISOU 1738 O LEU A1014 5118 3256 7684 1259 -178 8 O ATOM 1739 CB LEU A1014 5.284 -54.256 15.338 1.00 46.69 C ANISOU 1739 CB LEU A1014 5647 3790 8304 1181 -236 -40 C ATOM 1740 CG LEU A1014 3.919 -54.688 15.875 1.00 52.15 C ANISOU 1740 CG LEU A1014 6334 4505 8976 1151 -334 -54 C ATOM 1741 CD1 LEU A1014 2.799 -54.054 15.069 1.00 50.63 C ANISOU 1741 CD1 LEU A1014 6209 4280 8749 1144 -334 -28 C ATOM 1742 CD2 LEU A1014 3.802 -56.205 15.853 1.00 49.81 C ANISOU 1742 CD2 LEU A1014 6134 4228 8564 1176 -400 -4 C ATOM 1743 N LYS A1015 8.398 -53.842 14.952 1.00 44.91 N ANISOU 1743 N LYS A1015 5372 3548 8145 1232 -67 -33 N ATOM 1744 CA LYS A1015 9.671 -54.119 14.296 1.00 46.07 C ANISOU 1744 CA LYS A1015 5576 3677 8250 1277 -6 10 C ATOM 1745 C LYS A1015 10.711 -54.594 15.302 1.00 46.29 C ANISOU 1745 C LYS A1015 5500 3746 8342 1274 1 -24 C ATOM 1746 O LYS A1015 11.498 -55.502 15.012 1.00 47.05 O ANISOU 1746 O LYS A1015 5665 3844 8367 1316 9 23 O ATOM 1747 CB LYS A1015 10.165 -52.872 13.563 1.00 51.29 C ANISOU 1747 CB LYS A1015 6226 4301 8961 1277 78 9 C ATOM 1748 CG LYS A1015 9.257 -52.413 12.432 1.00 58.43 C ANISOU 1748 CG LYS A1015 7242 5165 9792 1289 76 48 C ATOM 1749 CD LYS A1015 9.802 -51.161 11.760 1.00 72.25 C ANISOU 1749 CD LYS A1015 8971 6883 11600 1287 156 45 C ATOM 1750 CE LYS A1015 8.920 -50.711 10.605 1.00 73.77 C ANISOU 1750 CE LYS A1015 9274 7038 11716 1303 150 83 C ATOM 1751 NZ LYS A1015 8.908 -51.697 9.487 1.00 84.96 N ANISOU 1751 NZ LYS A1015 10870 8436 12974 1359 121 153 N ATOM 1752 N VAL A1016 10.730 -53.991 16.493 1.00 41.83 N ANISOU 1752 N VAL A1016 4768 3217 7908 1224 -4 -107 N ATOM 1753 CA VAL A1016 11.678 -54.408 17.524 1.00 43.53 C ANISOU 1753 CA VAL A1016 4873 3480 8186 1219 -2 -149 C ATOM 1754 C VAL A1016 11.471 -55.876 17.873 1.00 47.51 C ANISOU 1754 C VAL A1016 5432 4016 8603 1244 -79 -119 C ATOM 1755 O VAL A1016 12.435 -56.620 18.093 1.00 49.23 O ANISOU 1755 O VAL A1016 5646 4256 8804 1273 -67 -100 O ATOM 1756 CB VAL A1016 11.544 -53.507 18.765 1.00 44.80 C ANISOU 1756 CB VAL A1016 4850 3681 8493 1157 -6 -254 C ATOM 1757 CG1 VAL A1016 12.367 -54.060 19.920 1.00 45.25 C ANISOU 1757 CG1 VAL A1016 4790 3801 8600 1150 -21 -303 C ATOM 1758 CG2 VAL A1016 11.972 -52.085 18.436 1.00 45.07 C ANISOU 1758 CG2 VAL A1016 4826 3684 8616 1133 80 -281 C ATOM 1759 N ILE A1017 10.213 -56.317 17.930 1.00 43.82 N ANISOU 1759 N ILE A1017 5018 3553 8081 1233 -160 -111 N ATOM 1760 CA ILE A1017 9.933 -57.716 18.237 1.00 45.47 C ANISOU 1760 CA ILE A1017 5284 3791 8201 1254 -239 -79 C ATOM 1761 C ILE A1017 10.373 -58.612 17.087 1.00 46.53 C ANISOU 1761 C ILE A1017 5593 3891 8197 1313 -215 18 C ATOM 1762 O ILE A1017 10.964 -59.677 17.304 1.00 46.98 O ANISOU 1762 O ILE A1017 5677 3970 8202 1343 -233 47 O ATOM 1763 CB ILE A1017 8.438 -57.901 18.558 1.00 41.45 C ANISOU 1763 CB ILE A1017 4787 3294 7667 1223 -334 -95 C ATOM 1764 CG1 ILE A1017 8.082 -57.189 19.866 1.00 44.77 C ANISOU 1764 CG1 ILE A1017 5028 3763 8219 1168 -367 -200 C ATOM 1765 CG2 ILE A1017 8.090 -59.384 18.639 1.00 43.85 C ANISOU 1765 CG2 ILE A1017 5182 3621 7858 1246 -415 -46 C ATOM 1766 CD1 ILE A1017 6.593 -56.992 20.071 1.00 42.63 C ANISOU 1766 CD1 ILE A1017 4759 3496 7944 1133 -443 -222 C ATOM 1767 N GLU A1018 10.099 -58.198 15.848 1.00 47.39 N ANISOU 1767 N GLU A1018 5820 3946 8239 1332 -176 67 N ATOM 1768 CA GLU A1018 10.432 -59.031 14.697 1.00 49.91 C ANISOU 1768 CA GLU A1018 6315 4235 8415 1388 -158 152 C ATOM 1769 C GLU A1018 11.935 -59.252 14.585 1.00 53.53 C ANISOU 1769 C GLU A1018 6764 4695 8881 1424 -96 168 C ATOM 1770 O GLU A1018 12.382 -60.336 14.194 1.00 58.56 O ANISOU 1770 O GLU A1018 7506 5332 9414 1468 -104 222 O ATOM 1771 CB GLU A1018 9.888 -58.394 13.419 1.00 52.35 C ANISOU 1771 CB GLU A1018 6737 4492 8660 1401 -128 186 C ATOM 1772 CG GLU A1018 8.375 -58.445 13.300 1.00 56.41 C ANISOU 1772 CG GLU A1018 7301 5003 9129 1377 -190 193 C ATOM 1773 CD GLU A1018 7.852 -57.626 12.137 1.00 70.40 C ANISOU 1773 CD GLU A1018 9160 6730 10860 1386 -157 216 C ATOM 1774 OE1 GLU A1018 8.675 -57.142 11.331 1.00 76.04 O ANISOU 1774 OE1 GLU A1018 9914 7414 11563 1415 -96 232 O ATOM 1775 OE2 GLU A1018 6.619 -57.461 12.031 1.00 74.21 O ANISOU 1775 OE2 GLU A1018 9667 7209 11322 1363 -196 218 O ATOM 1776 N LYS A1019 12.730 -58.238 14.921 1.00 52.69 N ANISOU 1776 N LYS A1019 6533 4590 8897 1405 -32 121 N ATOM 1777 CA LYS A1019 14.181 -58.317 14.834 1.00 56.38 C ANISOU 1777 CA LYS A1019 6976 5060 9386 1434 33 134 C ATOM 1778 C LYS A1019 14.835 -58.631 16.174 1.00 57.56 C ANISOU 1778 C LYS A1019 6976 5266 9626 1417 24 86 C ATOM 1779 O LYS A1019 16.058 -58.516 16.297 1.00 62.61 O ANISOU 1779 O LYS A1019 7559 5915 10313 1431 84 84 O ATOM 1780 CB LYS A1019 14.743 -57.008 14.274 1.00 59.94 C ANISOU 1780 CB LYS A1019 7388 5478 9908 1425 115 120 C ATOM 1781 CG LYS A1019 14.330 -56.724 12.837 1.00 61.24 C ANISOU 1781 CG LYS A1019 7702 5591 9977 1450 126 170 C ATOM 1782 CD LYS A1019 14.910 -55.410 12.339 1.00 75.67 C ANISOU 1782 CD LYS A1019 9479 7389 11883 1439 205 154 C ATOM 1783 CE LYS A1019 14.603 -55.189 10.865 1.00 85.82 C ANISOU 1783 CE LYS A1019 10912 8627 13069 1469 209 203 C ATOM 1784 NZ LYS A1019 15.189 -53.918 10.353 1.00 83.20 N ANISOU 1784 NZ LYS A1019 10531 8268 12815 1459 285 192 N ATOM 1785 N ALA A1020 14.054 -59.026 17.175 1.00 55.92 N ANISOU 1785 N ALA A1020 6702 5101 9445 1387 -52 45 N ATOM 1786 CA ALA A1020 14.614 -59.334 18.482 1.00 60.85 C ANISOU 1786 CA ALA A1020 7180 5789 10150 1371 -72 -9 C ATOM 1787 C ALA A1020 15.419 -60.628 18.432 1.00 66.37 C ANISOU 1787 C ALA A1020 7943 6506 10767 1422 -77 49 C ATOM 1788 O ALA A1020 15.176 -61.509 17.602 1.00 60.14 O ANISOU 1788 O ALA A1020 7314 5689 9847 1461 -98 124 O ATOM 1789 CB ALA A1020 13.504 -59.449 19.526 1.00 55.02 C ANISOU 1789 CB ALA A1020 6360 5097 9450 1328 -166 -71 C ATOM 1790 N ASP A1021 16.389 -60.736 19.339 1.00 71.73 N ANISOU 1790 N ASP A1021 8494 7238 11522 1419 -58 12 N ATOM 1791 CA ASP A1021 17.277 -61.890 19.392 1.00 81.28 C ANISOU 1791 CA ASP A1021 9743 8471 12668 1467 -54 64 C ATOM 1792 C ASP A1021 16.935 -62.861 20.512 1.00 77.44 C ANISOU 1792 C ASP A1021 9194 8056 12175 1460 -143 39 C ATOM 1793 O ASP A1021 17.111 -64.071 20.341 1.00 79.89 O ANISOU 1793 O ASP A1021 9596 8373 12385 1501 -172 102 O ATOM 1794 CB ASP A1021 18.728 -61.428 19.558 1.00 88.07 C ANISOU 1794 CB ASP A1021 10510 9347 13608 1476 34 51 C ATOM 1795 CG ASP A1021 19.166 -60.477 18.461 1.00 93.23 C ANISOU 1795 CG ASP A1021 11219 9935 14269 1482 118 75 C ATOM 1796 OD1 ASP A1021 18.747 -60.672 17.300 1.00 92.69 O ANISOU 1796 OD1 ASP A1021 11311 9811 14095 1510 117 136 O ATOM 1797 OD2 ASP A1021 19.924 -59.531 18.760 1.00101.54 O ANISOU 1797 OD2 ASP A1021 12154 10997 15430 1458 182 30 O ATOM 1798 N ASN A1022 16.454 -62.364 21.649 1.00 71.40 N ANISOU 1798 N ASN A1022 8276 7348 11506 1410 -190 -53 N ATOM 1799 CA ASN A1022 16.102 -63.191 22.795 1.00 65.79 C ANISOU 1799 CA ASN A1022 7495 6732 10771 1389 -281 -88 C ATOM 1800 C ASN A1022 14.697 -62.830 23.263 1.00 59.19 C ANISOU 1800 C ASN A1022 6631 5924 9932 1330 -360 -145 C ATOM 1801 O ASN A1022 14.067 -61.896 22.757 1.00 55.97 O ANISOU 1801 O ASN A1022 6235 5441 9590 1323 -344 -162 O ATOM 1802 CB ASN A1022 17.114 -63.017 23.934 1.00 64.01 C ANISOU 1802 CB ASN A1022 7104 6620 10598 1354 -253 -153 C ATOM 1803 CG ASN A1022 17.323 -61.565 24.306 1.00 56.95 C ANISOU 1803 CG ASN A1022 6066 5726 9847 1310 -199 -240 C ATOM 1804 OD1 ASN A1022 16.513 -60.974 25.019 1.00 56.55 O ANISOU 1804 OD1 ASN A1022 5931 5724 9833 1248 -243 -318 O ATOM 1805 ND2 ASN A1022 18.415 -60.981 23.824 1.00 60.14 N ANISOU 1805 ND2 ASN A1022 6442 6074 10333 1343 -102 -226 N ATOM 1806 N ALA A1023 14.208 -63.581 24.252 1.00 57.84 N ANISOU 1806 N ALA A1023 6424 5866 9687 1289 -445 -173 N ATOM 1807 CA ALA A1023 12.862 -63.347 24.765 1.00 56.33 C ANISOU 1807 CA ALA A1023 6207 5710 9485 1233 -526 -223 C ATOM 1808 C ALA A1023 12.776 -62.045 25.549 1.00 53.45 C ANISOU 1808 C ALA A1023 5679 5389 9243 1172 -504 -328 C ATOM 1809 O ALA A1023 11.741 -61.368 25.510 1.00 52.62 O ANISOU 1809 O ALA A1023 5566 5256 9172 1141 -532 -363 O ATOM 1810 CB ALA A1023 12.427 -64.521 25.641 1.00 52.34 C ANISOU 1810 CB ALA A1023 5703 5317 8868 1207 -620 -224 C ATOM 1811 N ALA A1024 13.842 -61.675 26.262 1.00 52.74 N ANISOU 1811 N ALA A1024 5456 5364 9218 1153 -453 -380 N ATOM 1812 CA ALA A1024 13.796 -60.470 27.083 1.00 50.73 C ANISOU 1812 CA ALA A1024 5042 5157 9078 1091 -433 -485 C ATOM 1813 C ALA A1024 13.524 -59.235 26.234 1.00 51.33 C ANISOU 1813 C ALA A1024 5134 5114 9257 1101 -373 -493 C ATOM 1814 O ALA A1024 12.754 -58.354 26.637 1.00 53.54 O ANISOU 1814 O ALA A1024 5341 5402 9598 1052 -389 -562 O ATOM 1815 CB ALA A1024 15.103 -60.311 27.859 1.00 51.10 C ANISOU 1815 CB ALA A1024 4955 5283 9177 1076 -381 -531 C ATOM 1816 N GLN A1025 14.147 -59.149 25.056 1.00 52.49 N ANISOU 1816 N GLN A1025 5373 5148 9422 1165 -300 -422 N ATOM 1817 CA GLN A1025 13.897 -58.012 24.176 1.00 50.94 C ANISOU 1817 CA GLN A1025 5208 4843 9303 1172 -239 -419 C ATOM 1818 C GLN A1025 12.446 -57.987 23.715 1.00 50.86 C ANISOU 1818 C GLN A1025 5293 4788 9245 1163 -301 -399 C ATOM 1819 O GLN A1025 11.839 -56.915 23.607 1.00 49.12 O ANISOU 1819 O GLN A1025 5042 4539 9082 1125 -283 -438 O ATOM 1820 CB GLN A1025 14.844 -58.057 22.978 1.00 52.91 C ANISOU 1820 CB GLN A1025 5571 5018 9513 1220 -151 -331 C ATOM 1821 CG GLN A1025 16.300 -57.799 23.337 1.00 61.43 C ANISOU 1821 CG GLN A1025 6551 6132 10658 1223 -75 -353 C ATOM 1822 CD GLN A1025 17.229 -57.909 22.143 1.00 68.67 C ANISOU 1822 CD GLN A1025 7584 6980 11527 1274 7 -262 C ATOM 1823 OE1 GLN A1025 16.787 -58.124 21.014 1.00 71.91 O ANISOU 1823 OE1 GLN A1025 8151 7320 11850 1305 10 -187 O ATOM 1824 NE2 GLN A1025 18.526 -57.763 22.388 1.00 69.94 N ANISOU 1824 NE2 GLN A1025 7669 7167 11738 1280 72 -271 N ATOM 1825 N VAL A1026 11.871 -59.159 23.438 1.00 49.37 N ANISOU 1825 N VAL A1026 5219 4592 8946 1195 -374 -336 N ATOM 1826 CA VAL A1026 10.457 -59.221 23.082 1.00 47.09 C ANISOU 1826 CA VAL A1026 5015 4271 8604 1182 -442 -317 C ATOM 1827 C VAL A1026 9.601 -58.741 24.247 1.00 45.71 C ANISOU 1827 C VAL A1026 4713 4181 8473 1112 -503 -412 C ATOM 1828 O VAL A1026 8.650 -57.971 24.063 1.00 48.29 O ANISOU 1828 O VAL A1026 5037 4466 8844 1091 -516 -436 O ATOM 1829 CB VAL A1026 10.075 -60.649 22.650 1.00 47.63 C ANISOU 1829 CB VAL A1026 5231 4330 8535 1222 -512 -232 C ATOM 1830 CG1 VAL A1026 8.589 -60.729 22.328 1.00 45.68 C ANISOU 1830 CG1 VAL A1026 5068 4059 8230 1203 -586 -214 C ATOM 1831 CG2 VAL A1026 10.909 -61.085 21.451 1.00 45.87 C ANISOU 1831 CG2 VAL A1026 5151 4047 8230 1275 -440 -136 C ATOM 1832 N LYS A1027 9.929 -59.181 25.464 1.00 44.96 N ANISOU 1832 N LYS A1027 4515 4215 8354 1070 -539 -465 N ATOM 1833 CA LYS A1027 9.173 -58.754 26.637 1.00 50.86 C ANISOU 1833 CA LYS A1027 5140 5058 9127 997 -594 -556 C ATOM 1834 C LYS A1027 9.218 -57.240 26.794 1.00 50.43 C ANISOU 1834 C LYS A1027 4973 4974 9214 965 -531 -633 C ATOM 1835 O LYS A1027 8.189 -56.597 27.038 1.00 47.39 O ANISOU 1835 O LYS A1027 4554 4589 8862 927 -563 -678 O ATOM 1836 CB LYS A1027 9.721 -59.440 27.890 1.00 54.22 C ANISOU 1836 CB LYS A1027 5467 5625 9511 964 -629 -599 C ATOM 1837 CG LYS A1027 8.966 -59.095 29.167 1.00 58.53 C ANISOU 1837 CG LYS A1027 5887 6279 10073 889 -689 -692 C ATOM 1838 CD LYS A1027 9.693 -59.599 30.402 1.00 62.32 C ANISOU 1838 CD LYS A1027 6253 6896 10529 857 -707 -741 C ATOM 1839 CE LYS A1027 8.980 -59.167 31.675 1.00 62.11 C ANISOU 1839 CE LYS A1027 6096 6976 10526 784 -761 -839 C ATOM 1840 NZ LYS A1027 9.656 -59.678 32.899 1.00 63.66 N ANISOU 1840 NZ LYS A1027 6181 7311 10695 753 -782 -887 N ATOM 1841 N ASP A1028 10.408 -56.651 26.660 1.00 51.22 N ANISOU 1841 N ASP A1028 5013 5049 9399 981 -440 -649 N ATOM 1842 CA ASP A1028 10.542 -55.208 26.830 1.00 56.53 C ANISOU 1842 CA ASP A1028 5575 5694 10211 949 -375 -725 C ATOM 1843 C ASP A1028 9.649 -54.457 25.850 1.00 48.48 C ANISOU 1843 C ASP A1028 4639 4563 9218 960 -358 -696 C ATOM 1844 O ASP A1028 8.959 -53.502 26.226 1.00 48.61 O ANISOU 1844 O ASP A1028 4585 4586 9299 912 -360 -760 O ATOM 1845 CB ASP A1028 12.005 -54.796 26.655 1.00 64.58 C ANISOU 1845 CB ASP A1028 6543 6694 11301 968 -277 -728 C ATOM 1846 CG ASP A1028 12.901 -55.342 27.752 1.00 72.92 C ANISOU 1846 CG ASP A1028 7491 7873 12341 945 -289 -770 C ATOM 1847 OD1 ASP A1028 12.372 -55.928 28.720 1.00 75.38 O ANISOU 1847 OD1 ASP A1028 7762 8293 12586 904 -370 -805 O ATOM 1848 OD2 ASP A1028 14.136 -55.186 27.646 1.00 76.42 O ANISOU 1848 OD2 ASP A1028 7895 8309 12832 964 -217 -765 O ATOM 1849 N ALA A1029 9.646 -54.878 24.584 1.00 46.38 N ANISOU 1849 N ALA A1029 4535 4211 8876 1010 -338 -593 N ATOM 1850 CA ALA A1029 8.809 -54.212 23.592 1.00 46.13 C ANISOU 1850 CA ALA A1029 4601 4098 8829 1007 -319 -552 C ATOM 1851 C ALA A1029 7.329 -54.450 23.869 1.00 42.84 C ANISOU 1851 C ALA A1029 4204 3694 8380 988 -415 -565 C ATOM 1852 O ALA A1029 6.510 -53.536 23.720 1.00 44.48 O ANISOU 1852 O ALA A1029 4399 3874 8628 957 -409 -589 O ATOM 1853 CB ALA A1029 9.177 -54.692 22.189 1.00 42.23 C ANISOU 1853 CB ALA A1029 4278 3530 8238 1063 -277 -439 C ATOM 1854 N LEU A1030 6.966 -55.668 24.275 1.00 43.04 N ANISOU 1854 N LEU A1030 4259 3763 8332 1006 -506 -546 N ATOM 1855 CA LEU A1030 5.563 -55.962 24.549 1.00 41.55 C ANISOU 1855 CA LEU A1030 4094 3594 8100 985 -603 -552 C ATOM 1856 C LEU A1030 5.071 -55.214 25.782 1.00 42.46 C ANISOU 1856 C LEU A1030 4056 3799 8279 912 -626 -658 C ATOM 1857 O LEU A1030 3.912 -54.785 25.831 1.00 40.47 O ANISOU 1857 O LEU A1030 3803 3536 8036 886 -667 -676 O ATOM 1858 CB LEU A1030 5.368 -57.468 24.719 1.00 42.99 C ANISOU 1858 CB LEU A1030 4360 3835 8139 996 -686 -498 C ATOM 1859 CG LEU A1030 5.468 -58.301 23.438 1.00 39.03 C ANISOU 1859 CG LEU A1030 4036 3239 7554 1065 -685 -386 C ATOM 1860 CD1 LEU A1030 5.494 -59.782 23.771 1.00 41.14 C ANISOU 1860 CD1 LEU A1030 4366 3578 7690 1072 -758 -344 C ATOM 1861 CD2 LEU A1030 4.314 -57.985 22.496 1.00 38.25 C ANISOU 1861 CD2 LEU A1030 4051 3073 7410 1062 -700 -338 C ATOM 1862 N THR A1031 5.932 -55.048 26.788 1.00 46.05 N ANISOU 1862 N THR A1031 4379 4343 8777 878 -602 -729 N ATOM 1863 CA THR A1031 5.538 -54.288 27.969 1.00 47.76 C ANISOU 1863 CA THR A1031 4446 4644 9058 809 -618 -835 C ATOM 1864 C THR A1031 5.211 -52.845 27.602 1.00 47.28 C ANISOU 1864 C THR A1031 4343 4502 9121 799 -556 -875 C ATOM 1865 O THR A1031 4.262 -52.259 28.138 1.00 41.54 O ANISOU 1865 O THR A1031 3556 3803 8426 754 -589 -930 O ATOM 1866 CB THR A1031 6.646 -54.339 29.022 1.00 51.32 C ANISOU 1866 CB THR A1031 4767 5197 9536 780 -594 -901 C ATOM 1867 OG1 THR A1031 6.936 -55.704 29.350 1.00 53.04 O ANISOU 1867 OG1 THR A1031 5026 5490 9636 792 -650 -859 O ATOM 1868 CG2 THR A1031 6.224 -53.600 30.286 1.00 53.03 C ANISOU 1868 CG2 THR A1031 4831 5506 9812 707 -615 -1012 C ATOM 1869 N LYS A1032 5.982 -52.259 26.684 1.00 48.62 N ANISOU 1869 N LYS A1032 4551 4578 9345 832 -464 -841 N ATOM 1870 CA LYS A1032 5.687 -50.908 26.217 1.00 46.77 C ANISOU 1870 CA LYS A1032 4309 4280 9180 804 -398 -858 C ATOM 1871 C LYS A1032 4.363 -50.865 25.467 1.00 47.86 C ANISOU 1871 C LYS A1032 4554 4358 9272 814 -439 -805 C ATOM 1872 O LYS A1032 3.531 -49.980 25.701 1.00 48.39 O ANISOU 1872 O LYS A1032 4573 4420 9392 775 -442 -851 O ATOM 1873 CB LYS A1032 6.821 -50.405 25.323 1.00 50.18 C ANISOU 1873 CB LYS A1032 4785 4648 9635 826 -291 -814 C ATOM 1874 CG LYS A1032 8.083 -50.001 26.065 1.00 55.79 C ANISOU 1874 CG LYS A1032 5369 5408 10419 799 -233 -881 C ATOM 1875 CD LYS A1032 9.202 -49.668 25.091 1.00 58.99 C ANISOU 1875 CD LYS A1032 5832 5748 10833 829 -136 -822 C ATOM 1876 CE LYS A1032 10.369 -48.984 25.784 1.00 79.47 C ANISOU 1876 CE LYS A1032 8298 8383 13516 792 -71 -893 C ATOM 1877 NZ LYS A1032 11.455 -48.634 24.826 1.00 79.65 N ANISOU 1877 NZ LYS A1032 8373 8341 13550 820 22 -834 N ATOM 1878 N MET A1033 4.150 -51.816 24.554 1.00 43.25 N ANISOU 1878 N MET A1033 4119 3730 8582 863 -470 -706 N ATOM 1879 CA MET A1033 2.938 -51.805 23.741 1.00 43.18 C ANISOU 1879 CA MET A1033 4223 3668 8514 871 -506 -647 C ATOM 1880 C MET A1033 1.691 -51.965 24.602 1.00 44.03 C ANISOU 1880 C MET A1033 4275 3825 8628 840 -604 -696 C ATOM 1881 O MET A1033 0.656 -51.348 24.325 1.00 44.23 O ANISOU 1881 O MET A1033 4320 3821 8665 821 -615 -693 O ATOM 1882 CB MET A1033 3.011 -52.910 22.687 1.00 45.31 C ANISOU 1882 CB MET A1033 4663 3898 8655 925 -524 -535 C ATOM 1883 CG MET A1033 4.138 -52.721 21.683 1.00 44.37 C ANISOU 1883 CG MET A1033 4614 3728 8515 959 -426 -477 C ATOM 1884 SD MET A1033 4.498 -54.208 20.729 1.00 47.64 S ANISOU 1884 SD MET A1033 5206 4118 8776 1022 -447 -363 S ATOM 1885 CE MET A1033 3.055 -54.294 19.674 1.00 43.95 C ANISOU 1885 CE MET A1033 4887 3604 8207 1029 -489 -290 C ATOM 1886 N ARG A1034 1.769 -52.786 25.652 1.00 43.22 N ANISOU 1886 N ARG A1034 4102 3805 8514 835 -675 -739 N ATOM 1887 CA ARG A1034 0.607 -52.995 26.510 1.00 43.31 C ANISOU 1887 CA ARG A1034 4073 3900 8482 784 -765 -776 C ATOM 1888 C ARG A1034 0.182 -51.694 27.180 1.00 48.36 C ANISOU 1888 C ARG A1034 4583 4558 9235 734 -737 -869 C ATOM 1889 O ARG A1034 -0.994 -51.315 27.140 1.00 50.11 O ANISOU 1889 O ARG A1034 4814 4765 9463 716 -775 -872 O ATOM 1890 CB ARG A1034 0.910 -54.064 27.560 1.00 41.58 C ANISOU 1890 CB ARG A1034 3811 3809 8178 757 -828 -797 C ATOM 1891 CG ARG A1034 -0.330 -54.572 28.281 1.00 46.11 C ANISOU 1891 CG ARG A1034 4377 4464 8680 716 -932 -811 C ATOM 1892 CD ARG A1034 0.008 -55.587 29.358 1.00 46.20 C ANISOU 1892 CD ARG A1034 4338 4604 8612 689 -990 -835 C ATOM 1893 NE ARG A1034 -1.195 -56.130 29.978 1.00 54.05 N ANISOU 1893 NE ARG A1034 5334 5670 9533 654 -1090 -839 N ATOM 1894 CZ ARG A1034 -1.848 -55.560 30.982 1.00 56.13 C ANISOU 1894 CZ ARG A1034 5484 6007 9837 598 -1118 -918 C ATOM 1895 NH1 ARG A1034 -1.434 -54.425 31.523 1.00 59.14 N ANISOU 1895 NH1 ARG A1034 5739 6402 10330 569 -1055 -1005 N ATOM 1896 NH2 ARG A1034 -2.948 -56.141 31.453 1.00 56.87 N ANISOU 1896 NH2 ARG A1034 5592 6161 9856 572 -1210 -910 N ATOM 1897 N ALA A1035 1.131 -50.996 27.808 1.00 47.30 N ANISOU 1897 N ALA A1035 4324 4456 9191 711 -671 -946 N ATOM 1898 CA ALA A1035 0.807 -49.730 28.457 1.00 49.95 C ANISOU 1898 CA ALA A1035 4535 4807 9637 662 -639 -1038 C ATOM 1899 C ALA A1035 0.243 -48.729 27.457 1.00 50.52 C ANISOU 1899 C ALA A1035 4675 4774 9746 665 -585 -1003 C ATOM 1900 O ALA A1035 -0.689 -47.980 27.773 1.00 54.23 O ANISOU 1900 O ALA A1035 5099 5248 10259 630 -597 -1045 O ATOM 1901 CB ALA A1035 2.048 -49.160 29.144 1.00 47.83 C ANISOU 1901 CB ALA A1035 4154 4589 9432 627 -566 -1111 C ATOM 1902 N ALA A1036 0.797 -48.699 26.242 1.00 49.10 N ANISOU 1902 N ALA A1036 4605 4510 9540 705 -523 -922 N ATOM 1903 CA ALA A1036 0.291 -47.783 25.225 1.00 51.42 C ANISOU 1903 CA ALA A1036 4968 4722 9848 705 -470 -877 C ATOM 1904 C ALA A1036 -1.119 -48.164 24.793 1.00 55.94 C ANISOU 1904 C ALA A1036 5629 5272 10353 717 -546 -823 C ATOM 1905 O ALA A1036 -1.972 -47.290 24.599 1.00 56.61 O ANISOU 1905 O ALA A1036 5706 5330 10472 695 -534 -832 O ATOM 1906 CB ALA A1036 1.233 -47.764 24.021 1.00 44.66 C ANISOU 1906 CB ALA A1036 4212 3801 8955 745 -391 -796 C ATOM 1907 N ALA A1037 -1.385 -49.463 24.636 1.00 50.65 N ANISOU 1907 N ALA A1037 5045 4614 9584 750 -625 -767 N ATOM 1908 CA ALA A1037 -2.719 -49.903 24.241 1.00 50.85 C ANISOU 1908 CA ALA A1037 5158 4623 9539 757 -704 -714 C ATOM 1909 C ALA A1037 -3.755 -49.510 25.287 1.00 57.26 C ANISOU 1909 C ALA A1037 5862 5485 10408 715 -765 -791 C ATOM 1910 O ALA A1037 -4.780 -48.900 24.964 1.00 60.23 O ANISOU 1910 O ALA A1037 6259 5830 10795 701 -771 -779 O ATOM 1911 CB ALA A1037 -2.726 -51.416 24.017 1.00 48.98 C ANISOU 1911 CB ALA A1037 5025 4398 9186 794 -781 -646 C ATOM 1912 N LEU A1038 -3.504 -49.857 26.552 1.00 58.61 N ANISOU 1912 N LEU A1038 5915 5744 10609 694 -808 -870 N ATOM 1913 CA LEU A1038 -4.407 -49.445 27.622 1.00 63.36 C ANISOU 1913 CA LEU A1038 6415 6427 11233 635 -854 -943 C ATOM 1914 C LEU A1038 -4.528 -47.929 27.694 1.00 64.39 C ANISOU 1914 C LEU A1038 6459 6516 11489 610 -777 -1006 C ATOM 1915 O LEU A1038 -5.602 -47.405 28.012 1.00 64.69 O ANISOU 1915 O LEU A1038 6461 6565 11554 582 -807 -1033 O ATOM 1916 CB LEU A1038 -3.923 -50.002 28.960 1.00 60.30 C ANISOU 1916 CB LEU A1038 5926 6174 10810 591 -891 -1010 C ATOM 1917 CG LEU A1038 -4.043 -51.516 29.139 1.00 59.54 C ANISOU 1917 CG LEU A1038 5902 6145 10574 598 -980 -956 C ATOM 1918 CD1 LEU A1038 -3.301 -51.965 30.387 1.00 66.42 C ANISOU 1918 CD1 LEU A1038 6668 7141 11427 562 -996 -1023 C ATOM 1919 CD2 LEU A1038 -5.504 -51.934 29.206 1.00 62.85 C ANISOU 1919 CD2 LEU A1038 6370 6586 10923 581 -1074 -925 C ATOM 1920 N ASP A1039 -3.442 -47.209 27.406 1.00 65.99 N ANISOU 1920 N ASP A1039 6640 6684 11748 607 -676 -1022 N ATOM 1921 CA ASP A1039 -3.510 -45.753 27.371 1.00 66.18 C ANISOU 1921 CA ASP A1039 6605 6674 11865 571 -596 -1068 C ATOM 1922 C ASP A1039 -4.390 -45.273 26.224 1.00 71.89 C ANISOU 1922 C ASP A1039 7432 7315 12569 588 -580 -991 C ATOM 1923 O ASP A1039 -5.159 -44.318 26.381 1.00 74.21 O ANISOU 1923 O ASP A1039 7680 7597 12919 558 -565 -1024 O ATOM 1924 CB ASP A1039 -2.103 -45.168 27.251 1.00 67.47 C ANISOU 1924 CB ASP A1039 6732 6821 12083 564 -495 -1091 C ATOM 1925 CG ASP A1039 -2.111 -43.668 27.040 1.00 79.37 C ANISOU 1925 CG ASP A1039 8196 8282 13679 530 -408 -1123 C ATOM 1926 OD1 ASP A1039 -2.493 -42.937 27.978 1.00 85.46 O ANISOU 1926 OD1 ASP A1039 8863 9093 14516 478 -408 -1211 O ATOM 1927 OD2 ASP A1039 -1.734 -43.221 25.937 1.00 79.48 O ANISOU 1927 OD2 ASP A1039 8284 8225 13690 554 -339 -1058 O ATOM 1928 N ALA A1040 -4.291 -45.925 25.064 1.00 73.94 N ANISOU 1928 N ALA A1040 7831 7522 12741 636 -581 -887 N ATOM 1929 CA ALA A1040 -5.141 -45.582 23.931 1.00 80.22 C ANISOU 1929 CA ALA A1040 8733 8254 13493 653 -571 -807 C ATOM 1930 C ALA A1040 -6.585 -46.021 24.128 1.00 80.09 C ANISOU 1930 C ALA A1040 8741 8253 13435 648 -670 -791 C ATOM 1931 O ALA A1040 -7.455 -45.586 23.366 1.00 84.87 O ANISOU 1931 O ALA A1040 9412 8817 14019 653 -665 -740 O ATOM 1932 CB ALA A1040 -4.584 -46.209 22.651 1.00 79.35 C ANISOU 1932 CB ALA A1040 8768 8097 13285 703 -544 -702 C ATOM 1933 N GLN A1041 -6.860 -46.862 25.125 1.00 75.28 N ANISOU 1933 N GLN A1041 8082 7708 12813 639 -760 -833 N ATOM 1934 CA GLN A1041 -8.208 -47.331 25.411 1.00 75.51 C ANISOU 1934 CA GLN A1041 8127 7760 12804 633 -861 -820 C ATOM 1935 C GLN A1041 -8.962 -46.393 26.349 1.00 82.31 C ANISOU 1935 C GLN A1041 8862 8657 13755 588 -866 -906 C ATOM 1936 O GLN A1041 -9.903 -46.829 27.023 1.00 77.69 O ANISOU 1936 O GLN A1041 8244 8124 13150 575 -956 -924 O ATOM 1937 CB GLN A1041 -8.154 -48.739 26.007 1.00 68.69 C ANISOU 1937 CB GLN A1041 7273 6958 11869 647 -960 -815 C ATOM 1938 CG GLN A1041 -9.428 -49.546 25.820 1.00 69.95 C ANISOU 1938 CG GLN A1041 7517 7131 11931 648 -1065 -753 C ATOM 1939 CD GLN A1041 -9.342 -50.921 26.452 1.00 72.11 C ANISOU 1939 CD GLN A1041 7810 7501 12086 633 -1150 -741 C ATOM 1940 OE1 GLN A1041 -8.402 -51.221 27.189 1.00 71.94 O ANISOU 1940 OE1 GLN A1041 7722 7548 12063 618 -1135 -789 O ATOM 1941 NE2 GLN A1041 -10.324 -51.767 26.165 1.00 76.20 N ANISOU 1941 NE2 GLN A1041 8421 8027 12504 636 -1240 -675 N ATOM 1942 N LYS A1042 -8.569 -45.124 26.408 1.00 78.23 N ANISOU 1942 N LYS A1042 8275 8119 13329 562 -771 -957 N ATOM 1943 CA LYS A1042 -9.220 -44.153 27.278 1.00 74.18 C ANISOU 1943 CA LYS A1042 7647 7638 12901 515 -764 -1041 C ATOM 1944 C LYS A1042 -9.371 -42.813 26.567 1.00 68.88 C ANISOU 1944 C LYS A1042 6984 6898 12290 505 -672 -1028 C ATOM 1945 O LYS A1042 -10.225 -42.655 25.694 1.00 65.42 O ANISOU 1945 O LYS A1042 6630 6412 11817 523 -680 -956 O ATOM 1946 CB LYS A1042 -8.425 -43.976 28.573 1.00 70.88 C ANISOU 1946 CB LYS A1042 7094 7303 12535 474 -746 -1149 C ATOM 1947 N SER A1055 -22.971 -46.967 20.211 1.00 90.19 N ANISOU 1947 N SER A1055 10613 9453 14202 598 -1420 -202 N ATOM 1948 CA SER A1055 -22.762 -46.859 18.771 1.00103.79 C ANISOU 1948 CA SER A1055 12455 11130 15849 628 -1355 -127 C ATOM 1949 C SER A1055 -22.150 -48.147 18.214 1.00106.56 C ANISOU 1949 C SER A1055 12924 11489 16076 646 -1385 -76 C ATOM 1950 O SER A1055 -21.376 -48.811 18.902 1.00105.19 O ANISOU 1950 O SER A1055 12723 11342 15903 643 -1410 -114 O ATOM 1951 CB SER A1055 -21.861 -45.664 18.453 1.00105.14 C ANISOU 1951 CB SER A1055 12584 11261 16104 644 -1225 -161 C ATOM 1952 OG SER A1055 -21.324 -45.760 17.145 1.00 99.87 O ANISOU 1952 OG SER A1055 12034 10557 15354 679 -1161 -96 O ATOM 1953 N PRO A1056 -22.495 -48.508 16.965 1.00103.15 N ANISOU 1953 N PRO A1056 12622 11036 15534 666 -1378 7 N ATOM 1954 CA PRO A1056 -21.927 -49.733 16.381 1.00 99.35 C ANISOU 1954 CA PRO A1056 12257 10562 14928 683 -1398 55 C ATOM 1955 C PRO A1056 -20.437 -49.606 16.114 1.00 97.58 C ANISOU 1955 C PRO A1056 12042 10314 14720 713 -1305 37 C ATOM 1956 O PRO A1056 -19.655 -50.497 16.460 1.00 93.18 O ANISOU 1956 O PRO A1056 11501 9777 14126 716 -1329 26 O ATOM 1957 CB PRO A1056 -22.715 -49.908 15.074 1.00 92.60 C ANISOU 1957 CB PRO A1056 11525 9690 13968 698 -1396 141 C ATOM 1958 CG PRO A1056 -23.878 -48.976 15.168 1.00 99.73 C ANISOU 1958 CG PRO A1056 12372 10586 14933 681 -1407 139 C ATOM 1959 CD PRO A1056 -23.434 -47.852 16.039 1.00 98.25 C ANISOU 1959 CD PRO A1056 12049 10388 14895 674 -1353 61 C ATOM 1960 N GLU A1057 -20.036 -48.498 15.486 1.00101.55 N ANISOU 1960 N GLU A1057 12536 10774 15273 734 -1198 35 N ATOM 1961 CA GLU A1057 -18.620 -48.278 15.209 1.00101.06 C ANISOU 1961 CA GLU A1057 12480 10689 15228 761 -1104 18 C ATOM 1962 C GLU A1057 -17.805 -48.282 16.496 1.00 99.41 C ANISOU 1962 C GLU A1057 12152 10506 15113 741 -1112 -66 C ATOM 1963 O GLU A1057 -16.672 -48.778 16.522 1.00 99.03 O ANISOU 1963 O GLU A1057 12122 10460 15045 758 -1084 -74 O ATOM 1964 CB GLU A1057 -18.435 -46.960 14.457 1.00102.21 C ANISOU 1964 CB GLU A1057 12620 10790 15426 781 -994 23 C ATOM 1965 CG GLU A1057 -17.012 -46.709 13.982 1.00101.42 C ANISOU 1965 CG GLU A1057 12542 10663 15330 811 -893 18 C ATOM 1966 CD GLU A1057 -16.843 -45.347 13.335 1.00100.63 C ANISOU 1966 CD GLU A1057 12427 10522 15285 827 -789 18 C ATOM 1967 OE1 GLU A1057 -17.403 -44.361 13.861 1.00 96.33 O ANISOU 1967 OE1 GLU A1057 11785 9977 14839 802 -780 -24 O ATOM 1968 OE2 GLU A1057 -16.152 -45.264 12.298 1.00 99.03 O ANISOU 1968 OE2 GLU A1057 12312 10290 15025 865 -717 59 O ATOM 1969 N MET A1058 -18.365 -47.733 17.577 1.00101.54 N ANISOU 1969 N MET A1058 12298 10797 15484 708 -1147 -130 N ATOM 1970 CA MET A1058 -17.676 -47.764 18.863 1.00103.97 C ANISOU 1970 CA MET A1058 12487 11138 15880 689 -1158 -217 C ATOM 1971 C MET A1058 -17.675 -49.164 19.462 1.00 97.79 C ANISOU 1971 C MET A1058 11729 10399 15028 682 -1263 -213 C ATOM 1972 O MET A1058 -16.734 -49.532 20.175 1.00 92.19 O ANISOU 1972 O MET A1058 10967 9713 14348 682 -1262 -263 O ATOM 1973 CB MET A1058 -18.325 -46.776 19.831 1.00109.45 C ANISOU 1973 CB MET A1058 13044 11846 16697 656 -1163 -290 C ATOM 1974 CG MET A1058 -17.527 -45.500 20.044 1.00117.25 C ANISOU 1974 CG MET A1058 13936 12813 17800 652 -1050 -355 C ATOM 1975 SD MET A1058 -15.990 -45.776 20.947 1.00122.19 S ANISOU 1975 SD MET A1058 14481 13467 18480 648 -1019 -434 S ATOM 1976 CE MET A1058 -16.617 -46.373 22.516 1.00115.29 C ANISOU 1976 CE MET A1058 