HEADER MEMBRANE PROTEIN 18-MAY-16 5K2C TITLE 1.9 ANGSTROM A2A ADENOSINE RECEPTOR STRUCTURE WITH SULFUR SAD PHASING TITLE 2 AND PHASE EXTENSION USING XFEL DATA COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A/SOLUBLE CYTOCHROME B562 CHIMERA; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CYTOCHROME B-562; COMPND 5 ENGINEERED: 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_TAXID: 7108 KEYWDS A2A ADENOSINE RECEPTOR, SULFUR SAD, GPCR, MEMBRANE PROTEIN, KEYWDS 2 STRUCTURAL GENOMICS, PSI-BIOLOGY, GPCR NETWORK EXPDTA X-RAY DIFFRACTION AUTHOR A.BATYUK,L.GALLI,A.ISHCHENKO,G.W.HAN,C.GATI,P.POPOV,M.-Y.LEE, AUTHOR 2 B.STAUCH,T.A.WHITE,A.BARTY,A.AQUILA,M.S.HUNTER,M.LIANG,S.BOUTET, AUTHOR 3 M.PU,Z.-J.LIU,G.NELSON,D.JAMES,C.LI,Y.ZHAO,J.C.H.SPENCE,W.LIU, AUTHOR 4 P.FROMME,V.KATRITCH,U.WEIERSTALL,R.C.STEVENS,V.CHEREZOV,GPCR NETWORK AUTHOR 5 (GPCR) REVDAT 6 28-NOV-18 5K2C 1 REMARK REVDAT 5 14-FEB-18 5K2C 1 REMARK REVDAT 4 22-NOV-17 5K2C 1 REMARK REVDAT 3 23-NOV-16 5K2C 1 AUTHOR REVDAT 2 12-OCT-16 5K2C 1 JRNL REVDAT 1 21-SEP-16 5K2C 0 JRNL AUTH A.BATYUK,L.GALLI,A.ISHCHENKO,G.W.HAN,C.GATI,P.A.POPOV, JRNL AUTH 2 M.Y.LEE,B.STAUCH,T.A.WHITE,A.BARTY,A.AQUILA,M.S.HUNTER, JRNL AUTH 3 M.LIANG,S.BOUTET,M.PU,Z.J.LIU,G.NELSON,D.JAMES,C.LI,Y.ZHAO, JRNL AUTH 4 J.C.SPENCE,W.LIU,P.FROMME,V.KATRITCH,U.WEIERSTALL, JRNL AUTH 5 R.C.STEVENS,V.CHEREZOV JRNL TITL NATIVE PHASING OF X-RAY FREE-ELECTRON LASER DATA FOR A G JRNL TITL 2 PROTEIN-COUPLED RECEPTOR. JRNL REF SCI ADV V. 2 00292 2016 JRNL REFN ESSN 2375-2548 JRNL PMID 27679816 JRNL DOI 10.1126/SCIADV.1600292 REMARK 2 REMARK 2 RESOLUTION. 1.90 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.10_2155 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 : MLHL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 23.44 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 41828 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.174 REMARK 3 R VALUE (WORKING SET) : 0.173 REMARK 3 FREE R VALUE : 0.208 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.750 REMARK 3 FREE R VALUE TEST SET COUNT : 1988 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 23.4386 - 4.5688 1.00 3023 157 0.1864 0.2188 REMARK 3 2 4.5688 - 3.6307 1.00 2920 135 0.1442 0.1878 REMARK 3 3 3.6307 - 3.1730 1.00 2882 146 0.1439 0.1650 REMARK 3 4 3.1730 - 2.8835 1.00 2826 144 0.1399 0.2158 REMARK 3 5 2.8835 - 2.6771 1.00 2861 135 0.1363 0.1500 REMARK 3 6 2.6771 - 2.5195 1.00 2807 167 0.1416 0.1795 REMARK 3 7 2.5195 - 2.3934 1.00 2828 135 0.1524 0.1954 REMARK 3 8 2.3934 - 2.2893 1.00 2860 124 0.1722 0.2273 REMARK 3 9 2.2893 - 2.2013 1.00 2795 158 0.1966 0.2351 REMARK 3 10 2.2013 - 2.1254 1.00 2797 137 0.2239 0.2218 REMARK 3 11 2.1254 - 2.0589 1.00 2835 135 0.2498 0.2888 REMARK 3 12 2.0589 - 2.0001 1.00 2797 126 0.3167 0.3305 REMARK 3 13 2.0001 - 1.9475 1.00 2794 171 0.4180 0.4154 REMARK 3 14 1.9475 - 1.9000 1.00 2815 118 0.4519 0.4335 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.750 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 46.90 REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.010 3598 REMARK 3 ANGLE : 1.176 4848 REMARK 3 CHIRALITY : 0.059 558 REMARK 3 PLANARITY : 0.006 576 REMARK 3 DIHEDRAL : 15.025 2166 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 -2 THROUGH 208 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.9021 84.3288 50.2567 REMARK 3 T TENSOR REMARK 3 T11: 0.2298 T22: 0.2809 REMARK 3 T33: 0.2130 T12: -0.0089 REMARK 3 T13: 0.0152 T23: -0.0107 REMARK 3 L TENSOR REMARK 3 L11: 1.3440 L22: 2.1970 REMARK 3 L33: 1.7016 L12: 0.2544 REMARK 3 L13: 0.1445 L23: -0.1463 REMARK 3 S TENSOR REMARK 3 S11: -0.0082 S12: 0.0495 S13: -0.0212 REMARK 3 S21: -0.0713 S22: 0.0127 S23: -0.0549 REMARK 3 S31: 0.0522 S32: 0.0898 S33: -0.0053 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1106 ) REMARK 3 ORIGIN FOR THE GROUP (A): -20.7709 35.7680 51.4366 REMARK 3 T TENSOR REMARK 3 T11: 0.7951 T22: 0.5561 REMARK 3 T33: 1.2393 T12: -0.1141 REMARK 3 T13: -0.0758 T23: 0.1081 REMARK 3 L TENSOR REMARK 3 L11: 3.6718 L22: 7.9756 REMARK 3 L33: 2.9104 L12: -2.8653 REMARK 3 L13: 0.9945 L23: 3.0315 REMARK 3 S TENSOR REMARK 3 S11: 0.3390 S12: 0.3484 S13: -0.2607 REMARK 3 S21: 0.4511 S22: 0.1546 S23: 0.2084 REMARK 3 S31: 0.2985 S32: -0.0893 S33: -0.5671 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 308) REMARK 3 ORIGIN FOR THE GROUP (A): -1.6374 79.2198 60.4654 REMARK 3 T TENSOR REMARK 3 T11: 0.2576 T22: 0.2658 REMARK 3 T33: 0.1989 T12: -0.0310 REMARK 3 T13: 0.0456 T23: -0.0108 REMARK 3 L TENSOR REMARK 3 L11: 1.2956 L22: 5.3643 REMARK 3 L33: 1.7308 L12: -0.8150 REMARK 3 L13: 0.3292 L23: -0.4918 REMARK 3 S TENSOR REMARK 3 S11: 0.0061 S12: -0.1086 S13: -0.1512 REMARK 3 S21: 0.4416 S22: 0.0165 S23: 0.1308 REMARK 3 S31: 0.2480 S32: 0.0098 S33: -0.0140 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 5K2C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-MAY-16. REMARK 100 THE DEPOSITION ID IS D_1000221568. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 01-APR-15 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : 5.0 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : N REMARK 200 RADIATION SOURCE : FREE ELECTRON LASER REMARK 200 BEAMLINE : CXI REMARK 200 X-RAY GENERATOR MODEL : SLAC LCLS BEAMLINE CXI REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.27 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : K-B MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : CS-PAD CXI-1 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : CRYSTFEL REMARK 200 DATA SCALING SOFTWARE : CRYSTFEL REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41882 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900 REMARK 200 RESOLUTION RANGE LOW (A) : 24.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 291.0 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 62.00 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD REMARK 200 SOFTWARE USED: SHELXD, PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.79 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 28 % (V/V) PEG 400, 40 MM SODIUM REMARK 280 THIOCYANATE AND 100 MM SODIUM CITRATE BUFFER PH 5.0, 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 71.40000 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 71.40000 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 20.18000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 90.37000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 20.18000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 90.37000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 71.40000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 20.18000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 90.37000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 71.40000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 20.18000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 90.37000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 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 ASP A -3 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 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 ASP A -2 OD1 OD2 REMARK 470 ARG A 107 CZ NH1 NH2 REMARK 470 GLN A 148 CD OE1 NE2 REMARK 470 GLU A 161 CG CD OE1 OE2 REMARK 470 ARG A 199 NE CZ NH1 NH2 REMARK 470 LYS A1015 CE NZ REMARK 470 ASP A1021 CG OD1 OD2 REMARK 470 GLN A1025 CG CD OE1 NE2 REMARK 470 GLU A1057 CG CD OE1 OE2 REMARK 470 MET A1058 CG SD CE REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 ARG A1062 CZ NH1 NH2 REMARK 470 LYS A1077 CD CE NZ REMARK 470 GLN A1093 CG CD OE1 NE2 REMARK 470 LYS A1095 CD CE NZ REMARK 470 ARG A 220 CD NE CZ NH1 NH2 REMARK 470 ARG A 222 NE CZ NH1 NH2 REMARK 470 GLN A 226 CD OE1 NE2 REMARK 470 LYS A 227 CE NZ REMARK 470 LYS A 301 CE NZ REMARK 470 VAL A 307 CG1 CG2 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 1398 O HOH A 1400 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O GLY A -1 NH2 ARG A 300 4566 2.10 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -53.79 -122.55 REMARK 500 TYR A1101 -47.64 -134.84 REMARK 500 VAL A 307 -6.63 -146.31 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLC A 1206 REMARK 610 OLC A 1207 REMARK 610 OLC A 1208 REMARK 610 OLC A 1209 REMARK 610 OLC A 1210 REMARK 610 OLC A 1211 REMARK 610 OLC A 1212 REMARK 610 OLC A 1213 REMARK 610 OLC 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 OLA A 1222 REMARK 610 OLA A 1223 REMARK 610 OLA A 1225 REMARK 610 OLC A 1227 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A1202 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 132.5 REMARK 620 3 HOH A1332 O 82.6 116.7 REMARK 620 4 HOH A1315 O 105.4 117.9 87.1 REMARK 620 5 HOH A1381 O 81.2 77.4 163.4 93.9 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZMA A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1223 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1224 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1225 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 1226 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1227 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5K2A RELATED DB: PDB REMARK 900 RELATED ID: 5K2B RELATED DB: PDB REMARK 900 RELATED ID: 5K2D RELATED DB: PDB DBREF 5K2C A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5K2C A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5K2C A 219 316 UNP P29274 AA2AR_HUMAN 219 316 SEQADV 5K2C MET A -24 UNP P29274 INITIATING METHIONINE SEQADV 5K2C LYS A -23 UNP P29274 EXPRESSION TAG SEQADV 5K2C THR A -22 UNP P29274 EXPRESSION TAG SEQADV 5K2C ILE A -21 UNP P29274 EXPRESSION TAG SEQADV 5K2C ILE A -20 UNP P29274 EXPRESSION TAG SEQADV 5K2C ALA A -19 UNP P29274 EXPRESSION TAG SEQADV 5K2C LEU A -18 UNP P29274 EXPRESSION TAG SEQADV 5K2C SER A -17 UNP P29274 EXPRESSION TAG SEQADV 5K2C TYR A -16 UNP P29274 EXPRESSION TAG SEQADV 5K2C ILE A -15 UNP P29274 EXPRESSION TAG SEQADV 5K2C PHE A -14 UNP P29274 EXPRESSION TAG SEQADV 5K2C CYS A -13 UNP P29274 EXPRESSION TAG SEQADV 5K2C LEU A -12 UNP P29274 EXPRESSION TAG SEQADV 5K2C VAL A -11 UNP P29274 EXPRESSION TAG SEQADV 5K2C PHE A -10 UNP P29274 EXPRESSION TAG SEQADV 5K2C ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 5K2C ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5K2C TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5K2C LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5K2C ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5K2C ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5K2C ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5K2C ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5K2C GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5K2C ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5K2C PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5K2C TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5K2C ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 5K2C LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 5K2C HIS A 317 UNP P29274 EXPRESSION TAG SEQADV 5K2C HIS A 318 UNP P29274 EXPRESSION TAG SEQADV 5K2C HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5K2C HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5K2C HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5K2C HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5K2C HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5K2C HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5K2C HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5K2C 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 ALA 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 THR 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 ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY SEQRES 12 A 447 THR ARG ALA LYS 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 ASN 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 LEU 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 LEU ALA ILE ILE VAL 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 SER 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 ZMA A1201 25 HET NA A1202 1 HET CLR A1203 28 HET CLR A1204 28 HET CLR A1205 28 HET OLC A1206 18 HET OLC A1207 11 HET OLC A1208 17 HET OLC A1209 16 HET OLC A1210 17 HET OLC A1211 14 HET OLC A1212 12 HET OLC A1213 18 HET OLC A1214 17 HET OLA A1215 12 HET OLA A1216 16 HET OLA A1217 10 HET OLA A1218 11 HET OLA A1219 9 HET OLA A1220 9 HET OLA A1221 12 HET OLA A1222 13 HET OLA A1223 11 HET OLA A1224 20 HET OLA A1225 19 HET PEG A1226 7 HET OLC A1227 16 HETNAM ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3, HETNAM 2 ZMA 5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL HETNAM NA SODIUM ION HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETNAM PEG DI(HYDROXYETHYL)ETHER HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 ZMA C16 H15 N7 O2 FORMUL 3 NA NA 1+ FORMUL 4 CLR 3(C27 H46 O) FORMUL 7 OLC 10(C21 H40 O4) FORMUL 16 OLA 11(C18 H34 O2) FORMUL 27 PEG C4 H10 O3 FORMUL 29 HOH *105(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 THR A 68 1 11 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ILE A 108 VAL A 116 1 9 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLY A 158 1 9 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 ALA A 1020 1 43 HELIX 13 AB4 ASN A 1022 ALA A 1043 1 22 HELIX 14 AB5 GLU A 1057 GLU A 1081 1 25 HELIX 15 AB6 LYS A 1083 TYR A 1101 1 19 HELIX 16 AB7 TYR A 1101 CYS A 259 1 47 HELIX 17 AB8 PRO A 266 ILE A 292 1 27 HELIX 18 AB9 ILE A 292 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 2.02 SSBOND 2 CYS A 74 CYS A 146 1555 1555 1.95 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.02 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 LINK OD1 ASP A 52 NA NA A1202 1555 1555 2.36 LINK OG SER A 91 NA NA A1202 1555 1555 2.49 LINK NA NA A1202 O HOH A1332 1555 1555 2.37 LINK NA NA A1202 O HOH A1315 1555 1555 2.46 LINK NA NA A1202 O HOH A1381 1555 1555 2.39 SITE 1 AC1 11 PHE A 168 GLU A 169 MET A 177 TRP A 246 SITE 2 AC1 11 LEU A 249 HIS A 250 ASN A 253 MET A 270 SITE 3 AC1 11 HOH A1320 HOH A1322 HOH A1375 SITE 1 AC2 5 ASP A 52 SER A 91 HOH A1315 HOH A1332 SITE 2 AC2 5 HOH A1381 SITE 1 AC3 7 ALA A 72 ALA A 73 ILE A 80 CLR A1205 SITE 2 AC3 7 OLC A1206 OLC A1207 OLC A1227 SITE 1 AC4 5 CYS A 262 SER A 263 OLC A1212 OLC A1214 SITE 2 AC4 5 OLA A1217 SITE 1 AC5 4 CLR A1203 OLC A1206 OLC A1214 HOH A1337 SITE 1 AC6 5 PHE A 70 CLR A1203 CLR A1205 OLC A1211 SITE 2 AC6 5 OLC A1214 SITE 1 AC7 1 CLR A1203 SITE 1 AC8 4 VAL A 31 TRP A 32 VAL A 46 OLA A1225 SITE 1 AC9 5 TYR A 43 LYS A 122 ILE A 125 TRP A 129 SITE 2 AC9 5 OLA A1224 SITE 1 AD1 6 MET A 140 LEU A 141 TYR A 179 ALA A 184 SITE 2 AD1 6 OLA A1221 OLA A1224 SITE 1 AD2 4 ILE A 64 THR A 65 OLC A1206 OLC A1214 SITE 1 AD3 2 CLR A1204 OLC A1214 SITE 1 AD4 6 SER A 6 SER A 67 LEU A 267 OLA A1216 SITE 2 AD4 6 HOH A1352 HOH A1383 SITE 1 AD5 6 CLR A1204 CLR A1205 OLC A1206 OLC A1211 SITE 2 AD5 6 OLC A1212 HOH A1380 SITE 1 AD6 1 TRP A 268 SITE 1 AD7 2 TYR A 290 OLC A1213 SITE 1 AD8 1 CLR A1204 SITE 1 AD9 1 ILE A 10 SITE 1 AE1 2 SER A 7 THR A 11 SITE 1 AE2 2 ALA A 97 CYS A 128 SITE 1 AE3 6 TYR A 179 PHE A 258 OLC A1210 OLC A1227 SITE 2 AE3 6 HOH A1360 HOH A1374 SITE 1 AE4 1 LEU A 244 SITE 1 AE5 3 SER A 7 TRP A 29 PHE A 286 SITE 1 AE6 2 OLC A1209 OLC A1210 SITE 1 AE7 6 TRP A 29 TRP A 32 PHE A 201 VAL A 229 SITE 2 AE7 6 LYS A 233 OLC A1208 SITE 1 AE8 3 ARG A 120 GLY A 123 ILE A 127 SITE 1 AE9 3 PHE A 258 CLR A1203 OLA A1221 CRYST1 40.360 180.740 142.800 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 0.024777 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005533 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007003 0.00000 ATOM 1 N ASP A -2 2.444 119.371 68.094 1.00109.11 N ANISOU 1 N ASP A -2 17059 10617 13779 -279 81 -2326 N ATOM 2 CA ASP A -2 2.847 118.403 69.110 1.00109.10 C ANISOU 2 CA ASP A -2 17047 10836 13571 -359 71 -2390 C ATOM 3 C ASP A -2 2.680 116.975 68.607 1.00109.05 C ANISOU 3 C ASP A -2 16797 11098 13539 -325 103 -2240 C ATOM 4 O ASP A -2 3.018 116.675 67.461 1.00107.90 O ANISOU 4 O ASP A -2 16480 11012 13505 -371 41 -2063 O ATOM 5 CB ASP A -2 2.044 118.603 70.398 1.00107.12 C ANISOU 5 CB ASP A -2 16884 10607 13210 -223 199 -2559 C ATOM 6 CG ASP A -2 2.723 119.544 71.372 1.00103.54 C ANISOU 6 CG ASP A -2 16588 10062 12690 -339 111 -2690 C ATOM 7 N GLY A -1 2.155 116.100 69.469 1.00103.26 N ANISOU 7 N GLY A -1 16043 10534 12656 -247 204 -2304 N ATOM 8 CA GLY A -1 2.009 114.689 69.150 1.00 96.98 C ANISOU 8 CA GLY A -1 15021 10002 11824 -223 232 -2169 C ATOM 9 C GLY A -1 3.086 113.826 69.781 1.00 88.63 C ANISOU 9 C GLY A -1 13950 9124 10600 -397 117 -2158 C ATOM 10 O GLY A -1 4.245 114.247 69.850 1.00 86.79 O ANISOU 10 O GLY A -1 13786 8836 10354 -579 -39 -2167 O ATOM 11 N ALA A 0 2.720 112.635 70.257 1.00 81.05 N ANISOU 11 N ALA A 0 12901 8373 9520 -347 187 -2135 N ATOM 12 CA ALA A 0 3.683 111.737 70.882 1.00 77.82 C ANISOU 12 CA ALA A 0 12476 8137 8954 -493 75 -2114 C ATOM 13 C ALA A 0 4.868 111.497 69.945 1.00 73.31 C ANISOU 13 C ALA A 0 11756 7619 8480 -644 -91 -1965 C ATOM 14 O ALA A 0 4.659 111.262 68.751 1.00 75.18 O ANISOU 14 O ALA A 0 11819 7882 8865 -594 -69 -1827 O ATOM 15 CB ALA A 0 3.018 110.405 71.220 1.00 72.38 C ANISOU 15 CB ALA A 0 11675 7659 8165 -401 183 -2064 C ATOM 16 N PRO A 1 6.109 111.576 70.431 1.00 64.29 N ANISOU 16 N PRO A 1 10674 6493 7261 -827 -256 -1991 N ATOM 17 CA PRO A 1 7.271 111.311 69.563 1.00 56.30 C ANISOU 17 CA PRO A 1 9496 5546 6348 -970 -400 -1850 C ATOM 18 C PRO A 1 7.099 110.005 68.810 1.00 56.86 C ANISOU 18 C PRO A 1 9331 5814 6458 -904 -357 -1690 C ATOM 19 O PRO A 1 6.740 108.973 69.399 1.00 52.40 O ANISOU 19 O PRO A 1 8735 5402 5775 -843 -308 -1686 O ATOM 20 CB PRO A 1 8.446 111.235 70.544 1.00 60.39 C ANISOU 20 CB PRO A 1 10099 6113 6732 -1149 -570 -1913 C ATOM 21 CG PRO A 1 8.019 112.106 71.710 1.00 59.72 C ANISOU 21 CG PRO A 1 10290 5883 6520 -1135 -539 -2113 C ATOM 22 CD PRO A 1 6.507 111.971 71.798 1.00 59.86 C ANISOU 22 CD PRO A 1 10338 5886 6520 -916 -322 -2156 C ATOM 23 N PRO A 2 7.312 110.025 67.493 1.00 51.48 N ANISOU 23 N PRO A 2 8493 5129 5937 -913 -367 -1555 N ATOM 24 CA PRO A 2 7.038 108.825 66.689 1.00 48.77 C ANISOU 24 CA PRO A 2 7941 4956 5634 -838 -313 -1414 C ATOM 25 C PRO A 2 7.889 107.626 67.075 1.00 44.73 C ANISOU 25 C PRO A 2 7325 4639 5033 -914 -399 -1359 C ATOM 26 O PRO A 2 7.455 106.482 66.885 1.00 44.68 O ANISOU 26 O PRO A 2 7199 4774 5002 -829 -338 -1287 O ATOM 27 CB PRO A 2 7.344 109.288 65.252 1.00 53.61 C ANISOU 27 CB PRO A 2 8447 5503 6417 -872 -332 -1295 C ATOM 28 CG PRO A 2 7.191 110.755 65.273 1.00 52.65 C ANISOU 28 CG PRO A 2 8491 5153 6359 -891 -337 -1376 C ATOM 29 CD PRO A 2 7.627 111.204 66.665 1.00 52.99 C ANISOU 29 CD PRO A 2 8718 5141 6276 -977 -405 -1533 C ATOM 30 N ILE A 3 9.088 107.857 67.609 1.00 46.64 N ANISOU 30 N ILE A 3 7606 4884 5232 -1073 -548 -1391 N ATOM 31 CA ILE A 3 9.992 106.759 67.926 1.00 49.23 C ANISOU 31 CA ILE A 3 7819 5389 5496 -1144 -651 -1328 C ATOM 32 C ILE A 3 9.429 105.845 69.026 1.00 47.42 C ANISOU 32 C ILE A 3 7657 5268 5093 -1065 -610 -1375 C ATOM 33 O ILE A 3 9.772 104.661 69.075 1.00 46.90 O ANISOU 33 O ILE A 3 7473 5358 4990 -1059 -646 -1292 O ATOM 34 CB ILE A 3 11.370 107.333 68.307 1.00 52.95 C ANISOU 34 CB ILE A 3 8318 5829 5971 -1336 -832 -1359 C ATOM 35 CG1 ILE A 3 12.431 106.240 68.339 1.00 54.89 C ANISOU 35 CG1 ILE A 3 8392 6256 6207 -1405 -948 -1264 C ATOM 36 CG2 ILE A 3 11.306 108.020 69.654 1.00 58.34 C ANISOU 36 CG2 ILE A 3 9238 6421 6506 -1385 -887 -1521 C ATOM 37 CD1 ILE A 3 13.717 106.691 68.999 1.00 62.27 C ANISOU 37 CD1 ILE A 3 9356 7183 7120 -1589 -1143 -1307 C ATOM 38 N MET A 4 8.552 106.354 69.904 1.00 45.81 N ANISOU 38 N MET A 4 7644 4980 4781 -1000 -527 -1504 N ATOM 39 CA MET A 4 7.962 105.489 70.934 1.00 48.80 C ANISOU 39 CA MET A 4 8094 5464 4985 -930 -467 -1541 C ATOM 40 C MET A 4 7.104 104.386 70.324 1.00 42.00 C ANISOU 40 C MET A 4 7078 4713 4165 -797 -337 -1434 C ATOM 41 O MET A 4 7.287 103.201 70.621 1.00 42.09 O ANISOU 41 O MET A 4 7022 4870 4101 -794 -361 -1365 O ATOM 42 CB MET A 4 7.150 106.321 71.923 1.00 44.26 C ANISOU 42 CB MET A 4 7753 4772 4291 -881 -375 -1707 C ATOM 43 CG MET A 4 7.986 107.358 72.587 1.00 43.79 C ANISOU 43 CG MET A 4 7867 4598 4175 -1020 -513 -1823 C ATOM 44 SD MET A 4 7.159 108.305 73.868 1.00 55.17 S ANISOU 44 SD MET A 4 9617 5900 5446 -971 -412 -2041 S ATOM 45 CE MET A 4 7.000 107.071 75.174 1.00 57.17 C ANISOU 45 CE MET A 4 9947 6341 5436 -958 -399 -2052 C ATOM 46 N GLY A 5 6.152 104.748 69.461 1.00 40.01 N ANISOU 46 N GLY A 5 6773 4391 4038 -689 -206 -1416 N ATOM 47 CA GLY A 5 5.383 103.719 68.790 1.00 37.25 C ANISOU 47 CA GLY A 5 6269 4145 3741 -581 -103 -1312 C ATOM 48 C GLY A 5 6.220 102.870 67.847 1.00 41.85 C ANISOU 48 C GLY A 5 6661 4831 4409 -631 -190 -1171 C ATOM 49 O GLY A 5 5.975 101.664 67.712 1.00 38.36 O ANISOU 49 O GLY A 5 6117 4512 3947 -583 -156 -1092 O ATOM 50 N SER A 6 7.228 103.467 67.194 1.00 39.84 N ANISOU 50 N SER A 6 6360 4527 4252 -732 -296 -1139 N ATOM 51 CA SER A 6 8.087 102.669 66.307 1.00 43.95 C ANISOU 51 CA SER A 6 6696 5150 4851 -777 -365 -1013 C ATOM 52 C SER A 6 8.850 101.604 67.085 1.00 38.70 C ANISOU 52 C SER A 6 6001 4621 4085 -825 -460 -987 C ATOM 53 O SER A 6 9.049 100.488 66.582 1.00 41.35 O ANISOU 53 O SER A 6 6194 5066 4451 -795 -460 -889 O ATOM 54 CB SER A 6 9.096 103.549 65.560 1.00 43.09 C ANISOU 54 CB SER A 6 6545 4969 4858 -892 -453 -986 C ATOM 55 OG SER A 6 8.432 104.356 64.632 1.00 53.65 O ANISOU 55 OG SER A 6 7890 6193 6303 -842 -371 -973 O ATOM 56 N SER A 7 9.328 101.963 68.279 1.00 38.79 N ANISOU 56 N SER A 7 6148 4614 3976 -902 -552 -1074 N ATOM 57 CA SER A 7 10.045 101.022 69.146 1.00 43.53 C ANISOU 57 CA SER A 7 6742 5334 4464 -947 -663 -1050 C ATOM 58 C SER A 7 9.196 99.803 69.475 1.00 41.61 C ANISOU 58 C SER A 7 6492 5186 4133 -838 -568 -1008 C ATOM 59 O SER A 7 9.713 98.688 69.529 1.00 38.79 O ANISOU 59 O SER A 7 6041 4937 3759 -839 -632 -923 O ATOM 60 CB SER A 7 10.476 101.703 70.446 1.00 45.52 C ANISOU 60 CB SER A 7 7182 5540 4573 -1040 -770 -1165 C ATOM 61 OG SER A 7 11.473 102.682 70.196 1.00 58.12 O ANISOU 61 OG SER A 7 8768 7060 6254 -1170 -893 -1192 O ATOM 62 N VAL A 8 7.900 100.003 69.733 1.00 39.21 N ANISOU 62 N VAL A 8 6284 4837 3778 -746 -415 -1066 N ATOM 63 CA VAL A 8 7.029 98.874 70.030 1.00 40.05 C ANISOU 63 CA VAL A 8 6378 5029 3810 -656 -312 -1023 C ATOM 64 C VAL A 8 6.890 97.998 68.799 1.00 39.50 C ANISOU 64 C VAL A 8 6114 5017 3878 -600 -271 -902 C ATOM 65 O VAL A 8 7.054 96.776 68.864 1.00 40.40 O ANISOU 65 O VAL A 8 6160 5228 3963 -583 -293 -821 O ATOM 66 CB VAL A 8 5.659 99.366 70.541 1.00 40.28 C ANISOU 66 CB VAL A 8 6533 4998 3774 -572 -143 -1115 C ATOM 67 CG1 VAL A 8 4.668 98.176 70.762 1.00 35.40 C ANISOU 67 CG1 VAL A 8 5880 4473 3098 -487 -18 -1059 C ATOM 68 CG2 VAL A 8 5.815 100.201 71.804 1.00 36.67 C ANISOU 68 CG2 VAL A 8 6292 4481 3159 -627 -176 -1249 C ATOM 69 N TYR A 9 6.619 98.622 67.642 1.00 38.00 N ANISOU 69 N TYR A 9 5842 4761 3835 -572 -220 -888 N ATOM 70 CA TYR A 9 6.419 97.883 66.406 1.00 36.01 C ANISOU 70 CA TYR A 9 5424 4555 3702 -520 -178 -784 C ATOM 71 C TYR A 9 7.653 97.050 66.051 1.00 34.71 C ANISOU 71 C TYR A 9 5141 4475 3571 -575 -293 -699 C ATOM 72 O TYR A 9 7.543 95.875 65.700 1.00 33.04 O ANISOU 72 O TYR A 9 4839 4341 3373 -530 -273 -623 O ATOM 73 CB TYR A 9 6.047 98.869 65.269 1.00 37.35 C ANISOU 73 CB TYR A 9 5553 4630 4006 -497 -127 -785 C ATOM 74 CG TYR A 9 6.172 98.279 63.901 1.00 36.74 C ANISOU 74 CG TYR A 9 5320 4597 4044 -476 -118 -682 C ATOM 75 CD1 TYR A 9 5.319 97.247 63.478 1.00 36.34 C ANISOU 75 CD1 TYR A 9 5195 4608 4004 -394 -39 -626 C ATOM 76 CD2 TYR A 9 7.152 98.718 63.027 1.00 35.23 C ANISOU 76 CD2 TYR A 9 5057 4386 3942 -545 -186 -640 C ATOM 77 CE1 TYR A 9 5.441 96.674 62.230 1.00 36.52 C ANISOU 77 CE1 TYR A 9 5093 4669 4115 -377 -35 -542 C ATOM 78 CE2 TYR A 9 7.279 98.153 61.776 1.00 34.66 C ANISOU 78 CE2 TYR A 9 4856 4359 3954 -525 -167 -551 C ATOM 79 CZ TYR A 9 6.429 97.145 61.374 1.00 36.46 C ANISOU 79 CZ TYR A 9 5028 4644 4183 -440 -95 -507 C ATOM 80 OH TYR A 9 6.600 96.598 60.123 1.00 38.65 O ANISOU 80 OH TYR A 9 5195 4962 4531 -426 -82 -430 O ATOM 81 N ILE A 10 8.833 97.643 66.147 1.00 31.99 N ANISOU 81 N ILE A 10 4793 4115 3248 -673 -415 -714 N ATOM 82 CA ILE A 10 10.074 96.956 65.754 1.00 38.98 C ANISOU 82 CA ILE A 10 5539 5079 4190 -721 -521 -635 C ATOM 83 C ILE A 10 10.365 95.774 66.697 1.00 32.47 C ANISOU 83 C ILE A 10 4728 4349 3262 -707 -588 -603 C ATOM 84 O ILE A 10 10.783 94.691 66.264 1.00 40.18 O ANISOU 84 O ILE A 10 5584 5399 4284 -675 -609 -520 O ATOM 85 CB ILE A 10 11.228 97.995 65.751 1.00 41.02 C ANISOU 85 CB ILE A 10 5790 5295 4501 -842 -636 -664 C ATOM 86 CG1 ILE A 10 11.121 98.932 64.534 1.00 38.97 C ANISOU 86 CG1 ILE A 10 5484 4954 4370 -859 -573 -654 C ATOM 87 CG2 ILE A 10 12.627 97.370 65.896 1.00 43.26 C ANISOU 87 CG2 ILE A 10 5954 5670 4812 -907 -778 -608 C ATOM 88 CD1 ILE A 10 12.103 100.112 64.593 1.00 44.61 C ANISOU 88 CD1 ILE A 10 6216 5599 5134 -992 -672 -690 C ATOM 89 N THR A 11 10.234 96.002 67.999 1.00 33.94 N ANISOU 89 N THR A 11 5068 4525 3303 -736 -630 -670 N ATOM 90 CA THR A 11 10.464 94.949 68.993 1.00 34.37 C ANISOU 90 CA THR A 11 5166 4658 3234 -728 -701 -635 C ATOM 91 C THR A 11 9.576 93.738 68.719 1.00 36.13 C ANISOU 91 C THR A 11 5350 4925 3452 -629 -589 -567 C ATOM 92 O THR A 11 10.046 92.588 68.743 1.00 35.55 O ANISOU 92 O THR A 11 5207 4919 3382 -606 -648 -484 O ATOM 93 CB THR A 11 10.194 95.512 70.390 1.00 33.54 C ANISOU 93 CB THR A 11 5268 4524 2949 -770 -729 -730 C ATOM 94 OG1 THR A 11 11.100 96.586 70.666 1.00 37.47 O ANISOU 94 OG1 THR A 11 5807 4977 3453 -877 -856 -795 O ATOM 95 CG2 THR A 11 10.419 94.417 71.501 1.00 37.69 C ANISOU 95 CG2 THR A 11 5866 5133 3320 -768 -811 -683 C ATOM 96 N VAL A 12 8.298 93.988 68.399 1.00 31.81 N ANISOU 96 N VAL A 12 4838 4335 2913 -568 -431 -598 N ATOM 97 CA VAL A 12 7.359 92.901 68.104 1.00 35.75 C ANISOU 97 CA VAL A 12 5296 4870 3417 -487 -321 -537 C ATOM 98 C VAL A 12 7.749 92.172 66.820 1.00 36.72 C ANISOU 98 C VAL A 12 5247 5020 3683 -457 -330 -452 C ATOM 99 O VAL A 12 7.776 90.930 66.780 1.00 33.35 O ANISOU 99 O VAL A 12 4775 4642 3253 -422 -336 -379 O ATOM 100 CB VAL A 12 5.911 93.440 68.054 1.00 36.51 C ANISOU 100 CB VAL A 12 5451 4917 3506 -433 -157 -595 C ATOM 101 CG1 VAL A 12 4.932 92.382 67.490 1.00 36.77 C ANISOU 101 CG1 VAL A 12 5404 4983 3584 -363 -48 -527 C ATOM 102 CG2 VAL A 12 5.471 93.951 69.448 1.00 38.48 C ANISOU 102 CG2 VAL A 12 5883 5149 3590 -451 -124 -683 C ATOM 103 N GLU A 13 8.053 92.926 65.743 1.00 30.50 N ANISOU 103 N GLU A 13 4374 4196 3019 -470 -325 -460 N ATOM 104 CA GLU A 13 8.544 92.320 64.503 1.00 31.10 C ANISOU 104 CA GLU A 13 4298 4301 3217 -449 -330 -388 C ATOM 105 C GLU A 13 9.770 91.431 64.726 1.00 30.17 C ANISOU 105 C GLU A 13 4108 4248 3107 -465 -447 -331 C ATOM 106 O GLU A 13 9.872 90.339 64.133 1.00 34.26 O ANISOU 106 O GLU A 13 4540 4802 3677 -414 -432 -267 O ATOM 107 CB GLU A 13 8.907 93.417 63.472 1.00 28.94 C ANISOU 107 CB GLU A 13 3965 3981 3051 -485 -324 -404 C ATOM 108 CG GLU A 13 7.712 94.159 62.912 1.00 32.03 C ANISOU 108 CG GLU A 13 4394 4304 3471 -447 -213 -436 C ATOM 109 CD GLU A 13 7.022 93.421 61.743 1.00 36.58 C ANISOU 109 CD GLU A 13 4884 4900 4115 -380 -132 -378 C ATOM 110 OE1 GLU A 13 6.788 94.052 60.674 1.00 35.94 O ANISOU 110 OE1 GLU A 13 4766 4778 4111 -375 -94 -368 O ATOM 111 OE2 GLU A 13 6.709 92.223 61.889 1.00 34.00 O ANISOU 111 OE2 GLU A 13 4537 4623 3760 -338 -114 -342 O ATOM 112 N LEU A 14 10.728 91.894 65.536 1.00 31.99 N ANISOU 112 N LEU A 14 4368 4489 3296 -534 -570 -354 N ATOM 113 CA LEU A 14 11.933 91.101 65.764 1.00 32.31 C ANISOU 113 CA LEU A 14 4322 4593 3361 -543 -697 -296 C ATOM 114 C LEU A 14 11.595 89.817 66.523 1.00 37.10 C ANISOU 114 C LEU A 14 4986 5234 3876 -486 -711 -246 C ATOM 115 O LEU A 14 12.134 88.746 66.212 1.00 37.34 O ANISOU 115 O LEU A 14 4921 5302 3965 -438 -750 -175 O ATOM 116 CB LEU A 14 12.991 91.923 66.517 1.00 31.64 C ANISOU 116 CB LEU A 14 4255 4514 3251 -640 -844 -332 C ATOM 117 CG LEU A 14 13.587 93.122 65.743 1.00 40.11 C ANISOU 117 CG LEU A 14 5253 5553 4435 -716 -851 -365 C ATOM 118 CD1 LEU A 14 14.579 93.928 66.582 1.00 46.17 C ANISOU 118 CD1 LEU A 14 6048 6319 5174 -829 -1008 -406 C ATOM 119 CD2 LEU A 14 14.225 92.672 64.455 1.00 40.57 C ANISOU 119 CD2 LEU A 14 5122 5649 4644 -690 -818 -299 C ATOM 120 N ALA A 15 10.689 89.908 67.507 1.00 28.61 N ANISOU 120 N ALA A 15 4069 4141 2659 -488 -671 -281 N ATOM 121 CA ALA A 15 10.254 88.726 68.255 1.00 36.21 C ANISOU 121 CA ALA A 15 5107 5129 3523 -446 -668 -227 C ATOM 122 C ALA A 15 9.620 87.694 67.329 1.00 34.61 C ANISOU 122 C ALA A 15 4825 4922 3402 -371 -564 -168 C ATOM 123 O ALA A 15 9.854 86.481 67.477 1.00 33.23 O ANISOU 123 O ALA A 15 4634 4767 3226 -331 -605 -93 O ATOM 124 CB ALA A 15 9.257 89.131 69.357 1.00 32.30 C ANISOU 124 CB ALA A 15 4796 4616 2861 -467 -602 -283 C ATOM 125 N ILE A 16 8.768 88.158 66.412 1.00 30.82 N ANISOU 125 N ILE A 16 4310 4409 2990 -352 -437 -202 N ATOM 126 CA ILE A 16 8.128 87.284 65.426 1.00 33.54 C ANISOU 126 CA ILE A 16 4582 4747 3414 -293 -346 -158 C ATOM 127 C ILE A 16 9.180 86.650 64.513 1.00 35.71 C ANISOU 127 C ILE A 16 4722 5041 3806 -265 -406 -109 C ATOM 128 O ILE A 16 9.128 85.453 64.219 1.00 35.18 O ANISOU 128 O ILE A 16 4623 4974 3768 -215 -396 -54 O ATOM 129 CB ILE A 16 7.062 88.079 64.624 1.00 34.11 C ANISOU 129 CB ILE A 16 4641 4783 3535 -284 -222 -207 C ATOM 130 CG1 ILE A 16 5.889 88.504 65.526 1.00 35.87 C ANISOU 130 CG1 ILE A 16 4983 4989 3655 -290 -137 -253 C ATOM 131 CG2 ILE A 16 6.523 87.274 63.398 1.00 33.39 C ANISOU 131 CG2 ILE A 16 4463 4687 3538 -235 -150 -166 C ATOM 132 CD1 ILE A 16 4.887 89.423 64.780 1.00 37.91 C ANISOU 132 CD1 ILE A 16 5219 5208 3979 -270 -30 -301 C ATOM 133 N ALA A 17 10.156 87.440 64.062 1.00 33.08 N ANISOU 133 N ALA A 17 4307 4719 3543 -299 -461 -131 N ATOM 134 CA ALA A 17 11.184 86.925 63.160 1.00 33.60 C ANISOU 134 CA ALA A 17 4231 4810 3725 -270 -496 -91 C ATOM 135 C ALA A 17 11.969 85.771 63.794 1.00 34.13 C ANISOU 135 C ALA A 17 4276 4905 3786 -231 -599 -30 C ATOM 136 O ALA A 17 12.232 84.754 63.134 1.00 35.95 O ANISOU 136 O ALA A 17 4431 5137 4091 -165 -583 13 O ATOM 137 CB ALA A 17 12.134 88.064 62.761 1.00 29.67 C ANISOU 137 CB ALA A 17 3653 4325 3297 -333 -540 -121 C ATOM 138 N VAL A 18 12.344 85.914 65.069 1.00 34.46 N ANISOU 138 N VAL A 18 4393 4965 3736 -268 -711 -25 N ATOM 139 CA VAL A 18 13.104 84.871 65.780 1.00 37.64 C ANISOU 139 CA VAL A 18 4786 5391 4125 -230 -834 44 C ATOM 140 C VAL A 18 12.303 83.573 65.867 1.00 38.53 C ANISOU 140 C VAL A 18 4968 5471 4202 -163 -776 98 C ATOM 141 O VAL A 18 12.836 82.471 65.648 1.00 37.56 O ANISOU 141 O VAL A 18 4784 5342 4146 -94 -819 159 O ATOM 142 CB VAL A 18 13.511 85.364 67.183 1.00 40.99 C ANISOU 142 CB VAL A 18 5310 5838 4426 -294 -970 36 C ATOM 143 CG1 VAL A 18 14.077 84.220 68.022 1.00 40.36 C ANISOU 143 CG1 VAL A 18 5254 5776 4306 -250 -1102 121 C ATOM 144 CG2 VAL A 18 14.553 86.466 67.079 1.00 43.78 C ANISOU 144 CG2 VAL A 18 5572 6222 4842 -365 -1061 -6 C ATOM 145 N LEU A 19 11.014 83.678 66.180 1.00 33.11 N ANISOU 145 N LEU A 19 4404 4757 3419 -183 -675 76 N ATOM 146 CA LEU A 19 10.199 82.474 66.327 1.00 35.02 C ANISOU 146 CA LEU A 19 4716 4966 3626 -142 -618 130 C ATOM 147 C LEU A 19 9.892 81.818 64.985 1.00 33.83 C ANISOU 147 C LEU A 19 4474 4783 3598 -87 -527 137 C ATOM 148 O LEU A 19 9.781 80.585 64.916 1.00 34.53 O ANISOU 148 O LEU A 19 4577 4836 3706 -38 -528 194 O ATOM 149 CB LEU A 19 8.908 82.805 67.080 1.00 33.09 C ANISOU 149 CB LEU A 19 4613 4712 3249 -187 -526 105 C ATOM 150 CG LEU A 19 9.141 83.305 68.516 1.00 36.17 C ANISOU 150 CG LEU A 19 5131 5129 3483 -240 -609 96 C ATOM 151 CD1 LEU A 19 7.842 83.969 69.021 1.00 35.76 C ANISOU 151 CD1 LEU A 19 5195 5071 3321 -280 -477 39 C ATOM 152 CD2 LEU A 19 9.626 82.183 69.476 1.00 39.27 C ANISOU 152 CD2 LEU A 19 5601 5523 3795 -223 -724 192 C ATOM 153 N ALA A 20 9.715 82.620 63.927 1.00 33.13 N ANISOU 153 N ALA A 20 4307 4698 3581 -98 -452 79 N ATOM 154 CA ALA A 20 9.463 82.080 62.596 1.00 34.46 C ANISOU 154 CA ALA A 20 4402 4842 3849 -54 -372 78 C ATOM 155 C ALA A 20 10.661 81.287 62.115 1.00 35.89 C ANISOU 155 C ALA A 20 4484 5026 4126 9 -434 111 C ATOM 156 O ALA A 20 10.508 80.209 61.538 1.00 35.53 O ANISOU 156 O ALA A 20 4429 4941 4129 66 -401 135 O ATOM 157 CB ALA A 20 9.165 83.211 61.597 1.00 31.85 C ANISOU 157 CB ALA A 20 4018 4521 3564 -84 -297 17 C ATOM 158 N ILE A 21 11.864 81.826 62.327 1.00 31.10 N ANISOU 158 N ILE A 21 3797 4463 3555 1 -523 110 N ATOM 159 CA ILE A 21 13.079 81.129 61.933 1.00 34.46 C ANISOU 159 CA ILE A 21 4105 4902 4087 70 -581 142 C ATOM 160 C ILE A 21 13.231 79.833 62.729 1.00 37.35 C ANISOU 160 C ILE A 21 4527 5232 4433 132 -660 212 C ATOM 161 O ILE A 21 13.380 78.750 62.151 1.00 37.49 O ANISOU 161 O ILE A 21 4514 5206 4524 213 -636 236 O ATOM 162 CB ILE A 21 14.297 82.054 62.098 1.00 34.29 C ANISOU 162 CB ILE A 21 3973 4943 4114 32 -666 129 C ATOM 163 CG1 ILE A 21 14.249 83.200 61.062 1.00 32.96 C ANISOU 163 CG1 ILE A 21 3740 4794 3989 -23 -574 71 C ATOM 164 CG2 ILE A 21 15.584 81.272 61.927 1.00 39.07 C ANISOU 164 CG2 ILE A 21 4443 5569 4834 111 -740 172 C ATOM 165 CD1 ILE A 21 15.322 84.297 61.401 1.00 37.73 C ANISOU 165 CD1 ILE A 21 4257 5451 4627 -95 -664 58 C ATOM 166 N LEU A 22 13.102 79.915 64.064 1.00 34.00 N ANISOU 166 N LEU A 22 4206 4814 3896 94 -750 246 N ATOM 167 CA LEU A 22 13.387 78.757 64.922 1.00 34.00 C ANISOU 167 CA LEU A 22 4267 4782 3869 147 -851 330 C ATOM 168 C LEU A 22 12.423 77.607 64.650 1.00 37.09 C ANISOU 168 C LEU A 22 4747 5094 4253 186 -765 361 C ATOM 169 O LEU A 22 12.846 76.455 64.504 1.00 36.63 O ANISOU 169 O LEU A 22 4672 4981 4263 269 -803 413 O ATOM 170 CB LEU A 22 13.329 79.146 66.406 1.00 36.78 C ANISOU 170 CB LEU A 22 4743 5161 4071 83 -955 358 C ATOM 171 CG LEU A 22 14.524 79.948 66.915 1.00 44.72 C ANISOU 171 CG LEU A 22 5670 6234 5087 52 -1100 351 C ATOM 172 CD1 LEU A 22 14.329 80.381 68.385 1.00 47.08 C ANISOU 172 CD1 LEU A 22 6127 6556 5205 -23 -1198 364 C ATOM 173 CD2 LEU A 22 15.795 79.119 66.775 1.00 52.93 C ANISOU 173 CD2 LEU A 22 6577 7278 6255 145 -1220 414 C ATOM 174 N GLY A 23 11.118 77.895 64.588 1.00 33.33 N ANISOU 174 N GLY A 23 4361 4602 3701 125 -652 329 N ATOM 175 CA GLY A 23 10.155 76.820 64.425 1.00 34.78 C ANISOU 175 CA GLY A 23 4628 4711 3875 139 -580 363 C ATOM 176 C GLY A 23 10.219 76.170 63.049 1.00 35.19 C ANISOU 176 C GLY A 23 4600 4715 4055 201 -514 336 C ATOM 177 O GLY A 23 10.030 74.956 62.919 1.00 36.39 O ANISOU 177 O GLY A 23 4800 4788 4240 246 -511 378 O ATOM 178 N ASN A 24 10.501 76.957 62.014 1.00 31.01 N ANISOU 178 N ASN A 24 3962 4229 3593 202 -462 266 N ATOM 179 CA ASN A 24 10.503 76.426 60.658 1.00 34.46 C ANISOU 179 CA ASN A 24 4341 4627 4126 253 -387 230 C ATOM 180 C ASN A 24 11.821 75.731 60.306 1.00 34.94 C ANISOU 180 C ASN A 24 4308 4673 4294 356 -441 245 C ATOM 181 O ASN A 24 11.813 74.796 59.498 1.00 36.05 O ANISOU 181 O ASN A 24 4448 4748 4502 420 -395 233 O ATOM 182 CB ASN A 24 10.135 77.552 59.683 1.00 29.63 C ANISOU 182 CB ASN A 24 3672 4064 3522 204 -300 156 C ATOM 183 CG ASN A 24 8.650 77.863 59.749 1.00 34.46 C ANISOU 183 CG ASN A 24 4369 4664 4062 132 -229 141 C ATOM 184 OD1 ASN A 24 7.841 77.038 59.325 1.00 32.30 O ANISOU 184 OD1 ASN A 24 4144 4332 3796 134 -182 144 O ATOM 185 ND2 ASN A 24 8.272 79.004 60.372 1.00 31.39 N ANISOU 185 ND2 ASN A 24 4000 4322 3605 69 -226 124 N ATOM 186 N VAL A 25 12.949 76.168 60.884 1.00 31.41 N ANISOU 186 N VAL A 25 3780 4284 3872 374 -538 268 N ATOM 187 CA VAL A 25 14.173 75.363 60.850 1.00 35.58 C ANISOU 187 CA VAL A 25 4218 4795 4508 484 -611 304 C ATOM 188 C VAL A 25 13.921 73.991 61.461 1.00 40.12 C ANISOU 188 C VAL A 25 4902 5268 5072 544 -665 375 C ATOM 189 O VAL A 25 14.423 72.972 60.975 1.00 38.88 O ANISOU 189 O VAL A 25 4714 5044 5016 650 -664 385 O ATOM 190 CB VAL A 25 15.320 76.102 61.571 1.00 35.85 C ANISOU 190 CB VAL A 25 4148 4914 4561 474 -733 327 C ATOM 191 CG1 VAL A 25 16.449 75.140 61.952 1.00 36.09 C ANISOU 191 CG1 VAL A 25 4105 4919 4689 591 -849 392 C ATOM 192 CG2 VAL A 25 15.830 77.247 60.678 1.00 36.75 C ANISOU 192 CG2 VAL A 25 4122 5108 4733 434 -668 259 C ATOM 193 N LEU A 26 13.136 73.936 62.534 1.00 38.70 N ANISOU 193 N LEU A 26 4863 5071 4771 477 -706 427 N ATOM 194 CA LEU A 26 12.845 72.650 63.163 1.00 37.17 C ANISOU 194 CA LEU A 26 4791 4775 4557 517 -755 509 C ATOM 195 C LEU A 26 12.044 