13500 12662 17644 615 -1135 -507 C ATOM 1977 N LYS A1059 -18.717 -49.953 19.190 1.00 95.43 N ANISOU 1977 N LYS A1059 11507 10115 14635 675 -1354 -155 N ATOM 1978 CA LYS A1059 -18.740 -51.332 19.665 1.00 86.98 C ANISOU 1978 CA LYS A1059 10474 9090 13484 668 -1453 -142 C ATOM 1979 C LYS A1059 -17.603 -52.143 19.058 1.00 79.39 C ANISOU 1979 C LYS A1059 9606 8119 12441 698 -1418 -107 C ATOM 1980 O LYS A1059 -17.083 -53.061 19.702 1.00 75.43 O ANISOU 1980 O LYS A1059 9095 7652 11912 696 -1468 -126 O ATOM 1981 CB LYS A1059 -20.092 -51.970 19.341 1.00 84.89 C ANISOU 1981 CB LYS A1059 10287 8843 13126 652 -1547 -79 C ATOM 1982 CG LYS A1059 -20.263 -53.391 19.860 1.00 78.66 C ANISOU 1982 CG LYS A1059 9536 8107 12246 638 -1655 -64 C ATOM 1983 CD LYS A1059 -20.288 -54.401 18.723 1.00 72.51 C ANISOU 1983 CD LYS A1059 8916 7319 11315 652 -1665 22 C ATOM 1984 CE LYS A1059 -20.784 -55.759 19.194 1.00 72.75 C ANISOU 1984 CE LYS A1059 8991 7406 11246 627 -1778 44 C ATOM 1985 NZ LYS A1059 -21.194 -56.628 18.056 1.00 68.70 N ANISOU 1985 NZ LYS A1059 8627 6889 10587 630 -1791 125 N ATOM 1986 N ASP A1060 -17.199 -51.815 17.830 1.00 80.70 N ANISOU 1986 N ASP A1060 9859 8238 12564 727 -1330 -57 N ATOM 1987 CA ASP A1060 -16.086 -52.503 17.189 1.00 78.19 C ANISOU 1987 CA ASP A1060 9630 7908 12171 759 -1285 -22 C ATOM 1988 C ASP A1060 -14.734 -51.948 17.613 1.00 74.02 C ANISOU 1988 C ASP A1060 9020 7369 11734 772 -1202 -81 C ATOM 1989 O ASP A1060 -13.733 -52.668 17.536 1.00 67.84 O ANISOU 1989 O ASP A1060 8277 6591 10908 792 -1186 -72 O ATOM 1990 CB ASP A1060 -16.225 -52.415 15.667 1.00 78.14 C ANISOU 1990 CB ASP A1060 9753 7862 12074 789 -1223 57 C ATOM 1991 CG ASP A1060 -17.580 -52.889 15.178 1.00 86.51 C ANISOU 1991 CG ASP A1060 10890 8934 13046 775 -1296 114 C ATOM 1992 OD1 ASP A1060 -18.152 -53.806 15.805 1.00 81.39 O ANISOU 1992 OD1 ASP A1060 10242 8328 12353 749 -1400 114 O ATOM 1993 OD2 ASP A1060 -18.076 -52.341 14.171 1.00 91.23 O ANISOU 1993 OD2 ASP A1060 11545 9501 13617 790 -1249 158 O ATOM 1994 N PHE A1061 -14.678 -50.688 18.054 1.00 79.36 N ANISOU 1994 N PHE A1061 9583 8033 12536 758 -1147 -142 N ATOM 1995 CA PHE A1061 -13.429 -50.151 18.581 1.00 78.23 C ANISOU 1995 CA PHE A1061 9350 7889 12487 762 -1073 -207 C ATOM 1996 C PHE A1061 -13.128 -50.708 19.966 1.00 74.17 C ANISOU 1996 C PHE A1061 8735 7426 12021 741 -1139 -278 C ATOM 1997 O PHE A1061 -11.957 -50.900 20.313 1.00 70.98 O ANISOU 1997 O PHE A1061 8295 7032 11643 751 -1103 -311 O ATOM 1998 CB PHE A1061 -13.483 -48.621 18.625 1.00 83.91 C ANISOU 1998 CB PHE A1061 9979 8582 13321 749 -990 -252 C ATOM 1999 CG PHE A1061 -13.447 -47.962 17.266 1.00 83.80 C ANISOU 1999 CG PHE A1061 10053 8517 13268 777 -904 -190 C ATOM 2000 CD1 PHE A1061 -12.829 -48.577 16.186 1.00 77.33 C ANISOU 2000 CD1 PHE A1061 9364 7675 12343 816 -869 -120 C ATOM 2001 CD2 PHE A1061 -14.029 -46.719 17.076 1.00 85.49 C ANISOU 2001 CD2 PHE A1061 10222 8708 13552 766 -856 -203 C ATOM 2002 CE1 PHE A1061 -12.797 -47.967 14.946 1.00 73.66 C ANISOU 2002 CE1 PHE A1061 8980 7166 11841 845 -791 -67 C ATOM 2003 CE2 PHE A1061 -13.999 -46.105 15.837 1.00 81.96 C ANISOU 2003 CE2 PHE A1061 9856 8218 13068 795 -779 -147 C ATOM 2004 CZ PHE A1061 -13.383 -46.731 14.772 1.00 76.07 C ANISOU 2004 CZ PHE A1061 9238 7450 12214 835 -748 -81 C ATOM 2005 N ARG A1062 -14.162 -50.975 20.767 1.00 75.86 N ANISOU 2005 N ARG A1062 8900 7678 12246 713 -1237 -302 N ATOM 2006 CA ARG A1062 -13.943 -51.633 22.051 1.00 74.42 C ANISOU 2006 CA ARG A1062 8631 7555 12091 698 -1309 -363 C ATOM 2007 C ARG A1062 -13.536 -53.087 21.855 1.00 66.15 C ANISOU 2007 C ARG A1062 7683 6527 10925 718 -1367 -311 C ATOM 2008 O ARG A1062 -12.698 -53.610 22.599 1.00 61.68 O ANISOU 2008 O ARG A1062 7065 5998 10374 722 -1380 -352 O ATOM 2009 CB ARG A1062 -15.201 -51.537 22.915 1.00 80.91 C ANISOU 2009 CB ARG A1062 9380 8418 12946 667 -1399 -396 C ATOM 2010 CG ARG A1062 -15.375 -50.191 23.599 1.00 86.35 C ANISOU 2010 CG ARG A1062 9927 9110 13772 643 -1347 -481 C ATOM 2011 CD ARG A1062 -16.562 -50.185 24.553 1.00 92.57 C ANISOU 2011 CD ARG A1062 10637 9962 14575 607 -1432 -515 C ATOM 2012 NE ARG A1062 -17.698 -49.444 24.014 1.00 98.96 N ANISOU 2012 NE ARG A1062 11467 10724 15408 604 -1432 -482 N ATOM 2013 CZ ARG A1062 -18.722 -49.987 23.368 1.00 99.22 C ANISOU 2013 CZ ARG A1062 11603 10746 15349 605 -1498 -401 C ATOM 2014 NH1 ARG A1062 -18.800 -51.292 23.161 1.00 94.84 N ANISOU 2014 NH1 ARG A1062 11143 10214 14677 612 -1577 -344 N ATOM 2015 NH2 ARG A1062 -19.695 -49.199 22.920 1.00 99.35 N ANISOU 2015 NH2 ARG A1062 11628 10733 15389 596 -1484 -376 N ATOM 2016 N HIS A1063 -14.117 -53.756 20.856 1.00 59.57 N ANISOU 2016 N HIS A1063 6991 5674 9969 728 -1398 -221 N ATOM 2017 CA HIS A1063 -13.715 -55.124 20.551 1.00 57.96 C ANISOU 2017 CA HIS A1063 6893 5485 9643 746 -1440 -166 C ATOM 2018 C HIS A1063 -12.305 -55.175 19.976 1.00 55.41 C ANISOU 2018 C HIS A1063 6610 5132 9309 780 -1345 -153 C ATOM 2019 O HIS A1063 -11.594 -56.168 20.167 1.00 50.42 O ANISOU 2019 O HIS A1063 6013 4523 8621 795 -1368 -142 O ATOM 2020 CB HIS A1063 -14.709 -55.754 19.575 1.00 55.46 C ANISOU 2020 CB HIS A1063 6716 5159 9197 744 -1485 -79 C ATOM 2021 CG HIS A1063 -14.445 -57.201 19.291 1.00 52.97 C ANISOU 2021 CG HIS A1063 6510 4866 8749 754 -1532 -25 C ATOM 2022 ND1 HIS A1063 -14.339 -58.148 20.286 1.00 51.47 N ANISOU 2022 ND1 HIS A1063 6287 4732 8536 741 -1616 -49 N ATOM 2023 CD2 HIS A1063 -14.270 -57.863 18.122 1.00 54.57 C ANISOU 2023 CD2 HIS A1063 6855 5047 8832 777 -1501 50 C ATOM 2024 CE1 HIS A1063 -14.107 -59.330 19.744 1.00 50.39 C ANISOU 2024 CE1 HIS A1063 6270 4605 8272 753 -1636 10 C ATOM 2025 NE2 HIS A1063 -14.062 -59.185 18.432 1.00 50.67 N ANISOU 2025 NE2 HIS A1063 6411 4593 8247 774 -1565 69 N ATOM 2026 N GLY A1064 -11.883 -54.119 19.279 1.00 51.88 N ANISOU 2026 N GLY A1064 6161 4637 8912 795 -1238 -152 N ATOM 2027 CA GLY A1064 -10.544 -54.105 18.714 1.00 49.20 C ANISOU 2027 CA GLY A1064 5859 4272 8565 829 -1145 -138 C ATOM 2028 C GLY A1064 -9.463 -54.019 19.775 1.00 47.56 C ANISOU 2028 C GLY A1064 5531 4090 8448 825 -1126 -215 C ATOM 2029 O GLY A1064 -8.443 -54.709 19.690 1.00 47.57 O ANISOU 2029 O GLY A1064 5568 4097 8411 850 -1106 -200 O ATOM 2030 N PHE A1065 -9.666 -53.172 20.787 1.00 49.05 N ANISOU 2030 N PHE A1065 5575 4301 8761 795 -1129 -301 N ATOM 2031 CA PHE A1065 -8.680 -53.061 21.856 1.00 50.79 C ANISOU 2031 CA PHE A1065 5670 4558 9071 789 -1111 -383 C ATOM 2032 C PHE A1065 -8.695 -54.284 22.764 1.00 51.86 C ANISOU 2032 C PHE A1065 5786 4756 9162 787 -1213 -398 C ATOM 2033 O PHE A1065 -7.664 -54.626 23.353 1.00 50.61 O ANISOU 2033 O PHE A1065 5571 4629 9029 797 -1199 -436 O ATOM 2034 CB PHE A1065 -8.920 -51.788 22.670 1.00 54.93 C ANISOU 2034 CB PHE A1065 6043 5096 9733 755 -1079 -475 C ATOM 2035 CG PHE A1065 -8.396 -50.542 22.012 1.00 58.41 C ANISOU 2035 CG PHE A1065 6470 5486 10236 757 -958 -480 C ATOM 2036 CD1 PHE A1065 -7.032 -50.343 21.870 1.00 55.12 C ANISOU 2036 CD1 PHE A1065 6036 5058 9849 773 -872 -494 C ATOM 2037 CD2 PHE A1065 -9.262 -49.569 21.544 1.00 60.30 C ANISOU 2037 CD2 PHE A1065 6714 5693 10505 744 -930 -469 C ATOM 2038 CE1 PHE A1065 -6.543 -49.202 21.266 1.00 60.65 C ANISOU 2038 CE1 PHE A1065 6725 5716 10603 774 -764 -495 C ATOM 2039 CE2 PHE A1065 -8.778 -48.423 20.940 1.00 57.78 C ANISOU 2039 CE2 PHE A1065 6383 5332 10239 747 -821 -471 C ATOM 2040 CZ PHE A1065 -7.417 -48.239 20.802 1.00 64.59 C ANISOU 2040 CZ PHE A1065 7229 6184 11128 761 -739 -484 C ATOM 2041 N ASP A1066 -9.845 -54.951 22.894 1.00 54.86 N ANISOU 2041 N ASP A1066 6211 5160 9474 774 -1317 -367 N ATOM 2042 CA ASP A1066 -9.880 -56.211 23.630 1.00 53.80 C ANISOU 2042 CA ASP A1066 6081 5104 9257 764 -1409 -365 C ATOM 2043 C ASP A1066 -9.024 -57.265 22.941 1.00 51.53 C ANISOU 2043 C ASP A1066 5912 4786 8882 808 -1403 -298 C ATOM 2044 O ASP A1066 -8.336 -58.050 23.605 1.00 52.02 O ANISOU 2044 O ASP A1066 5947 4918 8901 802 -1420 -316 O ATOM 2045 CB ASP A1066 -11.321 -56.704 23.768 1.00 59.47 C ANISOU 2045 CB ASP A1066 6838 5856 9903 736 -1513 -333 C ATOM 2046 CG ASP A1066 -12.132 -55.870 24.738 1.00 68.77 C ANISOU 2046 CG ASP A1066 7885 7097 11148 683 -1529 -407 C ATOM 2047 OD1 ASP A1066 -11.534 -55.271 25.657 1.00 78.55 O ANISOU 2047 OD1 ASP A1066 8992 8393 12461 656 -1482 -492 O ATOM 2048 OD2 ASP A1066 -13.371 -55.819 24.585 1.00 72.91 O ANISOU 2048 OD2 ASP A1066 8437 7614 11650 668 -1588 -379 O ATOM 2049 N ILE A1067 -9.059 -57.301 21.608 1.00 46.93 N ANISOU 2049 N ILE A1067 5465 4143 8221 827 -1353 -218 N ATOM 2050 CA ILE A1067 -8.188 -58.207 20.869 1.00 42.39 C ANISOU 2050 CA ILE A1067 5007 3552 7547 861 -1321 -155 C ATOM 2051 C ILE A1067 -6.734 -57.779 21.016 1.00 41.41 C ANISOU 2051 C ILE A1067 4819 3416 7498 884 -1228 -193 C ATOM 2052 O ILE A1067 -5.835 -58.618 21.153 1.00 39.44 O ANISOU 2052 O ILE A1067 4592 3184 7207 907 -1228 -180 O ATOM 2053 CB ILE A1067 -8.609 -58.261 19.389 1.00 41.61 C ANISOU 2053 CB ILE A1067 5060 3403 7347 877 -1281 -67 C ATOM 2054 CG1 ILE A1067 -10.035 -58.801 19.253 1.00 46.71 C ANISOU 2054 CG1 ILE A1067 5770 4068 7910 851 -1376 -29 C ATOM 2055 CG2 ILE A1067 -7.638 -59.122 18.595 1.00 42.53 C ANISOU 2055 CG2 ILE A1067 5291 3504 7366 915 -1233 -6 C ATOM 2056 CD1 ILE A1067 -10.652 -58.561 17.888 1.00 49.73 C ANISOU 2056 CD1 ILE A1067 6269 4407 8219 860 -1333 41 C ATOM 2057 N LEU A1068 -6.479 -56.469 20.996 1.00 41.19 N ANISOU 2057 N LEU A1068 4708 3361 7581 877 -1147 -240 N ATOM 2058 CA LEU A1068 -5.105 -55.979 21.016 1.00 38.14 C ANISOU 2058 CA LEU A1068 4268 2962 7264 895 -1049 -270 C ATOM 2059 C LEU A1068 -4.433 -56.276 22.350 1.00 38.13 C ANISOU 2059 C LEU A1068 4135 3022 7329 887 -1080 -348 C ATOM 2060 O LEU A1068 -3.324 -56.821 22.388 1.00 37.41 O ANISOU 2060 O LEU A1068 4053 2941 7222 912 -1051 -340 O ATOM 2061 CB LEU A1068 -5.082 -54.479 20.727 1.00 41.91 C ANISOU 2061 CB LEU A1068 4684 3401 7840 882 -958 -304 C ATOM 2062 CG LEU A1068 -3.706 -53.903 20.388 1.00 41.49 C ANISOU 2062 CG LEU A1068 4608 3322 7836 902 -843 -314 C ATOM 2063 CD1 LEU A1068 -3.252 -54.385 19.018 1.00 43.67 C ANISOU 2063 CD1 LEU A1068 5042 3552 7998 946 -792 -217 C ATOM 2064 CD2 LEU A1068 -3.733 -52.386 20.446 1.00 39.86 C ANISOU 2064 CD2 LEU A1068 4308 3095 7744 878 -767 -367 C ATOM 2065 N VAL A1069 -5.082 -55.912 23.457 1.00 36.33 N ANISOU 2065 N VAL A1069 3783 2847 7175 851 -1135 -425 N ATOM 2066 CA VAL A1069 -4.502 -56.185 24.770 1.00 41.48 C ANISOU 2066 CA VAL A1069 4314 3618 7827 810 -1146 -498 C ATOM 2067 C VAL A1069 -4.404 -57.687 25.002 1.00 40.34 C ANISOU 2067 C VAL A1069 4238 3536 7553 816 -1220 -453 C ATOM 2068 O VAL A1069 -3.435 -58.178 25.595 1.00 39.18 O ANISOU 2068 O VAL A1069 4044 3452 7389 813 -1206 -477 O ATOM 2069 CB VAL A1069 -5.324 -55.494 25.874 1.00 46.97 C ANISOU 2069 CB VAL A1069 4878 4392 8575 747 -1178 -581 C ATOM 2070 CG1 VAL A1069 -4.760 -55.831 27.248 1.00 46.48 C ANISOU 2070 CG1 VAL A1069 4695 4460 8507 705 -1195 -655 C ATOM 2071 CG2 VAL A1069 -5.341 -53.990 25.658 1.00 48.14 C ANISOU 2071 CG2 VAL A1069 4956 4478 8857 743 -1097 -628 C ATOM 2072 N GLY A1070 -5.402 -58.440 24.539 1.00 37.01 N ANISOU 2072 N GLY A1070 3927 3096 7037 822 -1301 -387 N ATOM 2073 CA GLY A1070 -5.344 -59.886 24.677 1.00 38.72 C ANISOU 2073 CA GLY A1070 4221 3362 7129 829 -1371 -339 C ATOM 2074 C GLY A1070 -4.192 -60.497 23.902 1.00 40.04 C ANISOU 2074 C GLY A1070 4481 3473 7259 887 -1322 -282 C ATOM 2075 O GLY A1070 -3.497 -61.385 24.401 1.00 36.92 O ANISOU 2075 O GLY A1070 4079 3142 6806 889 -1335 -281 O ATOM 2076 N GLN A1071 -3.976 -60.032 22.669 1.00 37.07 N ANISOU 2076 N GLN A1071 4193 2977 6916 936 -1262 -232 N ATOM 2077 CA GLN A1071 -2.866 -60.546 21.873 1.00 34.26 C ANISOU 2077 CA GLN A1071 3931 2586 6499 977 -1193 -174 C ATOM 2078 C GLN A1071 -1.519 -60.134 22.453 1.00 33.69 C ANISOU 2078 C GLN A1071 3744 2530 6526 991 -1124 -232 C ATOM 2079 O GLN A1071 -0.548 -60.894 22.364 1.00 36.32 O ANISOU 2079 O GLN A1071 4115 2872 6814 1022 -1104 -202 O ATOM 2080 CB GLN A1071 -2.992 -60.065 20.429 1.00 34.02 C ANISOU 2080 CB GLN A1071 4021 2483 6422 991 -1113 -108 C ATOM 2081 CG GLN A1071 -4.116 -60.734 19.659 1.00 39.71 C ANISOU 2081 CG GLN A1071 4879 3193 7015 985 -1169 -35 C ATOM 2082 CD GLN A1071 -4.329 -60.124 18.289 1.00 38.52 C ANISOU 2082 CD GLN A1071 4827 2982 6828 1000 -1087 19 C ATOM 2083 OE1 GLN A1071 -4.247 -58.908 18.119 1.00 38.42 O ANISOU 2083 OE1 GLN A1071 4755 2938 6904 996 -1021 -12 O ATOM 2084 NE2 GLN A1071 -4.601 -60.968 17.302 1.00 42.82 N ANISOU 2084 NE2 GLN A1071 5519 3513 7236 1016 -1088 99 N ATOM 2085 N ILE A1072 -1.432 -58.937 23.036 1.00 37.62 N ANISOU 2085 N ILE A1072 4104 3045 7146 961 -1079 -313 N ATOM 2086 CA ILE A1072 -0.196 -58.536 23.697 1.00 38.43 C ANISOU 2086 CA ILE A1072 4089 3193 7320 952 -1008 -374 C ATOM 2087 C ILE A1072 0.048 -59.400 24.927 1.00 36.86 C ANISOU 2087 C ILE A1072 3818 3128 7060 916 -1063 -412 C ATOM 2088 O ILE A1072 1.183 -59.808 25.202 1.00 38.46 O ANISOU 2088 O ILE A1072 3993 3366 7255 930 -1027 -417 O ATOM 2089 CB ILE A1072 -0.241 -57.038 24.052 1.00 41.21 C ANISOU 2089 CB ILE A1072 4313 3537 7810 921 -947 -455 C ATOM 2090 CG1 ILE A1072 -0.265 -56.193 22.775 1.00 34.66 C ANISOU 2090 CG1 ILE A1072 3563 2599 7007 945 -867 -408 C ATOM 2091 CG2 ILE A1072 0.955 -56.661 24.916 1.00 38.10 C ANISOU 2091 CG2 ILE A1072 3782 3208 7485 901 -887 -529 C ATOM 2092 CD1 ILE A1072 -0.630 -54.742 23.003 1.00 43.07 C ANISOU 2092 CD1 ILE A1072 4527 3652 8185 908 -819 -474 C ATOM 2093 N ASP A1073 -1.012 -59.701 25.683 1.00 37.98 N ANISOU 2093 N ASP A1073 3928 3347 7157 869 -1151 -438 N ATOM 2094 CA ASP A1073 -0.867 -60.565 26.850 1.00 41.53 C ANISOU 2094 CA ASP A1073 4314 3924 7543 835 -1209 -470 C ATOM 2095 C ASP A1073 -0.419 -61.965 26.449 1.00 40.15 C ANISOU 2095 C ASP A1073 4256 3748 7251 875 -1238 -391 C ATOM 2096 O ASP A1073 0.443 -62.560 27.107 1.00 40.22 O ANISOU 2096 O ASP A1073 4217 3832 7231 873 -1233 -407 O ATOM 2097 CB ASP A1073 -2.185 -60.630 27.623 1.00 40.20 C ANISOU 2097 CB ASP A1073 4102 3828 7345 781 -1298 -503 C ATOM 2098 CG ASP A1073 -2.499 -59.341 28.355 1.00 48.34 C ANISOU 2098 CG ASP A1073 4989 4891 8488 734 -1271 -596 C ATOM 2099 OD1 ASP A1073 -1.635 -58.439 28.375 1.00 47.27 O ANISOU 2099 OD1 ASP A1073 4778 4733 8451 737 -1185 -642 O ATOM 2100 OD2 ASP A1073 -3.613 -59.231 28.910 1.00 47.46 O ANISOU 2100 OD2 ASP A1073 4841 4827 8366 692 -1336 -623 O ATOM 2101 N ASP A1074 -0.997 -62.512 25.377 1.00 37.67 N ANISOU 2101 N ASP A1074 4097 3350 6866 912 -1271 -306 N ATOM 2102 CA ASP A1074 -0.602 -63.843 24.925 1.00 39.33 C ANISOU 2102 CA ASP A1074 4430 3550 6964 952 -1297 -228 C ATOM 2103 C ASP A1074 0.882 -63.883 24.583 1.00 39.18 C ANISOU 2103 C ASP A1074 4415 3501 6971 997 -1209 -213 C ATOM 2104 O ASP A1074 1.605 -64.796 25.000 1.00 38.81 O ANISOU 2104 O ASP A1074 4369 3513 6864 1007 -1217 -200 O ATOM 2105 CB ASP A1074 -1.442 -64.259 23.715 1.00 36.99 C ANISOU 2105 CB ASP A1074 4301 3153 6600 985 -1336 -141 C ATOM 2106 CG ASP A1074 -2.916 -64.394 24.043 1.00 40.31 C ANISOU 2106 CG ASP A1074 4728 3609 6981 942 -1432 -146 C ATOM 2107 OD1 ASP A1074 -3.284 -64.208 25.222 1.00 41.86 O ANISOU 2107 OD1 ASP A1074 4800 3907 7198 887 -1468 -215 O ATOM 2108 OD2 ASP A1074 -3.708 -64.684 23.119 1.00 34.33 O ANISOU 2108 OD2 ASP A1074 4098 2776 6171 962 -1471 -80 O ATOM 2109 N ALA A1075 1.357 -62.896 23.820 1.00 38.38 N ANISOU 2109 N ALA A1075 4316 3307 6960 1026 -1122 -212 N ATOM 2110 CA ALA A1075 2.771 -62.860 23.464 1.00 40.50 C ANISOU 2110 CA ALA A1075 4584 3542 7261 1070 -1034 -197 C ATOM 2111 C ALA A1075 3.648 -62.597 24.680 1.00 38.08 C ANISOU 2111 C ALA A1075 4117 3343 7011 1035 -1003 -277 C ATOM 2112 O ALA A1075 4.770 -63.109 24.756 1.00 39.43 O ANISOU 2112 O ALA A1075 4284 3534 7163 1062 -964 -261 O ATOM 2113 CB ALA A1075 3.020 -61.795 22.397 1.00 37.02 C ANISOU 2113 CB ALA A1075 4176 2978 6911 1107 -948 -180 C ATOM 2114 N LEU A1076 3.156 -61.813 25.641 1.00 38.30 N ANISOU 2114 N LEU A1076 4009 3439 7105 975 -1020 -364 N ATOM 2115 CA LEU A1076 3.964 -61.493 26.812 1.00 42.02 C ANISOU 2115 CA LEU A1076 4321 4012 7632 938 -991 -447 C ATOM 2116 C LEU A1076 4.159 -62.717 27.698 1.00 39.69 C ANISOU 2116 C LEU A1076 4010 3832 7239 923 -1054 -444 C ATOM 2117 O LEU A1076 5.231 -62.898 28.287 1.00 41.84 O ANISOU 2117 O LEU A1076 4205 4167 7523 922 -1019 -470 O ATOM 2118 CB LEU A1076 3.317 -60.354 27.600 1.00 45.95 C ANISOU 2118 CB LEU A1076 4686 4552 8222 878 -996 -540 C ATOM 2119 CG LEU A1076 4.211 -59.672 28.638 1.00 53.16 C ANISOU 2119 CG LEU A1076 5430 5547 9223 841 -945 -633 C ATOM 2120 CD1 LEU A1076 5.325 -58.891 27.957 1.00 53.10 C ANISOU 2120 CD1 LEU A1076 5412 5457 9309 877 -836 -629 C ATOM 2121 CD2 LEU A1076 3.391 -58.764 29.540 1.00 62.39 C ANISOU 2121 CD2 LEU A1076 6476 6772 10458 777 -970 -724 C ATOM 2122 N LYS A1077 3.137 -63.569 27.808 1.00 43.04 N ANISOU 2122 N LYS A1077 4503 4284 7565 911 -1147 -412 N ATOM 2123 CA LYS A1077 3.299 -64.804 28.568 1.00 43.90 C ANISOU 2123 CA LYS A1077 4610 4496 7575 901 -1207 -400 C ATOM 2124 C LYS A1077 4.305 -65.729 27.897 1.00 45.29 C ANISOU 2124 C LYS A1077 4889 4633 7689 962 -1173 -323 C ATOM 2125 O LYS A1077 5.159 -66.320 28.567 1.00 47.88 O ANISOU 2125 O LYS A1077 5164 5042 7989 962 -1166 -334 O ATOM 2126 CB LYS A1077 1.953 -65.511 28.729 1.00 48.29 C ANISOU 2126 CB LYS A1077 5228 5079 8042 878 -1312 -375 C ATOM 2127 CG LYS A1077 2.032 -66.775 29.576 1.00 54.99 C ANISOU 2127 CG LYS A1077 6069 6036 8788 864 -1378 -366 C ATOM 2128 CD LYS A1077 0.711 -67.521 29.617 1.00 60.03 C ANISOU 2128 CD LYS A1077 6783 6691 9336 845 -1480 -332 C ATOM 2129 CE LYS A1077 0.885 -68.903 30.230 1.00 66.12 C ANISOU 2129 CE LYS A1077 7575 7550 9997 845 -1538 -304 C ATOM 2130 NZ LYS A1077 1.531 -69.862 29.291 1.00 67.19 N ANISOU 2130 NZ LYS A1077 7854 7617 10058 906 -1519 -214 N ATOM 2131 N LEU A1078 4.214 -65.872 26.573 1.00 43.01 N ANISOU 2131 N LEU A1078 4747 4222 7375 1014 -1152 -244 N ATOM 2132 CA LEU A1078 5.173 -66.702 25.854 1.00 42.96 C ANISOU 2132 CA LEU A1078 4845 4168 7311 1076 -1114 -168 C ATOM 2133 C LEU A1078 6.592 -66.177 26.034 1.00 44.41 C ANISOU 2133 C LEU A1078 4937 4361 7575 1092 -1019 -198 C ATOM 2134 O LEU A1078 7.527 -66.956 26.252 1.00 44.58 O ANISOU 2134 O LEU A1078 4962 4425 7552 1116 -1001 -174 O ATOM 2135 CB LEU A1078 4.802 -66.759 24.372 1.00 34.67 C ANISOU 2135 CB LEU A1078 3961 2977 6233 1128 -1101 -85 C ATOM 2136 CG LEU A1078 3.476 -67.453 24.056 1.00 41.07 C ANISOU 2136 CG LEU A1078 4884 3770 6950 1120 -1197 -41 C ATOM 2137 CD1 LEU A1078 3.053 -67.192 22.617 1.00 38.58 C ANISOU 2137 CD1 LEU A1078 4712 3316 6632 1164 -1178 26 C ATOM 2138 CD2 LEU A1078 3.589 -68.946 24.321 1.00 41.87 C ANISOU 2138 CD2 LEU A1078 5056 3926 6927 1131 -1255 7 C ATOM 2139 N ALA A1079 6.769 -64.856 25.956 1.00 40.83 N ANISOU 2139 N ALA A1079 4400 3871 7242 1079 -955 -251 N ATOM 2140 CA ALA A1079 8.094 -64.276 26.146 1.00 42.25 C ANISOU 2140 CA ALA A1079 4485 4060 7507 1090 -864 -284 C ATOM 2141 C ALA A1079 8.624 -64.558 27.546 1.00 46.54 C ANISOU 2141 C ALA A1079 4888 4748 8048 1046 -883 -349 C ATOM 2142 O ALA A1079 9.795 -64.916 27.714 1.00 50.35 O ANISOU 2142 O ALA A1079 5342 5261 8528 1070 -837 -338 O ATOM 2143 CB ALA A1079 8.046 -62.771 25.883 1.00 45.27 C ANISOU 2143 CB ALA A1079 4799 4382 8022 1076 -800 -336 C ATOM 2144 N ASN A1080 7.777 -64.398 28.566 1.00 49.20 N ANISOU 2144 N ASN A1080 5135 5175 8384 984 -949 -416 N ATOM 2145 CA ASN A1080 8.198 -64.683 29.933 1.00 48.02 C ANISOU 2145 CA ASN A1080 4851 5167 8226 942 -974 -479 C ATOM 2146 C ASN A1080 8.569 -66.147 30.125 1.00 48.96 C ANISOU 2146 C ASN A1080 5034 5343 8227 967 -1014 -421 C ATOM 2147 O ASN A1080 9.337 -66.465 31.039 1.00 50.03 O ANISOU 2147 O ASN A1080 5072 5580 8356 952 -1009 -454 O ATOM 2148 CB ASN A1080 7.093 -64.292 30.916 1.00 47.95 C ANISOU 2148 CB ASN A1080 4751 5238 8231 874 -1043 -555 C ATOM 2149 CG ASN A1080 7.015 -62.794 31.139 1.00 52.09 C ANISOU 2149 CG ASN A1080 5161 5745 8885 838 -994 -638 C ATOM 2150 OD1 ASN A1080 8.037 -62.112 31.203 1.00 54.84 O ANISOU 2150 OD1 ASN A1080 5431 6087 9318 841 -915 -673 O ATOM 2151 ND2 ASN A1080 5.799 -62.274 31.259 1.00 51.07 N ANISOU 2151 ND2 ASN A1080 5022 5607 8775 803 -1039 -669 N ATOM 2152 N GLU A1081 8.042 -67.042 29.293 1.00 51.01 N ANISOU 2152 N GLU A1081 5452 5538 8391 1005 -1054 -335 N ATOM 2153 CA GLU A1081 8.401 -68.452 29.326 1.00 53.19 C ANISOU 2153 CA GLU A1081 5806 5851 8553 1036 -1087 -271 C ATOM 2154 C GLU A1081 9.650 -68.758 28.506 1.00 55.19 C ANISOU 2154 C GLU A1081 6129 6038 8804 1102 -1007 -206 C ATOM 2155 O GLU A1081 9.998 -69.932 28.344 1.00 52.56 O ANISOU 2155 O GLU A1081 5880 5715 8375 1138 -1024 -142 O ATOM 2156 CB GLU A1081 7.233 -69.306 28.822 1.00 51.99 C ANISOU 2156 CB GLU A1081 5795 5660 8297 1045 -1169 -209 C ATOM 2157 CG GLU A1081 6.049 -69.365 29.776 1.00 58.46 C ANISOU 2157 CG GLU A1081 6552 6568 9092 982 -1261 -260 C ATOM 2158 CD GLU A1081 4.903 -70.197 29.231 1.00 69.07 C ANISOU 2158 CD GLU A1081 8037 7870 10337 990 -1341 -196 C ATOM 2159 OE1 GLU A1081 4.732 -70.239 27.994 1.00 67.45 O ANISOU 2159 OE1 GLU A1081 7968 7545 10115 1034 -1324 -129 O ATOM 2160 OE2 GLU A1081 4.176 -70.812 30.039 1.00 72.90 O ANISOU 2160 OE2 GLU A1081 8496 8442 10760 953 -1423 -211 O ATOM 2161 N GLY A1082 10.328 -67.734 27.987 1.00 52.62 N ANISOU 2161 N GLY A1082 5770 5643 8580 1120 -919 -222 N ATOM 2162 CA GLY A1082 11.523 -67.949 27.198 1.00 51.13 C ANISOU 2162 CA GLY A1082 5643 5389 8396 1183 -839 -161 C ATOM 2163 C GLY A1082 11.288 -68.466 25.799 1.00 47.90 C ANISOU 2163 C GLY A1082 5423 4853 7926 1246 -832 -62 C ATOM 2164 O GLY A1082 12.253 -68.823 25.117 1.00 49.91 O ANISOU 2164 O GLY A1082 5744 5053 8166 1305 -771 -2 O ATOM 2165 N LYS A1083 10.035 -68.515 25.341 1.00 44.02 N ANISOU 2165 N LYS A1083 5020 4310 7395 1237 -893 -43 N ATOM 2166 CA LYS A1083 9.712 -69.021 24.007 1.00 43.83 C ANISOU 2166 CA LYS A1083 5181 4165 7306 1294 -895 49 C ATOM 2167 C LYS A1083 9.719 -67.846 23.032 1.00 40.62 C ANISOU 2167 C LYS A1083 4798 3641 6994 1316 -826 52 C ATOM 2168 O LYS A1083 8.690 -67.249 22.708 1.00 38.77 O ANISOU 2168 O LYS A1083 4585 3360 6785 1296 -855 38 O ATOM 2169 CB LYS A1083 8.372 -69.746 24.024 1.00 45.23 C ANISOU 2169 CB LYS A1083 5444 4352 7388 1272 -999 72 C ATOM 2170 CG LYS A1083 8.283 -70.841 25.081 1.00 49.35 C ANISOU 2170 CG LYS A1083 5931 4998 7823 1244 -1070 63 C ATOM 2171 CD LYS A1083 6.883 -71.425 25.169 1.00 52.14 C ANISOU 2171 CD LYS A1083 6352 5363 8094 1214 -1175 77 C ATOM 2172 CE LYS A1083 6.792 -72.484 26.257 1.00 53.52 C ANISOU 2172 CE LYS A1083 6486 5663 8188 1185 -1243 66 C ATOM 2173 NZ LYS A1083 5.402 -72.991 26.434 1.00 53.49 N ANISOU 2173 NZ LYS A1083 6534 5679 8112 1151 -1346 74 N ATOM 2174 N VAL A1084 10.920 -67.519 22.549 1.00 42.12 N ANISOU 2174 N VAL A1084 4982 3783 7239 1361 -731 72 N ATOM 2175 CA VAL A1084 11.096 -66.328 21.721 1.00 41.83 C ANISOU 2175 CA VAL A1084 4946 3643 7306 1382 -654 68 C ATOM 2176 C VAL A1084 10.351 -66.472 20.397 1.00 39.57 C ANISOU 2176 C VAL A1084 4841 3272 6921 1398 -646 143 C ATOM 2177 O VAL A1084 9.646 -65.554 19.963 1.00 36.86 O ANISOU 2177 O VAL A1084 4505 2891 6609 1372 -631 125 O ATOM 2178 CB VAL A1084 12.595 -66.042 21.501 1.00 45.56 C ANISOU 2178 CB VAL A1084 5377 4094 7840 1422 -549 80 C ATOM 2179 CG1 VAL A1084 13.310 -67.246 20.887 1.00 46.56 C ANISOU 2179 CG1 VAL A1084 5635 4203 7852 1480 -529 171 C ATOM 2180 CG2 VAL A1084 12.774 -64.809 20.625 1.00 49.87 C ANISOU 2180 CG2 VAL A1084 5939 4569 8440 1419 -455 78 C ATOM 2181 N LYS A1085 10.498 -67.620 19.733 1.00 38.44 N ANISOU 2181 N LYS A1085 4848 3116 6643 1434 -647 226 N ATOM 2182 CA LYS A1085 9.848 -67.803 18.438 1.00 39.89 C ANISOU 2182 CA LYS A1085 5202 3242 6711 1443 -621 296 C ATOM 2183 C LYS A1085 8.331 -67.836 18.580 1.00 37.45 C ANISOU 2183 C LYS A1085 4915 2945 6370 1396 -712 281 C ATOM 2184 O LYS A1085 7.612 -67.289 17.734 1.00 37.60 O ANISOU 2184 O LYS A1085 5002 2920 6365 1384 -686 299 O ATOM 2185 CB LYS A1085 10.356 -69.082 17.773 1.00 40.04 C ANISOU 2185 CB LYS A1085 5363 3255 6596 1486 -594 383 C ATOM 2186 CG LYS A1085 11.791 -68.993 17.268 1.00 43.72 C ANISOU 2186 CG LYS A1085 5848 3694 7070 1540 -488 414 C ATOM 2187 CD LYS A1085 11.900 -68.109 16.033 1.00 41.95 C ANISOU 2187 CD LYS A1085 5704 3402 6833 1559 -396 436 C ATOM 2188 CE LYS A1085 13.297 -68.172 15.432 1.00 52.24 C ANISOU 2188 CE LYS A1085 7058 4680 8109 1618 -312 467 C ATOM 2189 NZ LYS A1085 13.399 -67.413 14.155 1.00 66.75 N ANISOU 2189 NZ LYS A1085 9001 6458 9904 1641 -255 478 N ATOM 2190 N GLU A1086 7.824 -68.468 19.642 1.00 39.29 N ANISOU 2190 N GLU A1086 5089 3241 6598 1371 -819 248 N ATOM 2191 CA GLU A1086 6.382 -68.489 19.862 1.00 45.61 C ANISOU 2191 CA GLU A1086 5902 4058 7370 1325 -911 230 C ATOM 2192 C GLU A1086 5.849 -67.087 20.128 1.00 39.19 C ANISOU 2192 C GLU A1086 4980 3230 6682 1291 -907 160 C ATOM 2193 O GLU A1086 4.734 -66.749 19.714 1.00 39.15 O ANISOU 2193 O GLU A1086 5021 3203 6652 1262 -934 165 O ATOM 2194 CB GLU A1086 6.037 -69.423 21.023 1.00 46.97 C ANISOU 2194 CB GLU A1086 6023 4310 7512 1308 -1025 206 C ATOM 2195 CG GLU A1086 5.891 -70.885 20.622 1.00 57.45 C ANISOU 2195 CG GLU A1086 7494 5654 8680 1319 -1054 282 C ATOM 2196 CD GLU A1086 5.485 -71.779 21.780 1.00 61.24 C ANISOU 2196 CD GLU A1086 7926 6219 9122 1299 -1168 259 C ATOM 2197 OE1 GLU A1086 4.724 -71.317 22.655 1.00 63.26 O ANISOU 2197 OE1 GLU A1086 8076 6523 9435 1257 -1239 195 O ATOM 2198 OE2 GLU A1086 5.932 -72.947 21.815 1.00 61.47 O ANISOU 2198 OE2 GLU A1086 8020 6278 9056 1319 -1176 306 O ATOM 2199 N ALA A1087 6.635 -66.254 20.814 1.00 37.97 N ANISOU 2199 N ALA A1087 4675 3089 6661 1290 -867 93 N ATOM 2200 CA ALA A1087 6.192 -64.896 21.110 1.00 39.70 C ANISOU 2200 CA ALA A1087 4783 3299 7004 1254 -852 21 C ATOM 2201 C ALA A1087 6.169 -64.037 19.852 1.00 38.97 C ANISOU 2201 C ALA A1087 4772 3129 6906 1263 -759 57 C ATOM 2202 O ALA A1087 5.225 -63.268 19.637 1.00 37.00 O ANISOU 2202 O ALA A1087 4517 2857 6683 1232 -770 37 O ATOM 2203 CB ALA A1087 7.099 -64.271 22.170 1.00 40.18 C ANISOU 2203 CB ALA A1087 4662 3420 7186 1238 -816 -63 C ATOM 2204 N GLN A1088 7.197 -64.154 19.009 1.00 39.10 N ANISOU 2204 N GLN A1088 4864 3108 6886 1306 -667 111 N ATOM 2205 CA GLN A1088 7.230 -63.374 17.776 1.00 37.69 C ANISOU 2205 CA GLN A1088 4769 2863 6688 1320 -579 147 C ATOM 2206 C GLN A1088 6.061 -63.733 16.868 1.00 40.33 C ANISOU 2206 C GLN A1088 5247 3171 6907 1316 -608 205 C ATOM 2207 O GLN A1088 5.404 -62.846 16.310 1.00 39.67 O ANISOU 2207 O GLN A1088 5178 3054 6840 1300 -584 200 O ATOM 2208 CB GLN A1088 8.562 -63.594 17.056 1.00 38.56 C ANISOU 2208 CB GLN A1088 4944 2946 6762 1373 -484 197 C ATOM 2209 CG GLN A1088 9.752 -62.961 17.763 1.00 39.56 C ANISOU 2209 CG GLN A1088 4924 3092 7015 1374 -431 141 C ATOM 2210 CD GLN A1088 11.083 -63.364 17.153 1.00 47.26 C ANISOU 2210 CD GLN A1088 5964 4049 7945 1428 -353 193 C ATOM 2211 OE1 GLN A1088 11.330 -64.542 16.893 1.00 39.47 O ANISOU 2211 OE1 GLN A1088 5078 3068 6851 1463 -369 252 O ATOM 2212 NE2 GLN A1088 11.949 -62.382 16.922 1.00 45.01 N ANISOU 2212 NE2 GLN A1088 5621 3743 7739 1433 -268 171 N ATOM 2213 N ALA A1089 5.782 -65.029 16.709 1.00 35.67 N ANISOU 2213 N ALA A1089 4756 2599 6196 1327 -656 259 N ATOM 2214 CA ALA A1089 4.648 -65.443 15.887 1.00 37.74 C ANISOU 2214 CA ALA A1089 5142 2847 6352 1315 -681 312 C ATOM 2215 C ALA A1089 3.341 -64.889 16.437 1.00 37.57 C ANISOU 2215 C ALA A1089 5055 2842 6378 1263 -764 262 C ATOM 2216 O ALA A1089 2.484 -64.425 15.675 1.00 41.45 O ANISOU 2216 O ALA A1089 5603 3304 6841 1250 -751 282 O ATOM 2217 CB ALA A1089 4.590 -66.968 15.803 1.00 34.22 C ANISOU 2217 CB ALA A1089 4789 2431 5782 1323 -722 369 C ATOM 2218 N ALA A1090 3.168 -64.928 17.760 1.00 35.27 N ANISOU 2218 N ALA A1090 4641 2601 6159 1234 -848 195 N ATOM 2219 CA ALA A1090 1.959 -64.376 18.362 1.00 37.04 C ANISOU 2219 CA ALA A1090 4793 2844 6437 1186 -926 144 C ATOM 2220 C ALA A1090 1.881 -62.869 18.155 1.00 39.61 C ANISOU 2220 C ALA A1090 5046 3131 6872 1173 -862 101 C ATOM 2221 O ALA A1090 0.797 -62.326 17.907 1.00 39.74 O ANISOU 2221 O ALA A1090 5073 3134 6893 1146 -887 96 O ATOM 2222 CB ALA A1090 1.915 -64.714 19.852 1.00 38.32 C ANISOU 2222 CB ALA A1090 4827 3074 6657 1163 -1019 78 C ATOM 2223 N ALA A1091 3.019 -62.178 18.253 1.00 39.08 N ANISOU 2223 N ALA A1091 4904 3050 6894 1191 -779 71 N ATOM 2224 CA ALA A1091 3.025 -60.735 18.043 1.00 38.07 C ANISOU 2224 CA ALA A1091 4708 2889 6868 1177 -711 32 C ATOM 2225 C ALA A1091 2.644 -60.377 16.614 1.00 43.30 C ANISOU 2225 C ALA A1091 5503 3494 7454 1195 -651 97 C ATOM 2226 O ALA A1091 2.062 -59.312 16.375 1.00 43.32 O ANISOU 2226 O ALA A1091 5475 3473 7510 1174 -629 74 O ATOM 2227 CB ALA A1091 4.401 -60.162 18.382 1.00 39.78 C ANISOU 2227 CB ALA A1091 4825 3107 7183 1191 -630 -8 C ATOM 2228 N GLU A1092 2.961 -61.248 15.653 1.00 44.16 N ANISOU 2228 N GLU A1092 5758 3584 7438 1236 -621 176 N ATOM 2229 CA GLU A1092 2.641 -60.957 14.260 1.00 48.59 C ANISOU 2229 CA GLU A1092 6447 4095 7919 1259 -557 237 C ATOM 2230 C GLU A1092 1.136 -60.894 14.036 1.00 47.64 C ANISOU 2230 C GLU A1092 6361 3976 7762 1226 -617 247 C ATOM 2231 O GLU A1092 0.676 -60.224 13.104 1.00 50.54 O ANISOU 2231 O GLU A1092 6787 4308 8108 1233 -570 272 O ATOM 2232 CB GLU A1092 3.271 -62.010 13.348 1.00 55.81 C ANISOU 2232 CB GLU A1092 7502 4996 8706 1307 -510 317 C ATOM 2233 CG GLU A1092 3.506 -61.535 11.922 1.00 66.73 C ANISOU 2233 CG GLU A1092 8999 6328 10029 1348 -410 368 C ATOM 2234 CD GLU A1092 4.581 -60.467 11.831 1.00 66.73 C ANISOU 2234 CD GLU A1092 8947 6301 10106 1369 -341 332 C ATOM 2235 OE1 GLU A1092 5.310 -60.267 12.826 1.00 67.63 O ANISOU 2235 OE1 GLU A1092 8937 6439 10320 1355 -351 279 O ATOM 2236 OE2 GLU A1092 4.697 -59.827 10.765 1.00 66.78 O ANISOU 2236 OE2 GLU A1092 9032 6267 10075 1397 -279 355 O ATOM 2237 N GLN A1093 0.354 -61.576 14.877 1.00 42.89 N ANISOU 2237 N GLN A1093 5727 3420 7150 1191 -724 228 N ATOM 2238 CA GLN A1093 -1.098 -61.507 14.758 1.00 45.19 C ANISOU 2238 CA GLN A1093 6042 3717 7411 1156 -790 234 C ATOM 2239 C GLN A1093 -1.626 -60.109 15.042 1.00 45.21 C ANISOU 2239 C GLN A1093 5946 3705 7528 1129 -782 177 C ATOM 2240 O GLN A1093 -2.754 -59.790 14.649 1.00 47.96 O ANISOU 2240 O GLN A1093 6325 4045 7855 1109 -808 190 O ATOM 2241 CB GLN A1093 -1.755 -62.510 15.708 1.00 41.36 C ANISOU 2241 CB GLN A1093 5534 3287 6893 1125 -912 218 C ATOM 2242 CG GLN A1093 -1.191 -63.919 15.613 1.00 50.44 C ANISOU 2242 CG GLN A1093 6765 4460 7938 1147 -925 266 C ATOM 2243 CD GLN A1093 -1.212 -64.462 14.199 1.00 51.57 C ANISOU 2243 CD GLN A1093 7056 4575 7963 1173 -860 350 C ATOM 2244 OE1 GLN A1093 -2.243 -64.437 13.527 1.00 49.94 O ANISOU 2244 OE1 GLN A1093 6909 4360 7705 1156 -873 380 O ATOM 2245 NE2 GLN A1093 -0.067 -64.951 13.737 1.00 51.40 N ANISOU 2245 NE2 GLN A1093 7084 4539 7906 1215 -785 388 N ATOM 2246 N LEU A1094 -0.838 -59.269 15.718 1.00 43.19 N ANISOU 2246 N LEU A1094 5566 3449 7396 1125 -744 114 N ATOM 2247 CA LEU A1094 -1.271 -57.901 15.984 1.00 40.78 C ANISOU 2247 CA LEU A1094 5159 3131 7204 1096 -724 58 C ATOM 2248 C LEU A1094 -1.491 -57.123 14.695 1.00 45.69 C ANISOU 2248 C LEU A1094 5867 3702 7792 1116 -645 102 C ATOM 2249 O LEU A1094 -2.318 -56.205 14.658 1.00 43.67 O ANISOU 2249 O LEU A1094 5571 3433 7586 1091 -648 80 O ATOM 2250 CB LEU A1094 -0.239 -57.192 16.861 1.00 35.13 C ANISOU 2250 CB LEU A1094 4298 2428 6622 1088 -680 -17 C ATOM 2251 CG LEU A1094 -0.050 -57.778 18.262 1.00 41.58 C ANISOU 2251 CG LEU A1094 5004 3304 7492 1067 -756 -77 C ATOM 2252 CD1 LEU A1094 1.249 -57.282 18.874 1.00 40.44 C ANISOU 2252 CD1 LEU A1094 4742 3171 7452 1071 -691 -133 C ATOM 2253 CD2 LEU A1094 -1.229 -57.423 19.154 1.00 39.98 C ANISOU 2253 CD2 LEU A1094 4709 3132 7349 1020 -839 -136 C ATOM 2254 N LYS A1095 -0.763 -57.470 13.630 1.00 48.63 N ANISOU 2254 N LYS A1095 6357 4044 8077 1163 -574 164 N ATOM 2255 CA LYS A1095 -0.938 -56.775 12.359 1.00 54.20 C ANISOU 2255 CA LYS A1095 7151 4702 8739 1188 -501 207 C ATOM 2256 C LYS A1095 -2.359 -56.938 11.835 1.00 53.95 C ANISOU 2256 C LYS A1095 7191 4669 8639 1173 -547 243 C ATOM 2257 O LYS A1095 -2.934 -55.998 11.274 1.00 54.47 O ANISOU 2257 O LYS A1095 7265 4708 8723 1170 -516 246 O ATOM 2258 CB LYS A1095 0.074 -57.292 11.337 1.00 54.62 C ANISOU 2258 CB LYS A1095 7327 4729 8696 1245 -426 267 C ATOM 2259 CG LYS A1095 1.499 -56.842 11.606 1.00 59.03 C ANISOU 2259 CG LYS A1095 7822 5281 9326 1263 -366 234 C ATOM 2260 CD LYS A1095 2.465 -57.413 10.582 1.00 64.97 C ANISOU 2260 CD LYS A1095 8706 6009 9972 1323 -303 293 C ATOM 2261 CE LYS A1095 3.843 -56.784 10.710 1.00 72.84 C ANISOU 2261 CE LYS A1095 9637 6995 11043 1339 -243 261 C ATOM 2262 NZ LYS A1095 4.805 -57.340 9.720 1.00 82.02 N ANISOU 2262 NZ LYS A1095 10931 8134 12099 1398 -198 312 N ATOM 2263 N THR A1096 -2.944 -58.124 12.009 1.00 50.71 N ANISOU 2263 N THR A1096 6828 4289 8151 1161 -621 272 N ATOM 2264 CA THR A1096 -4.328 -58.325 11.594 1.00 53.95 C ANISOU 2264 CA THR A1096 7293 4705 8502 1140 -672 304 C ATOM 2265 C THR A1096 -5.265 -57.405 12.366 1.00 50.77 C ANISOU 2265 C THR A1096 6781 4312 8198 1095 -729 245 C ATOM 2266 O THR A1096 -6.163 -56.787 11.782 1.00 50.44 O ANISOU 2266 O THR A1096 6764 4251 8149 1088 -721 261 O ATOM 2267 CB THR A1096 -4.727 -59.788 11.788 1.00 55.74 C ANISOU 2267 CB THR A1096 7574 4970 8634 1127 -751 336 C ATOM 2268 OG1 THR A1096 -3.864 -60.627 11.012 1.00 59.13 O ANISOU 2268 OG1 THR A1096 8099 5389 8978 1167 -687 394 O ATOM 2269 CG2 THR A1096 -6.171 -60.012 11.358 1.00 59.50 C ANISOU 2269 CG2 THR A1096 8101 5457 9049 1100 -809 367 C ATOM 2270 N THR A1097 -5.070 -57.300 13.682 1.00 48.25 N ANISOU 2270 N THR A1097 6334 4024 7974 1066 -782 176 N ATOM 2271 CA THR A1097 -5.875 -56.375 14.473 1.00 47.94 C ANISOU 2271 CA THR A1097 6178 3996 8041 1024 -824 115 C ATOM 2272 C THR A1097 -5.600 -54.932 14.072 1.00 49.24 C ANISOU 2272 C THR A1097 6296 4121 8290 1031 -732 92 C ATOM 2273 O THR A1097 -6.512 -54.098 14.061 1.00 46.01 O ANISOU 2273 O THR A1097 5851 3705 7928 1008 -741 76 O ATOM 2274 CB THR A1097 -5.592 -56.575 15.962 1.00 45.06 C ANISOU 2274 CB THR A1097 5682 3676 7764 996 -888 41 C ATOM 2275 OG1 THR A1097 -5.658 -57.970 16.282 1.00 47.24 O ANISOU 2275 OG1 THR A1097 6010 3989 7952 996 -967 66 O ATOM 2276 CG2 THR A1097 -6.606 -55.812 16.806 1.00 44.06 C ANISOU 2276 CG2 THR A1097 5441 3567 7732 952 -943 -20 C ATOM 2277 N ARG A1098 -4.345 -54.622 13.741 1.00 51.58 N ANISOU 2277 N ARG A1098 6595 4395 8607 1061 -643 92 N ATOM 2278 CA ARG A1098 -3.996 -53.266 13.332 1.00 52.41 C ANISOU 2278 CA ARG A1098 6661 4466 8787 1067 -555 72 C ATOM 2279 C ARG A1098 -4.715 -52.876 12.047 1.00 53.16 C ANISOU 2279 C ARG A1098 6868 4525 8807 1088 -522 131 C ATOM 2280 O ARG A1098 -5.221 -51.754 11.924 1.00 52.88 O ANISOU 2280 O ARG A1098 6786 4472 8834 1073 -497 111 O ATOM 2281 CB ARG A1098 -2.481 -53.159 13.155 1.00 52.66 C ANISOU 2281 CB ARG A1098 6687 4484 8837 1098 -474 69 C ATOM 2282 CG ARG A1098 -1.976 -51.778 12.763 1.00 56.60 C ANISOU 2282 CG ARG A1098 7141 4952 9414 1101 -384 46 C ATOM 2283 CD ARG A1098 -0.511 -51.833 12.361 1.00 59.32 C ANISOU 2283 CD ARG A1098 7511 5281 9749 1138 -309 60 C ATOM 2284 NE ARG A1098 -0.305 -52.678 11.191 1.00 59.48 N ANISOU 2284 NE ARG A1098 7700 5279 9622 1190 -295 139 N ATOM 2285 CZ ARG A1098 0.882 -53.036 10.720 1.00 63.68 C ANISOU 2285 CZ ARG A1098 8287 5798 10109 1230 -246 164 C ATOM 2286 NH1 ARG A1098 2.004 -52.639 11.299 1.00 60.86 N ANISOU 2286 NH1 ARG A1098 7829 5449 9846 1224 -204 121 N ATOM 2287 NH2 ARG A1098 0.945 -53.813 9.643 1.00 65.49 N ANISOU 2287 NH2 ARG A1098 8677 6009 10199 1277 -237 232 N ATOM 2288 N ASN A1099 -4.774 -53.791 11.077 1.00 51.81 N ANISOU 2288 N ASN A1099 6842 4343 8501 1123 -517 204 N ATOM 2289 CA ASN A1099 -5.374 -53.464 9.789 1.00 54.93 C ANISOU 2289 CA ASN A1099 7348 4704 8818 1149 -477 260 C ATOM 2290 C ASN A1099 -6.891 -53.360 9.879 1.00 55.35 C ANISOU 2290 C ASN A1099 7392 4770 8868 1115 -544 265 C ATOM 2291 O ASN A1099 -7.501 -52.589 9.130 1.00 59.61 O ANISOU 2291 O ASN A1099 7965 5283 9400 1123 -512 285 O ATOM 2292 CB ASN A1099 -4.983 -54.513 8.748 1.00 51.75 C ANISOU 2292 CB ASN A1099 7095 4290 8276 1195 -443 334 C ATOM 2293 CG ASN A1099 -3.481 -54.630 8.573 1.00 60.09 C ANISOU 2293 CG ASN A1099 8173 5333 9325 1233 -378 334 C ATOM 2294 OD1 ASN A1099 -2.730 -53.720 8.924 1.00 62.12 O ANISOU 2294 OD1 ASN A1099 8347 5579 9675 1231 -343 286 O ATOM 2295 ND2 ASN A1099 -3.035 -55.754 8.023 1.00 61.91 N ANISOU 2295 ND2 ASN A1099 8508 5564 9450 1266 -358 388 N ATOM 2296 N ALA A1100 -7.515 -54.114 10.785 1.00 47.69 N ANISOU 2296 N ALA A1100 6377 3840 7902 1079 -641 247 N ATOM 2297 CA ALA A1100 -8.968 -54.196 10.839 1.00 48.67 C ANISOU 2297 CA ALA A1100 6506 3981 8007 1048 -716 259 C ATOM 2298 C ALA A1100 -9.600 -53.290 11.887 1.00 52.21 C ANISOU 2298 C ALA A1100 6815 4442 8579 1004 -761 190 C ATOM 2299 O ALA A1100 -10.809 -53.047 11.814 1.00 53.73 O ANISOU 2299 O ALA A1100 7008 4639 8768 983 -806 199 O ATOM 2300 CB ALA A1100 -9.404 -55.640 11.110 1.00 47.99 C ANISOU 2300 CB ALA A1100 6468 3934 7833 1033 -805 285 C ATOM 2301 N TYR A1101 -8.829 -52.786 12.851 1.00 50.49 N ANISOU 2301 N TYR A1101 6477 4233 8473 990 -745 122 N ATOM 2302 CA TYR A1101 -9.408 -51.999 13.935 1.00 52.99 C ANISOU 2302 CA TYR A1101 6655 4569 8912 947 -785 52 C ATOM 2303 C TYR A1101 -8.583 -50.760 14.259 1.00 47.32 C ANISOU 2303 C TYR A1101 5829 3834 8318 943 -700 -7 C ATOM 2304 O TYR A1101 -9.088 -49.636 14.182 1.00 48.65 O ANISOU 2304 O TYR A1101 5947 3985 8554 929 -668 -28 O ATOM 2305 CB TYR A1101 -9.556 -52.860 15.192 1.00 50.42 C ANISOU 2305 CB TYR A1101 6260 4293 8605 917 -885 10 C ATOM 2306 CG TYR A1101 -10.507 -54.024 15.031 1.00 54.15 C ANISOU 2306 CG TYR A1101 6821 4789 8963 909 -981 60 C ATOM 2307 CD1 TYR A1101 -11.878 -53.845 15.153 1.00 55.44 C ANISOU 2307 CD1 TYR A1101 6975 4964 9126 880 -1048 63 C ATOM 2308 CD2 TYR A1101 -10.034 -55.302 14.761 1.00 53.40 C ANISOU 2308 CD2 TYR A1101 6819 4709 8762 929 -1003 103 C ATOM 2309 CE1 TYR A1101 -12.753 -54.905 15.008 1.00 60.54 C ANISOU 2309 CE1 TYR A1101 7700 5637 9667 869 -1137 108 C ATOM 2310 CE2 TYR A1101 -10.901 -56.368 14.615 1.00 53.76 C ANISOU 2310 CE2 TYR A1101 6943 4780 8702 916 -1089 147 C ATOM 2311 CZ TYR A1101 -12.259 -56.164 14.740 1.00 56.67 C ANISOU 2311 CZ TYR A1101 7299 5161 9071 885 -1157 148 C ATOM 2312 OH TYR A1101 -13.127 -57.222 14.595 1.00 68.90 O ANISOU 2312 OH TYR A1101 8924 6741 10513 869 -1242 190 O ATOM 2313 N ILE A1102 -7.314 -50.955 14.624 1.00 48.82 N ANISOU 2313 N ILE A1102 5982 4029 8537 954 -662 -34 N ATOM 2314 CA ILE A1102 -6.522 -49.859 15.175 1.00 47.62 C ANISOU 2314 CA ILE A1102 5705 3872 8514 940 -592 -102 C ATOM 2315 C ILE A1102 -6.369 -48.736 14.157 1.00 46.41 C ANISOU 2315 C ILE A1102 5588 3675 8372 959 -498 -77 C ATOM 2316 O ILE A1102 -6.503 -47.553 14.494 1.00 49.54 O ANISOU 2316 O ILE A1102 5885 4064 8873 933 -459 -126 O ATOM 2317 CB ILE A1102 -5.152 -50.376 15.652 1.00 46.49 C ANISOU 2317 CB ILE A1102 5529 3746 8389 952 -568 -126 C ATOM 2318 CG1 ILE A1102 -5.324 -51.581 16.586 1.00 47.66 C ANISOU 2318 CG1 ILE A1102 5656 3940 8512 938 -668 -144 C ATOM 2319 CG2 ILE A1102 -4.380 -49.266 16.350 1.00 46.55 C ANISOU 2319 CG2 ILE A1102 5394 3756 8536 928 -502 -204 C ATOM 2320 CD1 ILE A1102 -6.291 -51.350 17.737 1.00 51.23 C ANISOU 2320 CD1 ILE A1102 5995 4429 9041 892 -746 -210 C ATOM 2321 N GLN A1103 -6.079 -49.080 12.901 1.00 47.38 N ANISOU 2321 N GLN A1103 5850 3767 8385 1004 -459 -3 N ATOM 2322 CA GLN A1103 -5.895 -48.044 11.889 1.00 48.64 C ANISOU 2322 CA GLN A1103 6049 3885 8546 1027 -374 20 C ATOM 2323 C GLN A1103 -7.186 -47.270 11.658 1.00 50.57 C ANISOU 2323 C GLN A1103 6285 4118 8810 1010 -389 25 C ATOM 2324 O GLN A1103 -7.161 -46.047 11.471 1.00 47.68 O ANISOU 2324 O GLN A1103 5867 3731 8516 1003 -330 4 O ATOM 2325 CB GLN A1103 -5.402 -48.662 10.582 1.00 54.35 C ANISOU 2325 CB GLN A1103 6933 4582 9136 1083 -339 96 C ATOM 2326 CG GLN A1103 -4.935 -47.636 9.561 1.00 63.21 C ANISOU 2326 CG GLN A1103 8094 5663 10259 1112 -253 115 C ATOM 2327 CD GLN A1103 -4.720 -48.234 8.186 1.00 78.57 C ANISOU 2327 CD GLN A1103 10211 7582 12059 1168 -232 189 C ATOM 2328 OE1 GLN A1103 -3.818 -49.047 7.983 1.00 80.98 O ANISOU 2328 OE1 GLN A1103 10578 7889 12303 1197 -221 209 O ATOM 2329 NE2 GLN A1103 -5.555 -47.837 7.232 1.00 88.07 N ANISOU 2329 NE2 GLN A1103 11496 8761 13205 1185 -226 227 N ATOM 2330 N LYS A1104 -8.326 -47.964 11.668 1.00 44.34 N ANISOU 2330 N LYS A1104 5544 3345 7958 1001 -469 53 N ATOM 2331 CA LYS A1104 -9.603 -47.281 11.495 1.00 46.39 C ANISOU 2331 CA LYS A1104 5793 3598 8237 983 -490 59 C ATOM 2332 C LYS A1104 -9.896 -46.357 12.670 1.00 47.91 C ANISOU 2332 C LYS A1104 5823 3807 8574 936 -498 -21 C ATOM 2333 O LYS A1104 -10.406 -45.247 12.480 1.00 47.45 O ANISOU 2333 O LYS A1104 5726 3731 8573 926 -462 -32 O ATOM 2334 CB LYS A1104 -10.723 -48.305 11.315 1.00 45.45 C ANISOU 2334 CB LYS A1104 5753 3495 8020 980 -579 106 C ATOM 2335 CG LYS A1104 -10.684 -49.013 9.971 1.00 53.84 C ANISOU 2335 CG LYS A1104 6982 4537 8938 1026 -557 188 C ATOM 2336 CD LYS A1104 -11.638 -50.194 9.922 1.00 60.68 C ANISOU 2336 CD LYS A1104 7917 5430 9710 1016 -645 230 C ATOM 2337 CE LYS A1104 -11.539 -50.932 8.594 1.00 60.87 C ANISOU 2337 CE LYS A1104 8098 5436 9595 1059 -610 308 C ATOM 2338 NZ LYS A1104 -10.176 -51.489 8.359 1.00 61.68 N ANISOU 2338 NZ LYS A1104 8248 5531 9657 1093 -558 318 N ATOM 2339 N TYR A1105 -9.576 -46.791 13.891 1.00 45.52 N ANISOU 2339 N TYR A1105 5424 3540 8330 906 -544 -80 N ATOM 2340 CA TYR A1105 -9.749 -45.922 15.050 1.00 48.74 C ANISOU 2340 CA TYR A1105 5674 3967 8876 862 -545 -165 C ATOM 2341 C TYR A1105 -8.909 -44.657 14.911 1.00 45.79 C ANISOU 2341 C TYR A1105 5236 3570 8593 861 -438 -199 C ATOM 2342 O TYR A1105 -9.389 -43.547 15.163 1.00 43.66 O ANISOU 2342 O TYR A1105 4886 3293 8409 835 -409 -236 O ATOM 2343 CB TYR A1105 -9.385 -46.674 16.330 1.00 49.82 C ANISOU 2343 CB TYR A1105 5726 4149 9052 837 -607 -224 C ATOM 2344 CG TYR A1105 -9.174 -45.770 17.524 1.00 55.31 C ANISOU 2344 CG TYR A1105 6257 4867 9892 795 -586 -323 C ATOM 2345 CD1 TYR A1105 -10.245 -45.354 18.304 1.00 61.69 C ANISOU 2345 CD1 TYR A1105 6981 5696 10764 759 -637 -370 C ATOM 2346 CD2 TYR A1105 -7.903 -45.330 17.870 1.00 58.27 C ANISOU 2346 CD2 TYR A1105 6559 5243 10338 792 -513 -372 C ATOM 2347 CE1 TYR A1105 -10.055 -44.523 19.394 1.00 70.61 C ANISOU 2347 CE1 TYR A1105 7961 6848 12020 720 -613 -465 C ATOM 2348 CE2 TYR A1105 -7.703 -44.500 18.957 1.00 65.44 C ANISOU 2348 CE2 TYR A1105 7317 6174 11374 750 -490 -466 C ATOM 2349 CZ TYR A1105 -8.782 -44.100 19.715 1.00 71.98 C ANISOU 2349 CZ TYR A1105 8065 7023 12259 715 -539 -514 C ATOM 2350 OH TYR A1105 -8.588 -43.274 20.799 1.00 82.37 O ANISOU 2350 OH TYR A1105 9235 8365 13697 673 -514 -612 O ATOM 2351 N LEU A1106 -7.644 -44.811 14.510 1.00 45.99 N ANISOU 2351 N LEU A1106 5293 3582 8597 887 -378 -186 N ATOM 2352 CA LEU A1106 -6.773 -43.652 14.334 1.00 44.32 C ANISOU 2352 CA LEU A1106 5025 3348 8466 885 -278 -214 C ATOM 2353 C LEU A1106 -7.380 -42.646 13.366 1.00 42.29 C ANISOU 2353 C LEU A1106 4813 3055 8202 898 -230 -178 C ATOM 2354 O LEU A1106 -7.344 -41.434 13.612 1.00 42.42 O ANISOU 2354 O LEU A1106 4738 3061 8319 873 -175 -221 O ATOM 2355 CB LEU A1106 -5.398 -44.107 13.839 1.00 48.02 C ANISOU 2355 CB LEU A1106 5549 3806 8890 920 -228 -188 C ATOM 2356 CG LEU A1106 -4.423 -43.022 13.366 1.00 57.70 C ANISOU 2356 CG LEU A1106 6747 5003 10173 927 -124 -197 C ATOM 2357 CD1 LEU A1106 -4.011 -42.117 14.515 1.00 60.27 C ANISOU 2357 CD1 LEU A1106 6906 5348 10648 877 -90 -289 C ATOM 2358 CD2 LEU A1106 -3.200 -43.650 12.711 1.00 57.66 C ANISOU 2358 CD2 LEU A1106 6823 4986 10098 969 -88 -156 C ATOM 2359 N GLU A 219 -7.947 -43.128 12.258 1.00 41.31 N ANISOU 2359 N GLU A 219 6658 3845 5194 1007 101 -655 N ATOM 2360 CA GLU A 219 -8.457 -42.222 11.236 1.00 41.15 C ANISOU 2360 CA GLU A 219 6675 3844 5116 955 120 -668 C ATOM 2361 C GLU A 219 -9.710 -41.492 11.703 1.00 44.27 C ANISOU 2361 C GLU A 219 7048 4264 5508 861 46 -620 C ATOM 2362 O GLU A 219 -9.912 -40.326 11.344 1.00 42.75 O ANISOU 2362 O GLU A 219 6793 4145 5304 817 68 -608 O ATOM 2363 CB GLU A 219 -8.732 -42.998 9.950 1.00 43.54 C ANISOU 2363 CB GLU A 219 7119 4085 5341 928 123 -701 C ATOM 2364 CG GLU A 219 -7.475 -43.586 9.323 1.00 49.53 C ANISOU 2364 CG GLU A 219 7881 4842 6098 1011 203 -744 C ATOM 2365 CD GLU A 219 -7.771 -44.628 8.260 1.00 59.90 C ANISOU 2365 CD GLU A 219 9340 6080 7339 992 190 -772 C ATOM 2366 OE1 GLU A 219 -8.915 -45.126 8.208 1.00 61.97 O ANISOU 2366 OE1 GLU A 219 9698 6284 7562 917 108 -752 O ATOM 2367 OE2 GLU A 219 -6.853 -44.951 7.477 1.00 60.39 O ANISOU 2367 OE2 GLU A 219 9419 6144 7384 1052 259 -811 O ATOM 2368 N ARG A 220 -10.556 -42.146 12.502 1.00 44.71 N ANISOU 2368 N ARG A 220 7129 4283 5576 813 -43 -579 N ATOM 2369 CA ARG A 220 -11.749 -41.471 13.003 1.00 45.15 C ANISOU 2369 CA ARG A 220 7128 4392 5635 711 -114 -519 C ATOM 2370 C ARG A 220 -11.395 -40.474 14.098 1.00 42.55 C ANISOU 2370 C ARG A 220 6631 4161 5376 730 -100 -484 C ATOM 2371 O ARG A 220 -12.012 -39.407 14.196 1.00 36.14 O ANISOU 2371 O ARG A 220 5747 3423 4564 667 -116 -450 O ATOM 2372 CB ARG A 220 -12.765 -42.493 13.514 1.00 49.89 C ANISOU 2372 CB ARG A 220 7805 4925 6226 652 -212 -483 C ATOM 2373 CG ARG A 220 -13.181 -43.544 12.488 1.00 63.35 C ANISOU 2373 CG ARG A 220 9686 6524 7861 627 -238 -516 C ATOM 2374 CD ARG A 220 -13.512 -42.939 11.128 1.00 72.43 C ANISOU 2374 CD ARG A 220 10894 7685 8942 580 -210 -542 C ATOM 2375 NE ARG A 220 -13.884 -43.958 10.154 1.00 93.07 N ANISOU 2375 NE ARG A 220 13678 10198 11486 556 -237 -573 N ATOM 2376 CZ ARG A 220 -13.021 -44.751 9.533 1.00 79.92 C ANISOU 2376 CZ ARG A 220 12062 8502 9803 621 -182 -616 C ATOM 2377 NH1 ARG A 220 -11.723 -44.693 9.784 1.00 68.27 N ANISOU 2377 NH1 ARG A 220 10511 7056 8372 724 -102 -644 N ATOM 2378 NH2 ARG A 220 -13.471 -45.628 8.641 1.00 86.55 N ANISOU 2378 NH2 ARG A 220 13024 9283 10579 580 -210 -629 N ATOM 2379 N ALA A 221 -10.407 -40.801 14.933 1.00 40.12 N ANISOU 2379 N ALA A 221 6261 3855 5128 816 -73 -491 N ATOM 2380 CA ALA A 221 -9.937 -39.834 15.919 1.00 38.62 C ANISOU 2380 CA ALA A 221 5914 3758 5003 840 -55 -463 C ATOM 2381 C ALA A 221 -9.332 -38.617 15.234 1.00 37.90 C ANISOU 2381 C ALA A 221 5755 3738 4906 853 22 -486 C ATOM 2382 O ALA A 221 -9.558 -37.477 15.656 1.00 38.44 O ANISOU 2382 O ALA A 221 5721 3889 4998 818 18 -454 O ATOM 2383 CB ALA A 221 -8.918 -40.487 16.852 1.00 47.19 C ANISOU 2383 CB ALA A 221 6954 4826 6151 935 -39 -470 C ATOM 2384 N ARG A 222 -8.563 -38.841 14.167 1.00 37.18 N ANISOU 2384 N ARG A 222 5726 3616 4784 905 94 -540 N ATOM 2385 CA ARG A 222 -7.986 -37.733 13.415 1.00 40.40 C ANISOU 2385 CA ARG A 222 6080 4088 5181 914 170 -561 C ATOM 2386 C ARG A 222 -9.069 -36.933 12.703 1.00 41.67 C ANISOU 2386 C ARG A 222 6270 4276 5287 814 143 -543 C ATOM 2387 O ARG A 222 -9.038 -35.696 12.703 1.00 37.52 O ANISOU 2387 O ARG A 222 5654 3828 4772 788 165 -527 O ATOM 2388 CB ARG A 222 -6.967 -38.272 12.414 1.00 43.10 C ANISOU 2388 CB ARG A 222 6492 4387 5495 992 252 -623 C ATOM 2389 CG ARG A 222 -6.202 -37.215 11.639 1.00 50.91 C ANISOU 2389 CG ARG A 222 7425 5444 6476 1012 341 -646 C ATOM 2390 CD ARG A 222 -5.190 -37.874 10.717 1.00 63.80 C ANISOU 2390 CD ARG A 222 9118 7039 8083 1090 420 -701 C ATOM 2391 NE ARG A 222 -4.203 -38.645 11.467 1.00 74.35 N ANISOU 2391 NE ARG A 222 10387 8379 9482 1158 431 -701 N ATOM 2392 CZ ARG A 222 -3.521 -39.675 10.983 1.00 75.02 C ANISOU 2392 CZ ARG A 222 10520 8428 9558 1204 461 -732 C ATOM 2393 NH1 ARG A 222 -3.710 -40.114 9.749 1.00 69.74 N ANISOU 2393 NH1 ARG A 222 9967 7714 8817 1191 482 -765 N ATOM 2394 NH2 ARG A 222 -2.631 -40.285 11.761 1.00 70.66 N ANISOU 2394 NH2 ARG A 222 9896 7883 9068 1263 467 -728 N ATOM 2395 N SER A 223 -10.036 -37.622 12.094 1.00 38.91 N ANISOU 2395 N SER A 223 6046 3859 4877 757 92 -545 N ATOM 2396 CA SER A 223 -11.137 -36.928 11.437 1.00 38.25 C ANISOU 2396 CA SER A 223 5992 3798 4741 660 57 -524 C ATOM 2397 C SER A 223 -11.910 -36.063 12.424 1.00 38.95 C ANISOU 2397 C SER A 223 5973 3960 4867 601 1 -463 C ATOM 2398 O SER A 223 -12.270 -34.922 12.113 1.00 38.89 O ANISOU 2398 O SER A 223 5917 4014 4844 554 8 -447 O ATOM 2399 CB SER A 223 -12.066 -37.943 10.772 1.00 40.78 C ANISOU 2399 CB SER A 223 6465 4031 4998 607 0 -530 C ATOM 2400 OG SER A 223 -13.156 -37.301 10.135 1.00 53.18 O ANISOU 2400 OG SER A 223 8064 5625 6517 512 -38 -508 O ATOM 2401 N THR A 224 -12.170 -36.586 13.624 1.00 34.90 N ANISOU 2401 N THR A 224 5423 3438 4398 604 -55 -429 N ATOM 2402 CA THR A 224 -12.919 -35.822 14.616 1.00 35.49 C ANISOU 2402 CA THR A 224 5398 3581 4506 553 -109 -371 C ATOM 2403 C THR A 224 -12.141 -34.593 15.069 1.00 35.37 C ANISOU 2403 C THR A 224 5248 3652 4537 590 -57 -368 C ATOM 2404 O THR A 224 -12.719 -33.512 15.235 1.00 34.05 O ANISOU 2404 O THR A 224 5016 3551 4371 540 -75 -336 O ATOM 2405 CB THR A 224 -13.264 -36.711 15.811 1.00 34.36 C ANISOU 2405 CB THR A 224 5248 3409 4400 556 -174 -337 C ATOM 2406 OG1 THR A 224 -14.117 -37.779 15.381 1.00 35.10 O ANISOU 2406 OG1 THR A 224 5466 3423 4447 507 -231 -333 O ATOM 2407 CG2 THR A 224 -13.969 -35.913 16.899 1.00 39.78 C ANISOU 2407 CG2 THR A 224 5825 4169 5119 513 -223 -278 C ATOM 2408 N LEU A 225 -10.830 -34.736 15.274 1.00 35.54 N ANISOU 2408 N LEU A 225 5228 3675 4600 678 6 -400 N ATOM 2409 CA LEU A 225 -10.019 -33.589 15.668 1.00 33.20 C ANISOU 2409 CA LEU A 225 4806 3460 4349 711 55 -397 C ATOM 2410 C LEU A 225 -9.988 -32.534 14.569 1.00 33.19 C ANISOU 2410 C LEU A 225 4806 3497 4308 680 103 -414 C ATOM 2411 O LEU A 225 -10.108 -31.335 14.847 1.00 32.62 O ANISOU 2411 O LEU A 225 4647 3495 4252 652 104 -389 O ATOM 2412 CB LEU A 225 -8.601 -34.045 16.017 1.00 34.35 C ANISOU 2412 CB LEU A 225 4911 3596 4544 811 112 -428 C ATOM 2413 CG LEU A 225 -8.407 -34.593 17.433 1.00 34.11 C ANISOU 2413 CG LEU A 225 4823 3563 4575 849 70 -402 C ATOM 2414 CD1 LEU A 225 -7.029 -35.215 17.590 1.00 41.01 C ANISOU 2414 CD1 LEU A 225 5677 4415 5488 951 127 -437 C ATOM 2415 CD2 LEU A 225 -8.611 -33.494 18.463 1.00 39.82 C ANISOU 2415 CD2 LEU A 225 5423 4368 5341 824 43 -359 C ATOM 2416 N GLN A 226 -9.833 -32.959 13.313 1.00 33.07 N ANISOU 2416 N GLN A 226 4893 3434 4238 684 143 -454 N ATOM 2417 CA GLN A 226 -9.795 -31.999 12.214 1.00 37.84 C ANISOU 2417 CA GLN A 226 5506 4072 4799 654 190 -470 C ATOM 2418 C GLN A 226 -11.126 -31.276 12.060 1.00 34.42 C ANISOU 2418 C GLN A 226 5082 3666 4330 560 130 -431 C ATOM 2419 O GLN A 226 -11.152 -30.101 11.678 1.00 30.21 O ANISOU 2419 O GLN A 226 4502 3188 3786 531 154 -423 O ATOM 2420 CB GLN A 226 -9.413 -32.707 10.914 1.00 38.31 C ANISOU 2420 CB GLN A 226 5685 4070 4801 679 241 -521 C ATOM 2421 CG GLN A 226 -7.961 -33.163 10.878 1.00 46.57 C ANISOU 2421 CG GLN A 226 6711 5106 5878 780 321 -563 C ATOM 2422 CD GLN A 226 -7.650 -34.054 9.690 1.00 58.85 C ANISOU 2422 CD GLN A 226 8395 6590 7374 813 365 -615 C ATOM 2423 OE1 GLN A 226 -8.541 -34.422 8.924 1.00 62.56 O ANISOU 2423 OE1 GLN A 226 8979 7012 7778 757 330 -620 O ATOM 2424 NE2 GLN A 226 -6.379 -34.406 9.532 1.00 59.94 N ANISOU 2424 NE2 GLN A 226 8517 6723 7532 904 443 -653 N ATOM 2425 N LYS A 227 -12.239 -31.953 12.355 1.00 33.99 N ANISOU 2425 N LYS A 227 5083 3574 4258 510 50 -404 N ATOM 2426 CA LYS A 227 -13.535 -31.286 12.316 1.00 31.61 C ANISOU 2426 CA LYS A 227 4779 3304 3928 422 -12 -361 C ATOM 2427 C LYS A 227 -13.672 -30.267 13.440 1.00 31.48 C ANISOU 2427 C LYS A 227 4632 3366 3964 416 -33 -318 C ATOM 2428 O LYS A 227 -14.326 -29.234 13.261 1.00 29.61 O ANISOU 2428 O LYS A 227 4363 3179 3710 364 -49 -293 O ATOM 2429 CB LYS A 227 -14.662 -32.316 12.395 1.00 34.55 C ANISOU 2429 CB LYS A 227 5237 3618 4270 370 -92 -339 C ATOM 2430 CG LYS A 227 -14.822 -33.155 11.138 1.00 41.76 C ANISOU 2430 CG LYS A 227 6295 4455 5116 354 -86 -376 C ATOM 2431 CD LYS A 227 -15.844 -34.264 11.335 1.00 56.49 C ANISOU 2431 CD LYS A 227 8245 6260 6961 304 -169 -353 C ATOM 2432 CE LYS A 227 -16.001 -35.104 10.076 1.00 71.19 C ANISOU 2432 CE LYS A 227 10257 8040 8752 286 -167 -393 C ATOM 2433 NZ LYS A 227 -16.872 -36.292 10.298 1.00 92.55 N ANISOU 2433 NZ LYS A 227 13049 10675 11439 242 -249 -373 N ATOM 2434 N GLU A 228 -13.066 -30.535 14.600 1.00 30.70 N ANISOU 2434 N GLU A 228 4459 3278 3928 469 -33 -310 N ATOM 2435 CA GLU A 228 -13.102 -29.566 15.689 1.00 29.39 C ANISOU 2435 CA GLU A 228 4171 3184 3810 469 -50 -274 C ATOM 2436 C GLU A 228 -12.223 -28.360 15.381 1.00 30.09 C ANISOU 2436 C GLU A 228 4190 3329 3915 493 16 -291 C ATOM 2437 O GLU A 228 -12.570 -27.227 15.731 1.00 27.42 O ANISOU 2437 O GLU A 228 3781 3050 3586 464 1 -263 O ATOM 2438 CB GLU A 228 -12.663 -30.224 16.996 1.00 35.06 C ANISOU 2438 CB GLU A 228 4837 3896 4589 520 -71 -261 C ATOM 2439 CG GLU A 228 -13.631 -31.269 17.519 1.00 38.24 C ANISOU 2439 CG GLU A 228 5293 4255 4983 488 -145 -231 C ATOM 2440 CD GLU A 228 -13.244 -31.779 18.893 1.00 42.62 C ANISOU 2440 CD GLU A 228 5786 4811 5596 534 -168 -213 C ATOM 2441 OE1 GLU A 228 -13.056 -30.947 19.806 1.00 41.35 O ANISOU 2441 OE1 GLU A 228 5522 4713 5477 548 -171 -190 O ATOM 2442 OE2 GLU A 228 -13.119 -33.011 19.059 1.00 45.20 O ANISOU 2442 OE2 GLU A 228 6173 5074 5927 559 -185 -222 O ATOM 2443 N VAL A 229 -11.079 -28.584 14.730 1.00 27.63 N ANISOU 2443 N VAL A 229 3896 2998 3604 547 89 -336 N ATOM 2444 CA VAL A 229 -10.228 -27.469 14.329 1.00 27.87 C ANISOU 2444 CA VAL A 229 3864 3080 3646 564 155 -352 C ATOM 2445 C VAL A 229 -10.952 -26.596 13.314 1.00 30.42 C ANISOU 2445 C VAL A 229 4226 3421 3910 497 155 -346 C ATOM 2446 O VAL A 229 -10.887 -25.362 13.371 1.00 30.48 O ANISOU 2446 O VAL A 229 4166 3486 3927 478 167 -331 O ATOM 2447 CB VAL A 229 -8.889 -27.991 13.776 1.00 33.16 C ANISOU 2447 CB VAL A 229 4549 3726 4324 635 236 -400 C ATOM 2448 CG1 VAL A 229 -8.078 -26.854 13.174 1.00 38.53 C ANISOU 2448 CG1 VAL A 229 5175 4458 5005 642 307 -414 C ATOM 2449 CG2 VAL A 229 -8.100 -28.690 14.871 1.00 35.26 C ANISOU 2449 CG2 VAL A 229 4758 3983 4655 705 236 -402 C ATOM 2450 N HIS A 230 -11.662 -27.224 12.374 1.00 30.09 N ANISOU 2450 N HIS A 230 4297 3329 3807 460 139 -357 N ATOM 2451 CA HIS A 230 -12.409 -26.467 11.376 1.00 30.17 C ANISOU 2451 CA HIS A 230 4352 3353 3758 395 133 -350 C ATOM 2452 C HIS A 230 -13.514 -25.645 12.025 1.00 28.47 C ANISOU 2452 C HIS A 230 4084 3184 3548 339 65 -299 C ATOM 2453 O HIS A 230 -13.724 -24.480 11.667 1.00 28.56 O ANISOU 2453 O HIS A 230 