71.737 62.225 1.00 36.49 C ANISOU 195 C LEU A 26 4761 4586 4516 537 -646 481 C ATOM 196 O LEU A 26 12.299 70.530 62.157 1.00 38.59 O ANISOU 196 O LEU A 26 5066 4747 4848 621 -676 523 O ATOM 197 CB LEU A 26 12.097 72.904 64.468 1.00 40.16 C ANISOU 197 CB LEU A 26 5313 5169 4777 422 -795 566 C ATOM 198 CG LEU A 26 11.814 71.751 65.410 1.00 49.54 C ANISOU 198 CG LEU A 26 6650 6266 5908 436 -861 674 C ATOM 199 CD1 LEU A 26 13.106 71.062 65.820 1.00 49.75 C ANISOU 199 CD1 LEU A 26 6632 6262 6011 550 -1015 749 C ATOM 200 CD2 LEU A 26 11.063 72.281 66.640 1.00 49.21 C ANISOU 200 CD2 LEU A 26 6741 6270 5686 325 -871 712 C ATOM 201 N VAL A 27 11.070 72.296 61.500 1.00 33.05 N ANISOU 201 N VAL A 27 4335 4174 4048 460 -528 410 N ATOM 202 CA VAL A 27 10.328 71.529 60.495 1.00 36.90 C ANISOU 202 CA VAL A 27 4867 4575 4579 466 -435 371 C ATOM 203 C VAL A 27 11.279 70.924 59.457 1.00 38.08 C ANISOU 203 C VAL A 27 4933 4682 4855 584 -420 327 C ATOM 204 O VAL A 27 11.193 69.736 59.132 1.00 41.61 O ANISOU 204 O VAL A 27 5444 5010 5355 643 -412 335 O ATOM 205 CB VAL A 27 9.265 72.418 59.820 1.00 38.83 C ANISOU 205 CB VAL A 27 5105 4872 4775 369 -330 300 C ATOM 206 CG1 VAL A 27 8.617 71.689 58.623 1.00 34.26 C ANISOU 206 CG1 VAL A 27 4558 4214 4244 373 -250 248 C ATOM 207 CG2 VAL A 27 8.184 72.825 60.840 1.00 37.98 C ANISOU 207 CG2 VAL A 27 5087 4789 4554 264 -322 340 C ATOM 208 N CYS A 28 12.175 71.748 58.897 1.00 36.08 N ANISOU 208 N CYS A 28 4538 4519 4651 617 -405 277 N ATOM 209 CA CYS A 28 13.089 71.274 57.868 1.00 38.36 C ANISOU 209 CA CYS A 28 4735 4784 5057 729 -364 227 C ATOM 210 C CYS A 28 14.011 70.192 58.405 1.00 46.12 C ANISOU 210 C CYS A 28 5707 5690 6128 856 -455 289 C ATOM 211 O CYS A 28 14.260 69.176 57.731 1.00 46.98 O ANISOU 211 O CYS A 28 5830 5700 6321 956 -417 261 O ATOM 212 CB CYS A 28 13.911 72.446 57.335 1.00 35.51 C ANISOU 212 CB CYS A 28 4216 4548 4728 723 -332 178 C ATOM 213 SG CYS A 28 12.910 73.622 56.465 1.00 39.94 S ANISOU 213 SG CYS A 28 4794 5175 5206 599 -221 106 S ATOM 214 N ATRP A 29 14.553 70.419 59.609 0.50 41.65 N ANISOU 214 N ATRP A 29 5117 5165 5543 859 -582 371 N ATOM 215 N BTRP A 29 14.526 70.374 59.625 0.50 41.49 N ANISOU 215 N BTRP A 29 5102 5139 5522 859 -583 373 N ATOM 216 CA ATRP A 29 15.414 69.450 60.280 0.50 42.40 C ANISOU 216 CA ATRP A 29 5204 5190 5716 978 -699 451 C ATOM 217 CA BTRP A 29 15.449 69.389 60.178 0.50 42.38 C ANISOU 217 CA BTRP A 29 5197 5182 5724 988 -692 445 C ATOM 218 C ATRP A 29 14.716 68.098 60.412 0.50 42.79 C ANISOU 218 C ATRP A 29 5421 5075 5761 1009 -700 493 C ATOM 219 C BTRP A 29 14.742 68.065 60.485 0.50 42.90 C ANISOU 219 C BTRP A 29 5438 5086 5775 1012 -709 499 C ATOM 220 O ATRP A 29 15.290 67.049 60.084 0.50 43.69 O ANISOU 220 O ATRP A 29 5529 5082 5988 1142 -713 499 O ATOM 221 O BTRP A 29 15.348 66.991 60.340 0.50 43.08 O ANISOU 221 O BTRP A 29 5461 5002 5907 1145 -742 522 O ATOM 222 CB ATRP A 29 15.797 70.013 61.653 0.50 45.75 C ANISOU 222 CB ATRP A 29 5620 5689 6072 935 -847 537 C ATOM 223 CB BTRP A 29 16.128 69.972 61.419 0.50 46.10 C ANISOU 223 CB BTRP A 29 5616 5738 6161 970 -843 525 C ATOM 224 CG ATRP A 29 16.997 69.408 62.325 0.50 55.57 C ANISOU 224 CG ATRP A 29 6793 6911 7408 1058 -999 619 C ATOM 225 CG BTRP A 29 17.300 69.183 61.929 0.50 56.18 C ANISOU 225 CG BTRP A 29 6823 6974 7550 1112 -977 601 C ATOM 226 CD1ATRP A 29 17.586 68.203 62.046 0.50 60.43 C ANISOU 226 CD1ATRP A 29 7391 7415 8155 1212 -1023 646 C ATOM 227 CD1BTRP A 29 17.381 68.515 63.123 0.50 59.32 C ANISOU 227 CD1BTRP A 29 7322 7308 7908 1138 -1126 718 C ATOM 228 CD2ATRP A 29 17.757 69.984 63.405 0.50 57.36 C ANISOU 228 CD2ATRP A 29 6959 7229 7608 1042 -1159 687 C ATOM 229 CD2BTRP A 29 18.566 68.981 61.275 0.50 60.75 C ANISOU 229 CD2BTRP A 29 7210 7571 8300 1251 -976 571 C ATOM 230 NE1ATRP A 29 18.664 68.000 62.881 0.50 62.24 N ANISOU 230 NE1ATRP A 29 7538 7662 8448 1299 -1191 734 N ATOM 231 NE1BTRP A 29 18.611 67.912 63.247 0.50 62.47 N ANISOU 231 NE1BTRP A 29 7603 7682 8451 1292 -1233 766 N ATOM 232 CE2ATRP A 29 18.791 69.078 63.720 0.50 59.08 C ANISOU 232 CE2ATRP A 29 7109 7390 7948 1192 -1283 761 C ATOM 233 CE2BTRP A 29 19.354 68.179 62.126 0.50 62.73 C ANISOU 233 CE2BTRP A 29 7446 7766 8623 1366 -1138 674 C ATOM 234 CE3ATRP A 29 17.663 71.183 64.129 0.50 54.90 C ANISOU 234 CE3ATRP A 29 6646 7034 7179 916 -1215 689 C ATOM 235 CE3BTRP A 29 19.104 69.394 60.053 0.50 60.86 C ANISOU 235 CE3BTRP A 29 7065 7646 8414 1291 -850 472 C ATOM 236 CZ2ATRP A 29 19.719 69.325 64.726 0.50 54.17 C ANISOU 236 CZ2ATRP A 29 6413 6834 7335 1213 -1473 843 C ATOM 237 CZ2BTRP A 29 20.651 67.787 61.793 0.50 67.56 C ANISOU 237 CZ2BTRP A 29 7869 8381 9418 1528 -1177 677 C ATOM 238 CZ3ATRP A 29 18.589 71.427 65.124 0.50 54.36 C ANISOU 238 CZ3ATRP A 29 6519 7027 7110 930 -1398 760 C ATOM 239 CZ3BTRP A 29 20.387 69.001 59.728 0.50 60.68 C ANISOU 239 CZ3BTRP A 29 6862 7631 8562 1443 -871 471 C ATOM 240 CH2ATRP A 29 19.602 70.498 65.416 0.50 54.69 C ANISOU 240 CH2ATRP A 29 6487 7018 7273 1075 -1531 840 C ATOM 241 CH2BTRP A 29 21.146 68.209 60.592 0.50 64.91 C ANISOU 241 CH2BTRP A 29 7368 8112 9184 1564 -1034 571 C ATOM 242 N ALA A 30 13.465 68.114 60.890 1.00 36.03 N ANISOU 242 N ALA A 30 4716 4193 4783 886 -681 521 N ATOM 243 CA ALA A 30 12.708 66.877 61.095 1.00 42.00 C ANISOU 243 CA ALA A 30 5639 4792 5528 884 -681 571 C ATOM 244 C ALA A 30 12.570 66.082 59.796 1.00 40.27 C ANISOU 244 C ALA A 30 5433 4465 5402 946 -583 485 C ATOM 245 O ALA A 30 12.768 64.864 59.789 1.00 44.24 O ANISOU 245 O ALA A 30 6013 4818 5979 1036 -615 518 O ATOM 246 CB ALA A 30 11.317 67.200 61.656 1.00 38.14 C ANISOU 246 CB ALA A 30 5275 4319 4897 723 -643 598 C ATOM 247 N VAL A 31 12.248 66.763 58.685 1.00 38.20 N ANISOU 247 N VAL A 31 5109 4272 5134 901 -469 374 N ATOM 248 CA VAL A 31 12.057 66.063 57.418 1.00 39.01 C ANISOU 248 CA VAL A 31 5244 4279 5298 946 -375 282 C ATOM 249 C VAL A 31 13.385 65.500 56.919 1.00 42.04 C ANISOU 249 C VAL A 31 5535 4620 5818 1124 -378 250 C ATOM 250 O VAL A 31 13.452 64.380 56.397 1.00 42.86 O ANISOU 250 O VAL A 31 5714 4576 5994 1211 -352 218 O ATOM 251 CB VAL A 31 11.392 66.993 56.386 1.00 38.74 C ANISOU 251 CB VAL A 31 5174 4339 5206 850 -266 182 C ATOM 252 CG1 VAL A 31 11.373 66.322 54.979 1.00 41.45 C ANISOU 252 CG1 VAL A 31 5550 4598 5602 905 -173 73 C ATOM 253 CG2 VAL A 31 9.966 67.340 56.828 1.00 35.25 C ANISOU 253 CG2 VAL A 31 4825 3913 4655 690 -258 211 C ATOM 254 N TRP A 32 14.464 66.252 57.097 1.00 42.11 N ANISOU 254 N TRP A 32 5378 4751 5870 1182 -408 258 N ATOM 255 CA TRP A 32 15.788 65.744 56.768 1.00 43.40 C ANISOU 255 CA TRP A 32 5423 4889 6179 1359 -415 242 C ATOM 256 C TRP A 32 16.114 64.474 57.545 1.00 49.02 C ANISOU 256 C TRP A 32 6216 5445 6966 1472 -526 333 C ATOM 257 O TRP A 32 16.679 63.519 56.991 1.00 49.32 O ANISOU 257 O TRP A 32 6250 5366 7123 1621 -496 296 O ATOM 258 CB TRP A 32 16.835 66.824 57.057 1.00 43.07 C ANISOU 258 CB TRP A 32 5178 5014 6171 1374 -455 258 C ATOM 259 CG TRP A 32 18.261 66.338 56.892 1.00 55.38 C ANISOU 259 CG TRP A 32 6581 6563 7898 1558 -478 260 C ATOM 260 CD1 TRP A 32 19.032 65.708 57.825 1.00 56.75 C ANISOU 260 CD1 TRP A 32 6717 6686 8159 1671 -622 358 C ATOM 261 CD2 TRP A 32 19.073 66.461 55.720 1.00 58.17 C ANISOU 261 CD2 TRP A 32 6787 6964 8352 1651 -350 160 C ATOM 262 NE1 TRP A 32 20.274 65.432 57.305 1.00 59.85 N ANISOU 262 NE1 TRP A 32 6931 7090 8718 1837 -594 325 N ATOM 263 CE2 TRP A 32 20.325 65.892 56.017 1.00 61.45 C ANISOU 263 CE2 TRP A 32 7063 7357 8930 1825 -416 201 C ATOM 264 CE3 TRP A 32 18.866 67.021 54.456 1.00 66.49 C ANISOU 264 CE3 TRP A 32 7813 8080 9369 1603 -184 46 C ATOM 265 CZ2 TRP A 32 21.357 65.836 55.088 1.00 69.45 C ANISOU 265 CZ2 TRP A 32 7901 8410 10077 1956 -305 124 C ATOM 266 CZ3 TRP A 32 19.899 66.970 53.535 1.00 74.31 C ANISOU 266 CZ3 TRP A 32 8649 9111 10475 1723 -73 -27 C ATOM 267 CH2 TRP A 32 21.126 66.383 53.857 1.00 71.78 C ANISOU 267 CH2 TRP A 32 8182 8770 10323 1898 -125 8 C ATOM 268 N LEU A 33 15.793 64.454 58.838 1.00 50.16 N ANISOU 268 N LEU A 33 6439 5581 7038 1409 -652 454 N ATOM 269 CA LEU A 33 16.264 63.392 59.727 1.00 50.55 C ANISOU 269 CA LEU A 33 6553 5502 7153 1519 -786 567 C ATOM 270 C LEU A 33 15.492 62.091 59.554 1.00 47.86 C ANISOU 270 C LEU A 33 6413 4950 6823 1529 -762 577 C ATOM 271 O LEU A 33 16.070 61.012 59.674 1.00 53.84 O ANISOU 271 O LEU A 33 7205 5558 7692 1676 -821 619 O ATOM 272 CB LEU A 33 16.135 63.844 61.179 1.00 61.15 C ANISOU 272 CB LEU A 33 7936 6912 8386 1432 -927 696 C ATOM 273 CG LEU A 33 17.338 63.788 62.107 1.00 77.62 C ANISOU 273 CG LEU A 33 9923 9031 10538 1542 -1097 798 C ATOM 274 CD1 LEU A 33 18.379 64.802 61.657 1.00 81.28 C ANISOU 274 CD1 LEU A 33 10142 9662 11077 1583 -1083 731 C ATOM 275 CD2 LEU A 33 16.881 64.045 63.537 1.00 77.85 C ANISOU 275 CD2 LEU A 33 10074 9093 10412 1428 -1226 923 C ATOM 276 N ASN A 34 14.197 62.169 59.285 1.00 50.55 N ANISOU 276 N ASN A 34 6882 5268 7056 1375 -683 542 N ATOM 277 CA ASN A 34 13.281 61.046 59.466 1.00 51.68 C ANISOU 277 CA ASN A 34 7232 5223 7180 1328 -689 586 C ATOM 278 C ASN A 34 12.698 60.634 58.117 1.00 46.84 C ANISOU 278 C ASN A 34 6676 4526 6597 1311 -559 450 C ATOM 279 O ASN A 34 11.864 61.350 57.550 1.00 44.90 O ANISOU 279 O ASN A 34 6423 4372 6266 1178 -473 376 O ATOM 280 CB ASN A 34 12.188 61.437 60.457 1.00 49.25 C ANISOU 280 CB ASN A 34 7029 4963 6720 1144 -720 676 C ATOM 281 CG ASN A 34 11.179 60.341 60.698 1.00 51.96 C ANISOU 281 CG ASN A 34 7578 5124 7041 1067 -719 733 C ATOM 282 OD1 ASN A 34 11.186 59.288 60.044 1.00 53.71 O ANISOU 282 OD1 ASN A 34 7882 5170 7357 1137 -696 693 O ATOM 283 ND2 ASN A 34 10.286 60.589 61.638 1.00 48.36 N ANISOU 283 ND2 ASN A 34 7211 4706 6459 916 -738 825 N ATOM 284 N SER A 35 13.101 59.447 57.644 1.00 49.70 N ANISOU 284 N SER A 35 7108 4702 7076 1445 -555 420 N ATOM 285 CA SER A 35 12.624 58.916 56.365 1.00 53.88 C ANISOU 285 CA SER A 35 7717 5125 7630 1439 -443 283 C ATOM 286 C SER A 35 11.110 58.755 56.323 1.00 46.89 C ANISOU 286 C SER A 35 6986 4186 6643 1239 -418 284 C ATOM 287 O SER A 35 10.510 58.854 55.247 1.00 53.86 O ANISOU 287 O SER A 35 7897 5071 7497 1171 -326 163 O ATOM 288 CB SER A 35 13.275 57.560 56.086 1.00 65.23 C ANISOU 288 CB SER A 35 9235 6340 9209 1618 -460 265 C ATOM 289 OG SER A 35 14.676 57.660 56.144 1.00 73.69 O ANISOU 289 OG SER A 35 10144 7460 10395 1814 -484 269 O ATOM 290 N ASN A 36 10.474 58.471 57.457 1.00 45.60 N ANISOU 290 N ASN A 36 6926 3974 6426 1140 -497 420 N ATOM 291 CA ASN A 36 9.013 58.427 57.490 1.00 48.81 C ANISOU 291 CA ASN A 36 7446 4356 6741 937 -465 430 C ATOM 292 C ASN A 36 8.375 59.748 57.092 1.00 49.63 C ANISOU 292 C ASN A 36 7441 4669 6746 808 -393 364 C ATOM 293 O ASN A 36 7.190 59.771 56.756 1.00 51.73 O ANISOU 293 O ASN A 36 7768 4928 6959 656 -349 334 O ATOM 294 CB ASN A 36 8.506 58.062 58.879 1.00 52.78 C ANISOU 294 CB ASN A 36 8057 4807 7189 848 -547 598 C ATOM 295 CG ASN A 36 8.789 56.635 59.239 1.00 68.65 C ANISOU 295 CG ASN A 36 10224 6573 9288 932 -619 676 C ATOM 296 OD1 ASN A 36 8.816 55.761 58.369 1.00 70.90 O ANISOU 296 OD1 ASN A 36 10587 6688 9662 990 -589 590 O ATOM 297 ND2 ASN A 36 9.013 56.380 60.532 1.00 72.68 N ANISOU 297 ND2 ASN A 36 10792 7053 9769 942 -718 839 N ATOM 298 N LEU A 37 9.112 60.851 57.148 1.00 46.30 N ANISOU 298 N LEU A 37 6858 4429 6304 862 -387 348 N ATOM 299 CA LEU A 37 8.556 62.141 56.788 1.00 45.19 C ANISOU 299 CA LEU A 37 6620 4474 6075 750 -324 292 C ATOM 300 C LEU A 37 8.954 62.565 55.391 1.00 43.60 C ANISOU 300 C LEU A 37 6334 4331 5903 806 -239 149 C ATOM 301 O LEU A 37 8.545 63.635 54.953 1.00 43.53 O ANISOU 301 O LEU A 37 6247 4464 5827 723 -188 100 O ATOM 302 CB LEU A 37 8.990 63.214 57.799 1.00 43.39 C ANISOU 302 CB LEU A 37 6285 4412 5789 741 -371 369 C ATOM 303 CG LEU A 37 8.402 63.123 59.214 1.00 47.31 C ANISOU 303 CG LEU A 37 6869 4901 6206 648 -436 505 C ATOM 304 CD1 LEU A 37 9.047 64.154 60.167 1.00 43.36 C ANISOU 304 CD1 LEU A 37 6271 4556 5645 661 -494 564 C ATOM 305 CD2 LEU A 37 6.879 63.303 59.164 1.00 48.03 C ANISOU 305 CD2 LEU A 37 7025 5005 6218 469 -371 499 C ATOM 306 N GLN A 38 9.754 61.767 54.692 1.00 45.03 N ANISOU 306 N GLN A 38 6530 4401 6177 948 -219 84 N ATOM 307 CA GLN A 38 10.220 62.113 53.345 1.00 50.63 C ANISOU 307 CA GLN A 38 7170 5165 6903 1009 -123 -55 C ATOM 308 C GLN A 38 9.243 61.521 52.334 1.00 56.62 C ANISOU 308 C GLN A 38 8066 5817 7631 927 -72 -151 C ATOM 309 O GLN A 38 9.425 60.421 51.828 1.00 59.44 O ANISOU 309 O GLN A 38 8530 6005 8051 1004 -58 -208 O ATOM 310 CB GLN A 38 11.645 61.611 53.120 1.00 47.45 C ANISOU 310 CB GLN A 38 6698 4712 6618 1215 -111 -83 C ATOM 311 CG GLN A 38 12.700 62.416 53.906 1.00 51.48 C ANISOU 311 CG GLN A 38 7032 5367 7162 1287 -161 -7 C ATOM 312 CD GLN A 38 14.008 61.678 54.076 1.00 54.52 C ANISOU 312 CD GLN A 38 7354 5673 7688 1492 -193 10 C ATOM 313 OE1 GLN A 38 14.315 60.738 53.331 1.00 59.11 O ANISOU 313 OE1 GLN A 38 7995 6115 8349 1607 -138 -69 O ATOM 314 NE2 GLN A 38 14.782 62.076 55.079 1.00 48.58 N ANISOU 314 NE2 GLN A 38 6485 5003 6972 1543 -288 112 N ATOM 315 N ASN A 39 8.187 62.264 52.045 1.00 54.63 N ANISOU 315 N ASN A 39 7813 5661 7285 769 -51 -170 N ATOM 316 CA ASN A 39 7.202 61.888 51.045 1.00 50.98 C ANISOU 316 CA ASN A 39 7460 5129 6782 670 -19 -261 C ATOM 317 C ASN A 39 6.829 63.169 50.319 1.00 48.38 C ANISOU 317 C ASN A 39 7038 4980 6365 590 30 -316 C ATOM 318 O ASN A 39 7.218 64.264 50.738 1.00 44.53 O ANISOU 318 O ASN A 39 6418 4647 5853 597 36 -272 O ATOM 319 CB ASN A 39 5.979 61.220 51.684 1.00 46.00 C ANISOU 319 CB ASN A 39 6947 4388 6141 529 -79 -190 C ATOM 320 CG ASN A 39 5.391 62.066 52.827 1.00 50.09 C ANISOU 320 CG ASN A 39 7391 5034 6607 423 -113 -71 C ATOM 321 OD1 ASN A 39 4.962 63.188 52.616 1.00 54.09 O ANISOU 321 OD1 ASN A 39 7805 5699 7050 349 -85 -88 O ATOM 322 ND2 ASN A 39 5.386 61.523 54.038 1.00 51.16 N ANISOU 322 ND2 ASN A 39 7576 5096 6765 420 -169 49 N ATOM 323 N VAL A 40 6.051 63.039 49.241 1.00 45.45 N ANISOU 323 N VAL A 40 6744 4581 5943 507 55 -410 N ATOM 324 CA VAL A 40 5.804 64.185 48.358 1.00 43.16 C ANISOU 324 CA VAL A 40 6383 4447 5569 451 100 -469 C ATOM 325 C VAL A 40 5.048 65.271 49.093 1.00 42.05 C ANISOU 325 C VAL A 40 6149 4441 5385 338 66 -380 C ATOM 326 O VAL A 40 5.305 66.475 48.911 1.00 40.84 O ANISOU 326 O VAL A 40 5887 4440 5190 339 96 -381 O ATOM 327 CB VAL A 40 5.039 63.740 47.090 1.00 47.25 C ANISOU 327 CB VAL A 40 7023 4898 6032 376 109 -580 C ATOM 328 CG1 VAL A 40 4.374 64.931 46.430 1.00 43.24 C ANISOU 328 CG1 VAL A 40 6454 4545 5431 275 116 -600 C ATOM 329 CG2 VAL A 40 5.967 63.066 46.130 1.00 48.90 C ANISOU 329 CG2 VAL A 40 7303 5023 6253 505 177 -696 C ATOM 330 N THR A 41 4.061 64.873 49.896 1.00 39.98 N ANISOU 330 N THR A 41 5934 4124 5134 235 11 -307 N ATOM 331 CA THR A 41 3.282 65.873 50.621 1.00 39.93 C ANISOU 331 CA THR A 41 5841 4241 5089 134 -6 -231 C ATOM 332 C THR A 41 4.195 66.794 51.428 1.00 42.35 C ANISOU 332 C THR A 41 6034 4664 5393 209 5 -173 C ATOM 333 O THR A 41 4.031 68.019 51.416 1.00 39.74 O ANISOU 333 O THR A 41 5611 4471 5018 174 22 -168 O ATOM 334 CB THR A 41 2.284 65.170 51.542 1.00 40.67 C ANISOU 334 CB THR A 41 5999 4250 5204 29 -48 -149 C ATOM 335 OG1 THR A 41 1.663 64.093 50.830 1.00 39.94 O ANISOU 335 OG1 THR A 41 6026 4016 5135 -30 -69 -204 O ATOM 336 CG2 THR A 41 1.258 66.126 52.015 1.00 38.60 C ANISOU 336 CG2 THR A 41 5655 4108 4902 -85 -46 -98 C ATOM 337 N ASN A 42 5.186 66.218 52.111 1.00 40.01 N ANISOU 337 N ASN A 42 5746 4308 5149 315 -14 -131 N ATOM 338 CA ASN A 42 6.060 67.009 52.957 1.00 35.20 C ANISOU 338 CA ASN A 42 5032 3802 4539 377 -26 -72 C ATOM 339 C ASN A 42 7.141 67.756 52.174 1.00 40.05 C ANISOU 339 C ASN A 42 5543 4511 5163 466 22 -137 C ATOM 340 O ASN A 42 7.809 68.617 52.755 1.00 37.58 O ANISOU 340 O ASN A 42 5128 4303 4848 494 10 -97 O ATOM 341 CB ASN A 42 6.671 66.108 54.038 1.00 35.28 C ANISOU 341 CB ASN A 42 5087 3715 4602 451 -85 13 C ATOM 342 CG ASN A 42 5.645 65.719 55.103 1.00 40.11 C ANISOU 342 CG ASN A 42 5782 4277 5182 343 -125 108 C ATOM 343 OD1 ASN A 42 4.661 66.417 55.298 1.00 39.02 O ANISOU 343 OD1 ASN A 42 5621 4218 4985 226 -106 121 O ATOM 344 ND2 ASN A 42 5.856 64.603 55.762 1.00 41.36 N ANISOU 344 ND2 ASN A 42 6034 4300 5382 382 -173 175 N ATOM 345 N TYR A 43 7.330 67.484 50.878 1.00 34.98 N ANISOU 345 N TYR A 43 4928 3840 4524 502 79 -236 N ATOM 346 CA TYR A 43 8.185 68.390 50.105 1.00 36.71 C ANISOU 346 CA TYR A 43 5044 4174 4731 555 142 -291 C ATOM 347 C TYR A 43 7.548 69.769 49.999 1.00 35.87 C ANISOU 347 C TYR A 43 4877 4202 4551 449 149 -278 C ATOM 348 O TYR A 43 8.243 70.793 50.039 1.00 34.24 O ANISOU 348 O TYR A 43 4563 4107 4340 468 172 -268 O ATOM 349 CB TYR A 43 8.468 67.826 48.710 1.00 40.71 C ANISOU 349 CB TYR A 43 5611 4625 5233 609 216 -403 C ATOM 350 CG TYR A 43 9.213 66.503 48.781 1.00 53.28 C ANISOU 350 CG TYR A 43 7257 6075 6912 737 219 -425 C ATOM 351 CD1 TYR A 43 9.867 66.132 49.951 1.00 61.25 C ANISOU 351 CD1 TYR A 43 8220 7049 8002 815 161 -339 C ATOM 352 CD2 TYR A 43 9.275 65.641 47.702 1.00 60.12 C ANISOU 352 CD2 TYR A 43 8227 6838 7778 786 276 -532 C ATOM 353 CE1 TYR A 43 10.542 64.932 50.060 1.00 65.32 C ANISOU 353 CE1 TYR A 43 8784 7424 8609 945 153 -349 C ATOM 354 CE2 TYR A 43 9.962 64.429 47.800 1.00 66.88 C ANISOU 354 CE2 TYR A 43 9137 7548 8725 918 281 -555 C ATOM 355 CZ TYR A 43 10.587 64.086 48.992 1.00 70.24 C ANISOU 355 CZ TYR A 43 9507 7937 9245 1000 217 -458 C ATOM 356 OH TYR A 43 11.276 62.901 49.139 1.00 79.21 O ANISOU 356 OH TYR A 43 10692 8920 10484 1142 211 -468 O ATOM 357 N PHE A 44 6.226 69.803 49.846 1.00 30.75 N ANISOU 357 N PHE A 44 4292 3537 3853 336 128 -279 N ATOM 358 CA PHE A 44 5.498 71.066 49.844 1.00 32.92 C ANISOU 358 CA PHE A 44 4512 3924 4072 244 126 -259 C ATOM 359 C PHE A 44 5.486 71.699 51.226 1.00 34.46 C ANISOU 359 C PHE A 44 4645 4176 4273 224 90 -174 C ATOM 360 O PHE A 44 5.555 72.923 51.324 1.00 35.58 O ANISOU 360 O PHE A 44 4712 4421 4387 199 100 -163 O ATOM 361 CB PHE A 44 4.076 70.850 49.319 1.00 31.56 C ANISOU 361 CB PHE A 44 4409 3717 3864 138 104 -280 C ATOM 362 CG PHE A 44 4.050 70.382 47.870 1.00 38.76 C ANISOU 362 CG PHE A 44 5396 4587 4744 143 130 -374 C ATOM 363 CD1 PHE A 44 4.437 71.241 46.838 1.00 39.91 C ANISOU 363 CD1 PHE A 44 5511 4819 4834 156 175 -422 C ATOM 364 CD2 PHE A 44 3.681 69.088 47.548 1.00 39.09 C ANISOU 364 CD2 PHE A 44 5552 4497 4803 133 110 -415 C ATOM 365 CE1 PHE A 44 4.453 70.802 45.505 1.00 46.00 C ANISOU 365 CE1 PHE A 44 6369 5554 5553 161 204 -512 C ATOM 366 CE2 PHE A 44 3.701 68.644 46.199 1.00 42.64 C ANISOU 366 CE2 PHE A 44 6090 4902 5207 139 133 -516 C ATOM 367 CZ PHE A 44 4.098 69.501 45.191 1.00 38.72 C ANISOU 367 CZ PHE A 44 5567 4503 4642 155 182 -564 C ATOM 368 N VAL A 45 5.424 70.887 52.294 1.00 33.72 N ANISOU 368 N VAL A 45 4595 4010 4208 232 48 -114 N ATOM 369 CA VAL A 45 5.556 71.419 53.651 1.00 35.58 C ANISOU 369 CA VAL A 45 4791 4298 4431 221 14 -35 C ATOM 370 C VAL A 45 6.907 72.113 53.828 1.00 31.46 C ANISOU 370 C VAL A 45 4173 3852 3927 299 9 -34 C ATOM 371 O VAL A 45 6.992 73.202 54.421 1.00 34.27 O ANISOU 371 O VAL A 45 4470 4299 4252 267 -3 -8 O ATOM 372 CB VAL A 45 5.348 70.289 54.679 1.00 33.48 C ANISOU 372 CB VAL A 45 4609 3930 4181 220 -31 35 C ATOM 373 CG1 VAL A 45 5.850 70.692 56.102 1.00 34.23 C ANISOU 373 CG1 VAL A 45 4680 4075 4253 235 -78 116 C ATOM 374 CG2 VAL A 45 3.883 69.857 54.717 1.00 33.44 C ANISOU 374 CG2 VAL A 45 4675 3876 4156 109 -23 49 C ATOM 375 N VAL A 46 7.985 71.492 53.324 1.00 31.40 N ANISOU 375 N VAL A 46 4146 3805 3978 402 19 -64 N ATOM 376 CA VAL A 46 9.318 72.098 53.437 1.00 33.99 C ANISOU 376 CA VAL A 46 4359 4211 4344 474 16 -61 C ATOM 377 C VAL A 46 9.404 73.393 52.634 1.00 35.52 C ANISOU 377 C VAL A 46 4477 4513 4506 431 72 -106 C ATOM 378 O VAL A 46 10.053 74.367 53.059 1.00 34.34 O ANISOU 378 O VAL A 46 4237 4451 4361 425 55 -84 O ATOM 379 CB VAL A 46 10.403 71.103 52.998 1.00 39.76 C ANISOU 379 CB VAL A 46 5072 4875 5160 604 30 -87 C ATOM 380 CG1 VAL A 46 11.746 71.837 52.818 1.00 39.71 C ANISOU 380 CG1 VAL A 46 4916 4968 5205 667 49 -98 C ATOM 381 CG2 VAL A 46 10.527 69.970 54.029 1.00 44.30 C ANISOU 381 CG2 VAL A 46 5711 5344 5777 657 -49 -18 C ATOM 382 N SER A 47 8.804 73.412 51.437 1.00 35.10 N ANISOU 382 N SER A 47 4467 4450 4419 399 132 -167 N ATOM 383 CA SER A 47 8.823 74.629 50.618 1.00 33.64 C ANISOU 383 CA SER A 47 4229 4359 4195 354 182 -199 C ATOM 384 C SER A 47 8.064 75.753 51.319 1.00 31.80 C ANISOU 384 C SER A 47 3981 4184 3918 265 147 -157 C ATOM 385 O SER A 47 8.460 76.923 51.265 1.00 33.00 O ANISOU 385 O SER A 47 4064 4413 4059 241 159 -152 O ATOM 386 CB SER A 47 8.220 74.345 49.223 1.00 34.72 C ANISOU 386 CB SER A 47 4439 4467 4286 332 236 -266 C ATOM 387 OG SER A 47 8.073 75.540 48.461 1.00 38.75 O ANISOU 387 OG SER A 47 4919 5061 4745 278 272 -281 O ATOM 388 N LEU A 48 6.973 75.408 51.988 1.00 31.57 N ANISOU 388 N LEU A 48 4017 4112 3866 216 110 -127 N ATOM 389 CA LEU A 48 6.227 76.375 52.791 1.00 34.06 C ANISOU 389 CA LEU A 48 4321 4475 4145 146 88 -92 C ATOM 390 C LEU A 48 7.055 76.870 53.991 1.00 35.65 C ANISOU 390 C LEU A 48 4475 4718 4353 164 46 -50 C ATOM 391 O LEU A 48 7.052 78.070 54.309 1.00 33.36 O ANISOU 391 O LEU A 48 4147 4490 4039 125 43 -46 O ATOM 392 CB LEU A 48 4.916 75.714 53.238 1.00 30.58 C ANISOU 392 CB LEU A 48 3952 3978 3687 92 73 -69 C ATOM 393 CG LEU A 48 3.939 76.536 54.090 1.00 37.50 C ANISOU 393 CG LEU A 48 4823 4895 4529 24 71 -38 C ATOM 394 CD1 LEU A 48 3.480 77.764 53.309 1.00 40.04 C ANISOU 394 CD1 LEU A 48 5102 5275 4836 -9 95 -69 C ATOM 395 CD2 LEU A 48 2.721 75.672 54.487 1.00 39.76 C ANISOU 395 CD2 LEU A 48 5168 5125 4813 -29 70 -12 C ATOM 396 N ALA A 49 7.782 75.967 54.664 1.00 33.19 N ANISOU 396 N ALA A 49 4170 4367 4073 223 5 -18 N ATOM 397 CA ALA A 49 8.645 76.373 55.782 1.00 32.44 C ANISOU 397 CA ALA A 49 4032 4313 3981 240 -57 24 C ATOM 398 C ALA A 49 9.765 77.311 55.323 1.00 32.51 C ANISOU 398 C ALA A 49 3931 4397 4025 257 -48 -1 C ATOM 399 O ALA A 49 10.153 78.249 56.052 1.00 32.49 O ANISOU 399 O ALA A 49 3888 4451 4005 224 -90 16 O ATOM 400 CB ALA A 49 9.251 75.120 56.447 1.00 33.96 C ANISOU 400 CB ALA A 49 4253 4441 4211 312 -115 70 C ATOM 401 N ALA A 50 10.336 77.028 54.149 1.00 31.89 N ANISOU 401 N ALA A 50 3806 4317 3994 306 8 -42 N ATOM 402 CA ALA A 50 11.374 77.878 53.548 1.00 34.49 C ANISOU 402 CA ALA A 50 4024 4719 4360 313 40 -63 C ATOM 403 C ALA A 50 10.859 79.285 53.297 1.00 32.85 C ANISOU 403 C ALA A 50 3814 4564 4103 223 64 -75 C ATOM 404 O ALA A 50 11.557 80.275 53.550 1.00 33.73 O ANISOU 404 O ALA A 50 3852 4734 4230 192 46 -66 O ATOM 405 CB ALA A 50 11.866 77.281 52.224 1.00 33.19 C ANISOU 405 CB ALA A 50 3835 4541 4236 376 125 -112 C ATOM 406 N ALA A 51 9.648 79.389 52.784 1.00 30.35 N ANISOU 406 N ALA A 51 3576 4222 3734 180 98 -93 N ATOM 407 CA ALA A 51 9.018 80.696 52.622 1.00 30.05 C ANISOU 407 CA ALA A 51 3545 4218 3654 106 111 -97 C ATOM 408 C ALA A 51 8.851 81.403 53.963 1.00 34.36 C ANISOU 408 C ALA A 51 4098 4779 4180 67 52 -70 C ATOM 409 O ALA A 51 9.035 82.622 54.044 1.00 31.93 O ANISOU 409 O ALA A 51 3762 4504 3864 21 49 -74 O ATOM 410 CB ALA A 51 7.661 80.528 51.930 1.00 30.52 C ANISOU 410 CB ALA A 51 3681 4244 3673 77 139 -114 C ATOM 411 N ASP A 52 8.496 80.659 55.040 1.00 30.19 N ANISOU 411 N ASP A 52 3619 4219 3633 80 7 -44 N ATOM 412 CA ASP A 52 8.324 81.322 56.334 1.00 28.80 C ANISOU 412 CA ASP A 52 3469 4061 3415 41 -41 -25 C ATOM 413 C ASP A 52 9.666 81.659 56.993 1.00 33.03 C ANISOU 413 C ASP A 52 3941 4634 3973 49 -109 -11 C ATOM 414 O ASP A 52 9.767 82.678 57.687 1.00 34.34 O ANISOU 414 O ASP A 52 4113 4827 4108 0 -143 -16 O ATOM 415 CB ASP A 52 7.443 80.465 57.271 1.00 26.87 C ANISOU 415 CB ASP A 52 3309 3775 3125 39 -56 5 C ATOM 416 CG ASP A 52 5.990 80.498 56.855 1.00 30.98 C ANISOU 416 CG ASP A 52 3873 4273 3624 5 3 -9 C ATOM 417 OD1 ASP A 52 5.601 81.481 56.173 1.00 30.76 O ANISOU 417 OD1 ASP A 52 3821 4266 3600 -21 37 -39 O ATOM 418 OD2 ASP A 52 5.241 79.550 57.146 1.00 32.15 O ANISOU 418 OD2 ASP A 52 4075 4381 3760 1 12 13 O ATOM 419 N ILE A 53 10.709 80.850 56.772 1.00 31.60 N ANISOU 419 N ILE A 53 3698 4456 3854 111 -132 4 N ATOM 420 CA ILE A 53 12.050 81.258 57.201 1.00 31.11 C ANISOU 420 CA ILE A 53 3540 4442 3837 116 -199 17 C ATOM 421 C ILE A 53 12.440 82.570 56.527 1.00 32.96 C ANISOU 421 C ILE A 53 3706 4722 4093 58 -162 -12 C ATOM 422 O ILE A 53 12.994 83.483 57.170 1.00 32.75 O ANISOU 422 O ILE A 53 3647 4730 4066 5 -222 -10 O ATOM 423 CB ILE A 53 13.077 80.142 56.901 1.00 30.90 C ANISOU 423 CB ILE A 53 3435 4410 3896 210 -214 36 C ATOM 424 CG1 ILE A 53 12.890 78.935 57.849 1.00 32.48 C ANISOU 424 CG1 ILE A 53 3709 4555 4078 263 -284 83 C ATOM 425 CG2 ILE A 53 14.509 80.649 57.051 1.00 32.29 C ANISOU 425 CG2 ILE A 53 3471 4650 4147 214 -268 46 C ATOM 426 CD1 ILE A 53 13.610 77.658 57.327 1.00 32.15 C ANISOU 426 CD1 ILE A 53 3616 4473 4127 375 -277 92 C ATOM 427 N ALA A 54 12.122 82.704 55.227 1.00 32.77 N ANISOU 427 N ALA A 54 3675 4694 4082 58 -67 -38 N ATOM 428 CA ALA A 54 12.491 83.924 54.506 1.00 31.02 C ANISOU 428 CA ALA A 54 3400 4509 3877 -2 -25 -54 C ATOM 429 C ALA A 54 11.698 85.144 54.996 1.00 28.48 C ANISOU 429 C ALA A 54 3149 4172 3499 -78 -44 -63 C ATOM 430 O ALA A 54 12.178 86.278 54.874 1.00 31.93 O ANISOU 430 O ALA A 54 3550 4628 3954 -140 -48 -67 O ATOM 431 CB ALA A 54 12.300 83.734 53.004 1.00 33.60 C ANISOU 431 CB ALA A 54 3724 4833 4209 16 78 -73 C ATOM 432 N VAL A 55 10.477 84.948 55.498 1.00 29.70 N ANISOU 432 N VAL A 55 3404 4289 3594 -76 -46 -68 N ATOM 433 CA VAL A 55 9.778 86.046 56.178 1.00 30.77 C ANISOU 433 CA VAL A 55 3603 4407 3682 -131 -63 -83 C ATOM 434 C VAL A 55 10.612 86.566 57.353 1.00 31.77 C ANISOU 434 C VAL A 55 3718 4554 3801 -168 -149 -83 C ATOM 435 O VAL A 55 10.795 87.777 57.521 1.00 32.65 O ANISOU 435 O VAL A 55 3835 4661 3909 -229 -165 -103 O ATOM 436 CB VAL A 55 8.365 85.606 56.615 1.00 30.50 C ANISOU 436 CB VAL A 55 3659 4338 3593 -115 -41 -86 C ATOM 437 CG1 VAL A 55 7.707 86.647 57.592 1.00 30.41 C ANISOU 437 CG1 VAL A 55 3715 4310 3529 -156 -52 -109 C ATOM 438 CG2 VAL A 55 7.463 85.451 55.378 1.00 27.13 C ANISOU 438 CG2 VAL A 55 3241 3892 3177 -102 27 -91 C ATOM 439 N GLY A 56 11.172 85.666 58.164 1.00 33.63 N ANISOU 439 N GLY A 56 3940 4805 4031 -135 -215 -59 N ATOM 440 CA GLY A 56 11.960 86.134 59.297 1.00 32.41 C ANISOU 440 CA GLY A 56 3781 4674 3859 -175 -318 -57 C ATOM 441 C GLY A 56 13.280 86.778 58.889 1.00 35.17 C ANISOU 441 C GLY A 56 4008 5064 4290 -214 -353 -57 C ATOM 442 O GLY A 56 13.713 87.765 59.488 1.00 34.30 O ANISOU 442 O GLY A 56 3902 4961 4169 -287 -418 -75 O ATOM 443 N VAL A 57 13.960 86.205 57.893 1.00 30.90 N ANISOU 443 N VAL A 57 3358 4550 3834 -170 -309 -38 N ATOM 444 CA VAL A 57 15.298 86.659 57.530 1.00 34.99 C ANISOU 444 CA VAL A 57 3734 5119 4443 -203 -333 -30 C ATOM 445 C VAL A 57 15.249 87.921 56.670 1.00 34.06 C ANISOU 445 C VAL A 57 3605 4994 4341 -284 -263 -49 C ATOM 446 O VAL A 57 16.131 88.781 56.776 1.00 34.31 O ANISOU 446 O VAL A 57 3562 5052 4423 -361 -305 -47 O ATOM 447 CB VAL A 57 16.050 85.520 56.809 1.00 37.72 C ANISOU 447 CB VAL A 57 3964 5496 4874 -113 -294 -7 C ATOM 448 CG1 VAL A 57 17.394 86.011 56.215 1.00 39.53 C ANISOU 448 CG1 VAL A 57 4021 5787 5211 -147 -279 2 C ATOM 449 CG2 VAL A 57 16.304 84.388 57.805 1.00 38.58 C ANISOU 449 CG2 VAL A 57 4077 5601 4981 -39 -392 24 C ATOM 450 N LEU A 58 14.248 88.041 55.794 1.00 31.89 N ANISOU 450 N LEU A 58 3404 4683 4030 -272 -165 -61 N ATOM 451 CA LEU A 58 14.241 89.097 54.781 1.00 34.97 C ANISOU 451 CA LEU A 58 3786 5064 4437 -336 -94 -63 C ATOM 452 C LEU A 58 13.010 89.991 54.852 1.00 30.95 C ANISOU 452 C LEU A 58 3406 4489 3864 -369 -79 -83 C ATOM 453 O LEU A 58 13.153 91.211 54.926 1.00 34.56 O ANISOU 453 O LEU A 58 3883 4919 4330 -447 -95 -90 O ATOM 454 CB LEU A 58 14.337 88.486 53.360 1.00 34.68 C ANISOU 454 CB LEU A 58 3703 5050 4423 -289 16 -51 C ATOM 455 CG LEU A 58 15.701 87.955 52.904 1.00 42.39 C ANISOU 455 CG LEU A 58 4527 6093 5486 -265 45 -35 C ATOM 456 CD1 LEU A 58 15.530 87.209 51.574 1.00 40.55 C ANISOU 456 CD1 LEU A 58 4295 5869 5242 -203 165 -41 C ATOM 457 CD2 LEU A 58 16.738 89.080 52.773 1.00 40.63 C ANISOU 457 CD2 LEU A 58 4205 5905 5327 -367 41 -19 C ATOM 458 N ALA A 59 11.796 89.422 54.820 1.00 27.80 N ANISOU 458 N ALA A 59 3093 4060 3411 -311 -49 -92 N ATOM 459 CA ALA A 59 10.612 90.274 54.729 1.00 30.62 C ANISOU 459 CA ALA A 59 3547 4359 3727 -329 -24 -107 C ATOM 460 C ALA A 59 10.440 91.147 55.974 1.00 32.88 C ANISOU 460 C ALA A 59 3898 4609 3984 -371 -86 -138 C ATOM 461 O ALA A 59 9.956 92.286 55.859 1.00 30.42 O ANISOU 461 O ALA A 59 3645 4243 3670 -408 -73 -154 O ATOM 462 CB ALA A 59 9.345 89.443 54.500 1.00 26.09 C ANISOU 462 CB ALA A 59 3031 3768 3114 -263 15 -109 C ATOM 463 N ILE A 60 10.792 90.650 57.163 1.00 30.13 N ANISOU 463 N ILE A 60 3556 4284 3608 -365 -154 -149 N ATOM 464 CA ILE A 60 10.580 91.475 58.356 1.00 28.47 C ANISOU 464 CA ILE A 60 3430 4038 3347 -407 -207 -189 C ATOM 465 C ILE A 60 11.617 92.601 58.405 1.00 29.64 C ANISOU 465 C ILE A 60 3547 4177 3539 -499 -262 -201 C ATOM 466 O ILE A 60 11.236 93.757 58.651 1.00 31.19 O ANISOU 466 O ILE A 60 3823 4309 3720 -545 -263 -238 O ATOM 467 CB ILE A 60 10.545 90.616 59.630 1.00 30.94 C ANISOU 467 CB ILE A 60 3785 4378 3592 -379 -266 -193 C ATOM 468 CG1 ILE A 60 9.178 89.890 59.694 1.00 32.00 C ANISOU 468 CG1 ILE A 60 3985 4496 3677 -314 -195 -191 C ATOM 469 CG2 ILE A 60 10.847 91.473 60.881 1.00 31.36 C ANISOU 469 CG2 ILE A 60 3914 4413 3588 -443 -347 -237 C ATOM 470 CD1 ILE A 60 9.015 88.826 60.828 1.00 32.13 C ANISOU 470 CD1 ILE A 60 4052 4535 3620 -283 -232 -175 C ATOM 471 N PRO A 61 12.916 92.350 58.152 1.00 29.79 N ANISOU 471 N PRO A 61 3446 4252 3622 -531 -304 -172 N ATOM 472 CA PRO A 61 13.845 93.496 58.033 1.00 31.45 C ANISOU 472 CA PRO A 61 3613 4449 3888 -636 -344 -177 C ATOM 473 C PRO A 61 13.408 94.505 56.963 1.00 34.52 C ANISOU 473 C PRO A 61 4034 4776 4305 -672 -262 -170 C ATOM 474 O PRO A 61 13.499 95.725 57.173 1.00 31.47 O ANISOU 474 O PRO A 61 3702 4325 3928 -754 -291 -194 O ATOM 475 CB PRO A 61 15.197 92.828 57.704 1.00 32.31 C ANISOU 475 CB PRO A 61 3555 4643 4079 -642 -372 -135 C ATOM 476 CG PRO A 61 15.098 91.432 58.366 1.00 36.84 C ANISOU 476 CG PRO A 61 4121 5260 4615 -547 -411 -124 C ATOM 477 CD PRO A 61 13.633 91.043 58.218 1.00 34.29 C ANISOU 477 CD PRO A 61 3918 4893 4218 -475 -333 -137 C ATOM 478 N PHE A 62 12.891 94.031 55.832 1.00 28.70 N ANISOU 478 N PHE A 62 3281 4050 3575 -613 -169 -138 N ATOM 479 CA PHE A 62 12.351 94.944 54.820 1.00 32.46 C ANISOU 479 CA PHE A 62 3806 4464 4061 -638 -103 -121 C ATOM 480 C PHE A 62 11.166 95.741 55.356 1.00 33.28 C ANISOU 480 C PHE A 62 4045 4476 4123 -624 -110 -161 C ATOM 481 O PHE A 62 11.029 96.930 55.055 1.00 31.71 O ANISOU 481 O PHE A 62 3903 4199 3946 -676 -105 -161 O ATOM 482 CB PHE A 62 11.892 94.181 53.572 1.00 27.87 C ANISOU 482 CB PHE A 62 3202 3914 3472 -572 -16 -84 C ATOM 483 CG PHE A 62 13.006 93.594 52.733 1.00 32.22 C ANISOU 483 CG PHE A 62 3632 4543 4068 -584 28 -47 C ATOM 484 CD1 PHE A 62 14.342 93.882 52.982 1.00 36.38 C ANISOU 484 CD1 PHE A 62 4053 5110 4658 -657 -5 -38 C ATOM 485 CD2 PHE A 62 12.696 92.782 51.651 1.00 35.54 C ANISOU 485 CD2 PHE A 62 4040 4995 4467 -523 106 -27 C ATOM 486 CE1 PHE A 62 15.368 93.339 52.188 1.00 40.26 C ANISOU 486 CE1 PHE A 62 4415 5680 5203 -659 54 -6 C ATOM 487 CE2 PHE A 62 13.691 92.249 50.842 1.00 32.29 C ANISOU 487 CE2 PHE A 62 3525 4652 4090 -524 167 -3 C ATOM 488 CZ PHE A 62 15.046 92.529 51.109 1.00 36.94 C ANISOU 488 CZ PHE A 62 3994 5288 4754 -588 149 8 C ATOM 489 N ALA A 63 10.255 95.087 56.085 1.00 28.87 N ANISOU 489 N ALA A 63 3539 3922 3509 -548 -112 -191 N ATOM 490 CA ALA A 63 9.093 95.791 56.636 1.00 30.20 C ANISOU 490 CA ALA A 63 3822 4011 3643 -520 -101 -235 C ATOM 491 C ALA A 63 9.522 96.866 57.630 1.00 29.40 C ANISOU 491 C ALA A 63 3789 3849 3532 -592 -163 -289 C ATOM 492 O ALA A 63 8.975 97.971 57.642 1.00 32.15 O ANISOU 492 O ALA A 63 4223 4101 3890 -603 -149 -318 O ATOM 493 CB ALA A 63 8.137 94.800 57.320 1.00 28.84 C ANISOU 493 CB ALA A 63 3678 3868 3412 -438 -80 -255 C ATOM 494 N ILE A 64 10.483 96.552 58.489 1.00 32.62 N ANISOU 494 N ILE A 64 4167 4306 3921 -640 -239 -306 N ATOM 495 CA ILE A 64 11.014 97.558 59.412 1.00 36.14 C ANISOU 495 CA ILE A 64 4681 4697 4353 -726 -316 -362 C ATOM 496 C ILE A 64 11.579 98.747 58.635 1.00 38.68 C ANISOU 496 C ILE A 64 4992 4951 4754 -818 -319 -344 C ATOM 497 O ILE A 64 11.315 99.921 58.958 1.00 37.01 O ANISOU 497 O ILE A 64 4888 4632 4543 -861 -334 -392 O ATOM 498 CB ILE A 64 12.066 96.916 60.340 1.00 35.57 C ANISOU 498 CB ILE A 64 4558 4704 4253 -767 -419 -366 C ATOM 499 CG1 ILE A 64 11.378 95.910 61.284 1.00 34.99 C ANISOU 499 CG1 ILE A 64 4540 4672 4081 -686 -418 -384 C ATOM 500 CG2 ILE A 64 12.889 97.997 61.098 1.00 33.68 C ANISOU 500 CG2 ILE A 64 4366 4417 4016 -888 -522 -417 C ATOM 501 CD1 ILE A 64 12.355 95.020 62.128 1.00 34.74 C ANISOU 501 CD1 ILE A 64 4456 4726 4018 -703 -527 -366 C ATOM 502 N THR A 65 12.363 98.458 57.593 1.00 33.46 N ANISOU 502 N THR A 65 4207 4346 4160 -850 -298 -275 N ATOM 503 CA THR A 65 12.997 99.513 56.791 1.00 34.38 C ANISOU 503 CA THR A 65 4304 4408 4351 -952 -291 -241 C ATOM 504 C THR A 65 11.960 100.431 56.148 1.00 35.49 C ANISOU 504 C THR A 65 4556 4433 4497 -925 -230 -236 C ATOM 505 O THR A 65 12.053 101.662 56.237 1.00 34.82 O ANISOU 505 O THR A 65 4551 4237 4441 -1001 -256 -254 O ATOM 506 CB THR A 65 13.868 98.865 55.700 1.00 39.99 C ANISOU 506 CB THR A 65 4862 5215 5118 -969 -244 -165 C ATOM 507 OG1 THR A 65 14.887 98.072 56.325 1.00 39.01 O ANISOU 507 OG1 THR A 65 4621 5190 5010 -986 -310 -168 O ATOM 508 CG2 THR A 65 14.529 99.916 54.829 1.00 44.78 C ANISOU 508 CG2 THR A 65 5446 5773 5794 -1085 -220 -118 C ATOM 509 N ILE A 66 10.954 99.843 55.496 1.00 31.77 N ANISOU 509 N ILE A 66 4091 3978 4000 -818 -159 -208 N ATOM 510 CA ILE A 66 9.975 100.657 54.782 1.00 35.52 C ANISOU 510 CA ILE A 66 4654 4353 4491 -783 -114 -188 C ATOM 511 C ILE A 66 9.058 101.448 55.731 1.00 34.55 C ANISOU 511 C ILE A 66 4660 4118 4349 -742 -131 -265 C ATOM 512 O ILE A 66 8.471 102.453 55.311 1.00 36.01 O ANISOU 512 O ILE A 66 4927 4187 4569 -732 -116 -257 O ATOM 513 CB ILE A 66 9.184 99.759 53.803 1.00 39.53 C ANISOU 513 CB ILE A 66 5122 4918 4978 -686 -50 -138 C ATOM 514 CG1 ILE A 66 8.571 100.607 52.687 1.00 46.47 C ANISOU 514 CG1 ILE A 66 6062 5712 5884 -679 -19 -81 C ATOM 515 CG2 ILE A 66 8.081 98.931 54.516 1.00 32.55 C ANISOU 515 CG2 ILE A 66 4257 4064 4046 -575 -38 -184 C ATOM 516 CD1 ILE A 66 8.077 99.786 51.480 1.00 48.31 C ANISOU 516 CD1 ILE A 66 6252 6011 6091 -618 29 -19 C ATOM 517 N SER A 67 8.934 101.041 57.006 1.00 32.94 N ANISOU 517 N SER A 67 4484 3942 4090 -717 -161 -340 N ATOM 518 CA SER A 67 8.164 101.843 57.958 1.00 38.34 C ANISOU 518 CA SER A 67 5298 4521 4747 -685 -163 -426 C ATOM 519 C SER A 67 8.797 103.211 58.213 1.00 39.15 C ANISOU 519 C SER A 67 5488 4500 4887 -791 -217 -463 C ATOM 520 O SER A 67 8.107 104.128 58.687 1.00 39.98 O ANISOU 520 O SER A 67 5719 4481 4993 -759 -206 -529 O ATOM 521 CB SER A 67 7.998 101.090 59.295 1.00 37.55 C ANISOU 521 CB SER A 67 5222 4486 4557 -650 -179 -495 C ATOM 522 OG SER A 67 9.200 101.042 60.048 1.00 37.37 O ANISOU 522 OG SER A 67 5189 4502 4506 -751 -269 -520 O ATOM 523 N THR A 68 10.087 103.387 57.902 1.00 39.21 N ANISOU 523 N THR A 68 5431 4533 4934 -917 -272 -423 N ATOM 524 CA THR A 68 10.710 104.674 58.166 1.00 41.97 C ANISOU 524 CA THR A 68 5863 4759 5325 -1036 -331 -458 C ATOM 525 C THR A 68 10.458 105.688 57.060 1.00 41.94 C ANISOU 525 C THR A 68 5906 4632 5398 -1057 -294 -396 C ATOM 526 O THR A 68 10.746 106.864 57.256 1.00 40.78 O ANISOU 526 O THR A 68 5857 4346 5291 -1143 -335 -427 O ATOM 527 CB THR A 68 12.224 104.521 58.369 1.00 48.73 C ANISOU 527 CB THR A 68 6621 5691 6205 -1180 -414 -441 C ATOM 528 OG1 THR A 68 12.848 104.127 57.136 1.00 40.36 O ANISOU 528 OG1 THR A 68 5421 4710 5206 -1215 -373 -333 O ATOM 529 CG2 THR A 68 12.523 103.463 59.464 1.00 41.95 C ANISOU 529 CG2 THR A 68 5716 4956 5268 -1155 -470 -487 C ATOM 530 N GLY A 69 9.964 105.267 55.898 1.00 41.11 N ANISOU 530 N GLY A 69 5742 4567 5310 -987 -226 -308 N ATOM 531 CA GLY A 69 9.799 106.201 54.791 1.00 39.39 C ANISOU 531 CA GLY A 69 5574 4238 5154 -1014 -202 -232 C ATOM 532 C GLY A 69 11.087 106.778 54.231 1.00 43.12 C ANISOU 532 C GLY A 69 6009 4694 5681 -1182 -226 -169 C ATOM 533 O GLY A 69 11.066 107.871 53.654 1.00 43.10 O ANISOU 533 O GLY A 69 6093 4553 5730 -1239 -226 -124 O ATOM 534 N PHE A 70 12.205 106.059 54.342 1.00 41.39 N ANISOU 534 N PHE A 70 5656 4611 5460 -1263 -244 -156 N ATOM 535 CA PHE A 70 13.504 106.585 53.897 1.00 43.14 C ANISOU 535 CA PHE A 70 5814 4832 5746 -1435 -262 -99 C ATOM 536 C PHE A 70 13.521 106.893 52.385 1.00 41.21 C ANISOU 536 C PHE A 70 5561 4568 5529 -1464 -183 23 C ATOM 537 O PHE A 70 12.766 106.328 51.588 1.00 38.31 O ANISOU 537 O PHE A 70 5189 4246 5120 -1352 -120 72 O ATOM 538 CB PHE A 70 14.612 105.581 54.243 1.00 46.24 C ANISOU 538 CB PHE A 70 6033 5396 6140 -1484 -286 -103 C ATOM 539 CG PHE A 70 14.617 104.357 53.355 1.00 48.16 C ANISOU 539 CG PHE A 70 6150 5791 6360 -1401 -203 -37 C ATOM 540 CD1 PHE A 70 13.541 103.493 53.328 1.00 48.50 C ANISOU 540 CD1 PHE A 70 6217 5876 6336 -1242 -166 -54 C ATOM 541 CD2 PHE A 70 15.699 104.091 52.532 1.00 56.06 C ANISOU 541 CD2 PHE A 70 7008 6886 7406 -1487 -156 38 C ATOM 542 CE1 PHE A 70 13.538 102.382 52.500 1.00 52.19 C ANISOU 542 CE1 PHE A 70 6585 6467 6779 -1173 -95 -3 C ATOM 543 CE2 PHE A 70 15.708 102.982 51.708 1.00 51.00 C ANISOU 543 CE2 PHE A 70 6267 6372 6737 -1407 -71 86 C ATOM 544 CZ PHE A 70 14.629 102.131 51.689 1.00 50.50 C ANISOU 544 CZ PHE A 70 6245 6339 6603 -1252 -47 63 C ATOM 545 N CYS A 71 14.423 107.786 51.987 1.00 41.93 N ANISOU 545 N CYS A 71 5652 4594 5685 -1626 -191 77 N ATOM 546 CA CYS A 71 14.582 108.117 50.572 1.00 43.86 C ANISOU 546 CA CYS A 71 5896 4825 5943 -1678 -112 202 C ATOM 547 C CYS A 71 15.254 106.967 49.820 1.00 44.96 C ANISOU 547 C CYS A 71 5862 5162 6059 -1676 -31 260 C ATOM 548 O CYS A 71 16.268 106.429 50.265 1.00 48.92 O ANISOU 548 O CYS A 71 6217 5778 6592 -1739 -45 235 O ATOM 549 CB CYS A 71 15.416 109.401 50.423 1.00 43.64 C ANISOU 549 CB CYS A 71 5917 4669 5995 -1872 -137 246 C ATOM 550 SG CYS A 71 14.656 110.848 51.189 1.00 52.31 S ANISOU 550 SG CYS A 71 7243 5502 7129 -1876 -224 177 S ATOM 551 N ALA A 72 14.721 106.623 48.654 1.00 43.83 N ANISOU 551 N ALA A 72 5739 5053 5861 -1606 50 339 N ATOM 552 CA ALA A 72 15.253 105.513 47.889 1.00 44.71 C ANISOU 552 CA ALA A 72 5710 5340 5937 -1587 139 381 C ATOM 553 C ALA A 72 14.890 105.696 46.429 1.00 46.29 C ANISOU 553 C ALA A 72 5981 5527 6081 -1583 225 490 C ATOM 554 O ALA A 72 13.868 106.308 46.099 1.00 44.89 O ANISOU 554 O ALA A 72 5954 5229 5875 -1528 198 520 O ATOM 555 CB ALA A 72 14.718 104.161 48.396 1.00 41.58 C ANISOU 555 CB ALA A 72 5251 5057 5490 -1430 129 307 C ATOM 556 N ALA A 73 15.728 105.134 45.560 1.00 46.13 N ANISOU 556 N ALA A 73 5852 5636 6041 -1635 327 548 N ATOM 557 CA ALA A 73 15.342 104.992 44.168 1.00 48.10 C ANISOU 557 CA ALA A 73 6168 5909 6199 -1609 415 638 C ATOM 558 C ALA A 73 14.061 104.170 44.096 1.00 46.01 C ANISOU 558 C ALA A 73 5963 5666 5854 -1430 386 598 C ATOM 559 O ALA A 73 13.882 103.195 44.832 1.00 40.06 O ANISOU 559 O ALA A 73 5130 4989 5103 -1333 359 510 O ATOM 560 CB ALA A 73 16.462 104.339 43.349 1.00 50.93 C ANISOU 560 CB ALA A 73 6389 6423 6540 -1675 547 682 C ATOM 561 N CYS A 74 13.151 104.589 43.221 1.00 44.13 N ANISOU 561 N CYS A 74 5866 5353 5549 -1391 383 668 N ATOM 562 CA CYS A 74 11.785 104.103 43.334 1.00 44.79 C ANISOU 562 CA CYS A 74 6013 5419 5587 -1233 322 629 C ATOM 563 C CYS A 74 11.719 102.604 43.060 1.00 45.71 C ANISOU 563 C CYS A 74 6040 5692 5634 -1144 371 586 C ATOM 564 O CYS A 74 10.982 101.885 43.735 1.00 42.70 O ANISOU 564 O CYS A 74 5636 5333 5255 -1030 321 509 O ATOM 565 CB CYS A 74 10.862 104.902 42.401 1.00 48.87 C ANISOU 565 CB CYS A 74 6691 5824 6055 -1213 292 725 C ATOM 566 SG CYS A 74 9.067 104.599 42.719 1.00 49.50 S ANISOU 566 SG CYS A 74 6835 5850 6121 -1023 191 678 S ATOM 567 N HIS A 75 12.535 102.100 42.118 1.00 41.95 N ANISOU 567 N HIS A 75 5513 5324 5102 -1197 477 629 N ATOM 568 CA HIS A 75 12.532 100.663 41.869 1.00 41.08 C ANISOU 568 CA HIS A 75 5328 5349 4933 -1110 528 577 C ATOM 569 C HIS A 75 13.211 99.878 42.987 1.00 39.78 C ANISOU 569 C HIS A 75 5009 5258 4846 -1085 522 485 C ATOM 570 O HIS A 75 12.830 98.735 43.234 1.00 37.26 O ANISOU 570 O HIS A 75 4650 5004 4502 -980 514 423 O ATOM 571 CB HIS A 75 13.163 100.360 40.511 1.00 47.54 C ANISOU 571 CB HIS A 75 6151 6254 5658 -1163 654 641 C ATOM 572 CG HIS A 75 12.283 100.775 39.369 1.00 60.49 C ANISOU 572 CG HIS A 75 7957 7841 7184 -1154 642 724 C ATOM 573 ND1 HIS A 75 12.182 102.085 38.948 1.00 62.53 N ANISOU 573 ND1 HIS A 75 8330 7987 7441 -1241 619 825 N ATOM 574 CD2 HIS A 75 11.389 100.074 38.631 1.00 62.78 C ANISOU 574 CD2 HIS A 75 8326 8164 7363 -1067 626 722 C ATOM 575 CE1 HIS A 75 11.296 102.165 37.972 1.00 65.12 C ANISOU 575 CE1 HIS A 75 8798 8289 7658 -1202 590 889 C ATOM 576 NE2 HIS A 75 10.800 100.959 37.761 1.00 68.40 N ANISOU 576 NE2 HIS A 75 9191 8794 8003 -1101 590 825 N ATOM 577 N GLY A 76 14.197 100.458 43.683 1.00 39.45 N ANISOU 577 N GLY A 76 4885 5205 4898 -1182 515 479 N ATOM 578 CA GLY A 76 14.688 99.811 44.894 1.00 43.46 C ANISOU 578 CA GLY A 76 5266 5767 5479 -1151 471 395 C ATOM 579 C GLY A 76 13.627 99.761 45.978 1.00 39.58 C ANISOU 579 C GLY A 76 4839 5206 4994 -1060 360 328 C ATOM 580 O GLY A 76 13.466 98.748 46.668 1.00 38.63 O ANISOU 580 O GLY A 76 4660 5145 4873 -973 333 262 O ATOM 581 N CYS A 77 12.901 100.867 46.149 1.00 38.74 N ANISOU 581 N CYS A 77 4855 4969 4897 -1079 301 345 N ATOM 582 CA CYS A 77 11.770 100.908 47.068 1.00 35.41 C ANISOU 582 CA CYS A 77 4503 4476 4477 -985 218 283 C ATOM 583 C CYS A 77 10.740 99.827 46.733 1.00 33.65 C ANISOU 583 C CYS A 77 4291 4306 4186 -854 227 266 C ATOM 584 O CYS A 77 10.277 99.099 47.618 1.00 31.59 O ANISOU 584 O CYS A 77 4002 4073 3927 -775 192 198 O ATOM 585 CB CYS A 77 11.118 102.303 46.997 1.00 34.04 C ANISOU 585 CB CYS A 77 4465 4144 4324 -1012 174 317 C ATOM 586 SG CYS A 77 9.663 102.481 48.065 1.00 38.87 S ANISOU 586 SG CYS A 77 5159 4662 4947 -886 95 238 S ATOM 587 N LEU A 78 10.354 99.718 45.452 1.00 33.46 N ANISOU 587 N LEU A 78 4319 4296 4099 -840 271 330 N ATOM 588 CA LEU A 78 9.389 98.690 45.047 1.00 32.92 C ANISOU 588 CA LEU A 78 4265 4278 3967 -732 269 314 C ATOM 589 C LEU A 78 9.853 97.297 45.423 1.00 32.85 C ANISOU 589 C LEU A 78 4151 4380 3951 -688 300 253 C ATOM 590 O LEU A 78 9.041 96.446 45.811 1.00 32.98 O ANISOU 590 O LEU A 78 4164 4416 3951 -600 270 208 O ATOM 591 CB LEU A 78 9.143 98.724 43.535 1.00 36.93 C ANISOU 591 CB LEU A 78 4844 4798 4389 -744 309 391 C ATOM 592 CG LEU A 78 8.130 99.739 43.056 1.00 42.97 C ANISOU 592 CG LEU A 78 5731 5453 5143 -731 248 454 C ATOM 593 CD1 LEU A 78 8.173 99.853 41.491 1.00 38.86 C ANISOU 593 CD1 LEU A 78 5293 4953 4520 -772 289 547 C ATOM 594 CD2 LEU A 78 6.737 99.364 43.607 1.00 35.09 C ANISOU 594 CD2 LEU A 78 4744 4428 4162 -614 172 407 C ATOM 595 N PHE A 79 11.142 97.011 45.253 1.00 35.69 N ANISOU 595 N PHE A 79 4421 4813 4326 -747 364 258 N ATOM 596 CA PHE A 79 11.584 95.657 45.556 1.00 33.84 C ANISOU 596 CA PHE A 79 4089 4674 4093 -689 391 205 C ATOM 597 C PHE A 79 11.419 95.352 47.058 1.00 32.28 C ANISOU 597 C PHE A 79 3852 4464 3948 -647 313 141 C ATOM 598 O PHE A 79 10.923 94.279 47.439 1.00 33.83 O ANISOU 598 O PHE A 79 4037 4691 4126 -563 296 100 O ATOM 599 CB PHE A 79 13.032 95.459 45.077 1.00 35.33 C ANISOU 599 CB PHE A 79 4171 4944 4306 -751 481 224 C ATOM 600 CG PHE A 79 13.556 94.086 45.380 1.00 44.59 C ANISOU 600 CG PHE A 79 5240 6205 5498 -678 507 172 C ATOM 601 CD1 PHE A 79 13.213 93.007 44.562 1.00 44.63 C ANISOU 601 CD1 PHE A 79 5271 6254 5433 -603 565 154 C ATOM 602 CD2 PHE A 79 14.313 93.851 46.524 1.00 43.23 C ANISOU 602 CD2 PHE A 79 4956 6059 5408 -680 460 138 C ATOM 603 CE1 PHE A 79 13.653 91.737 44.844 1.00 44.86 C ANISOU 603 CE1 PHE A 79 5218 6342 5486 -527 587 105 C ATOM 604 CE2 PHE A 79 14.759 92.574 46.817 1.00 47.84 C ANISOU 604 CE2 PHE A 79 5451 6712 6016 -601 473 98 C ATOM 605 CZ PHE A 79 14.430 91.514 45.973 1.00 46.88 C ANISOU 605 CZ PHE A 79 5357 6622 5834 -521 541 81 C ATOM 606 N ILE A 80 11.776 96.318 47.920 1.00 33.41 N ANISOU 606 N ILE A 80 3993 4554 4147 -711 261 134 N ATOM 607 CA ILE A 80 11.597 96.183 49.370 1.00 34.43 C ANISOU 607 CA ILE A 80 4113 4666 4304 -683 184 73 C ATOM 608 C ILE A 80 10.126 96.016 49.719 1.00 30.01 C ANISOU 608 C ILE A 80 3641 4056 3706 -596 153 46 C ATOM 609 O ILE A 80 9.768 95.267 50.644 1.00 30.55 O ANISOU 609 O ILE A 80 3697 4145 3764 -537 122 -1 O ATOM 610 CB ILE A 80 12.196 97.422 50.086 1.00 40.20 C ANISOU 610 CB ILE A 80 4853 5332 5088 -782 133 67 C ATOM 611 CG1 ILE A 80 13.707 97.384 49.996 1.00 51.76 C ANISOU 611 CG1 ILE A 80 6193 6866 6609 -869 151 87 C ATOM 612 CG2 ILE A 80 11.775 97.507 51.531 1.00 52.36 C ANISOU 612 CG2 ILE A 80 6433 6833 6629 -755 53 0 C ATOM 613 CD1 ILE A 80 14.217 96.036 50.204 1.00 52.90 C ANISOU 613 CD1 ILE A 80 6227 7115 6757 -804 163 66 C ATOM 614 N ALA A 81 9.255 96.746 49.016 1.00 33.48 N ANISOU 614 N ALA A 81 4167 4427 4129 -589 158 80 N ATOM 615 CA ALA A 81 7.824 96.730 49.329 1.00 33.99 C ANISOU 615 CA ALA A 81 4295 4441 4177 -507 128 58 C ATOM 616 C ALA A 81 7.150 95.436 48.879 1.00 30.52 C ANISOU 616 C ALA A 81 3834 4066 3695 -432 147 54 C ATOM 617 O ALA A 81 6.220 94.951 49.541 1.00 34.29 O ANISOU 617 O ALA A 81 4319 4540 4170 -367 126 18 O ATOM 618 CB ALA A 81 7.145 97.936 48.646 1.00 31.12 C ANISOU 618 CB ALA A 81 4020 3980 3824 -516 116 105 C ATOM 619 N CYS A 82 7.592 94.862 47.769 1.00 30.23 N ANISOU 619 N CYS A 82 3777 4087 3623 -443 190 87 N ATOM 620 CA CYS A 82 6.854 93.754 47.135 1.00 32.39 C ANISOU 620 CA CYS A 82 4057 4402 3849 -382 200 83 C ATOM 621 C CYS A 82 7.424 92.367 47.413 1.00 33.21 C ANISOU 621 C CYS A 82 4095 4579 3946 -352 227 45 C ATOM 622 O CYS A 82 6.754 91.369 47.108 1.00 30.18 O ANISOU 622 O CYS A 82 3723 4214 3530 -302 226 30 O ATOM 623 CB CYS A 82 6.826 93.934 45.608 1.00 31.07 C ANISOU 623 CB CYS A 82 3939 4242 3623 -406 230 139 C ATOM 624 SG CYS A 82 5.831 95.371 45.088 1.00 36.79 S ANISOU 624 SG CYS A 82 4759 4870 4350 -415 178 201 S ATOM 625 N PHE A 83 8.651 92.272 47.922 1.00 30.87 N ANISOU 625 N PHE A 83 3729 4317 3683 -382 244 33 N ATOM 626 CA PHE A 83 9.266 90.957 48.100 1.00 28.10 C ANISOU 626 CA PHE A 83 3313 4028 3336 -341 267 4 C ATOM 627 C PHE A 83 8.400 90.034 48.970 1.00 28.42 C ANISOU 627 C PHE A 83 3369 4058 3372 -277 224 -30 C ATOM 628 O PHE A 83 8.314 88.830 48.707 1.00 32.83 O ANISOU 628 O PHE A 83 3920 4641 3914 -230 242 -46 O ATOM 629 CB PHE A 83 10.670 91.107 48.715 1.00 30.78 C ANISOU 629 CB PHE A 83 3558 4403 3732 -379 268 1 C ATOM 630 CG PHE A 83 11.378 89.792 48.861 1.00 38.35 C ANISOU 630 CG PHE A 83 4440 5419 4711 -323 288 -21 C ATOM 631 CD1 PHE A 83 11.811 89.112 47.740 1.00 39.82 C ANISOU 631 CD1 PHE A 83 4604 5648 4880 -298 369 -20 C ATOM 632 CD2 PHE A 83 11.549 89.202 50.104 1.00 38.41 C ANISOU 632 CD2 PHE A 83 4413 5432 4748 -289 226 -44 C ATOM 633 CE1 PHE A 83 12.442 87.871 47.855 1.00 42.86 C ANISOU 633 CE1 PHE A 83 4922 6070 5293 -231 391 -46 C ATOM 634 CE2 PHE A 83 12.186 87.971 50.217 1.00 38.10 C ANISOU 634 CE2 PHE A 83 4309 5433 4736 -227 236 -56 C ATOM 635 CZ PHE A 83 12.621 87.312 49.089 1.00 38.77 C ANISOU 635 CZ PHE A 83 4363 5549 4818 -193 320 -60 C ATOM 636 N VAL A 84 7.737 90.576 49.999 1.00 34.74 N ANISOU 636 N VAL A 84 4198 4817 4184 -277 176 -43 N ATOM 637 CA VAL A 84 6.873 89.737 50.833 1.00 31.04 C ANISOU 637 CA VAL A 84 3746 4342 3705 -227 151 -67 C ATOM 638 C VAL A 84 5.743 89.122 49.999 1.00 30.97 C ANISOU 638 C VAL A 84 3772 4325 3669 -194 163 -62 C ATOM 639 O VAL A 84 5.209 88.076 50.355 1.00 29.67 O ANISOU 639 O VAL A 84 3609 4165 3497 -161 156 -77 O ATOM 640 CB VAL A 84 6.295 90.544 52.017 1.00 31.94 C ANISOU 640 CB VAL A 84 3894 4414 3826 -235 118 -86 C ATOM 641 CG1 VAL A 84 5.358 91.638 51.533 1.00 33.11 C ANISOU 641 CG1 VAL A 84 4091 4510 3981 -239 120 -75 C ATOM 642 CG2 VAL A 84 5.567 89.602 53.025 1.00 31.47 C ANISOU 642 CG2 VAL A 84 3848 4361 3748 -193 108 -107 C ATOM 643 N LEU A 85 5.315 89.795 48.925 1.00 25.26 N ANISOU 643 N LEU A 85 3082 3585 2930 -210 170 -36 N ATOM 644 CA LEU A 85 4.234 89.254 48.097 1.00 30.92 C ANISOU 644 CA LEU A 85 3831 4298 3618 -187 159 -30 C ATOM 645 C LEU A 85 4.689 88.022 47.326 1.00 30.50 C ANISOU 645 C LEU A 85 3778 4280 3529 -176 188 -44 C ATOM 646 O LEU A 85 3.869 87.158 46.963 1.00 32.30 O ANISOU 646 O LEU A 85 4030 4504 3737 -158 170 -56 O ATOM 647 CB LEU A 85 3.752 90.330 47.098 1.00 30.93 C ANISOU 647 CB LEU A 85 3877 4272 3604 -207 144 11 C ATOM 648 CG LEU A 85 3.243 91.654 47.682 1.00 33.91 C ANISOU 648 CG LEU A 85 4267 4593 4026 -208 117 25 C ATOM 649 CD1 LEU A 85 2.871 92.639 46.540 1.00 33.29 C ANISOU 649 CD1 LEU A 85 4240 4477 3930 -224 94 80 C ATOM 650 CD2 LEU A 85 2.059 91.417 48.627 1.00 28.69 C ANISOU 650 CD2 LEU A 85 3587 3914 3400 -163 95 -1 C ATOM 651 N VAL A 86 5.982 87.943 47.034 1.00 25.06 N ANISOU 651 N VAL A 86 3062 3623 2837 -187 234 -46 N ATOM 652 CA VAL A 86 6.546 86.725 46.431 1.00 29.15 C ANISOU 652 CA VAL A 86 3576 4170 3330 -160 276 -73 C ATOM 653 C VAL A 86 6.428 85.561 47.415 1.00 33.59 C ANISOU 653 C VAL A 86 4117 4721 3925 -116 254 -101 C ATOM 654 O VAL A 86 5.991 84.450 47.063 1.00 30.02 O ANISOU 654 O VAL A 86 3698 4254 3453 -90 253 -126 O ATOM 655 CB VAL A 86 8.022 86.957 46.047 1.00 28.57 C ANISOU 655 CB VAL A 86 3451 4138 3266 -175 342 -68 C ATOM 656 CG1 VAL A 86 8.688 85.634 45.549 1.00 26.27 C ANISOU 656 CG1 VAL A 86 3146 3872 2965 -125 399 -107 C ATOM 657 CG2 VAL A 86 8.197 88.086 44.971 1.00 26.41 C ANISOU 657 CG2 VAL A 86 3212 3873 2949 -232 377 -28 C ATOM 658 N LEU A 87 6.820 85.808 48.672 1.00 29.32 N ANISOU 658 N LEU A 87 3531 4180 3428 -115 229 -97 N ATOM 659 CA LEU A 87 6.791 84.750 49.693 1.00 29.31 C ANISOU 659 CA LEU A 87 3519 4167 3449 -77 204 -110 C ATOM 660 C LEU A 87 5.366 84.315 49.968 1.00 29.26 C ANISOU 660 C LEU A 87 3562 4127 3428 -76 176 -112 C ATOM 661 O LEU A 87 5.088 83.118 50.153 1.00 33.35 O ANISOU 661 O LEU A 87 4099 4623 3947 -52 170 -122 O ATOM 662 CB LEU A 87 7.462 85.243 50.980 1.00 27.74 C ANISOU 662 CB LEU A 87 3279 3980 3281 -86 171 -101 C ATOM 663 CG LEU A 87 8.904 85.711 50.822 1.00 30.11 C ANISOU 663 CG LEU A 87 3507 4319 3615 -100 186 -95 C ATOM 664 CD1 LEU A 87 9.513 86.145 52.193 1.00 26.78 C ANISOU 664 CD1 LEU A 87 3049 3906 3218 -118 127 -88 C ATOM 665 CD2 LEU A 87 9.693 84.553 50.188 1.00 30.49 C ANISOU 665 CD2 LEU A 87 3517 4387 3683 -46 227 -107 C ATOM 666 N ATHR A 88 4.440 85.267 49.973 0.50 27.13 N ANISOU 666 N ATHR A 88 3308 3848 3153 -102 162 -100 N ATOM 667 N BTHR A 88 4.430 85.268 50.023 0.50 27.31 N ANISOU 667 N BTHR A 88 3330 3870 3176 -102 161 -100 N ATOM 668 CA ATHR A 88 3.055 84.921 50.264 0.50 27.74 C ANISOU 668 CA ATHR A 88 3405 3902 3232 -103 142 -99 C ATOM 669 CA BTHR A 88 3.044 84.866 50.263 0.50 27.45 C ANISOU 669 CA BTHR A 88 3370 3865 3196 -103 142 -100 C ATOM 670 C ATHR A 88 2.402 84.185 49.095 0.50 29.09 C ANISOU 670 C ATHR A 88 3606 4064 3384 -107 133 -106 C ATOM 671 C BTHR A 88 2.501 84.070 49.087 0.50 29.02 C ANISOU 671 C BTHR A 88 3597 4055 3373 -105 135 -108 C ATOM 672 O ATHR A 88 1.521 83.338 49.312 0.50 30.14 O ANISOU 672 O ATHR A 88 3748 4178 3527 -112 117 -111 O ATOM 673 O BTHR A 88 1.794 83.070 49.283 0.50 31.84 O ANISOU 673 O BTHR A 88 3968 4392 3738 -107 122 -115 O ATOM 674 CB ATHR A 88 2.294 86.201 50.610 0.50 30.23 C ANISOU 674 CB ATHR A 88 3716 4208 3563 -116 132 -88 C ATOM 675 CB BTHR A 88 2.144 86.080 50.521 0.50 29.97 C ANISOU 675 CB BTHR A 88 3684 4174 3529 -115 130 -88 C ATOM 676 OG1ATHR A 88 3.039 86.932 51.601 0.50 28.05 O ANISOU 676 OG1ATHR A 88 3431 3934 3294 -120 136 -93 O ATOM 677 OG1BTHR A 88 1.980 86.836 49.311 0.50 37.65 O ANISOU 677 OG1BTHR A 88 4671 5144 4490 -127 121 -72 O ATOM 678 CG2ATHR A 88 0.894 85.883 51.112 0.50 22.56 C ANISOU 678 CG2ATHR A 88 2739 3224 2610 -112 125 -87 C ATOM 679 CG2BTHR A 88 2.756 86.966 51.562 0.50 30.30 C ANISOU 679 CG2BTHR A 88 3718 4215 3580 -119 135 -92 C ATOM 680 N GLN A 89 2.805 84.503 47.854 1.00 29.27 N ANISOU 680 N GLN A 89 3649 4099 3372 -115 144 -107 N ATOM 681 CA GLN A 89 2.317 83.765 46.688 1.00 31.71 C ANISOU 681 CA GLN A 89 4006 4401 3640 -124 130 -123 C ATOM 682 C GLN A 89 2.893 82.355 46.662 1.00 32.71 C ANISOU 682 C GLN A 89 4154 4512 3762 -99 154 -159 C ATOM 683 O GLN A 89 2.183 81.394 46.335 1.00 29.94 O ANISOU 683 O GLN A 89 3844 4132 3402 -109 128 -180 O ATOM 684 CB GLN A 89 2.664 84.485 45.381 1.00 28.92 C ANISOU 684 CB GLN A 89 3690 4069 3230 -141 143 -112 C ATOM 685 CG GLN A 89 1.751 84.041 44.196 1.00 34.41 C ANISOU 685 CG GLN A 89 4449 4756 3868 -163 98 -120 C ATOM 686 CD GLN A 89 0.292 84.348 44.488 1.00 34.75 C ANISOU 686 CD GLN A 89 4467 4784 3951 -178 23 -95 C ATOM 687 OE1 GLN A 89 -0.025 85.389 45.098 1.00 33.57 O ANISOU 687 OE1 GLN A 89 4274 4634 3849 -171 14 -62 O ATOM 688 NE2 GLN A 89 -0.606 83.436 44.108 1.00 32.96 N ANISOU 688 NE2 GLN A 89 4263 4543 3716 -198 -28 -114 N ATOM 689 N SER A 90 4.181 82.207 47.002 1.00 27.56 N ANISOU 689 N SER A 90 3474 3874 3126 -67 198 -167 N ATOM 690 CA SER A 90 4.751 80.864 47.107 1.00 29.44 C ANISOU 690 CA SER A 90 3725 4084 3378 -25 218 -199 C ATOM 691 C SER A 90 3.998 80.024 48.146 1.00 33.11 C ANISOU 691 C SER A 90 4200 4503 3876 -25 177 -190 C ATOM 692 O SER A 90 3.741 78.828 47.925 1.00 30.40 O ANISOU 692 O SER A 90 3905 4110 3534 -16 170 -215 O ATOM 693 CB SER A 90 6.247 80.950 47.439 1.00 34.33 C ANISOU 693 CB SER A 90 4284 4731 4029 17 261 -199 C ATOM 694 OG SER A 90 6.802 79.640 47.615 1.00 37.12 O ANISOU 694 OG SER A 90 4644 5048 4411 75 274 -225 O ATOM 695 N SER A 91 3.607 80.636 49.273 1.00 28.50 N ANISOU 695 N SER A 91 3580 3931 3316 -42 155 -156 N ATOM 696 CA SER A 91 2.834 79.906 50.286 1.00 25.97 C ANISOU 696 CA SER A 91 3274 3575 3017 -54 131 -139 C ATOM 697 C SER A 91 1.512 79.404 49.710 1.00 31.00 C ANISOU 697 C SER A 91 3943 4185 3652 -96 109 -147 C ATOM 698 O SER A 91 1.104 78.270 49.961 1.00 29.78 O ANISOU 698 O SER A 91 3822 3980 3511 -108 97 -148 O ATOM 699 CB SER A 91 2.556 80.798 51.526 1.00 28.91 C ANISOU 699 CB SER A 91 3614 3974 3397 -68 126 -109 C ATOM 700 OG SER A 91 3.790 81.196 52.135 1.00 30.67 O ANISOU 700 OG SER A 91 3811 4220 3623 -41 128 -103 O ATOM 701 N ILE A 92 0.816 80.257 48.963 1.00 30.11 N ANISOU 701 N ILE A 92 3817 4098 3524 -124 94 -146 N ATOM 702 CA ILE A 92 -0.475 79.890 48.404 1.00 29.42 C ANISOU 702 CA ILE A 92 3742 3994 3442 -169 53 -149 C ATOM 703 C ILE A 92 -0.335 78.699 47.458 1.00 34.01 C ANISOU 703 C ILE A 92 4394 4531 3996 -178 38 -190 C ATOM 704 O ILE A 92 -1.137 77.755 47.503 1.00 35.48 O ANISOU 704 O ILE A 92 4604 4675 4204 -218 8 -196 O ATOM 705 CB ILE A 92 -1.087 81.114 47.698 1.00 32.12 C ANISOU 705 CB ILE A 92 4057 4373 3774 -184 26 -135 C ATOM 706 CG1 ILE A 92 -1.688 82.044 48.777 1.00 37.22 C ANISOU 706 CG1 ILE A 92 4638 5039 4467 -179 38 -103 C ATOM 707 CG2 ILE A 92 -2.135 80.670 46.689 1.00 35.26 C ANISOU 707 CG2 ILE A 92 4475 4759 4161 -228 -36 -145 C ATOM 708 CD1 ILE A 92 -1.889 83.478 48.309 1.00 39.46 C ANISOU 708 CD1 ILE A 92 4897 5345 4749 -168 23 -85 C ATOM 709 N PHE A 93 0.697 78.717 46.608 1.00 29.37 N ANISOU 709 N PHE A 93 3844 3951 3362 -143 67 -222 N ATOM 710 CA PHE A 93 0.946 77.601 45.686 1.00 35.25 C ANISOU 710 CA PHE A 93 4673 4650 4072 -139 68 -276 C ATOM 711 C PHE A 93 1.260 76.298 46.436 1.00 40.14 C ANISOU 711 C PHE A 93 5318 5198 4736 -113 80 -288 C ATOM 712 O PHE A 93 0.775 75.221 46.062 1.00 32.46 O ANISOU 712 O PHE A 93 4414 4158 3762 -140 52 -321 O ATOM 713 CB PHE A 93 2.103 77.951 44.760 1.00 36.22 C ANISOU 713 CB PHE A 93 4820 4803 4137 -97 125 -306 C ATOM 714 CG PHE A 93 1.735 78.911 43.638 1.00 41.84 C ANISOU 714 CG PHE A 93 5555 5563 4778 -133 106 -300 C ATOM 715 CD1 PHE A 93 0.481 78.876 43.048 1.00 48.73 C ANISOU 715 CD1 PHE A 93 6463 6427 5625 -192 26 -299 C ATOM 716 CD2 PHE A 93 2.652 79.850 43.186 1.00 36.79 C ANISOU 716 CD2 PHE A 93 4901 4976 4102 -114 162 -288 C ATOM 717 CE1 PHE A 93 0.160 79.765 41.996 1.00 60.00 C ANISOU 717 CE1 PHE A 93 7921 7895 6980 -220 -6 -282 C ATOM 718 CE2 PHE A 93 2.335 80.759 42.148 1.00 36.21 C ANISOU 718 CE2 PHE A 93 4865 4939 3955 -150 142 -268 C ATOM 719 CZ PHE A 93 1.108 80.710 41.548 1.00 45.69 C ANISOU 719 CZ PHE A 93 6112 6128 5120 -197 55 -264 C ATOM 720 N SER A 94 2.098 76.367 47.473 1.00 29.79 N ANISOU 720 N SER A 94 3962 3894 3462 -64 111 -260 N ATOM 721 CA SER A 94 2.358 75.180 48.292 1.00 31.65 C ANISOU 721 CA SER A 94 4226 4057 3742 -36 109 -253 C ATOM 722 C SER A 94 1.075 74.663 48.941 1.00 34.34 C ANISOU 722 C SER A 94 4583 4357 4109 -107 68 -221 C ATOM 723 O SER A 94 0.821 73.454 48.951 1.00 34.90 O ANISOU 723 O SER A 94 4720 4341 4201 -122 51 -233 O ATOM 724 CB SER A 94 3.411 75.489 49.372 1.00 33.48 C ANISOU 724 CB SER A 94 4402 4316 4004 22 127 -215 C ATOM 725 OG SER A 94 4.670 75.635 48.765 1.00 35.05 O ANISOU 725 OG SER A 94 4579 4539 4200 88 169 -247 O ATOM 726 N LEU A 95 0.267 75.564 49.532 1.00 32.60 N ANISOU 726 N LEU A 95 4300 4192 3895 -151 59 -179 N ATOM 727 CA LEU A 95 -0.980 75.114 50.135 1.00 31.07 C ANISOU 727 CA LEU A 95 4101 3972 3733 -222 38 -146 C ATOM 728 C LEU A 95 -1.872 74.447 49.096 1.00 34.71 C ANISOU 728 C LEU A 95 4602 4389 4196 -286 -6 -181 C ATOM 729 O LEU A 95 -2.502 73.430 49.379 1.00 31.06 O ANISOU 729 O LEU A 95 4174 3860 3766 -340 -25 -171 O ATOM 730 CB LEU A 95 -1.724 76.275 50.804 1.00 30.71 C ANISOU 730 CB LEU A 95 3973 3999 3696 -248 51 -108 C ATOM 731 CG LEU A 95 -0.988 76.849 52.033 1.00 33.15 C ANISOU 731 CG LEU A 95 4260 4340 3995 -204 86 -76 C ATOM 732 CD1 LEU A 95 -1.654 78.127 52.507 1.00 33.60 C ANISOU 732 CD1 LEU A 95 4250 4462 4054 -217 106 -59 C ATOM 733 CD2 LEU A 95 -0.972 75.788 53.149 1.00 31.65 C ANISOU 733 CD2 LEU A 95 4115 4097 3814 -216 94 -36 C ATOM 734 N LEU A 96 -1.965 75.020 47.897 1.00 30.14 N ANISOU 734 N LEU A 96 4025 3847 3579 -289 -30 -218 N ATOM 735 CA LEU A 96 -2.838 74.422 46.883 1.00 31.55 C ANISOU 735 CA LEU A 96 4250 3990 3748 -358 -92 -255 C ATOM 736 C LEU A 96 -2.319 73.059 46.424 1.00 31.13 C ANISOU 736 C LEU A 96 4311 3837 3681 -349 -94 -310 C ATOM 737 O LEU A 96 -3.110 72.143 46.133 1.00 35.70 O ANISOU 737 O LEU A 96 4939 4347 4278 -424 -145 -330 O ATOM 738 CB LEU A 96 -2.974 75.386 45.689 1.00 37.70 C ANISOU 738 CB LEU A 96 5023 4832 4470 -359 -125 -275 C ATOM 739 CG LEU A 96 -3.796 74.966 44.458 1.00 40.92 C ANISOU 739 CG LEU A 96 5487 5220 4842 -429 -209 -316 C ATOM 740 CD1 LEU A 96 -5.211 74.623 44.857 1.00 37.79 C ANISOU 740 CD1 LEU A 96 5028 4811 4519 -519 -273 -284 C ATOM 741 CD2 LEU A 96 -3.811 76.111 43.405 1.00 39.93 C ANISOU 741 CD2 LEU A 96 5360 5167 4646 -419 -241 -315 C ATOM 742 N ALA A 97 -0.997 72.910 46.310 1.00 31.67 N ANISOU 742 N ALA A 97 4420 3890 3723 -260 -40 -340 N ATOM 743 CA ALA A 97 -0.437 71.629 45.882 1.00 33.67 C ANISOU 743 CA ALA A 97 4783 4038 3972 -230 -31 -400 C ATOM 744 C ALA A 97 -0.728 70.544 46.913 1.00 41.81 C ANISOU 744 C ALA A 97 5841 4973 5073 -253 -44 -364 C ATOM 745 O ALA A 97 -1.017 69.401 46.552 1.00 37.52 O ANISOU 745 O ALA A 97 5395 4320 4542 -288 -74 -404 O ATOM 746 CB ALA A 97 1.072 71.755 45.682 1.00 31.07 C ANISOU 746 CB ALA A 97 4460 3723 3622 -115 42 -430 C ATOM 747 N ILE A 98 -0.624 70.892 48.203 1.00 37.83 N ANISOU 747 N ILE A 98 5266 4501 4608 -238 -23 -287 N ATOM 748 CA ILE A 98 -0.904 69.940 49.279 1.00 36.27 C ANISOU 748 CA ILE A 98 5101 4218 4463 -266 -31 -234 C ATOM 749 C ILE A 98 -2.344 69.461 49.194 1.00 37.44 C ANISOU 749 C ILE A 98 5259 4328 4638 -395 -76 -222 C ATOM 750 O ILE A 98 -2.616 68.258 49.300 1.00 37.94 O ANISOU 750 O ILE A 98 5406 4272 4736 -440 -99 -223 O ATOM 751 CB ILE A 98 -0.599 70.576 50.649 1.00 35.17 C ANISOU 751 CB ILE A 98 4889 4141 4332 -236 -2 -154 C ATOM 752 CG1 ILE A 98 0.907 70.739 50.818 1.00 35.03 C ANISOU 752 CG1 ILE A 98 4866 4136 4307 -115 25 -162 C ATOM 753 CG2 ILE A 98 -1.194 69.710 51.803 1.00 37.51 C ANISOU 753 CG2 ILE A 98 5222 4366 4665 -295 -8 -82 C ATOM 754 CD1 ILE A 98 1.327 71.644 52.008 1.00 35.90 C ANISOU 754 CD1 ILE A 98 4902 4330 4408 -87 39 -98 C ATOM 755 N ALA A 99 -3.290 70.388 48.967 1.00 34.93 N ANISOU 755 N ALA A 99 4852 4106 4315 -458 -94 -210 N ATOM 756 CA ALA A 99 -4.692 69.991 48.862 1.00 33.70 C ANISOU 756 CA ALA A 99 4676 3929 4201 -584 -142 -196 C ATOM 757 C ALA A 99 -4.907 69.032 47.699 1.00 38.22 C ANISOU 757 C ALA A 99 5352 4406 4763 -635 -206 -271 C ATOM 758 O ALA A 99 -5.603 68.019 47.842 1.00 37.28 O ANISOU 758 O ALA A 99 5278 4194 4692 -730 -241 -263 O ATOM 759 CB ALA A 99 -5.579 71.231 48.707 1.00 33.45 C ANISOU 759 CB ALA A 99 4516 4018 4174 -619 -156 -175 C ATOM 760 N ILE A 100 -4.295 69.324 46.543 1.00 34.36 N ANISOU 760 N ILE A 100 4914 3935 4205 -579 -219 -346 N ATOM 761 CA ILE A 100 -4.477 68.484 45.360 1.00 40.20 C ANISOU 761 CA ILE A 100 5772 4589 4911 -626 -279 -433 C ATOM 762 C ILE A 100 -3.829 67.118 45.564 1.00 40.53 C ANISOU 762 C ILE A 100 5944 4477 4977 -594 -258 -467 C ATOM 763 O ILE A 100 -4.353 66.096 45.123 1.00 40.20 O ANISOU 763 O ILE A 100 6001 4323 4951 -675 -314 -513 O ATOM 764 CB ILE A 100 -3.918 69.218 44.118 1.00 36.32 C ANISOU 764 CB ILE A 100 5313 4167 4321 -568 -279 -500 C ATOM 765 CG1 ILE A 100 -4.773 70.461 43.853 1.00 42.18 C ANISOU 765 CG1 ILE A 100 5940 5036 5050 -615 -326 -459 C ATOM 766 CG2 ILE A 100 -3.928 68.314 42.848 1.00 37.82 C ANISOU 766 CG2 ILE A 100 5659 4265 4446 -602 -329 -608 C ATOM 767 CD1 ILE A 100 -4.222 71.382 42.763 1.00 43.35 C ANISOU 767 CD1 ILE A 100 6113 5263 5096 -560 -321 -497 C ATOM 768 N ASP A 101 -2.661 67.095 46.209 1.00 37.23 N ANISOU 768 N ASP A 101 5532 4047 4568 -473 -184 -447 N ATOM 769 CA ASP A 101 -1.984 65.852 46.545 1.00 40.11 C ANISOU 769 CA ASP A 101 6007 4262 4972 -420 -165 -463 C ATOM 770 C ASP A 101 -2.879 64.932 47.380 1.00 39.84 C ANISOU 770 C ASP A 101 6002 4124 5011 -530 -203 -400 C ATOM 771 O ASP A 101 -3.006 63.734 47.095 1.00 42.24 O ANISOU 771 O ASP A 101 6434 4274 5343 -567 -236 -442 O ATOM 772 CB ASP A 101 -0.691 66.199 47.298 1.00 35.33 C ANISOU 772 CB ASP A 101 5355 3692 4376 -278 -96 -424 C ATOM 773 CG ASP A 101 0.046 64.959 47.759 1.00 42.25 C ANISOU 773 CG ASP A 101 6332 4414 5308 -205 -84 -423 C ATOM 774 OD1 ASP A 101 0.690 64.324 46.902 1.00 40.13 O ANISOU 774 OD1 ASP A 101 6159 4060 5028 -134 -67 -516 O ATOM 775 OD2 ASP A 101 -0.081 64.592 48.945 1.00 43.55 O ANISOU 775 OD2 ASP A 101 6488 4535 5522 -220 -93 -331 O ATOM 776 N ARG A 102 -3.498 65.471 48.433 1.00 37.38 N ANISOU 776 N ARG A 102 5580 3891 4730 -584 -192 -299 N ATOM 777 CA ARG A 102 -4.365 64.644 49.279 1.00 36.38 C ANISOU 777 CA ARG A 102 5474 3678 4669 -699 -211 -227 C ATOM 778 C ARG A 102 -5.635 64.229 48.538 1.00 39.43 C ANISOU 778 C ARG A 102 5872 4029 5081 -855 -283 -262 C ATOM 779 O ARG A 102 -6.184 63.159 48.804 1.00 41.73 O ANISOU 779 O ARG A 102 6235 4191 5428 -956 -312 -241 O ATOM 780 CB ARG A 102 -4.703 65.397 50.575 1.00 40.79 C ANISOU 780 CB ARG A 102 5914 4346 5241 -715 -162 -117 C ATOM 781 CG ARG A 102 -3.449 65.721 51.467 1.00 41.45 C ANISOU 781 CG ARG A 102 5996 4455 5298 -576 -110 -72 C ATOM 782 CD ARG A 102 -2.812 64.416 51.990 1.00 42.96 C ANISOU 782 CD ARG A 102 6320 4482 5523 -537 -118 -41 C ATOM 783 NE ARG A 102 -1.928 63.776 51.004 1.00 44.56 N ANISOU 783 NE ARG A 102 6620 4582 5728 -444 -136 -137 N ATOM 784 CZ ARG A 102 -1.596 62.483 51.003 1.00 46.15 C ANISOU 784 CZ ARG A 102 6958 4604 5974 -422 -158 -147 C ATOM 785 NH1 ARG A 102 -2.095 61.662 51.917 1.00 43.74 N ANISOU 785 NH1 ARG A 102 6713 4194 5711 -501 -173 -57 N ATOM 786 NH2 ARG A 102 -0.771 62.001 50.089 1.00 40.26 N ANISOU 786 NH2 ARG A 102 6294 3775 5228 -322 -158 -246 N ATOM 787 N TYR A 103 -6.100 65.045 47.588 1.00 40.10 N ANISOU 787 N TYR A 103 5891 4219 5128 -882 -322 -314 N ATOM 788 CA TYR A 103 -7.267 64.665 46.802 1.00 40.42 C ANISOU 788 CA TYR A 103 5938 4231 5190 -1030 -414 -352 C ATOM 789 C TYR A 103 -6.950 63.494 45.876 1.00 43.51 C ANISOU 789 C TYR A 103 6515 4460 5559 -1045 -466 -456 C ATOM 790 O TYR A 103 -7.727 62.525 45.777 1.00 41.66 O ANISOU 790 O TYR A 103 6342 4109 5376 -1180 -530 -465 O ATOM 791 CB TYR A 103 -7.779 65.876 46.016 1.00 43.85 C ANISOU 791 CB TYR A 103 6261 4819 5582 -1040 -457 -374 C ATOM 792 CG TYR A 103 -8.925 65.524 45.109 1.00 51.22 C ANISOU 792 CG TYR A 103 7198 5731 6531 -1187 -576 -416 C ATOM 793 CD1 TYR A 103 -10.183 65.275 45.629 1.00 53.55 C ANISOU 793 CD1 TYR A 103 7390 6032 6925 -1333 -614 -351 C ATOM 794 CD2 TYR A 103 -8.736 65.392 43.737 1.00 54.35 C ANISOU 794 CD2 TYR A 103 7707 6103 6842 -1187 -650 -522 C ATOM 795 CE1 TYR A 103 -11.234 64.930 44.809 1.00 54.18 C ANISOU 795 CE1 TYR A 103 7460 6094 7031 -1478 -738 -387 C ATOM 796 CE2 TYR A 103 -9.777 65.037 42.903 1.00 56.07 C ANISOU 796 CE2 TYR A 103 7940 6299 7067 -1330 -780 -563 C ATOM 797 CZ TYR A 103 -11.024 64.817 43.445 1.00 60.34 C ANISOU 797 CZ TYR A 103 8359 6847 7720 -1476 -830 -494 C ATOM 798 OH TYR A 103 -12.070 64.471 42.629 1.00 70.67 O ANISOU 798 OH TYR A 103 9665 8140 9048 -1628 -973 -532 O ATOM 799 N ILE A 104 -5.812 63.555 45.184 1.00 40.30 N ANISOU 799 N ILE A 104 6200 4037 5076 -912 -434 -539 N ATOM 800 CA ILE A 104 -5.421 62.418 44.348 1.00 43.12 C ANISOU 800 CA ILE A 104 6747 4229 5409 -905 -463 -649 C ATOM 801 C ILE A 104 -5.279 61.159 45.194 1.00 45.12 C ANISOU 801 C ILE A 104 7095 4300 5748 -920 -450 -612 C ATOM 802 O ILE A 104 -5.711 60.067 44.793 1.00 45.28 O ANISOU 802 O ILE A 104 7249 4160 5795 -1013 -511 -666 O ATOM 803 CB ILE A 104 -4.114 62.721 43.600 1.00 43.61 C ANISOU 803 CB ILE A 104 6875 4312 5381 -740 -398 -737 C ATOM 804 CG1 ILE A 104 -4.300 63.902 42.650 1.00 47.91 C ANISOU 804 CG1 ILE A 104 7355 5021 5829 -744 -419 -771 C ATOM 805 CG2 ILE A 104 -3.593 61.431 42.891 1.00 44.11 C ANISOU 805 CG2 ILE A 104 7147 4183 5429 -707 -402 -857 C ATOM 806 CD1 ILE A 104 -2.982 64.528 42.222 1.00 50.38 C ANISOU 806 CD1 ILE A 104 7675 5403 6065 -582 -324 -815 C ATOM 807 N ALA A 105 -4.678 61.293 46.383 1.00 42.40 N ANISOU 807 N ALA A 105 6694 3970 5444 -832 -377 -515 N ATOM 808 CA ALA A 105 -4.456 60.134 47.257 1.00 46.09 C ANISOU 808 CA ALA A 105 7261 4263 5987 -831 -367 -460 C ATOM 809 C ALA A 105 -5.766 59.468 47.689 1.00 46.70 C ANISOU 809 C ALA A 105 7344 4264 6136 -1031 -423 -397 C ATOM 810 O ALA A 105 -5.839 58.238 47.809 1.00 51.55 O ANISOU 810 O ALA A 105 8100 4681 6804 -1082 -451 -401 O ATOM 811 CB ALA A 105 -3.639 60.565 48.476 1.00 45.29 C ANISOU 811 CB ALA A 105 7086 4223 5900 -710 -294 -355 C ATOM 812 N ILE A 106 -6.816 60.243 47.947 1.00 43.73 N ANISOU 812 N ILE A 106 6811 4033 5771 -1146 -436 -335 N ATOM 813 CA ILE A 106 -8.043 59.584 48.391 1.00 49.35 C ANISOU 813 CA ILE A 106 7509 4677 6563 -1341 -477 -270 C ATOM 814 C ILE A 106 -8.915 59.131 47.229 1.00 54.32 C ANISOU 814 C ILE A 106 8188 5249 7203 -1487 -586 -365 C ATOM 815 O ILE A 106 -9.747 58.229 47.404 1.00 53.45 O ANISOU 815 O ILE A 106 8121 5019 7169 -1652 -635 -337 O ATOM 816 CB ILE A 106 -8.873 60.478 49.329 1.00 56.20 C ANISOU 816 CB ILE A 106 8180 5713 7460 -1411 -431 -153 C ATOM 817 CG1 ILE A 106 -9.869 59.621 50.129 1.00 57.07 C ANISOU 817 CG1 ILE A 106 8290 5732 7661 -1591 -431 -57 C ATOM 818 CG2 ILE A 106 -9.588 61.577 48.538 1.00 49.67 C ANISOU 818 CG2 ILE A 106 7203 5060 6611 -1448 -474 -196 C ATOM 819 CD1 ILE A 106 -10.225 60.220 51.462 1.00 57.94 C ANISOU 819 CD1 ILE A 106 8266 5963 7787 -1607 -336 76 C ATOM 820 N ARG A 107 -8.733 59.709 46.046 1.00 52.44 N ANISOU 820 N ARG A 107 7952 5086 6885 -1438 -630 -473 N ATOM 821 CA ARG A 107 -9.600 59.451 44.907 1.00 56.01 C ANISOU 821 CA ARG A 107 8441 5515 7327 -1578 -751 -561 C ATOM 822 C ARG A 107 -9.095 58.289 44.066 1.00 60.55 C ANISOU 822 C ARG A 107 9254 5883 7868 -1571 -796 -690 C ATOM 823 O ARG A 107 -9.884 57.425 43.654 1.00 63.03 O ANISOU 823 O ARG A 107 9653 6072 8223 -1736 -894 -732 O ATOM 824 CB ARG A 107 -9.717 60.726 44.055 1.00 60.33 C ANISOU 824 CB ARG A 107 8879 6255 7788 -1535 -783 -603 C ATOM 825 CG ARG A 107 -10.920 60.748 43.144 1.00 74.56 C ANISOU 825 CG ARG A 107 10645 8090 9595 -1704 -925 -646 C ATOM 826 CD ARG A 107 -12.207 60.818 43.949 1.00 79.11 C ANISOU 826 CD ARG A 107 11038 8722 10298 -1864 -950 -531 C ATOM 827 NE ARG A 107 -13.382 60.721 43.090 1.00 79.88 N ANISOU 827 NE ARG A 107 11089 8840 10421 -2038 -1104 -570 N ATOM 828 N ILE A 108 -7.793 58.238 43.812 1.00 58.26 N ANISOU 828 N ILE A 108 9074 5550 7512 -1383 -724 -756 N ATOM 829 CA ILE A 108 -7.220 57.142 43.033 1.00 56.82 C ANISOU 829 CA ILE A 108 9125 5165 7299 -1348 -745 -889 C ATOM 830 C ILE A 108 -5.982 56.616 43.745 1.00 53.52 C ANISOU 830 C ILE A 108 8787 4631 6915 -1170 -641 -866 C ATOM 831 O ILE A 108 -4.868 56.684 43.199 1.00 52.24 O ANISOU 831 O ILE A 108 8701 4458 6688 -998 -579 -956 O ATOM 832 CB ILE A 108 -6.906 57.579 41.592 1.00 62.42 C ANISOU 832 CB ILE A 108 9907 5938 7872 -1296 -773 -1035 C ATOM 833 CG1 ILE A 108 -6.184 58.928 41.567 1.00 63.22 C ANISOU 833 CG1 ILE A 108 9872 6250 7898 -1143 -687 -1006 C ATOM 834 CG2 ILE A 108 -8.184 57.627 40.766 1.00 60.50 C ANISOU 834 CG2 ILE A 108 9655 5729 7602 -1497 -919 -1078 C ATOM 835 CD1 ILE A 108 -5.615 59.277 40.197 1.00 68.26 C ANISOU 835 CD1 ILE A 108 10611 6935 8390 -1066 -681 -1145 C ATOM 836 N PRO A 109 -6.139 56.056 44.946 1.00 56.38 N ANISOU 836 N PRO A 109 9138 4904 7381 -1208 -622 -745 N ATOM 837 CA PRO A 109 -4.965 55.604 45.715 1.00 56.44 C ANISOU 837 CA PRO A 109 9209 4809 7425 -1033 -541 -701 C ATOM 838 C PRO A 109 -4.072 54.601 44.980 1.00 60.37 C ANISOU 838 C PRO A 109 9922 5100 7917 -915 -532 -837 C ATOM 839 O PRO A 109 -2.857 54.570 45.220 1.00 57.05 O ANISOU 839 O PRO A 109 9520 4655 7500 -714 -455 -841 O ATOM 840 CB PRO A 109 -5.602 54.978 46.970 1.00 57.74 C ANISOU 840 CB PRO A 109 9366 4880 7692 -1153 -553 -552 C ATOM 841 CG PRO A 109 -6.977 54.580 46.535 1.00 59.10 C ANISOU 841 CG PRO A 109 9553 5008 7896 -1393 -647 -572 C ATOM 842 CD PRO A 109 -7.410 55.645 45.570 1.00 58.46 C ANISOU 842 CD PRO A 109 9354 5126 7732 -1423 -682 -648 C ATOM 843 N LEU A 110 -4.635 53.768 44.103 1.00 62.55 N ANISOU 843 N LEU A 110 10358 5221 8187 -1033 -608 -950 N ATOM 844 CA LEU A 110 -3.811 52.803 43.385 1.00 70.17 C ANISOU 844 CA LEU A 110 11541 5978 9142 -915 -590 -1094 C ATOM 845 C LEU A 110 -2.901 53.474 42.366 1.00 68.99 C ANISOU 845 C LEU A 110 11392 5946 8876 -749 -520 -1225 C ATOM 846 O LEU A 110 -1.826 52.949 42.058 1.00 72.87 O ANISOU 846 O LEU A 110 12001 6319 9368 -571 -448 -1315 O ATOM 847 CB LEU A 110 -4.696 51.772 42.687 1.00 77.00 C ANISOU 847 CB LEU A 110 12591 6645 10020 -1101 -697 -1193 C ATOM 848 CG LEU A 110 -5.638 51.005 43.610 1.00 83.43 C ANISOU 848 CG LEU A 110 13421 7322 10957 -1291 -764 -1068 C ATOM 849 CD1 LEU A 110 -6.439 49.959 42.832 1.00 87.60 C ANISOU 849 CD1 LEU A 110 14143 7639 11501 -1479 -877 -1182 C ATOM 850 CD2 LEU A 110 -4.851 50.370 44.754 1.00 83.88 C ANISOU 850 CD2 LEU A 110 13525 7233 11111 -1160 -699 -957 C ATOM 851 N ARG A 111 -3.321 54.603 41.810 1.00 62.63 N ANISOU 851 N ARG A 111 10459 5365 7973 -805 -536 -1237 N ATOM 852 CA ARG A 111 -2.525 55.330 40.833 1.00 65.35 C ANISOU 852 CA ARG A 111 10800 5837 8194 -669 -465 -1345 C ATOM 853 C ARG A 111 -1.596 56.363 41.458 1.00 61.16 C ANISOU 853 C ARG A 111 10086 5487 7665 -503 -359 -1254 C ATOM 854 O ARG A 111 -0.759 56.926 40.742 1.00 57.06 O ANISOU 854 O ARG A 111 9557 5064 7057 -374 -279 -1332 O ATOM 855 CB ARG A 111 -3.442 56.033 39.823 1.00 71.60 C ANISOU 855 CB ARG A 111 11568 6769 8868 -816 -550 -1402 C ATOM 856 CG ARG A 111 -4.015 55.082 38.776 1.00 86.43 C ANISOU 856 CG ARG A 111 13668 8479 10693 -940 -645 -1553 C ATOM 857 CD ARG A 111 -5.381 55.529 38.290 1.00 93.44 C ANISOU 857 CD ARG A 111 14497 9471 11534 -1160 -790 -1541 C ATOM 858 NE ARG A 111 -6.181 54.394 37.840 1.00 99.17 N ANISOU 858 NE ARG A 111 15402 9997 12281 -1333 -914 -1628 N ATOM 859 CZ ARG A 111 -6.823 53.560 38.656 1.00102.24 C ANISOU 859 CZ ARG A 111 15799 10236 12811 -1460 -970 -1552 C ATOM 860 NH1 ARG A 111 -6.761 53.724 39.974 1.00 98.27 N ANISOU 860 NH1 ARG A 111 15143 9766 12430 -1428 -910 -1387 N ATOM 861 NH2 ARG A 111 -7.526 52.553 38.153 1.00108.34 N ANISOU 861 NH2 ARG A 111 16717 10845 13603 -1615 -1078 -1632 N ATOM 862 N TYR A 112 -1.713 56.613 42.765 1.00 54.64 N ANISOU 862 N TYR A 112 9121 4707 6931 -511 -356 -1092 N ATOM 863 CA TYR A 112 -1.050 57.770 43.357 1.00 56.94 C ANISOU 863 CA TYR A 112 9225 5198 7212 -396 -282 -1002 C ATOM 864 C TYR A 112 0.461 57.706 43.157 1.00 59.38 C ANISOU 864 C TYR A 112 9557 5487 7517 -171 -175 -1062 C ATOM 865 O TYR A 112 1.075 58.654 42.651 1.00 58.32 O ANISOU 865 O TYR A 112 9336 