4067 3241 3545 307 73 -287 O ATOM 2454 CB HIS A 230 -12.989 -27.422 10.333 1.00 30.83 C ANISOU 2454 CB HIS A 230 4571 3369 3775 366 118 -371 C ATOM 2455 CG HIS A 230 -13.766 -26.741 9.251 1.00 35.05 C ANISOU 2455 CG HIS A 230 5161 3913 4244 300 109 -365 C ATOM 2456 ND1 HIS A 230 -13.181 -26.281 8.091 1.00 38.14 N ANISOU 2456 ND1 HIS A 230 5589 4307 4595 305 177 -397 N ATOM 2457 CD2 HIS A 230 -15.083 -26.443 9.151 1.00 38.39 C ANISOU 2457 CD2 HIS A 230 5607 4344 4633 227 40 -328 C ATOM 2458 CE1 HIS A 230 -14.103 -25.729 7.324 1.00 38.01 C ANISOU 2458 CE1 HIS A 230 5621 4298 4524 238 148 -382 C ATOM 2459 NE2 HIS A 230 -15.266 -25.814 7.944 1.00 40.54 N ANISOU 2459 NE2 HIS A 230 5932 4623 4848 191 64 -340 N ATOM 2460 N ALA A 231 -14.234 -26.233 12.983 1.00 31.21 N ANISOU 2460 N ALA A 231 4420 3522 3917 327 -3 -268 N ATOM 2461 CA ALA A 231 -15.295 -25.499 13.663 1.00 28.69 C ANISOU 2461 CA ALA A 231 4047 3249 3603 280 -66 -217 C ATOM 2462 C ALA A 231 -14.729 -24.367 14.510 1.00 28.05 C ANISOU 2462 C ALA A 231 3850 3233 3573 308 -47 -204 C ATOM 2463 O ALA A 231 -15.310 -23.278 14.569 1.00 25.26 O ANISOU 2463 O ALA A 231 3458 2928 3211 273 -67 -177 O ATOM 2464 CB ALA A 231 -16.121 -26.451 14.527 1.00 27.88 C ANISOU 2464 CB ALA A 231 3957 3124 3512 264 -137 -186 C ATOM 2465 N ALA A 232 -13.596 -24.605 15.177 1.00 24.13 N ANISOU 2465 N ALA A 232 3299 2740 3131 372 -10 -222 N ATOM 2466 CA ALA A 232 -12.984 -23.554 15.980 1.00 24.84 C ANISOU 2466 CA ALA A 232 3281 2889 3271 398 7 -211 C ATOM 2467 C ALA A 232 -12.497 -22.402 15.112 1.00 22.63 C ANISOU 2467 C ALA A 232 2988 2640 2973 386 60 -227 C ATOM 2468 O ALA A 232 -12.527 -21.245 15.546 1.00 27.37 O ANISOU 2468 O ALA A 232 3518 3290 3591 375 53 -206 O ATOM 2469 CB ALA A 232 -11.829 -24.125 16.802 1.00 24.05 C ANISOU 2469 CB ALA A 232 3128 2782 3230 468 34 -228 C ATOM 2470 N LYS A 233 -12.045 -22.692 13.889 1.00 23.22 N ANISOU 2470 N LYS A 233 3131 2683 3010 389 113 -263 N ATOM 2471 CA LYS A 233 -11.639 -21.623 12.984 1.00 24.87 C ANISOU 2471 CA LYS A 233 3335 2919 3195 372 164 -275 C ATOM 2472 C LYS A 233 -12.841 -20.806 12.531 1.00 25.80 C ANISOU 2472 C LYS A 233 3481 3056 3266 304 121 -246 C ATOM 2473 O LYS A 233 -12.762 -19.577 12.437 1.00 23.79 O ANISOU 2473 O LYS A 233 3183 2844 3013 286 132 -234 O ATOM 2474 CB LYS A 233 -10.899 -22.202 11.779 1.00 27.49 C ANISOU 2474 CB LYS A 233 3739 3214 3493 393 233 -319 C ATOM 2475 CG LYS A 233 -9.488 -22.670 12.091 1.00 39.05 C ANISOU 2475 CG LYS A 233 5157 4675 5005 466 294 -349 C ATOM 2476 CD LYS A 233 -8.782 -23.195 10.851 1.00 44.73 C ANISOU 2476 CD LYS A 233 5949 5361 5686 490 367 -393 C ATOM 2477 CE LYS A 233 -7.366 -23.652 11.171 1.00 53.29 C ANISOU 2477 CE LYS A 233 6980 6448 6819 569 429 -420 C ATOM 2478 NZ LYS A 233 -6.680 -24.237 9.984 1.00 62.07 N ANISOU 2478 NZ LYS A 233 8164 7527 7891 600 504 -464 N ATOM 2479 N SER A 234 -13.962 -21.472 12.245 1.00 23.95 N ANISOU 2479 N SER A 234 3320 2789 2990 265 68 -233 N ATOM 2480 CA SER A 234 -15.174 -20.745 11.888 1.00 27.57 C ANISOU 2480 CA SER A 234 3801 3269 3407 202 20 -201 C ATOM 2481 C SER A 234 -15.586 -19.792 13.004 1.00 25.15 C ANISOU 2481 C SER A 234 3402 3017 3138 198 -21 -162 C ATOM 2482 O SER A 234 -15.919 -18.630 12.747 1.00 21.79 O ANISOU 2482 O SER A 234 2956 2627 2696 170 -25 -145 O ATOM 2483 CB SER A 234 -16.302 -21.727 11.578 1.00 25.64 C ANISOU 2483 CB SER A 234 3639 2982 3119 162 -37 -189 C ATOM 2484 OG SER A 234 -15.943 -22.594 10.519 1.00 28.44 O ANISOU 2484 OG SER A 234 4090 3282 3435 166 -1 -228 O ATOM 2485 N ALA A 235 -15.560 -20.267 14.252 1.00 21.67 N ANISOU 2485 N ALA A 235 2907 2583 2746 228 -51 -146 N ATOM 2486 CA ALA A 235 -15.908 -19.408 15.379 1.00 25.32 C ANISOU 2486 CA ALA A 235 3283 3096 3242 230 -88 -111 C ATOM 2487 C ALA A 235 -14.910 -18.267 15.534 1.00 24.20 C ANISOU 2487 C ALA A 235 3073 2991 3132 256 -42 -122 C ATOM 2488 O ALA A 235 -15.297 -17.135 15.847 1.00 20.66 O ANISOU 2488 O ALA A 235 2582 2583 2685 239 -63 -98 O ATOM 2489 CB ALA A 235 -15.978 -20.232 16.663 1.00 27.03 C ANISOU 2489 CB ALA A 235 3460 3308 3502 260 -125 -95 C ATOM 2490 N ALA A 236 -13.622 -18.546 15.324 1.00 23.49 N ANISOU 2490 N ALA A 236 2971 2886 3066 296 20 -158 N ATOM 2491 CA ALA A 236 -12.616 -17.496 15.426 1.00 23.43 C ANISOU 2491 CA ALA A 236 2899 2914 3090 315 64 -168 C ATOM 2492 C ALA A 236 -12.778 -16.459 14.322 1.00 22.50 C ANISOU 2492 C ALA A 236 2812 2809 2927 274 88 -169 C ATOM 2493 O ALA A 236 -12.522 -15.271 14.550 1.00 19.95 O ANISOU 2493 O ALA A 236 2438 2523 2621 268 94 -158 O ATOM 2494 CB ALA A 236 -11.214 -18.103 15.382 1.00 22.57 C ANISOU 2494 CB ALA A 236 2771 2790 3017 368 127 -203 C ATOM 2495 N ILE A 237 -13.198 -16.883 13.128 1.00 21.12 N ANISOU 2495 N ILE A 237 2726 2602 2696 244 100 -182 N ATOM 2496 CA ILE A 237 -13.433 -15.933 12.044 1.00 17.17 C ANISOU 2496 CA ILE A 237 2263 2112 2148 202 119 -181 C ATOM 2497 C ILE A 237 -14.567 -14.986 12.410 1.00 21.24 C ANISOU 2497 C ILE A 237 2760 2659 2650 165 56 -140 C ATOM 2498 O ILE A 237 -14.513 -13.785 12.119 1.00 19.91 O ANISOU 2498 O ILE A 237 2575 2517 2473 145 66 -131 O ATOM 2499 CB ILE A 237 -13.724 -16.681 10.730 1.00 21.86 C ANISOU 2499 CB ILE A 237 2962 2663 2679 178 137 -202 C ATOM 2500 CG1 ILE A 237 -12.448 -17.347 10.209 1.00 24.64 C ANISOU 2500 CG1 ILE A 237 3331 2992 3040 220 214 -246 C ATOM 2501 CG2 ILE A 237 -14.302 -15.726 9.689 1.00 21.11 C ANISOU 2501 CG2 ILE A 237 2913 2580 2528 126 136 -192 C ATOM 2502 CD1 ILE A 237 -12.695 -18.384 9.131 1.00 24.49 C ANISOU 2502 CD1 ILE A 237 3420 2921 2964 209 228 -272 C ATOM 2503 N ILE A 238 -15.612 -15.512 13.052 1.00 16.76 N ANISOU 2503 N ILE A 238 2197 2090 2082 155 -8 -114 N ATOM 2504 CA ILE A 238 -16.737 -14.678 13.464 1.00 21.22 C ANISOU 2504 CA ILE A 238 2740 2687 2634 127 -68 -74 C ATOM 2505 C ILE A 238 -16.269 -13.617 14.453 1.00 17.56 C ANISOU 2505 C ILE A 238 2190 2265 2218 153 -68 -62 C ATOM 2506 O ILE A 238 -16.588 -12.429 14.318 1.00 15.86 O ANISOU 2506 O ILE A 238 1962 2076 1989 133 -79 -45 O ATOM 2507 CB ILE A 238 -17.854 -15.551 14.065 1.00 22.84 C ANISOU 2507 CB ILE A 238 2958 2886 2835 116 -133 -46 C ATOM 2508 CG1 ILE A 238 -18.354 -16.577 13.041 1.00 27.93 C ANISOU 2508 CG1 ILE A 238 3696 3486 3430 84 -139 -57 C ATOM 2509 CG2 ILE A 238 -18.998 -14.683 14.556 1.00 25.98 C ANISOU 2509 CG2 ILE A 238 3325 3325 3223 94 -191 -3 C ATOM 2510 CD1 ILE A 238 -19.354 -16.034 12.053 1.00 26.15 C ANISOU 2510 CD1 ILE A 238 3526 3265 3144 30 -165 -39 C ATOM 2511 N ALA A 239 -15.502 -14.033 15.463 1.00 18.29 N ANISOU 2511 N ALA A 239 2224 2360 2365 197 -59 -71 N ATOM 2512 CA ALA A 239 -15.014 -13.089 16.462 1.00 15.08 C ANISOU 2512 CA ALA A 239 1736 1989 2003 222 -63 -61 C ATOM 2513 C ALA A 239 -14.044 -12.088 15.849 1.00 18.73 C ANISOU 2513 C ALA A 239 2185 2462 2469 217 -10 -79 C ATOM 2514 O ALA A 239 -14.054 -10.904 16.208 1.00 15.95 O ANISOU 2514 O ALA A 239 1795 2138 2127 212 -23 -64 O ATOM 2515 CB ALA A 239 -14.349 -13.843 17.613 1.00 20.66 C ANISOU 2515 CB ALA A 239 2389 2695 2766 270 -64 -68 C ATOM 2516 N GLY A 240 -13.199 -12.543 14.924 1.00 19.21 N ANISOU 2516 N GLY A 240 2278 2499 2521 220 51 -111 N ATOM 2517 CA GLY A 240 -12.263 -11.635 14.285 1.00 20.62 C ANISOU 2517 CA GLY A 240 2444 2689 2701 212 105 -125 C ATOM 2518 C GLY A 240 -12.955 -10.603 13.416 1.00 17.93 C ANISOU 2518 C GLY A 240 2147 2356 2310 164 95 -110 C ATOM 2519 O GLY A 240 -12.532 -9.446 13.358 1.00 20.20 O ANISOU 2519 O GLY A 240 2407 2664 2605 152 109 -104 O ATOM 2520 N LEU A 241 -14.024 -11.005 12.725 1.00 16.66 N ANISOU 2520 N LEU A 241 2057 2177 2096 134 68 -102 N ATOM 2521 CA LEU A 241 -14.767 -10.053 11.906 1.00 16.74 C ANISOU 2521 CA LEU A 241 2112 2194 2056 89 52 -84 C ATOM 2522 C LEU A 241 -15.500 -9.033 12.766 1.00 16.49 C ANISOU 2522 C LEU A 241 2036 2192 2036 86 -5 -50 C ATOM 2523 O LEU A 241 -15.653 -7.876 12.357 1.00 15.86 O ANISOU 2523 O LEU A 241 1964 2125 1935 62 -7 -37 O ATOM 2524 CB LEU A 241 -15.748 -10.794 11.000 1.00 19.21 C ANISOU 2524 CB LEU A 241 2509 2480 2310 58 32 -82 C ATOM 2525 CG LEU A 241 -15.115 -11.555 9.830 1.00 18.47 C ANISOU 2525 CG LEU A 241 2479 2352 2184 53 91 -117 C ATOM 2526 CD1 LEU A 241 -16.142 -12.435 9.147 1.00 22.91 C ANISOU 2526 CD1 LEU A 241 3126 2886 2694 24 58 -114 C ATOM 2527 CD2 LEU A 241 -14.498 -10.584 8.835 1.00 30.02 C ANISOU 2527 CD2 LEU A 241 3961 3822 3621 31 143 -126 C ATOM 2528 N PHE A 242 -15.959 -9.436 13.953 1.00 15.80 N ANISOU 2528 N PHE A 242 1906 2117 1980 112 -51 -34 N ATOM 2529 CA PHE A 242 -16.529 -8.468 14.884 1.00 14.99 C ANISOU 2529 CA PHE A 242 1757 2047 1892 119 -99 -4 C ATOM 2530 C PHE A 242 -15.502 -7.406 15.251 1.00 14.35 C ANISOU 2530 C PHE A 242 1626 1980 1846 132 -73 -12 C ATOM 2531 O PHE A 242 -15.818 -6.212 15.299 1.00 13.16 O ANISOU 2531 O PHE A 242 1469 1845 1685 119 -94 5 O ATOM 2532 CB PHE A 242 -17.036 -9.183 16.139 1.00 18.35 C ANISOU 2532 CB PHE A 242 2142 2482 2346 148 -145 12 C ATOM 2533 CG PHE A 242 -17.643 -8.262 17.163 1.00 15.05 C ANISOU 2533 CG PHE A 242 1678 2099 1942 162 -193 41 C ATOM 2534 CD1 PHE A 242 -16.849 -7.631 18.106 1.00 13.54 C ANISOU 2534 CD1 PHE A 242 1426 1924 1796 193 -188 36 C ATOM 2535 CD2 PHE A 242 -19.008 -8.035 17.185 1.00 15.25 C ANISOU 2535 CD2 PHE A 242 1721 2141 1932 146 -245 74 C ATOM 2536 CE1 PHE A 242 -17.407 -6.784 19.047 1.00 17.12 C ANISOU 2536 CE1 PHE A 242 1843 2406 2257 209 -233 61 C ATOM 2537 CE2 PHE A 242 -19.570 -7.191 18.123 1.00 15.00 C ANISOU 2537 CE2 PHE A 242 1648 2141 1909 166 -287 100 C ATOM 2538 CZ PHE A 242 -18.767 -6.566 19.057 1.00 14.02 C ANISOU 2538 CZ PHE A 242 1470 2029 1827 198 -280 92 C ATOM 2539 N ALA A 243 -14.260 -7.824 15.501 1.00 15.10 N ANISOU 2539 N ALA A 243 1684 2069 1983 157 -28 -38 N ATOM 2540 CA ALA A 243 -13.217 -6.868 15.852 1.00 16.56 C ANISOU 2540 CA ALA A 243 1818 2270 2205 165 -3 -44 C ATOM 2541 C ALA A 243 -12.879 -5.960 14.677 1.00 15.86 C ANISOU 2541 C ALA A 243 1765 2177 2084 127 34 -49 C ATOM 2542 O ALA A 243 -12.703 -4.750 14.852 1.00 17.68 O ANISOU 2542 O ALA A 243 1976 2421 2321 115 26 -37 O ATOM 2543 CB ALA A 243 -11.973 -7.611 16.336 1.00 19.65 C ANISOU 2543 CB ALA A 243 2160 2659 2648 200 36 -68 C ATOM 2544 N ALEU A 244 -12.789 -6.528 13.472 0.50 17.96 N ANISOU 2544 N ALEU A 244 2088 2422 2312 107 76 -65 N ATOM 2545 N BLEU A 244 -12.791 -6.518 13.468 0.50 17.96 N ANISOU 2545 N BLEU A 244 2088 2422 2312 106 76 -65 N ATOM 2546 CA ALEU A 244 -12.454 -5.731 12.297 0.50 18.31 C ANISOU 2546 CA ALEU A 244 2172 2464 2323 69 116 -68 C ATOM 2547 CA BLEU A 244 -12.440 -5.697 12.314 0.50 18.32 C ANISOU 2547 CA BLEU A 244 2171 2465 2324 69 116 -68 C ATOM 2548 C ALEU A 244 -13.516 -4.672 12.029 0.50 17.20 C ANISOU 2548 C ALEU A 244 2066 2328 2142 37 69 -40 C ATOM 2549 C BLEU A 244 -13.520 -4.663 12.020 0.50 17.20 C ANISOU 2549 C BLEU A 244 2066 2328 2141 37 69 -40 C ATOM 2550 O ALEU A 244 -13.192 -3.525 11.699 0.50 17.67 O ANISOU 2550 O ALEU A 244 2126 2393 2194 14 81 -33 O ATOM 2551 O BLEU A 244 -13.209 -3.522 11.658 0.50 17.67 O ANISOU 2551 O BLEU A 244 2128 2393 2192 13 81 -33 O ATOM 2552 CB ALEU A 244 -12.294 -6.644 11.079 0.50 19.36 C ANISOU 2552 CB ALEU A 244 2367 2572 2415 58 165 -91 C ATOM 2553 CB BLEU A 244 -12.201 -6.578 11.087 0.50 19.40 C ANISOU 2553 CB BLEU A 244 2369 2579 2423 58 168 -91 C ATOM 2554 CG ALEU A 244 -11.829 -5.992 9.773 0.50 21.63 C ANISOU 2554 CG ALEU A 244 2699 2856 2663 21 217 -98 C ATOM 2555 CG BLEU A 244 -10.862 -7.317 11.002 0.50 23.60 C ANISOU 2555 CG BLEU A 244 2871 3107 2988 86 236 -122 C ATOM 2556 CD1ALEU A 244 -10.334 -5.711 9.813 0.50 28.33 C ANISOU 2556 CD1ALEU A 244 3493 3718 3552 33 281 -114 C ATOM 2557 CD1BLEU A 244 -10.779 -8.096 9.696 0.50 24.66 C ANISOU 2557 CD1BLEU A 244 3080 3216 3073 75 285 -145 C ATOM 2558 CD2ALEU A 244 -12.184 -6.870 8.582 0.50 23.98 C ANISOU 2558 CD2ALEU A 244 3081 3127 2904 5 242 -114 C ATOM 2559 CD2BLEU A 244 -9.687 -6.354 11.126 0.50 26.73 C ANISOU 2559 CD2BLEU A 244 3210 3526 3420 83 275 -123 C ATOM 2560 N CYS A 245 -14.793 -5.040 12.169 1.00 14.16 N ANISOU 2560 N CYS A 245 1710 1941 1729 35 16 -22 N ATOM 2561 CA CYS A 245 -15.875 -4.117 11.839 1.00 14.94 C ANISOU 2561 CA CYS A 245 1845 2046 1787 9 -29 6 C ATOM 2562 C CYS A 245 -16.039 -3.021 12.885 1.00 13.76 C ANISOU 2562 C CYS A 245 1645 1918 1665 25 -70 26 C ATOM 2563 O CYS A 245 -16.436 -1.901 12.543 1.00 13.35 O ANISOU 2563 O CYS A 245 1617 1869 1588 5 -89 44 O ATOM 2564 CB CYS A 245 -17.187 -4.886 11.676 1.00 13.98 C ANISOU 2564 CB CYS A 245 1764 1920 1629 1 -75 21 C ATOM 2565 SG CYS A 245 -17.272 -5.936 10.203 1.00 18.44 S ANISOU 2565 SG CYS A 245 2413 2454 2140 -30 -39 1 S ATOM 2566 N TRP A 246 -15.744 -3.311 14.154 1.00 12.92 N ANISOU 2566 N TRP A 246 1476 1824 1609 64 -86 24 N ATOM 2567 CA TRP A 246 -15.951 -2.341 15.223 1.00 12.65 C ANISOU 2567 CA TRP A 246 1399 1809 1599 84 -129 42 C ATOM 2568 C TRP A 246 -14.703 -1.553 15.594 1.00 14.02 C ANISOU 2568 C TRP A 246 1530 1985 1813 88 -102 30 C ATOM 2569 O TRP A 246 -14.831 -0.456 16.146 1.00 10.72 O ANISOU 2569 O TRP A 246 1098 1575 1402 92 -133 44 O ATOM 2570 CB TRP A 246 -16.478 -3.038 16.484 1.00 11.55 C ANISOU 2570 CB TRP A 246 1217 1686 1486 123 -171 52 C ATOM 2571 CG TRP A 246 -17.947 -3.336 16.432 1.00 11.42 C ANISOU 2571 CG TRP A 246 1230 1678 1432 120 -219 78 C ATOM 2572 CD1 TRP A 246 -18.534 -4.529 16.135 1.00 13.94 C ANISOU 2572 CD1 TRP A 246 1573 1990 1732 113 -225 80 C ATOM 2573 CD2 TRP A 246 -19.014 -2.415 16.683 1.00 11.61 C ANISOU 2573 CD2 TRP A 246 1261 1720 1430 122 -269 108 C ATOM 2574 NE1 TRP A 246 -19.904 -4.409 16.186 1.00 14.59 N ANISOU 2574 NE1 TRP A 246 1672 2089 1781 107 -277 111 N ATOM 2575 CE2 TRP A 246 -20.222 -3.118 16.517 1.00 12.15 C ANISOU 2575 CE2 TRP A 246 1351 1797 1468 116 -303 129 C ATOM 2576 CE3 TRP A 246 -19.064 -1.061 17.028 1.00 12.11 C ANISOU 2576 CE3 TRP A 246 1316 1793 1494 130 -290 119 C ATOM 2577 CZ2 TRP A 246 -21.466 -2.516 16.689 1.00 11.17 C ANISOU 2577 CZ2 TRP A 246 1234 1696 1314 120 -354 162 C ATOM 2578 CZ3 TRP A 246 -20.298 -0.466 17.199 1.00 14.70 C ANISOU 2578 CZ3 TRP A 246 1656 2139 1792 138 -340 149 C ATOM 2579 CH2 TRP A 246 -21.484 -1.194 17.028 1.00 11.85 C ANISOU 2579 CH2 TRP A 246 1311 1792 1402 134 -370 171 C ATOM 2580 N LEU A 247 -13.510 -2.075 15.315 1.00 15.12 N ANISOU 2580 N LEU A 247 1649 2117 1978 87 -46 5 N ATOM 2581 CA LEU A 247 -12.296 -1.391 15.753 1.00 16.34 C ANISOU 2581 CA LEU A 247 1754 2278 2177 89 -23 -4 C ATOM 2582 C LEU A 247 -12.140 0.001 15.155 1.00 13.31 C ANISOU 2582 C LEU A 247 1395 1890 1772 52 -19 7 C ATOM 2583 O LEU A 247 -11.710 0.910 15.887 1.00 14.72 O ANISOU 2583 O LEU A 247 1538 2074 1979 55 -39 13 O ATOM 2584 CB LEU A 247 -11.068 -2.248 15.427 1.00 18.45 C ANISOU 2584 CB LEU A 247 1995 2542 2473 95 42 -30 C ATOM 2585 CG LEU A 247 -10.662 -3.270 16.490 1.00 22.80 C ANISOU 2585 CG LEU A 247 2490 3100 3073 140 37 -42 C ATOM 2586 CD1 LEU A 247 -9.573 -4.184 15.951 1.00 26.93 C ANISOU 2586 CD1 LEU A 247 3000 3619 3615 149 104 -67 C ATOM 2587 CD2 LEU A 247 -10.195 -2.571 17.761 1.00 24.63 C ANISOU 2587 CD2 LEU A 247 2658 3349 3353 160 5 -35 C ATOM 2588 N PRO A 248 -12.434 0.241 13.876 1.00 15.87 N ANISOU 2588 N PRO A 248 1781 2201 2046 14 4 10 N ATOM 2589 CA PRO A 248 -12.260 1.603 13.341 1.00 13.76 C ANISOU 2589 CA PRO A 248 1539 1928 1760 -22 6 23 C ATOM 2590 C PRO A 248 -12.997 2.668 14.135 1.00 14.38 C ANISOU 2590 C PRO A 248 1617 2009 1838 -12 -60 45 C ATOM 2591 O PRO A 248 -12.407 3.701 14.477 1.00 14.19 O ANISOU 2591 O PRO A 248 1574 1982 1834 -23 -66 50 O ATOM 2592 CB PRO A 248 -12.788 1.468 11.907 1.00 16.26 C ANISOU 2592 CB PRO A 248 1931 2231 2015 -57 29 26 C ATOM 2593 CG PRO A 248 -12.504 0.047 11.555 1.00 20.20 C ANISOU 2593 CG PRO A 248 2431 2729 2516 -44 70 3 C ATOM 2594 CD PRO A 248 -12.767 -0.725 12.815 1.00 18.47 C ANISOU 2594 CD PRO A 248 2162 2520 2336 2 35 1 C ATOM 2595 N LEU A 249 -14.275 2.444 14.446 1.00 10.21 N ANISOU 2595 N LEU A 249 1109 1486 1286 9 -110 60 N ATOM 2596 CA LEU A 249 -15.031 3.427 15.214 1.00 11.42 C ANISOU 2596 CA LEU A 249 1261 1643 1434 27 -171 81 C ATOM 2597 C LEU A 249 -14.462 3.586 16.621 1.00 13.94 C ANISOU 2597 C LEU A 249 1517 1972 1806 62 -191 75 C ATOM 2598 O LEU A 249 -14.409 4.700 17.153 1.00 10.64 O ANISOU 2598 O LEU A 249 1097 1551 1397 65 -222 83 O ATOM 2599 CB LEU A 249 -16.503 3.019 15.264 1.00 11.23 C ANISOU 2599 CB LEU A 249 1264 1630 1375 45 -215 99 C ATOM 2600 CG LEU A 249 -17.505 4.027 15.829 1.00 15.08 C ANISOU 2600 CG LEU A 249 1763 2124 1845 66 -276 124 C ATOM 2601 CD1 LEU A 249 -17.399 5.370 15.126 1.00 15.76 C ANISOU 2601 CD1 LEU A 249 1894 2190 1904 36 -277 134 C ATOM 2602 CD2 LEU A 249 -18.918 3.471 15.711 1.00 16.37 C ANISOU 2602 CD2 LEU A 249 1946 2302 1971 79 -311 145 C ATOM 2603 N HIS A 250 -14.035 2.483 17.242 1.00 14.45 N ANISOU 2603 N HIS A 250 1534 2048 1907 88 -177 60 N ATOM 2604 CA HIS A 250 -13.371 2.585 18.539 1.00 13.72 C ANISOU 2604 CA HIS A 250 1381 1966 1867 118 -193 53 C ATOM 2605 C HIS A 250 -12.082 3.390 18.433 1.00 13.25 C ANISOU 2605 C HIS A 250 1300 1897 1836 91 -166 43 C ATOM 2606 O HIS A 250 -11.774 4.204 19.310 1.00 10.63 O ANISOU 2606 O HIS A 250 944 1567 1529 101 -197 47 O ATOM 2607 CB HIS A 250 -13.073 1.193 19.095 1.00 12.26 C ANISOU 2607 CB HIS A 250 1152 1792 1714 148 -178 39 C ATOM 2608 CG HIS A 250 -14.254 0.517 19.718 1.00 14.64 C ANISOU 2608 CG HIS A 250 1455 2106 2002 181 -220 52 C ATOM 2609 ND1 HIS A 250 -14.899 1.018 20.829 1.00 15.77 N ANISOU 2609 ND1 HIS A 250 1580 2263 2148 214 -274 67 N ATOM 2610 CD2 HIS A 250 -14.890 -0.637 19.404 1.00 14.53 C ANISOU 2610 CD2 HIS A 250 1456 2093 1970 186 -216 53 C ATOM 2611 CE1 HIS A 250 -15.887 0.208 21.164 1.00 15.18 C ANISOU 2611 CE1 HIS A 250 1506 2202 2059 236 -299 80 C ATOM 2612 NE2 HIS A 250 -15.903 -0.805 20.317 1.00 15.85 N ANISOU 2612 NE2 HIS A 250 1612 2279 2133 218 -266 72 N ATOM 2613 N ILE A 251 -11.312 3.170 17.367 1.00 12.68 N ANISOU 2613 N ILE A 251 1238 1819 1760 56 -107 33 N ATOM 2614 CA ILE A 251 -10.041 3.868 17.212 1.00 14.12 C ANISOU 2614 CA ILE A 251 1395 1999 1972 26 -76 27 C ATOM 2615 C ILE A 251 -10.276 5.355 16.977 1.00 13.27 C ANISOU 2615 C ILE A 251 1327 1876 1840 -5 -104 45 C ATOM 2616 O ILE A 251 -9.519 6.202 17.466 1.00 13.18 O ANISOU 2616 O ILE A 251 1290 1861 1858 -18 -115 47 O ATOM 2617 CB ILE A 251 -9.226 3.223 16.076 1.00 14.33 C ANISOU 2617 CB ILE A 251 1423 2026 1994 0 -1 14 C ATOM 2618 CG1 ILE A 251 -8.774 1.822 16.498 1.00 14.33 C ANISOU 2618 CG1 ILE A 251 1376 2039 2029 37 25 -6 C ATOM 2619 CG2 ILE A 251 -8.027 4.090 15.713 1.00 19.06 C ANISOU 2619 CG2 ILE A 251 2003 2625 2614 -41 33 15 C ATOM 2620 CD1 ILE A 251 -8.271 0.960 15.358 1.00 24.44 C ANISOU 2620 CD1 ILE A 251 2673 3318 3296 24 95 -21 C ATOM 2621 N ILE A 252 -11.338 5.699 16.244 1.00 13.92 N ANISOU 2621 N ILE A 252 1474 1946 1868 -17 -121 59 N ATOM 2622 CA ILE A 252 -11.685 7.105 16.051 1.00 13.39 C ANISOU 2622 CA ILE A 252 1451 1860 1774 -40 -154 77 C ATOM 2623 C ILE A 252 -12.011 7.757 17.388 1.00 13.27 C ANISOU 2623 C ILE A 252 1418 1846 1780 -4 -217 83 C ATOM 2624 O ILE A 252 -11.559 8.871 17.684 1.00 13.17 O ANISOU 2624 O ILE A 252 1409 1817 1778 -21 -238 88 O ATOM 2625 CB ILE A 252 -12.855 7.239 15.062 1.00 15.66 C ANISOU 2625 CB ILE A 252 1811 2139 2000 -52 -164 92 C ATOM 2626 CG1 ILE A 252 -12.404 6.856 13.652 1.00 13.50 C ANISOU 2626 CG1 ILE A 252 1567 1861 1701 -96 -101 87 C ATOM 2627 CG2 ILE A 252 -13.409 8.661 15.092 1.00 12.09 C ANISOU 2627 CG2 ILE A 252 1405 1668 1522 -61 -211 113 C ATOM 2628 CD1 ILE A 252 -13.548 6.641 12.682 1.00 17.53 C ANISOU 2628 CD1 ILE A 252 2143 2366 2151 -105 -108 98 C ATOM 2629 N ASN A 253 -12.811 7.077 18.213 1.00 12.00 N ANISOU 2629 N ASN A 253 1239 1701 1622 45 -249 83 N ATOM 2630 CA ASN A 253 -13.112 7.606 19.540 1.00 12.69 C ANISOU 2630 CA ASN A 253 1306 1790 1725 85 -306 87 C ATOM 2631 C ASN A 253 -11.845 7.801 20.361 1.00 12.65 C ANISOU 2631 C ASN A 253 1247 1786 1775 83 -302 73 C ATOM 2632 O ASN A 253 -11.760 8.746 21.154 1.00 13.85 O ANISOU 2632 O ASN A 253 1400 1927 1935 93 -344 76 O ATOM 2633 CB ASN A 253 -14.079 6.681 20.281 1.00 12.65 C ANISOU 2633 CB ASN A 253 1282 1809 1717 137 -332 89 C ATOM 2634 CG ASN A 253 -15.472 6.677 19.677 1.00 12.12 C ANISOU 2634 CG ASN A 253 1264 1744 1595 143 -352 109 C ATOM 2635 OD1 ASN A 253 -15.850 7.588 18.942 1.00 17.07 O ANISOU 2635 OD1 ASN A 253 1944 2355 2188 120 -361 121 O ATOM 2636 ND2 ASN A 253 -16.250 5.649 19.998 1.00 13.72 N ANISOU 2636 ND2 ASN A 253 1451 1969 1792 173 -362 113 N ATOM 2637 N CYS A 254 -10.852 6.924 20.191 1.00 12.84 N ANISOU 2637 N CYS A 254 1224 1820 1833 71 -253 58 N ATOM 2638 CA CYS A 254 -9.587 7.105 20.899 1.00 13.80 C ANISOU 2638 CA CYS A 254 1290 1946 2009 65 -249 48 C ATOM 2639 C CYS A 254 -8.871 8.370 20.439 1.00 13.21 C ANISOU 2639 C CYS A 254 1234 1851 1934 13 -245 55 C ATOM 2640 O CYS A 254 -8.299 9.097 21.260 1.00 14.08 O ANISOU 2640 O CYS A 254 1323 1954 2073 10 -277 55 O ATOM 2641 CB CYS A 254 -8.691 5.882 20.704 1.00 15.71 C ANISOU 2641 CB CYS A 254 1478 2206 2286 66 -193 32 C ATOM 2642 SG CYS A 254 -9.211 4.413 21.626 1.00 16.31 S ANISOU 2642 SG CYS A 254 1516 2302 2377 128 -206 23 S ATOM 2643 N PHE A 255 -8.885 8.654 19.133 1.00 14.88 N ANISOU 2643 N PHE A 255 1489 2051 2113 -31 -208 62 N ATOM 2644 CA PHE A 255 -8.262 9.882 18.646 1.00 15.84 C ANISOU 2644 CA PHE A 255 1634 2152 2231 -84 -206 73 C ATOM 2645 C PHE A 255 -9.000 11.109 19.165 1.00 16.52 C ANISOU 2645 C PHE A 255 1771 2212 2294 -76 -273 86 C ATOM 2646 O PHE A 255 -8.377 12.076 19.620 1.00 17.79 O ANISOU 2646 O PHE A 255 1929 2356 2475 -98 -299 90 O ATOM 2647 CB PHE A 255 -8.214 9.887 17.117 1.00 16.78 C ANISOU 2647 CB PHE A 255 1796 2266 2314 -131 -152 80 C ATOM 2648 CG PHE A 255 -7.007 9.197 16.552 1.00 16.45 C ANISOU 2648 CG PHE A 255 1705 2244 2301 -157 -80 70 C ATOM 2649 CD1 PHE A 255 -5.829 9.895 16.338 1.00 21.73 C ANISOU 2649 CD1 PHE A 255 2348 2911 2996 -207 -57 77 C ATOM 2650 CD2 PHE A 255 -7.045 7.846 16.253 1.00 20.75 C ANISOU 2650 CD2 PHE A 255 2228 2808 2847 -131 -38 55 C ATOM 2651 CE1 PHE A 255 -4.715 9.258 15.826 1.00 24.64 C ANISOU 2651 CE1 PHE A 255 2667 3304 3391 -227 12 70 C ATOM 2652 CE2 PHE A 255 -5.937 7.205 15.743 1.00 21.70 C ANISOU 2652 CE2 PHE A 255 2305 2948 2993 -148 30 45 C ATOM 2653 CZ PHE A 255 -4.769 7.911 15.531 1.00 23.44 C ANISOU 2653 CZ PHE A 255 2495 3171 3239 -194 56 53 C ATOM 2654 N THR A 256 -10.332 11.091 19.096 1.00 15.72 N ANISOU 2654 N THR A 256 1715 2107 2149 -43 -303 93 N ATOM 2655 CA THR A 256 -11.119 12.178 19.663 1.00 14.69 C ANISOU 2655 CA THR A 256 1631 1955 1995 -21 -367 104 C ATOM 2656 C THR A 256 -10.757 12.410 21.124 1.00 16.89 C ANISOU 2656 C THR A 256 1872 2235 2312 12 -411 95 C ATOM 2657 O THR A 256 -10.582 13.555 21.558 1.00 18.22 O ANISOU 2657 O THR A 256 2066 2376 2480 3 -452 99 O ATOM 2658 CB THR A 256 -12.611 11.862 19.533 1.00 14.91 C ANISOU 2658 CB THR A 256 1696 1991 1978 21 -390 113 C ATOM 2659 OG1 THR A 256 -12.928 11.575 18.166 1.00 15.59 O ANISOU 2659 OG1 THR A 256 1819 2077 2029 -12 -351 121 O ATOM 2660 CG2 THR A 256 -13.454 13.032 20.014 1.00 18.70 C ANISOU 2660 CG2 THR A 256 2227 2449 2429 48 -452 126 C ATOM 2661 N PHE A 257 -10.622 11.329 21.892 1.00 17.09 N ANISOU 2661 N PHE A 257 1837 2288 2368 49 -404 82 N ATOM 2662 CA PHE A 257 -10.419 11.441 23.331 1.00 19.32 C ANISOU 2662 CA PHE A 257 2085 2574 2680 88 -449 73 C ATOM 2663 C PHE A 257 -8.976 11.795 23.675 1.00 19.68 C ANISOU 2663 C PHE A 257 2089 2614 2775 51 -443 65 C ATOM 2664 O PHE A 257 -8.729 12.731 24.444 1.00 20.96 O ANISOU 2664 O PHE A 257 2262 2756 2946 51 -490 65 O ATOM 2665 CB PHE A 257 -10.821 10.130 24.008 1.00 16.84 C ANISOU 2665 CB PHE A 257 1725 2294 2380 140 -445 65 C ATOM 2666 CG PHE A 257 -10.679 10.147 25.505 1.00 18.21 C ANISOU 2666 CG PHE A 257 1864 2475 2580 184 -490 57 C ATOM 2667 CD1 PHE A 257 -11.503 10.942 26.283 1.00 19.44 C ANISOU 2667 CD1 PHE A 257 2062 2620 2702 219 -536 63 C ATOM 2668 CD2 PHE A 257 -9.733 9.354 26.133 1.00 15.56 C ANISOU 2668 CD2 PHE A 257 1461 2158 2294 190 -475 44 C ATOM 2669 CE1 PHE A 257 -11.378 10.955 27.663 1.00 19.49 C ANISOU 2669 CE1 PHE A 257 2073 2636 2697 239 -522 58 C ATOM 2670 CE2 PHE A 257 -9.604 9.364 27.510 1.00 20.75 C ANISOU 2670 CE2 PHE A 257 2125 2823 2936 213 -474 41 C ATOM 2671 CZ PHE A 257 -10.429 10.168 28.274 1.00 19.91 C ANISOU 2671 CZ PHE A 257 2076 2705 2782 234 -495 49 C ATOM 2672 N PHE A 258 -8.011 11.063 23.117 1.00 18.79 N ANISOU 2672 N PHE A 258 1928 2519 2694 19 -386 59 N ATOM 2673 CA PHE A 258 -6.622 11.193 23.539 1.00 21.51 C ANISOU 2673 CA PHE A 258 2216 2868 3091 -10 -378 54 C ATOM 2674 C PHE A 258 -5.857 12.307 22.834 1.00 23.35 C ANISOU 2674 C PHE A 258 2471 3077 3324 -80 -369 65 C ATOM 2675 O PHE A 258 -4.799 12.711 23.330 1.00 22.09 O ANISOU 2675 O PHE A 258 2271 2916 3205 -108 -381 65 O ATOM 2676 CB PHE A 258 -5.874 9.874 23.317 1.00 19.06 C ANISOU 2676 CB PHE A 258 1836 2589 2816 -7 -320 43 C ATOM 2677 CG PHE A 258 -6.259 8.785 24.277 1.00 23.64 C ANISOU 2677 CG PHE A 258 2378 3192 3412 56 -335 32 C ATOM 2678 CD1 PHE A 258 -6.116 8.963 25.643 1.00 22.77 C ANISOU 2678 CD1 PHE A 258 2241 3083 3327 88 -388 27 C ATOM 2679 CD2 PHE A 258 -6.746 7.575 23.812 1.00 17.92 C ANISOU 2679 CD2 PHE A 258 1648 2484 2676 81 -297 27 C ATOM 2680 CE1 PHE A 258 -6.463 7.962 26.527 1.00 23.77 C ANISOU 2680 CE1 PHE A 258 2334 3230 3466 144 -401 19 C ATOM 2681 CE2 PHE A 258 -7.095 6.570 24.690 1.00 22.26 C ANISOU 2681 CE2 PHE A 258 2166 3053 3240 135 -312 19 C ATOM 2682 CZ PHE A 258 -6.953 6.763 26.052 1.00 23.32 C ANISOU 2682 CZ PHE A 258 2274 3191 3396 166 -361 16 C ATOM 2683 N CYS A 259 -6.341 12.811 21.696 1.00 21.44 N ANISOU 2683 N CYS A 259 2290 2818 3039 -112 -351 78 N ATOM 2684 CA CYS A 259 -5.650 13.860 20.944 1.00 23.45 C ANISOU 2684 CA CYS A 259 2570 3049 3290 -182 -339 92 C ATOM 2685 C CYS A 259 -6.568 15.068 20.787 1.00 25.06 C ANISOU 2685 C CYS A 259 2864 3213 3446 -186 -389 105 C ATOM 2686 O CYS A 259 -7.100 15.319 19.695 1.00 23.56 O ANISOU 2686 O CYS A 259 2728 3010 3213 -207 -367 117 O ATOM 2687 CB CYS A 259 -5.180 13.361 19.579 1.00 25.61 C ANISOU 2687 CB CYS A 259 2836 3339 3557 -224 -262 98 C ATOM 2688 SG CYS A 259 -4.147 14.579 18.726 1.00 34.51 S ANISOU 2688 SG CYS A 259 3981 4446 4686 -316 -242 119 S ATOM 2689 N PRO A 260 -6.761 15.854 21.849 1.00 26.10 N ANISOU 2689 N PRO A 260 3015 3321 3582 -164 -456 103 N ATOM 2690 CA PRO A 260 -7.562 17.083 21.710 1.00 30.91 C ANISOU 2690 CA PRO A 260 3712 3886 4145 -165 -505 115 C ATOM 2691 C PRO A 260 -6.956 18.097 20.756 1.00 35.17 C ANISOU 2691 C PRO A 260 4292 4396 4675 -243 -492 134 C ATOM 2692 O PRO A 260 -7.661 19.022 20.332 1.00 34.81 O ANISOU 2692 O PRO A 260 4326 4314 4586 -249 -521 146 O ATOM 2693 CB PRO A 260 -7.623 17.630 23.144 1.00 35.89 C ANISOU 2693 CB PRO A 260 4345 4500 4790 -127 -575 105 C ATOM 2694 CG PRO A 260 -6.431 17.042 23.829 1.00 31.80 C ANISOU 2694 CG PRO A 260 3743 4008 4332 -140 -563 94 C ATOM 2695 CD PRO A 260 -6.243 15.682 23.218 1.00 28.23 C ANISOU 2695 CD PRO A 260 3232 3600 3895 -135 -493 89 C ATOM 2696 N ASP A 261 -5.673 17.961 20.413 1.00 28.53 N ANISOU 2696 N ASP A 261 3398 3568 3873 -302 -451 137 N ATOM 2697 CA ASP A 261 -5.051 18.812 19.407 1.00 35.63 C ANISOU 2697 CA ASP A 261 4329 4446 4763 -382 -429 159 C ATOM 2698 C ASP A 261 -5.302 18.326 17.985 1.00 34.66 C ANISOU 2698 C ASP A 261 4224 4339 4607 -404 -362 168 C ATOM 2699 O ASP A 261 -5.021 19.068 17.037 1.00 31.21 O ANISOU 2699 O ASP A 261 3828 3880 4148 -466 -344 188 O ATOM 2700 CB ASP A 261 -3.542 18.898 19.649 1.00 37.91 C ANISOU 2700 CB ASP A 261 4548 4748 5108 -439 -412 162 C ATOM 2701 CG ASP A 261 -3.199 19.531 20.981 1.00 43.50 C ANISOU 2701 CG ASP A 261 5247 5434 5846 -431 -484 156 C ATOM 2702 OD1 ASP A 261 -3.960 20.411 21.435 1.00 48.06 O ANISOU 2702 OD1 ASP A 261 5898 5969 6393 -408 -548 156 O ATOM 2703 OD2 ASP A 261 -2.168 19.148 21.573 1.00 49.73 O ANISOU 2703 OD2 ASP A 261 5958 6249 6688 -445 -477 150 O ATOM 2704 N CYS A 262 -5.806 17.107 17.815 1.00 28.78 N ANISOU 2704 N CYS A 262 3452 3628 3856 -357 -325 154 N ATOM 2705 CA CYS A 262 -6.137 16.596 16.493 1.00 26.63 C ANISOU 2705 CA CYS A 262 3203 3368 3546 -373 -267 161 C ATOM 2706 C CYS A 262 -7.515 17.088 16.070 1.00 30.08 C ANISOU 2706 C CYS A 262 3728 3779 3923 -350 -301 170 C ATOM 2707 O CYS A 262 -8.430 17.198 16.891 1.00 26.91 O ANISOU 2707 O CYS A 262 3346 3367 3511 -293 -356 164 O ATOM 2708 CB CYS A 262 -6.120 15.065 16.484 1.00 31.95 C ANISOU 2708 CB CYS A 262 3817 4086 4237 -333 -218 142 C ATOM 2709 SG CYS A 262 -4.512 14.280 16.753 1.00 39.64 S ANISOU 2709 SG CYS A 262 4684 5099 5278 -354 -163 131 S ATOM 2710 N SER A 263 -7.659 17.387 14.783 1.00 28.61 N ANISOU 2710 N SER A 263 3594 3581 3696 -393 -268 187 N ATOM 2711 CA SER A 263 -8.978 17.677 14.241 1.00 27.63 C ANISOU 2711 CA SER A 263 3547 3438 3513 -370 -293 197 C ATOM 2712 C SER A 263 -9.859 16.438 14.338 1.00 25.02 C ANISOU 2712 C SER A 263 3196 3139 3171 -310 -283 182 C ATOM 2713 O SER A 263 -9.401 15.312 14.126 1.00 19.95 O ANISOU 2713 O SER A 263 2502 2530 2549 -308 -230 169 O ATOM 2714 CB SER A 263 -8.872 18.132 12.786 1.00 28.59 C ANISOU 2714 CB SER A 263 3725 3545 3594 -431 -255 218 C ATOM 2715 OG SER A 263 -8.201 19.376 12.688 1.00 38.92 O ANISOU 2715 OG SER A 263 5062 4818 4906 -489 -273 236 O ATOM 2716 N HIS A 264 -11.129 16.646 14.669 1.00 21.91 N ANISOU 2716 N HIS A 264 2844 2735 2745 -259 -334 186 N ATOM 2717 CA HIS A 264 -12.057 15.529 14.754 1.00 22.51 C ANISOU 2717 CA HIS A 264 2905 2841 2808 -207 -330 177 C ATOM 2718 C HIS A 264 -12.182 14.851 13.394 1.00 22.30 C ANISOU 2718 C HIS A 264 2898 2826 2747 -237 -274 181 C ATOM 2719 O HIS A 264 -12.189 15.513 12.352 1.00 25.23 O ANISOU 2719 O HIS A 264 3326 3177 3083 -283 -261 198 O ATOM 2720 CB HIS A 264 -13.425 16.018 15.231 1.00 23.14 C ANISOU 2720 CB HIS A 264 3030 2910 2855 -153 -395 187 C ATOM 2721 CG HIS A 264 -14.335 14.924 15.700 1.00 20.11 C ANISOU 2721 CG HIS A 264 2615 2559 2467 -94 -403 179 C ATOM 2722 ND1 HIS A 264 -14.834 13.956 14.856 1.00 19.38 N ANISOU 2722 ND1 HIS A 264 2526 2488 2350 -97 -369 181 N ATOM 2723 CD2 HIS A 264 -14.844 14.654 16.925 1.00 21.53 C ANISOU 2723 CD2 HIS A 264 2762 2755 2664 -32 -442 172 C ATOM 2724 CE1 HIS A 264 -15.607 13.133 15.542 1.00 22.16 C ANISOU 2724 CE1 HIS A 264 2847 2868 2706 -43 -388 176 C ATOM 2725 NE2 HIS A 264 -15.630 13.534 16.800 1.00 19.98 N ANISOU 2725 NE2 HIS A 264 2547 2591 2455 -3 -431 172 N ATOM 2726 N ALA A 265 -12.264 13.526 13.407 1.00 21.02 N ANISOU 2726 N ALA A 265 2694 2696 2596 -213 -242 166 N ATOM 2727 CA ALA A 265 -12.487 12.790 12.172 1.00 21.17 C ANISOU 2727 CA ALA A 265 2739 2727 2580 -235 -194 167 C ATOM 2728 C ALA A 265 -13.668 13.400 11.419 1.00 19.38 C ANISOU 2728 C ALA A 265 2591 2481 2292 -238 -226 188 C ATOM 2729 O ALA A 265 -14.688 13.731 12.038 1.00 19.10 O ANISOU 2729 O ALA A 265 2571 2441 2243 -195 -284 197 O ATOM 2730 CB ALA A 265 -12.758 11.314 12.471 1.00 22.21 C ANISOU 2730 CB ALA A 265 2825 2888 2724 -196 -175 148 C ATOM 2731 N PRO A 266 -13.575 13.568 10.101 1.00 23.89 N ANISOU 2731 N PRO A 266 3212 3042 2823 -287 -190 199 N ATOM 2732 CA PRO A 266 -14.642 14.259 9.370 1.00 22.96 C ANISOU 2732 CA PRO A 266 3172 2904 2646 -292 -225 222 C ATOM 2733 C PRO A 266 -15.935 13.458 9.351 1.00 19.94 C ANISOU 2733 C PRO A 266 2800 2541 2237 -249 -250 224 C ATOM 2734 O PRO A 266 -15.961 12.250 9.594 1.00 16.64 O ANISOU 2734 O PRO A 266 2339 2150 1836 -228 -229 207 O ATOM 2735 CB PRO A 266 -14.066 14.417 7.959 1.00 25.34 C ANISOU 2735 CB PRO A 266 3517 3196 2915 -357 -170 230 C ATOM 2736 CG PRO A 266 -13.059 13.335 7.836 1.00 26.89 C ANISOU 2736 CG PRO A 266 3657 3418 3142 -369 -101 207 C ATOM 2737 CD PRO A 266 -12.485 13.137 9.207 1.00 26.80 C ANISOU 2737 CD PRO A 266 3569 3418 3195 -336 -115 191 C ATOM 2738 N LEU A 267 -17.024 14.165 9.037 1.00 22.35 N ANISOU 2738 N LEU A 267 3163 2831 2497 -239 -298 247 N ATOM 2739 CA LEU A 267 -18.349 13.556 9.090 1.00 20.10 C ANISOU 2739 CA LEU A 267 2884 2567 2185 -198 -333 255 C ATOM 2740 C LEU A 267 -18.442 12.334 8.184 1.00 24.11 C ANISOU 2740 C LEU A 267 3397 3093 2671 -219 -290 246 C ATOM 2741 O LEU A 267 -19.029 11.315 8.566 1.00 21.08 O ANISOU 2741 O LEU A 267 2982 2734 2293 -187 -299 239 O ATOM 2742 CB LEU A 267 -19.411 14.589 8.709 1.00 23.85 C ANISOU 2742 CB LEU A 267 3425 3023 2613 -189 -386 284 C ATOM 2743 CG LEU A 267 -20.856 14.090 8.627 1.00 26.82 C ANISOU 2743 CG LEU A 267 3811 3423 2956 -152 -425 299 C ATOM 2744 CD1 LEU A 267 -21.271 13.405 9.916 1.00 26.46 C ANISOU 2744 CD1 LEU A 267 3699 3408 2946 -93 -449 290 C ATOM 2745 CD2 LEU A 267 -21.796 15.240 8.312 1.00 30.60 C ANISOU 2745 CD2 LEU A 267 4351 3882 3392 -139 -478 329 C ATOM 2746 N TRP A 268 -17.874 12.412 6.978 1.00 23.02 N ANISOU 2746 N TRP A 268 3300 2941 2505 -274 -243 246 N ATOM 2747 CA TRP A 268 -17.991 11.289 6.053 1.00 26.36 C ANISOU 2747 CA TRP A 268 3739 3377 2899 -293 -203 237 C ATOM 2748 C TRP A 268 -17.273 10.053 6.581 1.00 20.74 C ANISOU 2748 C TRP A 268 2963 2687 2232 -278 -161 207 C ATOM 2749 O TRP A 268 -17.699 8.925 6.305 1.00 21.05 O ANISOU 2749 O TRP A 268 3002 2740 2258 -270 -151 198 O ATOM 2750 CB TRP A 268 -17.450 11.674 4.674 1.00 26.42 C ANISOU 2750 CB TRP A 268 3807 3367 2865 -354 -157 243 C ATOM 2751 CG TRP A 268 -15.982 11.958 4.641 1.00 27.51 C ANISOU 2751 CG TRP A 268 3918 3499 3035 -387 -100 231 C ATOM 2752 CD1 TRP A 268 -15.381 13.178 4.740 1.00 33.74 C ANISOU 2752 CD1 TRP A 268 4716 4266 3835 -413 -105 244 C ATOM 2753 CD2 TRP A 268 -14.927 11.003 4.487 1.00 27.11 C ANISOU 2753 CD2 TRP A 268 3826 3464 3010 -399 -31 205 C ATOM 2754 NE1 TRP A 268 -14.016 13.041 4.661 1.00 28.04 N ANISOU 2754 NE1 TRP A 268 3957 3551 3146 -444 -43 230 N ATOM 2755 CE2 TRP A 268 -13.712 11.714 4.507 1.00 26.25 C ANISOU 2755 CE2 TRP A 268 3696 3349 2929 -432 5 206 C ATOM 2756 CE3 TRP A 268 -14.893 9.613 4.339 1.00 28.21 C ANISOU 2756 CE3 TRP A 268 3944 3622 3151 -383 4 181 C ATOM 2757 CZ2 TRP A 268 -12.476 11.084 4.384 1.00 28.82 C ANISOU 2757 CZ2 TRP A 268 3976 3691 3285 -448 76 185 C ATOM 2758 CZ3 TRP A 268 -13.668 8.990 4.218 1.00 26.91 C ANISOU 2758 CZ3 TRP A 268 3740 3470 3016 -395 74 159 C ATOM 2759 CH2 TRP A 268 -12.475 9.724 4.240 1.00 32.05 C ANISOU 2759 CH2 TRP A 268 4364 4118 3694 -425 111 161 C ATOM 2760 N LEU A 269 -16.191 10.240 7.340 1.00 20.21 N ANISOU 2760 N LEU A 269 2840 2620 2218 -275 -139 193 N ATOM 2761 CA LEU A 269 -15.503 9.099 7.935 1.00 19.01 C ANISOU 2761 CA LEU A 269 2623 2489 2112 -254 -104 166 C ATOM 2762 C LEU A 269 -16.308 8.517 9.091 1.00 16.17 C ANISOU 2762 C LEU A 269 2221 2146 1776 -198 -153 164 C ATOM 2763 O LEU A 269 -16.327 7.295 9.289 1.00 16.32 O ANISOU 2763 O LEU A 269 2210 2181 1808 -179 -135 148 O ATOM 2764 CB LEU A 269 -14.108 9.512 8.407 1.00 17.72 C ANISOU 2764 CB LEU A 269 2411 2324 1999 -268 -70 155 C ATOM 2765 CG LEU A 269 -13.215 8.377 8.918 1.00 22.37 C ANISOU 2765 CG LEU A 269 2930 2934 2637 -250 -26 128 C ATOM 2766 CD1 LEU A 269 -13.037 7.305 7.857 1.00 27.46 C ANISOU 2766 CD1 LEU A 269 3597 3584 3254 -266 33 113 C ATOM 2767 CD2 LEU A 269 -11.860 8.909 9.360 1.00 23.44 C ANISOU 2767 CD2 LEU A 269 3016 3070 2821 -268 2 122 C ATOM 2768 N MET A 270 -16.971 9.374 9.872 1.00 14.13 N ANISOU 2768 N MET A 270 1963 1885 1522 -169 -213 181 N ATOM 2769 CA MET A 270 -17.873 8.876 10.905 1.00 16.57 C ANISOU 2769 CA MET A 270 2237 2214 1844 -116 -260 184 C ATOM 2770 C MET A 270 -18.964 8.012 10.290 1.00 13.92 C ANISOU 2770 C MET A 270 1930 1892 1469 -113 -271 193 C ATOM 2771 O MET A 270 -19.252 6.913 10.777 1.00 16.58 O ANISOU 2771 O MET A 270 2230 2248 1821 -88 -273 185 O ATOM 2772 CB MET A 270 -18.491 10.041 11.680 1.00 17.08 C ANISOU 2772 CB MET A 270 2309 2273 1909 -85 -321 203 C ATOM 2773 CG MET A 270 -17.488 10.954 12.367 1.00 20.10 C ANISOU 2773 CG MET A 270 2669 2638 2329 -88 -320 195 C ATOM 2774 SD MET A 270 -16.374 10.086 13.489 1.00 16.65 S ANISOU 2774 SD MET A 270 2146 2219 1961 -68 -292 167 S ATOM 2775 CE MET A 270 -17.534 9.297 14.606 1.00 17.35 C ANISOU 2775 CE MET A 270 2198 2337 2055 -1 -339 171 C ATOM 2776 N TYR A 271 -19.584 8.497 9.211 1.00 15.05 N ANISOU 2776 N TYR A 271 2138 2022 1557 -142 -281 212 N ATOM 2777 CA TYR A 271 -20.580 7.697 8.507 1.00 17.73 C ANISOU 2777 CA TYR A 271 2510 2373 1855 -148 -293 221 C ATOM 2778 C TYR A 271 -19.996 6.355 8.081 1.00 19.40 C ANISOU 2778 C TYR A 271 2711 2587 2073 -165 -240 196 C ATOM 2779 O TYR A 271 -20.610 5.302 8.287 1.00 15.81 O ANISOU 2779 O TYR A 271 2241 2148 1617 -149 -254 194 O ATOM 2780 CB TYR A 271 -21.103 8.457 7.282 1.00 23.08 C ANISOU 2780 CB TYR A 271 3263 3033 2472 -184 -303 243 C ATOM 2781 CG TYR A 271 -22.050 9.608 7.569 1.00 22.29 C ANISOU 2781 CG TYR A 271 3183 2931 2354 -160 -366 273 C ATOM 2782 CD1 TYR A 271 -22.823 9.642 8.724 1.00 24.43 C ANISOU 2782 CD1 TYR A 271 3412 3224 2646 -105 -416 284 C ATOM 2783 CD2 TYR A 271 -22.182 10.656 6.665 1.00 27.03 C ANISOU 2783 CD2 TYR A 271 3849 3508 2913 -190 -374 291 C ATOM 2784 CE1 TYR A 271 -23.691 10.691 8.973 1.00 26.47 C ANISOU 2784 CE1 TYR A 271 3691 3482 2886 -77 -470 310 C ATOM 2785 CE2 TYR A 271 -23.046 11.706 6.905 1.00 28.39 C ANISOU 2785 CE2 TYR A 271 4044 3676 3067 -163 -431 318 C ATOM 2786 CZ TYR A 271 -23.796 11.720 8.060 1.00 31.74 C ANISOU 2786 CZ TYR A 271 4424 4124 3513 -105 -478 327 C ATOM 2787 OH TYR A 271 -24.656 12.769 8.300 1.00 34.48 O ANISOU 2787 OH TYR A 271 4794 4467 3840 -72 -533 354 O ATOM 2788 N LEU A 272 -18.803 6.377 7.481 1.00 16.36 N ANISOU 2788 N LEU A 272 2334 2188 1695 -198 -179 176 N ATOM 2789 CA LEU A 272 -18.203 5.141 6.988 1.00 16.73 C ANISOU 2789 CA LEU A 272 2378 2235 1743 -211 -125 150 C ATOM 2790 C LEU A 272 -17.921 4.172 8.127 1.00 13.96 C ANISOU 2790 C LEU A 272 1957 1900 1446 -170 -123 132 C ATOM 2791 O LEU A 272 -18.187 2.970 8.011 1.00 13.29 O ANISOU 2791 O LEU A 272 1874 1820 1356 -163 -116 121 O ATOM 2792 CB LEU A 272 -16.917 5.452 6.222 1.00 17.58 C ANISOU 2792 CB LEU A 272 2499 2330 1850 -248 -56 136 C ATOM 2793 CG LEU A 272 -16.169 4.256 5.626 1.00 25.25 C ANISOU 2793 CG LEU A 272 3471 3301 2820 -257 9 107 C ATOM 2794 CD1 LEU A 272 -17.066 3.457 4.691 1.00 28.89 C ANISOU 2794 CD1 LEU A 272 3996 3756 3225 -271 2 108 C ATOM 2795 CD2 LEU A 272 -14.922 4.726 4.893 1.00 28.42 C ANISOU 2795 CD2 LEU A 272 3881 3696 3220 -293 77 98 C ATOM 2796 N ALA A 273 -17.375 4.673 9.238 1.00 13.52 N ANISOU 2796 N ALA A 273 1845 1852 1442 -144 -133 130 N ATOM 2797 CA ALA A 273 -17.065 3.796 10.359 1.00 13.94 C ANISOU 2797 CA ALA A 273 1831 1919 1545 -105 -133 114 C ATOM 2798 C ALA A 273 -18.328 3.238 11.001 1.00 12.06 C ANISOU 2798 C ALA A 273 1584 1698 1301 -73 -189 129 C ATOM 2799 O ALA A 273 -18.322 2.101 11.486 1.00 11.96 O ANISOU 2799 O ALA A 273 1539 1694 1310 -52 -184 117 O ATOM 2800 CB ALA A 273 -16.230 4.543 11.398 1.00 14.95 C ANISOU 2800 CB ALA A 273 1905 2050 1725 -87 -136 110 C ATOM 2801 N ILE A 274 -19.412 4.015 11.017 1.00 13.84 N ANISOU 2801 N ILE A 274 1834 1927 1495 -68 -241 157 N ATOM 2802 CA ILE A 274 -20.668 3.523 11.578 1.00 14.16 C ANISOU 2802 CA ILE A 274 1863 1990 1527 -38 -294 176 C ATOM 2803 C ILE A 274 -21.258 2.439 10.686 1.00 13.51 C ANISOU 2803 C ILE A 274 1818 1906 1408 -63 -288 177 C ATOM 2804 O ILE A 274 -21.707 1.394 11.168 1.00 11.76 O ANISOU 2804 O ILE A 274 1572 1699 1198 -46 -303 177 O ATOM 2805 CB ILE A 274 -21.652 4.690 11.782 1.00 15.53 C ANISOU 2805 CB ILE A 274 2053 2171 1677 -23 -349 207 C ATOM 2806 CG1 ILE A 274 -21.182 5.571 12.941 1.00 14.20 C ANISOU 2806 CG1 ILE A 274 1843 2004 1548 11 -364 204 C ATOM 2807 CG2 ILE A 274 -23.058 4.162 12.042 1.00 16.73 C ANISOU 2807 CG2 ILE A 274 2199 2349 1807 -2 -399 232 C ATOM 2808 CD1 ILE A 274 -21.888 6.909 13.031 1.00 17.45 C ANISOU 2808 CD1 ILE A 274 2281 2413 1935 26 -410 229 C ATOM 2809 N AVAL A 275 -21.266 2.681 9.373 0.50 13.67 N ANISOU 2809 N AVAL A 275 1903 1909 1383 -105 -268 178 N ATOM 2810 N BVAL A 275 -21.268 2.657 9.369 0.50 13.19 N ANISOU 2810 N BVAL A 275 1841 1848 1322 -105 -268 177 N ATOM 2811 CA AVAL A 275 -21.782 1.700 8.423 0.50 15.30 C ANISOU 2811 CA AVAL A 275 2155 2109 1548 -133 -263 176 C ATOM 2812 CA BVAL A 275 -21.843 1.641 8.492 0.50 15.30 C ANISOU 2812 CA BVAL A 275 2153 2111 1550 -130 -266 177 C ATOM 2813 C AVAL A 275 -21.007 0.394 8.530 0.50 16.01 C ANISOU 2813 C AVAL A 275 2226 2191 1664 -129 -219 145 C ATOM 2814 C BVAL A 275 -21.007 0.367 8.524 0.50 13.85 C ANISOU 2814 C BVAL A 275 1953 1918 1391 -129 -218 145 C ATOM 2815 O AVAL A 275 -21.587 -0.698 8.488 0.50 14.37 O ANISOU 2815 O AVAL A 275 2027 1987 1447 -130 -234 145 O ATOM 2816 O BVAL A 275 -21.552 -0.738 8.434 0.50 14.32 O ANISOU 2816 O BVAL A 275 2023 1979 1440 -131 -231 144 O ATOM 2817 CB AVAL A 275 -21.727 2.281 6.997 0.50 17.82 C ANISOU 2817 CB AVAL A 275 2549 2408 1814 -178 -243 179 C ATOM 2818 CB BVAL A 275 -22.007 2.175 7.056 0.50 18.03 C ANISOU 2818 CB BVAL A 275 2575 2438 1836 -176 -255 184 C ATOM 2819 CG1AVAL A 275 -21.749 1.175 5.962 0.50 19.22 C ANISOU 2819 CG1AVAL A 275 2777 2572 1955 -210 -215 164 C ATOM 2820 CG1BVAL A 275 -22.990 3.338 7.034 0.50 17.70 C ANISOU 2820 CG1BVAL A 275 2552 2406 1769 -172 -310 219 C ATOM 2821 CG2AVAL A 275 -22.879 3.250 6.776 0.50 18.18 C ANISOU 2821 CG2AVAL A 275 2623 2462 1822 -181 -301 216 C ATOM 2822 CG2BVAL A 275 -20.670 2.586 6.469 0.50 17.49 C ANISOU 2822 CG2BVAL A 275 2522 2350 1774 -199 -189 161 C ATOM 2823 N LEU A 276 -19.683 0.484 8.663 1.00 13.78 N ANISOU 2823 N LEU A 276 1918 1900 1417 -126 -165 119 N ATOM 2824 CA LEU A 276 -18.859 -0.715 8.777 1.00 15.11 C ANISOU 2824 CA LEU A 276 2066 2061 1613 -116 -119 88 C ATOM 2825 C LEU A 276 -19.226 -1.511 10.024 1.00 14.18 C ANISOU 2825 C LEU A 276 1894 1960 1536 -76 -153 91 C ATOM 2826 O LEU A 276 -19.372 -2.737 9.972 1.00 10.84 O ANISOU 2826 O LEU A 276 1478 1530 1111 -73 -148 80 O ATOM 2827 CB LEU A 276 -17.378 -0.338 8.798 1.00 17.46 C ANISOU 2827 CB LEU A 276 2336 2354 1946 -116 -59 65 C ATOM 2828 CG LEU A 276 -16.405 -1.512 8.935 1.00 18.40 C ANISOU 2828 CG LEU A 276 2428 2467 2097 -99 -7 33 C ATOM 2829 CD1 LEU A 276 -16.522 -2.445 7.743 1.00 24.56 C ANISOU 2829 CD1 LEU A 276 3275 3228 2830 -122 24 18 C ATOM 2830 CD2 LEU A 276 -14.981 -1.012 9.082 1.00 24.18 C ANISOU 2830 CD2 LEU A 276 3117 3201 2868 -96 46 17 C ATOM 2831 N ALA A 277 -19.375 -0.827 11.161 1.00 13.06 N ANISOU 2831 N ALA A 277 1698 1836 1427 -46 -188 106 N ATOM 2832 CA ALA A 277 -19.772 -1.518 12.382 1.00 10.81 C ANISOU 2832 CA ALA A 277 1361 1569 1176 -8 -221 112 C ATOM 2833 C ALA A 277 -21.098 -2.244 12.191 1.00 13.70 C ANISOU 2833 C ALA A 277 1753 1943 1508 -16 -265 134 C ATOM 2834 O ALA A 277 -21.245 -3.402 12.595 1.00 10.22 O ANISOU 2834 O ALA A 277 1297 1504 1082 -5 -270 129 O ATOM 2835 CB ALA A 277 -19.868 -0.526 13.541 1.00 12.81 C ANISOU 2835 CB ALA A 277 1566 1843 1460 25 -256 127 C ATOM 2836 N HIS A 278 -22.072 -1.582 11.563 1.00 11.94 N ANISOU 2836 N HIS A 278 1570 1726 1239 -37 -299 160 N ATOM 2837 CA HIS A 278 -23.373 -2.208 11.371 1.00 12.07 C ANISOU 2837 CA HIS A 278 1608 1755 1223 -48 -345 185 C ATOM 2838 C HIS A 278 -23.309 -3.371 10.387 1.00 14.01 C ANISOU 2838 C HIS A 278 1906 1976 1441 -83 -322 168 C ATOM 2839 O HIS A 278 -24.097 -4.315 10.504 1.00 13.19 O ANISOU 2839 O HIS A 278 1807 1878 1328 -89 -354 181 O ATOM 2840 CB HIS A 278 -24.387 -1.164 10.906 1.00 15.31 C ANISOU 2840 CB HIS A 278 2047 2179 1592 -60 -387 218 C ATOM 2841 CG HIS A 278 -24.735 -0.158 11.959 1.00 16.09 C ANISOU 2841 CG HIS A 278 2098 2304 1712 -20 -421 239 C ATOM 2842 ND1 HIS A 278 -25.337 1.047 11.667 1.00 17.35 N ANISOU 2842 ND1 HIS A 278 2278 2470 1842 -19 -450 263 N ATOM 2843 CD2 HIS A 278 -24.566 -0.178 13.302 1.00 16.63 C ANISOU 2843 CD2 HIS A 278 2102 2391 1824 24 -432 239 C ATOM 2844 CE1 HIS A 278 -25.521 1.728 12.785 1.00 17.85 C ANISOU 2844 CE1 HIS A 278 2295 2554 1931 25 -476 275 C ATOM 2845 NE2 HIS A 278 -25.063 1.006 13.793 1.00 15.84 N ANISOU 2845 NE2 HIS A 278 1988 2308 1720 51 -466 261 N ATOM 2846 N ATHR A 279 -22.384 -3.324 9.427 0.50 15.70 N ANISOU 2846 N ATHR A 279 2161 2162 1640 -106 -267 140 N ATOM 2847 N BTHR A 279 -22.389 -3.334 9.416 0.50 15.29 N ANISOU 2847 N BTHR A 279 2111 2111 1589 -106 -267 140 N ATOM 2848 CA ATHR A 279 -22.259 -4.414 8.469 0.50 16.48 C ANISOU 2848 CA ATHR A 279 2318 2235 1710 -135 -241 120 C ATOM 2849 CA BTHR A 279 -22.292 -4.440 8.466 0.50 16.49 C ANISOU 2849 CA BTHR A 279 2319 2235 1710 -135 -243 120 C ATOM 2850 C ATHR A 279 -21.887 -5.729 9.140 0.50 12.54 C ANISOU 2850 C ATHR A 279 1790 1727 1246 -112 -230 101 C ATOM 2851 C BTHR A 279 -21.889 -5.742 9.141 0.50 13.98 C ANISOU 2851 C BTHR A 279 1972 1909 1429 -112 -230 101 C ATOM 2852 O ATHR A 279 -22.117 -6.796 8.561 0.50 14.33 O ANISOU 2852 O ATHR A 279 2063 1932 1448 -132 -228 91 O ATOM 2853 O BTHR A 279 -22.087 -6.814 8.560 0.50 14.37 O ANISOU 2853 O BTHR A 279 2068 1937 1453 -131 -227 90 O ATOM 2854 CB ATHR A 279 -21.216 -4.067 7.407 0.50 19.61 C ANISOU 2854 CB ATHR A 279 2758 2607 2086 -156 -177 92 C ATOM 2855 CB BTHR A 279 -21.287 -4.137 7.349 0.50 19.65 C ANISOU 2855 CB BTHR A 279 2768 2612 2088 -158 -179 93 C ATOM 2856 OG1ATHR A 279 -21.607 -2.871 6.720 0.50 19.09 O ANISOU 2856 OG1ATHR A 279 2725 2544 1982 -181 -190 112 O ATOM 2857 OG1BTHR A 279 -20.022 -3.776 7.915 0.50 20.83 O ANISOU 2857 OG1BTHR A 279 2866 2762 2286 -132 -131 71 O ATOM 2858 CG2ATHR A 279 -21.092 -5.200 6.414 0.50 21.86 C ANISOU 2858 CG2ATHR A 279 3108 2863 2335 -180 -149 69 C ATOM 2859 CG2BTHR A 279 -21.794 -3.023 6.446 0.50 19.58 C ANISOU 2859 CG2BTHR A 279 2807 2604 2030 -190 -194 113 C ATOM 2860 N ASN A 280 -21.318 -5.679 10.345 1.00 13.13 N ANISOU 2860 N ASN A 280 1794 1816 1379 -71 -224 96 N ATOM 2861 CA ASN A 280 -21.001 -6.910 11.056 1.00 14.53 C ANISOU 2861 CA ASN A 280 1944 1987 1592 -47 -218 81 C ATOM 2862 C ASN A 280 -22.256 -7.726 11.310 1.00 14.53 C ANISOU 2862 C ASN A 280 1952 1993 1574 -57 -275 108 C ATOM 2863 O ASN A 280 -22.191 -8.955 11.410 1.00 14.03 O ANISOU 2863 O ASN A 280 1901 1911 1519 -56 -273 96 O ATOM 2864 CB ASN A 280 -20.301 -6.600 12.378 1.00 15.37 C ANISOU 2864 CB ASN A 280 1969 2111 1759 -3 -212 77 C ATOM 2865 CG ASN A 280 -19.921 -7.854 13.139 1.00 15.57 C ANISOU 2865 CG ASN A 280 1965 2128 1823 25 -205 63 C ATOM 2866 OD1 ASN A 280 -20.498 -8.165 14.180 1.00 20.31 O ANISOU 2866 OD1 ASN A 280 2525 2747 2445 46 -247 84 O ATOM 2867 ND2 ASN A 280 -18.959 -8.595 12.606 1.00 19.39 N ANISOU 2867 ND2 ASN A 280 2472 2583 2313 26 -152 29 N ATOM 2868 N SER A 281 -23.405 -7.064 11.418 1.00 12.12 N ANISOU 2868 N SER A 281 1643 1716 1247 -68 -329 146 N ATOM 2869 CA SER A 281 -24.660 -7.777 11.606 1.00 17.41 C ANISOU 2869 CA SER A 281 2317 2399 1898 -82 -386 177 C ATOM 2870 C SER A 281 -25.136 -8.490 10.342 1.00 17.19 C ANISOU 2870 C SER A 281 2370 2344 1817 -132 -392 174 C ATOM 2871 O SER A 281 -26.172 -9.161 10.386 1.00 16.08 O ANISOU 2871 O SER A 281 2240 2211 1659 -153 -441 200 O ATOM 2872 CB SER A 281 -25.729 -6.799 12.094 1.00 14.92 C ANISOU 2872 CB SER A 281 1967 2126 1574 -74 -438 220 C ATOM 2873 OG SER A 281 -25.331 -6.182 13.312 1.00 17.32 O ANISOU 2873 OG SER A 281 2202 2453 1923 -27 -436 222 O ATOM 2874 N VAL A 282 -24.408 -8.372 9.231 1.00 16.87 N ANISOU 2874 N VAL A 282 2388 2272 1751 -151 -344 143 N ATOM 2875 CA VAL A 282 -24.785 -9.021 7.982 1.00 15.51 C ANISOU 2875 CA VAL A 282 2300 2070 1523 -197 -348 136 C ATOM 2876 C VAL A 282 -23.916 -10.238 7.687 1.00 18.99 C ANISOU 2876 C VAL A 282 2777 2469 1969 -194 -302 95 C ATOM 2877 O VAL A 282 -24.362 -11.143 6.963 1.00 21.20 O ANISOU 2877 O VAL A 282 3123 2721 2211 -227 -318 90 O ATOM 2878 CB VAL A 282 -24.684 -8.020 6.811 1.00 16.54 C ANISOU 2878 CB VAL A 282 2483 2195 1608 -224 -328 133 C ATOM 2879 CG1 VAL A 282 -25.035 -8.694 5.505 1.00 19.48 C ANISOU 2879 CG1 VAL A 282 2948 2535 1919 -270 -330 123 C ATOM 2880 CG2 VAL A 282 -25.586 -6.820 7.058 1.00 15.36 C ANISOU 2880 CG2 VAL A 282 2304 2083 1450 -224 -376 174 C ATOM 2881 N VAL A 283 -22.698 -10.294 8.232 1.00 14.40 N ANISOU 2881 N VAL A 283 2155 1881 1435 -154 -249 65 N ATOM 2882 CA VAL A 283 -21.708 -11.222 7.697 1.00 20.28 C ANISOU 2882 CA VAL A 283 2942 2586 2178 -147 -192 21 C ATOM 2883 C VAL A 283 -21.843 -12.628 8.277 1.00 19.16 C ANISOU 2883 C VAL A 283 2800 2423 2057 -135 -211 16 C ATOM 2884 O VAL A 283 -21.506 -13.605 7.601 1.00 23.47 O ANISOU 2884 O VAL A 283 3409 2928 2580 -143 -186 -13 O ATOM 2885 CB VAL A 283 -20.287 -10.678 7.922 1.00 19.96 C ANISOU 2885 CB VAL A 283 2858 2548 2177 -111 -124 -7 C ATOM 2886 CG1 VAL A 283 -20.117 -9.349 7.224 1.00 22.05 C ANISOU 2886 CG1 VAL A 283 3134 2827 2416 -131 -104 -2 C ATOM 2887 CG2 VAL A 283 -19.970 -10.554 9.404 1.00 17.13 C ANISOU 2887 CG2 VAL A 283 2406 2216 1886 -68 -135 2 C ATOM 2888 N ASN A 284 -22.302 -12.771 9.525 1.00 17.27 N ANISOU 2888 N ASN A 284 2495 2209 1859 -115 -254 42 N ATOM 2889 CA ASN A 284 -22.297 -14.092 10.153 1.00 20.03 C ANISOU 2889 CA ASN A 284 2841 2537 2233 -100 -268 37 C ATOM 2890 C ASN A 284 -23.065 -15.138 9.355 1.00 19.61 C ANISOU 2890 C ASN A 284 2872 2448 2131 -144 -300 39 C ATOM 2891 O ASN A 284 -22.541 -16.252 9.177 1.00 21.53 O ANISOU 2891 O ASN A 284 3156 2649 2376 -135 -277 9 O ATOM 2892 CB ASN A 284 -22.831 -13.981 11.583 1.00 22.27 C ANISOU 2892 CB ASN A 284 3043 2859 2560 -78 -314 72 C ATOM 2893 CG ASN A 284 -21.876 -13.248 12.500 1.00 22.96 C ANISOU 2893 CG ASN A 284 3053 2970 2701 -29 -281 62 C ATOM 2894 OD1 ASN A 284 -20.719 -13.011 12.146 1.00 20.23 O ANISOU 2894 OD1 ASN A 284 2709 2610 2368 -10 -221 27 O ATOM 2895 ND2 ASN A 284 -22.350 -12.889 13.686 1.00 26.48 N ANISOU 2895 ND2 ASN A 284 3430 3454 3178 -8 -319 93 N ATOM 2896 N PRO A 285 -24.278 -14.879 8.865 1.00 19.39 N ANISOU 2896 N PRO A 285 2874 2435 2060 -191 -354 72 N ATOM 2897 CA PRO A 285 -24.970 -15.907 8.069 1.00 20.94 C ANISOU 2897 CA PRO A 285 3155 2594 2208 -237 -387 73 C ATOM 2898 C PRO A 285 -24.154 -16.414 6.892 1.00 21.39 C ANISOU 2898 C PRO A 285 3300 2597 2229 -243 -333 24 C ATOM 2899 O PRO A 285 -24.258 -17.596 6.542 1.00 22.91 O ANISOU 2899 O PRO A 285 3558 2745 2401 -259 -344 9 O ATOM 2900 CB PRO A 285 -26.246 -15.188 7.612 1.00 21.31 C ANISOU 2900 CB PRO A 285 3211 2672 2213 -283 -445 116 C ATOM 2901 CG PRO A 285 -26.484 -14.157 8.651 1.00 21.90 C ANISOU 2901 CG PRO A 285 3190 2803 2326 -254 -460 148 C ATOM 2902 CD PRO A 285 -25.122 -13.691 9.079 1.00 20.55 C ANISOU 2902 CD PRO A 285 2978 2631 2199 -202 -392 113 C ATOM 2903 N PHE A 286 -23.335 -15.561 6.272 1.00 22.82 N ANISOU 2903 N PHE A 286 3488 2782 2400 -230 -274 -1 N ATOM 2904 CA PHE A 286 -22.513 -16.018 5.156 1.00 26.56 C ANISOU 2904 CA PHE A 286 4044 3211 2838 -230 -216 -47 C ATOM 2905 C PHE A 286 -21.388 -16.926 5.634 1.00 24.68 C ANISOU 2905 C PHE A 286 3793 2943 2641 -180 -165 -86 C ATOM 2906 O PHE A 286 -21.044 -17.904 4.959 1.00 24.14 O ANISOU 2906 O PHE A 286 3802 2825 2544 -180 -141 -119 O ATOM 2907 CB PHE A 286 -21.947 -14.823 4.392 1.00 26.45 C ANISOU 2907 CB PHE A 286 4035 3214 2803 -232 -165 -59 C ATOM 2908 CG PHE A 286 -22.966 -14.097 3.568 1.00 32.22 C ANISOU 2908 CG PHE A 286 4808 3958 3476 -283 -208 -30 C ATOM 2909 CD1 PHE A 286 -23.760 -13.115 4.133 1.00 28.90 C ANISOU 2909 CD1 PHE A 286 4327 3585 3071 -292 -256 15 C ATOM 2910 CD2 PHE A 286 -23.132 -14.400 2.226 1.00 27.97 C ANISOU 2910 CD2 PHE A 286 4373 3386 2869 -321 -201 -47 C ATOM 2911 CE1 PHE A 286 -24.701 -12.446 3.376 1.00 31.35 C ANISOU 2911 CE1 PHE A 286 4674 3908 3329 -336 -297 43 C ATOM 2912 CE2 PHE A 286 -24.072 -13.736 1.463 1.00 32.16 C ANISOU 2912 CE2 PHE A 286 4943 3930 3347 -369 -243 -18 C ATOM 2913 CZ PHE A 286 -24.858 -12.757 2.039 1.00 33.21 C ANISOU 2913 CZ PHE A 286 5011 4111 3498 -376 -292 27 C ATOM 2914 N ILE A 287 -20.803 -16.623 6.794 1.00 22.45 N ANISOU 2914 N ILE A 287 3417 2689 2425 -135 -150 -82 N ATOM 2915 CA ILE A 287 -19.756 -17.485 7.335 1.00 25.15 C ANISOU 2915 CA ILE A 287 3740 3006 2810 -84 -107 -114 C ATOM 2916 C ILE A 287 -20.311 -18.876 7.613 1.00 26.60 C ANISOU 2916 C ILE A 287 3965 3151 2990 -92 -151 -111 C ATOM 2917 O ILE A 287 -19.683 -19.890 7.285 1.00 29.76 O ANISOU 2917 O ILE A 287 4419 3504 3385 -71 -119 -148 O ATOM 2918 CB ILE A 287 -19.146 -16.856 8.601 1.00 27.73 C ANISOU 2918 CB ILE A 287 3955 3375 3208 -38 -94 -104 C ATOM 2919 CG1 ILE A 287 -18.583 -15.463 8.299 1.00 28.57 C ANISOU 2919 CG1 ILE A 287 4025 3515 3316 -35 -53 -106 C ATOM 2920 CG2 ILE A 287 -18.057 -17.756 9.173 1.00 26.46 C ANISOU 2920 CG2 ILE A 287 3772 3190 3093 16 -52 -136 C ATOM 2921 CD1 ILE A 287 -17.390 -15.458 7.360 1.00 35.81 C ANISOU 2921 CD1 ILE A 287 4978 4411 4217 -20 30 -149 C ATOM 2922 N TYR A 288 -21.500 -18.948 8.217 1.00 23.44 N ANISOU 2922 N TYR A 288 3543 2770 2592 -123 -227 -67 N ATOM 2923 CA TYR A 288 -22.112 -20.246 8.485 1.00 26.49 C ANISOU 2923 CA TYR A 288 3970 3121 2974 -140 -276 -58 C ATOM 2924 C TYR A 288 -22.369 -21.009 7.191 1.00 25.11 C ANISOU 2924 C TYR A 288 3915 2891 2734 -179 -279 -81 C ATOM 2925 O TYR A 288 -22.096 -22.212 7.104 1.00 27.05 O ANISOU 2925 O TYR A 288 4218 3083 2976 -169 -275 -106 O ATOM 2926 CB TYR A 288 -23.419 -20.063 9.257 1.00 23.08 C ANISOU 2926 CB TYR A 288 3491 2729 2551 -173 -355 0 C ATOM 2927 CG TYR A 288 -23.271 -19.310 10.558 1.00 24.03 C ANISOU 2927 CG TYR A 288 3498 2903 2729 -134 -357 24 C ATOM 2928 CD1 TYR A 288 -22.156 -19.488 11.365 1.00 25.56 C ANISOU 2928 CD1 TYR A 288 3640 3094 2978 -76 -313 0 C ATOM 2929 CD2 TYR A 288 -24.246 -18.415 10.976 1.00 22.72 C ANISOU 2929 CD2 TYR A 288 3279 2792 2562 -155 -404 71 C ATOM 2930 CE1 TYR A 288 -22.017 -18.798 12.554 1.00 24.06 C ANISOU 2930 CE1 TYR A 288 3352 2952 2838 -42 -318 21 C ATOM 2931 CE2 TYR A 288 -24.115 -17.718 12.162 1.00 19.88 C ANISOU 2931 CE2 TYR A 288 2822 2479 2251 -117 -406 91 C ATOM 2932 CZ TYR A 288 -23.000 -17.914 12.947 1.00 22.78 C ANISOU 2932 CZ TYR A 288 3145 2841 2671 -63 -364 66 C ATOM 2933 OH TYR A 288 -22.867 -17.224 14.127 1.00 19.68 O ANISOU 2933 OH TYR A 288 2660 2493 2323 -27 -369 84 O ATOM 2934 N ALA A 289 -22.901 -20.326 6.175 1.00 25.58 N ANISOU 2934 N ALA A 289 4019 2960 2739 -223 -288 -74 N ATOM 2935 CA ALA A 289 -23.231 -20.997 4.923 1.00 25.98 C ANISOU 2935 CA ALA A 289 4190 2961 2722 -265 -297 -94 C ATOM 2936 C ALA A 289 -21.983 -21.469 4.189 1.00 30.71 C ANISOU 2936 C ALA A 289 4851 3512 3305 -226 -217 -154 C ATOM 2937 O ALA A 289 -22.010 -22.519 3.538 1.00 33.28 O ANISOU 2937 O ALA A 289 5274 3780 3592 -239 -221 -180 O ATOM 2938 CB ALA A 289 -24.046 -20.065 4.028 1.00 29.47 C ANISOU 2938 CB ALA A 289 4660 3427 3109 -317 -325 -70 