5514 7308 -85 -108 -1096 O ATOM 866 CB TYR A 112 -1.406 57.878 44.845 1.00 52.84 C ANISOU 866 CB TYR A 112 8590 4702 6784 -443 -296 -829 C ATOM 867 CG TYR A 112 -0.648 58.964 45.578 1.00 48.05 C ANISOU 867 CG TYR A 112 7812 4273 6172 -322 -228 -739 C ATOM 868 CD1 TYR A 112 -1.112 60.280 45.599 1.00 40.12 C ANISOU 868 CD1 TYR A 112 6648 3484 5113 -378 -228 -693 C ATOM 869 CD2 TYR A 112 0.544 58.682 46.235 1.00 54.87 C ANISOU 869 CD2 TYR A 112 8674 5084 7088 -152 -173 -702 C ATOM 870 CE1 TYR A 112 -0.408 61.283 46.261 1.00 45.17 C ANISOU 870 CE1 TYR A 112 7144 4273 5747 -276 -170 -620 C ATOM 871 CE2 TYR A 112 1.248 59.678 46.901 1.00 52.93 C ANISOU 871 CE2 TYR A 112 8273 5001 6838 -55 -125 -624 C ATOM 872 CZ TYR A 112 0.762 60.975 46.910 1.00 47.74 C ANISOU 872 CZ TYR A 112 7471 4548 6120 -123 -122 -587 C ATOM 873 OH TYR A 112 1.449 61.967 47.558 1.00 48.30 O ANISOU 873 OH TYR A 112 7401 4767 6184 -37 -80 -518 O ATOM 874 N ASN A 113 1.073 56.585 43.522 1.00 61.52 N ANISOU 874 N ASN A 113 9942 5558 7875 -73 -157 -1075 N ATOM 875 CA ASN A 113 2.529 56.517 43.538 1.00 73.35 C ANISOU 875 CA ASN A 113 11424 7042 9403 155 -57 -1108 C ATOM 876 C ASN A 113 3.133 56.583 42.137 1.00 73.97 C ANISOU 876 C ASN A 113 11582 7136 9386 244 23 -1283 C ATOM 877 O ASN A 113 4.269 57.044 41.981 1.00 77.75 O ANISOU 877 O ASN A 113 11976 7704 9860 411 126 -1306 O ATOM 878 CB ASN A 113 2.973 55.255 44.271 1.00 79.87 C ANISOU 878 CB ASN A 113 12358 7634 10356 243 -69 -1074 C ATOM 879 CG ASN A 113 2.758 55.364 45.765 1.00 80.93 C ANISOU 879 CG ASN A 113 12392 7790 10569 206 -118 -884 C ATOM 880 OD1 ASN A 113 2.949 56.433 46.344 1.00 76.51 O ANISOU 880 OD1 ASN A 113 11655 7428 9986 222 -99 -792 O ATOM 881 ND2 ASN A 113 2.350 54.267 46.395 1.00 85.59 N ANISOU 881 ND2 ASN A 113 13106 8171 11242 149 -179 -826 N ATOM 882 N GLY A 114 2.401 56.149 41.110 1.00 66.88 N ANISOU 882 N GLY A 114 10843 6160 8408 129 -21 -1405 N ATOM 883 CA GLY A 114 2.911 56.291 39.758 1.00 66.46 C ANISOU 883 CA GLY A 114 10879 6140 8234 199 59 -1570 C ATOM 884 C GLY A 114 2.660 57.648 39.139 1.00 67.13 C ANISOU 884 C GLY A 114 10850 6472 8184 134 70 -1563 C ATOM 885 O GLY A 114 3.285 57.993 38.130 1.00 72.71 O ANISOU 885 O GLY A 114 11596 7249 8782 213 163 -1672 O ATOM 886 N LEU A 115 1.753 58.423 39.713 1.00 60.27 N ANISOU 886 N LEU A 115 9848 5731 7321 -6 -17 -1438 N ATOM 887 CA LEU A 115 1.431 59.736 39.185 1.00 61.49 C ANISOU 887 CA LEU A 115 9895 6107 7362 -69 -22 -1417 C ATOM 888 C LEU A 115 2.248 60.820 39.879 1.00 61.21 C ANISOU 888 C LEU A 115 9655 6243 7359 41 60 -1311 C ATOM 889 O LEU A 115 2.842 61.681 39.217 1.00 58.62 O ANISOU 889 O LEU A 115 9277 6055 6942 102 139 -1344 O ATOM 890 CB LEU A 115 -0.067 59.995 39.358 1.00 67.41 C ANISOU 890 CB LEU A 115 10607 6897 8108 -279 -164 -1348 C ATOM 891 CG LEU A 115 -0.831 61.025 38.530 1.00 75.93 C ANISOU 891 CG LEU A 115 11643 8142 9063 -392 -227 -1355 C ATOM 892 CD1 LEU A 115 -2.306 60.892 38.849 1.00 79.52 C ANISOU 892 CD1 LEU A 115 12065 8582 9565 -589 -374 -1292 C ATOM 893 CD2 LEU A 115 -0.376 62.431 38.793 1.00 79.49 C ANISOU 893 CD2 LEU A 115 11911 8803 9490 -325 -163 -1266 C ATOM 894 N VAL A 116 2.278 60.789 41.210 1.00 57.12 N ANISOU 894 N VAL A 116 9026 5714 6964 58 40 -1182 N ATOM 895 CA VAL A 116 2.862 61.854 42.018 1.00 53.77 C ANISOU 895 CA VAL A 116 8407 5451 6572 128 86 -1069 C ATOM 896 C VAL A 116 4.208 61.350 42.517 1.00 54.85 C ANISOU 896 C VAL A 116 8524 5518 6797 315 170 -1068 C ATOM 897 O VAL A 116 4.284 60.652 43.523 1.00 61.87 O ANISOU 897 O VAL A 116 9419 6296 7793 344 135 -996 O ATOM 898 CB VAL A 116 1.941 62.253 43.170 1.00 53.36 C ANISOU 898 CB VAL A 116 8246 5451 6577 13 5 -927 C ATOM 899 CG1 VAL A 116 2.480 63.506 43.861 1.00 49.97 C ANISOU 899 CG1 VAL A 116 7632 5200 6154 71 48 -831 C ATOM 900 CG2 VAL A 116 0.528 62.474 42.656 1.00 55.02 C ANISOU 900 CG2 VAL A 116 8482 5694 6730 -170 -89 -937 C ATOM 901 N THR A 117 5.272 61.689 41.807 1.00 54.84 N ANISOU 901 N THR A 117 8499 5583 6755 442 279 -1143 N ATOM 902 CA THR A 117 6.611 61.230 42.141 1.00 53.55 C ANISOU 902 CA THR A 117 8298 5364 6686 634 364 -1154 C ATOM 903 C THR A 117 7.428 62.384 42.700 1.00 52.92 C ANISOU 903 C THR A 117 8008 5468 6630 701 412 -1063 C ATOM 904 O THR A 117 7.098 63.558 42.511 1.00 49.67 O ANISOU 904 O THR A 117 7509 5221 6140 617 410 -1027 O ATOM 905 CB THR A 117 7.326 60.668 40.916 1.00 54.80 C ANISOU 905 CB THR A 117 8574 5453 6796 743 475 -1316 C ATOM 906 OG1 THR A 117 7.497 61.722 39.953 1.00 55.54 O ANISOU 906 OG1 THR A 117 8622 5722 6759 719 550 -1364 O ATOM 907 CG2 THR A 117 6.514 59.518 40.293 1.00 56.96 C ANISOU 907 CG2 THR A 117 9077 5531 7033 667 420 -1424 C ATOM 908 N GLY A 118 8.524 62.030 43.368 1.00 53.10 N ANISOU 908 N GLY A 118 7955 5453 6769 857 450 -1028 N ATOM 909 CA GLY A 118 9.389 63.042 43.949 1.00 52.63 C ANISOU 909 CA GLY A 118 7695 5556 6747 921 483 -945 C ATOM 910 C GLY A 118 9.964 63.978 42.906 1.00 53.39 C ANISOU 910 C GLY A 118 7723 5806 6758 942 598 -1013 C ATOM 911 O GLY A 118 10.005 65.196 43.108 1.00 48.85 O ANISOU 911 O GLY A 118 7018 5396 6148 886 598 -946 O ATOM 912 N THR A 119 10.382 63.431 41.756 1.00 53.67 N ANISOU 912 N THR A 119 7859 5784 6750 1015 703 -1149 N ATOM 913 CA THR A 119 10.992 64.289 40.749 1.00 53.47 C ANISOU 913 CA THR A 119 7776 5905 6634 1035 830 -1209 C ATOM 914 C THR A 119 9.962 65.221 40.134 1.00 47.23 C ANISOU 914 C THR A 119 7033 5221 5691 862 789 -1202 C ATOM 915 O THR A 119 10.267 66.384 39.848 1.00 53.39 O ANISOU 915 O THR A 119 7708 6163 6414 832 840 -1168 O ATOM 916 CB THR A 119 11.691 63.463 39.665 1.00 65.17 C ANISOU 916 CB THR A 119 9366 7302 8093 1160 969 -1363 C ATOM 917 OG1 THR A 119 10.765 62.547 39.083 1.00 75.63 O ANISOU 917 OG1 THR A 119 10918 8473 9345 1094 919 -1458 O ATOM 918 CG2 THR A 119 12.835 62.695 40.258 1.00 59.17 C ANISOU 918 CG2 THR A 119 8522 6456 7503 1354 1019 -1362 C ATOM 919 N ARG A 120 8.730 64.747 39.947 1.00 45.57 N ANISOU 919 N ARG A 120 6973 4920 5421 743 687 -1225 N ATOM 920 CA ARG A 120 7.688 65.635 39.440 1.00 45.29 C ANISOU 920 CA ARG A 120 6964 4985 5258 583 624 -1204 C ATOM 921 C ARG A 120 7.353 66.714 40.458 1.00 47.69 C ANISOU 921 C ARG A 120 7105 5408 5608 515 551 -1060 C ATOM 922 O ARG A 120 7.157 67.879 40.091 1.00 50.44 O ANISOU 922 O ARG A 120 7394 5893 5875 447 557 -1026 O ATOM 923 CB ARG A 120 6.441 64.840 39.057 1.00 47.48 C ANISOU 923 CB ARG A 120 7420 5139 5483 467 518 -1259 C ATOM 924 CG ARG A 120 6.623 63.991 37.795 1.00 53.59 C ANISOU 924 CG ARG A 120 8388 5813 6161 502 585 -1422 C ATOM 925 CD ARG A 120 5.437 63.060 37.548 1.00 56.01 C ANISOU 925 CD ARG A 120 8872 5971 6438 384 462 -1477 C ATOM 926 NE ARG A 120 5.748 62.114 36.494 1.00 55.63 N ANISOU 926 NE ARG A 120 9023 5800 6316 438 530 -1643 N ATOM 927 CZ ARG A 120 4.990 61.085 36.133 1.00 56.87 C ANISOU 927 CZ ARG A 120 9369 5791 6449 362 447 -1730 C ATOM 928 NH1 ARG A 120 5.402 60.291 35.151 1.00 56.06 N ANISOU 928 NH1 ARG A 120 9454 5578 6269 426 526 -1894 N ATOM 929 NH2 ARG A 120 3.827 60.849 36.737 1.00 50.08 N ANISOU 929 NH2 ARG A 120 8512 4873 5642 218 292 -1658 N ATOM 930 N ALA A 121 7.305 66.354 41.747 1.00 44.09 N ANISOU 930 N ALA A 121 6584 4895 5274 534 485 -975 N ATOM 931 CA ALA A 121 7.029 67.349 42.780 1.00 43.27 C ANISOU 931 CA ALA A 121 6338 4898 5205 477 426 -848 C ATOM 932 C ALA A 121 8.113 68.414 42.820 1.00 44.89 C ANISOU 932 C ALA A 121 6392 5245 5418 542 506 -815 C ATOM 933 O ALA A 121 7.813 69.593 43.006 1.00 42.50 O ANISOU 933 O ALA A 121 6006 5062 5080 469 483 -751 O ATOM 934 CB ALA A 121 6.898 66.683 44.148 1.00 44.93 C ANISOU 934 CB ALA A 121 6526 5018 5529 493 352 -766 C ATOM 935 N LYS A 122 9.380 68.012 42.682 1.00 44.32 N ANISOU 935 N LYS A 122 6278 5158 5404 681 600 -857 N ATOM 936 CA LYS A 122 10.476 68.980 42.688 1.00 53.82 C ANISOU 936 CA LYS A 122 7323 6497 6628 736 681 -827 C ATOM 937 C LYS A 122 10.352 69.960 41.519 1.00 54.50 C ANISOU 937 C LYS A 122 7427 6696 6584 665 751 -863 C ATOM 938 O LYS A 122 10.603 71.163 41.680 1.00 43.28 O ANISOU 938 O LYS A 122 5893 5401 5152 623 762 -798 O ATOM 939 CB LYS A 122 11.828 68.258 42.642 1.00 59.16 C ANISOU 939 CB LYS A 122 7944 7132 7403 904 776 -874 C ATOM 940 CG LYS A 122 12.293 67.751 43.996 1.00 71.18 C ANISOU 940 CG LYS A 122 9379 8595 9069 984 701 -794 C ATOM 941 CD LYS A 122 13.087 66.447 43.902 1.00 81.85 C ANISOU 941 CD LYS A 122 10765 9814 10520 1148 750 -858 C ATOM 942 CE LYS A 122 13.145 65.745 45.265 1.00 87.33 C ANISOU 942 CE LYS A 122 11439 10408 11334 1201 633 -767 C ATOM 943 NZ LYS A 122 13.690 64.340 45.189 1.00 93.18 N ANISOU 943 NZ LYS A 122 12251 10978 12175 1356 658 -824 N ATOM 944 N GLY A 123 9.963 69.465 40.335 1.00 45.53 N ANISOU 944 N GLY A 123 6446 5511 5341 646 792 -964 N ATOM 945 CA GLY A 123 9.751 70.363 39.212 1.00 45.90 C ANISOU 945 CA GLY A 123 6536 5660 5243 569 842 -988 C ATOM 946 C GLY A 123 8.612 71.336 39.455 1.00 45.27 C ANISOU 946 C GLY A 123 6447 5642 5112 430 725 -904 C ATOM 947 O GLY A 123 8.704 72.510 39.099 1.00 44.71 O ANISOU 947 O GLY A 123 6322 5685 4980 379 751 -861 O ATOM 948 N ILE A 124 7.510 70.853 40.037 1.00 39.12 N ANISOU 948 N ILE A 124 5718 4783 4361 366 599 -880 N ATOM 949 CA ILE A 124 6.371 71.720 40.327 1.00 37.33 C ANISOU 949 CA ILE A 124 5466 4610 4106 246 491 -803 C ATOM 950 C ILE A 124 6.764 72.806 41.324 1.00 38.62 C ANISOU 950 C ILE A 124 5466 4866 4341 251 488 -700 C ATOM 951 O ILE A 124 6.355 73.967 41.195 1.00 41.66 O ANISOU 951 O ILE A 124 5811 5337 4681 182 462 -648 O ATOM 952 CB ILE A 124 5.187 70.884 40.849 1.00 40.55 C ANISOU 952 CB ILE A 124 5940 4914 4552 181 374 -796 C ATOM 953 CG1 ILE A 124 4.552 70.085 39.709 1.00 48.79 C ANISOU 953 CG1 ILE A 124 7156 5881 5501 133 348 -895 C ATOM 954 CG2 ILE A 124 4.151 71.779 41.463 1.00 41.85 C ANISOU 954 CG2 ILE A 124 6030 5140 4730 84 280 -704 C ATOM 955 CD1 ILE A 124 3.554 69.059 40.210 1.00 58.87 C ANISOU 955 CD1 ILE A 124 8499 7034 6835 71 245 -898 C ATOM 956 N ILE A 125 7.549 72.441 42.343 1.00 34.86 N ANISOU 956 N ILE A 125 4902 4366 3977 332 505 -671 N ATOM 957 CA ILE A 125 7.983 73.425 43.343 1.00 39.51 C ANISOU 957 CA ILE A 125 5347 5037 4630 333 491 -582 C ATOM 958 C ILE A 125 8.838 74.518 42.683 1.00 40.14 C ANISOU 958 C ILE A 125 5355 5229 4669 338 580 -578 C ATOM 959 O ILE A 125 8.629 75.709 42.925 1.00 35.78 O ANISOU 959 O ILE A 125 4740 4751 4102 275 553 -516 O ATOM 960 CB ILE A 125 8.718 72.718 44.500 1.00 38.56 C ANISOU 960 CB ILE A 125 5159 4865 4627 422 478 -553 C ATOM 961 CG1 ILE A 125 7.714 71.850 45.300 1.00 39.16 C ANISOU 961 CG1 ILE A 125 5307 4838 4735 387 383 -527 C ATOM 962 CG2 ILE A 125 9.425 73.750 45.411 1.00 35.62 C ANISOU 962 CG2 ILE A 125 4637 4586 4309 429 470 -476 C ATOM 963 CD1 ILE A 125 8.329 70.984 46.360 1.00 37.60 C ANISOU 963 CD1 ILE A 125 5082 4566 4638 471 357 -494 C ATOM 964 N ALA A 126 9.775 74.134 41.803 1.00 39.35 N ANISOU 964 N ALA A 126 5269 5135 4548 409 693 -646 N ATOM 965 CA ALA A 126 10.608 75.126 41.105 1.00 34.30 C ANISOU 965 CA ALA A 126 4564 4603 3866 403 796 -640 C ATOM 966 C ALA A 126 9.755 76.075 40.279 1.00 43.06 C ANISOU 966 C ALA A 126 5751 5762 4847 293 772 -621 C ATOM 967 O ALA A 126 9.958 77.300 40.296 1.00 40.67 O ANISOU 967 O ALA A 126 5378 5541 4532 242 783 -559 O ATOM 968 CB ALA A 126 11.614 74.418 40.205 1.00 37.39 C ANISOU 968 CB ALA A 126 4976 4987 4242 496 938 -728 C ATOM 969 N ILE A 127 8.797 75.517 39.526 1.00 40.44 N ANISOU 969 N ILE A 127 5569 5375 4420 254 732 -674 N ATOM 970 CA ILE A 127 7.931 76.340 38.695 1.00 41.50 C ANISOU 970 CA ILE A 127 5784 5552 4431 156 688 -652 C ATOM 971 C ILE A 127 7.117 77.294 39.556 1.00 39.48 C ANISOU 971 C ILE A 127 5456 5320 4223 89 576 -557 C ATOM 972 O ILE A 127 6.919 78.459 39.197 1.00 37.86 O ANISOU 972 O ILE A 127 5241 5177 3966 31 566 -503 O ATOM 973 CB ILE A 127 7.015 75.452 37.833 1.00 43.44 C ANISOU 973 CB ILE A 127 6200 5728 4576 123 638 -728 C ATOM 974 CG1 ILE A 127 7.828 74.779 36.728 1.00 49.28 C ANISOU 974 CG1 ILE A 127 7039 6459 5227 180 769 -831 C ATOM 975 CG2 ILE A 127 5.914 76.290 37.258 1.00 44.44 C ANISOU 975 CG2 ILE A 127 6387 5892 4605 19 542 -684 C ATOM 976 CD1 ILE A 127 7.073 73.643 35.999 1.00 54.18 C ANISOU 976 CD1 ILE A 127 7841 6984 5762 161 721 -931 C ATOM 977 N CYS A 128 6.604 76.807 40.685 1.00 36.49 N ANISOU 977 N CYS A 128 5037 4887 3942 96 496 -536 N ATOM 978 CA CYS A 128 5.806 77.660 41.560 1.00 33.97 C ANISOU 978 CA CYS A 128 4650 4587 3667 41 406 -457 C ATOM 979 C CYS A 128 6.629 78.823 42.138 1.00 36.40 C ANISOU 979 C CYS A 128 4842 4965 4023 49 444 -396 C ATOM 980 O CYS A 128 6.115 79.932 42.329 1.00 38.80 O ANISOU 980 O CYS A 128 5117 5303 4321 -4 399 -339 O ATOM 981 CB CYS A 128 5.200 76.799 42.665 1.00 38.89 C ANISOU 981 CB CYS A 128 5261 5140 4375 49 336 -449 C ATOM 982 SG CYS A 128 3.795 75.837 42.025 1.00 44.44 S ANISOU 982 SG CYS A 128 6090 5767 5027 -14 252 -496 S ATOM 983 N TRP A 129 7.898 78.581 42.450 1.00 36.53 N ANISOU 983 N TRP A 129 4786 4998 4096 115 520 -408 N ATOM 984 CA TRP A 129 8.738 79.667 42.943 1.00 39.30 C ANISOU 984 CA TRP A 129 5023 5414 4494 108 549 -355 C ATOM 985 C TRP A 129 9.009 80.698 41.844 1.00 38.83 C ANISOU 985 C TRP A 129 4984 5418 4353 58 613 -340 C ATOM 986 O TRP A 129 8.968 81.901 42.104 1.00 36.08 O ANISOU 986 O TRP A 129 4592 5104 4014 5 590 -280 O ATOM 987 CB TRP A 129 10.046 79.104 43.491 1.00 36.72 C ANISOU 987 CB TRP A 129 4599 5096 4258 189 605 -370 C ATOM 988 CG TRP A 129 9.937 78.721 44.945 1.00 37.33 C ANISOU 988 CG TRP A 129 4624 5135 4425 216 521 -339 C ATOM 989 CD1 TRP A 129 9.811 77.468 45.459 1.00 39.12 C ANISOU 989 CD1 TRP A 129 4881 5288 4694 274 489 -361 C ATOM 990 CD2 TRP A 129 9.947 79.621 46.065 1.00 34.78 C ANISOU 990 CD2 TRP A 129 4226 4842 4147 179 459 -278 C ATOM 991 NE1 TRP A 129 9.746 77.526 46.842 1.00 40.89 N ANISOU 991 NE1 TRP A 129 5055 5502 4981 275 411 -309 N ATOM 992 CE2 TRP A 129 9.820 78.836 47.237 1.00 35.99 C ANISOU 992 CE2 TRP A 129 4371 4947 4358 217 392 -264 C ATOM 993 CE3 TRP A 129 10.045 81.008 46.190 1.00 36.09 C ANISOU 993 CE3 TRP A 129 4345 5062 4307 114 452 -236 C ATOM 994 CZ2 TRP A 129 9.820 79.393 48.534 1.00 37.60 C ANISOU 994 CZ2 TRP A 129 4524 5166 4598 193 323 -214 C ATOM 995 CZ3 TRP A 129 10.029 81.568 47.492 1.00 33.05 C ANISOU 995 CZ3 TRP A 129 3908 4682 3969 93 380 -195 C ATOM 996 CH2 TRP A 129 9.932 80.744 48.637 1.00 38.53 C ANISOU 996 CH2 TRP A 129 4597 5338 4705 133 319 -187 C ATOM 997 N VAL A 130 9.237 80.251 40.604 1.00 37.63 N ANISOU 997 N VAL A 130 4913 5273 4110 69 691 -392 N ATOM 998 CA VAL A 130 9.435 81.199 39.499 1.00 38.47 C ANISOU 998 CA VAL A 130 5063 5438 4115 13 754 -368 C ATOM 999 C VAL A 130 8.182 82.043 39.288 1.00 38.02 C ANISOU 999 C VAL A 130 5077 5371 3998 -65 648 -315 C ATOM 1000 O VAL A 130 8.256 83.277 39.167 1.00 38.93 O ANISOU 1000 O VAL A 130 5172 5520 4098 -118 647 -249 O ATOM 1001 CB VAL A 130 9.823 80.468 38.196 1.00 42.64 C ANISOU 1001 CB VAL A 130 5693 5974 4534 40 862 -443 C ATOM 1002 CG1 VAL A 130 9.920 81.492 37.046 1.00 49.66 C ANISOU 1002 CG1 VAL A 130 6649 6925 5295 -33 921 -405 C ATOM 1003 CG2 VAL A 130 11.152 79.741 38.331 1.00 41.18 C ANISOU 1003 CG2 VAL A 130 5419 5804 4423 130 987 -495 C ATOM 1004 N LEU A 131 7.005 81.389 39.231 1.00 32.20 N ANISOU 1004 N LEU A 131 4421 4582 3232 -72 553 -341 N ATOM 1005 CA LEU A 131 5.755 82.128 39.065 1.00 37.33 C ANISOU 1005 CA LEU A 131 5117 5223 3845 -134 442 -290 C ATOM 1006 C LEU A 131 5.521 83.116 40.211 1.00 40.18 C ANISOU 1006 C LEU A 131 5376 5585 4308 -147 388 -222 C ATOM 1007 O LEU A 131 4.936 84.183 40.002 1.00 37.81 O ANISOU 1007 O LEU A 131 5089 5291 3986 -190 336 -163 O ATOM 1008 CB LEU A 131 4.576 81.161 38.974 1.00 36.05 C ANISOU 1008 CB LEU A 131 5025 5008 3666 -143 346 -331 C ATOM 1009 CG LEU A 131 4.611 80.176 37.799 1.00 47.89 C ANISOU 1009 CG LEU A 131 6655 6489 5050 -141 376 -411 C ATOM 1010 CD1 LEU A 131 3.414 79.222 37.887 1.00 47.53 C ANISOU 1010 CD1 LEU A 131 6666 6381 5014 -165 264 -448 C ATOM 1011 CD2 LEU A 131 4.579 80.941 36.505 1.00 49.90 C ANISOU 1011 CD2 LEU A 131 7008 6792 5161 -190 389 -388 C ATOM 1012 N SER A 132 5.905 82.742 41.438 1.00 35.43 N ANISOU 1012 N SER A 132 4682 4968 3811 -108 392 -230 N ATOM 1013 CA SER A 132 5.719 83.611 42.600 1.00 31.73 C ANISOU 1013 CA SER A 132 4132 4497 3426 -119 347 -179 C ATOM 1014 C SER A 132 6.521 84.900 42.470 1.00 32.60 C ANISOU 1014 C SER A 132 4204 4646 3539 -150 391 -133 C ATOM 1015 O SER A 132 6.047 85.976 42.857 1.00 33.10 O ANISOU 1015 O SER A 132 4254 4697 3627 -181 343 -85 O ATOM 1016 CB SER A 132 6.135 82.863 43.881 1.00 32.14 C ANISOU 1016 CB SER A 132 4113 4531 3568 -73 345 -199 C ATOM 1017 OG SER A 132 5.247 81.758 44.108 1.00 36.78 O ANISOU 1017 OG SER A 132 4742 5072 4162 -59 296 -228 O ATOM 1018 N PHE A 133 7.762 84.799 41.983 1.00 31.23 N ANISOU 1018 N PHE A 133 4004 4511 3350 -141 489 -147 N ATOM 1019 CA PHE A 133 8.557 86.002 41.714 1.00 37.17 C ANISOU 1019 CA PHE A 133 4722 5300 4102 -189 542 -97 C ATOM 1020 C PHE A 133 7.874 86.887 40.679 1.00 41.72 C ANISOU 1020 C PHE A 133 5396 5870 4584 -245 520 -50 C ATOM 1021 O PHE A 133 7.759 88.106 40.865 1.00 39.37 O ANISOU 1021 O PHE A 133 5093 5559 4308 -290 490 10 O ATOM 1022 CB PHE A 133 9.966 85.612 41.254 1.00 38.61 C ANISOU 1022 CB PHE A 133 4849 5534 4287 -170 666 -123 C ATOM 1023 CG PHE A 133 10.922 85.426 42.394 1.00 43.85 C ANISOU 1023 CG PHE A 133 5377 6213 5070 -138 673 -130 C ATOM 1024 CD1 PHE A 133 11.649 86.507 42.890 1.00 42.16 C ANISOU 1024 CD1 PHE A 133 5076 6023 4918 -190 678 -83 C ATOM 1025 CD2 PHE A 133 11.064 84.188 43.004 1.00 41.91 C ANISOU 1025 CD2 PHE A 133 5098 5950 4877 -60 660 -179 C ATOM 1026 CE1 PHE A 133 12.529 86.350 43.961 1.00 45.10 C ANISOU 1026 CE1 PHE A 133 5324 6415 5399 -167 663 -88 C ATOM 1027 CE2 PHE A 133 11.926 84.020 44.073 1.00 43.83 C ANISOU 1027 CE2 PHE A 133 5221 6206 5226 -27 646 -175 C ATOM 1028 CZ PHE A 133 12.659 85.109 44.576 1.00 44.02 C ANISOU 1028 CZ PHE A 133 5152 6266 5308 -82 642 -131 C ATOM 1029 N ALA A 134 7.381 86.277 39.593 1.00 38.11 N ANISOU 1029 N ALA A 134 5043 5416 4021 -242 524 -75 N ATOM 1030 CA ALA A 134 6.788 87.053 38.508 1.00 39.00 C ANISOU 1030 CA ALA A 134 5263 5528 4027 -295 495 -24 C ATOM 1031 C ALA A 134 5.536 87.760 38.970 1.00 37.01 C ANISOU 1031 C ALA A 134 5018 5228 3815 -305 364 24 C ATOM 1032 O ALA A 134 5.295 88.919 38.610 1.00 37.28 O ANISOU 1032 O ALA A 134 5089 5249 3827 -345 333 95 O ATOM 1033 CB ALA A 134 6.476 86.145 37.308 1.00 43.52 C ANISOU 1033 CB ALA A 134 5956 6114 4467 -291 509 -71 C ATOM 1034 N ILE A 135 4.727 87.080 39.777 1.00 31.19 N ANISOU 1034 N ILE A 135 4245 4464 3144 -268 293 -12 N ATOM 1035 CA ILE A 135 3.477 87.646 40.259 1.00 31.92 C ANISOU 1035 CA ILE A 135 4325 4516 3287 -268 182 24 C ATOM 1036 C ILE A 135 3.737 88.730 41.303 1.00 37.09 C ANISOU 1036 C ILE A 135 4906 5149 4038 -268 185 61 C ATOM 1037 O ILE A 135 3.125 89.804 41.270 1.00 32.10 O ANISOU 1037 O ILE A 135 4290 4483 3423 -280 129 115 O ATOM 1038 CB ILE A 135 2.589 86.532 40.845 1.00 31.46 C ANISOU 1038 CB ILE A 135 4241 4440 3273 -238 125 -25 C ATOM 1039 CG1 ILE A 135 1.963 85.671 39.742 1.00 40.32 C ANISOU 1039 CG1 ILE A 135 5454 5566 4301 -253 81 -54 C ATOM 1040 CG2 ILE A 135 1.474 87.129 41.695 1.00 31.70 C ANISOU 1040 CG2 ILE A 135 4216 4439 3391 -227 44 7 C ATOM 1041 CD1 ILE A 135 0.980 84.595 40.341 1.00 41.26 C ANISOU 1041 CD1 ILE A 135 5543 5656 4477 -242 15 -96 C ATOM 1042 N GLY A 136 4.581 88.432 42.304 1.00 29.81 N ANISOU 1042 N GLY A 136 3906 4237 3184 -251 237 28 N ATOM 1043 CA GLY A 136 4.765 89.383 43.396 1.00 28.25 C ANISOU 1043 CA GLY A 136 3651 4014 3070 -257 225 48 C ATOM 1044 C GLY A 136 5.545 90.609 42.972 1.00 32.14 C ANISOU 1044 C GLY A 136 4157 4501 3552 -308 261 99 C ATOM 1045 O GLY A 136 5.407 91.677 43.581 1.00 32.69 O ANISOU 1045 O GLY A 136 4218 4527 3676 -324 231 126 O ATOM 1046 N LEU A 137 6.384 90.480 41.932 1.00 29.98 N ANISOU 1046 N LEU A 137 3913 4269 3209 -339 334 111 N ATOM 1047 CA LEU A 137 7.199 91.610 41.478 1.00 33.04 C ANISOU 1047 CA LEU A 137 4312 4656 3586 -404 383 168 C ATOM 1048 C LEU A 137 6.634 92.288 40.240 1.00 34.09 C ANISOU 1048 C LEU A 137 4558 4768 3626 -439 361 235 C ATOM 1049 O LEU A 137 7.300 93.153 39.665 1.00 32.68 O ANISOU 1049 O LEU A 137 4411 4588 3418 -502 411 293 O ATOM 1050 CB LEU A 137 8.652 91.176 41.235 1.00 30.46 C ANISOU 1050 CB LEU A 137 3924 4395 3256 -425 497 149 C ATOM 1051 CG LEU A 137 9.367 90.647 42.519 1.00 34.03 C ANISOU 1051 CG LEU A 137 4253 4864 3811 -394 503 98 C ATOM 1052 CD1 LEU A 137 10.797 90.331 42.157 1.00 38.66 C ANISOU 1052 CD1 LEU A 137 4762 5518 4408 -411 614 89 C ATOM 1053 CD2 LEU A 137 9.358 91.667 43.697 1.00 32.82 C ANISOU 1053 CD2 LEU A 137 4060 4663 3746 -424 439 116 C ATOM 1054 N THR A 138 5.418 91.937 39.825 1.00 31.02 N ANISOU 1054 N THR A 138 4231 4363 3192 -404 280 234 N ATOM 1055 CA THR A 138 4.794 92.632 38.689 1.00 31.63 C ANISOU 1055 CA THR A 138 4421 4417 3180 -433 230 308 C ATOM 1056 C THR A 138 4.852 94.166 38.771 1.00 29.81 C ANISOU 1056 C THR A 138 4216 4119 2990 -472 207 391 C ATOM 1057 O THR A 138 5.046 94.808 37.720 1.00 35.46 O ANISOU 1057 O THR A 138 5027 4828 3618 -524 221 466 O ATOM 1058 CB THR A 138 3.335 92.126 38.556 1.00 39.27 C ANISOU 1058 CB THR A 138 5416 5368 4137 -385 113 296 C ATOM 1059 OG1 THR A 138 3.333 90.867 37.876 1.00 41.53 O ANISOU 1059 OG1 THR A 138 5741 5706 4332 -380 133 241 O ATOM 1060 CG2 THR A 138 2.454 93.080 37.764 1.00 37.45 C ANISOU 1060 CG2 THR A 138 5273 5093 3864 -396 15 384 C ATOM 1061 N PRO A 139 4.709 94.816 39.935 1.00 31.07 N ANISOU 1061 N PRO A 139 4312 4221 3271 -454 174 384 N ATOM 1062 CA PRO A 139 4.841 96.294 39.940 1.00 30.02 C ANISOU 1062 CA PRO A 139 4223 4007 3175 -496 156 459 C ATOM 1063 C PRO A 139 6.165 96.784 39.389 1.00 32.97 C ANISOU 1063 C PRO A 139 4618 4402 3509 -589 256 503 C ATOM 1064 O PRO A 139 6.214 97.878 38.799 1.00 31.77 O ANISOU 1064 O PRO A 139 4549 4188 3333 -642 244 592 O ATOM 1065 CB PRO A 139 4.681 96.649 41.431 1.00 30.70 C ANISOU 1065 CB PRO A 139 4232 4041 3391 -462 129 409 C ATOM 1066 CG PRO A 139 3.717 95.586 41.939 1.00 31.87 C ANISOU 1066 CG PRO A 139 4329 4221 3558 -382 85 344 C ATOM 1067 CD PRO A 139 4.218 94.312 41.228 1.00 29.39 C ANISOU 1067 CD PRO A 139 4011 4000 3154 -393 140 313 C ATOM 1068 N AMET A 140 7.254 96.019 39.543 0.50 34.00 N ANISOU 1068 N AMET A 140 4670 4612 3635 -612 355 452 N ATOM 1069 N BMET A 140 7.241 96.000 39.563 0.50 33.84 N ANISOU 1069 N BMET A 140 4648 4592 3616 -610 354 450 N ATOM 1070 CA AMET A 140 8.539 96.448 38.986 0.50 35.01 C ANISOU 1070 CA AMET A 140 4795 4774 3734 -704 465 495 C ATOM 1071 CA BMET A 140 8.540 96.350 38.991 0.50 35.14 C ANISOU 1071 CA BMET A 140 4807 4795 3748 -700 467 489 C ATOM 1072 C AMET A 140 8.557 96.453 37.461 0.50 37.28 C ANISOU 1072 C AMET A 140 5199 5094 3872 -744 514 560 C ATOM 1073 C BMET A 140 8.457 96.581 37.494 0.50 36.74 C ANISOU 1073 C BMET A 140 5137 5014 3809 -744 500 567 C ATOM 1074 O AMET A 140 9.514 96.967 36.870 0.50 35.53 O ANISOU 1074 O AMET A 140 4992 4893 3613 -832 612 616 O ATOM 1075 O BMET A 140 9.236 97.370 36.950 0.50 37.71 O ANISOU 1075 O BMET A 140 5294 5131 3904 -836 573 639 O ATOM 1076 CB AMET A 140 9.687 95.558 39.491 0.50 35.03 C ANISOU 1076 CB AMET A 140 4666 4862 3780 -703 559 423 C ATOM 1077 CB BMET A 140 9.573 95.245 39.249 0.50 33.81 C ANISOU 1077 CB BMET A 140 4526 4726 3596 -688 566 415 C ATOM 1078 CG AMET A 140 9.776 95.410 41.025 0.50 36.39 C ANISOU 1078 CG AMET A 140 4730 5016 4081 -667 507 358 C ATOM 1079 CG BMET A 140 9.705 94.783 40.708 0.50 35.94 C ANISOU 1079 CG BMET A 140 4676 4995 3985 -639 528 338 C ATOM 1080 SD AMET A 140 11.237 94.515 41.631 0.50 32.31 S ANISOU 1080 SD AMET A 140 4052 4594 3631 -668 596 295 S ATOM 1081 SD BMET A 140 10.594 95.951 41.730 0.50 45.05 S ANISOU 1081 SD BMET A 140 5754 6103 5261 -719 521 358 S ATOM 1082 CE AMET A 140 12.554 95.700 41.318 0.50 36.59 C ANISOU 1082 CE AMET A 140 4551 5141 4212 -803 676 365 C ATOM 1083 CE BMET A 140 12.174 96.046 40.884 0.50 39.93 C ANISOU 1083 CE BMET A 140 5043 5535 4594 -815 668 398 C ATOM 1084 N LEU A 141 7.558 95.868 36.805 1.00 34.77 N ANISOU 1084 N LEU A 141 4964 4787 3462 -691 451 554 N ATOM 1085 CA LEU A 141 7.495 95.887 35.344 1.00 39.78 C ANISOU 1085 CA LEU A 141 5734 5451 3930 -731 480 615 C ATOM 1086 C LEU A 141 6.784 97.109 34.805 1.00 42.76 C ANISOU 1086 C LEU A 141 6234 5741 4273 -762 385 732 C ATOM 1087 O LEU A 141 6.714 97.276 33.574 1.00 41.97 O ANISOU 1087 O LEU A 141 6267 5658 4021 -805 395 802 O ATOM 1088 CB LEU A 141 6.806 94.622 34.816 1.00 39.74 C ANISOU 1088 CB LEU A 141 5772 5500 3827 -670 447 549 C ATOM 1089 CG LEU A 141 7.444 93.301 35.265 1.00 46.30 C ANISOU 1089 CG LEU A 141 6502 6403 4688 -626 536 434 C ATOM 1090 CD1 LEU A 141 6.679 92.132 34.680 1.00 50.91 C ANISOU 1090 CD1 LEU A 141 7154 7016 5172 -577 490 372 C ATOM 1091 CD2 LEU A 141 8.897 93.246 34.814 1.00 45.06 C ANISOU 1091 CD2 LEU A 141 6314 6314 4491 -681 711 433 C ATOM 1092 N GLY A 142 6.273 97.975 35.690 1.00 36.29 N ANISOU 1092 N GLY A 142 5381 4824 3585 -738 293 754 N ATOM 1093 CA GLY A 142 5.693 99.229 35.228 1.00 38.07 C ANISOU 1093 CA GLY A 142 5720 4946 3799 -761 206 870 C ATOM 1094 C GLY A 142 4.348 99.538 35.866 1.00 38.01 C ANISOU 1094 C GLY A 142 5697 4854 3892 -665 54 864 C ATOM 1095 O GLY A 142 3.855 100.654 35.741 1.00 37.21 O ANISOU 1095 O GLY A 142 5667 4645 3825 -662 -25 951 O ATOM 1096 N TRP A 143 3.747 98.577 36.568 1.00 32.25 N ANISOU 1096 N TRP A 143 4871 4165 3216 -584 19 765 N ATOM 1097 CA TRP A 143 2.450 98.815 37.206 1.00 34.58 C ANISOU 1097 CA TRP A 143 5131 4393 3613 -491 -106 755 C ATOM 1098 C TRP A 143 2.720 99.379 38.602 1.00 28.50 C ANISOU 1098 C TRP A 143 4276 3559 2995 -474 -80 705 C ATOM 1099 O TRP A 143 2.664 98.680 39.613 1.00 30.96 O ANISOU 1099 O TRP A 143 4483 3906 3373 -433 -60 610 O ATOM 1100 CB TRP A 143 1.633 97.535 37.261 1.00 32.84 C ANISOU 1100 CB TRP A 143 4855 4247 3376 -428 -154 680 C ATOM 1101 CG TRP A 143 0.159 97.742 37.631 1.00 38.33 C ANISOU 1101 CG TRP A 143 5512 4889 4163 -338 -286 688 C ATOM 1102 CD1 TRP A 143 -0.476 98.937 37.979 1.00 38.01 C ANISOU 1102 CD1 TRP A 143 5478 4738 4224 -291 -358 743 C ATOM 1103 CD2 TRP A 143 -0.851 96.736 37.643 1.00 35.50 C ANISOU 1103 CD2 TRP A 143 5098 4582 3808 -286 -358 639 C ATOM 1104 NE1 TRP A 143 -1.823 98.697 38.226 1.00 34.56 N ANISOU 1104 NE1 TRP A 143 4976 4295 3861 -203 -462 729 N ATOM 1105 CE2 TRP A 143 -2.072 97.359 38.029 1.00 34.75 C ANISOU 1105 CE2 TRP A 143 4957 4419 3827 -207 -466 669 C ATOM 1106 CE3 TRP A 143 -0.842 95.357 37.380 1.00 34.78 C ANISOU 1106 CE3 TRP A 143 4989 4582 3644 -299 -340 571 C ATOM 1107 CZ2 TRP A 143 -3.272 96.640 38.154 1.00 35.58 C ANISOU 1107 CZ2 TRP A 143 4983 4558 3978 -151 -553 637 C ATOM 1108 CZ3 TRP A 143 -2.042 94.635 37.535 1.00 35.63 C ANISOU 1108 CZ3 TRP A 143 5033 4710 3795 -250 -434 537 C ATOM 1109 CH2 TRP A 143 -3.240 95.289 37.906 1.00 32.27 C ANISOU 1109 CH2 TRP A 143 4548 4229 3485 -182 -538 574 C ATOM 1110 N ASN A 144 3.074 100.662 38.647 1.00 34.74 N ANISOU 1110 N ASN A 144 5123 4248 3828 -517 -80 772 N ATOM 1111 CA ASN A 144 3.538 101.247 39.901 1.00 35.12 C ANISOU 1111 CA ASN A 144 5113 4233 4000 -525 -48 720 C ATOM 1112 C ASN A 144 3.292 102.746 39.837 1.00 37.36 C ANISOU 1112 C ASN A 144 5488 4363 4343 -534 -103 801 C ATOM 1113 O ASN A 144 2.961 103.296 38.783 1.00 36.70 O ANISOU 1113 O ASN A 144 5512 4233 4199 -546 -153 909 O ATOM 1114 CB ASN A 144 5.028 100.924 40.164 1.00 33.48 C ANISOU 1114 CB ASN A 144 4849 4094 3777 -620 69 681 C ATOM 1115 CG ASN A 144 5.963 101.508 39.085 1.00 37.52 C ANISOU 1115 CG ASN A 144 5442 4605 4209 -734 134 779 C ATOM 1116 OD1 ASN A 144 5.987 102.710 38.865 1.00 38.54 O ANISOU 1116 OD1 ASN A 144 5657 4623 4364 -780 106 861 O ATOM 1117 ND2 ASN A 144 6.755 100.653 38.438 1.00 32.24 N ANISOU 1117 ND2 ASN A 144 4748 4055 3446 -781 229 770 N ATOM 1118 N ASN A 145 3.453 103.411 40.983 1.00 35.81 N ANISOU 1118 N ASN A 145 5263 4081 4262 -528 -98 749 N ATOM 1119 CA ASN A 145 3.225 104.847 41.069 1.00 38.14 C ANISOU 1119 CA ASN A 145 5652 4208 4633 -529 -148 809 C ATOM 1120 C ASN A 145 4.522 105.646 41.013 1.00 44.10 C ANISOU 1120 C ASN A 145 6456 4909 5391 -670 -85 849 C ATOM 1121 O ASN A 145 4.533 106.801 41.445 1.00 42.94 O ANISOU 1121 O ASN A 145 6375 4612 5330 -686 -115 866 O ATOM 1122 CB ASN A 145 2.470 105.208 42.358 1.00 43.34 C ANISOU 1122 CB ASN A 145 6270 4781 5418 -429 -185 720 C ATOM 1123 CG ASN A 145 1.040 104.670 42.398 1.00 47.67 C ANISOU 1123 CG ASN A 145 6765 5357 5990 -289 -252 698 C ATOM 1124 OD1 ASN A 145 0.378 104.537 41.376 1.00 46.59 O ANISOU 1124 OD1 ASN A 145 6661 5237 5804 -255 -316 779 O ATOM 1125 ND2 ASN A 145 0.567 104.371 43.595 1.00 50.07 N ANISOU 1125 ND2 ASN A 145 6988 5668 6369 -214 -237 591 N ATOM 1126 N CYS A 146 5.618 105.057 40.511 1.00 41.15 N ANISOU 1126 N CYS A 146 6048 4652 4935 -773 4 862 N ATOM 1127 CA CYS A 146 6.885 105.790 40.451 1.00 42.30 C ANISOU 1127 CA CYS A 146 6217 4760 5097 -920 71 904 C ATOM 1128 C CYS A 146 6.785 107.004 39.558 1.00 50.43 C ANISOU 1128 C CYS A 146 7399 5655 6109 -977 39 1043 C ATOM 1129 O CYS A 146 7.558 107.959 39.725 1.00 54.34 O ANISOU 1129 O CYS A 146 7935 6053 6657 -1090 64 1080 O ATOM 1130 CB CYS A 146 8.024 104.901 39.945 1.00 41.15 C ANISOU 1130 CB CYS A 146 5993 4774 4869 -1008 185 901 C ATOM 1131 SG CYS A 146 8.472 103.605 41.149 1.00 41.93 S ANISOU 1131 SG CYS A 146 5912 5007 5012 -962 224 747 S ATOM 1132 N GLY A 147 5.871 106.981 38.587 1.00 46.83 N ANISOU 1132 N GLY A 147 7030 5188 5576 -911 -23 1125 N ATOM 1133 CA GLY A 147 5.730 108.101 37.675 1.00 49.50 C ANISOU 1133 CA GLY A 147 7528 5397 5885 -960 -66 1274 C ATOM 1134 C GLY A 147 4.926 109.258 38.215 1.00 55.62 C ANISOU 1134 C GLY A 147 8378 5969 6787 -885 -171 1292 C ATOM 1135 O GLY A 147 4.814 110.290 37.552 1.00 58.67 O ANISOU 1135 O GLY A 147 8906 6217 7168 -921 -217 1420 O ATOM 1136 N GLN A 148 4.361 109.115 39.412 1.00 53.96 N ANISOU 1136 N GLN A 148 8082 5731 6688 -779 -204 1167 N ATOM 1137 CA GLN A 148 3.530 110.143 40.035 1.00 58.41 C ANISOU 1137 CA GLN A 148 8706 6104 7381 -683 -290 1158 C ATOM 1138 C GLN A 148 3.969 110.323 41.480 1.00 53.80 C ANISOU 1138 C GLN A 148 8059 5480 6904 -696 -251 1019 C ATOM 1139 O GLN A 148 3.232 109.977 42.408 1.00 50.73 O ANISOU 1139 O GLN A 148 7596 5100 6577 -575 -270 909 O ATOM 1140 CB GLN A 148 2.052 109.757 39.962 1.00 67.78 C ANISOU 1140 CB GLN A 148 9859 7304 8590 -504 -382 1148 C ATOM 1141 CG GLN A 148 1.543 109.505 38.542 1.00 75.05 C ANISOU 1141 CG GLN A 148 10844 8276 9395 -488 -447 1279 C ATOM 1142 N PRO A 149 5.169 110.853 41.711 1.00 55.75 N ANISOU 1142 N PRO A 149 8331 5683 7167 -850 -195 1022 N ATOM 1143 CA PRO A 149 5.678 110.942 43.084 1.00 55.36 C ANISOU 1143 CA PRO A 149 8223 5612 7200 -879 -169 885 C ATOM 1144 C PRO A 149 4.904 111.946 43.923 1.00 55.62 C ANISOU 1144 C PRO A 149 8338 5444 7350 -784 -233 829 C ATOM 1145 O PRO A 149 4.257 112.865 43.419 1.00 58.25 O ANISOU 1145 O PRO A 149 8791 5615 7727 -731 -294 915 O ATOM 1146 CB PRO A 149 7.134 111.388 42.901 1.00 55.08 C ANISOU 1146 CB PRO A 149 8202 5568 7158 -1082 -111 930 C ATOM 1147 CG PRO A 149 7.145 112.120 41.602 1.00 56.43 C ANISOU 1147 CG PRO A 149 8504 5652 7285 -1145 -121 1099 C ATOM 1148 CD PRO A 149 6.127 111.398 40.733 1.00 57.29 C ANISOU 1148 CD PRO A 149 8610 5852 7305 -1014 -153 1153 C ATOM 1149 N LYS A 150 4.980 111.748 45.238 1.00 56.76 N ANISOU 1149 N LYS A 150 8423 5600 7544 -758 -218 681 N ATOM 1150 CA LYS A 150 4.475 112.718 46.204 1.00 51.32 C ANISOU 1150 CA LYS A 150 7819 4720 6960 -690 -256 598 C ATOM 1151 C LYS A 150 5.575 113.741 46.417 1.00 48.64 C ANISOU 1151 C LYS A 150 7575 4243 6663 -862 -256 608 C ATOM 1152 O LYS A 150 6.508 113.515 47.190 1.00 48.26 O ANISOU 1152 O LYS A 150 7472 4254 6609 -971 -229 523 O ATOM 1153 CB LYS A 150 4.087 112.039 47.510 1.00 54.67 C ANISOU 1153 CB LYS A 150 8155 5223 7394 -597 -233 435 C ATOM 1154 CG LYS A 150 2.987 110.992 47.362 1.00 59.57 C ANISOU 1154 CG LYS A 150 8670 5980 7982 -441 -228 423 C ATOM 1155 CD LYS A 150 1.616 111.576 47.655 1.00 67.06 C ANISOU 1155 CD LYS A 150 9662 6796 9020 -262 -262 395 C ATOM 1156 CE LYS A 150 0.496 110.570 47.358 1.00 72.19 C ANISOU 1156 CE LYS A 150 10195 7583 9651 -123 -267 404 C ATOM 1157 NZ LYS A 150 0.620 109.297 48.138 1.00 77.01 N ANISOU 1157 NZ LYS A 150 10679 8380 10203 -123 -210 301 N ATOM 1158 N GLU A 151 5.466 114.870 45.728 1.00 52.81 N ANISOU 1158 N GLU A 151 8246 4581 7237 -891 -296 718 N ATOM 1159 CA GLU A 151 6.520 115.879 45.791 1.00 65.01 C ANISOU 1159 CA GLU A 151 9890 5983 8827 -1076 -298 749 C ATOM 1160 C GLU A 151 6.571 116.591 47.136 1.00 68.22 C ANISOU 1160 C GLU A 151 10363 6235 9322 -1076 -324 599 C ATOM 1161 O GLU A 151 7.643 117.056 47.543 1.00 68.15 O ANISOU 1161 O GLU A 151 10382 6174 9338 -1252 -323 571 O ATOM 1162 CB GLU A 151 6.356 116.877 44.650 1.00 70.49 C ANISOU 1162 CB GLU A 151 10735 6506 9541 -1109 -336 921 C ATOM 1163 CG GLU A 151 6.926 116.351 43.328 1.00 81.55 C ANISOU 1163 CG GLU A 151 12097 8057 10831 -1216 -290 1074 C ATOM 1164 CD GLU A 151 8.358 115.806 43.468 1.00 96.34 C ANISOU 1164 CD GLU A 151 13854 10090 12660 -1409 -209 1049 C ATOM 1165 OE1 GLU A 151 9.127 116.314 44.318 1.00102.91 O ANISOU 1165 OE1 GLU A 151 14691 10847 13564 -1527 -211 971 O ATOM 1166 OE2 GLU A 151 8.718 114.861 42.729 1.00 99.55 O ANISOU 1166 OE2 GLU A 151 14161 10699 12965 -1442 -147 1103 O ATOM 1167 N GLY A 152 5.445 116.677 47.844 1.00 68.17 N ANISOU 1167 N GLY A 152 10382 6158 9362 -886 -345 499 N ATOM 1168 CA GLY A 152 5.471 117.257 49.179 1.00 64.83 C ANISOU 1168 CA GLY A 152 10030 5604 9000 -878 -355 337 C ATOM 1169 C GLY A 152 6.237 116.396 50.165 1.00 63.18 C ANISOU 1169 C GLY A 152 9705 5573 8729 -960 -325 210 C ATOM 1170 O GLY A 152 7.081 116.890 50.923 1.00 64.42 O ANISOU 1170 O GLY A 152 9914 5657 8905 -1096 -346 130 O ATOM 1171 N LYS A 153 5.951 115.095 50.173 1.00 56.31 N ANISOU 1171 N LYS A 153 8680 4932 7783 -880 -287 192 N ATOM 1172 CA LYS A 153 6.720 114.180 51.004 1.00 56.64 C ANISOU 1172 CA LYS A 153 8606 5153 7761 -956 -265 96 C ATOM 1173 C LYS A 153 8.176 114.125 50.565 1.00 58.05 C ANISOU 1173 C LYS A 153 8730 5403 7922 -1172 -266 167 C ATOM 1174 O LYS A 153 9.084 114.084 51.406 1.00 58.78 O ANISOU 1174 O LYS A 153 8793 5528 8012 -1291 -285 83 O ATOM 1175 CB LYS A 153 6.123 112.780 50.947 1.00 56.51 C ANISOU 1175 CB LYS A 153 8443 5356 7674 -832 -224 86 C ATOM 1176 CG LYS A 153 4.831 112.620 51.692 1.00 62.52 C ANISOU 1176 CG LYS A 153 9214 6093 8449 -639 -209 -13 C ATOM 1177 CD LYS A 153 4.395 111.171 51.700 1.00 60.64 C ANISOU 1177 CD LYS A 153 8825 6077 8140 -553 -170 -23 C ATOM 1178 CE LYS A 153 2.888 111.083 51.845 1.00 58.98 C ANISOU 1178 CE LYS A 153 8608 5838 7963 -353 -152 -54 C ATOM 1179 NZ LYS A 153 2.396 109.693 51.912 1.00 58.05 N ANISOU 1179 NZ LYS A 153 8349 5922 7785 -279 -115 -67 N ATOM 1180 N AASN A 154 8.407 114.047 49.249 0.50 54.67 N ANISOU 1180 N AASN A 154 8276 5017 7477 -1223 -242 320 N ATOM 1181 N BASN A 154 8.430 114.128 49.256 0.50 54.75 N ANISOU 1181 N BASN A 154 8296 5015 7493 -1229 -245 320 N ATOM 1182 CA AASN A 154 9.757 114.043 48.699 0.50 55.69 C ANISOU 1182 CA AASN A 154 8348 5216 7597 -1427 -220 401 C ATOM 1183 CA BASN A 154 9.807 113.953 48.819 0.50 55.68 C ANISOU 1183 CA BASN A 154 8334 5230 7594 -1428 -220 386 C ATOM 1184 C AASN A 154 10.575 115.178 49.297 0.50 60.03 C ANISOU 1184 C AASN A 154 8992 5594 8224 -1593 -266 363 C ATOM 1185 C BASN A 154 10.662 115.189 49.140 0.50 60.23 C ANISOU 1185 C BASN A 154 9013 5624 8247 -1609 -261 383 C ATOM 1186 O AASN A 154 11.613 114.961 49.935 0.50 59.39 O ANISOU 1186 O AASN A 154 8828 5590 8148 -1727 -278 302 O ATOM 1187 O BASN A 154 11.852 115.043 49.444 0.50 61.53 O ANISOU 1187 O BASN A 154 9091 5868 8421 -1775 -261 364 O ATOM 1188 CB AASN A 154 9.682 114.166 47.174 0.50 55.95 C ANISOU 1188 CB AASN A 154 8407 5250 7600 -1449 -186 576 C ATOM 1189 CB BASN A 154 9.841 113.581 47.333 0.50 55.50 C ANISOU 1189 CB BASN A 154 8274 5298 7516 -1441 -169 546 C ATOM 1190 CG AASN A 154 11.038 114.377 46.524 0.50 60.62 C ANISOU 1190 CG AASN A 154 8959 5883 8191 -1668 -144 673 C ATOM 1191 CG BASN A 154 9.094 112.245 47.015 0.50 52.05 C ANISOU 1191 CG BASN A 154 7727 5053 6996 -1283 -135 540 C ATOM 1192 OD1AASN A 154 12.062 113.932 47.033 0.50 63.50 O ANISOU 1192 OD1AASN A 154 9201 6366 8561 -1780 -126 619 O ATOM 1193 OD1BASN A 154 8.764 111.437 47.897 0.50 