C ATOM 2939 N TYR A 290 -20.885 -20.718 4.280 1.00 30.88 N ANISOU 2939 N TYR A 290 4818 3559 3355 -179 -145 -175 N ATOM 2940 CA TYR A 290 -19.680 -21.085 3.545 1.00 35.15 C ANISOU 2940 CA TYR A 290 5411 4065 3881 -140 -62 -230 C ATOM 2941 C TYR A 290 -18.857 -22.146 4.265 1.00 37.41 C ANISOU 2941 C TYR A 290 5681 4319 4214 -82 -35 -257 C ATOM 2942 O TYR A 290 -18.154 -22.921 3.608 1.00 38.36 O ANISOU 2942 O TYR A 290 5873 4391 4310 -56 13 -302 O ATOM 2943 CB TYR A 290 -18.816 -19.847 3.295 1.00 44.73 C ANISOU 2943 CB TYR A 290 6570 5320 5104 -118 6 -239 C ATOM 2944 CG TYR A 290 -19.114 -19.146 1.989 1.00 53.79 C ANISOU 2944 CG TYR A 290 7786 6470 6182 -161 17 -241 C ATOM 2945 CD1 TYR A 290 -18.663 -19.667 0.783 1.00 67.85 C ANISOU 2945 CD1 TYR A 290 9669 8207 7904 -162 65 -282 C ATOM 2946 CD2 TYR A 290 -19.840 -17.964 1.960 1.00 52.63 C ANISOU 2946 CD2 TYR A 290 7604 6368 6026 -200 -19 -201 C ATOM 2947 CE1 TYR A 290 -18.930 -19.033 -0.414 1.00 72.29 C ANISOU 2947 CE1 TYR A 290 10296 8771 8398 -203 75 -283 C ATOM 2948 CE2 TYR A 290 -20.112 -17.322 0.767 1.00 58.87 C ANISOU 2948 CE2 TYR A 290 8459 7159 6751 -240 -10 -201 C ATOM 2949 CZ TYR A 290 -19.655 -17.861 -0.417 1.00 65.49 C ANISOU 2949 CZ TYR A 290 9398 7955 7531 -243 36 -242 C ATOM 2950 OH TYR A 290 -19.923 -17.225 -1.608 1.00 69.36 O ANISOU 2950 OH TYR A 290 9954 8445 7952 -283 44 -241 O ATOM 2951 N ARG A 291 -18.932 -22.211 5.597 1.00 32.67 N ANISOU 2951 N ARG A 291 4992 3743 3679 -60 -65 -231 N ATOM 2952 CA ARG A 291 -18.034 -23.062 6.365 1.00 31.45 C ANISOU 2952 CA ARG A 291 4808 3565 3575 2 -35 -255 C ATOM 2953 C ARG A 291 -18.716 -24.211 7.092 1.00 33.04 C ANISOU 2953 C ARG A 291 5029 3733 3792 -8 -102 -237 C ATOM 2954 O ARG A 291 -18.020 -25.128 7.539 1.00 35.32 O ANISOU 2954 O ARG A 291 5321 3987 4112 40 -80 -261 O ATOM 2955 CB ARG A 291 -17.265 -22.223 7.397 1.00 30.97 C ANISOU 2955 CB ARG A 291 4623 3559 3585 48 -4 -245 C ATOM 2956 CG ARG A 291 -16.258 -21.265 6.779 1.00 37.83 C ANISOU 2956 CG ARG A 291 5469 4454 4451 70 75 -269 C ATOM 2957 CD ARG A 291 -15.338 -20.658 7.828 1.00 35.74 C ANISOU 2957 CD ARG A 291 5088 4234 4259 119 107 -266 C ATOM 2958 NE ARG A 291 -14.609 -21.679 8.573 1.00 35.91 N ANISOU 2958 NE ARG A 291 5087 4230 4327 176 123 -285 N ATOM 2959 CZ ARG A 291 -13.471 -22.233 8.177 1.00 37.48 C ANISOU 2959 CZ ARG A 291 5306 4403 4531 226 193 -328 C ATOM 2960 NH1 ARG A 291 -12.890 -21.886 7.039 1.00 37.46 N ANISOU 2960 NH1 ARG A 291 5346 4399 4490 227 257 -356 N ATOM 2961 NH2 ARG A 291 -12.900 -23.161 8.941 1.00 36.88 N ANISOU 2961 NH2 ARG A 291 5207 4304 4500 279 198 -341 N ATOM 2962 N ILE A 292 -20.039 -24.195 7.228 1.00 26.93 N ANISOU 2962 N ILE A 292 4265 2969 2998 -69 -181 -194 N ATOM 2963 CA ILE A 292 -20.764 -25.223 7.967 1.00 32.94 C ANISOU 2963 CA ILE A 292 5036 3704 3774 -86 -249 -168 C ATOM 2964 C ILE A 292 -21.780 -25.843 7.019 1.00 35.05 C ANISOU 2964 C ILE A 292 5415 3929 3974 -154 -302 -162 C ATOM 2965 O ILE A 292 -22.763 -25.194 6.638 1.00 32.27 O ANISOU 2965 O ILE A 292 5065 3608 3588 -211 -346 -129 O ATOM 2966 CB ILE A 292 -21.444 -24.660 9.221 1.00 31.63 C ANISOU 2966 CB ILE A 292 4764 3599 3654 -95 -300 -114 C ATOM 2967 CG1 ILE A 292 -20.448 -23.824 10.030 1.00 31.46 C ANISOU 2967 CG1 ILE A 292 4637 3624 3692 -34 -247 -121 C ATOM 2968 CG2 ILE A 292 -21.993 -25.797 10.075 1.00 32.65 C ANISOU 2968 CG2 ILE A 292 4899 3702 3805 -105 -358 -90 C ATOM 2969 CD1 ILE A 292 -21.036 -23.192 11.270 1.00 29.05 C ANISOU 2969 CD1 ILE A 292 4229 3378 3430 -36 -291 -72 C ATOM 2970 N ARG A 293 -21.552 -27.106 6.649 1.00 37.34 N ANISOU 2970 N ARG A 293 5799 4147 4243 -148 -302 -193 N ATOM 2971 CA ARG A 293 -22.411 -27.761 5.667 1.00 39.47 C ANISOU 2971 CA ARG A 293 6186 4366 4443 -212 -351 -194 C ATOM 2972 C ARG A 293 -23.840 -27.898 6.179 1.00 34.73 C ANISOU 2972 C ARG A 293 5567 3786 3841 -281 -449 -133 C ATOM 2973 O ARG A 293 -24.798 -27.691 5.425 1.00 37.20 O ANISOU 2973 O ARG A 293 5930 4103 4103 -348 -496 -112 O ATOM 2974 CB ARG A 293 -21.838 -29.133 5.309 1.00 45.63 C ANISOU 2974 CB ARG A 293 7070 5060 5206 -185 -334 -240 C ATOM 2975 CG ARG A 293 -22.545 -29.821 4.149 1.00 51.49 C ANISOU 2975 CG ARG A 293 7951 5741 5870 -246 -375 -252 C ATOM 2976 CD ARG A 293 -21.882 -31.145 3.788 1.00 64.95 C ANISOU 2976 CD ARG A 293 9765 7357 7557 -210 -352 -303 C ATOM 2977 NE ARG A 293 -20.491 -30.974 3.382 1.00 86.52 N ANISOU 2977 NE ARG A 293 12500 10081 10293 -130 -250 -360 N ATOM 2978 CZ ARG A 293 -19.720 -31.947 2.915 1.00 91.31 C ANISOU 2978 CZ ARG A 293 13198 10616 10879 -83 -208 -413 C ATOM 2979 NH1 ARG A 293 -20.173 -33.182 2.770 1.00 91.42 N ANISOU 2979 NH1 ARG A 293 13317 10552 10864 -107 -261 -421 N ATOM 2980 NH2 ARG A 293 -18.462 -31.673 2.582 1.00 92.89 N ANISOU 2980 NH2 ARG A 293 13385 10824 11087 -9 -112 -459 N ATOM 2981 N GLU A 294 -24.007 -28.249 7.456 1.00 36.74 N ANISOU 2981 N GLU A 294 5749 4057 4153 -267 -480 -101 N ATOM 2982 CA GLU A 294 -25.352 -28.438 7.990 1.00 36.13 C ANISOU 2982 CA GLU A 294 5649 4002 4075 -331 -570 -40 C ATOM 2983 C GLU A 294 -26.167 -27.154 7.894 1.00 34.45 C ANISOU 2983 C GLU A 294 5372 3867 3852 -368 -594 2 C ATOM 2984 O GLU A 294 -27.366 -27.193 7.595 1.00 33.06 O ANISOU 2984 O GLU A 294 5219 3701 3641 -438 -663 43 O ATOM 2985 CB GLU A 294 -25.280 -28.924 9.437 1.00 41.22 C ANISOU 2985 CB GLU A 294 6218 4660 4785 -301 -589 -13 C ATOM 2986 CG GLU A 294 -26.560 -29.583 9.926 1.00 45.26 C ANISOU 2986 CG GLU A 294 6734 5172 5292 -368 -681 44 C ATOM 2987 CD GLU A 294 -26.847 -30.896 9.221 1.00 48.84 C ANISOU 2987 CD GLU A 294 7318 5538 5702 -412 -719 28 C ATOM 2988 OE1 GLU A 294 -25.881 -31.595 8.849 1.00 51.35 O ANISOU 2988 OE1 GLU A 294 7707 5789 6014 -368 -673 -28 O ATOM 2989 OE2 GLU A 294 -28.037 -31.225 9.032 1.00 44.55 O ANISOU 2989 OE2 GLU A 294 6805 4993 5127 -490 -796 70 O ATOM 2990 N PHE A 295 -25.537 -26.005 8.146 1.00 31.88 N ANISOU 2990 N PHE A 295 4965 3593 3554 -322 -540 -5 N ATOM 2991 CA PHE A 295 -26.223 -24.732 7.948 1.00 30.90 C ANISOU 2991 CA PHE A 295 4790 3535 3415 -351 -557 29 C ATOM 2992 C PHE A 295 -26.486 -24.482 6.468 1.00 30.05 C ANISOU 2992 C PHE A 295 4776 3406 3237 -394 -555 11 C ATOM 2993 O PHE A 295 -27.594 -24.095 6.078 1.00 29.81 O ANISOU 2993 O PHE A 295 4754 3402 3171 -453 -612 50 O ATOM 2994 CB PHE A 295 -25.400 -23.588 8.543 1.00 28.03 C ANISOU 2994 CB PHE A 295 4329 3225 3098 -290 -499 21 C ATOM 2995 CG PHE A 295 -25.784 -23.227 9.949 1.00 24.59 C ANISOU 2995 CG PHE A 295 3780 2845 2716 -273 -529 66 C ATOM 2996 CD1 PHE A 295 -26.985 -22.586 10.209 1.00 23.60 C ANISOU 2996 CD1 PHE A 295 3609 2776 2582 -313 -587 122 C ATOM 2997 CD2 PHE A 295 -24.940 -23.513 11.007 1.00 27.56 C ANISOU 2997 CD2 PHE A 295 4098 3222 3151 -214 -498 54 C ATOM 2998 CE1 PHE A 295 -27.340 -22.247 11.502 1.00 23.49 C ANISOU 2998 CE1 PHE A 295 3496 2817 2614 -293 -611 163 C ATOM 2999 CE2 PHE A 295 -25.291 -23.174 12.302 1.00 25.89 C ANISOU 2999 CE2 PHE A 295 3789 3063 2986 -197 -526 95 C ATOM 3000 CZ PHE A 295 -26.491 -22.541 12.548 1.00 23.90 C ANISOU 3000 CZ PHE A 295 3494 2866 2721 -235 -581 148 C ATOM 3001 N ARG A 296 -25.471 -24.696 5.628 1.00 29.35 N ANISOU 3001 N ARG A 296 4757 3270 3124 -365 -489 -47 N ATOM 3002 CA ARG A 296 -25.626 -24.477 4.194 1.00 30.71 C ANISOU 3002 CA ARG A 296 5025 3419 3225 -402 -481 -68 C ATOM 3003 C ARG A 296 -26.788 -25.290 3.636 1.00 37.38 C ANISOU 3003 C ARG A 296 5958 4228 4018 -478 -562 -46 C ATOM 3004 O ARG A 296 -27.638 -24.764 2.907 1.00 33.94 O ANISOU 3004 O ARG A 296 5549 3811 3534 -533 -602 -21 O ATOM 3005 CB ARG A 296 -24.323 -24.832 3.476 1.00 35.79 C ANISOU 3005 CB ARG A 296 5735 4011 3852 -353 -397 -135 C ATOM 3006 CG ARG A 296 -24.386 -24.695 1.965 1.00 43.14 C ANISOU 3006 CG ARG A 296 6774 4913 4703 -387 -382 -162 C ATOM 3007 CD ARG A 296 -23.006 -24.793 1.325 1.00 53.46 C ANISOU 3007 CD ARG A 296 8126 6189 5999 -329 -284 -225 C ATOM 3008 NE ARG A 296 -22.302 -26.022 1.677 1.00 53.27 N ANISOU 3008 NE ARG A 296 8137 6107 5997 -283 -261 -260 N ATOM 3009 CZ ARG A 296 -21.301 -26.107 2.544 1.00 50.25 C ANISOU 3009 CZ ARG A 296 7680 5735 5679 -213 -209 -277 C ATOM 3010 NH1 ARG A 296 -20.847 -25.046 3.192 1.00 43.34 N ANISOU 3010 NH1 ARG A 296 6691 4924 4854 -181 -175 -262 N ATOM 3011 NH2 ARG A 296 -20.734 -27.290 2.765 1.00 58.43 N ANISOU 3011 NH2 ARG A 296 8761 6712 6728 -173 -193 -309 N ATOM 3012 N GLN A 297 -26.844 -26.580 3.972 1.00 33.76 N ANISOU 3012 N GLN A 297 5546 3715 3567 -483 -591 -52 N ATOM 3013 CA GLN A 297 -27.907 -27.433 3.449 1.00 35.26 C ANISOU 3013 CA GLN A 297 5825 3864 3709 -559 -672 -31 C ATOM 3014 C GLN A 297 -29.271 -27.004 3.974 1.00 33.06 C ANISOU 3014 C GLN A 297 5476 3647 3439 -619 -754 42 C ATOM 3015 O GLN A 297 -30.260 -27.025 3.234 1.00 34.31 O ANISOU 3015 O GLN A 297 5688 3803 3545 -690 -815 67 O ATOM 3016 CB GLN A 297 -27.627 -28.892 3.805 1.00 33.85 C ANISOU 3016 CB GLN A 297 5707 3613 3542 -549 -685 -52 C ATOM 3017 CG GLN A 297 -26.419 -29.476 3.089 1.00 44.16 C ANISOU 3017 CG GLN A 297 7106 4848 4825 -497 -612 -125 C ATOM 3018 CD GLN A 297 -26.100 -30.888 3.534 1.00 50.93 C ANISOU 3018 CD GLN A 297 8019 5632 5699 -477 -624 -145 C ATOM 3019 OE1 GLN A 297 -26.480 -31.309 4.628 1.00 50.24 O ANISOU 3019 OE1 GLN A 297 7873 5556 5660 -483 -668 -107 O ATOM 3020 NE2 GLN A 297 -25.400 -31.632 2.685 1.00 54.61 N ANISOU 3020 NE2 GLN A 297 8602 6022 6125 -453 -585 -205 N ATOM 3021 N THR A 298 -29.347 -26.611 5.246 1.00 32.86 N ANISOU 3021 N THR A 298 5329 3678 3476 -589 -758 78 N ATOM 3022 CA THR A 298 -30.626 -26.170 5.793 1.00 30.70 C ANISOU 3022 CA THR A 298 4981 3470 3212 -637 -830 148 C ATOM 3023 C THR A 298 -31.071 -24.862 5.152 1.00 27.59 C ANISOU 3023 C THR A 298 4562 3131 2788 -655 -831 166 C ATOM 3024 O THR A 298 -32.265 -24.664 4.898 1.00 29.09 O ANISOU 3024 O THR A 298 4749 3352 2950 -717 -900 215 O ATOM 3025 CB THR A 298 -30.528 -26.019 7.310 1.00 31.11 C ANISOU 3025 CB THR A 298 4914 3571 3337 -594 -827 179 C ATOM 3026 OG1 THR A 298 -29.983 -27.217 7.877 1.00 34.50 O ANISOU 3026 OG1 THR A 298 5370 3944 3793 -571 -820 158 O ATOM 3027 CG2 THR A 298 -31.903 -25.760 7.910 1.00 28.71 C ANISOU 3027 CG2 THR A 298 4539 3332 3040 -644 -904 254 C ATOM 3028 N PHE A 299 -30.127 -23.957 4.884 1.00 30.08 N ANISOU 3028 N PHE A 299 4858 3460 3109 -601 -756 129 N ATOM 3029 CA PHE A 299 -30.473 -22.707 4.215 1.00 29.79 C ANISOU 3029 CA PHE A 299 4807 3469 3042 -616 -753 143 C ATOM 3030 C PHE A 299 -31.115 -22.973 2.859 1.00 33.01 C ANISOU 3030 C PHE A 299 5326 3842 3373 -684 -793 140 C ATOM 3031 O PHE A 299 -32.095 -22.317 2.488 1.00 34.80 O ANISOU 3031 O PHE A 299 5529 4108 3585 -722 -831 182 O ATOM 3032 CB PHE A 299 -29.229 -21.832 4.050 1.00 27.00 C ANISOU 3032 CB PHE A 299 4431 3123 2703 -552 -662 98 C ATOM 3033 CG PHE A 299 -28.697 -21.252 5.339 1.00 26.50 C ANISOU 3033 CG PHE A 299 4250 3107 2712 -490 -629 108 C ATOM 3034 CD1 PHE A 299 -29.449 -21.265 6.505 1.00 24.96 C ANISOU 3034 CD1 PHE A 299 3969 2957 2558 -493 -680 159 C ATOM 3035 CD2 PHE A 299 -27.438 -20.675 5.373 1.00 26.87 C ANISOU 3035 CD2 PHE A 299 4271 3154 2783 -430 -547 66 C ATOM 3036 CE1 PHE A 299 -28.950 -20.722 7.676 1.00 27.34 C ANISOU 3036 CE1 PHE A 299 4168 3300 2921 -436 -651 165 C ATOM 3037 CE2 PHE A 299 -26.936 -20.130 6.541 1.00 27.62 C ANISOU 3037 CE2 PHE A 299 4261 3290 2942 -376 -521 74 C ATOM 3038 CZ PHE A 299 -27.692 -20.155 7.693 1.00 24.77 C ANISOU 3038 CZ PHE A 299 3822 2972 2619 -378 -573 122 C ATOM 3039 N ARG A 300 -30.576 -23.934 2.105 1.00 36.39 N ANISOU 3039 N ARG A 300 5867 4194 3766 -690 -773 91 N ATOM 3040 CA ARG A 300 -31.144 -24.256 0.799 1.00 43.61 C ANISOU 3040 CA ARG A 300 6898 5069 4603 -755 -811 84 C ATOM 3041 C ARG A 300 -32.570 -24.775 0.932 1.00 41.75 C ANISOU 3041 C ARG A 300 6631 4840 4392 -812 -883 149 C ATOM 3042 O ARG A 300 -33.478 -24.318 0.228 1.00 43.36 O ANISOU 3042 O ARG A 300 6823 5063 4590 -849 -901 182 O ATOM 3043 CB ARG A 300 -30.266 -25.282 0.084 1.00 47.73 C ANISOU 3043 CB ARG A 300 7541 5503 5092 -740 -769 19 C ATOM 3044 CG ARG A 300 -28.982 -24.705 -0.475 1.00 61.50 C ANISOU 3044 CG ARG A 300 9303 7237 6827 -678 -668 -38 C ATOM 3045 CD ARG A 300 -28.394 -25.609 -1.542 1.00 74.79 C ANISOU 3045 CD ARG A 300 11128 8838 8452 -678 -637 -97 C ATOM 3046 NE ARG A 300 -27.283 -24.975 -2.242 1.00 87.87 N ANISOU 3046 NE ARG A 300 12805 10493 10088 -628 -543 -146 N ATOM 3047 CZ ARG A 300 -27.406 -24.244 -3.343 1.00 91.50 C ANISOU 3047 CZ ARG A 300 13315 10962 10487 -654 -531 -152 C ATOM 3048 NH1 ARG A 300 -28.588 -24.001 -3.887 1.00 89.92 N ANISOU 3048 NH1 ARG A 300 13135 10777 10253 -722 -602 -108 N ATOM 3049 NH2 ARG A 300 -26.313 -23.745 -3.913 1.00 93.67 N ANISOU 3049 NH2 ARG A 300 13607 11235 10748 -607 -439 -196 N ATOM 3050 N LYS A 301 -32.787 -25.739 1.829 1.00 39.99 N ANISOU 3050 N LYS A 301 6392 4601 4201 -821 -921 166 N ATOM 3051 CA LYS A 301 -34.130 -26.270 2.035 1.00 42.41 C ANISOU 3051 CA LYS A 301 6662 4916 4536 -875 -981 229 C ATOM 3052 C LYS A 301 -35.122 -25.149 2.324 1.00 43.81 C ANISOU 3052 C LYS A 301 6715 5176 4756 -879 -986 285 C ATOM 3053 O LYS A 301 -36.201 -25.087 1.724 1.00 47.75 O ANISOU 3053 O LYS A 301 7210 5681 5253 -926 -1015 320 O ATOM 3054 CB LYS A 301 -34.121 -27.289 3.176 1.00 43.51 C ANISOU 3054 CB LYS A 301 6781 5039 4712 -875 -1012 243 C ATOM 3055 CG LYS A 301 -33.547 -28.647 2.796 1.00 50.27 C ANISOU 3055 CG LYS A 301 7769 5801 5531 -887 -1023 198 C ATOM 3056 CD LYS A 301 -33.543 -29.599 3.983 1.00 58.18 C ANISOU 3056 CD LYS A 301 8747 6787 6572 -885 -1057 214 C ATOM 3057 CE LYS A 301 -33.197 -31.021 3.565 1.00 71.09 C ANISOU 3057 CE LYS A 301 10514 8322 8176 -903 -1073 176 C ATOM 3058 NZ LYS A 301 -31.829 -31.129 2.986 1.00 78.21 N ANISOU 3058 NZ LYS A 301 11512 9163 9042 -850 -1011 87 N ATOM 3059 N ILE A 302 -34.766 -24.245 3.239 1.00 39.92 N ANISOU 3059 N ILE A 302 6120 4744 4302 -827 -957 291 N ATOM 3060 CA ILE A 302 -35.663 -23.144 3.585 1.00 42.96 C ANISOU 3060 CA ILE A 302 6386 5205 4730 -818 -953 337 C ATOM 3061 C ILE A 302 -35.928 -22.274 2.362 1.00 47.71 C ANISOU 3061 C ILE A 302 7019 5813 5298 -833 -940 331 C ATOM 3062 O ILE A 302 -37.071 -21.893 2.084 1.00 53.18 O ANISOU 3062 O ILE A 302 7666 6533 6004 -861 -961 369 O ATOM 3063 CB ILE A 302 -35.075 -22.318 4.744 1.00 36.50 C ANISOU 3063 CB ILE A 302 5469 4445 3955 -752 -919 337 C ATOM 3064 CG1 ILE A 302 -35.015 -23.162 6.021 1.00 36.01 C ANISOU 3064 CG1 ILE A 302 5363 4385 3935 -740 -936 354 C ATOM 3065 CG2 ILE A 302 -35.902 -21.056 4.963 1.00 39.16 C ANISOU 3065 CG2 ILE A 302 5699 4853 4328 -733 -904 372 C ATOM 3066 CD1 ILE A 302 -34.195 -22.539 7.137 1.00 33.21 C ANISOU 3066 CD1 ILE A 302 4931 4072 3617 -672 -903 346 C ATOM 3067 N ILE A 303 -34.874 -21.947 1.616 1.00 40.77 N ANISOU 3067 N ILE A 303 6217 4905 4370 -813 -904 281 N ATOM 3068 CA ILE A 303 -35.016 -21.047 0.475 1.00 47.43 C ANISOU 3068 CA ILE A 303 7088 5754 5180 -823 -886 273 C ATOM 3069 C ILE A 303 -35.826 -21.710 -0.632 1.00 55.60 C ANISOU 3069 C ILE A 303 8201 6744 6180 -885 -923 284 C ATOM 3070 O ILE A 303 -36.785 -21.129 -1.155 1.00 60.83 O ANISOU 3070 O ILE A 303 8833 7432 6848 -910 -941 315 O ATOM 3071 CB ILE A 303 -33.629 -20.604 -0.023 1.00 42.84 C ANISOU 3071 CB ILE A 303 6572 5152 4554 -787 -830 216 C ATOM 3072 CG1 ILE A 303 -33.008 -19.616 0.968 1.00 38.28 C ANISOU 3072 CG1 ILE A 303 5902 4630 4011 -729 -796 217 C ATOM 3073 CG2 ILE A 303 -33.723 -19.982 -1.415 1.00 45.27 C ANISOU 3073 CG2 ILE A 303 6941 5447 4815 -807 -813 204 C ATOM 3074 CD1 ILE A 303 -31.495 -19.557 0.909 1.00 36.59 C ANISOU 3074 CD1 ILE A 303 5749 4393 3761 -691 -742 159 C ATOM 3075 N ARG A 304 -35.451 -22.934 -1.012 1.00 54.41 N ANISOU 3075 N ARG A 304 8155 6523 5994 -910 -935 256 N ATOM 3076 CA ARG A 304 -36.134 -23.605 -2.113 1.00 60.99 C ANISOU 3076 CA ARG A 304 9076 7307 6790 -968 -970 263 C ATOM 3077 C ARG A 304 -37.602 -23.858 -1.798 1.00 64.02 C ANISOU 3077 C ARG A 304 9395 7717 7214 -1016 -1027 327 C ATOM 3078 O ARG A 304 -38.436 -23.883 -2.710 1.00 72.33 O ANISOU 3078 O ARG A 304 10480 8756 8245 -1063 -1056 348 O ATOM 3079 CB ARG A 304 -35.436 -24.927 -2.438 1.00 62.72 C ANISOU 3079 CB ARG A 304 9419 7444 6968 -977 -971 221 C ATOM 3080 CG ARG A 304 -33.970 -24.790 -2.828 1.00 68.08 C ANISOU 3080 CG ARG A 304 10171 8092 7605 -928 -905 151 C ATOM 3081 CD ARG A 304 -33.326 -26.156 -3.024 1.00 73.04 C ANISOU 3081 CD ARG A 304 10914 8638 8200 -927 -901 106 C ATOM 3082 NE ARG A 304 -33.205 -26.513 -4.434 1.00 84.40 N ANISOU 3082 NE ARG A 304 12473 10019 9578 -946 -888 76 N ATOM 3083 CZ ARG A 304 -32.101 -26.380 -5.158 1.00 90.05 C ANISOU 3083 CZ ARG A 304 13263 10703 10248 -907 -820 15 C ATOM 3084 NH1 ARG A 304 -30.979 -25.909 -4.637 1.00 88.69 N ANISOU 3084 NH1 ARG A 304 13063 10549 10086 -847 -758 -27 N ATOM 3085 NH2 ARG A 304 -32.122 -26.732 -6.441 1.00 98.14 N ANISOU 3085 NH2 ARG A 304 14392 11679 11219 -928 -812 -4 N ATOM 3086 N SER A 305 -37.940 -24.042 -0.522 1.00 64.11 N ANISOU 3086 N SER A 305 9313 7766 7281 -1005 -1041 359 N ATOM 3087 CA SER A 305 -39.287 -24.446 -0.142 1.00 71.04 C ANISOU 3087 CA SER A 305 10133 8665 8195 -1050 -1090 417 C ATOM 3088 C SER A 305 -40.195 -23.278 0.218 1.00 79.57 C ANISOU 3088 C SER A 305 11090 9827 9318 -1035 -1083 457 C ATOM 3089 O SER A 305 -41.420 -23.421 0.131 1.00 90.84 O ANISOU 3089 O SER A 305 12482 11270 10761 -1078 -1119 502 O ATOM 3090 CB SER A 305 -39.228 -25.413 1.045 1.00 72.34 C ANISOU 3090 CB SER A 305 10270 8822 8394 -1050 -1108 432 C ATOM 3091 OG SER A 305 -38.482 -26.573 0.718 1.00 79.97 O ANISOU 3091 OG SER A 305 11357 9709 9321 -1064 -1119 396 O ATOM 3092 N HIS A 306 -39.639 -22.137 0.614 1.00 81.37 N ANISOU 3092 N HIS A 306 11253 10102 9563 -974 -1038 441 N ATOM 3093 CA HIS A 306 -40.434 -21.006 1.079 1.00 89.50 C ANISOU 3093 CA HIS A 306 12165 11206 10634 -947 -1026 474 C ATOM 3094 C HIS A 306 -40.181 -19.726 0.301 1.00 92.75 C ANISOU 3094 C HIS A 306 12580 11637 11024 -921 -997 455 C ATOM 3095 O HIS A 306 -41.125 -18.978 0.033 1.00 99.29 O ANISOU 3095 O HIS A 306 13359 12504 11864 -925 -1005 483 O ATOM 3096 CB HIS A 306 -40.164 -20.758 2.570 1.00 88.06 C ANISOU 3096 CB HIS A 306 11882 11072 10505 -892 -1000 482 C ATOM 3097 CG HIS A 306 -40.493 -21.929 3.443 1.00 90.35 C ANISOU 3097 CG HIS A 306 12157 11351 10822 -915 -1027 506 C ATOM 3098 ND1 HIS A 306 -39.759 -23.096 3.430 1.00 85.08 N ANISOU 3098 ND1 HIS A 306 11574 10621 10133 -935 -1043 483 N ATOM 3099 CD2 HIS A 306 -41.481 -22.117 4.350 1.00 94.35 C ANISOU 3099 CD2 HIS A 306 12578 11899 11373 -922 -1039 551 C ATOM 3100 CE1 HIS A 306 -40.278 -23.951 4.294 1.00 88.64 C ANISOU 3100 CE1 HIS A 306 11990 11074 10616 -956 -1068 516 C ATOM 3101 NE2 HIS A 306 -41.324 -23.381 4.865 1.00 95.38 N ANISOU 3101 NE2 HIS A 306 12740 11992 11510 -950 -1064 557 N ATOM 3102 N VAL A 307 -38.932 -19.447 -0.071 1.00 92.63 N ANISOU 3102 N VAL A 307 12624 11596 10976 -892 -962 409 N ATOM 3103 CA VAL A 307 -38.637 -18.238 -0.833 1.00100.05 C ANISOU 3103 CA VAL A 307 13571 12551 11892 -870 -933 393 C ATOM 3104 C VAL A 307 -38.907 -18.462 -2.315 1.00 97.05 C ANISOU 3104 C VAL A 307 13292 12125 11458 -922 -953 384 C ATOM 3105 O VAL A 307 -39.576 -17.653 -2.969 1.00106.57 O ANISOU 3105 O VAL A 307 14480 13352 12658 -930 -960 401 O ATOM 3106 CB VAL A 307 -37.183 -17.793 -0.588 1.00102.20 C ANISOU 3106 CB VAL A 307 13863 12820 12151 -820 -884 350 C ATOM 3107 CG1 VAL A 307 -36.921 -16.445 -1.250 1.00102.58 C ANISOU 3107 CG1 VAL A 307 13907 12889 12181 -797 -853 339 C ATOM 3108 CG2 VAL A 307 -36.886 -17.728 0.904 1.00 97.52 C ANISOU 3108 CG2 VAL A 307 13178 12266 11610 -773 -870 358 C ATOM 3109 N LEU A 308 -38.396 -19.559 -2.863 1.00 86.44 N ANISOU 3109 N LEU A 308 12055 10715 10072 -953 -962 357 N ATOM 3110 CA LEU A 308 -38.555 -19.860 -4.280 1.00 82.04 C ANISOU 3110 CA LEU A 308 11605 10108 9460 -999 -977 344 C ATOM 3111 C LEU A 308 -39.776 -20.744 -4.510 1.00 80.18 C ANISOU 3111 C LEU A 308 11382 9853 9229 -1062 -1037 383 C ATOM 3112 O LEU A 308 -40.405 -21.209 -3.559 1.00 83.92 O ANISOU 3112 O LEU A 308 11788 10349 9746 -1070 -1063 417 O ATOM 3113 CB LEU A 308 -37.299 -20.543 -4.823 1.00 77.69 C ANISOU 3113 CB LEU A 308 11173 9491 8854 -992 -945 288 C ATOM 3114 CG LEU A 308 -35.973 -19.877 -4.444 1.00 83.17 C ANISOU 3114 CG LEU A 308 11858 10200 9544 -932 -883 247 C ATOM 3115 CD1 LEU A 308 -34.795 -20.646 -5.026 1.00 74.95 C ANISOU 3115 CD1 LEU A 308 10938 9093 8446 -924 -847 189 C ATOM 3116 CD2 LEU A 308 -35.944 -18.423 -4.896 1.00 79.48 C ANISOU 3116 CD2 LEU A 308 11352 9775 9073 -910 -855 251 C TER 3117 LEU A 308 HETATM 3118 C1 PEG A1201 -16.954 -33.771 22.529 1.00 60.17 C HETATM 3119 O1 PEG A1201 -18.091 -34.500 22.910 1.00 58.67 O HETATM 3120 C2 PEG A1201 -17.402 -32.880 21.362 1.00 69.79 C HETATM 3121 O2 PEG A1201 -16.312 -32.797 20.461 1.00 70.14 O HETATM 3122 C3 PEG A1201 -16.679 -32.961 19.107 1.00 76.00 C HETATM 3123 C4 PEG A1201 -17.319 -31.639 18.658 1.00 81.41 C HETATM 3124 O4 PEG A1201 -18.512 -31.990 18.024 1.00 85.98 O HETATM 3125 C1 LJX A1202 -18.874 1.275 19.982 1.00 16.12 C HETATM 3126 C11 LJX A1202 -22.502 9.319 15.770 1.00 19.52 C HETATM 3127 C12 LJX A1202 -23.228 10.020 15.130 1.00 22.64 C HETATM 3128 C13 LJX A1202 -24.102 10.866 14.307 1.00 29.82 C HETATM 3129 C14 LJX A1202 -23.909 10.551 12.819 1.00 30.47 C HETATM 3130 C15 LJX A1202 -22.429 10.497 12.430 1.00 28.00 C HETATM 3131 C16 LJX A1202 -21.662 11.710 12.961 1.00 30.88 C HETATM 3132 C2 LJX A1202 -21.637 8.470 16.521 1.00 18.05 C HETATM 3133 C3 LJX A1202 -20.193 1.323 20.243 1.00 16.72 C HETATM 3134 C4 LJX A1202 -21.218 6.349 17.474 1.00 16.98 C HETATM 3135 C5 LJX A1202 -20.024 6.803 17.944 1.00 14.69 C HETATM 3136 C6 LJX A1202 -19.634 8.120 17.694 1.00 16.95 C HETATM 3137 C7 LJX A1202 -20.827 2.518 19.787 1.00 11.63 C HETATM 3138 C8 LJX A1202 -20.240 4.706 18.561 1.00 15.67 C HETATM 3139 C9 LJX A1202 -19.955 3.387 19.162 1.00 14.28 C HETATM 3140 N1 LJX A1202 -20.449 8.937 16.980 1.00 15.54 N HETATM 3141 N3 LJX A1202 -22.015 7.190 16.763 1.00 15.51 N HETATM 3142 S1 LJX A1202 -18.383 2.698 19.167 1.00 17.21 S HETATM 3143 C2' LJX A1202 -23.452 4.602 16.468 1.00 22.71 C HETATM 3144 C4' LJX A1202 -22.479 2.552 15.839 1.00 22.37 C HETATM 3145 C3' LJX A1202 -23.785 3.316 15.723 1.00 19.55 C HETATM 3146 C1' LJX A1202 -22.481 4.132 17.562 1.00 16.52 C HETATM 3147 N9 LJX A1202 -21.360 5.047 17.853 1.00 16.00 N HETATM 3148 N7 LJX A1202 -19.415 5.773 18.622 1.00 13.38 N HETATM 3149 N6 LJX A1202 -18.465 8.582 18.151 1.00 14.04 N HETATM 3150 O2' LJX A1202 -24.650 5.086 17.054 1.00 27.93 O HETATM 3151 O4' LJX A1202 -21.899 2.914 17.093 1.00 23.85 O HETATM 3152 O3' LJX A1202 -24.862 2.612 16.329 1.00 24.17 O HETATM 3153 NA NA A1203 -23.348 -8.455 16.656 1.00 27.01 NA1+ HETATM 3154 C18 OLC A1204 -33.639 -10.617 28.671 1.00 44.19 C HETATM 3155 C10 OLC A1204 -30.753 -3.414 33.805 1.00 44.23 C HETATM 3156 C9 OLC A1204 -30.067 -2.267 33.895 1.00 46.15 C HETATM 3157 C17 OLC A1204 -34.010 -9.142 28.682 1.00 51.24 C HETATM 3158 C11 OLC A1204 -31.893 -3.619 32.859 1.00 45.14 C HETATM 3159 C8 OLC A1204 -30.358 -1.058 33.061 1.00 46.08 C HETATM 3160 C24 OLC A1204 -35.027 10.565 32.955 1.00 59.49 C HETATM 3161 C16 OLC A1204 -33.104 -8.395 29.651 1.00 46.18 C HETATM 3162 C12 OLC A1204 -32.131 -5.110 32.666 1.00 43.53 C HETATM 3163 C7 OLC A1204 -31.004 0.020 33.916 1.00 48.16 C HETATM 3164 C15 OLC A1204 -33.650 -7.007 29.991 1.00 50.34 C HETATM 3165 C13 OLC A1204 -33.398 -5.314 31.842 1.00 47.13 C HETATM 3166 C6 OLC A1204 -30.668 1.383 33.327 1.00 46.32 C HETATM 3167 C14 OLC A1204 -33.549 -6.791 31.506 1.00 49.96 C HETATM 3168 C5 OLC A1204 -31.493 2.466 34.013 1.00 50.67 C HETATM 3169 C4 OLC A1204 -32.696 2.849 33.157 1.00 49.34 C HETATM 3170 C3 OLC A1204 -33.103 4.277 33.487 1.00 51.71 C HETATM 3171 C2 OLC A1204 -34.124 4.798 32.478 1.00 59.01 C HETATM 3172 C21 OLC A1204 -34.264 8.231 32.471 1.00 60.85 C HETATM 3173 C1 OLC A1204 -34.721 6.027 33.072 1.00 67.72 C HETATM 3174 C22 OLC A1204 -34.991 9.115 33.508 1.00 64.13 C HETATM 3175 O19 OLC A1204 -35.877 6.167 33.446 1.00 84.92 O HETATM 3176 O25 OLC A1204 -34.346 11.322 33.913 1.00 56.93 O HETATM 3177 O23 OLC A1204 -36.266 8.635 33.754 1.00 71.57 O HETATM 3178 O20 OLC A1204 -33.866 7.079 33.195 1.00 60.99 O HETATM 3179 C1 OLA A1205 -34.048 -26.563 21.326 1.00 67.03 C HETATM 3180 O1 OLA A1205 -33.529 -27.243 20.413 1.00 68.48 O HETATM 3181 O2 OLA A1205 -34.559 -27.153 22.305 1.00 73.13 O HETATM 3182 C2 OLA A1205 -34.059 -25.035 21.249 1.00 67.46 C HETATM 3183 C3 OLA A1205 -33.911 -24.551 19.809 1.00 56.53 C HETATM 3184 C4 OLA A1205 -34.160 -23.047 19.719 1.00 51.55 C HETATM 3185 C5 OLA A1205 -33.893 -22.531 18.308 1.00 48.69 C HETATM 3186 C6 OLA A1205 -33.843 -21.007 18.285 1.00 40.49 C HETATM 3187 C7 OLA A1205 -34.830 -20.436 17.270 1.00 42.63 C HETATM 3188 C8 OLA A1205 -34.891 -18.921 17.347 1.00 43.15 C HETATM 3189 C9 OLA A1205 -35.496 -18.469 18.651 1.00 45.24 C HETATM 3190 C10 OLA A1205 -35.596 -17.177 18.957 1.00 46.08 C HETATM 3191 C11 OLA A1205 -35.111 -16.101 18.017 1.00 41.19 C HETATM 3192 C12 OLA A1205 -35.849 -14.796 18.271 1.00 40.99 C HETATM 3193 C13 OLA A1205 -34.924 -13.683 18.768 1.00 40.30 C HETATM 3194 C14 OLA A1205 -34.856 -12.511 17.787 1.00 33.34 C HETATM 3195 C15 OLA A1205 -35.687 -11.315 18.248 1.00 36.00 C HETATM 3196 C16 OLA A1205 -34.874 -10.026 18.133 1.00 31.79 C HETATM 3197 C18 OLC A1206 -17.304 -7.175 5.477 1.00 44.98 C HETATM 3198 C10 OLC A1206 -20.348 -0.589 3.590 1.00 53.14 C HETATM 3199 C9 OLC A1206 -20.924 -0.093 2.489 1.00 58.28 C HETATM 3200 C17 OLC A1206 -16.858 -5.783 5.897 1.00 50.26 C HETATM 3201 C11 OLC A1206 -18.953 -0.243 4.006 1.00 51.52 C HETATM 3202 C8 OLC A1206 -20.231 0.851 1.560 1.00 59.86 C HETATM 3203 C24 OLC A1206 -20.667 13.219 2.584 1.00 62.46 C HETATM 3204 C16 OLC A1206 -17.801 -4.722 5.329 1.00 60.06 C HETATM 3205 C12 OLC A1206 -18.211 -1.495 4.426 1.00 51.46 C HETATM 3206 C7 OLC A1206 -19.991 2.191 2.245 1.00 49.55 C HETATM 3207 C15 OLC A1206 -17.931 -4.808 3.807 1.00 60.69 C HETATM 3208 C13 OLC A1206 -18.014 -2.376 3.199 1.00 63.45 C HETATM 3209 C6 OLC A1206 -21.028 3.202 1.781 1.00 45.82 C HETATM 3210 C14 OLC A1206 -18.816 -3.663 3.321 1.00 58.06 C HETATM 3211 C5 OLC A1206 -20.597 4.589 2.229 1.00 45.83 C HETATM 3212 C4 OLC A1206 -21.745 5.331 2.906 1.00 42.51 C HETATM 3213 C3 OLC A1206 -21.156 6.270 3.940 1.00 41.58 C HETATM 3214 C2 OLC A1206 -20.525 7.499 3.282 1.00 50.40 C HETATM 3215 C21 OLC A1206 -21.176 10.843 3.105 1.00 55.43 C HETATM 3216 C1 OLC A1206 -21.569 8.562 3.255 1.00 45.64 C HETATM 3217 C22 OLC A1206 -21.243 11.906 1.995 1.00 60.50 C HETATM 3218 O19 OLC A1206 -22.620 8.584 3.880 1.00 50.83 O HETATM 3219 O25 OLC A1206 -21.322 13.368 3.808 1.00 55.51 O HETATM 3220 O23 OLC A1206 -20.545 11.497 0.874 1.00 62.71 O HETATM 3221 O20 OLC A1206 -21.282 9.605 2.431 1.00 53.43 O HETATM 3222 C1 OLA A1207 -14.744 -18.950 4.694 1.00 73.64 C HETATM 3223 O1 OLA A1207 -14.824 -19.817 3.794 1.00 70.77 O HETATM 3224 O2 OLA A1207 -13.684 -18.857 5.353 1.00 73.25 O HETATM 3225 C2 OLA A1207 -15.923 -18.019 4.985 1.00 62.87 C HETATM 3226 C3 OLA A1207 -16.282 -17.189 3.755 1.00 66.04 C HETATM 3227 C4 OLA A1207 -16.956 -15.879 4.160 1.00 61.01 C HETATM 3228 C5 OLA A1207 -17.355 -15.068 2.930 1.00 54.12 C HETATM 3229 C6 OLA A1207 -18.511 -14.120 3.246 1.00 53.61 C HETATM 3230 C7 OLA A1207 -18.026 -12.845 3.934 1.00 54.65 C HETATM 3231 C8 OLA A1207 -18.902 -11.665 3.554 1.00 51.67 C HETATM 3232 C9 OLA A1207 -20.240 -11.739 4.245 1.00 48.77 C HETATM 3233 C10 OLA A1207 -21.243 -10.923 3.917 1.00 44.57 C HETATM 3234 C11 OLA A1207 -21.103 -9.879 2.838 1.00 43.72 C HETATM 3235 C12 OLA A1207 -21.900 -8.640 3.200 1.00 41.61 C HETATM 3236 C13 OLA A1207 -21.199 -7.383 2.693 1.00 44.14 C HETATM 3237 C14 OLA A1207 -21.777 -6.137 3.356 1.00 43.77 C HETATM 3238 C15 OLA A1207 -23.005 -5.602 2.625 1.00 40.17 C HETATM 3239 C16 OLA A1207 -23.077 -4.084 2.762 1.00 38.90 C HETATM 3240 C17 OLA A1207 -24.374 -3.530 2.180 1.00 37.49 C HETATM 3241 C18 OLA A1207 -24.309 -2.017 2.099 1.00 42.96 C HETATM 3242 C1 OLA A1208 -36.947 -23.480 23.025 1.00 70.00 C HETATM 3243 O1 OLA A1208 -37.166 -24.647 22.629 1.00 70.68 O HETATM 3244 O2 OLA A1208 -36.334 -23.314 24.104 1.00 72.52 O HETATM 3245 C2 OLA A1208 -37.421 -22.277 22.205 1.00 62.27 C HETATM 3246 C3 OLA A1208 -36.356 -21.182 22.160 1.00 65.27 C HETATM 3247 C4 OLA A1208 -36.985 -19.793 22.260 1.00 60.54 C HETATM 3248 C5 OLA A1208 -35.920 -18.730 22.527 1.00 60.92 C HETATM 3249 C6 OLA A1208 -36.506 -17.541 23.286 1.00 62.80 C HETATM 3250 C7 OLA A1208 -37.366 -16.669 22.373 1.00 62.72 C HETATM 3251 C8 OLA A1208 -38.034 -15.559 23.164 1.00 60.83 C HETATM 3252 C9 OLA A1208 -37.178 -14.315 23.172 1.00 56.46 C HETATM 3253 C10 OLA A1208 -37.222 -13.437 24.176 1.00 58.02 C HETATM 3254 C11 OLA A1208 -38.134 -13.642 25.360 1.00 64.76 C HETATM 3255 C12 OLA A1208 -37.926 -12.558 26.405 1.00 74.24 C HETATM 3256 C13 OLA A1208 -38.123 -13.088 27.827 1.00 75.23 C HETATM 3257 C14 OLA A1208 -39.426 -12.575 28.436 1.00 75.41 C HETATM 3258 C15 OLA A1208 -39.330 -11.086 28.762 1.00 80.16 C HETATM 3259 C16 OLA A1208 -39.540 -10.835 30.254 1.00 82.37 C HETATM 3260 C17 OLA A1208 -39.134 -9.413 30.637 1.00 75.07 C HETATM 3261 C18 OLA A1208 -40.141 -8.399 30.128 1.00 70.10 C HETATM 3262 C1 CLR A1209 -38.171 10.723 21.802 1.00 29.09 C HETATM 3263 C2 CLR A1209 -37.791 12.172 22.079 1.00 29.28 C HETATM 3264 C3 CLR A1209 -38.147 12.552 23.507 1.00 32.36 C HETATM 3265 C4 CLR A1209 -37.340 11.683 24.458 1.00 26.80 C HETATM 3266 C5 CLR A1209 -37.560 10.221 24.153 1.00 27.29 C HETATM 3267 C6 CLR A1209 -37.815 9.410 25.193 1.00 28.30 C HETATM 3268 C7 CLR A1209 -38.012 7.919 25.072 1.00 29.86 C HETATM 3269 C8 CLR A1209 -37.728 7.396 23.674 1.00 26.64 C HETATM 3270 C9 CLR A1209 -38.162 8.373 22.591 1.00 24.77 C HETATM 3271 C10 CLR A1209 -37.466 9.730 22.725 1.00 27.24 C HETATM 3272 C11 CLR A1209 -38.010 7.748 21.194 1.00 26.74 C HETATM 3273 C12 CLR A1209 -38.676 6.375 21.049 1.00 26.89 C HETATM 3274 C13 CLR A1209 -38.218 5.416 22.137 1.00 27.47 C HETATM 3275 C14 CLR A1209 -38.508 6.113 23.454 1.00 23.05 C HETATM 3276 C15 CLR A1209 -38.361 5.041 24.519 1.00 30.91 C HETATM 3277 C16 CLR A1209 -38.841 3.781 23.808 1.00 27.81 C HETATM 3278 C17 CLR A1209 -39.022 4.131 22.326 1.00 23.52 C HETATM 3279 C18 CLR A1209 -36.734 5.075 21.978 1.00 27.90 C HETATM 3280 C19 CLR A1209 -35.984 9.659 22.361 1.00 26.22 C HETATM 3281 C20 CLR A1209 -38.687 2.914 21.460 1.00 24.88 C HETATM 3282 C21 CLR A1209 -38.806 3.198 19.965 1.00 28.94 C HETATM 3283 C22 CLR A1209 -39.602 1.766 21.891 1.00 32.44 C HETATM 3284 C23 CLR A1209 -39.590 0.563 20.954 1.00 32.71 C HETATM 3285 C24 CLR A1209 -40.305 -0.613 21.613 1.00 45.22 C HETATM 3286 C25 CLR A1209 -39.858 -1.952 21.039 1.00 56.43 C HETATM 3287 C26 CLR A1209 -39.945 -3.043 22.096 1.00 66.59 C HETATM 3288 C27 CLR A1209 -40.698 -2.332 19.828 1.00 55.09 C HETATM 3289 O1 CLR A1209 -37.841 13.932 23.736 1.00 32.08 O HETATM 3290 C1 CLR A1210 -8.232 11.055 13.234 1.00 25.83 C HETATM 3291 C2 CLR A1210 -8.268 12.581 13.189 1.00 28.38 C HETATM 3292 C3 CLR A1210 -6.892 13.165 12.892 1.00 29.70 C HETATM 3293 C4 CLR A1210 -6.384 12.633 11.561 1.00 30.58 C HETATM 3294 C5 CLR A1210 -6.449 11.125 11.535 1.00 31.77 C HETATM 3295 C6 CLR A1210 -5.345 10.467 11.141 1.00 31.45 C HETATM 3296 C7 CLR A1210 -5.274 8.967 11.003 1.00 33.00 C HETATM 3297 C8 CLR A1210 -6.655 8.336 11.025 1.00 33.58 C HETATM 3298 C9 CLR A1210 -7.508 8.935 12.138 1.00 26.03 C HETATM 3299 C10 CLR A1210 -7.738 10.437 11.928 1.00 29.95 C HETATM 3300 C11 CLR A1210 -8.815 8.151 12.336 1.00 28.37 C HETATM 3301 C12 CLR A1210 -8.614 6.639 12.466 1.00 29.98 C HETATM 3302 C13 CLR A1210 -7.832 6.085 11.284 1.00 32.12 C HETATM 3303 C14 CLR A1210 -6.517 6.841 11.260 1.00 34.93 C HETATM 3304 C15 CLR A1210 -5.644 6.075 10.278 1.00 39.63 C HETATM 3305 C16 CLR A1210 -6.088 4.628 10.473 1.00 40.25 C HETATM 3306 C17 CLR A1210 -7.312 4.654 11.399 1.00 36.36 C HETATM 3307 C18 CLR A1210 -8.603 6.252 9.969 1.00 35.53 C HETATM 3308 C19 CLR A1210 -8.761 10.711 10.829 1.00 34.27 C HETATM 3309 C20 CLR A1210 -8.275 3.507 11.078 1.00 30.80 C HETATM 3310 C21 CLR A1210 -9.597 3.623 11.831 1.00 30.33 C HETATM 3311 C22 CLR A1210 -7.600 2.180 11.429 1.00 34.39 C HETATM 3312 C23 CLR A1210 -8.327 0.944 10.906 1.00 38.40 C HETATM 3313 C24 CLR A1210 -7.560 -0.307 11.316 1.00 49.55 C HETATM 3314 C25 CLR A1210 -8.335 -1.579 10.995 1.00 54.27 C HETATM 3315 C26 CLR A1210 -7.391 -2.703 10.586 1.00 57.11 C HETATM 3316 C27 CLR A1210 -9.186 -2.008 12.184 1.00 40.56 C HETATM 3317 O1 CLR A1210 -6.967 14.594 12.818 1.00 32.61 O HETATM 3318 C1 CLR A1211 -3.091 8.290 21.199 1.00 22.69 C HETATM 3319 C2 CLR A1211 -2.898 9.801 21.124 1.00 26.32 C HETATM 3320 C3 CLR A1211 -1.901 10.172 20.036 1.00 25.29 C HETATM 3321 C4 CLR A1211 -2.417 9.680 18.693 1.00 25.05 C HETATM 3322 C5 CLR A1211 -2.698 8.199 18.767 1.00 26.24 C HETATM 3323 C6 CLR A1211 -2.161 7.414 17.818 1.00 26.17 C HETATM 3324 C7 CLR A1211 -2.403 5.928 17.728 1.00 25.88 C HETATM 3325 C8 CLR A1211 -3.553 5.489 18.617 1.00 23.38 C HETATM 3326 C9 CLR A1211 -3.470 6.154 19.985 1.00 22.88 C HETATM 3327 C10 CLR A1211 -3.573 7.680 19.884 1.00 23.18 C HETATM 3328 C11 CLR A1211 -4.483 5.559 20.976 1.00 22.04 C HETATM 3329 C12 CLR A1211 -4.459 4.032 21.049 1.00 21.28 C HETATM 3330 C13 CLR A1211 -4.614 3.419 19.668 1.00 25.86 C HETATM 3331 C14 CLR A1211 -3.495 3.983 18.814 1.00 24.14 C HETATM 3332 C15 CLR A1211 -3.499 3.127 17.558 1.00 27.46 C HETATM 3333 C16 CLR A1211 -3.907 1.749 18.072 1.00 29.25 C HETATM 3334 C17 CLR A1211 -4.322 1.925 19.538 1.00 29.38 C HETATM 3335 C18 CLR A1211 -5.996 3.742 19.089 1.00 23.00 C HETATM 3336 C19 CLR A1211 -5.001 8.144 19.603 1.00 21.14 C HETATM 3337 C20 CLR A1211 -5.442 0.958 19.930 1.00 30.16 C HETATM 3338 C21 CLR A1211 -5.947 1.191 21.348 1.00 27.39 C HETATM 3339 C22 CLR A1211 -4.982 -0.495 19.832 1.00 36.15 C HETATM 3340 C23 CLR A1211 -6.118 -1.408 19.383 1.00 36.50 C HETATM 3341 C24 CLR A1211 -5.911 -2.842 19.861 1.00 39.72 C HETATM 3342 C25 CLR A1211 -5.267 -3.710 18.791 1.00 44.47 C HETATM 3343 C26 CLR A1211 -4.568 -4.903 19.428 1.00 49.62 C HETATM 3344 C27 CLR A1211 -6.301 -4.186 17.780 1.00 44.76 C HETATM 3345 O1 CLR A1211 -1.737 11.592 19.990 1.00 25.61 O HETATM 3346 C1 OLA A1212 -36.703 14.640 13.273 1.00 53.74 C HETATM 3347 O1 OLA A1212 -36.633 15.563 12.432 1.00 58.67 O HETATM 3348 O2 OLA A1212 -37.346 14.833 14.329 1.00 57.88 O HETATM 3349 C2 OLA A1212 -36.014 13.299 13.016 1.00 49.30 C HETATM 3350 C3 OLA A1212 -36.615 12.199 13.887 1.00 48.04 C HETATM 3351 C4 OLA A1212 -36.098 10.824 13.470 1.00 50.59 C HETATM 3352 C5 OLA A1212 -36.623 10.446 12.086 1.00 49.28 C HETATM 3353 C6 OLA A1212 -37.154 9.016 12.053 1.00 49.45 C HETATM 3354 C7 OLA A1212 -36.074 8.033 11.613 1.00 42.25 C HETATM 3355 C8 OLA A1212 -36.657 6.636 11.517 1.00 43.03 C HETATM 3356 C9 OLA A1212 -35.752 5.725 10.728 1.00 38.24 C HETATM 3357 C10 OLA A1212 -36.235 4.678 10.059 1.00 46.19 C HETATM 3358 C11 OLA A1212 -37.710 4.364 10.066 1.00 55.83 C HETATM 3359 C12 OLA A1212 -37.978 2.961 9.555 1.00 57.45 C HETATM 3360 C13 OLA A1212 -39.006 2.241 10.425 1.00 65.64 C HETATM 3361 C14 OLA A1212 -38.307 1.323 11.425 1.00 64.07 C HETATM 3362 C15 OLA A1212 -39.299 0.392 12.115 1.00 65.10 C HETATM 3363 C16 OLA A1212 -38.649 -0.959 12.403 1.00 63.34 C HETATM 3364 C17 OLA A1212 -38.604 -1.830 11.150 1.00 71.00 C HETATM 3365 C18 OLA A1212 -39.048 -3.245 11.468 1.00 63.09 C HETATM 3366 C4 OLA A1213 -13.290 -16.114 30.813 1.00 46.91 C HETATM 3367 C5 OLA A1213 -14.429 -15.470 31.601 1.00 55.85 C HETATM 3368 C6 OLA A1213 -14.431 -13.955 31.408 1.00 60.28 C HETATM 3369 C7 OLA A1213 -15.438 -13.270 32.331 1.00 56.34 C HETATM 3370 C8 OLA A1213 -15.809 -11.885 31.826 1.00 56.61 C HETATM 3371 C9 OLA A1213 -14.590 -11.073 31.457 1.00 51.48 C HETATM 3372 C10 OLA A1213 -14.704 -9.887 30.860 1.00 48.76 C HETATM 3373 C11 OLA A1213 -16.052 -9.297 30.522 1.00 50.01 C HETATM 3374 C12 OLA A1213 -15.965 -7.784 30.418 1.00 39.24 C HETATM 3375 C13 OLA A1213 -17.061 -7.109 31.239 1.00 34.29 C HETATM 3376 C14 OLA A1213 -16.447 -6.339 32.407 1.00 36.64 C HETATM 3377 C15 OLA A1213 -17.496 -5.518 33.155 1.00 40.78 C HETATM 3378 C16 OLA A1213 -17.048 -4.064 33.293 1.00 39.73 C HETATM 3379 C17 OLA A1213 -17.412 -3.502 34.665 1.00 32.10 C HETATM 3380 C1 OLA A1214 -20.498 -22.544 28.001 1.00 43.19 C HETATM 3381 O1 OLA A1214 -20.205 -23.451 27.189 1.00 40.58 O HETATM 3382 O2 OLA A1214 -21.562 -22.637 28.654 1.00 52.24 O HETATM 3383 C2 OLA A1214 -19.568 -21.344 28.191 1.00 37.19 C HETATM 3384 C3 OLA A1214 -20.232 -20.256 29.031 1.00 40.97 C HETATM 3385 C4 OLA A1214 -19.260 -19.109 29.304 1.00 42.75 C HETATM 3386 C5 OLA A1214 -19.983 -17.764 29.300 1.00 39.68 C HETATM 3387 C6 OLA A1214 -19.012 -16.619 29.576 1.00 40.30 C HETATM 3388 C7 OLA A1214 -19.347 -15.403 28.716 1.00 34.11 C HETATM 3389 C1 OLA A1215 -8.579 13.964 7.405 1.00 65.40 C HETATM 3390 O1 OLA A1215 -9.249 14.238 6.385 1.00 71.36 O HETATM 3391 O2 OLA A1215 -8.166 14.897 8.129 1.00 68.40 O HETATM 3392 C2 OLA A1215 -8.265 12.511 7.760 1.00 57.93 C HETATM 3393 C3 OLA A1215 -9.473 11.610 7.501 1.00 56.67 C HETATM 3394 C4 OLA A1215 -9.251 10.691 6.301 1.00 54.30 C HETATM 3395 C5 OLA A1215 -8.052 9.772 6.527 1.00 54.76 C HETATM 3396 C6 OLA A1215 -8.199 8.459 5.765 1.00 52.51 C HETATM 3397 C7 OLA A1215 -8.565 7.333 6.726 1.00 51.82 C HETATM 3398 C8 OLA A1215 -8.613 5.992 6.020 1.00 51.80 C HETATM 3399 C9 OLA A1215 -9.841 5.231 6.446 1.00 56.60 C HETATM 3400 C10 OLA A1215 -11.042 5.507 5.939 1.00 55.38 C HETATM 3401 C11 OLA A1215 -11.253 6.589 4.912 1.00 50.87 C HETATM 3402 C12 OLA A1215 -10.932 6.094 3.513 1.00 55.61 C HETATM 3403 C13 OLA A1215 -11.432 4.665 3.312 1.00 57.27 C HETATM 3404 C14 OLA A1215 -11.704 4.376 1.839 1.00 64.49 C HETATM 3405 C15 OLA A1215 -12.103 2.916 1.651 1.00 64.07 C HETATM 3406 C1 OLA A1216 -35.710 -15.499 4.999 1.00 64.77 C HETATM 3407 O1 OLA A1216 -36.818 -15.889 5.434 1.00 73.13 O HETATM 3408 O2 OLA A1216 -35.112 -14.579 5.600 1.00 62.22 O HETATM 3409 C2 OLA A1216 -35.095 -16.137 3.752 1.00 70.51 C HETATM 3410 C3 OLA A1216 -34.668 -15.070 2.746 1.00 75.73 C HETATM 3411 C4 OLA A1216 -33.660 -15.625 1.740 1.00 71.46 C HETATM 3412 C5 OLA A1216 -32.607 -14.577 1.384 1.00 55.78 C HETATM 3413 C6 OLA A1216 -31.582 -14.428 2.506 1.00 47.82 C HETATM 3414 C7 OLA A1216 -30.545 -13.362 2.159 1.00 43.96 C HETATM 3415 C8 OLA A1216 -29.400 -13.370 3.156 1.00 36.66 C HETATM 3416 C9 OLA A1216 -28.442 -12.242 2.877 1.00 36.45 C HETATM 3417 C10 OLA A1216 -28.107 -11.399 3.848 1.00 30.72 C HETATM 3418 C1 OLA A1217 -40.051 11.520 9.224 1.00 66.10 C HETATM 3419 O1 OLA A1217 -41.145 12.110 9.076 1.00 66.42 O HETATM 3420 O2 OLA A1217 -38.995 12.192 9.247 1.00 69.36 O HETATM 3421 C2 OLA A1217 -40.003 9.998 9.378 1.00 61.98 C HETATM 3422 C3 OLA A1217 -40.924 9.313 8.371 1.00 63.59 C HETATM 3423 C4 OLA A1217 -40.673 7.807 8.346 1.00 66.90 C HETATM 3424 C5 OLA A1217 -41.825 7.062 7.673 1.00 65.88 C HETATM 3425 C6 OLA A1217 -41.805 5.582 8.047 1.00 67.70 C HETATM 3426 C7 OLA A1217 -43.061 4.869 7.547 1.00 71.38 C HETATM 3427 C8 OLA A1217 -43.258 3.541 8.257 1.00 74.53 C HETATM 3428 C9 OLA A1217 -42.526 2.427 7.552 1.00 81.49 C HETATM 3429 C10 OLA A1217 -42.353 1.243 8.138 1.00 80.72 C HETATM 3430 C11 OLA A1217 -42.884 0.982 9.526 1.00 72.45 C HETATM 3431 C12 OLA A1217 -42.477 -0.397 10.015 1.00 74.60 C HETATM 3432 C13 OLA A1217 -43.287 -1.489 9.323 1.00 62.27 C HETATM 3433 C1 OLA A1218 -34.248 9.901 2.900 1.00 60.37 C HETATM 3434 O1 OLA A1218 -35.488 9.948 2.736 1.00 69.81 O HETATM 3435 O2 OLA A1218 -33.633 10.961 3.156 1.00 56.75 O HETATM 3436 C2 OLA A1218 -33.500 8.572 2.794 1.00 47.97 C HETATM 3437 C3 OLA A1218 -33.853 7.839 1.501 1.00 52.43 C HETATM 3438 C4 OLA A1218 -35.060 6.921 1.689 1.00 55.13 C HETATM 3439 C5 OLA A1218 -35.068 5.804 0.647 1.00 48.04 C HETATM 3440 C6 OLA A1218 -34.027 4.739 0.982 1.00 43.26 C HETATM 3441 C7 OLA A1218 -34.513 3.344 0.597 1.00 43.11 C HETATM 3442 C8 OLA A1218 -33.610 2.276 1.186 1.00 46.05 C HETATM 3443 C9 OLA A1218 -32.902 1.511 0.099 1.00 35.58 C HETATM 3444 C7 OLA A1219 -39.434 -19.561 15.385 1.00 52.03 C HETATM 3445 C8 OLA A1219 -38.159 -18.766 15.603 1.00 47.10 C HETATM 3446 C9 OLA A1219 -37.343 -18.690 14.335 1.00 46.25 C HETATM 3447 C10 OLA A1219 -37.374 -17.622 13.535 1.00 42.46 C HETATM 3448 C11 OLA A1219 -38.222 -16.411 13.830 1.00 44.49 C HETATM 3449 C12 OLA A1219 -37.364 -15.190 14.114 1.00 37.39 C HETATM 3450 C13 OLA A1219 -38.190 -13.912 13.979 1.00 42.37 C HETATM 3451 C14 OLA A1219 -37.510 -12.730 14.665 1.00 44.07 C HETATM 3452 C15 OLA A1219 -37.826 -11.424 13.938 1.00 46.64 C HETATM 3453 C16 OLA A1219 -38.814 -10.566 14.726 1.00 49.61 C HETATM 3454 C17 OLA A1219 -38.124 -9.859 15.891 1.00 40.08 C HETATM 3455 C1 OLA A1220 -7.886 -18.699 12.196 1.00 41.30 C HETATM 3456 C2 OLA A1220 -9.046 -17.704 12.165 1.00 38.21 C HETATM 3457 C3 OLA A1220 -8.556 -16.288 12.457 1.00 43.42 C HETATM 3458 C4 OLA A1220 -9.654 -15.447 13.102 1.00 48.37 C HETATM 3459 C5 OLA A1220 -9.460 -13.965 12.791 1.00 52.67 C HETATM 3460 C6 OLA A1220 -10.331 -13.527 11.612 1.00 44.06 C HETATM 3461 C7 OLA A1220 -9.803 -12.250 10.958 1.00 40.69 C HETATM 3462 C8 OLA A1220 -9.786 -11.071 11.918 1.00 43.35 C HETATM 3463 C9 OLA A1220 -8.784 -10.037 11.471 1.00 44.69 C HETATM 3464 C10 OLA A1220 -8.312 -9.123 12.319 1.00 41.30 C HETATM 3465 C11 OLA A1220 -8.763 -9.092 13.757 1.00 36.07 C HETATM 3466 C12 OLA A1220 -8.148 -7.913 14.489 1.00 32.99 C HETATM 3467 C1 OLA A1221 -3.672 8.618 30.225 1.00 57.60 C HETATM 3468 O1 OLA A1221 -3.968 9.477 29.363 1.00 57.61 O HETATM 3469 O2 OLA A1221 -3.773 8.913 31.437 1.00 62.16 O HETATM 3470 C2 OLA A1221 -3.193 7.227 29.805 1.00 54.34 C HETATM 3471 C3 OLA A1221 -4.298 6.194 30.006 1.00 50.11 C HETATM 3472 C4 OLA A1221 -3.719 4.793 30.179 1.00 53.20 C HETATM 3473 C5 OLA A1221 -4.658 3.745 29.586 1.00 52.53 C HETATM 3474 C6 OLA A1221 -4.413 2.368 30.199 1.00 53.70 C HETATM 3475 C7 OLA A1221 -4.461 1.274 29.133 1.00 58.43 C HETATM 3476 C8 OLA A1221 -4.954 -0.041 29.710 1.00 70.28 C HETATM 3477 C9 OLA A1221 -4.197 -1.195 29.095 1.00 76.67 C HETATM 3478 C10 OLA A1221 -4.794 -2.196 28.444 1.00 74.54 C HETATM 3479 C11 OLA A1221 -6.291 -2.263 28.263 1.00 55.00 C HETATM 3480 C12 OLA A1221 -6.688 -3.405 27.344 1.00 50.71 C HETATM 3481 C13 OLA A1221 -6.118 -4.739 27.823 1.00 56.78 C HETATM 3482 C8 OLC A1222 -14.573 1.537 0.067 1.00 57.87 C HETATM 3483 C24 OLC A1222 -16.556 13.198 1.191 1.00 54.62 C HETATM 3484 C7 OLC A1222 -15.750 2.490 0.158 1.00 62.50 C HETATM 3485 C6 OLC A1222 -15.259 3.837 0.679 1.00 66.94 C HETATM 3486 C5 OLC A1222 -16.084 4.972 0.089 1.00 66.65 C HETATM 3487 C4 OLC A1222 -16.823 5.706 1.200 1.00 65.59 C HETATM 3488 C3 OLC A1222 -17.160 7.104 0.721 1.00 59.57 C HETATM 3489 C2 OLC A1222 -15.919 7.988 0.657 1.00 55.61 C HETATM 3490 C21 OLC A1222 -15.085 11.196 1.127 1.00 49.23 C HETATM 3491 C1 OLC A1222 -16.428 9.385 0.571 1.00 57.12 C HETATM 3492 C22 OLC A1222 -15.301 12.591 0.509 1.00 47.50 C HETATM 3493 O19 OLC A1222 -17.554 9.770 0.851 1.00 60.43 O HETATM 3494 O25 OLC A1222 -16.320 14.574 1.204 1.00 54.92 O HETATM 3495 O23 OLC A1222 -14.182 13.388 0.676 1.00 52.54 O HETATM 3496 O20 OLC A1222 -15.518 10.294 0.131 1.00 56.17 O HETATM 3497 C24 OLC A1223 -41.545 -27.036 14.739 1.00 62.45 C HETATM 3498 C3 OLC A1223 -44.036 -21.070 13.723 1.00 45.90 C HETATM 3499 C2 OLC A1223 -43.171 -22.152 14.357 1.00 46.32 C HETATM 3500 C21 OLC A1223 -43.190 -25.699 13.441 1.00 60.01 C HETATM 3501 C1 OLC A1223 -43.527 -23.416 13.653 1.00 54.27 C HETATM 3502 C22 OLC A1223 -43.052 -26.875 14.425 1.00 61.59 C HETATM 3503 O19 OLC A1223 -44.194 -23.524 12.634 1.00 57.18 O HETATM 3504 O25 OLC A1223 -40.900 -26.676 13.555 1.00 63.95 O HETATM 3505 O23 OLC A1223 -43.799 -26.661 15.573 1.00 51.23 O HETATM 3506 O20 OLC A1223 -43.044 -24.543 14.238 1.00 55.56 O HETATM 3507 C1 OLA A1224 -32.388 -26.034 25.549 1.00 58.50 C HETATM 3508 O1 OLA A1224 -31.597 -26.600 24.763 1.00 61.23 O HETATM 3509 O2 OLA A1224 -33.060 -26.741 26.332 1.00 56.44 O HETATM 3510 C2 OLA A1224 -32.532 -24.511 25.554 1.00 54.08 C HETATM 3511 C3 OLA A1224 -31.975 -23.882 24.279 1.00 49.89 C HETATM 3512 C4 OLA A1224 -32.771 -22.632 23.910 1.00 51.05 C HETATM 3513 C5 OLA A1224 -31.967 -21.699 23.005 1.00 49.96 C HETATM 3514 C6 OLA A1224 -32.617 -20.318 22.936 1.00 49.19 C HETATM 3515 C7 OLA A1224 -31.591 -19.237 22.607 1.00 41.71 C HETATM 3516 C8 OLA A1224 -32.203 -17.856 22.760 1.00 41.70 C HETATM 3517 C9 OLA A1224 -31.467 -16.850 21.913 1.00 37.47 C HETATM 3518 C10 OLA A1224 -31.874 -15.584 21.792 1.00 41.52 C HETATM 3519 C11 OLA A1224 -33.099 -15.039 22.483 1.00 41.03 C HETATM 3520 C12 OLA A1224 -32.709 -13.853 23.346 1.00 34.57 C HETATM 3521 C13 OLA A1224 -33.545 -12.617 23.022 1.00 35.16 C HETATM 3522 C14 OLA A1224 -32.844 -11.359 23.526 1.00 31.99 C HETATM 3523 C15 OLA A1224 -33.827 -10.210 23.739 1.00 35.80 C HETATM 3524 C16 OLA A1224 -33.078 -8.925 24.087 1.00 35.14 C HETATM 3525 C17 OLA A1224 -34.041 -7.786 24.414 1.00 35.87 C HETATM 3526 C1 OLA A1225 -1.093 -22.702 25.347 1.00 59.79 C HETATM 3527 O1 OLA A1225 -0.941 -22.569 24.111 1.00 57.34 O HETATM 3528 O2 OLA A1225 -1.111 -23.854 25.839 1.00 59.84 O HETATM 3529 C2 OLA A1225 -1.258 -21.470 26.239 1.00 61.54 C HETATM 3530 C3 OLA A1225 -1.582 -20.233 25.405 1.00 53.51 C HETATM 3531 C4 OLA A1225 -2.069 -19.092 26.296 1.00 59.37 C HETATM 3532 C5 OLA A1225 -2.318 -17.822 25.480 1.00 54.78 C HETATM 3533 C6 OLA A1225 -1.723 -16.584 26.153 1.00 62.10 C HETATM 3534 C7 OLA A1225 -2.760 -15.474 26.317 1.00 62.45 C HETATM 3535 C8 OLA A1225 -2.914 -14.668 25.040 1.00 58.02 C HETATM 3536 C9 OLA A1225 -3.905 -13.545 25.246 1.00 49.31 C HETATM 3537 C10 OLA A1225 -3.596 -12.261 25.050 1.00 50.56 C HETATM 3538 C11 OLA A1225 -2.224 -11.823 24.604 1.00 63.08 C HETATM 3539 C12 OLA A1225 -2.133 -10.309 24.545 1.00 65.22 C HETATM 3540 C13 OLA A1225 -2.179 -9.700 25.945 1.00 68.74 C HETATM 3541 C5 OLA A1226 -6.719 -16.978 16.851 1.00 47.70 C HETATM 3542 C6 OLA A1226 -7.528 -15.771 16.379 1.00 50.24 C HETATM 3543 C7 OLA A1226 -8.673 -15.462 17.341 1.00 42.59 C HETATM 3544 C8 OLA A1226 -9.375 -14.169 16.962 1.00 40.38 C HETATM 3545 C9 OLA A1226 -10.343 -13.760 18.046 1.00 31.34 C HETATM 3546 C10 OLA A1226 -10.484 -12.491 18.432 1.00 31.10 C HETATM 3547 C11 OLA A1226 -9.691 -11.365 17.819 1.00 31.98 C HETATM 3548 C12 OLA A1226 -9.519 -10.226 18.807 1.00 32.36 C HETATM 3549 C13 OLA A1226 -8.430 -9.262 18.344 1.00 33.88 C HETATM 3550 C14 OLA A1226 -7.875 -8.462 19.520 1.00 36.07 C HETATM 3551 C15 OLA A1226 -8.422 -7.037 19.522 1.00 32.49 C HETATM 3552 C7 OLA A1227 -35.062 1.637 30.649 1.00 62.84 C HETATM 3553 C8 OLA A1227 -34.326 0.624 29.790 1.00 74.91 C HETATM 3554 C9 OLA A1227 -33.947 -0.593 30.601 1.00 59.20 C HETATM 3555 C10 OLA A1227 -34.565 -1.770 30.486 1.00 54.33 C HETATM 3556 C11 OLA A1227 -35.708 -1.996 29.530 1.00 59.84 C HETATM 3557 C12 OLA A1227 -35.339 -3.029 28.480 1.00 54.56 C HETATM 3558 C13 OLA A1227 -35.995 -4.377 28.774 1.00 52.64 C HETATM 3559 C14 OLA A1227 -36.639 -4.952 27.514 1.00 57.23 C HETATM 3560 C15 OLA A1227 -36.685 -6.479 27.560 1.00 53.34 C HETATM 3561 C16 OLA A1227 -37.691 -6.979 28.593 1.00 59.51 C HETATM 3562 C6 OLA A1228 -13.339 2.926 8.034 1.00 34.53 C HETATM 3563 C7 OLA A1228 -11.816 2.845 7.988 1.00 47.07 C HETATM 3564 C8 OLA A1228 -11.334 1.421 8.173 1.00 57.53 C HETATM 3565 C9 OLA A1228 -11.589 0.623 6.920 1.00 64.45 C HETATM 3566 C10 OLA A1228 -11.219 -0.652 6.829 1.00 66.68 C HETATM 3567 C11 OLA A1228 -10.530 -1.345 7.977 1.00 63.32 C HETATM 3568 C12 OLA A1228 -10.666 -2.852 7.856 1.00 60.85 C HETATM 3569 C13 OLA A1228 -9.779 -3.402 6.742 1.00 69.29 C HETATM 3570 C14 OLA A1228 -8.345 -3.598 7.229 1.00 68.05 C HETATM 3571 C15 OLA A1228 -7.597 -4.575 6.326 1.00 64.72 C HETATM 3572 C16 OLA A1228 -8.448 -5.810 6.042 1.00 58.84 C HETATM 3573 C17 OLA A1228 -7.605 -7.081 6.100 1.00 50.34 C HETATM 3574 C18 OLA A1228 -7.021 -7.282 7.487 1.00 46.96 C HETATM 3575 C1 OLA A1229 -13.232 -25.691 32.320 1.00 58.60 C HETATM 3576 O1 OLA A1229 -14.433 -25.644 32.670 1.00 62.81 O HETATM 3577 O2 OLA A1229 -12.441 -26.421 32.959 1.00 61.14 O HETATM 3578 C2 OLA A1229 -12.740 -24.869 31.127 1.00 59.20 C HETATM 3579 C3 OLA A1229 -13.010 -23.379 31.330 1.00 55.36 C HETATM 3580 C4 OLA A1229 -12.449 -22.565 30.167 1.00 49.82 C HETATM 3581 C5 OLA A1229 -12.332 -21.084 30.527 1.00 49.54 C HETATM 3582 C6 OLA A1229 -10.869 -20.650 30.595 1.00 54.30 C HETATM 3583 C7 OLA A1229 -10.217 -20.679 29.214 1.00 47.24 C HETATM 3584 C1 OLA A1230 -20.898 -24.562 32.940 1.00 65.27 C HETATM 3585 O1 OLA A1230 -21.565 -24.785 31.905 1.00 62.08 O HETATM 3586 O2 OLA A1230 -21.462 -24.644 34.055 1.00 67.36 O HETATM 3587 C2 OLA A1230 -19.417 -24.193 32.845 1.00 77.05 C HETATM 3588 C3 OLA A1230 -19.237 -22.916 32.023 1.00 74.93 C HETATM 3589 C4 OLA A1230 -18.347 -21.886 32.723 1.00 74.69 C HETATM 3590 C5 OLA A1230 -18.988 -20.499 32.709 1.00 63.79 C HETATM 3591 C1 OLA A1231 -39.422 14.978 17.692 1.00 55.80 C HETATM 3592 O1 OLA A1231 -39.196 15.612 18.749 1.00 58.19 O HETATM 3593 O2 OLA A1231 -39.364 15.583 16.598 1.00 59.46 O HETATM 3594 C2 OLA A1231 -39.762 13.488 17.741 1.00 49.72 C HETATM 3595 C3 OLA A1231 -38.734 12.659 16.975 1.00 46.69 C HETATM 3596 C4 OLA A1231 -38.445 11.351 17.708 1.00 42.80 C HETATM 3597 C5 OLA A1231 -37.718 10.355 16.808 1.00 40.66 C HETATM 3598 C6 OLA A1231 -37.823 8.936 17.364 1.00 36.45 C HETATM 3599 C7 OLA A1231 -37.346 7.910 16.340 1.00 40.44 C HETATM 3600 C8 OLA A1231 -37.693 6.502 16.782 1.00 38.69 C HETATM 3601 C9 OLA A1231 -36.667 5.520 16.270 1.00 39.62 C HETATM 3602 C10 OLA A1231 -37.001 4.391 15.644 1.00 36.53 C HETATM 3603 C11 OLA A1231 -38.438 4.010 15.400 1.00 44.16 C HETATM 3604 C12 OLA A1231 -38.542 2.600 14.852 1.00 43.64 C HETATM 3605 C13 OLA A1231 -38.515 1.560 15.972 1.00 46.22 C HETATM 3606 C14 OLA A1231 -39.821 0.766 16.026 1.00 52.08 C HETATM 3607 C15 OLA A1231 -39.608 -0.655 16.545 1.00 58.95 C HETATM 3608 C16 OLA A1231 -40.537 -1.625 15.818 1.00 61.54 C HETATM 3609 C17 OLA A1231 -40.352 -3.065 16.290 1.00 58.88 C HETATM 3610 C18 OLA A1231 -41.064 -4.030 15.360 1.00 59.97 C HETATM 3611 C1 OLA A1232 -31.992 8.889 36.553 1.00 48.73 C HETATM 3612 O1 OLA A1232 -30.920 9.513 36.727 1.00 44.20 O HETATM 3613 O2 OLA A1232 -33.073 9.445 36.856 1.00 49.50 O HETATM 3614 C2 OLA A1232 -31.977 7.474 35.968 1.00 40.86 C HETATM 3615 C3 OLA A1232 -32.437 6.422 36.976 1.00 39.62 C HETATM 3616 C4 OLA A1232 -31.686 5.108 36.759 1.00 38.57 C HETATM 3617 C5 OLA A1232 -32.421 3.918 37.381 1.00 39.95 C HETATM 3618 C6 OLA A1232 -31.487 3.050 38.227 1.00 39.36 C HETATM 3619 C7 OLA A1232 -31.739 1.556 38.025 1.00 45.61 C HETATM 3620 C8 OLA A1232 -30.515 0.746 38.418 1.00 36.61 C HETATM 3621 C9 OLA A1232 -30.908 -0.488 39.196 1.00 41.10 C HETATM 3622 C10 OLA A1232 -30.557 -1.722 38.825 1.00 39.19 C HETATM 3623 C11 OLA A1232 -29.733 -1.988 37.591 1.00 51.71 C HETATM 3624 C1 OLA A1233 -1.395 13.449 25.941 1.00 47.70 C HETATM 3625 O1 OLA A1233 -1.502 13.878 24.769 1.00 53.05 O HETATM 3626 O2 OLA A1233 -0.640 14.049 26.741 1.00 55.27 O HETATM 3627 C2 OLA A1233 -2.173 12.211 26.388 1.00 45.43 C HETATM 3628 C3 OLA A1233 -1.674 10.968 25.656 1.00 36.91 C HETATM 3629 C4 OLA A1233 -2.419 9.718 26.111 1.00 34.24 C HETATM 3630 C5 OLA A1233 -2.376 8.657 25.018 1.00 31.36 C HETATM 3631 C6 OLA A1233 -2.533 7.248 25.590 1.00 31.66 C HETATM 3632 C7 OLA A1233 -3.517 6.440 24.750 1.00 31.86 C HETATM 3633 C8 OLA A1233 -3.140 4.973 24.671 1.00 34.19 C HETATM 3634 C9 OLA A1233 -3.336 4.297 26.003 1.00 42.73 C HETATM 3635 C10 OLA A1233 -3.308 2.969 26.138 1.00 50.86 C HETATM 3636 C11 OLA A1233 -3.081 2.029 24.979 1.00 42.36 C HETATM 3637 C12 OLA A1233 -4.153 0.955 24.952 1.00 52.24 C HETATM 3638 C13 OLA A1233 -3.529 -0.428 24.788 1.00 61.54 C HETATM 3639 C14 OLA A1233 -4.546 -1.433 24.251 1.00 60.57 C HETATM 3640 C15 OLA A1233 -4.040 -2.861 24.448 1.00 67.18 C HETATM 3641 C16 OLA A1233 -4.026 -3.652 23.141 1.00 59.65 C HETATM 3642 C1 ETF A1234 -19.769 -21.698 15.102 1.00 38.64 C HETATM 3643 C2 ETF A1234 -19.127 -23.002 15.508 1.00 41.19 C HETATM 3644 O ETF A1234 -19.202 -23.866 14.413 1.00 43.21 O HETATM 3645 F1 ETF A1234 -19.207 -21.234 13.979 1.00 36.96 F HETATM 3646 F2 ETF A1234 -21.079 -21.831 14.867 1.00 43.37 F HETATM 3647 F3 ETF A1234 -19.626 -20.747 16.031 1.00 41.16 F HETATM 3648 C1 PEG A1235 -6.058 14.523 26.988 1.00 62.62 C HETATM 3649 O1 PEG A1235 -4.708 14.533 26.601 1.00 56.38 O HETATM 3650 C2 PEG A1235 -6.461 13.030 26.984 1.00 54.87 C HETATM 3651 O2 PEG A1235 -7.300 12.829 28.100 1.00 49.76 O HETATM 3652 C3 PEG A1235 -7.026 11.658 28.834 1.00 48.42 C HETATM 3653 C4 PEG A1235 -7.796 11.801 30.167 1.00 56.15 C HETATM 3654 O4 PEG A1235 -7.601 10.591 30.840 1.00 51.44 O HETATM 3655 C1 PEG A1236 -39.200 24.649 21.287 1.00 72.40 C HETATM 3656 O1 PEG A1236 -40.034 23.903 22.132 1.00 75.10 O HETATM 3657 C2 PEG A1236 -39.027 26.011 22.000 1.00 77.89 C HETATM 3658 O2 PEG A1236 -37.876 26.613 21.456 1.00 78.79 O HETATM 3659 C3 PEG A1236 -37.601 27.896 21.971 1.00 78.01 C HETATM 3660 C4 PEG A1236 -36.389 28.428 21.178 1.00 72.05 C HETATM 3661 O4 PEG A1236 -36.830 28.530 19.858 1.00 71.62 O HETATM 3662 C1 PEG A1237 -19.601 -28.741 9.102 1.00 50.43 C HETATM 3663 O1 PEG A1237 -20.927 -29.146 8.873 1.00 49.71 O HETATM 3664 C2 PEG A1237 -18.808 -29.259 7.879 1.00 56.72 C HETATM 3665 O2 PEG A1237 -18.663 -28.171 6.992 1.00 55.99 O HETATM 3666 C3 PEG A1237 -18.051 -28.507 5.763 1.00 72.79 C HETATM 3667 C4 PEG A1237 -17.102 -27.340 5.407 1.00 71.06 C HETATM 3668 O4 PEG A1237 -17.867 -26.451 4.647 1.00 49.87 O HETATM 3669 C18 OLC A1238 -38.794 -3.941 6.417 1.00 79.62 C HETATM 3670 C10 OLC A1238 -38.362 4.398 4.445 1.00 93.51 C HETATM 3671 C9 OLC A1238 -37.721 5.559 4.570 1.00 82.84 C HETATM 3672 C17 OLC A1238 -39.735 -3.099 5.571 1.00 93.26 C HETATM 3673 C11 OLC A1238 -38.766 3.594 5.631 1.00 89.98 C HETATM 3674 C8 OLC A1238 -37.363 6.122 5.902 1.00 71.91 C HETATM 3675 C24 OLC A1238 -30.251 16.552 8.058 1.00 70.15 C HETATM 3676 C16 OLC A1238 -39.055 -1.790 5.189 1.00101.37 C HETATM 3677 C12 OLC A1238 -39.548 2.366 5.188 1.00 91.04 C HETATM 3678 C7 OLC A1238 -36.556 7.397 5.718 1.00 67.44 C HETATM 3679 C15 OLC A1238 -39.341 -0.689 6.207 1.00107.61 C HETATM 3680 C13 OLC A1238 -38.562 1.260 4.838 1.00103.77 C HETATM 3681 C6 OLC A1238 -36.103 7.919 7.082 1.00 58.45 C HETATM 3682 C14 OLC A1238 -38.285 0.405 6.065 1.00103.41 