44.25 O ANISOU 1193 OD1BASN A 154 6658 4163 5990 -1188 -137 426 O ATOM 1194 ND2AASN A 154 11.046 115.059 45.382 0.50 65.16 N ANISOU 1194 ND2AASN A 154 9635 6364 8761 -1730 -128 825 N ATOM 1195 ND2BASN A 154 8.826 112.034 45.736 0.50 53.42 N ANISOU 1195 ND2BASN A 154 7912 5272 7115 -1263 -108 667 N ATOM 1196 N HIS A 155 10.079 116.402 49.138 1.00 61.74 N ANISOU 1196 N HIS A 155 9387 5567 8507 -1580 -303 393 N ATOM 1197 CA HIS A 155 10.828 117.576 49.577 1.00 65.30 C ANISOU 1197 CA HIS A 155 9952 5822 9036 -1751 -351 369 C ATOM 1198 C HIS A 155 10.904 117.679 51.094 1.00 66.94 C ANISOU 1198 C HIS A 155 10187 5988 9259 -1746 -401 178 C ATOM 1199 O HIS A 155 11.923 118.123 51.634 1.00 69.87 O ANISOU 1199 O HIS A 155 10569 6314 9666 -1931 -444 132 O ATOM 1200 CB HIS A 155 10.211 118.849 48.999 1.00 74.43 C ANISOU 1200 CB HIS A 155 11309 6708 10263 -1722 -381 453 C ATOM 1201 CG HIS A 155 10.272 118.914 47.508 1.00 79.43 C ANISOU 1201 CG HIS A 155 11950 7360 10871 -1765 -345 653 C ATOM 1202 ND1 HIS A 155 9.197 119.291 46.735 1.00 84.25 N ANISOU 1202 ND1 HIS A 155 12667 7857 11487 -1616 -362 750 N ATOM 1203 CD2 HIS A 155 11.272 118.620 46.647 1.00 82.40 C ANISOU 1203 CD2 HIS A 155 12238 7863 11206 -1935 -291 776 C ATOM 1204 CE1 HIS A 155 9.535 119.232 45.459 1.00 87.33 C ANISOU 1204 CE1 HIS A 155 13053 8303 11827 -1700 -327 925 C ATOM 1205 NE2 HIS A 155 10.788 118.826 45.379 1.00 84.61 N ANISOU 1205 NE2 HIS A 155 12592 8104 11450 -1893 -273 941 N ATOM 1206 N SER A 156 9.841 117.301 51.805 1.00 66.31 N ANISOU 1206 N SER A 156 10124 5920 9151 -1544 -397 66 N ATOM 1207 CA SER A 156 9.892 117.422 53.255 1.00 71.84 C ANISOU 1207 CA SER A 156 10874 6579 9844 -1541 -437 -117 C ATOM 1208 C SER A 156 10.908 116.457 53.849 1.00 77.76 C ANISOU 1208 C SER A 156 11462 7550 10531 -1653 -449 -169 C ATOM 1209 O SER A 156 11.552 116.781 54.851 1.00 82.56 O ANISOU 1209 O SER A 156 12113 8115 11142 -1764 -511 -280 O ATOM 1210 CB SER A 156 8.505 117.210 53.865 1.00 74.42 C ANISOU 1210 CB SER A 156 11247 6879 10149 -1299 -409 -220 C ATOM 1211 OG SER A 156 8.121 115.849 53.842 1.00 80.17 O ANISOU 1211 OG SER A 156 11812 7851 10798 -1187 -360 -218 O ATOM 1212 N GLN A 157 11.089 115.288 53.233 1.00 74.44 N ANISOU 1212 N GLN A 157 10865 7363 10058 -1627 -399 -90 N ATOM 1213 CA GLN A 157 12.110 114.346 53.668 1.00 71.26 C ANISOU 1213 CA GLN A 157 10295 7168 9612 -1726 -412 -119 C ATOM 1214 C GLN A 157 13.488 114.678 53.117 1.00 68.70 C ANISOU 1214 C GLN A 157 9899 6864 9342 -1955 -426 -28 C ATOM 1215 O GLN A 157 14.476 114.100 53.579 1.00 69.84 O ANISOU 1215 O GLN A 157 9906 7153 9477 -2059 -456 -58 O ATOM 1216 CB GLN A 157 11.742 112.926 53.245 1.00 73.48 C ANISOU 1216 CB GLN A 157 10419 7678 9821 -1596 -347 -78 C ATOM 1217 CG GLN A 157 10.336 112.507 53.618 1.00 82.48 C ANISOU 1217 CG GLN A 157 11603 8820 10917 -1376 -319 -143 C ATOM 1218 CD GLN A 157 10.168 112.240 55.092 1.00 92.23 C ANISOU 1218 CD GLN A 157 12864 10074 12104 -1330 -353 -301 C ATOM 1219 OE1 GLN A 157 10.417 111.122 55.561 1.00 96.56 O ANISOU 1219 OE1 GLN A 157 13293 10805 12588 -1309 -349 -335 O ATOM 1220 NE2 GLN A 157 9.733 113.262 55.839 1.00 92.84 N ANISOU 1220 NE2 GLN A 157 13110 9956 12207 -1311 -383 -400 N ATOM 1221 N GLY A 158 13.578 115.566 52.134 1.00 67.06 N ANISOU 1221 N GLY A 158 9770 6517 9191 -2035 -406 90 N ATOM 1222 CA GLY A 158 14.866 115.895 51.556 1.00 68.07 C ANISOU 1222 CA GLY A 158 9824 6667 9374 -2262 -400 187 C ATOM 1223 C GLY A 158 15.419 114.842 50.624 1.00 65.98 C ANISOU 1223 C GLY A 158 9361 6639 9071 -2279 -313 295 C ATOM 1224 O GLY A 158 16.634 114.668 50.542 1.00 68.04 O ANISOU 1224 O GLY A 158 9481 7003 9367 -2447 -306 328 O ATOM 1225 N CYS A 159 14.566 114.127 49.912 1.00 60.64 N ANISOU 1225 N CYS A 159 8666 6050 8325 -2110 -247 347 N ATOM 1226 CA CYS A 159 15.114 113.120 49.023 1.00 58.30 C ANISOU 1226 CA CYS A 159 8198 5970 7984 -2126 -158 437 C ATOM 1227 C CYS A 159 15.823 113.792 47.849 1.00 66.79 C ANISOU 1227 C CYS A 159 9286 6999 9091 -2294 -97 589 C ATOM 1228 O CYS A 159 15.566 114.948 47.510 1.00 68.16 O ANISOU 1228 O CYS A 159 9625 6967 9303 -2352 -118 650 O ATOM 1229 CB CYS A 159 14.019 112.175 48.550 1.00 53.77 C ANISOU 1229 CB CYS A 159 7612 5495 7323 -1915 -111 448 C ATOM 1230 SG CYS A 159 13.180 111.360 49.911 1.00 52.76 S ANISOU 1230 SG CYS A 159 7464 5425 7156 -1732 -165 282 S ATOM 1231 N GLY A 160 16.755 113.060 47.250 1.00 71.86 N ANISOU 1231 N GLY A 160 9753 7832 9717 -2375 -14 652 N ATOM 1232 CA GLY A 160 17.500 113.565 46.121 1.00 80.39 C ANISOU 1232 CA GLY A 160 10826 8905 10815 -2540 72 799 C ATOM 1233 C GLY A 160 16.750 113.362 44.821 1.00 80.80 C ANISOU 1233 C GLY A 160 10960 8973 10768 -2441 154 915 C ATOM 1234 O GLY A 160 15.565 113.025 44.788 1.00 72.18 O ANISOU 1234 O GLY A 160 9950 7862 9614 -2251 125 887 O ATOM 1235 N GLU A 161 17.476 113.569 43.724 1.00 82.93 N ANISOU 1235 N GLU A 161 11205 9285 11021 -2582 257 1051 N ATOM 1236 CA GLU A 161 16.896 113.424 42.396 1.00 81.20 C ANISOU 1236 CA GLU A 161 11077 9085 10688 -2518 336 1175 C ATOM 1237 C GLU A 161 16.641 111.959 42.089 1.00 73.29 C ANISOU 1237 C GLU A 161 9953 8307 9587 -2365 400 1134 C ATOM 1238 O GLU A 161 17.485 111.100 42.351 1.00 78.69 O ANISOU 1238 O GLU A 161 10443 9168 10288 -2392 457 1080 O ATOM 1239 CB GLU A 161 17.824 114.029 41.335 1.00 86.34 C ANISOU 1239 CB GLU A 161 11739 9730 11335 -2726 445 1332 C ATOM 1240 N GLY A 162 15.464 111.674 41.531 1.00 67.06 N ANISOU 1240 N GLY A 162 9277 7502 8701 -2202 382 1160 N ATOM 1241 CA GLY A 162 15.071 110.308 41.245 1.00 66.99 C ANISOU 1241 CA GLY A 162 9179 7679 8596 -2052 427 1115 C ATOM 1242 C GLY A 162 14.717 109.460 42.448 1.00 64.98 C ANISOU 1242 C GLY A 162 8821 7492 8377 -1917 360 959 C ATOM 1243 O GLY A 162 14.506 108.252 42.294 1.00 67.96 O ANISOU 1243 O GLY A 162 9111 8024 8687 -1806 398 915 O ATOM 1244 N GLN A 163 14.628 110.042 43.642 1.00 60.84 N ANISOU 1244 N GLN A 163 8317 6851 7949 -1925 262 873 N ATOM 1245 CA GLN A 163 14.278 109.285 44.837 1.00 55.57 C ANISOU 1245 CA GLN A 163 7571 6244 7301 -1805 199 730 C ATOM 1246 C GLN A 163 12.871 109.639 45.300 1.00 51.94 C ANISOU 1246 C GLN A 163 7249 5647 6839 -1653 112 682 C ATOM 1247 O GLN A 163 12.391 110.757 45.094 1.00 53.81 O ANISOU 1247 O GLN A 163 7638 5701 7107 -1668 71 732 O ATOM 1248 CB GLN A 163 15.254 109.551 45.990 1.00 56.55 C ANISOU 1248 CB GLN A 163 7605 6360 7520 -1920 152 648 C ATOM 1249 CG GLN A 163 16.697 109.229 45.707 1.00 55.29 C ANISOU 1249 CG GLN A 163 7274 6337 7395 -2070 226 685 C ATOM 1250 CD GLN A 163 17.549 109.313 46.963 1.00 60.28 C ANISOU 1250 CD GLN A 163 7801 6983 8120 -2160 148 591 C ATOM 1251 OE1 GLN A 163 17.486 110.293 47.716 1.00 57.85 O ANISOU 1251 OE1 GLN A 163 7593 6517 7872 -2228 55 548 O ATOM 1252 NE2 GLN A 163 18.338 108.278 47.204 1.00 61.90 N ANISOU 1252 NE2 GLN A 163 7810 7373 8338 -2155 178 556 N ATOM 1253 N VAL A 164 12.222 108.680 45.947 1.00 45.50 N ANISOU 1253 N VAL A 164 6375 4919 5995 -1505 89 584 N ATOM 1254 CA VAL A 164 10.942 108.919 46.598 1.00 49.86 C ANISOU 1254 CA VAL A 164 7023 5364 6559 -1359 19 518 C ATOM 1255 C VAL A 164 11.081 108.598 48.085 1.00 48.64 C ANISOU 1255 C VAL A 164 6810 5234 6436 -1335 -26 377 C ATOM 1256 O VAL A 164 11.973 107.860 48.513 1.00 43.70 O ANISOU 1256 O VAL A 164 6055 4742 5807 -1389 -12 335 O ATOM 1257 CB VAL A 164 9.818 108.074 45.975 1.00 50.04 C ANISOU 1257 CB VAL A 164 7043 5463 6508 -1198 32 539 C ATOM 1258 CG1 VAL A 164 9.708 108.334 44.494 1.00 44.86 C ANISOU 1258 CG1 VAL A 164 6454 4794 5796 -1227 65 679 C ATOM 1259 CG2 VAL A 164 10.094 106.611 46.229 1.00 47.11 C ANISOU 1259 CG2 VAL A 164 6523 5288 6087 -1152 71 478 C ATOM 1260 N ALA A 165 10.186 109.167 48.881 1.00 45.94 N ANISOU 1260 N ALA A 165 6571 4760 6125 -1247 -82 303 N ATOM 1261 CA ALA A 165 10.007 108.663 50.232 1.00 43.88 C ANISOU 1261 CA ALA A 165 6272 4542 5858 -1185 -113 169 C ATOM 1262 C ALA A 165 9.346 107.291 50.127 1.00 43.35 C ANISOU 1262 C ALA A 165 6111 4634 5725 -1049 -79 155 C ATOM 1263 O ALA A 165 8.266 107.158 49.545 1.00 41.96 O ANISOU 1263 O ALA A 165 5970 4441 5531 -932 -67 191 O ATOM 1264 CB ALA A 165 9.171 109.629 51.064 1.00 46.02 C ANISOU 1264 CB ALA A 165 6685 4630 6170 -1119 -160 90 C ATOM 1265 N CYS A 166 10.012 106.266 50.642 1.00 38.68 N ANISOU 1265 N CYS A 166 5399 4193 5104 -1068 -70 109 N ATOM 1266 CA CYS A 166 9.624 104.887 50.360 1.00 35.36 C ANISOU 1266 CA CYS A 166 4884 3926 4624 -968 -31 112 C ATOM 1267 C CYS A 166 8.532 104.485 51.340 1.00 39.17 C ANISOU 1267 C CYS A 166 5393 4402 5087 -836 -50 23 C ATOM 1268 O CYS A 166 8.800 104.033 52.460 1.00 40.17 O ANISOU 1268 O CYS A 166 5488 4578 5198 -835 -73 -59 O ATOM 1269 CB CYS A 166 10.819 103.937 50.460 1.00 36.21 C ANISOU 1269 CB CYS A 166 4851 4187 4720 -1034 -12 108 C ATOM 1270 SG CYS A 166 10.368 102.259 49.941 1.00 38.60 S ANISOU 1270 SG CYS A 166 5059 4653 4954 -915 40 119 S ATOM 1271 N LEU A 167 7.287 104.650 50.903 1.00 39.08 N ANISOU 1271 N LEU A 167 5438 4334 5076 -726 -42 44 N ATOM 1272 CA LEU A 167 6.111 104.287 51.683 1.00 37.92 C ANISOU 1272 CA LEU A 167 5304 4185 4920 -595 -41 -28 C ATOM 1273 C LEU A 167 5.221 103.406 50.815 1.00 34.64 C ANISOU 1273 C LEU A 167 4835 3850 4477 -500 -17 25 C ATOM 1274 O LEU A 167 4.940 103.762 49.663 1.00 36.06 O ANISOU 1274 O LEU A 167 5044 3994 4663 -496 -21 112 O ATOM 1275 CB LEU A 167 5.364 105.549 52.141 1.00 33.92 C ANISOU 1275 CB LEU A 167 4916 3503 4468 -548 -61 -68 C ATOM 1276 CG LEU A 167 6.188 106.403 53.150 1.00 43.80 C ANISOU 1276 CG LEU A 167 6240 4663 5739 -646 -93 -144 C ATOM 1277 CD1 LEU A 167 5.715 107.847 53.221 1.00 42.57 C ANISOU 1277 CD1 LEU A 167 6223 4301 5650 -630 -113 -159 C ATOM 1278 CD2 LEU A 167 6.154 105.776 54.536 1.00 44.92 C ANISOU 1278 CD2 LEU A 167 6364 4873 5831 -617 -92 -257 C ATOM 1279 N PHE A 168 4.770 102.280 51.382 1.00 30.70 N ANISOU 1279 N PHE A 168 4269 3453 3942 -431 1 -25 N ATOM 1280 CA PHE A 168 4.070 101.257 50.604 1.00 31.86 C ANISOU 1280 CA PHE A 168 4355 3691 4059 -364 17 17 C ATOM 1281 C PHE A 168 2.963 101.855 49.742 1.00 34.55 C ANISOU 1281 C PHE A 168 4739 3955 4433 -293 -4 76 C ATOM 1282 O PHE A 168 2.915 101.616 48.532 1.00 32.49 O ANISOU 1282 O PHE A 168 4472 3727 4143 -303 -13 155 O ATOM 1283 CB PHE A 168 3.501 100.176 51.537 1.00 35.59 C ANISOU 1283 CB PHE A 168 4771 4245 4507 -295 36 -50 C ATOM 1284 CG PHE A 168 2.915 98.976 50.802 1.00 31.44 C ANISOU 1284 CG PHE A 168 4180 3816 3951 -247 47 -14 C ATOM 1285 CD1 PHE A 168 1.589 98.981 50.380 1.00 31.91 C ANISOU 1285 CD1 PHE A 168 4235 3854 4036 -162 37 7 C ATOM 1286 CD2 PHE A 168 3.696 97.850 50.545 1.00 31.80 C ANISOU 1286 CD2 PHE A 168 4167 3968 3949 -285 63 -6 C ATOM 1287 CE1 PHE A 168 1.072 97.907 49.672 1.00 32.68 C ANISOU 1287 CE1 PHE A 168 4278 4033 4105 -135 33 37 C ATOM 1288 CE2 PHE A 168 3.173 96.744 49.853 1.00 34.58 C ANISOU 1288 CE2 PHE A 168 4475 4393 4270 -247 70 18 C ATOM 1289 CZ PHE A 168 1.867 96.773 49.426 1.00 31.60 C ANISOU 1289 CZ PHE A 168 4102 3994 3911 -180 51 38 C ATOM 1290 N GLU A 169 2.031 102.606 50.355 1.00 32.56 N ANISOU 1290 N GLU A 169 4532 3602 4238 -214 -13 36 N ATOM 1291 CA GLU A 169 0.862 103.053 49.602 1.00 31.06 C ANISOU 1291 CA GLU A 169 4358 3348 4094 -124 -43 92 C ATOM 1292 C GLU A 169 1.167 104.192 48.658 1.00 37.09 C ANISOU 1292 C GLU A 169 5212 3998 4882 -167 -82 180 C ATOM 1293 O GLU A 169 0.305 104.528 47.846 1.00 33.56 O ANISOU 1293 O GLU A 169 4783 3504 4464 -100 -125 249 O ATOM 1294 CB GLU A 169 -0.293 103.468 50.530 1.00 33.97 C ANISOU 1294 CB GLU A 169 4729 3647 4532 -7 -28 22 C ATOM 1295 CG GLU A 169 -0.869 102.239 51.304 1.00 33.21 C ANISOU 1295 CG GLU A 169 4537 3672 4408 43 16 -42 C ATOM 1296 CD GLU A 169 -2.173 102.522 52.051 1.00 34.44 C ANISOU 1296 CD GLU A 169 4670 3783 4634 167 50 -99 C ATOM 1297 OE1 GLU A 169 -2.760 103.598 51.859 1.00 34.56 O ANISOU 1297 OE1 GLU A 169 4729 3675 4728 236 31 -86 O ATOM 1298 OE2 GLU A 169 -2.628 101.638 52.807 1.00 34.47 O ANISOU 1298 OE2 GLU A 169 4607 3874 4616 197 100 -153 O ATOM 1299 N ASP A 170 2.360 104.792 48.736 1.00 32.20 N ANISOU 1299 N ASP A 170 4648 3332 4254 -282 -75 185 N ATOM 1300 CA ASP A 170 2.718 105.796 47.747 1.00 35.56 C ANISOU 1300 CA ASP A 170 5163 3655 4694 -343 -105 285 C ATOM 1301 C ASP A 170 3.275 105.177 46.466 1.00 37.56 C ANISOU 1301 C ASP A 170 5391 4013 4866 -414 -95 381 C ATOM 1302 O ASP A 170 3.219 105.817 45.408 1.00 39.14 O ANISOU 1302 O ASP A 170 5667 4148 5055 -439 -123 486 O ATOM 1303 CB ASP A 170 3.760 106.779 48.316 1.00 37.94 C ANISOU 1303 CB ASP A 170 5535 3851 5028 -455 -101 257 C ATOM 1304 CG ASP A 170 3.194 107.688 49.419 1.00 44.04 C ANISOU 1304 CG ASP A 170 6380 4476 5877 -388 -115 167 C ATOM 1305 OD1 ASP A 170 1.988 107.668 49.682 1.00 41.37 O ANISOU 1305 OD1 ASP A 170 6033 4110 5576 -249 -119 136 O ATOM 1306 OD2 ASP A 170 3.972 108.446 50.019 1.00 46.41 O ANISOU 1306 OD2 ASP A 170 6746 4686 6202 -478 -121 125 O ATOM 1307 N VAL A 171 3.842 103.966 46.519 1.00 31.75 N ANISOU 1307 N VAL A 171 4564 3432 4068 -448 -53 349 N ATOM 1308 CA VAL A 171 4.491 103.409 45.335 1.00 36.32 C ANISOU 1308 CA VAL A 171 5129 4106 4565 -517 -24 425 C ATOM 1309 C VAL A 171 3.769 102.196 44.748 1.00 34.58 C ANISOU 1309 C VAL A 171 4857 4001 4283 -445 -29 430 C ATOM 1310 O VAL A 171 3.904 101.944 43.540 1.00 36.22 O ANISOU 1310 O VAL A 171 5094 4255 4415 -477 -23 505 O ATOM 1311 CB VAL A 171 5.977 103.079 45.597 1.00 39.72 C ANISOU 1311 CB VAL A 171 5502 4613 4978 -633 36 401 C ATOM 1312 CG1 VAL A 171 6.744 104.363 45.953 1.00 41.12 C ANISOU 1312 CG1 VAL A 171 5738 4671 5215 -735 29 414 C ATOM 1313 CG2 VAL A 171 6.146 101.990 46.673 1.00 37.76 C ANISOU 1313 CG2 VAL A 171 5151 4465 4730 -598 53 298 C ATOM 1314 N VAL A 172 3.052 101.412 45.544 1.00 27.44 N ANISOU 1314 N VAL A 172 3883 3144 3398 -361 -35 352 N ATOM 1315 CA VAL A 172 2.361 100.222 45.043 1.00 29.73 C ANISOU 1315 CA VAL A 172 4123 3534 3638 -305 -45 351 C ATOM 1316 C VAL A 172 0.913 100.614 44.763 1.00 33.23 C ANISOU 1316 C VAL A 172 4585 3916 4123 -209 -117 384 C ATOM 1317 O VAL A 172 0.225 101.054 45.691 1.00 35.39 O ANISOU 1317 O VAL A 172 4841 4126 4479 -140 -128 336 O ATOM 1318 CB VAL A 172 2.419 99.045 46.033 1.00 33.03 C ANISOU 1318 CB VAL A 172 4451 4043 4057 -279 -11 260 C ATOM 1319 CG1 VAL A 172 1.707 97.814 45.417 1.00 33.92 C ANISOU 1319 CG1 VAL A 172 4524 4245 4121 -236 -26 263 C ATOM 1320 CG2 VAL A 172 3.887 98.674 46.401 1.00 30.12 C ANISOU 1320 CG2 VAL A 172 4047 3733 3663 -363 46 229 C ATOM 1321 N PRO A 173 0.417 100.474 43.530 1.00 36.30 N ANISOU 1321 N PRO A 173 5008 4323 4459 -200 -168 462 N ATOM 1322 CA PRO A 173 -0.956 100.915 43.230 1.00 34.95 C ANISOU 1322 CA PRO A 173 4843 4092 4343 -106 -255 504 C ATOM 1323 C PRO A 173 -1.974 100.044 43.943 1.00 32.24 C ANISOU 1323 C PRO A 173 4392 3808 4051 -24 -263 433 C ATOM 1324 O PRO A 173 -1.835 98.815 44.029 1.00 31.58 O ANISOU 1324 O PRO A 173 4252 3830 3916 -46 -233 387 O ATOM 1325 CB PRO A 173 -1.068 100.728 41.705 1.00 38.70 C ANISOU 1325 CB PRO A 173 5383 4604 4719 -137 -313 600 C ATOM 1326 CG PRO A 173 0.377 100.552 41.223 1.00 37.23 C ANISOU 1326 CG PRO A 173 5248 4466 4432 -254 -232 615 C ATOM 1327 CD PRO A 173 1.021 99.813 42.351 1.00 33.91 C ANISOU 1327 CD PRO A 173 4738 4107 4039 -268 -151 509 C ATOM 1328 N MET A 174 -3.033 100.682 44.419 1.00 32.96 N ANISOU 1328 N MET A 174 4453 3824 4247 72 -301 427 N ATOM 1329 CA MET A 174 -4.069 99.919 45.115 1.00 31.36 C ANISOU 1329 CA MET A 174 4135 3677 4102 146 -296 366 C ATOM 1330 C MET A 174 -4.900 99.070 44.141 1.00 30.19 C ANISOU 1330 C MET A 174 3940 3608 3923 158 -376 412 C ATOM 1331 O MET A 174 -5.427 98.037 44.549 1.00 30.33 O ANISOU 1331 O MET A 174 3866 3706 3953 170 -361 362 O ATOM 1332 CB MET A 174 -4.942 100.904 45.923 1.00 36.98 C ANISOU 1332 CB MET A 174 4821 4287 4945 252 -295 341 C ATOM 1333 CG MET A 174 -5.567 100.376 47.183 1.00 46.93 C ANISOU 1333 CG MET A 174 5980 5587 6263 308 -225 246 C ATOM 1334 SD MET A 174 -4.479 99.545 48.365 1.00 44.19 S ANISOU 1334 SD MET A 174 5636 5313 5842 228 -117 148 S ATOM 1335 CE MET A 174 -3.359 100.850 48.761 1.00 53.65 C ANISOU 1335 CE MET A 174 6955 6393 7038 185 -93 132 C ATOM 1336 N ASN A 175 -5.034 99.455 42.851 1.00 30.21 N ANISOU 1336 N ASN A 175 4011 3588 3879 145 -468 509 N ATOM 1337 CA ASN A 175 -5.797 98.573 41.957 1.00 30.58 C ANISOU 1337 CA ASN A 175 4021 3715 3881 144 -556 542 C ATOM 1338 C ASN A 175 -5.052 97.260 41.736 1.00 30.43 C ANISOU 1338 C ASN A 175 4012 3804 3746 57 -504 495 C ATOM 1339 O ASN A 175 -5.673 96.186 41.698 1.00 36.07 O ANISOU 1339 O ASN A 175 4656 4592 4456 58 -531 462 O ATOM 1340 CB ASN A 175 -6.169 99.239 40.611 1.00 34.54 C ANISOU 1340 CB ASN A 175 4607 4175 4342 150 -683 659 C ATOM 1341 CG ASN A 175 -5.014 100.042 39.962 1.00 37.71 C ANISOU 1341 CG ASN A 175 5159 4518 4649 78 -656 725 C ATOM 1342 OD1 ASN A 175 -3.836 99.808 40.211 1.00 39.92 O ANISOU 1342 OD1 ASN A 175 5476 4826 4865 1 -550 684 O ATOM 1343 ND2 ASN A 175 -5.375 100.990 39.136 1.00 36.97 N ANISOU 1343 ND2 ASN A 175 5147 4346 4555 103 -755 832 N ATOM 1344 N TYR A 176 -3.719 97.315 41.683 1.00 31.01 N ANISOU 1344 N TYR A 176 4161 3882 3739 -15 -422 485 N ATOM 1345 CA TYR A 176 -2.928 96.088 41.677 1.00 27.23 C ANISOU 1345 CA TYR A 176 3677 3494 3175 -78 -353 427 C ATOM 1346 C TYR A 176 -3.192 95.267 42.944 1.00 31.21 C ANISOU 1346 C TYR A 176 4076 4035 3748 -49 -300 338 C ATOM 1347 O TYR A 176 -3.392 94.046 42.877 1.00 28.85 O ANISOU 1347 O TYR A 176 3741 3805 3417 -65 -300 299 O ATOM 1348 CB TYR A 176 -1.423 96.416 41.544 1.00 27.95 C ANISOU 1348 CB TYR A 176 3838 3581 3198 -151 -266 433 C ATOM 1349 CG TYR A 176 -0.567 95.187 41.875 1.00 28.47 C ANISOU 1349 CG TYR A 176 3870 3732 3216 -190 -181 358 C ATOM 1350 CD1 TYR A 176 -0.240 94.247 40.877 1.00 36.24 C ANISOU 1350 CD1 TYR A 176 4896 4785 4088 -230 -173 357 C ATOM 1351 CD2 TYR A 176 -0.151 94.943 43.182 1.00 29.78 C ANISOU 1351 CD2 TYR A 176 3966 3902 3445 -179 -118 289 C ATOM 1352 CE1 TYR A 176 0.500 93.101 41.185 1.00 33.25 C ANISOU 1352 CE1 TYR A 176 4484 4470 3680 -248 -97 287 C ATOM 1353 CE2 TYR A 176 0.566 93.821 43.506 1.00 33.29 C ANISOU 1353 CE2 TYR A 176 4378 4415 3858 -202 -56 231 C ATOM 1354 CZ TYR A 176 0.879 92.896 42.513 1.00 36.85 C ANISOU 1354 CZ TYR A 176 4863 4925 4215 -231 -45 230 C ATOM 1355 OH TYR A 176 1.598 91.789 42.874 1.00 42.08 O ANISOU 1355 OH TYR A 176 5490 5639 4860 -239 16 171 O ATOM 1356 N MET A 177 -3.209 95.920 44.119 1.00 28.10 N ANISOU 1356 N MET A 177 3644 3589 3443 -10 -254 303 N ATOM 1357 CA MET A 177 -3.319 95.162 45.367 1.00 27.20 C ANISOU 1357 CA MET A 177 3453 3513 3371 6 -192 223 C ATOM 1358 C MET A 177 -4.690 94.525 45.504 1.00 29.18 C ANISOU 1358 C MET A 177 3612 3796 3680 53 -233 214 C ATOM 1359 O MET A 177 -4.823 93.443 46.089 1.00 30.33 O ANISOU 1359 O MET A 177 3705 3997 3824 39 -196 165 O ATOM 1360 CB MET A 177 -3.047 96.069 46.588 1.00 28.04 C ANISOU 1360 CB MET A 177 3559 3554 3541 33 -135 183 C ATOM 1361 CG MET A 177 -1.567 96.488 46.776 1.00 27.23 C ANISOU 1361 CG MET A 177 3522 3434 3392 -34 -86 174 C ATOM 1362 SD MET A 177 -0.491 95.058 46.877 1.00 31.51 S ANISOU 1362 SD MET A 177 4041 4077 3853 -96 -34 134 S ATOM 1363 CE MET A 177 -1.169 94.155 48.261 1.00 30.39 C ANISOU 1363 CE MET A 177 3825 3972 3751 -54 -1 63 C ATOM 1364 N VAL A 178 -5.736 95.206 45.037 1.00 26.53 N ANISOU 1364 N VAL A 178 3250 3421 3409 109 -311 263 N ATOM 1365 CA VAL A 178 -7.097 94.697 45.234 1.00 30.75 C ANISOU 1365 CA VAL A 178 3670 3988 4025 154 -350 257 C ATOM 1366 C VAL A 178 -7.514 93.736 44.111 1.00 30.34 C ANISOU 1366 C VAL A 178 3613 3999 3916 108 -442 288 C ATOM 1367 O VAL A 178 -7.914 92.592 44.375 1.00 32.85 O ANISOU 1367 O VAL A 178 3868 4376 4239 80 -433 250 O ATOM 1368 CB VAL A 178 -8.085 95.879 45.376 1.00 33.20 C ANISOU 1368 CB VAL A 178 3930 4229 4457 252 -390 290 C ATOM 1369 CG1 VAL A 178 -9.521 95.392 45.308 1.00 38.35 C ANISOU 1369 CG1 VAL A 178 4445 4925 5203 295 -449 301 C ATOM 1370 CG2 VAL A 178 -7.816 96.608 46.751 1.00 31.74 C ANISOU 1370 CG2 VAL A 178 3745 3985 4331 298 -278 227 C ATOM 1371 N TYR A 179 -7.442 94.191 42.853 1.00 30.08 N ANISOU 1371 N TYR A 179 3658 3948 3822 94 -536 357 N ATOM 1372 CA TYR A 179 -7.905 93.365 41.735 1.00 34.75 C ANISOU 1372 CA TYR A 179 4263 4594 4346 49 -640 383 C ATOM 1373 C TYR A 179 -6.932 92.221 41.427 1.00 35.21 C ANISOU 1373 C TYR A 179 4397 4705 4277 -34 -586 335 C ATOM 1374 O TYR A 179 -7.354 91.072 41.238 1.00 35.19 O ANISOU 1374 O TYR A 179 4365 4751 4255 -72 -618 302 O ATOM 1375 CB TYR A 179 -8.105 94.222 40.492 1.00 33.24 C ANISOU 1375 CB TYR A 179 4153 4368 4108 58 -759 477 C ATOM 1376 CG TYR A 179 -9.261 95.214 40.550 1.00 38.56 C ANISOU 1376 CG TYR A 179 4746 4989 4917 152 -851 536 C ATOM 1377 CD1 TYR A 179 -10.499 94.859 41.061 1.00 40.04 C ANISOU 1377 CD1 TYR A 179 4773 5205 5237 200 -888 518 C ATOM 1378 CD2 TYR A 179 -9.120 96.488 40.035 1.00 41.47 C ANISOU 1378 CD2 TYR A 179 5195 5276 5285 190 -901 617 C ATOM 1379 CE1 TYR A 179 -11.569 95.760 41.063 1.00 42.25 C ANISOU 1379 CE1 TYR A 179 4962 5438 5654 299 -971 573 C ATOM 1380 CE2 TYR A 179 -10.183 97.389 40.024 1.00 41.54 C ANISOU 1380 CE2 TYR A 179 5132 5226 5426 290 -995 676 C ATOM 1381 CZ TYR A 179 -11.399 97.016 40.553 1.00 46.04 C ANISOU 1381 CZ TYR A 179 5529 5831 6135 351 -1027 651 C ATOM 1382 OH TYR A 179 -12.446 97.912 40.561 1.00 51.47 O ANISOU 1382 OH TYR A 179 6125 6460 6969 464 -1112 707 O ATOM 1383 N PHE A 180 -5.630 92.511 41.352 1.00 32.84 N ANISOU 1383 N PHE A 180 4190 4391 3896 -63 -505 330 N ATOM 1384 CA PHE A 180 -4.666 91.515 40.871 1.00 36.24 C ANISOU 1384 CA PHE A 180 4694 4869 4207 -128 -455 290 C ATOM 1385 C PHE A 180 -4.183 90.602 42.007 1.00 34.65 C ANISOU 1385 C PHE A 180 4436 4690 4039 -133 -354 211 C ATOM 1386 O PHE A 180 -4.315 89.373 41.932 1.00 36.28 O ANISOU 1386 O PHE A 180 4634 4931 4218 -161 -356 167 O ATOM 1387 CB PHE A 180 -3.485 92.228 40.179 1.00 31.31 C ANISOU 1387 CB PHE A 180 4182 4229 3486 -161 -409 328 C ATOM 1388 CG PHE A 180 -2.560 91.292 39.365 1.00 34.28 C ANISOU 1388 CG PHE A 180 4643 4657 3725 -220 -359 296 C ATOM 1389 CD1 PHE A 180 -2.808 91.032 38.028 1.00 44.49 C ANISOU 1389 CD1 PHE A 180 6032 5974 4897 -255 -431 325 C ATOM 1390 CD2 PHE A 180 -1.447 90.699 39.965 1.00 37.77 C ANISOU 1390 CD2 PHE A 180 5069 5122 4160 -234 -242 235 C ATOM 1391 CE1 PHE A 180 -1.951 90.200 37.264 1.00 45.25 C ANISOU 1391 CE1 PHE A 180 6218 6115 4861 -302 -368 285 C ATOM 1392 CE2 PHE A 180 -0.577 89.865 39.224 1.00 42.31 C ANISOU 1392 CE2 PHE A 180 5713 5740 4623 -271 -182 200 C ATOM 1393 CZ PHE A 180 -0.836 89.612 37.875 1.00 43.19 C ANISOU 1393 CZ PHE A 180 5929 5873 4610 -304 -236 219 C ATOM 1394 N ASN A 181 -3.611 91.190 43.065 1.00 26.44 N ANISOU 1394 N ASN A 181 3367 3623 3054 -110 -274 194 N ATOM 1395 CA ASN A 181 -3.094 90.394 44.162 1.00 29.52 C ANISOU 1395 CA ASN A 181 3717 4034 3466 -114 -191 131 C ATOM 1396 C ASN A 181 -4.233 89.751 44.957 1.00 34.71 C ANISOU 1396 C ASN A 181 4283 4702 4202 -92 -206 106 C ATOM 1397 O ASN A 181 -4.272 88.529 45.109 1.00 32.01 O ANISOU 1397 O ASN A 181 3929 4389 3845 -119 -193 70 O ATOM 1398 CB ASN A 181 -2.199 91.242 45.082 1.00 31.87 C ANISOU 1398 CB ASN A 181 4016 4301 3792 -104 -120 121 C ATOM 1399 CG ASN A 181 -1.410 90.378 46.049 1.00 35.49 C ANISOU 1399 CG ASN A 181 4452 4788 4246 -116 -48 66 C ATOM 1400 OD1 ASN A 181 -1.836 90.158 47.182 1.00 36.73 O ANISOU 1400 OD1 ASN A 181 4559 4943 4455 -93 -25 36 O ATOM 1401 ND2 ASN A 181 -0.283 89.827 45.590 1.00 32.80 N ANISOU 1401 ND2 ASN A 181 4148 4475 3840 -148 -12 54 N ATOM 1402 N PHE A 182 -5.187 90.547 45.462 1.00 30.36 N ANISOU 1402 N PHE A 182 3667 4126 3744 -44 -225 124 N ATOM 1403 CA PHE A 182 -6.181 89.963 46.368 1.00 32.82 C ANISOU 1403 CA PHE A 182 3880 4456 4135 -28 -207 98 C ATOM 1404 C PHE A 182 -7.179 89.081 45.608 1.00 31.25 C ANISOU 1404 C PHE A 182 3638 4290 3946 -58 -292 112 C ATOM 1405 O PHE A 182 -7.321 87.893 45.902 1.00 34.39 O ANISOU 1405 O PHE A 182 4014 4713 4339 -99 -275 81 O ATOM 1406 CB PHE A 182 -6.928 91.053 47.168 1.00 29.03 C ANISOU 1406 CB PHE A 182 3333 3941 3756 42 -185 103 C ATOM 1407 CG PHE A 182 -7.981 90.506 48.101 1.00 32.21 C ANISOU 1407 CG PHE A 182 3626 4371 4241 58 -145 79 C ATOM 1408 CD1 PHE A 182 -7.744 89.315 48.821 1.00 35.20 C ANISOU 1408 CD1 PHE A 182 4000 4786 4590 10 -84 43 C ATOM 1409 CD2 PHE A 182 -9.193 91.176 48.286 1.00 39.06 C ANISOU 1409 CD2 PHE A 182 4393 5228 5220 122 -160 96 C ATOM 1410 CE1 PHE A 182 -8.691 88.804 49.685 1.00 34.98 C ANISOU 1410 CE1 PHE A 182 3878 4784 4629 12 -36 29 C ATOM 1411 CE2 PHE A 182 -10.155 90.685 49.178 1.00 42.43 C ANISOU 1411 CE2 PHE A 182 4706 5688 5726 132 -101 75 C ATOM 1412 CZ PHE A 182 -9.905 89.492 49.876 1.00 38.03 C ANISOU 1412 CZ PHE A 182 4154 5170 5126 69 -36 43 C ATOM 1413 N PHE A 183 -7.932 89.656 44.672 1.00 29.62 N ANISOU 1413 N PHE A 183 3416 4077 3762 -40 -395 161 N ATOM 1414 CA PHE A 183 -9.009 88.898 44.035 1.00 34.58 C ANISOU 1414 CA PHE A 183 3986 4737 4415 -73 -494 175 C ATOM 1415 C PHE A 183 -8.456 87.714 43.228 1.00 38.13 C ANISOU 1415 C PHE A 183 4528 5208 4750 -151 -522 148 C ATOM 1416 O PHE A 183 -8.836 86.552 43.445 1.00 37.63 O ANISOU 1416 O PHE A 183 4432 5164 4702 -199 -524 114 O ATOM 1417 CB PHE A 183 -9.846 89.814 43.129 1.00 34.05 C ANISOU 1417 CB PHE A 183 3893 4659 4387 -35 -620 242 C ATOM 1418 CG PHE A 183 -10.794 90.757 43.877 1.00 39.37 C ANISOU 1418 CG PHE A 183 4438 5310 5210 52 -609 264 C ATOM 1419 CD1 PHE A 183 -10.977 90.660 45.249 1.00 45.57 C ANISOU 1419 CD1 PHE A 183 5140 6099 6075 80 -488 218 C ATOM 1420 CD2 PHE A 183 -11.512 91.729 43.187 1.00 42.69 C ANISOU 1420 CD2 PHE A 183 4828 5705 5688 110 -720 331 C ATOM 1421 CE1 PHE A 183 -11.869 91.511 45.923 1.00 43.84 C ANISOU 1421 CE1 PHE A 183 4806 5861 5991 168 -461 228 C ATOM 1422 CE2 PHE A 183 -12.392 92.589 43.861 1.00 46.30 C ANISOU 1422 CE2 PHE A 183 5161 6135 6295 206 -703 346 C ATOM 1423 CZ PHE A 183 -12.556 92.471 45.237 1.00 38.64 C ANISOU 1423 CZ PHE A 183 4108 5172 5404 236 -564 287 C ATOM 1424 N ALA A 184 -7.552 87.993 42.294 1.00 29.52 N ANISOU 1424 N ALA A 184 3561 4110 3544 -165 -536 160 N ATOM 1425 CA ALA A 184 -7.136 86.954 41.354 1.00 36.67 C ANISOU 1425 CA ALA A 184 4564 5033 4334 -228 -567 129 C ATOM 1426 C ALA A 184 -6.117 85.995 41.970 1.00 36.37 C ANISOU 1426 C ALA A 184 4564 4994 4262 -246 -454 65 C ATOM 1427 O ALA A 184 -6.186 84.781 41.739 1.00 37.70 O ANISOU 1427 O ALA A 184 4762 5165 4399 -291 -468 21 O ATOM 1428 CB ALA A 184 -6.567 87.596 40.083 1.00 32.21 C ANISOU 1428 CB ALA A 184 4123 4468 3648 -238 -611 167 C ATOM 1429 N CYS A 185 -5.152 86.509 42.733 1.00 32.49 N ANISOU 1429 N CYS A 185 4075 4492 3779 -212 -352 59 N ATOM 1430 CA CYS A 185 -4.025 85.695 43.175 1.00 30.35 C ANISOU 1430 CA CYS A 185 3842 4220 3469 -220 -258 9 C ATOM 1431 C CYS A 185 -4.169 85.087 44.565 1.00 32.57 C ANISOU 1431 C CYS A 185 4052 4494 3828 -211 -202 -18 C ATOM 1432 O CYS A 185 -3.426 84.150 44.877 1.00 34.81 O ANISOU 1432 O CYS A 185 4368 4772 4086 -219 -151 -55 O ATOM 1433 CB CYS A 185 -2.726 86.521 43.137 1.00 33.35 C ANISOU 1433 CB CYS A 185 4267 4599 3804 -201 -187 19 C ATOM 1434 SG CYS A 185 -2.252 86.832 41.413 1.00 39.40 S ANISOU 1434 SG CYS A 185 5152 5380 4439 -231 -218 43 S ATOM 1435 N VAL A 186 -5.089 85.580 45.404 1.00 30.08 N ANISOU 1435 N VAL A 186 3647 4179 3604 -190 -206 2 N ATOM 1436 CA VAL A 186 -5.224 85.075 46.767 1.00 33.00 C ANISOU 1436 CA VAL A 186 3963 4546 4030 -186 -141 -17 C ATOM 1437 C VAL A 186 -6.599 84.463 46.960 1.00 35.01 C ANISOU 1437 C VAL A 186 4138 4810 4355 -215 -178 -9 C ATOM 1438 O VAL A 186 -6.734 83.304 47.380 1.00 35.87 O ANISOU 1438 O VAL A 186 4246 4912 4472 -255 -160 -28 O ATOM 1439 CB VAL A 186 -4.988 86.183 47.817 1.00 34.57 C ANISOU 1439 CB VAL A 186 4130 4739 4266 -139 -79 -10 C ATOM 1440 CG1 VAL A 186 -5.371 85.673 49.251 1.00 30.09 C ANISOU 1440 CG1 VAL A 186 3513 4176 3744 -139 -13 -26 C ATOM 1441 CG2 VAL A 186 -3.539 86.631 47.765 1.00 32.32 C ANISOU 1441 CG2 VAL A 186 3914 4446 3920 -129 -41 -19 C ATOM 1442 N LEU A 187 -7.627 85.252 46.690 1.00 33.00 N ANISOU 1442 N LEU A 187 3809 4566 4164 -196 -231 22 N ATOM 1443 CA LEU A 187 -8.969 84.806 46.996 1.00 35.16 C ANISOU 1443 CA LEU A 187 3972 4858 4530 -221 -256 34 C ATOM 1444 C LEU A 187 -9.411 83.655 46.074 1.00 34.73 C ANISOU 1444 C LEU A 187 3937 4806 4455 -298 -347 26 C ATOM 1445 O LEU A 187 -10.050 82.702 46.532 1.00 34.91 O ANISOU 1445 O LEU A 187 3907 4831 4528 -353 -339 19 O ATOM 1446 CB LEU A 187 -9.911 86.004 46.919 1.00 38.52 C ANISOU 1446 CB LEU A 187 4300 5293 5042 -165 -292 70 C ATOM 1447 CG LEU A 187 -11.329 85.738 47.390 1.00 52.66 C ANISOU 1447 CG LEU A 187 5940 7113 6956 -177 -297 84 C ATOM 1448 CD1 LEU A 187 -11.280 85.358 48.868 1.00 50.97 C ANISOU 1448 CD1 LEU A 187 5695 6905 6766 -179 -160 60 C ATOM 1449 CD2 LEU A 187 -12.198 86.964 47.164 1.00 52.68 C ANISOU 1449 CD2 LEU A 187 5843 7119 7054 -101 -344 121 C ATOM 1450 N VAL A 188 -9.113 83.718 44.772 1.00 33.88 N ANISOU 1450 N VAL A 188 3912 4694 4267 -313 -435 27 N ATOM 1451 CA VAL A 188 -9.503 82.612 43.885 1.00 35.18 C ANISOU 1451 CA VAL A 188 4117 4853 4397 -391 -527 6 C ATOM 1452 C VAL A 188 -8.819 81.310 44.301 1.00 38.77 C ANISOU 1452 C VAL A 188 4645 5273 4812 -432 -461 -43 C ATOM 1453 O VAL A 188 -9.517 80.295 44.448 1.00 35.58 O ANISOU 1453 O VAL A 188 4210 4854 4453 -500 -491 -55 O ATOM 1454 CB VAL A 188 -9.250 82.982 42.414 1.00 38.95 C ANISOU 1454 CB VAL A 188 4694 5335 4771 -397 -626 13 C ATOM 1455 CG1 VAL A 188 -9.285 81.701 41.516 1.00 38.01 C ANISOU 1455 CG1 VAL A 188 4670 5198 4574 -480 -698 -35 C ATOM 1456 CG2 VAL A 188 -10.303 83.965 41.942 1.00 39.09 C ANISOU 1456 CG2 VAL A 188 4624 5378 4850 -375 -735 73 C ATOM 1457 N PRO A 189 -7.496 81.272 44.545 1.00 33.79 N ANISOU 1457 N PRO A 189 4102 4624 4112 -393 -375 -68 N ATOM 1458 CA PRO A 189 -6.892 80.033 45.059 1.00 33.97 C ANISOU 1458 CA PRO A 189 4182 4605 4118 -415 -316 -107 C ATOM 1459 C PRO A 189 -7.443 79.579 46.392 1.00 36.78 C ANISOU 1459 C PRO A 189 4459 4954 4563 -434 -262 -89 C ATOM 1460 O PRO A 189 -7.581 78.369 46.602 1.00 42.06 O ANISOU 1460 O PRO A 189 5158 5580 5243 -488 -262 -105 O ATOM 1461 CB PRO A 189 -5.401 80.393 45.172 1.00 35.39 C ANISOU 1461 CB PRO A 189 4432 4782 4231 -353 -236 -123 C ATOM 1462 CG PRO A 189 -5.200 81.432 44.143 1.00 41.55 C ANISOU 1462 CG PRO A 189 5241 5591 4954 -331 -275 -108 C ATOM 1463 CD PRO A 189 -6.458 82.268 44.208 1.00 35.01 C ANISOU 1463 CD PRO A 189 4314 4789 4199 -334 -338 -61 C ATOM 1464 N LEU A 190 -7.725 80.491 47.329 1.00 34.04 N ANISOU 1464 N LEU A 190 4024 4640 4270 -393 -207 -56 N ATOM 1465 CA LEU A 190 -8.314 80.040 48.585 1.00 32.66 C ANISOU 1465 CA LEU A 190 3781 4465 4163 -419 -143 -38 C ATOM 1466 C LEU A 190 -9.664 79.376 48.351 1.00 34.79 C ANISOU 1466 C LEU A 190 3972 4738 4510 -500 -201 -23 C ATOM 1467 O LEU A 190 -9.990 78.382 49.004 1.00 32.94 O ANISOU 1467 O LEU A 190 3730 4478 4308 -561 -168 -16 O ATOM 1468 CB LEU A 190 -8.468 81.198 49.576 1.00 34.60 C ANISOU 1468 CB LEU A 190 3953 4746 4446 -359 -69 -17 C ATOM 1469 CG LEU A 190 -7.201 81.783 50.204 1.00 38.77 C ANISOU 1469 CG LEU A 190 4549 5269 4913 -297 -3 -29 C ATOM 1470 CD1 LEU A 190 -7.594 83.026 51.054 1.00 41.38 C ANISOU 1470 CD1 LEU A 190 4811 5628 5285 -245 56 -18 C ATOM 1471 CD2 LEU A 190 -6.452 80.726 51.039 1.00 40.11 C ANISOU 1471 CD2 LEU A 190 4786 5409 5044 -315 48 -35 C ATOM 1472 N LEU A 191 -10.491 79.944 47.476 1.00 34.52 N ANISOU 1472 N LEU A 191 3868 4735 4512 -507 -292 -11 N ATOM 1473 CA LEU A 191 -11.783 79.325 47.203 1.00 35.91 C ANISOU 1473 CA LEU A 191 3950 4920 4773 -593 -365 4 C ATOM 1474 C LEU A 191 -11.611 77.960 46.535 1.00 42.46 C ANISOU 1474 C LEU A 191 4884 5693 5557 -682 -431 -31 C ATOM 1475 O LEU A 191 -12.384 77.028 46.802 1.00 40.04 O ANISOU 1475 O LEU A 191 4531 5368 5316 -775 -446 -23 O ATOM 1476 CB LEU A 191 -12.625 80.252 46.322 1.00 36.48 C ANISOU 1476 CB LEU A 191 3931 5037 4891 -573 -473 29 C ATOM 1477 CG LEU A 191 -13.049 81.566 46.987 1.00 44.96 C ANISOU 1477 CG LEU A 191 4885 6154 6043 -484 -414 62 C ATOM 1478 CD1 LEU A 191 -13.897 82.417 46.042 1.00 48.26 C ANISOU 1478 CD1 LEU A 191 5214 6604 6517 -456 -540 95 C ATOM 1479 CD2 LEU A 191 -13.814 81.304 48.270 1.00 46.19 C ANISOU 1479 CD2 LEU A 191 4916 6334 6302 -504 -306 79 C ATOM 1480 N LEU A 192 -10.630 77.838 45.633 1.00 39.02 N ANISOU 1480 N LEU A 192 4590 5226 5009 -659 -467 -72 N ATOM 1481 CA LEU A 192 -10.335 76.542 45.019 1.00 40.58 C ANISOU 1481 CA LEU A 192 4910 5356 5153 -727 -513 -121 C ATOM 1482 C LEU A 192 -9.938 75.522 46.076 1.00 39.54 C ANISOU 1482 C LEU A 192 4817 5163 5043 -747 -421 -124 C ATOM 1483 O LEU A 192 -10.374 74.364 46.036 1.00 39.84 O ANISOU 1483 O LEU A 192 4886 5140 5110 -838 -456 -138 O ATOM 1484 CB LEU A 192 -9.198 76.681 43.996 1.00 40.23 C ANISOU 1484 CB LEU A 192 5012 5295 4979 -676 -528 -169 C ATOM 1485 CG LEU A 192 -9.458 77.514 42.745 1.00 46.11 C ANISOU 1485 CG LEU A 192 5771 6085 5665 -669 -630 -166 C ATOM 1486 CD1 LEU A 192 -8.207 77.561 41.865 1.00 47.14 C ANISOU 1486 CD1 LEU A 192 6056 6199 5656 -623 -606 -213 C ATOM 1487 CD2 LEU A 192 -10.638 76.921 41.983 1.00 51.58 C ANISOU 1487 CD2 LEU A 192 6442 6772 6385 -773 -774 -174 C ATOM 1488 N MET A 193 -9.102 75.943 47.029 1.00 37.86 N ANISOU 1488 N MET A 193 4610 4960 4814 -668 -313 -107 N ATOM 1489 CA MET A 193 -8.659 75.058 48.101 1.00 37.27 C ANISOU 1489 CA MET A 193 4581 4831 4751 -676 -233 -97 C ATOM 1490 C MET A 193 -9.828 74.598 48.957 1.00 38.48 C ANISOU 1490 C MET A 193 4638 4986 4997 -762 -211 -50 C ATOM 1491 O MET A 193 -9.882 73.436 49.376 1.00 45.68 O ANISOU 1491 O MET A 193 5603 5825 5927 -827 -197 -42 O ATOM 1492 CB MET A 193 -7.630 75.770 48.979 1.00 39.12 C ANISOU 1492 CB MET A 193 4824 5091 4947 -579 -140 -82 C ATOM 1493 CG MET A 193 -6.223 75.748 48.433 1.00 42.35 C ANISOU 1493 CG MET A 193 5341 5475 5275 -508 -133 -123 C ATOM 1494 SD MET A 193 -5.199 76.710 49.578 1.00 42.80 S ANISOU 1494 SD MET A 193 5377 5575 5311 -415 -43 -97 S ATOM 1495 CE MET A 193 -4.594 78.053 48.542 1.00 46.45 C ANISOU 1495 CE MET A 193 5835 6092 5722 -355 -63 -119 C ATOM 1496 N LEU A 194 -10.759 75.507 49.249 1.00 38.52 N ANISOU 1496 N LEU A 194 4500 5070 5068 -762 -199 -15 N ATOM 1497 CA LEU A 194 -11.956 75.132 49.987 1.00 40.27 C ANISOU 1497 CA LEU A 194 4605 5307 5388 -847 -165 29 C ATOM 1498 C LEU A 194 -12.728 74.046 49.249 1.00 40.30 C ANISOU 1498 C LEU A 194 4609 5263 5441 -973 -265 19 C ATOM 1499 O LEU A 194 -13.210 73.083 49.866 1.00 41.63 O ANISOU 1499 O LEU A 194 4769 5387 5660 -1069 -232 48 O ATOM 1500 CB LEU A 194 -12.831 76.367 50.216 1.00 44.70 C ANISOU 1500 CB LEU A 194 5000 5963 6022 -807 -142 57 C ATOM 1501 CG LEU A 194 -14.237 76.135 50.778 1.00 59.37 C ANISOU 1501 CG LEU A 194 6694 7860 8003 -892 -109 101 C ATOM 1502 CD1 LEU A 194 -14.167 75.614 52.212 1.00 60.94 C ANISOU 1502 CD1 LEU A 194 6910 8045 8198 -921 34 136 C ATOM 1503 CD2 LEU A 194 -15.072 77.417 50.697 1.00 62.82 C ANISOU 1503 CD2 LEU A 194 6963 8384 8523 -829 -109 116 C ATOM 1504 N GLY A 195 -12.859 74.185 47.928 1.00 38.69 N ANISOU 1504 N GLY A 195 4424 5061 5215 -984 -391 -20 N ATOM 1505 CA GLY A 195 -13.630 73.214 47.169 1.00 40.23 C ANISOU 1505 CA GLY A 195 4625 5210 5450 -1112 -506 -38 C ATOM 1506 C GLY A 195 -12.958 71.853 47.125 1.00 40.52 C ANISOU 1506 C GLY A 195 4834 5125 5436 -1163 -505 -76 C ATOM 1507 O GLY A 195 -13.628 70.817 47.215 1.00 44.03 O ANISOU 1507 O GLY A 195 5278 5509 5944 -1288 -539 -68 O ATOM 1508 N VAL A 196 -11.631 71.842 46.990 1.00 37.42 N ANISOU 1508 N VAL A 196 4586 4691 4940 -1065 -465 -115 N ATOM 1509 CA VAL A 196 -10.873 70.595 46.994 1.00 39.97 C ANISOU 1509 CA VAL A 196 5074 4890 5222 -1082 -453 -153 C ATOM 1510 C VAL A 196 -11.024 69.875 48.337 1.00 37.37 C ANISOU 1510 C VAL A 196 4734 4511 4955 -1127 -364 -92 C ATOM 1511 O VAL A 196 -11.360 68.689 48.373 1.00 37.59 O ANISOU 1511 O VAL A 196 4825 4436 5020 -1230 -393 -93 O ATOM 1512 CB VAL A 196 -9.396 70.855 46.635 1.00 39.36 C ANISOU 1512 CB VAL A 196 5120 4797 5038 -951 -414 -202 C ATOM 1513 CG1 VAL A 196 -8.571 69.563 46.798 1.00 38.56 C ANISOU 1513 CG1 VAL A 196 5175 4561 4915 -944 -387 -235 C ATOM 1514 CG2 VAL A 196 -9.286 71.380 45.178 1.00 38.79 C ANISOU 1514 CG2 VAL A 196 5090 4761 4888 -931 -502 -263 C ATOM 1515 N TYR A 197 -10.811 70.578 49.461 1.00 34.50 N ANISOU 1515 N TYR A 197 4299 4212 4595 -1060 -257 -35 N ATOM 1516 CA TYR A 197 -11.024 69.944 50.768 1.00 39.87 C ANISOU 