C HETATM 3683 C5 OLC A1238 -36.372 9.421 7.181 1.00 68.01 C HETATM 3684 C4 OLC A1238 -35.267 10.139 7.953 1.00 62.28 C HETATM 3685 C3 OLC A1238 -34.927 11.408 7.192 1.00 69.98 C HETATM 3686 C2 OLC A1238 -33.983 12.304 7.985 1.00 73.21 C HETATM 3687 C21 OLC A1238 -31.723 14.536 7.889 1.00 67.38 C HETATM 3688 C1 OLC A1238 -33.571 13.394 7.056 1.00 82.23 C HETATM 3689 C22 OLC A1238 -31.470 15.828 8.693 1.00 68.14 C HETATM 3690 O19 OLC A1238 -33.603 13.374 5.834 1.00 81.90 O HETATM 3691 O25 OLC A1238 -29.137 15.895 8.588 1.00 64.18 O HETATM 3692 O23 OLC A1238 -32.597 16.632 8.699 1.00 71.30 O HETATM 3693 O20 OLC A1238 -33.121 14.517 7.678 1.00 76.64 O HETATM 3694 C18 OLC A1239 -45.078 -2.574 14.858 1.00 57.70 C HETATM 3695 C10 OLC A1239 -41.152 5.013 12.914 1.00 48.58 C HETATM 3696 C9 OLC A1239 -40.503 6.135 12.597 1.00 51.54 C HETATM 3697 C17 OLC A1239 -44.866 -1.268 14.115 1.00 52.09 C HETATM 3698 C11 OLC A1239 -42.640 4.957 13.013 1.00 46.72 C HETATM 3699 C8 OLC A1239 -41.213 7.416 12.313 1.00 51.14 C HETATM 3700 C24 OLC A1239 -42.314 19.356 14.158 1.00 77.30 C HETATM 3701 C16 OLC A1239 -43.681 -0.536 14.712 1.00 45.00 C HETATM 3702 C12 OLC A1239 -43.076 3.756 13.837 1.00 39.17 C HETATM 3703 C7 OLC A1239 -41.419 8.188 13.605 1.00 46.26 C HETATM 3704 C15 OLC A1239 -43.870 0.972 14.680 1.00 47.62 C HETATM 3705 C13 OLC A1239 -42.694 2.485 13.095 1.00 49.61 C HETATM 3706 C6 OLC A1239 -40.474 9.377 13.640 1.00 51.12 C HETATM 3707 C14 OLC A1239 -43.787 1.446 13.239 1.00 46.34 C HETATM 3708 C5 OLC A1239 -41.127 10.576 12.970 1.00 48.59 C HETATM 3709 C4 OLC A1239 -41.537 11.608 14.018 1.00 45.14 C HETATM 3710 C3 OLC A1239 -41.682 12.965 13.352 1.00 51.33 C HETATM 3711 C2 OLC A1239 -41.265 14.082 14.304 1.00 62.83 C HETATM 3712 C21 OLC A1239 -40.761 17.430 13.841 1.00 79.92 C HETATM 3713 C1 OLC A1239 -41.803 15.346 13.726 1.00 67.95 C HETATM 3714 C22 OLC A1239 -40.991 18.717 14.658 1.00 79.70 C HETATM 3715 O19 OLC A1239 -42.420 15.471 12.677 1.00 62.60 O HETATM 3716 O25 OLC A1239 -42.161 20.719 14.418 1.00 86.00 O HETATM 3717 O23 OLC A1239 -41.040 18.438 16.013 1.00 72.67 O HETATM 3718 O20 OLC A1239 -41.563 16.454 14.479 1.00 78.83 O HETATM 3719 C18 OLC A1240 -42.023 -8.218 20.422 1.00 69.85 C HETATM 3720 C10 OLC A1240 -40.551 -3.400 28.648 1.00 78.87 C HETATM 3721 C9 OLC A1240 -40.199 -2.251 29.224 1.00 81.19 C HETATM 3722 C17 OLC A1240 -42.308 -7.021 21.317 1.00 77.42 C HETATM 3723 C11 OLC A1240 -40.475 -3.592 27.175 1.00 78.43 C HETATM 3724 C8 OLC A1240 -39.712 -1.087 28.430 1.00 83.35 C HETATM 3725 C24 OLC A1240 -36.429 10.416 28.916 1.00 54.43 C HETATM 3726 C16 OLC A1240 -41.842 -7.313 22.740 1.00 75.47 C HETATM 3727 C12 OLC A1240 -40.826 -5.031 26.810 1.00 79.34 C HETATM 3728 C7 OLC A1240 -39.507 0.114 29.347 1.00 88.60 C HETATM 3729 C15 OLC A1240 -40.769 -6.331 23.192 1.00 74.50 C HETATM 3730 C13 OLC A1240 -41.140 -5.091 25.321 1.00 74.32 C HETATM 3731 C6 OLC A1240 -39.224 1.356 28.507 1.00 77.05 C HETATM 3732 C14 OLC A1240 -40.642 -6.390 24.713 1.00 74.50 C HETATM 3733 C5 OLC A1240 -37.722 1.579 28.415 1.00 70.09 C HETATM 3734 C4 OLC A1240 -37.399 2.655 27.383 1.00 54.21 C HETATM 3735 C3 OLC A1240 -37.680 4.013 28.000 1.00 62.03 C HETATM 3736 C2 OLC A1240 -36.406 4.660 28.541 1.00 55.68 C HETATM 3737 C21 OLC A1240 -36.533 7.955 28.530 1.00 59.06 C HETATM 3738 C1 OLC A1240 -36.860 5.816 29.364 1.00 66.87 C HETATM 3739 C22 OLC A1240 -36.891 9.069 29.533 1.00 67.95 C HETATM 3740 O19 OLC A1240 -37.875 5.878 30.044 1.00 71.01 O HETATM 3741 O25 OLC A1240 -37.032 11.394 29.711 1.00 66.33 O HETATM 3742 O23 OLC A1240 -38.249 9.066 29.806 1.00 71.76 O HETATM 3743 O20 OLC A1240 -36.037 6.897 29.325 1.00 59.74 O HETATM 3744 O HOH A1301 -4.253 -63.756 27.134 1.00 45.35 O HETATM 3745 O HOH A1302 -43.402 21.976 13.099 1.00 78.02 O HETATM 3746 O HOH A1303 -23.989 -30.162 25.432 1.00 46.87 O HETATM 3747 O HOH A1304 -29.062 9.872 35.328 1.00 34.84 O HETATM 3748 O HOH A1305 -37.634 17.285 18.004 1.00 43.11 O HETATM 3749 O HOH A1306 -18.317 12.957 23.725 1.00 24.09 O HETATM 3750 O HOH A1307 -15.949 -16.728 19.328 1.00 20.68 O HETATM 3751 O HOH A1308 -23.611 15.142 33.199 1.00 30.39 O HETATM 3752 O HOH A1309 -18.996 -35.740 26.954 1.00 51.21 O HETATM 3753 O HOH A1310 -22.003 -24.362 15.078 1.00 39.64 O HETATM 3754 O HOH A1311 -25.280 -13.233 13.712 1.00 18.53 O HETATM 3755 O HOH A1312 -12.708 -33.514 21.494 1.00 42.91 O HETATM 3756 O HOH A1313 -16.252 -29.084 11.636 1.00 41.58 O HETATM 3757 O HOH A1314 -14.118 -26.915 17.707 1.00 29.25 O HETATM 3758 O HOH A1315 -22.364 -27.846 21.493 1.00 34.60 O HETATM 3759 O HOH A1316 -13.332 17.580 11.401 1.00 31.58 O HETATM 3760 O HOH A1317 -25.153 7.312 15.892 1.00 31.46 O HETATM 3761 O HOH A1318 -24.807 -10.120 17.146 1.00 30.98 O HETATM 3762 O HOH A1319 -25.485 -14.446 24.817 1.00 20.77 O HETATM 3763 O HOH A1320 -28.047 2.774 19.659 1.00 22.35 O HETATM 3764 O HOH A1321 -9.285 15.009 10.450 1.00 42.36 O HETATM 3765 O HOH A1322 -19.752 15.254 4.604 1.00 50.69 O HETATM 3766 O HOH A1323 5.747 -56.681 31.425 1.00 50.10 O HETATM 3767 O HOH A1324 14.747 -61.861 15.073 1.00 54.95 O HETATM 3768 O HOH A1325 -15.185 10.293 17.908 1.00 14.73 O HETATM 3769 O HOH A1326 -24.525 11.973 16.910 1.00 30.09 O HETATM 3770 O HOH A1327 -30.774 -34.557 15.183 1.00 48.34 O HETATM 3771 O HOH A1328 -11.603 -17.317 5.145 1.00 59.94 O HETATM 3772 O HOH A1329 -11.164 14.802 4.713 1.00 51.38 O HETATM 3773 O HOH A1330 -17.850 -39.885 29.335 1.00 61.37 O HETATM 3774 O HOH A1331 -25.497 -32.236 27.143 1.00 54.74 O HETATM 3775 O HOH A1332 -18.726 -11.389 13.225 1.00 17.62 O HETATM 3776 O HOH A1333 -24.767 24.052 29.961 1.00 45.62 O HETATM 3777 O HOH A1334 -25.872 -12.077 21.620 1.00 19.00 O HETATM 3778 O HOH A1335 -17.361 15.843 19.416 1.00 41.52 O HETATM 3779 O HOH A1336 -26.273 18.404 22.156 1.00 20.95 O HETATM 3780 O HOH A1337 -22.650 17.980 25.636 1.00 38.44 O HETATM 3781 O HOH A1338 -18.634 10.308 23.218 1.00 23.59 O HETATM 3782 O HOH A1339 -26.673 5.077 18.753 1.00 35.56 O HETATM 3783 O HOH A1340 3.391 -72.997 24.215 1.00 50.21 O HETATM 3784 O HOH A1341 -11.484 15.380 23.264 1.00 32.78 O HETATM 3785 O HOH A1342 -38.141 21.190 20.498 1.00 47.30 O HETATM 3786 O HOH A1343 -39.184 16.577 25.384 1.00 46.24 O HETATM 3787 O HOH A1344 -23.227 -4.733 14.055 1.00 16.62 O HETATM 3788 O HOH A1345 -21.218 -33.021 22.359 1.00 44.62 O HETATM 3789 O HOH A1346 -25.087 -15.863 14.693 1.00 21.27 O HETATM 3790 O HOH A1347 -4.410 -62.878 13.466 1.00 52.79 O HETATM 3791 O HOH A1348 -14.462 -57.921 22.946 1.00 57.57 O HETATM 3792 O HOH A1349 -5.049 -31.440 24.773 1.00 44.66 O HETATM 3793 O HOH A1350 -22.010 -6.458 15.584 1.00 19.87 O HETATM 3794 O HOH A1351 -25.823 7.836 13.365 1.00 21.60 O HETATM 3795 O HOH A1352 -26.105 -11.957 25.729 1.00 24.73 O HETATM 3796 O HOH A1353 0.342 -67.140 25.418 1.00 38.73 O HETATM 3797 O HOH A1354 0.099 -59.310 30.251 1.00 48.71 O HETATM 3798 O HOH A1355 -25.236 13.585 10.810 1.00 30.85 O HETATM 3799 O HOH A1356 -31.120 7.953 32.598 1.00 37.37 O HETATM 3800 O HOH A1357 -24.242 16.625 2.115 1.00 38.14 O HETATM 3801 O HOH A1358 -17.648 -17.303 17.180 1.00 28.31 O HETATM 3802 O HOH A1359 -13.618 -60.631 16.184 1.00 49.80 O HETATM 3803 O HOH A1360 -3.926 -25.928 25.028 1.00 36.32 O HETATM 3804 O HOH A1361 -28.772 12.656 8.736 1.00 39.70 O HETATM 3805 O HOH A1362 -2.269 13.607 22.170 1.00 32.77 O HETATM 3806 O HOH A1363 -27.477 2.900 17.118 1.00 16.49 O HETATM 3807 O HOH A1364 -0.756 -62.568 20.222 1.00 33.11 O HETATM 3808 O HOH A1365 -10.219 14.893 25.192 1.00 29.51 O HETATM 3809 O HOH A1366 -19.894 11.524 16.306 1.00 18.78 O HETATM 3810 O HOH A1367 -16.080 0.800 12.743 1.00 14.11 O HETATM 3811 O HOH A1368 4.067 -47.460 26.619 1.00 45.75 O HETATM 3812 O HOH A1369 -21.328 18.623 27.410 1.00 45.22 O HETATM 3813 O HOH A1370 -31.157 17.819 10.841 1.00 53.04 O HETATM 3814 O HOH A1371 -16.771 16.873 8.674 1.00 27.88 O HETATM 3815 O HOH A1372 -9.337 -29.087 9.886 1.00 47.29 O HETATM 3816 O HOH A1373 -10.340 19.381 20.827 1.00 36.86 O HETATM 3817 O HOH A1374 0.600 -61.881 29.776 1.00 45.75 O HETATM 3818 O HOH A1375 -9.542 14.949 18.465 1.00 30.35 O HETATM 3819 O HOH A1376 -4.328 -37.562 21.445 1.00 44.95 O HETATM 3820 O HOH A1377 -23.930 -11.114 11.441 1.00 19.23 O HETATM 3821 O HOH A1378 -19.831 17.753 30.605 1.00 53.53 O HETATM 3822 O HOH A1379 -13.501 -27.938 19.882 1.00 32.24 O HETATM 3823 O HOH A1380 -33.991 -29.869 22.568 1.00 61.26 O HETATM 3824 O HOH A1381 -32.048 -29.341 26.312 1.00 63.45 O HETATM 3825 O HOH A1382 -27.120 -11.537 6.672 1.00 26.81 O HETATM 3826 O HOH A1383 -15.220 3.598 21.875 1.00 14.31 O HETATM 3827 O HOH A1384 -19.503 -1.595 22.204 1.00 18.40 O HETATM 3828 O HOH A1385 -25.107 14.916 6.554 1.00 42.63 O HETATM 3829 O HOH A1386 -35.509 17.877 13.559 1.00 49.09 O HETATM 3830 O HOH A1387 -24.719 -6.618 17.935 1.00 29.00 O HETATM 3831 O HOH A1388 -20.801 -2.598 24.494 1.00 17.37 O HETATM 3832 O HOH A1389 -17.574 13.923 29.720 1.00 31.40 O HETATM 3833 O HOH A1390 -7.233 -16.887 28.299 1.00 44.94 O HETATM 3834 O HOH A1391 -32.670 23.612 25.931 1.00 46.81 O HETATM 3835 O HOH A1392 5.514 -75.828 26.650 1.00 30.68 O HETATM 3836 O HOH A1393 -22.418 -9.911 15.355 1.00 28.30 O HETATM 3837 O HOH A1394 -11.436 12.190 15.816 1.00 19.06 O HETATM 3838 O HOH A1395 -27.784 20.867 22.364 1.00 21.95 O HETATM 3839 O HOH A1396 -29.885 18.102 29.692 1.00 37.24 O HETATM 3840 O HOH A1397 7.055 -60.742 15.298 1.00 50.97 O HETATM 3841 O HOH A1398 14.098 -65.261 16.757 1.00 55.45 O HETATM 3842 O HOH A1399 -29.817 -29.346 23.538 1.00 49.03 O HETATM 3843 O HOH A1400 0.172 -52.174 30.244 1.00 50.63 O HETATM 3844 O HOH A1401 8.556 -66.699 15.066 1.00 33.21 O HETATM 3845 O HOH A1402 -34.105 14.003 30.247 1.00 36.80 O HETATM 3846 O HOH A1403 16.690 -66.435 18.722 1.00 58.90 O HETATM 3847 O HOH A1404 -36.367 -30.398 17.698 1.00 44.67 O HETATM 3848 O HOH A1405 -32.341 -33.119 10.305 1.00 54.00 O HETATM 3849 O HOH A1406 2.435 -68.231 18.696 1.00 47.09 O HETATM 3850 O HOH A1407 -25.804 18.754 24.869 1.00 23.98 O HETATM 3851 O HOH A1408 -3.534 16.462 21.747 1.00 32.42 O HETATM 3852 O HOH A1409 -22.534 -31.607 35.713 1.00 58.87 O HETATM 3853 O HOH A1410 -27.920 -31.887 17.784 1.00 43.54 O HETATM 3854 O HOH A1411 15.222 -55.661 18.241 1.00 51.75 O HETATM 3855 O HOH A1412 -20.748 -11.166 15.471 1.00 28.28 O HETATM 3856 O HOH A1413 -10.467 -24.428 7.833 1.00 44.03 O HETATM 3857 O HOH A1414 -18.108 -2.773 20.147 1.00 11.47 O HETATM 3858 O HOH A1415 -20.196 -36.140 29.711 1.00 53.34 O HETATM 3859 O HOH A1416 -5.617 -61.375 28.399 1.00 46.56 O HETATM 3860 O HOH A1417 -39.535 21.196 26.159 1.00 54.92 O HETATM 3861 O HOH A1418 -25.891 16.963 26.965 1.00 29.70 O HETATM 3862 O HOH A1419 -21.882 12.904 17.742 1.00 21.78 O HETATM 3863 O HOH A1420 -44.774 17.362 12.796 1.00 48.49 O HETATM 3864 O HOH A1421 -25.840 -31.411 17.049 1.00 45.24 O HETATM 3865 O HOH A1422 -17.371 12.082 32.720 1.00 32.46 O HETATM 3866 O HOH A1423 -30.247 -31.445 21.383 1.00 55.83 O HETATM 3867 O HOH A1424 -25.067 -29.594 23.057 1.00 33.39 O HETATM 3868 O HOH A1425 -38.275 25.435 17.088 1.00 57.21 O HETATM 3869 O HOH A1426 -4.464 -63.894 18.149 1.00 36.60 O HETATM 3870 O HOH A1427 -36.007 18.570 16.021 1.00 37.53 O HETATM 3871 O HOH A1428 15.808 -66.067 25.012 1.00 53.18 O HETATM 3872 O HOH A1429 -15.207 12.380 28.679 1.00 19.90 O HETATM 3873 O HOH A1430 -25.299 25.229 15.920 1.00 49.10 O HETATM 3874 O HOH A1431 -25.974 29.237 14.578 1.00 52.96 O HETATM 3875 O HOH A1432 -40.788 23.700 25.112 1.00 58.89 O HETATM 3876 O HOH A1433 -12.008 -35.866 28.705 1.00 48.61 O HETATM 3877 O HOH A1434 2.874 -73.483 29.175 1.00 52.01 O HETATM 3878 O HOH A1435 -17.399 13.606 26.263 1.00 27.22 O HETATM 3879 O HOH A1436 -19.796 12.608 32.788 1.00 33.81 O HETATM 3880 O HOH A1437 -2.526 16.810 24.722 1.00 50.39 O HETATM 3881 O HOH A1438 -9.234 13.477 16.642 1.00 24.74 O HETATM 3882 O HOH A1439 -2.779 -64.574 20.133 1.00 42.03 O HETATM 3883 O HOH A1440 -38.400 22.416 18.092 1.00 55.51 O HETATM 3884 O HOH A1441 -17.592 15.345 5.880 1.00 30.62 O HETATM 3885 O HOH A1442 -32.913 18.418 13.071 1.00 43.05 O HETATM 3886 O HOH A1443 -12.192 19.620 14.644 1.00 35.01 O HETATM 3887 O HOH A1444 15.532 -55.192 20.936 1.00 53.85 O HETATM 3888 O HOH A1445 -27.777 -30.922 22.153 1.00 49.09 O HETATM 3889 O HOH A1446 16.573 -64.356 17.182 1.00 77.99 O HETATM 3890 O HOH A1447 15.037 -64.662 14.213 1.00 61.05 O HETATM 3891 O HOH A1448 2.671 -53.072 30.797 1.00 46.81 O HETATM 3892 O HOH A1449 5.288 -59.240 32.250 1.00 49.38 O HETATM 3893 O HOH A1450 -31.071 -22.269 -2.738 1.00 38.97 O HETATM 3894 O HOH A1451 -30.760 -29.849 6.106 1.00 44.05 O HETATM 3895 O HOH A1452 -20.905 12.227 34.628 1.00 29.78 O HETATM 3896 O HOH A1453 -23.467 15.625 4.814 1.00 39.05 O HETATM 3897 O HOH A1454 -38.699 19.555 18.024 1.00 55.81 O HETATM 3898 O HOH A1455 -31.264 20.416 28.531 1.00 47.10 O HETATM 3899 O HOH A1456 -37.468 17.652 27.863 1.00 46.46 O HETATM 3900 O HOH A1457 -23.371 -26.882 13.593 1.00 40.41 O HETATM 3901 O HOH A1458 -20.838 -28.299 18.378 1.00 44.51 O HETATM 3902 O HOH A1459 -11.479 16.606 18.192 1.00 38.81 O HETATM 3903 O HOH A1460 -30.074 20.357 3.578 1.00 44.84 O HETATM 3904 O HOH A1461 3.743 -75.452 22.530 1.00 39.16 O HETATM 3905 O HOH A1462 11.080 -72.851 26.812 1.00 48.62 O HETATM 3906 O HOH A1463 -13.272 13.149 29.593 1.00 38.32 O HETATM 3907 O HOH A1464 -18.412 15.720 16.910 1.00 35.51 O HETATM 3908 O HOH A1465 -18.530 17.493 23.698 1.00 48.27 O HETATM 3909 O HOH A1466 -21.567 22.684 27.381 1.00 43.51 O HETATM 3910 O HOH A1467 -27.858 29.259 27.622 1.00 49.83 O HETATM 3911 O HOH A1468 -1.763 -28.013 24.710 1.00 50.59 O HETATM 3912 O HOH A1469 6.079 -75.825 24.089 1.00 31.63 O HETATM 3913 O HOH A1470 1.621 -57.565 32.270 1.00 51.37 O HETATM 3914 O HOH A1471 -31.747 16.914 31.068 1.00 49.84 O HETATM 3915 O HOH A1472 8.555 -62.621 13.174 1.00 51.28 O HETATM 3916 O HOH A1473 -21.417 15.342 17.496 1.00 29.19 O HETATM 3917 O HOH A1474 3.126 -55.726 31.192 1.00 50.37 O HETATM 3918 O HOH A1475 -19.338 14.087 14.800 1.00 35.65 O HETATM 3919 O HOH A1476 -18.122 -27.171 11.406 1.00 41.49 O HETATM 3920 O HOH A1477 -24.104 -53.229 16.929 1.00 57.59 O CONECT 420 3153 CONECT 556 1218 CONECT 572 1121 CONECT 592 1262 CONECT 697 3153 CONECT 1121 572 CONECT 1218 556 CONECT 1262 592 CONECT 2688 2709 CONECT 2709 2688 CONECT 3118 3119 3120 CONECT 3119 3118 CONECT 3120 3118 3121 CONECT 3121 3120 3122 CONECT 3122 3121 3123 CONECT 3123 3122 3124 CONECT 3124 3123 CONECT 3125 3133 3142 CONECT 3126 3127 3132 CONECT 3127 3126 3128 CONECT 3128 3127 3129 CONECT 3129 3128 3130 CONECT 3130 3129 3131 CONECT 3131 3130 CONECT 3132 3126 3140 3141 CONECT 3133 3125 3137 CONECT 3134 3135 3141 3147 CONECT 3135 3134 3136 3148 CONECT 3136 3135 3140 3149 CONECT 3137 3133 3139 CONECT 3138 3139 3147 3148 CONECT 3139 3137 3138 3142 CONECT 3140 3132 3136 CONECT 3141 3132 3134 CONECT 3142 3125 3139 CONECT 3143 3145 3146 3150 CONECT 3144 3145 3151 CONECT 3145 3143 3144 3152 CONECT 3146 3143 3147 3151 CONECT 3147 3134 3138 3146 CONECT 3148 3135 3138 CONECT 3149 3136 CONECT 3150 3143 CONECT 3151 3144 3146 CONECT 3152 3145 CONECT 3153 420 697 3761 3793 CONECT 3153 3830 3836 CONECT 3154 3157 CONECT 3155 3156 3158 CONECT 3156 3155 3159 CONECT 3157 3154 3161 CONECT 3158 3155 3162 CONECT 3159 3156 3163 CONECT 3160 3174 3176 CONECT 3161 3157 3164 CONECT 3162 3158 3165 CONECT 3163 3159 3166 CONECT 3164 3161 3167 CONECT 3165 3162 3167 CONECT 3166 3163 3168 CONECT 3167 3164 3165 CONECT 3168 3166 3169 CONECT 3169 3168 3170 CONECT 3170 3169 3171 CONECT 3171 3170 3173 CONECT 3172 3174 3178 CONECT 3173 3171 3175 3178 CONECT 3174 3160 3172 3177 CONECT 3175 3173 CONECT 3176 3160 CONECT 3177 3174 CONECT 3178 3172 3173 CONECT 3179 3180 3181 3182 CONECT 3180 3179 CONECT 3181 3179 CONECT 3182 3179 3183 CONECT 3183 3182 3184 CONECT 3184 3183 3185 CONECT 3185 3184 3186 CONECT 3186 3185 3187 CONECT 3187 3186 3188 CONECT 3188 3187 3189 CONECT 3189 3188 3190 CONECT 3190 3189 3191 CONECT 3191 3190 3192 CONECT 3192 3191 3193 CONECT 3193 3192 3194 CONECT 3194 3193 3195 CONECT 3195 3194 3196 CONECT 3196 3195 CONECT 3197 3200 CONECT 3198 3199 3201 CONECT 3199 3198 3202 CONECT 3200 3197 3204 CONECT 3201 3198 3205 CONECT 3202 3199 3206 CONECT 3203 3217 3219 CONECT 3204 3200 3207 CONECT 3205 3201 3208 CONECT 3206 3202 3209 CONECT 3207 3204 3210 CONECT 3208 3205 3210 CONECT 3209 3206 3211 CONECT 3210 3207 3208 CONECT 3211 3209 3212 CONECT 3212 3211 3213 CONECT 3213 3212 3214 CONECT 3214 3213 3216 CONECT 3215 3217 3221 CONECT 3216 3214 3218 3221 CONECT 3217 3203 3215 3220 CONECT 3218 3216 CONECT 3219 3203 CONECT 3220 3217 CONECT 3221 3215 3216 CONECT 3222 3223 3224 3225 CONECT 3223 3222 CONECT 3224 3222 CONECT 3225 3222 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 3236 CONECT 3236 3235 3237 CONECT 3237 3236 3238 CONECT 3238 3237 3239 CONECT 3239 3238 3240 CONECT 3240 3239 3241 CONECT 3241 3240 CONECT 3242 3243 3244 3245 CONECT 3243 3242 CONECT 3244 3242 CONECT 3245 3242 3246 CONECT 3246 3245 3247 CONECT 3247 3246 3248 CONECT 3248 3247 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 3252 CONECT 3252 3251 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3255 CONECT 3255 3254 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 CONECT 3262 3263 3271 CONECT 3263 3262 3264 CONECT 3264 3263 3265 3289 CONECT 3265 3264 3266 CONECT 3266 3265 3267 3271 CONECT 3267 3266 3268 CONECT 3268 3267 3269 CONECT 3269 3268 3270 3275 CONECT 3270 3269 3271 3272 CONECT 3271 3262 3266 3270 3280 CONECT 3272 3270 3273 CONECT 3273 3272 3274 CONECT 3274 3273 3275 3278 3279 CONECT 3275 3269 3274 3276 CONECT 3276 3275 3277 CONECT 3277 3276 3278 CONECT 3278 3274 3277 3281 CONECT 3279 3274 CONECT 3280 3271 CONECT 3281 3278 3282 3283 CONECT 3282 3281 CONECT 3283 3281 3284 CONECT 3284 3283 3285 CONECT 3285 3284 3286 CONECT 3286 3285 3287 3288 CONECT 3287 3286 CONECT 3288 3286 CONECT 3289 3264 CONECT 3290 3291 3299 CONECT 3291 3290 3292 CONECT 3292 3291 3293 3317 CONECT 3293 3292 3294 CONECT 3294 3293 3295 3299 CONECT 3295 3294 3296 CONECT 3296 3295 3297 CONECT 3297 3296 3298 3303 CONECT 3298 3297 3299 3300 CONECT 3299 3290 3294 3298 3308 CONECT 3300 3298 3301 CONECT 3301 3300 3302 CONECT 3302 3301 3303 3306 3307 CONECT 3303 3297 3302 3304 CONECT 3304 3303 3305 CONECT 3305 3304 3306 CONECT 3306 3302 3305 3309 CONECT 3307 3302 CONECT 3308 3299 CONECT 3309 3306 3310 3311 CONECT 3310 3309 CONECT 3311 3309 3312 CONECT 3312 3311 3313 CONECT 3313 3312 3314 CONECT 3314 3313 3315 3316 CONECT 3315 3314 CONECT 3316 3314 CONECT 3317 3292 CONECT 3318 3319 3327 CONECT 3319 3318 3320 CONECT 3320 3319 3321 3345 CONECT 3321 3320 3322 CONECT 3322 3321 3323 3327 CONECT 3323 3322 3324 CONECT 3324 3323 3325 CONECT 3325 3324 3326 3331 CONECT 3326 3325 3327 3328 CONECT 3327 3318 3322 3326 3336 CONECT 3328 3326 3329 CONECT 3329 3328 3330 CONECT 3330 3329 3331 3334 3335 CONECT 3331 3325 3330 3332 CONECT 3332 3331 3333 CONECT 3333 3332 3334 CONECT 3334 3330 3333 3337 CONECT 3335 3330 CONECT 3336 3327 CONECT 3337 3334 3338 3339 CONECT 3338 3337 CONECT 3339 3337 3340 CONECT 3340 3339 3341 CONECT 3341 3340 3342 CONECT 3342 3341 3343 3344 CONECT 3343 3342 CONECT 3344 3342 CONECT 3345 3320 CONECT 3346 3347 3348 3349 CONECT 3347 3346 CONECT 3348 3346 CONECT 3349 3346 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 3353 CONECT 3353 3352 3354 CONECT 3354 3353 3355 CONECT 3355 3354 3356 CONECT 3356 3355 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 3365 CONECT 3365 3364 CONECT 3366 3367 CONECT 3367 3366 3368 CONECT 3368 3367 3369 CONECT 3369 3368 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 CONECT 3374 3373 3375 CONECT 3375 3374 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3379 CONECT 3379 3378 CONECT 3380 3381 3382 3383 CONECT 3381 3380 CONECT 3382 3380 CONECT 3383 3380 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 CONECT 3389 3390 3391 3392 CONECT 3390 3389 CONECT 3391 3389 CONECT 3392 3389 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 CONECT 3403 3402 3404 CONECT 3404 3403 3405 CONECT 3405 3404 CONECT 3406 3407 3408 3409 CONECT 3407 3406 CONECT 3408 3406 CONECT 3409 3406 3410 CONECT 3410 3409 3411 CONECT 3411 3410 3412 CONECT 3412 3411 3413 CONECT 3413 3412 3414 CONECT 3414 3413 3415 CONECT 3415 3414 3416 CONECT 3416 3415 3417 CONECT 3417 3416 CONECT 3418 3419 3420 3421 CONECT 3419 3418 CONECT 3420 3418 CONECT 3421 3418 3422 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 3428 CONECT 3428 3427 3429 CONECT 3429 3428 3430 CONECT 3430 3429 3431 CONECT 3431 3430 3432 CONECT 3432 3431 CONECT 3433 3434 3435 3436 CONECT 3434 3433 CONECT 3435 3433 CONECT 3436 3433 3437 CONECT 3437 3436 3438 CONECT 3438 3437 3439 CONECT 3439 3438 3440 CONECT 3440 3439 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3442 CONECT 3444 3445 CONECT 3445 3444 3446 CONECT 3446 3445 3447 CONECT 3447 3446 3448 CONECT 3448 3447 3449 CONECT 3449 3448 3450 CONECT 3450 3449 3451 CONECT 3451 3450 3452 CONECT 3452 3451 3453 CONECT 3453 3452 3454 CONECT 3454 3453 CONECT 3455 3456 CONECT 3456 3455 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3459 CONECT 3459 3458 3460 CONECT 3460 3459 3461 CONECT 3461 3460 3462 CONECT 3462 3461 3463 CONECT 3463 3462 3464 CONECT 3464 3463 3465 CONECT 3465 3464 3466 CONECT 3466 3465 CONECT 3467 3468 3469 3470 CONECT 3468 3467 CONECT 3469 3467 CONECT 3470 3467 3471 CONECT 3471 3470 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 3475 CONECT 3475 3474 3476 CONECT 3476 3475 3477 CONECT 3477 3476 3478 CONECT 3478 3477 3479 CONECT 3479 3478 3480 CONECT 3480 3479 3481 CONECT 3481 3480 CONECT 3482 3484 CONECT 3483 3492 3494 CONECT 3484 3482 3485 CONECT 3485 3484 3486 CONECT 3486 3485 3487 CONECT 3487 3486 3488 CONECT 3488 3487 3489 CONECT 3489 3488 3491 CONECT 3490 3492 3496 CONECT 3491 3489 3493 3496 CONECT 3492 3483 3490 3495 CONECT 3493 3491 CONECT 3494 3483 CONECT 3495 3492 CONECT 3496 3490 3491 CONECT 3497 3502 3504 CONECT 3498 3499 CONECT 3499 3498 3501 CONECT 3500 3502 3506 CONECT 3501 3499 3503 3506 CONECT 3502 3497 3500 3505 CONECT 3503 3501 CONECT 3504 3497 CONECT 3505 3502 CONECT 3506 3500 3501 CONECT 3507 3508 3509 3510 CONECT 3508 3507 CONECT 3509 3507 CONECT 3510 3507 3511 CONECT 3511 3510 3512 CONECT 3512 3511 3513 CONECT 3513 3512 3514 CONECT 3514 3513 3515 CONECT 3515 3514 3516 CONECT 3516 3515 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3522 CONECT 3522 3521 3523 CONECT 3523 3522 3524 CONECT 3524 3523 3525 CONECT 3525 3524 CONECT 3526 3527 3528 3529 CONECT 3527 3526 CONECT 3528 3526 CONECT 3529 3526 3530 CONECT 3530 3529 3531 CONECT 3531 3530 3532 CONECT 3532 3531 3533 CONECT 3533 3532 3534 CONECT 3534 3533 3535 CONECT 3535 3534 3536 CONECT 3536 3535 3537 CONECT 3537 3536 3538 CONECT 3538 3537 3539 CONECT 3539 3538 3540 CONECT 3540 3539 CONECT 3541 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3545 CONECT 3545 3544 3546 CONECT 3546 3545 3547 CONECT 3547 3546 3548 CONECT 3548 3547 3549 CONECT 3549 3548 3550 CONECT 3550 3549 3551 CONECT 3551 3550 CONECT 3552 3553 CONECT 3553 3552 3554 CONECT 3554 3553 3555 CONECT 3555 3554 3556 CONECT 3556 3555 3557 CONECT 3557 3556 3558 CONECT 3558 3557 3559 CONECT 3559 3558 3560 CONECT 3560 3559 3561 CONECT 3561 3560 CONECT 3562 3563 CONECT 3563 3562 3564 CONECT 3564 3563 3565 CONECT 3565 3564 3566 CONECT 3566 3565 3567 CONECT 3567 3566 3568 CONECT 3568 3567 3569 CONECT 3569 3568 3570 CONECT 3570 3569 3571 CONECT 3571 3570 3572 CONECT 3572 3571 3573 CONECT 3573 3572 3574 CONECT 3574 3573 CONECT 3575 3576 3577 3578 CONECT 3576 3575 CONECT 3577 3575 CONECT 3578 3575 3579 CONECT 3579 3578 3580 CONECT 3580 3579 3581 CONECT 3581 3580 3582 CONECT 3582 3581 3583 CONECT 3583 3582 CONECT 3584 3585 3586 3587 CONECT 3585 3584 CONECT 3586 3584 CONECT 3587 3584 3588 CONECT 3588 3587 3589 CONECT 3589 3588 3590 CONECT 3590 3589 CONECT 3591 3592 3593 3594 CONECT 3592 3591 CONECT 3593 3591 CONECT 3594 3591 3595 CONECT 3595 3594 3596 CONECT 3596 3595 3597 CONECT 3597 3596 3598 CONECT 3598 3597 3599 CONECT 3599 3598 3600 CONECT 3600 3599 3601 CONECT 3601 3600 3602 CONECT 3602 3601 3603 CONECT 3603 3602 3604 CONECT 3604 3603 3605 CONECT 3605 3604 3606 CONECT 3606 3605 3607 CONECT 3607 3606 3608 CONECT 3608 3607 3609 CONECT 3609 3608 3610 CONECT 3610 3609 CONECT 3611 3612 3613 3614 CONECT 3612 3611 CONECT 3613 3611 CONECT 3614 3611 3615 CONECT 3615 3614 3616 CONECT 3616 3615 3617 CONECT 3617 3616 3618 CONECT 3618 3617 3619 CONECT 3619 3618 3620 CONECT 3620 3619 3621 CONECT 3621 3620 3622 CONECT 3622 3621 3623 CONECT 3623 3622 CONECT 3624 3625 3626 3627 CONECT 3625 3624 CONECT 3626 3624 CONECT 3627 3624 3628 CONECT 3628 3627 3629 CONECT 3629 3628 3630 CONECT 3630 3629 3631 CONECT 3631 3630 3632 CONECT 3632 3631 3633 CONECT 3633 3632 3634 CONECT 3634 3633 3635 CONECT 3635 3634 3636 CONECT 3636 3635 3637 CONECT 3637 3636 3638 CONECT 3638 3637 3639 CONECT 3639 3638 3640 CONECT 3640 3639 3641 CONECT 3641 3640 CONECT 3642 3643 3645 3646 3647 CONECT 3643 3642 3644 CONECT 3644 3643 CONECT 3645 3642 CONECT 3646 3642 CONECT 3647 3642 CONECT 3648 3649 3650 CONECT 3649 3648 CONECT 3650 3648 3651 CONECT 3651 3650 3652 CONECT 3652 3651 3653 CONECT 3653 3652 3654 CONECT 3654 3653 CONECT 3655 3656 3657 CONECT 3656 3655 CONECT 3657 3655 3658 CONECT 3658 3657 3659 CONECT 3659 3658 3660 CONECT 3660 3659 3661 CONECT 3661 3660 CONECT 3662 3663 3664 CONECT 3663 3662 CONECT 3664 3662 3665 CONECT 3665 3664 3666 CONECT 3666 3665 3667 CONECT 3667 3666 3668 CONECT 3668 3667 CONECT 3669 3672 CONECT 3670 3671 3673 CONECT 3671 3670 3674 CONECT 3672 3669 3676 CONECT 3673 3670 3677 CONECT 3674 3671 3678 CONECT 3675 3689 3691 CONECT 3676 3672 3679 CONECT 3677 3673 3680 CONECT 3678 3674 3681 CONECT 3679 3676 3682 CONECT 3680 3677 3682 CONECT 3681 3678 3683 CONECT 3682 3679 3680 CONECT 3683 3681 3684 CONECT 3684 3683 3685 CONECT 3685 3684 3686 CONECT 3686 3685 3688 CONECT 3687 3689 3693 CONECT 3688 3686 3690 3693 CONECT 3689 3675 3687 3692 CONECT 3690 3688 CONECT 3691 3675 CONECT 3692 3689 CONECT 3693 3687 3688 CONECT 3694 3697 CONECT 3695 3696 3698 CONECT 3696 3695 3699 CONECT 3697 3694 3701 CONECT 3698 3695 3702 CONECT 3699 3696 3703 CONECT 3700 3714 3716 CONECT 3701 3697 3704 CONECT 3702 3698 3705 CONECT 3703 3699 3706 CONECT 3704 3701 3707 CONECT 3705 3702 3707 CONECT 3706 3703 3708 CONECT 3707 3704 3705 CONECT 3708 3706 3709 CONECT 3709 3708 3710 CONECT 3710 3709 3711 CONECT 3711 3710 3713 CONECT 3712 3714 3718 CONECT 3713 3711 3715 3718 CONECT 3714 3700 3712 3717 CONECT 3715 3713 CONECT 3716 3700 CONECT 3717 3714 CONECT 3718 3712 3713 CONECT 3719 3722 CONECT 3720 3721 3723 CONECT 3721 3720 3724 CONECT 3722 3719 3726 CONECT 3723 3720 3727 CONECT 3724 3721 3728 CONECT 3725 3739 3741 CONECT 3726 3722 3729 CONECT 3727 3723 3730 CONECT 3728 3724 3731 CONECT 3729 3726 3732 CONECT 3730 3727 3732 CONECT 3731 3728 3733 CONECT 3732 3729 3730 CONECT 3733 3731 3734 CONECT 3734 3733 3735 CONECT 3735 3734 3736 CONECT 3736 3735 3738 CONECT 3737 3739 3743 CONECT 3738 3736 3740 3743 CONECT 3739 3725 3737 3742 CONECT 3740 3738 CONECT 3741 3725 CONECT 3742 3739 CONECT 3743 3737 3738 CONECT 3761 3153 CONECT 3793 3153 CONECT 3830 3153 CONECT 3836 3153 MASTER 401 0 40 19 2 0 0 6 3860 1 641 35 END