1516 CA TYR A 197 4976 4856 5317 -1111 -170 33 C ATOM 1517 C TYR A 197 -12.447 69.422 50.927 1.00 45.28 C ANISOU 1517 C TYR A 197 5558 5541 6107 -1265 -189 74 C ATOM 1518 O TYR A 197 -12.654 68.348 51.501 1.00 41.38 O ANISOU 1518 O TYR A 197 5119 4958 5645 -1357 -163 113 O ATOM 1519 CB TYR A 197 -10.675 70.905 51.920 1.00 38.41 C ANISOU 1519 CB TYR A 197 4733 4756 5105 -1021 -58 80 C ATOM 1520 CG TYR A 197 -9.188 70.881 52.167 1.00 38.35 C ANISOU 1520 CG TYR A 197 4852 4708 5010 -906 -31 63 C ATOM 1521 CD1 TYR A 197 -8.570 69.718 52.653 1.00 40.38 C ANISOU 1521 CD1 TYR A 197 5238 4852 5251 -916 -19 83 C ATOM 1522 CD2 TYR A 197 -8.383 71.976 51.836 1.00 35.21 C ANISOU 1522 CD2 TYR A 197 4445 4377 4557 -790 -28 28 C ATOM 1523 CE1 TYR A 197 -7.195 69.654 52.845 1.00 39.63 C ANISOU 1523 CE1 TYR A 197 5243 4721 5093 -804 -6 69 C ATOM 1524 CE2 TYR A 197 -7.004 71.919 51.991 1.00 30.71 C ANISOU 1524 CE2 TYR A 197 3973 3775 3922 -692 -10 11 C ATOM 1525 CZ TYR A 197 -6.411 70.757 52.517 1.00 39.67 C ANISOU 1525 CZ TYR A 197 5218 4806 5049 -695 0 31 C ATOM 1526 OH TYR A 197 -5.041 70.692 52.689 1.00 38.26 O ANISOU 1526 OH TYR A 197 5115 4600 4822 -589 10 19 O ATOM 1527 N ALEU A 198 -13.443 70.164 50.429 0.50 43.95 N ANISOU 1527 N ALEU A 198 5232 5467 5999 -1298 -236 73 N ATOM 1528 N BLEU A 198 -13.441 70.165 50.430 0.50 43.95 N ANISOU 1528 N BLEU A 198 5233 5467 5999 -1297 -235 73 N ATOM 1529 CA ALEU A 198 -14.820 69.680 50.496 0.50 43.95 C ANISOU 1529 CA ALEU A 198 5107 5477 6117 -1450 -263 111 C ATOM 1530 CA BLEU A 198 -14.817 69.681 50.494 0.50 43.95 C ANISOU 1530 CA BLEU A 198 5107 5476 6116 -1450 -263 111 C ATOM 1531 C ALEU A 198 -14.981 68.381 49.718 0.50 43.89 C ANISOU 1531 C ALEU A 198 5208 5345 6125 -1575 -375 74 C ATOM 1532 C BLEU A 198 -14.970 68.377 49.724 0.50 43.91 C ANISOU 1532 C BLEU A 198 5212 5346 6126 -1574 -374 74 C ATOM 1533 O ALEU A 198 -15.664 67.454 50.175 0.50 42.32 O ANISOU 1533 O ALEU A 198 4991 5086 6002 -1715 -361 117 O ATOM 1534 O BLEU A 198 -15.634 67.442 50.193 0.50 42.31 O ANISOU 1534 O BLEU A 198 4994 5083 5999 -1713 -359 117 O ATOM 1535 CB ALEU A 198 -15.785 70.745 49.968 0.50 44.64 C ANISOU 1535 CB ALEU A 198 4999 5687 6274 -1444 -316 112 C ATOM 1536 CB BLEU A 198 -15.773 70.740 49.947 0.50 44.62 C ANISOU 1536 CB BLEU A 198 5000 5684 6270 -1443 -319 111 C ATOM 1537 CG ALEU A 198 -16.219 71.846 50.939 0.50 43.10 C ANISOU 1537 CG ALEU A 198 4642 5609 6125 -1374 -192 163 C ATOM 1538 CG BLEU A 198 -17.255 70.370 49.930 0.50 49.00 C ANISOU 1538 CG BLEU A 198 5380 6271 6968 -1596 -359 151 C ATOM 1539 CD1ALEU A 198 -17.108 72.854 50.231 0.50 44.32 C ANISOU 1539 CD1ALEU A 198 4616 5864 6358 -1350 -270 159 C ATOM 1540 CD1BLEU A 198 -17.789 70.172 51.348 0.50 46.08 C ANISOU 1540 CD1BLEU A 198 4915 5928 6665 -1650 -197 229 C ATOM 1541 CD2ALEU A 198 -16.949 71.240 52.120 0.50 45.37 C ANISOU 1541 CD2ALEU A 198 4852 5897 6488 -1478 -72 233 C ATOM 1542 CD2BLEU A 198 -18.045 71.441 49.196 0.50 53.41 C ANISOU 1542 CD2BLEU A 198 5761 6941 7591 -1562 -447 145 C ATOM 1543 N ARG A 199 -14.342 68.291 48.545 1.00 43.44 N ANISOU 1543 N ARG A 199 5274 5240 5990 -1531 -479 -8 N ATOM 1544 CA ARG A 199 -14.368 67.053 47.768 1.00 46.60 C ANISOU 1544 CA ARG A 199 5813 5506 6385 -1636 -583 -64 C ATOM 1545 C ARG A 199 -13.626 65.915 48.472 1.00 40.66 C ANISOU 1545 C ARG A 199 5226 4609 5615 -1642 -514 -52 C ATOM 1546 O ARG A 199 -14.029 64.755 48.358 1.00 45.30 O ANISOU 1546 O ARG A 199 5888 5074 6250 -1773 -564 -58 O ATOM 1547 CB ARG A 199 -13.775 67.298 46.378 1.00 45.43 C ANISOU 1547 CB ARG A 199 5775 5349 6136 -1571 -689 -161 C ATOM 1548 CG ARG A 199 -14.619 68.227 45.504 1.00 52.65 C ANISOU 1548 CG ARG A 199 6553 6383 7069 -1591 -799 -169 C ATOM 1549 CD ARG A 199 -14.065 68.342 44.068 1.00 55.67 C ANISOU 1549 CD ARG A 199 7076 6748 7329 -1549 -910 -263 C ATOM 1550 N ILE A 200 -12.555 66.215 49.206 1.00 38.82 N ANISOU 1550 N ILE A 200 5054 4379 5317 -1504 -409 -31 N ATOM 1551 CA ILE A 200 -11.883 65.170 49.981 1.00 41.95 C ANISOU 1551 CA ILE A 200 5595 4640 5703 -1501 -350 -1 C ATOM 1552 C ILE A 200 -12.834 64.573 51.019 1.00 44.44 C ANISOU 1552 C ILE A 200 5847 4931 6109 -1644 -296 97 C ATOM 1553 O ILE A 200 -13.014 63.347 51.106 1.00 41.11 O ANISOU 1553 O ILE A 200 5530 4363 5728 -1753 -322 111 O ATOM 1554 CB ILE A 200 -10.607 65.732 50.631 1.00 41.74 C ANISOU 1554 CB ILE A 200 5617 4646 5598 -1328 -261 14 C ATOM 1555 CG1 ILE A 200 -9.552 66.039 49.570 1.00 40.62 C ANISOU 1555 CG1 ILE A 200 5563 4497 5373 -1202 -306 -83 C ATOM 1556 CG2 ILE A 200 -10.052 64.760 51.721 1.00 42.81 C ANISOU 1556 CG2 ILE A 200 5871 4661 5734 -1325 -198 79 C ATOM 1557 CD1 ILE A 200 -8.335 66.801 50.147 1.00 39.09 C ANISOU 1557 CD1 ILE A 200 5376 4364 5114 -1038 -226 -68 C ATOM 1558 N PHE A 201 -13.463 65.430 51.825 1.00 43.63 N ANISOU 1558 N PHE A 201 5575 4965 6039 -1649 -211 166 N ATOM 1559 CA PHE A 201 -14.357 64.913 52.859 1.00 43.36 C ANISOU 1559 CA PHE A 201 5473 4920 6080 -1785 -132 264 C ATOM 1560 C PHE A 201 -15.560 64.196 52.265 1.00 45.84 C ANISOU 1560 C PHE A 201 5720 5191 6505 -1978 -219 261 C ATOM 1561 O PHE A 201 -16.033 63.207 52.838 1.00 48.48 O ANISOU 1561 O PHE A 201 6088 5432 6898 -2119 -189 325 O ATOM 1562 CB PHE A 201 -14.798 66.046 53.783 1.00 47.21 C ANISOU 1562 CB PHE A 201 5791 5573 6575 -1741 -10 323 C ATOM 1563 CG PHE A 201 -13.657 66.720 54.482 1.00 47.80 C ANISOU 1563 CG PHE A 201 5937 5684 6540 -1574 69 330 C ATOM 1564 CD1 PHE A 201 -12.775 65.983 55.256 1.00 51.50 C ANISOU 1564 CD1 PHE A 201 6572 6051 6945 -1544 111 372 C ATOM 1565 CD2 PHE A 201 -13.477 68.085 54.391 1.00 49.66 C ANISOU 1565 CD2 PHE A 201 6074 6052 6741 -1452 94 298 C ATOM 1566 CE1 PHE A 201 -11.711 66.603 55.919 1.00 51.48 C ANISOU 1566 CE1 PHE A 201 6628 6088 6844 -1397 168 380 C ATOM 1567 CE2 PHE A 201 -12.419 68.711 55.044 1.00 50.80 C ANISOU 1567 CE2 PHE A 201 6284 6228 6789 -1313 158 301 C ATOM 1568 CZ PHE A 201 -11.538 67.967 55.804 1.00 52.25 C ANISOU 1568 CZ PHE A 201 6625 6320 6909 -1288 190 341 C ATOM 1569 N LEU A 202 -16.076 64.664 51.122 1.00 41.17 N ANISOU 1569 N LEU A 202 5036 4662 5945 -1996 -335 193 N ATOM 1570 CA LEU A 202 -17.189 63.948 50.488 1.00 47.27 C ANISOU 1570 CA LEU A 202 5748 5389 6823 -2189 -444 184 C ATOM 1571 C LEU A 202 -16.753 62.579 49.990 1.00 47.18 C ANISOU 1571 C LEU A 202 5960 5174 6792 -2266 -529 134 C ATOM 1572 O LEU A 202 -17.502 61.603 50.103 1.00 45.25 O ANISOU 1572 O LEU A 202 5719 4835 6637 -2450 -561 167 O ATOM 1573 CB LEU A 202 -17.765 64.772 49.332 1.00 48.96 C ANISOU 1573 CB LEU A 202 5831 5714 7059 -2181 -573 123 C ATOM 1574 CG LEU A 202 -18.771 65.842 49.739 1.00 58.98 C ANISOU 1574 CG LEU A 202 6829 7161 8421 -2182 -521 183 C ATOM 1575 CD1 LEU A 202 -18.884 66.901 48.654 1.00 62.85 C ANISOU 1575 CD1 LEU A 202 7235 7755 8888 -2094 -638 125 C ATOM 1576 CD2 LEU A 202 -20.139 65.170 50.013 1.00 58.74 C ANISOU 1576 CD2 LEU A 202 6640 7130 8547 -2397 -535 244 C ATOM 1577 N ALA A 203 -15.551 62.486 49.418 1.00 46.74 N ANISOU 1577 N ALA A 203 6090 5043 6625 -2129 -562 53 N ATOM 1578 CA ALA A 203 -15.077 61.195 48.916 1.00 45.66 C ANISOU 1578 CA ALA A 203 6178 4700 6470 -2179 -633 -9 C ATOM 1579 C ALA A 203 -14.874 60.207 50.060 1.00 48.04 C ANISOU 1579 C ALA A 203 6581 4866 6806 -2230 -543 80 C ATOM 1580 O ALA A 203 -15.256 59.043 49.957 1.00 51.39 O ANISOU 1580 O ALA A 203 7106 5129 7291 -2379 -597 81 O ATOM 1581 CB ALA A 203 -13.770 61.384 48.133 1.00 43.60 C ANISOU 1581 CB ALA A 203 6078 4402 6084 -1999 -658 -113 C ATOM 1582 N ALA A 204 -14.267 60.656 51.160 1.00 44.27 N ANISOU 1582 N ALA A 204 6091 4445 6286 -2112 -412 157 N ATOM 1583 CA ALA A 204 -14.100 59.784 52.315 1.00 47.60 C ANISOU 1583 CA ALA A 204 6611 4749 6727 -2160 -329 259 C ATOM 1584 C ALA A 204 -15.444 59.317 52.845 1.00 53.54 C ANISOU 1584 C ALA A 204 7250 5500 7591 -2383 -303 350 C ATOM 1585 O ALA A 204 -15.611 58.142 53.189 1.00 57.05 O ANISOU 1585 O ALA A 204 7816 5776 8084 -2509 -308 400 O ATOM 1586 CB ALA A 204 -13.318 60.519 53.406 1.00 45.73 C ANISOU 1586 CB ALA A 204 6357 4606 6412 -2003 -204 328 C ATOM 1587 N AARG A 205 -16.423 60.222 52.915 0.50 54.82 N ANISOU 1587 N AARG A 205 7177 5847 7807 -2436 -273 375 N ATOM 1588 N BARG A 205 -16.419 60.224 52.919 0.50 54.80 N ANISOU 1588 N BARG A 205 7174 5844 7803 -2435 -272 376 N ATOM 1589 CA AARG A 205 -17.722 59.848 53.469 0.50 58.71 C ANISOU 1589 CA AARG A 205 7528 6361 8417 -2646 -227 467 C ATOM 1590 CA BARG A 205 -17.722 59.858 53.469 0.50 58.71 C ANISOU 1590 CA BARG A 205 7526 6362 8417 -2645 -227 467 C ATOM 1591 C AARG A 205 -18.436 58.839 52.574 0.50 59.36 C ANISOU 1591 C AARG A 205 7645 6312 8597 -2843 -370 423 C ATOM 1592 C BARG A 205 -18.453 58.861 52.574 0.50 59.34 C ANISOU 1592 C BARG A 205 7638 6314 8595 -2843 -370 423 C ATOM 1593 O AARG A 205 -19.123 57.936 53.071 0.50 58.80 O ANISOU 1593 O AARG A 205 7579 6148 8614 -3035 -345 502 O ATOM 1594 O BARG A 205 -19.157 57.976 53.078 0.50 58.83 O ANISOU 1594 O BARG A 205 7573 6161 8621 -3036 -343 503 O ATOM 1595 CB AARG A 205 -18.584 61.096 53.677 0.50 61.79 C ANISOU 1595 CB AARG A 205 7641 6981 8854 -2635 -162 493 C ATOM 1596 CB BARG A 205 -18.554 61.125 53.695 0.50 61.67 C ANISOU 1596 CB BARG A 205 7627 6968 8835 -2628 -159 493 C ATOM 1597 CG AARG A 205 -19.911 60.812 54.376 0.50 70.05 C ANISOU 1597 CG AARG A 205 8509 8078 10030 -2837 -80 596 C ATOM 1598 CG BARG A 205 -20.029 60.881 53.982 0.50 70.00 C ANISOU 1598 CG BARG A 205 8478 8079 10040 -2844 -129 566 C ATOM 1599 CD AARG A 205 -20.859 62.008 54.317 0.50 74.13 C ANISOU 1599 CD AARG A 205 8732 8813 10623 -2823 -43 599 C ATOM 1600 CD BARG A 205 -20.691 62.125 54.574 0.50 73.87 C ANISOU 1600 CD BARG A 205 8712 8791 10565 -2789 -5 611 C ATOM 1601 NE AARG A 205 -21.562 62.105 53.039 0.50 77.48 N ANISOU 1601 NE AARG A 205 9037 9264 11138 -2897 -220 524 N ATOM 1602 NE BARG A 205 -20.433 62.245 56.007 0.50 73.75 N ANISOU 1602 NE BARG A 205 8727 8808 10487 -2748 193 708 N ATOM 1603 CZ AARG A 205 -22.312 63.143 52.683 0.50 81.30 C ANISOU 1603 CZ AARG A 205 9278 9921 11694 -2864 -243 509 C ATOM 1604 CZ BARG A 205 -21.170 61.657 56.941 0.50 75.61 C ANISOU 1604 CZ BARG A 205 8911 9034 10785 -2911 316 818 C ATOM 1605 NH1AARG A 205 -22.919 63.156 51.506 0.50 82.85 N ANISOU 1605 NH1AARG A 205 9385 10133 11963 -2938 -426 448 N ATOM 1606 NH1BARG A 205 -20.867 61.808 58.223 0.50 76.95 N ANISOU 1606 NH1BARG A 205 9132 9237 10868 -2864 492 902 N ATOM 1607 NH2AARG A 205 -22.449 64.172 53.507 0.50 82.45 N ANISOU 1607 NH2AARG A 205 9276 10217 11834 -2753 -87 555 N ATOM 1608 NH2BARG A 205 -22.211 60.914 56.591 0.50 76.56 N ANISOU 1608 NH2BARG A 205 8931 9111 11049 -3129 260 844 N ATOM 1609 N ARG A 206 -18.270 58.964 51.253 1.00 58.46 N ANISOU 1609 N ARG A 206 7570 6183 8460 -2807 -522 297 N ATOM 1610 CA ARG A 206 -18.916 58.028 50.329 1.00 60.96 C ANISOU 1610 CA ARG A 206 7938 6372 8853 -2995 -678 237 C ATOM 1611 C ARG A 206 -18.267 56.647 50.373 1.00 62.26 C ANISOU 1611 C ARG A 206 8382 6275 8998 -3038 -703 221 C ATOM 1612 O ARG A 206 -18.949 55.631 50.206 1.00 65.99 O ANISOU 1612 O ARG A 206 8902 6609 9564 -3247 -774 229 O ATOM 1613 CB ARG A 206 -18.862 58.592 48.905 1.00 65.09 C ANISOU 1613 CB ARG A 206 8449 6956 9327 -2935 -833 104 C ATOM 1614 CG ARG A 206 -19.444 57.678 47.833 1.00 75.88 C ANISOU 1614 CG ARG A 206 9896 8192 10744 -3119 -1016 20 C ATOM 1615 CD ARG A 206 -20.938 57.503 48.034 1.00 89.10 C ANISOU 1615 CD ARG A 206 11346 9926 12582 -3359 -1055 94 C ATOM 1616 NE ARG A 206 -21.566 56.780 46.932 1.00 99.04 N ANISOU 1616 NE ARG A 206 12643 11115 13872 -3456 -1216 -6 N ATOM 1617 CZ ARG A 206 -22.818 56.342 46.949 1.00105.66 C ANISOU 1617 CZ ARG A 206 13318 11984 14842 -3610 -1243 26 C ATOM 1618 NH1 ARG A 206 -23.576 56.548 48.019 1.00108.50 N ANISOU 1618 NH1 ARG A 206 13465 12445 15317 -3676 -1106 152 N ATOM 1619 NH2 ARG A 206 -23.310 55.695 45.901 1.00108.84 N ANISOU 1619 NH2 ARG A 206 13775 12320 15258 -3697 -1400 -72 N ATOM 1620 N GLN A 207 -16.944 56.590 50.552 1.00 61.42 N ANISOU 1620 N GLN A 207 8462 6092 8781 -2841 -653 194 N ATOM 1621 CA GLN A 207 -16.260 55.301 50.630 1.00 60.28 C ANISOU 1621 CA GLN A 207 8584 5692 8629 -2852 -673 181 C ATOM 1622 C GLN A 207 -16.615 54.570 51.917 1.00 57.17 C ANISOU 1622 C GLN A 207 8212 5208 8301 -2977 -572 335 C ATOM 1623 O GLN A 207 -16.881 53.362 51.900 1.00 63.58 O ANISOU 1623 O GLN A 207 9166 5810 9181 -3132 -622 351 O ATOM 1624 CB GLN A 207 -14.748 55.511 50.507 1.00 58.09 C ANISOU 1624 CB GLN A 207 8465 5377 8230 -2593 -643 118 C ATOM 1625 CG GLN A 207 -14.401 56.183 49.197 1.00 58.05 C ANISOU 1625 CG GLN A 207 8453 5453 8149 -2485 -732 -31 C ATOM 1626 CD GLN A 207 -12.913 56.368 48.961 1.00 64.98 C ANISOU 1626 CD GLN A 207 9475 6297 8918 -2241 -698 -102 C ATOM 1627 OE1 GLN A 207 -12.078 55.769 49.639 1.00 72.72 O ANISOU 1627 OE1 GLN A 207 10594 7148 9889 -2152 -637 -58 O ATOM 1628 NE2 GLN A 207 -12.576 57.206 47.985 1.00 59.07 N ANISOU 1628 NE2 GLN A 207 8690 5665 8089 -2133 -739 -206 N ATOM 1629 N LEU A 208 -16.650 55.291 53.037 1.00 53.78 N ANISOU 1629 N LEU A 208 7653 4933 7850 -2920 -428 451 N ATOM 1630 CA LEU A 208 -17.068 54.686 54.298 1.00 52.30 C ANISOU 1630 CA LEU A 208 7478 4685 7707 -3050 -317 609 C ATOM 1631 C LEU A 208 -18.497 54.170 54.206 1.00 57.40 C ANISOU 1631 C LEU A 208 7998 5317 8494 -3333 -346 654 C ATOM 1632 O LEU A 208 -18.802 53.066 54.683 1.00 63.84 O ANISOU 1632 O LEU A 208 8906 5983 9366 -3442 -320 723 O ATOM 1633 CB LEU A 208 -16.914 55.712 55.425 1.00 58.68 C ANISOU 1633 CB LEU A 208 8157 5691 8446 -2937 -158 704 C ATOM 1634 CG LEU A 208 -15.455 55.944 55.848 1.00 66.34 C ANISOU 1634 CG LEU A 208 9284 6635 9287 -2694 -122 701 C ATOM 1635 CD1 LEU A 208 -15.205 57.320 56.462 1.00 63.39 C ANISOU 1635 CD1 LEU A 208 8762 6494 8830 -2543 -15 724 C ATOM 1636 CD2 LEU A 208 -15.043 54.854 56.836 1.00 70.50 C ANISOU 1636 CD2 LEU A 208 10014 6971 9801 -2733 -75 822 C ATOM 1637 N ALA A1001 -19.379 54.932 53.551 1.00 77.33 N ANISOU 1637 N ALA A1001 8904 5310 15169 -885 702 1769 N ATOM 1638 CA ALA A1001 -20.751 54.479 53.336 1.00 75.85 C ANISOU 1638 CA ALA A1001 8836 5370 14612 -773 660 1906 C ATOM 1639 C ALA A1001 -20.785 53.191 52.523 1.00 74.54 C ANISOU 1639 C ALA A1001 8677 5443 14200 -835 728 1979 C ATOM 1640 O ALA A1001 -21.491 52.241 52.875 1.00 83.05 O ANISOU 1640 O ALA A1001 9762 6725 15069 -783 631 1933 O ATOM 1641 CB ALA A1001 -21.564 55.573 52.643 1.00 77.36 C ANISOU 1641 CB ALA A1001 9149 5467 14777 -697 708 2117 C ATOM 1642 N ASP A1002 -20.034 53.146 51.420 1.00 75.64 N ANISOU 1642 N ASP A1002 8821 5545 14373 -946 915 2091 N ATOM 1643 CA ASP A1002 -20.015 51.948 50.590 1.00 74.75 C ANISOU 1643 CA ASP A1002 8724 5658 14022 -972 958 2131 C ATOM 1644 C ASP A1002 -19.446 50.757 51.347 1.00 80.56 C ANISOU 1644 C ASP A1002 9338 6493 14781 -1016 830 1898 C ATOM 1645 O ASP A1002 -19.911 49.624 51.175 1.00 78.82 O ANISOU 1645 O ASP A1002 9135 6473 14341 -990 744 1886 O ATOM 1646 CB ASP A1002 -19.211 52.203 49.317 1.00 76.92 C ANISOU 1646 CB ASP A1002 9052 5862 14313 -1059 1233 2281 C ATOM 1647 CG ASP A1002 -19.923 53.117 48.359 1.00 84.34 C ANISOU 1647 CG ASP A1002 10233 6727 15084 -961 1338 2558 C ATOM 1648 OD1 ASP A1002 -21.124 53.350 48.566 1.00 86.73 O ANISOU 1648 OD1 ASP A1002 10618 7086 15249 -809 1142 2595 O ATOM 1649 OD2 ASP A1002 -19.290 53.602 47.398 1.00 90.93 O ANISOU 1649 OD2 ASP A1002 11192 7434 15924 -1021 1624 2732 O ATOM 1650 N LEU A1003 -18.429 50.989 52.176 1.00 73.61 N ANISOU 1650 N LEU A1003 8341 5443 14185 -1067 783 1691 N ATOM 1651 CA LEU A1003 -17.920 49.927 53.034 1.00 77.55 C ANISOU 1651 CA LEU A1003 8791 5993 14684 -1048 590 1446 C ATOM 1652 C LEU A1003 -19.032 49.354 53.898 1.00 70.92 C ANISOU 1652 C LEU A1003 8089 5277 13581 -933 432 1455 C ATOM 1653 O LEU A1003 -19.246 48.139 53.926 1.00 69.81 O ANISOU 1653 O LEU A1003 7993 5278 13254 -934 359 1432 O ATOM 1654 CB LEU A1003 -16.789 50.464 53.908 1.00 83.26 C ANISOU 1654 CB LEU A1003 9388 6472 15775 -1049 484 1175 C ATOM 1655 CG LEU A1003 -15.370 49.961 53.651 1.00 85.86 C ANISOU 1655 CG LEU A1003 9513 6732 16377 -1141 492 940 C ATOM 1656 CD1 LEU A1003 -15.194 49.427 52.229 1.00 86.82 C ANISOU 1656 CD1 LEU A1003 9590 7015 16385 -1259 753 1100 C ATOM 1657 CD2 LEU A1003 -14.382 51.092 53.944 1.00 81.30 C ANISOU 1657 CD2 LEU A1003 8728 5846 16315 -1199 525 754 C ATOM 1658 N GLU A1004 -19.767 50.231 54.588 1.00 71.23 N ANISOU 1658 N GLU A1004 8195 5248 13622 -839 405 1487 N ATOM 1659 CA GLU A1004 -20.832 49.803 55.486 1.00 78.08 C ANISOU 1659 CA GLU A1004 9181 6216 14269 -735 339 1489 C ATOM 1660 C GLU A1004 -21.962 49.113 54.725 1.00 74.04 C ANISOU 1660 C GLU A1004 8660 5906 13565 -769 420 1659 C ATOM 1661 O GLU A1004 -22.540 48.134 55.211 1.00 73.19 O ANISOU 1661 O GLU A1004 8605 5893 13309 -764 405 1646 O ATOM 1662 CB GLU A1004 -21.357 51.009 56.273 1.00 84.45 C ANISOU 1662 CB GLU A1004 10032 6914 15141 -609 318 1464 C ATOM 1663 CG GLU A1004 -22.556 50.708 57.179 1.00 93.18 C ANISOU 1663 CG GLU A1004 11248 8131 16026 -496 340 1472 C ATOM 1664 CD GLU A1004 -22.267 49.643 58.238 1.00101.74 C ANISOU 1664 CD GLU A1004 12506 9222 16927 -442 272 1353 C ATOM 1665 OE1 GLU A1004 -21.112 49.562 58.716 1.00106.16 O ANISOU 1665 OE1 GLU A1004 13129 9644 17561 -393 102 1173 O ATOM 1666 OE2 GLU A1004 -23.201 48.887 58.591 1.00102.03 O ANISOU 1666 OE2 GLU A1004 12625 9376 16767 -440 387 1430 O ATOM 1667 N ASP A1005 -22.282 49.602 53.526 1.00 70.08 N ANISOU 1667 N ASP A1005 8108 5443 13076 -789 499 1808 N ATOM 1668 CA ASP A1005 -23.336 48.976 52.741 1.00 71.69 C ANISOU 1668 CA ASP A1005 8287 5817 13134 -774 500 1907 C ATOM 1669 C ASP A1005 -22.973 47.548 52.363 1.00 71.30 C ANISOU 1669 C ASP A1005 8216 5879 12996 -850 455 1861 C ATOM 1670 O ASP A1005 -23.807 46.642 52.470 1.00 72.67 O ANISOU 1670 O ASP A1005 8357 6152 13104 -856 414 1849 O ATOM 1671 CB ASP A1005 -23.626 49.804 51.495 1.00 79.24 C ANISOU 1671 CB ASP A1005 9275 6762 14071 -716 538 2056 C ATOM 1672 CG ASP A1005 -24.456 51.021 51.803 1.00 93.06 C ANISOU 1672 CG ASP A1005 11045 8425 15887 -603 522 2096 C ATOM 1673 OD1 ASP A1005 -25.159 51.001 52.841 1.00 97.14 O ANISOU 1673 OD1 ASP A1005 11507 8969 16434 -560 495 2002 O ATOM 1674 OD2 ASP A1005 -24.408 51.993 51.013 1.00 98.82 O ANISOU 1674 OD2 ASP A1005 11870 9047 16629 -546 551 2222 O ATOM 1675 N ASN A1006 -21.733 47.325 51.919 1.00 68.93 N ANISOU 1675 N ASN A1006 7910 5546 12734 -913 470 1814 N ATOM 1676 CA ASN A1006 -21.316 45.971 51.575 1.00 72.17 C ANISOU 1676 CA ASN A1006 8297 6055 13069 -962 395 1734 C ATOM 1677 C ASN A1006 -21.361 45.058 52.792 1.00 71.69 C ANISOU 1677 C ASN A1006 8291 5960 12986 -975 285 1620 C ATOM 1678 O ASN A1006 -21.778 43.897 52.695 1.00 67.27 O ANISOU 1678 O ASN A1006 7738 5474 12348 -1001 214 1609 O ATOM 1679 CB ASN A1006 -19.920 45.996 50.964 1.00 72.68 C ANISOU 1679 CB ASN A1006 8313 6083 13220 -1015 459 1662 C ATOM 1680 CG ASN A1006 -19.923 46.532 49.554 1.00 80.06 C ANISOU 1680 CG ASN A1006 9272 7071 14076 -994 620 1815 C ATOM 1681 OD1 ASN A1006 -20.910 46.394 48.834 1.00 84.63 O ANISOU 1681 OD1 ASN A1006 9915 7760 14479 -907 579 1926 O ATOM 1682 ND2 ASN A1006 -18.818 47.146 49.146 1.00 82.22 N ANISOU 1682 ND2 ASN A1006 9507 7244 14490 -1059 807 1810 N ATOM 1683 N TRP A1007 -20.965 45.579 53.953 1.00 71.93 N ANISOU 1683 N TRP A1007 8396 5855 13079 -937 261 1536 N ATOM 1684 CA TRP A1007 -20.951 44.776 55.169 1.00 67.84 C ANISOU 1684 CA TRP A1007 8037 5273 12467 -898 163 1443 C ATOM 1685 C TRP A1007 -22.359 44.386 55.600 1.00 77.36 C ANISOU 1685 C TRP A1007 9302 6536 13554 -903 267 1566 C ATOM 1686 O TRP A1007 -22.599 43.234 55.982 1.00 74.27 O ANISOU 1686 O TRP A1007 9015 6133 13070 -939 247 1569 O ATOM 1687 CB TRP A1007 -20.241 45.549 56.273 1.00 70.43 C ANISOU 1687 CB TRP A1007 8465 5434 12861 -791 80 1297 C ATOM 1688 CG TRP A1007 -20.322 44.922 57.612 1.00 70.62 C ANISOU 1688 CG TRP A1007 8758 5371 12705 -680 -15 1222 C ATOM 1689 CD1 TRP A1007 -21.055 45.360 58.672 1.00 75.12 C ANISOU 1689 CD1 TRP A1007 9508 5900 13136 -567 61 1258 C ATOM 1690 CD2 TRP A1007 -19.636 43.748 58.053 1.00 69.69 C ANISOU 1690 CD2 TRP A1007 8815 5177 12487 -639 -200 1098 C ATOM 1691 NE1 TRP A1007 -20.869 44.530 59.745 1.00 78.87 N ANISOU 1691 NE1 TRP A1007 10303 6274 13390 -454 -31 1193 N ATOM 1692 CE2 TRP A1007 -20.003 43.531 59.390 1.00 72.30 C ANISOU 1692 CE2 TRP A1007 9484 5404 12582 -493 -216 1097 C ATOM 1693 CE3 TRP A1007 -18.756 42.853 57.442 1.00 69.32 C ANISOU 1693 CE3 TRP A1007 8694 5134 12512 -690 -354 981 C ATOM 1694 CZ2 TRP A1007 -19.519 42.461 60.129 1.00 72.16 C ANISOU 1694 CZ2 TRP A1007 9781 5258 12379 -389 -399 1007 C ATOM 1695 CZ3 TRP A1007 -18.270 41.799 58.174 1.00 71.90 C ANISOU 1695 CZ3 TRP A1007 9276 5342 12702 -592 -569 858 C ATOM 1696 CH2 TRP A1007 -18.652 41.606 59.506 1.00 76.52 C ANISOU 1696 CH2 TRP A1007 10245 5796 13032 -440 -599 883 C ATOM 1697 N GLU A1008 -23.309 45.325 55.548 1.00 78.07 N ANISOU 1697 N GLU A1008 9315 6667 13680 -871 390 1655 N ATOM 1698 CA GLU A1008 -24.663 44.989 55.973 1.00 79.85 C ANISOU 1698 CA GLU A1008 9526 6942 13870 -884 528 1726 C ATOM 1699 C GLU A1008 -25.379 44.122 54.942 1.00 74.61 C ANISOU 1699 C GLU A1008 8690 6383 13274 -976 516 1770 C ATOM 1700 O GLU A1008 -26.214 43.288 55.314 1.00 71.79 O ANISOU 1700 O GLU A1008 8309 6021 12946 -1045 613 1791 O ATOM 1701 CB GLU A1008 -25.461 46.260 56.281 1.00 85.62 C ANISOU 1701 CB GLU A1008 10196 7681 14654 -792 632 1747 C ATOM 1702 CG GLU A1008 -26.055 46.960 55.079 1.00 98.61 C ANISOU 1702 CG GLU A1008 11647 9404 16415 -773 603 1800 C ATOM 1703 CD GLU A1008 -26.816 48.223 55.461 1.00112.18 C ANISOU 1703 CD GLU A1008 13321 11104 18199 -655 662 1791 C ATOM 1704 OE1 GLU A1008 -26.910 48.514 56.675 1.00116.23 O ANISOU 1704 OE1 GLU A1008 13936 11566 18661 -592 752 1738 O ATOM 1705 OE2 GLU A1008 -27.317 48.925 54.552 1.00116.72 O ANISOU 1705 OE2 GLU A1008 13791 11705 18852 -593 600 1826 O ATOM 1706 N THR A1009 -25.039 44.277 53.660 1.00 71.11 N ANISOU 1706 N THR A1009 8142 6013 12863 -967 406 1775 N ATOM 1707 CA THR A1009 -25.575 43.396 52.628 1.00 72.00 C ANISOU 1707 CA THR A1009 8123 6218 13017 -999 317 1767 C ATOM 1708 C THR A1009 -25.184 41.943 52.880 1.00 71.71 C ANISOU 1708 C THR A1009 8144 6142 12961 -1093 249 1715 C ATOM 1709 O THR A1009 -26.014 41.033 52.756 1.00 75.65 O ANISOU 1709 O THR A1009 8542 6641 13563 -1157 236 1699 O ATOM 1710 CB THR A1009 -25.085 43.860 51.255 1.00 69.96 C ANISOU 1710 CB THR A1009 7844 6035 12702 -921 224 1785 C ATOM 1711 OG1 THR A1009 -25.726 45.088 50.932 1.00 74.92 O ANISOU 1711 OG1 THR A1009 8448 6666 13352 -817 259 1849 O ATOM 1712 CG2 THR A1009 -25.416 42.842 50.174 1.00 74.25 C ANISOU 1712 CG2 THR A1009 8302 6672 13237 -900 70 1729 C ATOM 1713 N LEU A1010 -23.924 41.710 53.244 1.00 71.17 N ANISOU 1713 N LEU A1010 8224 6012 12804 -1096 184 1662 N ATOM 1714 CA LEU A1010 -23.465 40.357 53.529 1.00 74.97 C ANISOU 1714 CA LEU A1010 8806 6426 13255 -1152 72 1597 C ATOM 1715 C LEU A1010 -24.242 39.752 54.689 1.00 72.79 C ANISOU 1715 C LEU A1010 8663 6024 12969 -1214 198 1664 C ATOM 1716 O LEU A1010 -24.706 38.614 54.608 1.00 74.53 O ANISOU 1716 O LEU A1010 8870 6190 13259 -1304 177 1674 O ATOM 1717 CB LEU A1010 -21.967 40.367 53.836 1.00 78.94 C ANISOU 1717 CB LEU A1010 9434 6862 13698 -1103 -50 1477 C ATOM 1718 CG LEU A1010 -21.021 40.509 52.642 1.00 84.29 C ANISOU 1718 CG LEU A1010 9975 7640 14411 -1081 -127 1387 C ATOM 1719 CD1 LEU A1010 -19.646 40.944 53.105 1.00 86.61 C ANISOU 1719 CD1 LEU A1010 10307 7841 14759 -1039 -182 1237 C ATOM 1720 CD2 LEU A1010 -20.932 39.207 51.849 1.00 85.15 C ANISOU 1720 CD2 LEU A1010 10034 7812 14509 -1099 -283 1310 C ATOM 1721 N ASN A1011 -24.407 40.514 55.770 1.00 73.45 N ANISOU 1721 N ASN A1011 8890 6045 12972 -1162 351 1711 N ATOM 1722 CA ASN A1011 -24.991 39.973 56.992 1.00 74.28 C ANISOU 1722 CA ASN A1011 9216 6016 12992 -1193 535 1792 C ATOM 1723 C ASN A1011 -26.502 39.795 56.872 1.00 77.36 C ANISOU 1723 C ASN A1011 9391 6435 13566 -1310 779 1875 C ATOM 1724 O ASN A1011 -27.054 38.792 57.350 1.00 80.25 O ANISOU 1724 O ASN A1011 9839 6675 13976 -1427 934 1947 O ATOM 1725 CB ASN A1011 -24.645 40.880 58.168 1.00 78.87 C ANISOU 1725 CB ASN A1011 10045 6531 13391 -1045 606 1780 C ATOM 1726 CG ASN A1011 -23.190 40.788 58.552 1.00 86.39 C ANISOU 1726 CG ASN A1011 11230 7381 14212 -919 338 1643 C ATOM 1727 OD1 ASN A1011 -22.637 39.698 58.649 1.00 91.17 O ANISOU 1727 OD1 ASN A1011 12005 7886 14751 -928 187 1605 O ATOM 1728 ND2 ASN A1011 -22.555 41.930 58.757 1.00 88.92 N ANISOU 1728 ND2 ASN A1011 11538 7704 14543 -792 251 1537 N ATOM 1729 N ASP A1012 -27.186 40.749 56.235 1.00 73.93 N ANISOU 1729 N ASP A1012 8676 6137 13277 -1280 814 1852 N ATOM 1730 CA ASP A1012 -28.631 40.624 56.065 1.00 80.60 C ANISOU 1730 CA ASP A1012 9243 7005 14376 -1366 998 1856 C ATOM 1731 C ASP A1012 -28.986 39.423 55.201 1.00 82.89 C ANISOU 1731 C ASP A1012 9338 7269 14889 -1487 870 1806 C ATOM 1732 O ASP A1012 -29.952 38.706 55.488 1.00 92.09 O ANISOU 1732 O ASP A1012 10363 8336 16292 -1629 1063 1814 O ATOM 1733 CB ASP A1012 -29.205 41.895 55.450 1.00 82.34 C ANISOU 1733 CB ASP A1012 9222 7359 14703 -1253 959 1797 C ATOM 1734 CG ASP A1012 -29.063 43.093 56.357 1.00 86.71 C ANISOU 1734 CG ASP A1012 9926 7914 15106 -1135 1091 1822 C ATOM 1735 OD1 ASP A1012 -28.797 42.904 57.562 1.00 91.36 O ANISOU 1735 OD1 ASP A1012 10784 8411 15519 -1131 1263 1873 O ATOM 1736 OD2 ASP A1012 -29.226 44.224 55.862 1.00 86.14 O ANISOU 1736 OD2 ASP A1012 9735 7916 15077 -1019 1003 1784 O ATOM 1737 N ASN A1013 -28.222 39.189 54.134 1.00 78.43 N ANISOU 1737 N ASN A1013 8746 6777 14275 -1431 560 1737 N ATOM 1738 CA ASN A1013 -28.544 38.084 53.244 1.00 78.14 C ANISOU 1738 CA ASN A1013 8525 6722 14443 -1497 378 1646 C ATOM 1739 C ASN A1013 -28.247 36.739 53.889 1.00 79.17 C ANISOU 1739 C ASN A1013 8838 6661 14582 -1639 415 1692 C ATOM 1740 O ASN A1013 -28.913 35.748 53.573 1.00 77.99 O ANISOU 1740 O ASN A1013 8512 6410 14712 -1756 382 1638 O ATOM 1741 CB ASN A1013 -27.804 38.239 51.924 1.00 73.60 C ANISOU 1741 CB ASN A1013 7917 6291 13755 -1356 66 1556 C ATOM 1742 CG ASN A1013 -28.471 39.237 51.014 1.00 84.02 C ANISOU 1742 CG ASN A1013 9046 7745 15131 -1210 -13 1503 C ATOM 1743 OD1 ASN A1013 -27.889 40.265 50.655 1.00 85.31 O ANISOU 1743 OD1 ASN A1013 9317 7999 15098 -1087 -34 1550 O ATOM 1744 ND2 ASN A1013 -29.710 38.948 50.638 1.00 75.19 N ANISOU 1744 ND2 ASN A1013 7646 6609 14312 -1215 -66 1391 N ATOM 1745 N LEU A1014 -27.269 36.693 54.798 1.00 77.11 N ANISOU 1745 N LEU A1014 8938 6317 14041 -1613 455 1773 N ATOM 1746 CA LEU A1014 -27.113 35.530 55.661 1.00 80.28 C ANISOU 1746 CA LEU A1014 9616 6486 14402 -1719 533 1854 C ATOM 1747 C LEU A1014 -28.384 35.255 56.451 1.00 85.15 C ANISOU 1747 C LEU A1014 10192 6952 15210 -1882 934 1978 C ATOM 1748 O LEU A1014 -28.785 34.096 56.614 1.00 81.68 O ANISOU 1748 O LEU A1014 9777 6302 14954 -2045 1017 2028 O ATOM 1749 CB LEU A1014 -25.935 35.735 56.608 1.00 80.31 C ANISOU 1749 CB LEU A1014 10049 6417 14049 -1592 483 1888 C ATOM 1750 CG LEU A1014 -24.576 35.263 56.104 1.00 81.87 C ANISOU 1750 CG LEU A1014 10346 6624 14136 -1495 107 1746 C ATOM 1751 CD1 LEU A1014 -23.454 36.053 56.760 1.00 82.24 C ANISOU 1751 CD1 LEU A1014 10633 6676 13937 -1321 14 1683 C ATOM 1752 CD2 LEU A1014 -24.424 33.785 56.390 1.00 82.20 C ANISOU 1752 CD2 LEU A1014 10608 6433 14192 -1568 2 1765 C ATOM 1753 N LYS A1015 -29.031 36.307 56.958 1.00 83.78 N ANISOU 1753 N LYS A1015 9947 6863 15022 -1847 1211 2020 N ATOM 1754 CA LYS A1015 -30.256 36.098 57.723 1.00 89.45 C ANISOU 1754 CA LYS A1015 10589 7452 15945 -2004 1666 2117 C ATOM 1755 C LYS A1015 -31.386 35.610 56.825 1.00 90.04 C ANISOU 1755 C LYS A1015 10144 7513 16553 -2162 1663 1990 C ATOM 1756 O LYS A1015 -32.188 34.761 57.232 1.00 98.03 O ANISOU 1756 O LYS A1015 11071 8314 17864 -2375 1966 2049 O ATOM 1757 CB LYS A1015 -30.650 37.384 58.449 1.00 92.72 C ANISOU 1757 CB LYS A1015 11028 7983 16219 -1891 1938 2144 C ATOM 1758 CG LYS A1015 -29.717 37.754 59.594 1.00 95.66 C ANISOU 1758 CG LYS A1015 11941 8304 16102 -1725 1987 2248 C ATOM 1759 CD LYS A1015 -29.808 39.237 59.939 1.00 95.30 C ANISOU 1759 CD LYS A1015 11864 8424 15924 -1543 2050 2192 C ATOM 1760 N VAL A1016 -31.449 36.120 55.594 1.00 87.24 N ANISOU 1760 N VAL A1016 9456 7354 16336 -2047 1315 1806 N ATOM 1761 CA VAL A1016 -32.458 35.670 54.640 1.00 85.28 C ANISOU 1761 CA VAL A1016 8721 7089 16591 -2122 1187 1615 C ATOM 1762 C VAL A1016 -32.306 34.178 54.359 1.00 91.84 C ANISOU 1762 C VAL A1016 9559 7711 17624 -2274 1046 1595 C ATOM 1763 O VAL A1016 -33.293 33.430 54.351 1.00 90.11 O ANISOU 1763 O VAL A1016 9035 7303 17899 -2466 1193 1523 O ATOM 1764 CB VAL A1016 -32.367 36.507 53.352 1.00 83.15 C ANISOU 1764 CB VAL A1016 8244 7058 16293 -1888 778 1435 C ATOM 1765 CG1 VAL A1016 -33.258 35.933 52.275 1.00 85.33 C ANISOU 1765 CG1 VAL A1016 8081 7302 17040 -1888 513 1185 C ATOM 1766 CG2 VAL A1016 -32.734 37.957 53.641 1.00 82.72 C ANISOU 1766 CG2 VAL A1016 8142 7149 16138 -1755 924 1443 C ATOM 1767 N ILE A1017 -31.067 33.721 54.143 1.00 87.14 N ANISOU 1767 N ILE A1017 9288 7123 16699 -2193 760 1634 N ATOM 1768 CA ILE A1017 -30.828 32.311 53.827 1.00 87.75 C ANISOU 1768 CA ILE A1017 9395 7000 16947 -2301 559 1591 C ATOM 1769 C ILE A1017 -31.259 31.417 54.980 1.00 88.93 C ANISOU 1769 C ILE A1017 9733 6810 17246 -2554 965 1783 C ATOM 1770 O ILE A1017 -31.886 30.372 54.772 1.00 91.89 O ANISOU 1770 O ILE A1017 9900 6946 18067 -2743 977 1728 O ATOM 1771 CB ILE A1017 -29.348 32.089 53.465 1.00 84.10 C ANISOU 1771 CB ILE A1017 9250 6623 16079 -2137 194 1571 C ATOM 1772 CG1 ILE A1017 -29.046 32.667 52.083 1.00 79.98 C ANISOU 1772 CG1 ILE A1017 8509 6385 15497 -1920 -179 1372 C ATOM 1773 CG2 ILE A1017 -28.991 30.604 53.522 1.00 85.75 C ANISOU 1773 CG2 ILE A1017 9613 6570 16397 -2246 36 1566 C ATOM 1774 CD1 ILE A1017 -27.563 32.912 51.837 1.00 80.36 C ANISOU 1774 CD1 ILE A1017 8834 6577 15123 -1751 -394 1363 C ATOM 1775 N GLU A1018 -30.929 31.807 56.211 1.00 92.83 N ANISOU 1775 N GLU A1018 10650 7253 17370 -2548 1307 2010 N ATOM 1776 CA GLU A1018 -31.307 30.997 57.364 1.00101.94 C ANISOU 1776 CA GLU A1018 12101 8066 18565 -2756 1753 2241 C ATOM 1777 C GLU A1018 -32.821 30.951 57.549 1.00108.52 C ANISOU 1777 C GLU A1018 12508 8780 19944 -2998 2225 2236 C ATOM 1778 O GLU A1018 -33.361 29.926 57.974 1.00112.59 O ANISOU 1778 O GLU A1018 13062 8999 20716 -3228 2509 2332 O ATOM 1779 CB GLU A1018 -30.628 31.537 58.620 1.00105.57 C ANISOU 1779 CB GLU A1018 13153 8519 18440 -2617 1980 2452 C ATOM 1780 CG GLU A1018 -29.113 31.418 58.594 1.00109.91 C ANISOU 1780 CG GLU A1018 14122 9106 18535 -2394 1527 2422 C ATOM 1781 CD GLU A1018 -28.440 32.342 59.591 1.00114.79 C ANISOU 1781 CD GLU A1018 15179 9803 18632 -2171 1615 2506 C ATOM 1782 OE1 GLU A1018 -29.105 33.282 60.074 1.00117.89 O ANISOU 1782 OE1 GLU A1018 15487 10309 18997 -2154 1960 2555 O ATOM 1783 OE2 GLU A1018 -27.248 32.134 59.893 1.00115.51 O ANISOU 1783 OE2 GLU A1018 15682 9837 18371 -1990 1307 2483 O ATOM 1784 N LYS A1019 -33.513 32.039 57.230 1.00112.39 N ANISOU 1784 N LYS A1019 12593 9519 20592 -2925 2292 2090 N ATOM 1785 CA LYS A1019 -34.961 32.122 57.355 1.00117.35 C ANISOU 1785 CA LYS A1019 12726 10065 21797 -3121 2710 2005 C ATOM 1786 C LYS A1019 -35.688 31.537 56.149 1.00112.22 C ANISOU 1786 C LYS A1019 11463 9369 21807 -3201 2377 1693 C ATOM 1787 O LYS A1019 -36.919 31.439 56.172 1.00119.91 O ANISOU 1787 O LYS A1019 11995 10313 23250 -3309 2626 1525 O ATOM 1788 CB LYS A1019 -35.354 33.595 57.564 1.00121.01 C ANISOU 1788 CB LYS A1019 13041 10816 22123 -2950 2862 1938 C ATOM 1789 CG LYS A1019 -36.831 33.880 57.792 1.00132.14 C ANISOU 1789 CG LYS A1019 13920 12182 24105 -3107 3317 1807 C ATOM 1790 CD LYS A1019 -37.442 34.597 56.594 1.00133.27 C ANISOU 1790 CD LYS A1019 13464 12544 24629 -2947 2889 1441 C ATOM 1791 CE LYS A1019 -38.953 34.720 56.732 1.00137.28 C ANISOU 1791 CE LYS A1019 13345 12969 25845 -3105 3273 1222 C ATOM 1792 NZ LYS A1019 -39.545 35.567 55.655 1.00135.53 N ANISOU 1792 NZ LYS A1019 12607 12959 25929 -2870 2810 842 N ATOM 1793 N ALA A1020 -34.969 31.119 55.112 1.00103.19 N ANISOU 1793 N ALA A1020 10319 8280 20610 -3072 1779 1557 N ATOM 1794 CA ALA A1020 -35.626 30.822 53.851 1.00101.81 C ANISOU 1794 CA ALA A1020 9574 8118 20990 -3037 1360 1202 C ATOM 1795 C ALA A1020 -36.382 29.496 53.919 1.00109.85 C ANISOU 1795 C ALA A1020 10381 8852 22505 -3258 1479 1110 C ATOM 1796 O ALA A1020 -36.198 28.673 54.823 1.00112.00 O ANISOU 1796 O ALA A1020 11036 8930 22589 -3421 1810 1347 O ATOM 1797 CB ALA A1020 -34.616 30.789 52.708 1.00 96.59 C ANISOU 1797 CB ALA A1020 9047 7662 19991 -2759 699 1065 C ATOM 1798 N ASP A1021 -37.244 29.295 52.924 1.00110.26 N ANISOU 1798 N ASP A1021 9851 8896 23145 -3209 1157 735 N ATOM 1799 CA ASP A1021 -38.036 28.079 52.836 1.00117.68 C ANISOU 1799 CA ASP A1021 10527 9595 24592 -3356 1196 573 C ATOM 1800 C ASP A1021 -38.046 27.508 51.423 1.00120.82 C ANISOU 1800 C ASP A1021 10580 9961 25365 -3188 481 193 C ATOM 1801 O ASP A1021 -38.868 26.631 51.132 1.00125.80 O ANISOU 1801 O ASP A1021 10858 10397 26544 -3252 416 -45 O ATOM 1802 CB ASP A1021 -39.465 28.355 53.314 1.00118.61 C ANISOU 1802 CB ASP A1021 10203 9672 25191 -3471 1667 438 C ATOM 1803 N ASN A1022 -37.158 27.968 50.543 1.00116.39 N ANISOU 1803 N ASN A1022 10125 9570 24528 -2963 -54 119 N ATOM 1804 CA ASN A1022 -37.181 27.577 49.140 1.00120.17 C ANISOU 1804 CA ASN A1022 10302 10057 25298 -2737 -774 -280 C ATOM 1805 C ASN A1022 -35.820 27.872 48.523 1.00112.05 C ANISOU 1805 C ASN A1022 9723 9295 23554 -2459 -1185 -201 C ATOM 1806 O ASN A1022 -35.164 28.854 48.883 1.00106.36 O ANISOU 1806 O ASN A1022 9361 8842 22209 -2349 -996 43 O ATOM 1807 CB ASN A1022 -38.301 28.310 48.385 1.00124.34 C ANISOU 1807 CB ASN A1022 10261 10689 26294 -2543 -1023 -685 C ATOM 1808 CG ASN A1022 -37.914 28.672 46.964 1.00124.91 C ANISOU 1808 CG ASN A1022 10336 11007 26116 -2100 -1772 -984 C ATOM 1809 OD1 ASN A1022 -37.335 29.732 46.720 1.00121.85 O ANISOU 1809 OD1 ASN A1022 10275 10958 25065 -1831 -1836 -858 O ATOM 1810 ND2 ASN A1022 -38.232 27.793 46.017 1.00127.95 N ANISOU 1810 ND2 ASN A1022 10424 11239 26954 -1974 -2323 -1378 N ATOM 1811 N ALA A1023 -35.410 27.012 47.581 1.00109.96 N ANISOU 1811 N ALA A1023 9453 8990 23336 -2299 -1733 -432 N ATOM 1812 CA ALA A1023 -34.078 27.131 46.990 1.00108.88 C ANISOU 1812 CA ALA A1023 9766 9131 22472 -2009 -2065 -374 C ATOM 1813 C ALA A1023 -33.895 28.456 46.254 1.00110.50 C ANISOU 1813 C ALA A1023 10048 9740 22196 -1645 -2235 -432 C ATOM 1814 O ALA A1023 -32.800 29.031 46.267 1.00105.59 O ANISOU 1814 O ALA A1023 9843 9365 20914 -1511 -2182 -226 O ATOM 1815 CB ALA A1023 -33.812 25.962 46.042 1.00102.76 C ANISOU 1815 CB ALA A1023 8917 8241 21884 -1869 -2634 -675 C ATOM 1816 N ALA A1024 -34.951 28.954 45.602 1.00115.99 N ANISOU 1816 N ALA A1024 10352 10480 23240 -1473 -2450 -726 N ATOM 1817 CA ALA A1024 -34.813 30.165 44.796 1.00117.46 C ANISOU 1817 CA ALA A1024 10670 11001 22958 -1085 -2667 -786 C ATOM 1818 C ALA A1024 -34.577 31.399 45.658 1.00111.96 C ANISOU 1818 C ALA A1024 10198 10462 21880 -1172 -2176 -442 C ATOM 1819 O ALA A1024 -33.883 32.327 45.227 1.00108.33 O ANISOU 1819 O ALA A1024 10059 10267 20837 -924 -2236 -328 O ATOM 1820 CB ALA A1024 -36.049 30.357 43.917 1.00122.55 C ANISOU 1820 CB ALA A1024 10865 11609 24091 -834 -3087 -1225 C ATOM 1821 N GLN A1025 -35.155 31.439 46.862 1.00108.96 N ANISOU 1821 N GLN A1025 9663 9907 21828 -1512 -1675 -281 N ATOM 1822 CA GLN A1025 -34.863 32.539 47.777 1.00105.55 C ANISOU 1822 CA GLN A1025 9478 9611 21015 -1582 -1219 34 C ATOM 1823 C GLN A1025 -33.422 32.468 48.262 1.00101.52 C ANISOU 1823 C GLN A1025 9492 9179 19902 -1629 -1072 348 C ATOM 1824 O GLN A1025 -32.725 33.489 48.314 1.00 99.02 O ANISOU 1824 O GLN A1025 9461 9076 19088 -1489 -995 510 O ATOM 1825 CB GLN A1025 -35.831 32.515 48.960 1.00107.94 C ANISOU 1825 CB GLN A1025 9516 9707 21790 -1908 -692 112 C ATOM 1826 N VAL A1026 -32.966 31.268 48.623 1.00100.71 N ANISOU 1826 N VAL A1026 9509 8876 19881 -1818 -1053 410 N ATOM 1827 CA VAL A1026 -31.557 31.056 48.939 1.00 90.12 C ANISOU 1827 CA VAL A1026 8631 7590 18019 -1807 -1040 614 C ATOM 1828 C VAL A1026 -30.687 31.460 47.755 1.00 87.00 C ANISOU 1828 C VAL A1026 8377 7475 17204 -1481 -1425 499 C ATOM 1829 O VAL A1026 -29.663 32.140 47.913 1.00 83.26 O ANISOU 1829 O VAL A1026 8210 7170 16255 -1397 -1329 657 O ATOM 1830 CB VAL A1026 -31.325 29.587 49.340 1.00 88.21 C ANISOU 1830 CB VAL A1026 8472 7048 17996 -2016 -1066 634 C ATOM 1831 CG1 VAL A1026 -29.856 29.228 49.260 1.00 85.60 C ANISOU 1831 CG1 VAL A1026 8540 6793 17189 -1906 -1258 698 C ATOM 1832 CG2 VAL A1026 -31.861 29.326 50.735 1.00 90.37 C ANISOU 1832 CG2 VAL A1026 8809 7041 18486 -2340 -541 874 C ATOM 1833 N LYS A1027 -31.089 31.047 46.550 1.00 91.29 N ANISOU 1833 N LYS A1027 8698 8055 17932 -1282 -1854 205 N ATOM 1834 CA LYS A1027 -30.344 31.390 45.343 1.00 98.14 C ANISOU 1834 CA LYS A1027 9736 9184 18369 -939 -2184 93 C ATOM 1835 C LYS A1027 -30.258 32.899 45.158 1.00103.04 C ANISOU 1835 C LYS A1027 10491 10029 18629 -770 -2035 224 C ATOM 1836 O LYS A1027 -29.183 33.441 44.861 1.00103.34 O ANISOU 1836 O LYS A1027 10825 10250 18189 -643 -1986 344 O ATOM 1837 CB LYS A1027 -31.004 30.736 44.130 1.00103.22 C ANISOU 1837 CB LYS A1027 10130 9804 19284 -706 -2689 -275 C ATOM 1838 CG LYS A1027 -30.737 31.441 42.815 1.00107.52 C ANISOU 1838 CG LYS A1027 10836 10621 19396 -277 -2988 -401 C ATOM 1839 CD LYS A1027 -29.522 30.873 42.105 1.00110.04 C ANISOU 1839 CD LYS A1027 11428 11078 19303 -100 -3180 -453 C ATOM 1840 CE LYS A1027 -29.363 31.500 40.725 1.00114.27 C ANISOU 1840 CE LYS A1027 12163 11861 19393 355 -3443 -579 C ATOM 1841 NZ LYS A1027 -28.329 30.818 39.895 1.00115.61 N ANISOU 1841 NZ LYS A1027 12548 12168 19209 569 -3649 -705 N ATOM 1842 N ASP A1028 -31.378 33.596 45.347 1.00101.23 N ANISOU 1842 N ASP A1028 10031 9767 18665 -775 -1947 191 N ATOM 1843 CA ASP A1028 -31.385 35.044 45.190 1.00 96.60 C ANISOU 1843 CA ASP A1028 9578 9351 17774 -605 -1836 307 C ATOM 1844 C ASP A1028 -30.437 35.711 46.175 1.00 85.18 C ANISOU 1844 C ASP A1028 8414 7950 15999 -769 -1430 623 C ATOM 1845 O ASP A1028 -29.666 36.606 45.809 1.00 83.47 O ANISOU 1845 O ASP A1028 8452 7887 15376 -619 -1387 745 O ATOM 1846 CB ASP A1028 -32.805 35.576 45.369 1.00106.28 C ANISOU 1846 CB ASP A1028 10463 10501 19419 -597 -1822 174 C ATOM 1847 CG ASP A1028 -32.833 37.064 45.631 1.00112.43 C ANISOU 1847 CG ASP A1028 11383 11393 19941 -505 -1617 342 C ATOM 1848 OD1 ASP A1028 -32.782 37.841 44.653 1.00114.82 O ANISOU 1848 OD1 ASP A1028 11845 11823 19959 -184 -1858 295 O ATOM 1849 OD2 ASP A1028 -32.893 37.458 46.817 1.00114.53 O ANISOU 1849 OD2 ASP A1028 11639 11606 20269 -736 -1217 524 O ATOM 1850 N ALA A1029 -30.484 35.290 47.439 1.00 80.27 N ANISOU 1850 N ALA A1029 7768 7171 15560 -1063 -1126 751 N ATOM 1851 CA ALA A1029 -29.704 35.966 48.467 1.00 78.71 C ANISOU 1851 CA ALA A1029 7835 6992 15080 -1172 -790 1001 C ATOM 1852 C ALA A1029 -28.211 35.736 48.268 1.00 81.67 C ANISOU 1852 C ALA A1029 8501 7442 15089 -1123 -864 1059 C ATOM 1853 O ALA A1029 -27.406 36.651 48.476 1.00 84.65 O ANISOU 1853 O ALA A1029 9072 7908 15182 -1075 -726 1184 O ATOM 1854 CB ALA A1029 -30.146 35.501 49.853 1.00 78.50 C ANISOU 1854 CB ALA A1029 7784 6763 15279 -1444 -458 1115 C ATOM 1855 N LEU A1030 -27.828 34.522 47.864 1.00 79.19 N ANISOU 1855 N LEU A1030 8187 7074 14828 -1133 -1089 938 N ATOM 1856 CA LEU A1030 -26.427 34.240 47.579 1.00 76.42 C ANISOU 1856 CA LEU A1030 8056 6804 14177 -1062 -1184 927 C ATOM 1857 C LEU A1030 -25.913 35.091 46.428 1.00 79.02 C ANISOU 1857 C LEU A1030 8455 7360 14208 -822 -1259 897 C ATOM 1858 O LEU A1030 -24.743 35.497 46.427 1.00 72.33 O ANISOU 1858 O LEU A1030 7776 6594 13110 -793 -1153 954 O ATOM 1859 CB LEU A1030 -26.239 32.759 47.254 1.00 78.21 C ANISOU 1859 CB LEU A1030 8245 6928 14545 -1082 -1458 759 C ATOM 1860 CG LEU A1030 -25.787 31.751 48.326 1.00 84.36 C ANISOU 1860 CG LEU A1030 9169 7474 15409 -1277 -1411 815 C ATOM 1861 CD1 LEU A1030 -24.945 32.369 49.441 1.00 83.21 C ANISOU 1861 CD1 LEU A1030 9286 7303 15027 -1341 -1162 989 C ATOM 1862 CD2 LEU A1030 -26.947 30.984 48.900 1.00 89.71 C ANISOU 1862 CD2 LEU A1030 9701 7893 16492 -1480 -1343 838 C ATOM 1863 N THR A1031 -26.766 35.364 45.441 1.00 78.97 N ANISOU 1863 N THR A1031 8333 7434 14237 -635 -1436 796 N ATOM 1864 CA THR A1031 -26.372 36.230 44.337 1.00 81.31 C ANISOU 1864 CA THR A1031 8787 7915 14193 -377 -1471 812 C ATOM 1865 C THR A1031 -26.102 37.655 44.820 1.00 78.47 C ANISOU 1865 C THR A1031 8557 7578 13682 -417 -1157 1036 C ATOM 1866 O THR A1031 -25.149 38.300 44.367 1.00 73.96 O ANISOU 1866 O THR A1031 8176 7099 12826 -336 -1020 1128 O ATOM 1867 CB THR A1031 -27.453 36.201 43.253 1.00 87.20 C ANISOU 1867 CB THR A1031 9434 8701 14999 -114 -1792 632 C ATOM 1868 OG1 THR A1031 -27.554 34.871 42.724 1.00 88.62 O ANISOU 1868 OG1 THR A1031 9499 8850 15321 -49 -2122 387 O ATOM 1869 CG2 THR A1031 -27.125 37.168 42.126 1.00 89.16 C ANISOU 1869 CG2 THR A1031 9949 9106 14821 192 -1805 691 C ATOM 1870 N LYS A1032 -26.903 38.155 45.760 1.00 80.32 N ANISOU 1870 N LYS A1032 8678 7711 14129 -549 -1015 1118 N ATOM 1871 CA LYS A1032 -26.627 39.486 46.292 1.00 79.91 C ANISOU 1871 CA LYS A1032 8744 7659 13960 -578 -752 1304 C ATOM 1872 C LYS A1032 -25.349 39.491 47.122 1.00 76.47 C ANISOU 1872 C LYS A1032 8436 7184 13435 -735 -553 1391 C ATOM 1873 O LYS A1032 -24.594 40.470 47.098 1.00 76.18 O ANISOU 1873 O LYS A1032 8528 7167 13252 -712 -390 1496 O ATOM 1874 CB LYS A1032 -27.810 39.988 47.117 1.00 82.99 C ANISOU 1874 CB LYS A1032 8972 7963 14599 -651 -656 1328 C ATOM 1875 CG LYS A1032 -29.128 39.959 46.361 1.00 91.84 C ANISOU 1875 CG LYS A1032 9895 9094 15907 -485 -897 1167 C ATOM 1876 CD LYS A1032 -30.244 40.609 47.161 1.00 98.90 C ANISOU 1876 CD LYS A1032 10593 9916 17069 -544 -762 1163 C ATOM 1877 CE LYS A1032 -31.622 40.330 46.552 1.00105.54 C ANISOU 1877 CE LYS A1032 11129 10729 18243 -409 -1032 913 C ATOM 1878 NZ LYS A1032 -31.725 40.711 45.111 1.00108.71 N ANISOU 1878 NZ LYS A1032 11657 11214 18435 -56 -1392 806 N ATOM 1879 N MET A1033 -25.081 38.405 47.857 1.00 73.85 N ANISOU 1879 N MET A1033 8079 6764 13216 -882 -584 1331 N ATOM 1880 CA MET A1033 -23.846 38.341 48.631 1.00 70.95 C ANISOU 1880 CA MET A1033 7847 6341 12771 -974 -484 1352 C ATOM 1881 C MET A1033 -22.631 38.303 47.720 1.00 74.09 C ANISOU 1881 C MET A1033 8301 6846 13004 -881 -527 1275 C ATOM 1882 O MET A1033 -21.595 38.900 48.038 1.00 74.35 O ANISOU 1882 O MET A1033 8396 6861 12991 -908 -391 1290 O ATOM 1883 CB MET A1033 -23.845 37.123 49.552 1.00 71.47 C ANISOU 1883 CB MET A1033 7945 6257 12953 -1105 -550 1303 C ATOM 1884 CG MET A1033 -24.752 37.277 50.723 1.00 73.61 C ANISOU 1884 CG MET A1033 8228 6395 13345 -1221 -374 1413 C ATOM 1885 SD MET A1033 -24.843 35.772 51.687 1.00 77.84 S ANISOU 1885 SD MET A1033 8885 6705 13985 -1370 -404 1409 S ATOM 1886 CE MET A1033 -23.166 35.706 52.293 1.00 73.38 C ANISOU 1886 CE MET A1033 8595 6087 13199 -1308 -496 1353 C ATOM 1887 N ARG A1034 -22.742 37.614 46.581 1.00 74.00 N ANISOU 1887 N ARG A1034 8251 6941 12926 -759 -710 1165 N ATOM 1888 CA ARG A1034 -21.597 37.494 45.686 1.00 75.89 C ANISOU 1888 CA ARG A1034 8547 7301 12989 -657 -703 1077 C ATOM 1889 C ARG A1034 -21.184 38.857 45.135 1.00 77.62 C ANISOU 1889 C ARG A1034 8861 7585 13046 -588 -440 1218 C ATOM 1890 O ARG A1034 -19.990 39.131 44.969 1.00 78.94 O ANISOU 1890 O ARG A1034 9049 7776 13166 -610 -264 1192 O ATOM 1891 CB ARG A1034 -21.917 36.519 44.554 1.00 74.69 C ANISOU 1891 CB ARG A1034 8367 7254 12758 -489 -965 917 C ATOM 1892 CG ARG A1034 -20.685 35.944 43.872 1.00 76.25 C ANISOU 1892 CG ARG A1034 8598 7563 12813 -401 -987 758 C ATOM 1893 CD ARG A1034 -21.052 35.088 42.670 1.00 79.10 C ANISOU 1893 CD ARG A1034 8964 8042 13047 -174 -1265 584 C ATOM 1894 NE ARG A1034 -19.952 34.218 42.263 1.00 83.04 N ANISOU 1894 NE ARG A1034 9452 8625 13476 -107 -1342 373 N ATOM 1895 CZ ARG A1034 -18.934 34.598 41.498 1.00 89.50 C ANISOU 1895 CZ ARG A1034 10345 9597 14065 5 -1116 341 C ATOM 1896 NH1 ARG A1034 -18.862 35.847 41.052 1.00 95.23 N ANISOU 1896 NH1 ARG A1034 11202 10383 14598 49 -785 546 N ATOM 1897 NH2 ARG A1034 -17.982 33.731 41.180 1.00 89.22 N ANISOU 1897 NH2 ARG A1034 10252 9637 14009 71 -1200 102 N ATOM 1898 N ALA A1035 -22.157 39.729 44.863 1.00 78.25 N ANISOU 1898 N ALA A1035 8990 7666 13077 -508 -405 1357 N ATOM 1899 CA ALA A1035 -21.840 41.047 44.316 1.00 76.98 C ANISOU 1899 CA ALA A1035 8977 7516 12756 -436 -159 1525 C ATOM 1900 C ALA A1035 -21.205 41.940 45.375 1.00 76.73 C ANISOU 1900 C ALA A1035 8916 7350 12888 -617 75 1615 C ATOM 1901 O ALA A1035 -20.193 42.605 45.120 1.00 78.92 O ANISOU 1901 O ALA A1035 9242 7599 13145 -652 320 1668 O ATOM 1902 CB ALA A1035 -23.104 41.694 43.753 1.00 74.19 C ANISOU 1902 CB ALA A1035 8711 7169 12308 -257 -265 1616 C ATOM 1903 N ALA A1036 -21.796 41.973 46.569 1.00 76.54 N ANISOU 1903 N ALA A1036 8811 7227 13046 -723 14 1618 N ATOM 1904 CA ALA A1036 -21.208 42.725 47.670 1.00 77.20 C ANISOU 1904 CA ALA A1036 8882 7174 13276 -847 164 1650 C ATOM 1905 C ALA A1036 -19.785 42.267 47.949 1.00 74.75 C ANISOU 1905 C ALA A1036 8523 6830 13048 -927 194 1500 C ATOM 1906 O ALA A1036 -18.908 43.086 48.253 1.00 75.93 O ANISOU 1906 O ALA A1036 8648 6880 13323 -985 354 1492 O ATOM 1907 CB ALA A1036 -22.069 42.576 48.924 1.00 79.18 C ANISOU 1907 CB ALA A1036 9097 7343 13644 -910 90 1648 C ATOM 1908 N ALA A1037 -19.537 40.959 47.849 1.00 74.09 N ANISOU 1908 N ALA A1037 8403 6805 12943 -922 16 1346 N ATOM 1909 CA ALA A1037 -18.209 40.440 48.149 1.00 68.94 C ANISOU 1909 CA ALA A1037 7687 6111 12395 -965 -18 1147 C ATOM 1910 C ALA A1037 -17.209 40.858 47.084 1.00 77.08 C ANISOU 1910 C ALA A1037 8658 7221 13409 -941 202 1110 C ATOM 1911 O ALA A1037 -16.082 41.251 47.407 1.00 77.74 O ANISOU 1911 O ALA A1037 8632 7214 13690 -1009 321 987 O ATOM 1912 CB ALA A1037 -18.254 38.918 48.288 1.00 68.55 C ANISOU 1912 CB ALA A1037 7639 6081 12327 -946 -291 990 C ATOM 1913 N LEU A1038 -17.604 40.799 45.810 1.00 78.32 N ANISOU 1913 N LEU A1038 8889 7529 13341 -831 269 1200 N ATOM 1914 CA LEU A1038 -16.721 41.282 44.754 1.00 84.10 C ANISOU 1914 CA LEU A1038 9630 8328 13996 -798 574 1218 C ATOM 1915 C LEU A1038 -16.514 42.789 44.840 1.00 88.34 C ANISOU 1915 C LEU A1038 10206 8724 14634 -882 900 1412 C ATOM 1916 O LEU A1038 -15.431 43.286 44.507 1.00 88.82 O ANISOU 1916 O LEU A1038 10187 8732 14827 -959 1215 1383 O ATOM 1917 CB LEU A1038 -17.280 40.893 43.388 1.00 86.68 C ANISOU 1917 CB LEU A1038 10121 8837 13978 -598 547 1280 C ATOM 1918 CG LEU A1038 -17.269 39.388 43.133 1.00 87.57 C ANISOU 1918 CG LEU A1038 10169 9074 14031 -505 236 1042 C ATOM 1919 CD1 LEU A1038 -17.603 39.086 41.686 1.00 90.42 C ANISOU 1919 CD1 LEU A1038 10702 9614 14038 -257 216 1051 C ATOM 1920 CD2 LEU A1038 -15.922 38.793 43.516 1.00 87.94 C ANISOU 1920 CD2 LEU A1038 10025 9105 14283 -596 261 786 C ATOM 1921 N ASP A1039 -17.534 43.530 45.280 1.00 90.47 N ANISOU 1921 N ASP A1039 10577 8913 14885 -874 842 1594 N ATOM 1922 CA ASP A1039 -17.369 44.967 45.466 1.00 95.98 C ANISOU 1922 CA ASP A1039 11316 9438 15715 -948 1099 1763 C ATOM 1923 C ASP A1039 -16.385 45.266 46.587 1.00 88.03 C ANISOU 1923 C ASP A1039 10098 8255 15092 -1108 1130 1591 C ATOM 1924 O ASP A1039 -15.533 46.149 46.450 1.00 89.20 O ANISOU 1924 O ASP A1039 10173 8257 15462 -1209 1418 1611 O ATOM 1925 CB ASP A1039 -18.718 45.626 45.755 1.00100.63 C ANISOU 1925 CB ASP A1039 12036 9984 16216 -872 971 1940 C ATOM 1926 CG ASP A1039 -19.482 45.950 44.495 1.00105.31 C ANISOU 1926 CG ASP A1039 12875 10655 16484 -684 1009 2131 C ATOM 1927 OD1 ASP A1039 -18.828 46.104 43.440 1.00108.06 O ANISOU 1927 OD1 ASP A1039 13360 11033 16666 -635 1261 2212 O ATOM 1928 OD2 ASP A1039 -20.726 46.054 44.562 1.00104.71 O ANISOU 1928 OD2 ASP A1039 12863 10601 16320 -565 791 2183 O ATOM 1929 N ALA A1040 -16.490 44.539 47.702 1.00 82.75 N ANISOU 1929 N ALA A1040 9349 7572 14519 -1119 831 1410 N ATOM 1930 CA ALA A1040 -15.598 44.782 48.830 1.00 81.63 C ANISOU 1930 CA ALA A1040 9059 7250 14708 -1197 767 1200 C ATOM 1931 C ALA A1040 -14.161 44.399 48.493 1.00 88.20 C ANISOU 1931 C ALA A1040 9678 8065 15767 -1254 864 947 C ATOM 1932 O ALA A1040 -13.223 45.121 48.849 1.00 89.59 O ANISOU 1932 O ALA A1040 9674 8059 16308 -1340 985 807 O ATOM 1933 CB ALA A1040 -16.084 44.018 50.060 1.00 77.37 C ANISOU 1933 CB ALA A1040 8585 6689 14123 -1144 428 1087 C ATOM 1934 N GLN A1041 -13.968 43.264 47.816 1.00 94.45 N ANISOU 1934 N GLN A1041 10456 9034 16398 -1200 800 848 N ATOM 1935 CA GLN A1041 -12.629 42.888 47.372 1.00103.76 C ANISOU 1935 CA GLN A1041 11406 10226 17794 -1238 926 584 C ATOM 1936 C GLN A1041 -12.051 43.942 46.439 1.00107.36 C ANISOU 1936 C GLN A1041 11785 10634 18373 -1338 1432 715 C ATOM 1937 O GLN A1041 -10.863 44.271 46.518 1.00109.04 O ANISOU 1937 O GLN A1041 11721 10716 18992 -1446 1626 495 O ATOM 1938 CB GLN A1041 -12.667 41.524 46.681 1.00106.76 C ANISOU 1938 CB GLN A1041 11816 10821 17925 -1131 773 475 C ATOM 1939 CG GLN A1041 -11.319 41.037 46.170 1.00114.11 C ANISOU 1939 CG GLN A1041 12493 11799 19065 -1140 899 163 C ATOM 1940 CD GLN A1041 -11.409 39.681 45.492 1.00120.95 C ANISOU 1940 CD GLN A1041 13406 12877 19671 -1001 704 37 C ATOM 1941 OE1 GLN A1041 -12.479 39.277 45.028 1.00123.17 O ANISOU 1941 OE1 GLN A1041 13912 13286 19600 -906 584 233 O ATOM 1942 NE2 GLN A1041 -10.286 38.967 45.439 1.00122.22 N ANISOU 1942 NE2 GLN A1041 13330 13060 20048 -974 637 -334 N ATOM 1943 N LYS A1042 -12.886 44.492 45.556 1.00111.89 N ANISOU 1943 N LYS A1042 12611 11281 18620 -1296 1654 1065 N ATOM 1944 CA LYS A1042 -12.432 45.526 44.637 1.00119.46 C ANISOU 1944 CA LYS A1042 13608 12157 19625 -1378 2176 1263 C ATOM 1945 C LYS A1042 -12.054 46.809 45.369 1.00122.54 C ANISOU 1945 C LYS A1042 13865 12241 20452 -1543 2329 1291 C ATOM 1946 O LYS A1042 -11.203 47.566 44.887 1.00125.22 O ANISOU 1946 O LYS A1042 14087 12424 21069 -1687 2782 1326 O ATOM 1947 CB LYS A1042 -13.522 45.805 43.600 1.00123.58 C ANISOU 1947 CB LYS A1042 14520 12796 19637 -1226 2278 1625 C ATOM 1948 CG LYS A1042 -13.044 46.520 42.348 1.00130.81 C ANISOU 1948 CG LYS A1042 15608 13676 20418 -1238 2841 1853 C ATOM 1949 CD LYS A1042 -12.289 45.575 41.426 1.00134.72 C ANISOU 1949 CD LYS A1042 16049 14383 20755 -1168 3032 1689 C ATOM 1950 CE LYS A1042 -11.926 46.258 40.117 1.00140.76 C ANISOU 1950 CE LYS A1042 17085 15123 21274 -1141 3650 1964 C ATOM 1951 NZ LYS A1042 -11.319 45.306 39.149 1.00143.76 N ANISOU 1951 NZ LYS A1042 17467 15751 21405 -1013 3838 1805 N ATOM 1952 N ALA A1043 -12.654 47.066 46.534 1.00121.03 N ANISOU 1952 N ALA A1043 13688 11946 20352 -1522 1977 1263 N ATOM 1953 CA ALA A1043 -12.495 48.333 47.238 1.00121.78 C ANISOU 1953 CA ALA A1043 13705 11751 20815 -1627 2050 1294 C ATOM 1954 C ALA A1043 -11.778 48.183 48.580 1.00122.35 C ANISOU 1954 C ALA A1043 13501 11666 21321 -1650 1732 901 C ATOM 1955 O ALA A1043 -12.060 48.926 49.523 1.00121.40 O ANISOU 1955 O ALA A1043 13394 11364 21370 -1635 1557 882 O ATOM 1956 CB ALA A1043 -13.858 48.996 47.436 1.00119.35 C ANISOU 1956 CB ALA A1043 13688 11430 20229 -1532 1922 1590 C ATOM 1957 N THR A1044 -10.849 47.236 48.685 1.00127.35 N ANISOU 1957 N THR A1044 13904 12358 22125 -1647 1618 557 N ATOM 1958 CA THR A1044 -10.102 47.032 49.928 1.00125.63 C ANISOU 1958 CA THR A1044 13461 11971 22302 -1607 1249 134 C ATOM 1959 C THR A1044 -8.660 46.615 49.644 1.00128.78 C ANISOU 1959 C THR A1044 13468 12318 23147 -1679 1353 -261 C ATOM 1960 O THR A1044 -7.975 47.219 48.820 1.00134.87 O ANISOU 1960 O THR A1044 14023 13006 24217 -1851 1834 -230 O ATOM 1961 CB THR A1044 -10.760 45.958 50.837 1.00119.24 C ANISOU 1961 CB THR A1044 12871 11285 21149 -1416 739 45 C ATOM 1962 OG1 THR A1044 -12.156 46.237 51.007 1.00113.61 O ANISOU 1962 OG1 THR A1044 12476 10651 20041 -1361 699 394 O ATOM 1963 CG2 THR A1044 -10.092 45.939 52.202 1.00120.03 C ANISOU 1963 CG2 THR A1044 12862 11166 21578 -1309 330 -356 C ATOM 1964 N PRO A1056 2.661 40.594 50.088 1.00151.20 N ANISOU 1964 N PRO A1056 12329 14750 30372 -1046 -138 -5671 N ATOM 1965 CA PRO A1056 2.675 40.756 51.547 1.00150.75 C ANISOU 1965 CA PRO A1056 12509 14466 30303 -702 -871 -5862 C ATOM 1966 C PRO A1056 1.287 40.628 52.177 1.00145.31 C ANISOU 1966 C PRO A1056 12495 13785 28933 -670 -1246 -5380 C ATOM 1967 O PRO A1056 0.665 39.565 52.094 1.00141.23 O ANISOU 1967 O PRO A1056 12374 13429 27857 -566 -1527 -5231 O ATOM 1968 CB PRO A1056 3.233 42.174 51.738 1.00154.48 C ANISOU 1968 CB PRO A1056 12651 14696 31347 -806 -502 -5914 C ATOM 1969 CG PRO A1056 2.949 42.875 50.451 1.00154.87 C ANISOU 1969 CG PRO A1056 12587 14836 31422 -1266 440 -5452 C ATOM 1970 CD PRO A1056 3.090 41.819 49.393 1.00155.84 C ANISOU 1970 CD PRO A1056 12583 15249 31378 -1349 696 -5509 C ATOM 1971 N GLU A1057 0.817 41.712 52.802 1.00143.21 N ANISOU 1971 N GLU A1057 12393 13352 28667 -716 -1217 -5120 N ATOM 1972 CA GLU A1057 -0.473 41.695 53.482 1.00137.81 C ANISOU 1972 CA GLU A1057 12350 12635 27376 -663 -1529 -4696 C ATOM 1973 C GLU A1057 -1.644 41.595 52.513 1.00133.09 C ANISOU 1973 C GLU A1057 12124 12363 26082 -857 -1007 -3970 C ATOM 1974 O GLU A1057 -2.748 41.230 52.932 1.00126.71 O ANISOU 1974 O GLU A1057 11876 11649 24619 -744 -1237 -3586 O ATOM 1975 CB GLU A1057 -0.620 42.945 54.353 1.00137.82 C ANISOU 1975 CB GLU A1057 12402 12439 27522 -610 -1591 -4610 C ATOM 1976 N MET A1058 -1.430 41.909 51.232 1.00135.16 N ANISOU 1976 N MET A1058 12098 12784 26471 -1124 -306 -3789 N ATOM 1977 CA MET A1058 -2.496 41.803 50.243 1.00133.04 C ANISOU 1977 CA MET A1058 12198 12819 25534 -1245 137 -3153 C ATOM 1978 C MET A1058 -2.679 40.381 49.723 1.00131.70 C ANISOU 1978 C MET A1058 12207 12928 24905 -1096 -46 -3174 C ATOM 1979 O MET A1058 -3.697 40.103 49.079 1.00127.54 O ANISOU 1979 O MET A1058 12049 12637 23772 -1118 135 -2697 O ATOM 1980 CB MET A1058 -2.227 42.754 49.073 1.00135.40 C ANISOU 1980 CB MET A1058 12226 13149 26071 -1544 968 -2915 C ATOM 1981 N LYS A1059 -1.722 39.481 49.976 1.00134.10 N ANISOU 1981 N LYS A1059 12247 13193 25513 -925 -437 -3748 N ATOM 1982 CA LYS A1059 -1.903 38.077 49.616 1.00134.31 C ANISOU 1982 CA LYS A1059 12471 13438 25122 -750 -717 -3805 C ATOM 1983 C LYS A1059 -2.777 37.357 50.636 1.00134.67 C ANISOU 1983 C LYS A1059 13071 13413 24683 -537 -1356 -3658 C ATOM 1984 O LYS A1059 -3.599 36.510 50.267 1.00131.75 O ANISOU 1984 O LYS A1059 13053 13228 23778 -486 -1434 -3369 O ATOM 1985 CB LYS A1059 -0.546 37.382 49.490 1.00135.39 C ANISOU 1985 CB LYS A1059 12118 13543 25780 -629 -909 -4497 C ATOM 1986 N ASP A1060 -2.597 37.675 51.921 1.00139.77 N ANISOU 1986 N ASP A1060 13808 13772 25526 -401 -1808 -3869 N ATOM 1987 CA ASP A1060 -3.519 37.205 52.951 1.00141.52 C ANISOU 1987 CA ASP A1060 14626 13898 25247 -220 -2284 -3640 C ATOM 1988 C ASP A1060 -4.930 37.719 52.687 1.00138.64 C ANISOU 1988 C ASP A1060 14614 13680 24384 -395 -1905 -2959 C ATOM 1989 O ASP A1060 -5.919 37.023 52.952 1.00134.31 O ANISOU 1989 O ASP A1060 14519 13185 23326 -328 -2086 -2652 O ATOM 1990 CB ASP A1060 -3.017 37.665 54.325 1.00144.84 C ANISOU 1990 CB ASP A1060 15089 13981 25962 -15 -2769 -3998 C ATOM 1991 CG ASP A1060 -3.570 36.837 55.467 1.00146.08 C ANISOU 1991 CG ASP A1060 15873 13993 25640 274 -3366 -3946 C ATOM 1992 OD1 ASP A1060 -4.765 36.481 55.430 1.00143.59 O ANISOU 1992 OD1 ASP A1060 16006 13800 24754 213 -3243 -3426 O ATOM 1993 OD2 ASP A1060 -2.800 36.547 56.408 1.00149.66 O ANISOU 1993 OD2 ASP A1060 16375 14229 26260 584 -3935 -4406 O ATOM 1994 N PHE A1061 -5.032 38.935 52.145 1.00135.32 N ANISOU 1994 N PHE A1061 13974 13300 24142 -622 -1372 -2734 N ATOM 1995 CA PHE A1061 -6.325 39.546 51.851 1.00130.34 C ANISOU 1995 CA PHE A1061 13638 12789 23094 -765 -1030 -2137 C ATOM 1996 C PHE A1061 -7.077 38.768 50.780 1.00126.46 C ANISOU 1996 C PHE A1061 13313 12587 22149 -809 -837 -1823 C ATOM 1997 O PHE A1061 -8.274 38.487 50.925 1.00123.51 O ANISOU 1997 O PHE A1061 13310 12285 21332 -793 -907 -1459 O ATOM 1998 CB PHE A1061 -6.103 40.999 51.420 1.00130.38 C ANISOU 1998 CB PHE A1061 13365 12732 23440 -977 -521 -2012 C ATOM 1999 CG PHE A1061 -7.295 41.639 50.770 1.00126.27 C ANISOU 1999 CG PHE A1061 13092 12360 22526 -1118 -112 -1432 C ATOM 2000 CD1 PHE A1061 -8.271 42.247 51.537 1.00124.30 C ANISOU 2000 CD1 PHE A1061 13140 12025 22061 -1096 -213 -1150 C ATOM 2001 CD2 PHE A1061 -7.423 41.660 49.390 1.00125.99 C ANISOU 2001 CD2 PHE A1061 13002 12540 22330 -1237 363 -1198 C ATOM 2002 CE1 PHE A1061 -9.355 42.844 50.946 1.00122.60 C ANISOU 2002 CE1 PHE A1061 13123 11930 21528 -1196 114 -674 C ATOM 2003 CE2 PHE A1061 -8.511 42.256 48.794 1.00125.45 C ANISOU 2003 CE2 PHE A1061 13191 12580 21894 -1311 667 -704 C ATOM 2004 CZ PHE A1061 -9.480 42.851 49.574 1.00123.68 C ANISOU 2004 CZ PHE A1061 13221 12261 21511 -1295 527 -454 C ATOM 2005 N ARG A1062 -6.393 38.433 49.682 1.00123.34 N ANISOU 2005 N ARG A1062 12628 12354 21883 -854 -581 -1984 N ATOM 2006 CA ARG A1062 -7.020 37.645 48.626 1.00120.63 C ANISOU 2006 CA ARG A1062 12440 12280 21113 -837 -458 -1760 C ATOM 2007 C ARG A1062 -7.501 36.305 49.162 1.00114.33 C ANISOU 2007 C ARG A1062 11935 11474 20032 -668 -999 -1819 C ATOM 2008 O ARG A1062 -8.594 35.847 48.811 1.00109.80 O ANISOU 2008 O ARG A1062 11639 11024 19057 -665 -1014 -1496 O ATOM 2009 CB ARG A1062 -6.040 37.436 47.468 1.00125.59 C ANISOU 2009 CB ARG A1062 12714 13071 21934 -860 -123 -2010 C ATOM 2010 CG ARG A1062 -5.589 38.716 46.771 1.00130.04 C ANISOU 2010 CG ARG A1062 13026 13628 22756 -1056 533 -1890 C ATOM 2011 CD ARG A1062 -4.386 38.470 45.858 1.00133.73 C ANISOU 2011 CD ARG A1062 13083 14204 23526 -1076 880 -2241 C ATOM 2012 NE ARG A1062 -4.704 37.589 44.739 1.00132.14 N ANISOU 2012 NE ARG A1062 13038 14304 22865 -958 979 -2150 N ATOM 2013 N HIS A1063 -6.703 35.671 50.030 1.00110.20 N ANISOU 2013 N HIS A1063 11362 10767 19740 -517 -1464 -2241 N ATOM 2014 CA HIS A1063 -7.067 34.353 50.543 1.00105.35 C ANISOU 2014 CA HIS A1063 11070 10089 18870 -351 -1974 -2296 C ATOM 2015 C HIS A1063 -8.381 34.404 51.309 1.00 94.94 C ANISOU 2015 C HIS A1063 10205 8679 17189 -376 -2062 -1866 C ATOM 2016 O HIS A1063 -9.211 33.493 51.195 1.00 86.40 O ANISOU 2016 O HIS A1063 9388 7634 15806 -357 -2203 -1672 O ATOM 2017 CB HIS A1063 -5.957 33.797 51.435 1.00107.00 C ANISOU 2017 CB HIS A1063 11210 10065 19380 -141 -2492 -2830 C ATOM 2018 CG HIS A1063 -6.217 32.399 51.910 1.00106.64 C ANISOU 2018 CG HIS A1063 11532 9908 19077 45 -3017 -2896 C ATOM 2019 ND1 HIS A1063 -6.356 31.334 51.044 1.00102.91 N ANISOU 2019 ND1 HIS A1063 11052 9593 18455 75 -3079 -2920 N ATOM 2020 CD2 HIS A1063 -6.387 31.894 53.156 1.00106.94 C ANISOU 2020 CD2 HIS A1063 11998 9667 18967 221 -3494 -2925 C ATOM 2021 CE1 HIS A1063 -6.588 30.232 51.736 1.00101.87 C ANISOU 2021 CE1 HIS A1063 11299 9261 18144 233 -3575 -2961 C ATOM 2022 NE2 HIS A1063 -6.613 30.544 53.019 1.00105.08 N ANISOU 2022 NE2 HIS A1063 12003 9399 18525 324 -3812 -2944 N ATOM 2023 N GLY A1064 -8.583 35.459 52.103 1.00 87.82 N ANISOU 2023 N GLY A1064 9374 7643 16349 -420 -1969 -1738 N ATOM 2024 CA GLY A1064 -9.838 35.600 52.819 1.00 84.30 C ANISOU 2024 CA GLY A1064 9326 7131 15575 -447 -1975 -1342 C ATOM 2025 C GLY A1064 -11.025 35.700 51.881 1.00 86.10 C ANISOU 2025 C GLY A1064 9592 7579 15545 -601 -1631 -922 C ATOM 2026 O GLY A1064 -12.021 34.987 52.040 1.00 82.40 O ANISOU 2026 O GLY A1064 9390 7105 14815 -605 -1728 -698 O ATOM 2027 N PHE A1065 -10.929 36.574 50.876 1.00 74.02 N ANISOU 2027 N PHE A1065 7801 6219 14103 -717 -1227 -826 N ATOM 2028 CA PHE A1065 -12.032 36.708 49.931 1.00 73.93 C ANISOU 2028 CA PHE A1065 7856 6405 13831 -801 -959 -469 C ATOM 2029 C PHE A1065 -12.146 35.496 49.018 1.00 79.69 C ANISOU 2029 C PHE A1065 8581 7289 14409 -737 -1086 -541 C ATOM 2030 O PHE A1065 -13.243 35.197 48.534 1.00 79.35 O ANISOU 2030 O PHE A1065 8667 7345 14139 -749 -1064 -302 O ATOM 2031 CB PHE A1065 -11.876 37.980 49.106 1.00 73.73 C ANISOU 2031 CB PHE A1065 7648 6479 13889 -902 -506 -329 C ATOM 2032 CG PHE A1065 -12.419 39.199 49.788 1.00 73.82 C ANISOU 2032 CG PHE A1065 7744 6368 13935 -974 -364 -104 C ATOM 2033 CD1 PHE A1065 -13.766 39.511 49.701 1.00 72.70 C ANISOU 2033 CD1 PHE A1065 7796 6287 13540 -1000 -277 242 C ATOM 2034 CD2 PHE A1065 -11.586 40.026 50.535 1.00 79.61 C ANISOU 2034 CD2 PHE A1065 8340 6914 14996 -995 -355 -286 C ATOM 2035 CE1 PHE A1065 -14.280 40.624 50.342 1.00 72.23 C ANISOU 2035 CE1 PHE A1065 7808 6120 13515 -1042 -165 420 C ATOM 2036 CE2 PHE A1065 -12.098 41.150 51.175 1.00 78.92 C ANISOU 2036 CE2 PHE A1065 8337 6708 14943 -1035 -258 -103 C ATOM 2037 CZ PHE A1065 -13.446 41.448 51.074 1.00 74.24 C ANISOU 2037 CZ PHE A1065 7955 6195 14060 -1057 -154 258 C ATOM 2038 N ASP A1066 -11.033 34.799 48.768 1.00 80.60 N ANISOU 2038 N ASP A1066 8525 7419 14682 -649 -1244 -908 N ATOM 2039 CA ASP A1066 -11.081 33.563 47.996 1.00 83.71 C ANISOU 2039 CA ASP A1066 8923 7938 14945 -552 -1435 -1032 C ATOM 2040 C ASP A1066 -11.921 32.513 48.705 1.00 79.53 C ANISOU 2040 C ASP A1066 8685 7256 14278 -518 -1816 -942 C ATOM 2041 O ASP A1066 -12.786 31.879 48.091 1.00 80.80 O ANISOU 2041 O ASP A1066 8926 7502 14273 -512 -1871 -806 O ATOM 2042 CB ASP A1066 -9.667 33.036 47.754 1.00 92.13 C ANISOU 2042 CB ASP A1066 9732 9022 16250 -446 -1561 -1495 C ATOM 2043 CG ASP A1066 -8.961 33.752 46.624 1.00 98.63 C ANISOU 2043 CG ASP A1066 10256 10051 17169 -484 -1092 -1569 C ATOM 2044 OD1 ASP A1066 -9.623 34.051 45.610 1.00101.86 O ANISOU 2044 OD1 ASP A1066 10735 10654 17313 -503 -792 -1300 O ATOM 2045 OD2 ASP A1066 -7.743 34.010 46.750 1.00100.15 O ANISOU 2045 OD2 ASP A1066 10151 10191 17709 -483 -1019 -1909 O ATOM 2046 N ILE A1067 -11.668 32.307 50.002 1.00 73.91 N ANISOU 2046 N ILE A1067 8151 6289 13643 -483 -2084 -1027 N ATOM 2047 CA ILE A1067 -12.503 31.398 50.783 1.00 76.56 C ANISOU 2047 CA ILE A1067 8830 6426 13832 -474 -2353 -876 C ATOM 2048 C ILE A1067 -13.958 31.855 50.754 1.00 78.48 C ANISOU 2048 C ILE A1067 9185 6712 13923 -619 -2091 -458 C ATOM 2049 O ILE A1067 -14.881 31.039 50.648 1.00 77.72 O ANISOU 2049 O ILE A1067 9213 6565 13751 -661 -2183 -315 O ATOM 2050 CB ILE A1067 -11.974 31.283 52.223 1.00 74.28 C ANISOU 2050 CB ILE A1067 8801 5843 13578 -369 -2637 -1006 C ATOM 2051 CG1 ILE A1067 -10.520 30.812 52.238 1.00 76.26 C ANISOU 2051 CG1 ILE A1067 8901 6034 14040 -190 -2965 -1495 C ATOM 2052 CG2 ILE A1067 -12.842 30.332 53.033 1.00 74.48 C ANISOU 2052 CG2 ILE A1067 9254 5629 13417 -369 -2834 -799 C ATOM 2053 CD1 ILE A1067 -9.922 30.725 53.637 1.00 77.78 C ANISOU 2053 CD1 ILE A1067 9378 5915 14259 -11 -3331 -1690 C ATOM 2054 N LEU A1068 -14.183 33.168 50.815 1.00 75.64 N ANISOU 2054 N LEU A1068 8747 6429 13565 -696 -1771 -286 N ATOM 2055 CA LEU A1068 -15.545 33.681 50.874 1.00 69.90 C ANISOU 2055 CA LEU A1068 8105 5730 12725 -807 -1546 64 C ATOM 2056 C LEU A1068 -16.288 33.433 49.569 1.00 69.79 C ANISOU 2056 C LEU A1068 7953 5917 12646 -824 -1466 154 C ATOM 2057 O LEU A1068 -17.412 32.913 49.572 1.00 69.69 O ANISOU 2057 O LEU A1068 8014 5860 12607 -877 -1513 304 O ATOM 2058 CB LEU A1068 -15.526 35.176 51.199 1.00 69.33 C ANISOU 2058 CB LEU A1068 7978 5679 12684 -852 -1267 186 C ATOM 2059 CG LEU A1068 -16.922 35.781 51.323 1.00 68.42 C ANISOU 2059 CG LEU A1068 7933 5589 12473 -941 -1053 508 C ATOM 2060 CD1 LEU A1068 -17.590 35.195 52.545 1.00 68.62 C ANISOU 2060 CD1 LEU A1068 8230 5410 12432 -962 -1150 614 C ATOM 2061 CD2 LEU A1068 -16.849 37.312 51.400 1.00 68.07 C ANISOU 2061 CD2 LEU A1068 7807 5581 12474 -966 -791 608 C ATOM 2062 N VAL A1069 -15.683 33.817 48.443 1.00 70.31 N ANISOU 2062 N VAL A1069 7827 6189 12699 -766 -1335 49 N ATOM 2063 CA VAL A1069 -16.363 33.697 47.155 1.00 70.72 C ANISOU 2063 CA VAL A1069 7813 6437 12622 -712 -1278 120 C ATOM 2064 C VAL A1069 -16.512 32.231 46.752 1.00 71.95 C ANISOU 2064 C VAL A1069 7977 6582 12779 -632 -1615 -54 C ATOM 2065 O VAL A1069 -17.551 31.822 46.216 1.00 73.74 O ANISOU 2065 O VAL A1069 8207 6841 12969 -609 -1711 21 O ATOM 2066 CB VAL A1069 -15.608 34.512 46.091 1.00 71.81 C ANISOU 2066 CB VAL A1069 7825 6774 12684 -647 -994 77 C ATOM 2067 CG1 VAL A1069 -16.241 34.332 44.726 1.00 73.00 C ANISOU 2067 CG1 VAL A1069 7995 7123 12619 -512 -980 124 C ATOM 2068 CG2 VAL A1069 -15.599 35.981 46.478 1.00 75.91 C ANISOU 2068 CG2 VAL A1069 8345 7251 13247 -743 -673 275 C ATOM 2069 N GLY A1070 -15.481 31.419 46.999 1.00 72.21 N ANISOU 2069 N GLY A1070 7996 6547 12894 -573 -1836 -323 N ATOM 2070 CA GLY A1070 -15.600 29.997 46.732 1.00 73.14 C ANISOU 2070 CA GLY A1070 8144 6604 13044 -494 -2198 -498 C ATOM 2071 C GLY A1070 -16.713 29.353 47.532 1.00 72.87 C ANISOU 2071 C GLY A1070 8278 6322 13088 -610 -2351 -319 C ATOM 2072 O GLY A1070 -17.427 28.483 47.031 1.00 73.74 O ANISOU 2072 O GLY A1070 8366 6398 13253 -592 -2549 -348 O ATOM 2073 N GLN A1071 -16.890 29.789 48.780 1.00 72.13 N ANISOU 2073 N GLN A1071 8351 6038 13016 -726 -2240 -140 N ATOM 2074 CA GLN A1071 -17.958 29.248 49.609 1.00 72.50 C ANISOU 2074 CA GLN A1071 8581 5835 13130 -857 -2271 66 C ATOM 2075 C GLN A1071 -19.327 29.672 49.100 1.00 72.31 C ANISOU 2075 C GLN A1071 8418 5901 13156 -948 -2079 265 C ATOM 2076 O GLN A1071 -20.272 28.874 49.116 1.00 73.48 O ANISOU 2076 O GLN A1071 8561 5898 13462 -1032 -2171 318 O ATOM 2077 CB GLN A1071 -17.759 29.674 51.057 1.00 72.28 C ANISOU 2077 CB GLN A1071 8817 5603 13044 -906 -2169 197 C ATOM 2078 CG GLN A1071 -16.823 28.750 51.814 1.00 75.01 C ANISOU 2078 CG GLN A1071 9417 5709 13376 -804 -2493 13 C ATOM 2079 CD GLN A1071 -16.381 29.301 53.151 1.00 74.91 C ANISOU 2079 CD GLN A1071 9690 5522 13251 -755 -2456 63 C ATOM 2080 OE1 GLN A1071 -16.331 30.516 53.350 1.00 76.81 O ANISOU 2080 OE1 GLN A1071 9847 5883 13457 -766 -2219 132 O ATOM 2081 NE2 GLN A1071 -16.055 28.406 54.080 1.00 75.53 N ANISOU 2081 NE2 GLN A1071 10144 5293 13261 -670 -2721 18 N ATOM 2082 N ILE A1072 -19.454 30.918 48.634 1.00 71.28 N ANISOU 2082 N ILE A1072 8164 5987 12933 -925 -1828 354 N ATOM 2083 CA ILE A1072 -20.707 31.352 48.024 1.00 71.49 C ANISOU 2083 CA ILE A1072 8052 6106 13004 -949 -1717 482 C ATOM 2084 C ILE A1072 -21.017 30.517 46.787 1.00 72.84 C ANISOU 2084 C ILE A1072 8085 6370 13222 -824 -1984 298 C ATOM 2085 O ILE A1072 -22.165 30.112 46.566 1.00 74.00 O ANISOU 2085 O ILE A1072 8125 6439 13552 -861 -2077 311 O ATOM 2086 CB ILE A1072 -20.651 32.856 47.697 1.00 70.69 C ANISOU 2086 CB ILE A1072 7902 6194 12761 -905 -1440 601 C ATOM 2087 CG1 ILE A1072 -20.532 33.677 48.983 1.00 71.75 C ANISOU 2087 CG1 ILE A1072 8159 6209 12893 -1015 -1219 761 C ATOM 2088 CG2 ILE A1072 -21.880 33.285 46.926 1.00 71.17 C ANISOU 2088 CG2 ILE A1072 7842 6353 12847 -859 -1408 678 C ATOM 2089 CD1 ILE A1072 -20.380 35.167 48.747 1.00 68.77 C ANISOU 2089 CD1 ILE A1072 7740 5965 12423 -983 -966 867 C ATOM 2090 N ASP A1073 -20.000 30.230 45.971 1.00 73.16 N ANISOU 2090 N ASP A1073 8107 6567 13124 -659 -2117 88 N ATOM 2091 CA ASP A1073 -20.226 29.448 44.757 1.00 74.80 C ANISOU 2091 CA ASP A1073 8217 6881 13323 -481 -2395 -123 C ATOM 2092 C ASP A1073 -20.577 27.996 45.081 1.00 76.03 C ANISOU 2092 C ASP A1073 8365 6788 13737 -543 -2732 -250 C ATOM 2093 O ASP A1073 -21.438 27.404 44.422 1.00 78.12 O ANISOU 2093 O ASP A1073 8509 7020 14153 -479 -2963 -356 O ATOM 2094 CB ASP A1073 -19.005 29.527 43.838 1.00 76.48 C ANISOU 2094 CB ASP A1073 8426 7333 13300 -280 -2388 -320 C ATOM 2095 CG ASP A1073 -18.845 30.906 43.183 1.00 82.39 C ANISOU 2095 CG ASP A1073 9195 8309 13800 -198 -2039 -181 C ATOM 2096 OD1 ASP A1073 -19.801 31.708 43.220 1.00 74.81 O ANISOU 2096 OD1 ASP A1073 8251 7342 12831 -237 -1907 26 O ATOM 2097 OD2 ASP A1073 -17.762 31.184 42.624 1.00 80.44 O ANISOU 2097 OD2 ASP A1073 8949 8230 13386 -94 -1881 -285 O ATOM 2098 N ASP A1074 -19.931 27.406 46.092 1.00 79.02 N ANISOU 2098 N ASP A1074 8885 6953 14185 -650 -2792 -254 N ATOM 2099 CA ASP A1074 -20.330 26.072 46.533 1.00 77.33 C ANISOU 2099 CA ASP A1074 8729 6428 14225 -739 -3067 -309 C ATOM 2100 C ASP A1074 -21.797 26.053 46.950 1.00 82.92 C ANISOU 2100 C ASP A1074 9370 6938 15199 -939 -2939 -105 C ATOM 2101 O ASP A1074 -22.536 25.123 46.607 1.00 80.34 O ANISOU 2101 O ASP A1074 8922 6441 15161 -972 -3168 -208 O ATOM 2102 CB ASP A1074 -19.450 25.599 47.692 1.00 77.22 C ANISOU 2102 CB ASP A1074 8976 6178 14187 -799 -3126 -297 C ATOM 2103 CG ASP A1074 -18.001 25.353 47.282 1.00 77.14 C ANISOU 2103 CG ASP A1074 8964 6311 14036 -594 -3334 -597 C ATOM 2104 OD1 ASP A1074 -17.714 25.299 46.070 1.00 77.57 O ANISOU 2104 OD1 ASP A1074 8831 6623 14018 -418 -3435 -814 O ATOM 2105 OD2 ASP A1074 -17.151 25.197 48.185 1.00 77.10 O ANISOU 2105 OD2 ASP A1074 9154 6150 13992 -585 -3404 -638 O ATOM 2106 N ALA A1075 -22.237 27.072 47.693 1.00 77.10 N ANISOU 2106 N ALA A1075 8678 6205 14412 -1074 -2572 154 N ATOM 2107 CA ALA A1075 -23.625 27.107 48.132 1.00 78.38 C ANISOU 2107 CA ALA A1075 8735 6189 14858 -1268 -2390 324 C ATOM 2108 C ALA A1075 -24.573 27.377 46.970 1.00 85.29 C ANISOU 2108 C ALA A1075 9295 7228 15885 -1164 -2499 193 C ATOM 2109 O ALA A1075 -25.710 26.892 46.977 1.00 88.27 O ANISOU 2109 O ALA A1075 9475 7414 16650 -1284 -2536 169 O ATOM 2110 CB ALA A1075 -23.808 28.153 49.229 1.00 77.18 C ANISOU 2110 CB ALA A1075 8719 6020 14584 -1396 -1978 599 C ATOM 2111 N LEU A1076 -24.129 28.133 45.961 1.00 78.22 N ANISOU 2111 N LEU A1076 8358 6656 14706 -927 -2554 93 N ATOM 2112 CA LEU A1076 -24.995 28.408 44.816 1.00 79.62 C ANISOU 2112 CA LEU A1076 8321 6977 14952 -750 -2718 -50 C ATOM 2113 C LEU A1076 -25.163 27.181 43.934 1.00 84.65 C ANISOU 2113 C LEU A1076 8832 7547 15782 -605 -3171 -358 C ATOM 2114 O LEU A1076 -26.262 26.914 43.443 1.00 84.31 O ANISOU 2114 O LEU A1076 8556 7421 16057 -561 -3376 -506 O ATOM 2115 CB LEU A1076 -24.443 29.572 43.995 1.00 78.41 C ANISOU 2115 CB LEU A1076 8259 7154 14378 -515 -2613 -29 C ATOM 2116 CG LEU A1076 -24.935 30.955 44.401 1.00 80.72 C ANISOU 2116 CG LEU A1076 8561 7510 14598 -579 -2278 205 C ATOM 2117 CD1 LEU A1076 -24.049 32.038 43.784 1.00 79.46 C ANISOU 2117 CD1 LEU A1076 8569 7607 14016 -402 -2108 276 C ATOM 2118 CD2 LEU A1076 -26.394 31.133 43.985 1.00 79.33 C ANISOU 2118 CD2 LEU A1076 8163 7290 14688 -521 -2404 131 C ATOM 2119 N LYS A1077 -24.077 26.441 43.699 1.00 86.29 N ANISOU 2119 N LYS A1077 9169 7788 15830 -505 -3365 -502 N ATOM 2120 CA LYS A1077 -24.169 25.212 42.918 1.00 89.90 C ANISOU 2120 CA LYS A1077 9520 8162 16474 -353 -3829 -821 C ATOM 2121 C LYS A1077 -25.171 24.247 43.543 1.00 96.22 C ANISOU 2121 C LYS A1077 10161 8557 17843 -605 -3945 -827 C ATOM 2122 O LYS A1077 -25.997 23.652 42.838 1.00100.96 O ANISOU 2122 O LYS A1077 10524 9058 18777 -510 -4281 -1074 O ATOM 2123 CB LYS A1077 -22.784 24.571 42.801 1.00 85.61 C ANISOU 2123 CB LYS A1077 9143 7686 15700 -238 -3979 -968 C ATOM 2124 CG LYS A1077 -22.677 23.489 41.749 1.00 89.34 C ANISOU 2124 CG LYS A1077 9532 8176 16239 23 -4473 -1345 C ATOM 2125 N LEU A1078 -25.112 24.085 44.869 1.00 93.69 N ANISOU 2125 N LEU A1078 9978 7975 17645 -915 -3661 -565 N ATOM 2126 CA LEU A1078 -26.142 23.343 45.588 1.00 89.46 C ANISOU 2126 CA LEU A1078 9321 7026 17645 -1209 -3603 -484 C ATOM 2127 C LEU A1078 -27.526 23.915 45.311 1.00 94.46 C ANISOU 2127 C LEU A1078 9612 7664 18615 -1260 -3497 -506 C ATOM 2128 O LEU A1078 -28.487 23.166 45.089 1.00 98.47 O ANISOU 2128 O LEU A1078 9829 7910 19676 -1350 -3685 -679 O ATOM 2129 CB LEU A1078 -25.847 23.380 47.088 1.00 87.56 C ANISOU 2129 CB LEU A1078 9383 6555 17330 -1484 -3208 -139 C ATOM 2130 CG LEU A1078 -25.370 22.137 47.839 1.00 91.19 C ANISOU 2130 CG LEU A1078 10113 6627 17907 -1618 -3322 -90 C ATOM 2131 CD1 LEU A1078 -24.876 21.043 46.903 1.00 93.66 C ANISOU 2131 CD1 LEU A1078 10360 6906 18321 -1420 -3874 -438 C ATOM 2132 CD2 LEU A1078 -24.285 22.533 48.831 1.00 86.97 C ANISOU 2132 CD2 LEU A1078 10001 6118 16924 -1610 -3124 116 C ATOM 2133 N ALA A1079 -27.644 25.244 45.308 1.00 92.36 N ANISOU 2133 N ALA A1079 9353 7671 18067 -1194 -3223 -367 N ATOM 2134 CA ALA A1079 -28.951 25.885 45.173 1.00 96.18 C ANISOU 2134 CA ALA A1079 9524 8153 18870 -1233 -3113 -392 C ATOM 2135 C ALA A1079 -29.588 25.574 43.822 1.00103.36 C ANISOU 2135 C ALA A1079 10140 9122 20011 -949 -3616 -788 C ATOM 2136 O ALA A1079 -30.773 25.224 43.748 1.00107.65 O ANISOU 2136 O ALA A1079 10315 9441 21146 -1042 -3721 -961 O ATOM 2137 CB ALA A1079 -28.816 27.398 45.373 1.00 88.55 C ANISOU 2137 CB ALA A1079 8675 7468 17501 -1167 -2781 -181 C ATOM 2138 N ASN A1080 -28.812 25.695 42.739 1.00106.37 N ANISOU 2138 N ASN A1080 10679 9794 19943 -583 -3929 -960 N ATOM 2139 CA ASN A1080 -29.334 25.423 41.403 1.00112.66 C ANISOU 2139 CA ASN A1080 11292 10669 20847 -224 -4452 -1356 C ATOM 2140 C ASN A1080 -29.822 23.987 41.252 1.00113.27 C ANISOU 2140 C ASN A1080 11107 10407 21525 -293 -4851 -1655 C ATOM 2141 O ASN A1080 -30.608 23.703 40.343 1.00113.74 O ANISOU 2141 O ASN A1080 10903 10423 21891 -49 -5305 -2028 O ATOM 2142 CB ASN A1080 -28.265 25.712 40.348 1.00115.12 C ANISOU 2142 CB ASN A1080 11906 11341 20493 179 -4636 -1450 C ATOM 2143 CG ASN A1080 -27.788 27.143 40.382 1.00116.00 C ANISOU 2143 CG ASN A1080 12266 11747 20063 251 -4245 -1168 C ATOM 2144 OD1 ASN A1080 -28.549 28.052 40.703 1.00119.18 O ANISOU 2144 OD1 ASN A1080 12578 12144 20560 175 -4035 -1029 O ATOM 2145 ND2 ASN A1080 -26.519 27.353 40.050 1.00113.61 N ANISOU 2145 ND2 ASN A1080 12255 11683 19227 393 -4137 -1100 N ATOM 2146 N GLU A1081 -29.366 23.082 42.114 1.00110.53 N ANISOU 2146 N GLU A1081 10846 9792 21358 -596 -4724 -1516 N ATOM 2147 CA GLU A1081 -29.808 21.698 42.121 1.00113.68 C ANISOU 2147 CA GLU A1081 11023 9791 22379 -726 -5045 -1746 C ATOM 2148 C GLU A1081 -30.904 21.443 43.149 1.00116.34 C ANISOU 2148 C GLU A1081 11086 9707 23410 -1177 -4702 -1590 C ATOM 2149 O GLU A1081 -31.280 20.289 43.364 1.00120.35 O ANISOU 2149 O GLU A1081 11426 9798 24502 -1381 -4849 -1704 O ATOM 2150 CB GLU A1081 -28.616 20.774 42.371 1.00113.66 C ANISOU 2150 CB GLU A1081 11327 9704 22153 -748 -5159 -1709 C ATOM 2151 CG GLU A1081 -27.550 20.867 41.290 1.00116.86 C ANISOU 2151 CG GLU A1081 11938 10503 21960 -303 -5490 -1930 C ATOM 2152 CD GLU A1081 -26.231 20.252 41.714 1.00124.22 C ANISOU 2152 CD GLU A1081 13184 11416 22600 -333 -5490 -1857 C ATOM 2153 OE1 GLU A1081 -26.158 19.731 42.846 1.00126.58 O ANISOU 2153 OE1 GLU A1081 13594 11372 23130 -672 -5285 -1627 O ATOM 2154 OE2 GLU A1081 -25.264 20.295 40.922 1.00127.63 O ANISOU 2154 OE2 GLU A1081 13766 12163 22564 1 -5687 -2038 O ATOM 2155 N GLY A1082 -31.419 22.491 43.789 1.00112.28 N ANISOU 2155 N GLY A1082 10527 9277 22858 -1339 -4221 -1335 N ATOM 2156 CA GLY A1082 -32.544 22.348 44.690 1.00114.50 C ANISOU 2156 CA GLY A1082 10508 9195 23800 -1742 -3834 -1218 C ATOM 2157 C GLY A1082 -32.241 21.733 46.036 1.00115.13 C ANISOU 2157 C GLY A1082 10858 8932 23954 -2154 -3368 -837 C ATOM 2158 O GLY A1082 -33.176 21.395 46.766 1.00119.92 O ANISOU 2158 O GLY A1082 11310 9329 24924 -2395 -2944 -710 O ATOM 2159 N LYS A1083 -30.970 21.560 46.393 1.00109.59 N ANISOU 2159 N LYS A1083 10651 8317 22672 -2102 -3352 -631 N ATOM 2160 CA LYS A1083 -30.616 21.069 47.722 1.00105.03 C ANISOU 2160 CA LYS A1083 10448 7429 22031 -2414 -2932 -254 C ATOM 2161 C LYS A1083 -30.550 22.271 48.659 1.00104.36 C ANISOU 2161 C LYS A1083 10581 7524 21549 -2510 -2371 100 C ATOM 2162 O LYS A1083 -29.484 22.803 48.976 1.00 99.98 O ANISOU 2162 O LYS A1083 10423 7203 20363 -2371 -2311 263 O ATOM 2163 CB LYS A1083 -29.303 20.299 47.682 1.00112.67 C ANISOU 2163 CB LYS A1083 11824 8353 22631 -2281 -3262 -267 C ATOM 2164 CG LYS A1083 -29.445 18.840 47.296 1.00122.18 C ANISOU 2164 CG LYS A1083 12941 9300 24182 -2253 -3621 -484 C ATOM 2165 CD LYS A1083 -28.096 18.133 47.288 1.00125.12 C ANISOU 2165 CD LYS A1083 13718 9626 24194 -2102 -3972 -524 C ATOM 2166 CE LYS A1083 -27.299 18.499 46.049 1.00125.69 C ANISOU 2166 CE LYS A1083 13711 10088 23957 -1716 -4479 -876 C ATOM 2167 NZ LYS A1083 -28.052 18.174 44.801 1.00130.31 N ANISOU 2167 NZ LYS A1083 13844 10711 24956 -1532 -4931 -1296 N ATOM 2168 N VAL A1084 -31.727 22.703 49.113 1.00102.35 N ANISOU 2168 N VAL A1084 10042 7188 21660 -2715 -1949 184 N ATOM 2169 CA VAL A1084 -31.795 23.937 49.889 1.00109.75 C ANISOU 2169 CA VAL A1084 11113 8306 22279 -2772 -1460 457 C ATOM 2170 C VAL A1084 -31.248 23.733 51.298 1.00106.70 C ANISOU 2170 C VAL A1084 11278 7731 21533 -2952 -1007 861 C ATOM 2171 O VAL A1084 -30.623 24.641 51.864 1.00 96.99 O ANISOU 2171 O VAL A1084 10368 6704 19779 -2865 -803 1064 O ATOM 2172 CB VAL A1084 -33.239 24.484 49.892 1.00111.42 C ANISOU 2172 CB VAL A1084 10829 8532 22974 -2879 -1171 361 C ATOM 2173 CG1 VAL A1084 -34.082 23.753 48.859 1.00114.95 C ANISOU 2173 CG1 VAL A1084 10772 8893 24012 -2793 -1584 -54 C ATOM 2174 CG2 VAL A1084 -33.873 24.404 51.279 1.00115.81 C ANISOU 2174 CG2 VAL A1084 11542 8932 23528 -3153 -454 671 C ATOM 2175 N LYS A1085 -31.447 22.547 51.879 1.00103.97 N ANISOU 2175 N LYS A1085 11116 7080 21308 -3118 -859 957 N ATOM 2176 CA LYS A1085 -30.937 22.286 53.221 1.00104.72 C ANISOU 2176 CA LYS A1085 11829 6975 20986 -3237 -468 1327 C ATOM 2177 C LYS A1085 -29.415 22.219 53.230 1.00100.99 C ANISOU 2177 C LYS A1085 11820 6517 20037 -3034 -852 1363 C ATOM 2178 O LYS A1085 -28.772 22.728 54.155 1.00 99.44 O ANISOU 2178 O LYS A1085 12087 6311 19385 -2995 -632 1615 O ATOM 2179 CB LYS A1085 -31.536 20.989 53.769 1.00110.47 C ANISOU 2179 CB LYS A1085 12674 7327 21974 -3470 -235 1419 C ATOM 2180 CG LYS A1085 -33.015 21.067 54.103 1.00115.18 C ANISOU 2180 CG LYS A1085 12894 7865 23005 -3707 283 1439 C ATOM 2181 CD LYS A1085 -33.288 22.076 55.202 1.00115.02 C ANISOU 2181 CD LYS A1085 13103 7946 22651 -3787 899 1731 C ATOM 2182 CE LYS A1085 -34.551 21.719 55.975 1.00122.37 C ANISOU 2182 CE LYS A1085 13915 8680 23901 -4073 1521 1856 C ATOM 2183 NZ LYS A1085 -35.746 21.542 55.101 1.00124.63 N ANISOU 2183 NZ LYS A1085 13427 8989 24938 -4135 1430 1506 N ATOM 2184 N GLU A1086 -28.818 21.581 52.219 1.00 99.96 N ANISOU 2184 N GLU A1086 11567 6401 20013 -2874 -1450 1080 N ATOM 2185 CA GLU A1086 -27.364 21.584 52.119 1.00 96.63 C ANISOU 2185 CA GLU A1086 11510 6102 19102 -2623 -1828 1024 C ATOM 2186 C GLU A1086 -26.842 22.973 51.771 1.00 92.12 C ANISOU 2186 C GLU A1086 10871 6050 18082 -2387 -1819 965 C ATOM 2187 O GLU A1086 -25.746 23.346 52.205 1.00 89.72 O ANISOU 2187 O GLU A1086 10926 5872 17292 -2225 -1865 1022 O ATOM 2188 CB GLU A1086 -26.889 20.558 51.083 1.00 97.10 C ANISOU 2188 CB GLU A1086 11436 6115 19344 -2473 -2441 689 C ATOM 2189 CG GLU A1086 -26.766 19.113 51.627 1.00107.27 C ANISOU 2189 CG GLU A1086 13041 6964 20751 -2578 -2525 760 C ATOM 2190 CD GLU A1086 -26.075 18.161 50.648 1.00109.79 C ANISOU 2190 CD GLU A1086 13279 7278 21159 -2362 -3183 402 C ATOM 2191 OE1 GLU A1086 -25.274 18.658 49.820 1.00110.35 O ANISOU 2191 OE1 GLU A1086 13243 7679 21006 -2099 -3543 149 O ATOM 2192 OE2 GLU A1086 -26.338 16.925 50.704 1.00106.49 O ANISOU 2192 OE2 GLU A1086 12906 6575 20980 -2431 -3297 365 O ATOM 2193 N ALA A1087 -27.612 23.742 50.991 1.00 91.40 N ANISOU 2193 N ALA A1087 10322 6227 18176 -2353 -1783 834 N ATOM 2194 CA ALA A1087 -27.218 25.107 50.659 1.00 87.70 C ANISOU 2194 CA ALA A1087 9809 6202 17313 -2150 -1732 814 C ATOM 2195 C ALA A1087 -27.198 25.982 51.904 1.00 86.85 C ANISOU 2195 C ALA A1087 9983 6092 16924 -2240 -1254 1120 C ATOM 2196 O ALA A1087 -26.246 26.738 52.127 1.00 83.98 O ANISOU 2196 O ALA A1087 9851 5942 16117 -2077 -1259 1158 O ATOM 2197 CB ALA A1087 -28.162 25.691 49.604 1.00 87.96 C ANISOU 2197 CB ALA A1087 9354 6454 17611 -2074 -1818 617 C ATOM 2198 N GLN A1088 -28.253 25.897 52.720 1.00 89.76 N ANISOU 2198 N GLN A1088 10320 6211 17575 -2493 -826 1318 N ATOM 2199 CA GLN A1088 -28.277 26.608 53.994 1.00 90.17 C ANISOU 2199 CA GLN A1088 10698 6227 17335 -2558 -354 1607 C ATOM 2200 C GLN A1088 -27.119 26.175 54.884 1.00 96.23 C ANISOU 2200 C GLN A1088 12074 6827 17664 -2470 -423 1746 C ATOM 2201 O GLN A1088 -26.450 27.014 55.501 1.00 87.40 O ANISOU 2201 O GLN A1088 11242 5855 16112 -2321 -337 1828 O ATOM 2202 CB GLN A1088 -29.609 26.366 54.703 1.00 93.99 C ANISOU 2202 CB GLN A1088 11055 6426 18229 -2856 159 1783 C ATOM 2203 CG GLN A1088 -30.797 27.048 54.063 1.00 94.63 C ANISOU 2203 CG GLN A1088 10538 6682 18735 -2911 276 1627 C ATOM 2204 CD GLN A1088 -32.110 26.594 54.672 1.00103.39 C ANISOU 2204 CD GLN A1088 11445 7519 20321 -3206 767 1715 C ATOM 2205 OE1 GLN A1088 -32.313 25.403 54.933 1.00103.33 O ANISOU 2205 OE1 GLN A1088 11557 7247 20458 -3350 821 1748 O ATOM 2206 NE2 GLN A1088 -33.006 27.545 54.917 1.00100.54 N ANISOU 2206 NE2 GLN A1088 10803 7310 20086 -3243 1130 1715 N ATOM 2207 N ALA A1089 -26.882 24.860 54.978 1.00 91.79 N ANISOU 2207 N ALA A1089 11719 5924 17232 -2541 -616 1748 N ATOM 2208 CA ALA A1089 -25.757 24.359 55.761 1.00 93.54 C ANISOU 2208 CA ALA A1089 12541 5951 17047 -2407 -781 1831 C ATOM 2209 C ALA A1089 -24.441 24.951 55.270 1.00 90.40 C ANISOU 2209 C ALA A1089 12160 5897 16292 -2103 -1186 1595 C ATOM 2210 O ALA A1089 -23.643 25.460 56.063 1.00 86.91 O ANISOU 2210 O ALA A1089 12097 5481 15446 -1943 -1172 1652 O ATOM 2211 CB ALA A1089 -25.708 22.835 55.703 1.00 95.18 C ANISOU 2211 CB ALA A1089 12915 5744 17507 -2506 -1018 1816 C ATOM 2212 N ALA A1090 -24.206 24.896 53.955 1.00 89.80 N ANISOU 2212 N ALA A1090 11672 6073 16376 -2009 -1540 1309 N ATOM 2213 CA ALA A1090 -22.973 25.422 53.383 1.00 85.63 C ANISOU 2213 CA ALA A1090 11107 5863 15566 -1749 -1852 1076 C ATOM 2214 C ALA A1090 -22.869 26.932 53.558 1.00 84.93 C ANISOU 2214 C ALA A1090 10947 6077 15246 -1679 -1594 1141 C ATOM 2215 O ALA A1090 -21.758 27.477 53.632 1.00 80.94 O ANISOU 2215 O ALA A1090 10548 5725 14479 -1498 -1727 1027 O ATOM 2216 CB ALA A1090 -22.889 25.051 51.904 1.00 82.09 C ANISOU 2216 CB ALA A1090 10258 5619 15312 -1657 -2203 782 C ATOM 2217 N ALA A1091 -24.006 27.618 53.633 1.00 87.37 N ANISOU 2217 N ALA A1091 11050 6451 15694 -1818 -1237 1297 N ATOM 2218 CA ALA A1091 -23.994 29.056 53.852 1.00 83.03 C ANISOU 2218 CA ALA A1091 10449 6150 14950 -1753 -998 1366 C ATOM 2219 C ALA A1091 -23.645 29.415 55.288 1.00 88.03 C ANISOU 2219 C ALA A1091 11529 6628 15290 -1722 -787 1544 C ATOM 2220 O ALA A1091 -23.284 30.567 55.554 1.00 87.78 O ANISOU 2220 O ALA A1091 11517 6775 15061 -1614 -690 1547 O ATOM 2221 CB ALA A1091 -25.348 29.656 53.476 1.00 80.67 C ANISOU 2221 CB ALA A1091 9784 5957 14910 -1876 -731 1432 C ATOM 2222 N GLU A1092 -23.746 28.461 56.217 1.00 90.97 N ANISOU 2222 N GLU A1092 12294 6648 15621 -1794 -723 1689 N ATOM 2223 CA GLU A1092 -23.317 28.725 57.587 1.00 99.26 C ANISOU 2223 CA GLU A1092 13876 7532 16308 -1686 -584 1836 C ATOM 2224 C GLU A1092 -21.802 28.803 57.697 1.00 98.29 C ANISOU 2224 C GLU A1092 13977 7445 15922 -1418 -1005 1615 C ATOM 2225 O GLU A1092 -21.281 29.432 58.625 1.00101.44 O ANISOU 2225 O GLU A1092 14703 7813 16026 -1247 -983 1629 O ATOM 2226 CB GLU A1092 -23.856 27.652 58.532 1.00110.40 C ANISOU 2226 CB GLU A1092 15726 8516 17703 -1816 -371 2082 C ATOM 2227 CG GLU A1092 -25.283 27.886 58.986 1.00117.72 C ANISOU 2227 CG GLU A1092 16554 9366 18807 -2054 213 2338 C ATOM 2228 CD GLU A1092 -25.481 29.275 59.553 1.00120.19 C ANISOU 2228 CD GLU A1092 16873 9905 18891 -1958 508 2399 C ATOM 2229 OE1 GLU A1092 -25.735 30.212 58.765 1.00119.18 O ANISOU 2229 OE1 GLU A1092 16254 10104 18925 -1957 492 2267 O ATOM 2230 OE2 GLU A1092 -25.367 29.432 60.786 1.00123.29 O ANISOU 2230 OE2 GLU A1092 17798 10133 18915 -1852 731 2572 O ATOM 2231 N GLN A1093 -21.081 28.167 56.772 1.00 92.01 N ANISOU 2231 N GLN A1093 12995 6710 15256 -1358 -1404 1371 N ATOM 2232 CA GLN A1093 -19.627 28.257 56.775 1.00 87.16 C ANISOU 2232 CA GLN A1093 12485 6147 14483 -1110 -1794 1095 C ATOM 2233 C GLN A1093 -19.157 29.689 56.549 1.00 87.08 C ANISOU 2233 C GLN A1093 12217 6445 14425 -1019 -1715 983 C ATOM 2234 O GLN A1093 -18.087 30.075 57.034 1.00 87.76 O ANISOU 2234 O GLN A1093 12455 6512 14378 -819 -1919 798 O ATOM 2235 CB GLN A1093 -19.047 27.328 55.708 1.00 83.93 C ANISOU 2235 CB GLN A1093 11851 5781 14258 -1073 -2180 834 C ATOM 2236 N LEU A1094 -19.942 30.492 55.823 1.00 82.67 N ANISOU 2236 N LEU A1094 11271 6138 14002 -1151 -1442 1073 N ATOM 2237 CA LEU A1094 -19.544 31.865 55.540 1.00 78.46 C ANISOU 2237 CA LEU A1094 10507 5858 13445 -1082 -1346 998 C ATOM 2238 C LEU A1094 -19.339 32.667 56.817 1.00 81.97 C ANISOU 2238 C LEU A1094 11258 6197 13690 -975 -1238 1062 C ATOM 2239 O LEU A1094 -18.549 33.617 56.829 1.00 77.92 O ANISOU 2239 O LEU A1094 10644 5790 13174 -860 -1298 909 O ATOM 2240 CB LEU A1094 -20.592 32.546 54.660 1.00 74.87 C ANISOU 2240 CB LEU A1094 9684 5630 13134 -1216 -1084 1120 C ATOM 2241 CG LEU A1094 -20.809 31.933 53.279 1.00 71.78 C ANISOU 2241 CG LEU A1094 8985 5377 12912 -1256 -1225 1016 C ATOM 2242 CD1 LEU A1094 -22.196 32.265 52.773 1.00 71.98 C ANISOU 2242 CD1 LEU A1094 8766 5493 13090 -1373 -1011 1155 C ATOM 2243 CD2 LEU A1094 -19.761 32.456 52.327 1.00 70.41 C ANISOU 2243 CD2 LEU A1094 8608 5434 12710 -1133 -1347 811 C ATOM 2244 N LYS A1095 -20.037 32.303 57.899 1.00 85.06 N ANISOU 2244 N LYS A1095 12032 6363 13926 -1002 -1064 1277 N ATOM 2245 CA LYS A1095 -19.950 33.091 59.123 1.00 88.63 C ANISOU 2245 CA LYS A1095 12816 6726 14132 -856 -948 1337 C ATOM 2246 C LYS A1095 -18.554 33.019 59.729 1.00 90.44 C ANISOU 2246 C LYS A1095 13335 6817 14212 -580 -1358 1071 C ATOM 2247 O LYS A1095 -18.056 34.016 60.265 1.00 87.20 O ANISOU 2247 O LYS A1095 12971 6436 13727 -414 -1406 950 O ATOM 2248 CB LYS A1095 -21.002 32.627 60.130 1.00 89.40 C ANISOU 2248 CB LYS A1095 13310 6604 14055 -930 -616 1636 C ATOM 2249 CG LYS A1095 -22.402 33.129 59.834 1.00 86.92 C ANISOU 2249 CG LYS A1095 12679 6432 13916 -1153 -163 1843 C ATOM 2250 N THR A1096 -17.900 31.855 59.644 1.00 90.21 N ANISOU 2250 N THR A1096 13478 6619 14177 -509 -1697 935 N ATOM 2251 CA THR A1096 -16.550 31.752 60.190 1.00 91.98 C ANISOU 2251 CA THR A1096 13942 6696 14309 -212 -2152 612 C ATOM 2252 C THR A1096 -15.540 32.501 59.325 1.00 87.61 C ANISOU 2252 C THR A1096 12866 6377 14045 -176 -2326 273 C ATOM 2253 O THR A1096 -14.563 33.045 59.850 1.00 86.55 O ANISOU 2253 O THR A1096 12783 6176 13928 50 -2584 -11 O ATOM 2254 CB THR A1096 -16.149 30.281 60.370 1.00 97.00 C ANISOU 2254 CB THR A1096 14936 7057 14864 -119 -2495 545 C ATOM 2255 OG1 THR A1096 -15.019 30.203 61.243 1.00103.52 O ANISOU 2255 OG1 THR A1096 16144 7666 15522 235 -2947 253 O ATOM 2256 CG2 THR A1096 -15.776 29.625 59.053 1.00 94.97 C ANISOU 2256 CG2 THR A1096 14227 6947 14910 -233 -2681 357 C ATOM 2257 N THR A1097 -15.773 32.566 58.011 1.00 83.63 N ANISOU 2257 N THR A1097 11867 6128 13780 -383 -2172 289 N ATOM 2258 CA THR A1097 -14.904 33.341 57.130 1.00 80.10 C ANISOU 2258 CA THR A1097 10944 5900 13589 -381 -2206 31 C ATOM 2259 C THR A1097 -15.084 34.838 57.353 1.00 76.66 C ANISOU 2259 C THR A1097 10367 5566 13195 -403 -1947 103 C ATOM 2260 O THR A1097 -14.108 35.602 57.352 1.00 73.52 O ANISOU 2260 O THR A1097 9769 5181 12983 -310 -2051 -160 O ATOM 2261 CB THR A1097 -15.210 32.988 55.680 1.00 77.26 C ANISOU 2261 CB THR A1097 10203 5774 13379 -555 -2082 69 C ATOM 2262 OG1 THR A1097 -15.286 31.568 55.561 1.00 78.85 O ANISOU 2262 OG1 THR A1097 10568 5848 13542 -544 -2315 41 O ATOM 2263 CG2 THR A1097 -14.133 33.528 54.761 1.00 76.17 C ANISOU 2263 CG2 THR A1097 9649 5821 13471 -527 -2109 -216 C ATOM 2264 N ARG A1098 -16.334 35.272 57.521 1.00 74.78 N ANISOU 2264 N ARG A1098 10195 5384 12835 -530 -1609 435 N ATOM 2265 CA ARG A1098 -16.605 36.670 57.827 1.00 74.47 C ANISOU 2265 CA ARG A1098 10067 5414 12815 -529 -1388 509 C ATOM 2266 C ARG A1098 -15.879 37.099 59.098 1.00 77.63 C ANISOU 2266 C ARG A1098 10764 5610 13123 -280 -1616 314 C ATOM 2267 O ARG A1098 -15.268 38.173 59.137 1.00 74.48 O ANISOU 2267 O ARG A1098 10164 5229 12907 -217 -1649 138 O ATOM 2268 CB ARG A1098 -18.113 36.878 57.954 1.00 71.66 C ANISOU 2268 CB ARG A1098 9771 5119 12336 -668 -1030 856 C ATOM 2269 CG ARG A1098 -18.564 38.325 58.077 1.00 71.91 C ANISOU 2269 CG ARG A1098 9665 5251 12409 -678 -791 943 C ATOM 2270 CD ARG A1098 -19.926 38.371 58.723 1.00 71.76 C ANISOU 2270 CD ARG A1098 9827 5212 12227 -733 -497 1209 C ATOM 2271 NE ARG A1098 -19.971 37.451 59.851 1.00 78.21 N ANISOU 2271 NE ARG A1098 11122 5807 12790 -633 -554 1256 N ATOM 2272 CZ ARG A1098 -21.079 37.059 60.474 1.00 82.26 C ANISOU 2272 CZ ARG A1098 11862 6241 13151 -702 -261 1497 C ATOM 2273 NH1 ARG A1098 -22.269 37.509 60.092 1.00 78.44 N ANISOU 2273 NH1 ARG A1098 11109 5900 12795 -867 78 1666 N ATOM 2274 NH2 ARG A1098 -20.990 36.204 61.485 1.00 84.82 N ANISOU 2274 NH2 ARG A1098 12697 6324 13206 -594 -298 1559 N ATOM 2275 N ASN A1099 -15.908 36.255 60.136 1.00 82.78 N ANISOU 2275 N ASN A1099 11918 6036 13499 -117 -1798 328 N ATOM 2276 CA ASN A1099 -15.247 36.587 61.395 1.00 88.51 C ANISOU 2276 CA ASN A1099 13019 6545 14066 197 -2080 119 C ATOM 2277 C ASN A1099 -13.731 36.484 61.283 1.00 94.11 C ANISOU 2277 C ASN A1099 13570 7162 15027 383 -2551 -350 C ATOM 2278 O ASN A1099 -13.008 37.264 61.910 1.00101.00 O ANISOU 2278 O ASN A1099 14452 7926 15997 603 -2783 -636 O ATOM 2279 CB ASN A1099 -15.737 35.667 62.510 1.00 92.39 C ANISOU 2279 CB ASN A1099 14185 6796 14123 349 -2116 299 C ATOM 2280 CG ASN A1099 -17.236 35.660 62.644 1.00 95.34 C ANISOU 2280 CG ASN A1099 14674 7237 14316 143 -1600 735 C ATOM 2281 OD1 ASN A1099 -17.896 36.663 62.393 1.00 92.99 O ANISOU 2281 OD1 ASN A1099 14088 7126 14119 16 -1286 855 O ATOM 2282 ND2 ASN A1099 -17.788 34.518 63.037 1.00101.43 N ANISOU 2282 ND2 ASN A1099 15855 7828 14854 105 -1506 962 N ATOM 2283 N ALA A1100 -13.228 35.521 60.507 1.00 90.64 N ANISOU 2283 N ALA A1100 12960 6747 14732 316 -2718 -478 N ATOM 2284 CA ALA A1100 -11.788 35.287 60.472 1.00 90.15 C ANISOU 2284 CA ALA A1100 12747 6577 14929 516 -3182 -972 C ATOM 2285 C ALA A1100 -11.046 36.243 59.541 1.00 93.54 C ANISOU 2285 C ALA A1100 12520 7183 15839 384 -3067 -1212 C ATOM 2286 O ALA A1100 -9.860 36.511 59.767 1.00 98.70 O ANISOU 2286 O ALA A1100 12988 7715 16798 563 -3396 -1667 O ATOM 2287 CB ALA A1100 -11.496 33.843 60.069 1.00 90.55 C ANISOU 2287 CB ALA A1100 12893 6565 14945 532 -3431 -1054 C ATOM 2288 N TYR A1101 -11.704 36.775 58.503 1.00 87.39 N ANISOU 2288 N TYR A1101 11392 6660 15152 88 -2606 -933 N ATOM 2289 CA TYR A1101 -10.988 37.585 57.520 1.00 84.82 C ANISOU 2289 CA TYR A1101 10502 6477 15247 -50 -2432 -1112 C ATOM 2290 C TYR A1101 -11.699 38.877 57.133 1.00 83.87 C ANISOU 2290 C TYR A1101 10198 6492 15178 -239 -1993 -821 C ATOM 2291 O TYR A1101 -11.076 39.944 57.093 1.00 85.09 O ANISOU 2291 O TYR A1101 10070 6598 15661 -254 -1926 -993 O ATOM 2292 CB TYR A1101 -10.730 36.780 56.247 1.00 84.68 C ANISOU 2292 CB TYR A1101 10204 6643 15329 -184 -2352 -1151 C ATOM 2293 CG TYR A1101 -10.045 35.461 56.475 1.00 89.08 C ANISOU 2293 CG TYR A1101 10908 7076 15865 -4 -2794 -1449 C ATOM 2294 CD1 TYR A1101 -8.681 35.393 56.725 1.00 92.70 C ANISOU 2294 CD1 TYR A1101 11173 7395 16654 182 -3151 -1969 C ATOM 2295 CD2 TYR A1101 -10.764 34.276 56.425 1.00 88.79 C ANISOU 2295 CD2 TYR A1101 11179 7032 15524 -15 -2874 -1237 C ATOM 2296 CE1 TYR A1101 -8.058 34.169 56.927 1.00 98.42 C ANISOU 2296 CE1 TYR A1101 12046 7990 17360 381 -3606 -2270 C ATOM 2297 CE2 TYR A1101 -10.158 33.066 56.628 1.00 91.49 C ANISOU 2297 CE2 TYR A1101 11689 7226 15845 159 -3301 -1499 C ATOM 2298 CZ TYR A1101 -8.810 33.011 56.876 1.00 96.97 C ANISOU 2298 CZ TYR A1101 12223 7797 16824 370 -3680 -2013 C ATOM 2299 OH TYR A1101 -8.228 31.782 57.069 1.00103.57 O ANISOU 2299 OH TYR A1101 13244 8471 17635 574 -4150 -2294 O ATOM 2300 N ILE A1102 -12.994 38.790 56.829 1.00 79.54 N ANISOU 2300 N ILE A1102 9786 6085 14349 -380 -1707 -405 N ATOM 2301 CA ILE A1102 -13.677 39.911 56.196 1.00 71.83 C ANISOU 2301 CA ILE A1102 8608 5256 13428 -551 -1315 -144 C ATOM 2302 C ILE A1102 -13.856 41.064 57.177 1.00 80.09 C ANISOU 2302 C ILE A1102 9763 6171 14495 -461 -1301 -135 C ATOM 2303 O ILE A1102 -13.708 42.234 56.811 1.00 72.50 O ANISOU 2303 O ILE A1102 8555 5223 13768 -542 -1110 -123 O ATOM 2304 CB ILE A1102 -15.023 39.454 55.614 1.00 70.97 C ANISOU 2304 CB ILE A1102 8585 5317 13064 -686 -1087 222 C ATOM 2305 CG1 ILE A1102 -14.836 38.191 54.758 1.00 76.85 C ANISOU 2305 CG1 ILE A1102 9262 6157 13782 -726 -1187 164 C ATOM 2306 CG2 ILE A1102 -15.650 40.564 54.804 1.00 69.27 C ANISOU 2306 CG2 ILE A1102 8163 5247 12908 -818 -745 447 C ATOM 2307 CD1 ILE A1102 -13.802 38.343 53.655 1.00 82.51 C ANISOU 2307 CD1 ILE A1102 9625 6987 14740 -765 -1132 -43 C ATOM 2308 N GLN A1103 -14.208 40.761 58.425 1.00 78.78 N ANISOU 2308 N GLN A1103 10002 5865 14066 -281 -1487 -129 N ATOM 2309 CA GLN A1103 -14.352 41.826 59.408 1.00 84.18 C ANISOU 2309 CA GLN A1103 10822 6427 14735 -140 -1510 -164 C ATOM 2310 C GLN A1103 -13.012 42.490 59.698 1.00 84.88 C ANISOU 2310 C GLN A1103 10700 6338 15211 -4 -1789 -591 C ATOM 2311 O GLN A1103 -12.957 43.704 59.925 1.00 88.94 O ANISOU 2311 O GLN A1103 11080 6785 15928 12 -1729 -643 O ATOM 2312 CB GLN A1103 -14.973 41.269 60.687 1.00 89.34 C ANISOU 2312 CB GLN A1103 12020 6963 14961 63 -1623 -71 C ATOM 2313 CG GLN A1103 -15.247 42.308 61.750 1.00 97.08 C ANISOU 2313 CG GLN A1103 13204 7842 15839 255 -1637 -101 C ATOM 2314 CD GLN A1103 -15.770 41.696 63.029 1.00106.59 C ANISOU 2314 CD GLN A1103 15018 8921 16560 493 -1710 -13 C ATOM 2315 OE1 GLN A1103 -16.447 40.667 63.007 1.00112.29 O ANISOU 2315 OE1 GLN A1103 15974 9673 17019 403 -1553 237 O ATOM 2316 NE2 GLN A1103 -15.449 42.317 64.157 1.00109.36 N ANISOU 2316 NE2 GLN A1103 15652 9107 16794 810 -1943 -223 N ATOM 2317 N LYS A1104 -11.928 41.713 59.668 1.00 87.11 N ANISOU 2317 N LYS A1104 10916 6527 15655 93 -2108 -929 N ATOM 2318 CA LYS A1104 -10.595 42.258 59.897 1.00 90.18 C ANISOU 2318 CA LYS A1104 11021 6728 16518 219 -2397 -1412 C ATOM 2319 C LYS A1104 -10.217 43.261 58.817 1.00 92.17 C ANISOU 2319 C LYS A1104 10723 7050 17249 -51 -2047 -1409 C ATOM 2320 O LYS A1104 -9.639 44.316 59.110 1.00 94.40 O ANISOU 2320 O LYS A1104 10774 7159 17933 -17 -2104 -1645 O ATOM 2321 CB LYS A1104 -9.585 41.112 59.953 1.00 95.88 C ANISOU 2321 CB LYS A1104 11745 7355 17331 372 -2799 -1787 C ATOM 2322 CG LYS A1104 -8.123 41.507 59.962 1.00106.16 C ANISOU 2322 CG LYS A1104 12618 8476 19241 468 -3086 -2359 C ATOM 2323 CD LYS A1104 -7.256 40.252 60.032 1.00116.20 C ANISOU 2323 CD LYS A1104 13930 9668 20554 654 -3518 -2733 C ATOM 2324 CE LYS A1104 -5.774 40.567 60.215 1.00124.21 C ANISOU 2324 CE LYS A1104 14509 10462 22222 811 -3894 -3404 C ATOM 2325 NZ LYS A1104 -4.961 39.313 60.291 1.00128.54 N ANISOU 2325 NZ LYS A1104 15086 11040 22713 1023 -4314 -3733 N ATOM 2326 N TYR A1105 -10.543 42.958 57.561 1.00 87.52 N ANISOU 2326 N TYR A1105 9946 6688 16621 -306 -1680 -1143 N ATOM 2327 CA TYR A1105 -10.178 43.861 56.481 1.00 87.60 C ANISOU 2327 CA TYR A1105 9521 6748 17016 -546 -1294 -1095 C ATOM 2328 C TYR A1105 -11.094 45.071 56.422 1.00 79.67 C ANISOU 2328 C TYR A1105 8570 5757 15946 -647 -995 -753 C ATOM 2329 O TYR A1105 -10.654 46.151 56.020 1.00 81.29 O ANISOU 2329 O TYR A1105 8485 5857 16546 -775 -778 -788 O ATOM 2330 CB TYR A1105 -10.158 43.100 55.159 1.00 94.37 C ANISOU 2330 CB TYR A1105 10226 7836 17794 -715 -1035 -959 C ATOM 2331 CG TYR A1105 -8.989 42.144 55.122 1.00107.55 C ANISOU 2331 CG TYR A1105 11717 9459 19688 -622 -1315 -1393 C ATOM 2332 CD1 TYR A1105 -7.711 42.581 55.457 1.00115.64 C ANISOU 2332 CD1 TYR A1105 12401 10268 21268 -564 -1484 -1869 C ATOM 2333 CD2 TYR A1105 -9.162 40.804 54.803 1.00111.67 C ANISOU 2333 CD2 TYR A1105 12391 10122 19916 -573 -1452 -1371 C ATOM 2334 CE1 TYR A1105 -6.634 41.723 55.446 1.00120.04 C ANISOU 2334 CE1 TYR A1105 12759 10774 22078 -451 -1776 -2326 C ATOM 2335 CE2 TYR A1105 -8.089 39.933 54.794 1.00116.95 C ANISOU 2335 CE2 TYR A1105 12900 10736 20800 -458 -1751 -1801 C ATOM 2336 CZ TYR A1105 -6.827 40.398 55.115 1.00122.35 C ANISOU 2336 CZ TYR A1105 13233 11225 22029 -390 -1913 -2286 C ATOM 2337 OH TYR A1105 -5.749 39.538 55.104 1.00129.14 O ANISOU 2337 OH TYR A1105 13894 12025 23149 -251 -2239 -2770 O ATOM 2338 N ALEU A1106 -12.362 44.904 56.805 0.50 75.39 N ANISOU 2338 N ALEU A1106 8379 5322 14943 -597 -966 -433 N ATOM 2339 N BLEU A1106 -12.348 44.941 56.846 0.50 75.45 N ANISOU 2339 N BLEU A1106 8388 5321 14960 -592 -973 -442 N ATOM 2340 CA ALEU A1106 -13.260 46.045 56.932 0.50 74.83 C ANISOU 2340 CA ALEU A1106 8373 5247 14811 -635 -759 -173 C ATOM 2341 CA BLEU A1106 -13.199 46.121 56.866 0.50 74.93 C ANISOU 2341 CA BLEU A1106 8356 5254 14861 -648 -743 -179 C ATOM 2342 C ALEU A1106 -12.719 47.051 57.939 0.50 76.90 C ANISOU 2342 C ALEU A1106 8601 5250 15366 -485 -975 -449 C ATOM 2343 C BLEU A1106 -12.809 47.077 57.990 0.50 76.81 C ANISOU 2343 C BLEU A1106 8613 5243 15328 -478 -974 -431 C ATOM 2344 O ALEU A1106 -12.728 48.261 57.688 0.50 77.70 O ANISOU 2344 O ALEU A1106 8525 5256 15743 -577 -797 -390 O ATOM 2345 O BLEU A1106 -13.020 48.287 57.866 0.50 77.36 O ANISOU 2345 O BLEU A1106 8567 5231 15597 -544 -807 -338 O ATOM 2346 CB ALEU A1106 -14.653 45.567 57.349 0.50 72.99 C ANISOU 2346 CB ALEU A1106 8492 5155 14087 -577 -723 126 C ATOM 2347 CB BLEU A1106 -14.664 45.710 56.972 0.50 72.83 C ANISOU 2347 CB BLEU A1106 8391 5166 14116 -638 -633 175 C ATOM 2348 CG ALEU A1106 -15.747 46.617 57.580 0.50 76.07 C ANISOU 2348 CG ALEU A1106 8966 5565 14371 -575 -539 369 C ATOM 2349 CG BLEU A1106 -15.211 45.045 55.705 0.50 71.31 C ANISOU 2349 CG BLEU A1106 8131 5203 13759 -803 -399 431 C ATOM 2350 CD1ALEU A1106 -16.596 46.788 56.329 0.50 73.66 C ANISOU 2350 CD1ALEU A1106 8550 5449 13986 -756 -218 698 C ATOM 2351 CD1BLEU A1106 -16.707 44.893 55.786 0.50 74.64 C ANISOU 2351 CD1BLEU A1106 8753 5759 13850 -807 -280 735 C ATOM 2352 CD2ALEU A1106 -16.626 46.278 58.788 0.50 73.58 C ANISOU 2352 CD2ALEU A1106 9019 5250 13688 -397 -637 429 C ATOM 2353 CD2BLEU A1106 -14.841 45.825 54.458 0.50 71.92 C ANISOU 2353 CD2BLEU A1106 7937 5314 14074 -964 -110 519 C ATOM 2354 N GLU A 219 -12.235 46.563 59.083 1.00 68.63 N ANISOU 2354 N GLU A 219 10764 3740 11573 -2234 -551 691 N ATOM 2355 CA GLU A 219 -11.728 47.446 60.129 1.00 69.92 C ANISOU 2355 CA GLU A 219 10933 4067 11567 -2159 -276 838 C ATOM 2356 C GLU A 219 -10.491 48.203 59.673 1.00 68.86 C ANISOU 2356 C GLU A 219 10914 4124 11127 -1919 -421 713 C ATOM 2357 O GLU A 219 -10.359 49.401 59.953 1.00 71.37 O ANISOU 2357 O GLU A 219 11126 4649 11343 -1891 -316 746 O ATOM 2358 CB GLU A 219 -11.418 46.647 61.392 1.00 77.48 C ANISOU 2358 CB GLU A 219 12076 4870 12492 -2140 -21 1047 C ATOM 2359 CG GLU A 219 -12.636 46.175 62.140 1.00 87.09 C ANISOU 2359 CG GLU A 219 13243 5944 13905 -2398 222 1213 C ATOM 2360 CD GLU A 219 -12.285 45.155 63.197 1.00 96.52 C ANISOU 2360 CD GLU A 219 14660 6947 15068 -2350 434 1394 C ATOM 2361 OE1 GLU A 219 -11.167 45.231 63.748 1.00101.28 O ANISOU 2361 OE1 GLU A 219 15290 7610 15581 -2106 397 1503 O ATOM 2362 OE2 GLU A 219 -13.117 44.269 63.469 1.00 99.87 O ANISOU 2362 OE2 GLU A 219 15168 7179 15599 -2561 479 1476 O ATOM 2363 N ARG A 220 -9.581 47.539 58.954 1.00 65.87 N ANISOU 2363 N ARG A 220 10768 3682 10578 -1743 -652 566 N ATOM 2364 CA ARG A 220 -8.375 48.228 58.489 1.00 62.12 C ANISOU 2364 CA ARG A 220 10432 3388 9782 -1506 -758 438 C ATOM 2365 C ARG A 220 -8.702 49.257 57.413 1.00 63.22 C ANISOU 2365 C ARG A 220 10405 3689 9925 -1519 -910 273 C ATOM 2366 O ARG A 220 -8.102 50.339 57.378 1.00 63.23 O ANISOU 2366 O ARG A 220 10401 3892 9734 -1409 -877 239 O ATOM 2367 CB ARG A 220 -7.348 47.221 57.969 1.00 65.24 C ANISOU 2367 CB ARG A 220 11114 3673 10002 -1299 -922 321 C ATOM 2368 CG ARG A 220 -6.999 46.134 58.967 1.00 71.12 C ANISOU 2368 CG ARG A 220 12030 4249 10744 -1269 -808 476 C ATOM 2369 N ALA A 221 -9.649 48.940 56.524 1.00 64.11 N ANISOU 2369 N ALA A 221 10397 3717 10244 -1649 -1087 171 N ATOM 2370 CA ALA A 221 -10.097 49.924 55.541 1.00 62.23 C ANISOU 2370 CA ALA A 221 9992 3632 10020 -1668 -1241 33 C ATOM 2371 C ALA A 221 -10.684 51.145 56.233 1.00 60.45 C ANISOU 2371 C ALA A 221 9487 3580 9903 -1787 -1041 157 C ATOM 2372 O ALA A 221 -10.354 52.290 55.896 1.00 54.45 O ANISOU 2372 O ALA A 221 8669 3017 9004 -1705 -1062 90 O ATOM 2373 CB ALA A 221 -11.120 49.290 54.593 1.00 66.56 C ANISOU 2373 CB ALA A 221 10465 4043 10783 -1796 -1483 -68 C ATOM 2374 N ARG A 222 -11.533 50.916 57.236 1.00 65.73 N ANISOU 2374 N ARG A 222 9992 4177 10804 -1970 -817 344 N ATOM 2375 CA ARG A 222 -12.151 52.027 57.954 1.00 66.44 C ANISOU 2375 CA ARG A 222 9819 4433 10993 -2073 -582 473 C ATOM 2376 C ARG A 222 -11.103 52.899 58.641 1.00 62.37 C ANISOU 2376 C ARG A 222 9411 4079 10209 -1928 -424 540 C ATOM 2377 O ARG A 222 -11.159 54.132 58.558 1.00 66.03 O ANISOU 2377 O ARG A 222 9709 4744 10634 -1912 -384 523 O ATOM 2378 CB ARG A 222 -13.162 51.481 58.962 1.00 71.07 C ANISOU 2378 CB ARG A 222 10283 4905 11815 -2269 -331 670 C ATOM 2379 CG ARG A 222 -13.944 52.540 59.721 1.00 70.99 C ANISOU 2379 CG ARG A 222 9999 5075 11898 -2367 -69 809 C ATOM 2380 CD ARG A 222 -15.049 51.870 60.550 1.00 75.82 C ANISOU 2380 CD ARG A 222 10500 5571 12738 -2556 132 989 C ATOM 2381 N SER A 223 -10.134 52.280 59.327 1.00 62.68 N ANISOU 2381 N SER A 223 9734 4040 10042 -1812 -346 618 N ATOM 2382 CA SER A 223 -9.137 53.065 60.064 1.00 59.30 C ANISOU 2382 CA SER A 223 9386 3875 9271 -1618 -161 660 C ATOM 2383 C SER A 223 -8.243 53.853 59.126 1.00 56.97 C ANISOU 2383 C SER A 223 9102 3817 8727 -1413 -318 459 C ATOM 2384 O SER A 223 -7.845 54.977 59.443 1.00 61.51 O ANISOU 2384 O SER A 223 9582 4668 9123 -1314 -190 461 O ATOM 2385 CB SER A 223 -8.273 52.160 60.937 1.00 64.39 C ANISOU 2385 CB SER A 223 10329 4405 9733 -1504 -77 766 C ATOM 2386 OG SER A 223 -9.072 51.227 61.618 1.00 76.05 O ANISOU 2386 OG SER A 223 11844 5604 11447 -1694 38 943 O ATOM 2387 N THR A 224 -7.900 53.275 57.973 1.00 57.61 N ANISOU 2387 N THR A 224 9321 3782 8788 -1341 -582 288 N ATOM 2388 CA THR A 224 -7.121 54.015 56.986 1.00 54.61 C ANISOU 2388 CA THR A 224 8960 3605 8183 -1149 -700 105 C ATOM 2389 C THR A 224 -7.875 55.246 56.500 1.00 53.58 C ANISOU 2389 C THR A 224 8563 3656 8137 -1237 -714 55 C ATOM 2390 O THR A 224 -7.285 56.320 56.336 1.00 57.31 O ANISOU 2390 O THR A 224 8971 4394 8411 -1102 -653 1 O ATOM 2391 CB THR A 224 -6.765 53.111 55.803 1.00 56.62 C ANISOU 2391 CB THR A 224 9450 3659 8404 -1061 -963 -68 C ATOM 2392 OG1 THR A 224 -6.111 51.933 56.288 1.00 65.29 O ANISOU 2392 OG1 THR A 224 10791 4567 9450 -978 -949 -15 O ATOM 2393 CG2 THR A 224 -5.835 53.843 54.859 1.00 58.37 C ANISOU 2393 CG2 THR A 224 9728 4086 8363 -834 -1019 -234 C ATOM 2394 N ALEU A 225 -9.183 55.118 56.267 0.50 52.95 N ANISOU 2394 N ALEU A 225 8315 3425 8377 -1464 -803 79 N ATOM 2395 N BLEU A 225 -9.177 55.098 56.234 0.50 52.97 N ANISOU 2395 N BLEU A 225 8322 3423 8379 -1462 -811 74 N ATOM 2396 CA ALEU A 225 -9.942 56.276 55.803 0.50 50.66 C ANISOU 2396 CA ALEU A 225 7761 3292 8196 -1540 -837 36 C ATOM 2397 CA BLEU A 225 -9.985 56.244 55.825 0.50 50.92 C ANISOU 2397 CA BLEU A 225 7789 3314 8243 -1549 -836 41 C ATOM 2398 C ALEU A 225 -10.064 57.332 56.899 0.50 49.87 C ANISOU 2398 C ALEU A 225 7456 3427 8064 -1551 -527 178 C ATOM 2399 C BLEU A 225 -9.993 57.313 56.908 0.50 49.82 C ANISOU 2399 C BLEU A 225 7465 3424 8041 -1540 -525 177 C ATOM 2400 O ALEU A 225 -9.947 58.532 56.625 0.50 50.91 O ANISOU 2400 O ALEU A 225 7464 3796 8085 -1479 -500 122 O ATOM 2401 O BLEU A 225 -9.737 58.491 56.639 0.50 50.42 O ANISOU 2401 O BLEU A 225 7440 3745 7972 -1447 -497 115 O ATOM 2402 CB ALEU A 225 -11.318 55.833 55.298 0.50 52.76 C ANISOU 2402 CB ALEU A 225 7865 3331 8851 -1770 -1028 29 C ATOM 2403 CB BLEU A 225 -11.415 55.795 55.512 0.50 52.92 C ANISOU 2403 CB BLEU A 225 7859 3343 8905 -1795 -982 64 C ATOM 2404 CG ALEU A 225 -11.327 54.926 54.058 0.50 52.51 C ANISOU 2404 CG ALEU A 225 8008 3163 8780 -1715 -1333 -147 C ATOM 2405 CG BLEU A 225 -11.916 55.838 54.067 0.50 53.18 C ANISOU 2405 CG BLEU A 225 7862 3374 8969 -1781 -1297 -123 C ATOM 2406 CD1ALEU A 225 -12.727 54.416 53.758 0.50 55.62 C ANISOU 2406 CD1ALEU A 225 8190 3444 9499 -1899 -1449 -131 C ATOM 2407 CD1BLEU A 225 -11.512 57.131 53.394 0.50 48.98 C ANISOU 2407 CD1BLEU A 225 7314 3043 8252 -1665 -1374 -234 C ATOM 2408 CD2ALEU A 225 -10.767 55.644 52.832 0.50 50.02 C ANISOU 2408 CD2ALEU A 225 7816 2971 8217 -1547 -1534 -339 C ATOM 2409 CD2BLEU A 225 -11.419 54.648 53.286 0.50 52.80 C ANISOU 2409 CD2BLEU A 225 8112 3156 8793 -1684 -1509 -250 C ATOM 2410 N GLN A 226 -10.273 56.912 58.150 1.00 51.04 N ANISOU 2410 N GLN A 226 7603 3502 8287 -1630 -285 363 N ATOM 2411 CA GLN A 226 -10.361 57.884 59.235 1.00 51.03 C ANISOU 2411 CA GLN A 226 7472 3703 8213 -1620 18 493 C ATOM 2412 C GLN A 226 -9.040 58.600 59.464 1.00 50.35 C ANISOU 2412 C GLN A 226 7521 3867 7741 -1389 73 442 C ATOM 2413 O GLN A 226 -9.035 59.777 59.848 1.00 50.45 O ANISOU 2413 O GLN A 226 7407 4099 7661 -1350 216 462 O ATOM 2414 CB GLN A 226 -10.820 57.194 60.516 1.00 52.35 C ANISOU 2414 CB GLN A 226 7679 3708 8501 -1736 275 707 C ATOM 2415 CG GLN A 226 -12.145 56.464 60.350 1.00 67.83 C ANISOU 2415 CG GLN A 226 9468 5399 10906 -1985 245 783 C ATOM 2416 N LYS A 227 -7.911 57.909 59.257 1.00 50.54 N ANISOU 2416 N LYS A 227 7791 3850 7560 -1234 -38 379 N ATOM 2417 CA LYS A 227 -6.616 58.580 59.337 1.00 51.07 C ANISOU 2417 CA LYS A 227 7943 4141 7320 -1015 -20 321 C ATOM 2418 C LYS A 227 -6.474 59.635 58.252 1.00 46.86 C ANISOU 2418 C LYS A 227 7280 3797 6728 -949 -129 170 C ATOM 2419 O LYS A 227 -5.969 60.734 58.513 1.00 44.04 O ANISOU 2419 O LYS A 227 6849 3669 6217 -858 -38 165 O ATOM 2420 CB LYS A 227 -5.478 57.566 59.233 1.00 60.52 C ANISOU 2420 CB LYS A 227 9395 5230 8369 -856 -123 284 C ATOM 2421 CG LYS A 227 -5.350 56.662 60.424 1.00 69.97 C ANISOU 2421 CG LYS A 227 10762 6271 9552 -873 -12 444 C ATOM 2422 CD LYS A 227 -4.271 55.621 60.194 1.00 79.95 C ANISOU 2422 CD LYS A 227 12265 7406 10706 -706 -144 395 C ATOM 2423 N GLU A 228 -6.904 59.320 57.022 1.00 46.72 N ANISOU 2423 N GLU A 228 7259 3671 6821 -991 -337 45 N ATOM 2424 CA GLU A 228 -6.829 60.308 55.945 1.00 47.89 C ANISOU 2424 CA GLU A 228 7323 3976 6895 -926 -443 -91 C ATOM 2425 C GLU A 228 -7.725 61.499 56.227 1.00 44.04 C ANISOU 2425 C GLU A 228 6574 3634 6525 -1038 -345 -40 C ATOM 2426 O GLU A 228 -7.371 62.626 55.897 1.00 43.11 O ANISOU 2426 O GLU A 228 6381 3721 6276 -951 -324 -95 O ATOM 2427 CB GLU A 228 -7.215 59.696 54.593 1.00 53.36 C ANISOU 2427 CB GLU A 228 8117 4490 7667 -951 -711 -233 C ATOM 2428 CG GLU A 228 -6.325 58.563 54.166 1.00 57.40 C ANISOU 2428 CG GLU A 228 8913 4848 8049 -814 -808 -308 C ATOM 2429 CD GLU A 228 -6.556 58.159 52.723 1.00 62.23 C ANISOU 2429 CD GLU A 228 9683 5307 8656 -791 -1074 -478 C ATOM 2430 OE1 GLU A 228 -6.434 59.008 51.796 1.00 68.46 O ANISOU 2430 OE1 GLU A 228 10471 6223 9319 -709 -1143 -585 O ATOM 2431 OE2 GLU A 228 -6.867 56.987 52.524 1.00 54.54 O ANISOU 2431 OE2 GLU A 228 8860 4068 7794 -854 -1220 -503 O ATOM 2432 N VAL A 229 -8.898 61.267 56.822 1.00 43.81 N ANISOU 2432 N VAL A 229 6396 3488 6764 -1228 -271 71 N ATOM 2433 CA VAL A 229 -9.771 62.385 57.185 1.00 42.41 C ANISOU 2433 CA VAL A 229 5955 3436 6721 -1319 -139 132 C ATOM 2434 C VAL A 229 -9.095 63.258 58.228 1.00 44.99 C ANISOU 2434 C VAL A 229 6293 3976 6825 -1214 105 206 C ATOM 2435 O VAL A 229 -9.035 64.485 58.095 1.00 46.20 O ANISOU 2435 O VAL A 229 6331 4322 6900 -1161 144 168 O ATOM 2436 CB VAL A 229 -11.127 61.858 57.684 1.00 48.21 C ANISOU 2436 CB VAL A 229 6517 3979 7824 -1536 -63 256 C ATOM 2437 CG1 VAL A 229 -11.950 62.969 58.308 1.00 49.02 C ANISOU 2437 CG1 VAL A 229 6356 4208 8062 -1602 154 346 C ATOM 2438 CG2 VAL A 229 -11.874 61.222 56.544 1.00 50.04 C ANISOU 2438 CG2 VAL A 229 6698 4006 8310 -1651 -367 162 C ATOM 2439 N HIS A 230 -8.536 62.625 59.263 1.00 47.38 N ANISOU 2439 N HIS A 230 6761 4228 7012 -1174 245 308 N ATOM 2440 CA HIS A 230 -7.871 63.367 60.332 1.00 46.67 C ANISOU 2440 CA HIS A 230 6729 4305 6698 -1073 435 378 C ATOM 2441 C HIS A 230 -6.698 64.173 59.789 1.00 43.45 C ANISOU 2441 C HIS A 230 6358 4097 6056 -899 333 259 C ATOM 2442 O HIS A 230 -6.510 65.336 60.157 1.00 40.62 O ANISOU 2442 O HIS A 230 5924 3916 5592 -852 425 262 O ATOM 2443 CB HIS A 230 -7.404 62.390 61.426 1.00 48.16 C ANISOU 2443 CB HIS A 230 7143 4368 6786 -1046 539 500 C ATOM 2444 CG HIS A 230 -6.784 63.068 62.609 1.00 64.18 C ANISOU 2444 CG HIS A 230 9278 6529 8578 -946 701 576 C ATOM 2445 ND1 HIS A 230 -5.440 63.376 62.675 1.00 67.75 N ANISOU 2445 ND1 HIS A 230 9850 7105 8788 -771 602 517 N ATOM 2446 CD2 HIS A 230 -7.330 63.519 63.765 1.00 65.62 C ANISOU 2446 CD2 HIS A 230 9475 6724 8732 -991 946 704 C ATOM 2447 CE1 HIS A 230 -5.185 63.984 63.818 1.00 66.11 C ANISOU 2447 CE1 HIS A 230 9732 6974 8411 -721 737 597 C ATOM 2448 NE2 HIS A 230 -6.314 64.081 64.498 1.00 66.87 N ANISOU 2448 NE2 HIS A 230 9793 7006 8608 -845 956 708 N ATOM 2449 N ALA A 231 -5.901 63.565 58.907 1.00 41.75 N ANISOU 2449 N ALA A 231 6257 3838 5767 -802 156 158 N ATOM 2450 CA ALA A 231 -4.772 64.259 58.296 1.00 39.22 C ANISOU 2450 CA ALA A 231 5954 3686 5262 -637 87 56 C ATOM 2451 C ALA A 231 -5.236 65.400 57.395 1.00 43.10 C ANISOU 2451 C ALA A 231 6281 4307 5789 -660 42 -29 C ATOM 2452 O ALA A 231 -4.638 66.484 57.401 1.00 42.72 O ANISOU 2452 O ALA A 231 6173 4440 5617 -576 86 -53 O ATOM 2453 CB ALA A 231 -3.926 63.250 57.509 1.00 41.61 C ANISOU 2453 CB ALA A 231 6426 3881 5504 -521 -53 -27 C ATOM 2454 N ALA A 232 -6.317 65.195 56.626 1.00 41.89 N ANISOU 2454 N ALA A 232 6051 4048 5817 -777 -64 -71 N ATOM 2455 CA ALA A 232 -6.834 66.297 55.807 1.00 39.60 C ANISOU 2455 CA ALA A 232 5614 3866 5564 -797 -128 -141 C ATOM 2456 C ALA A 232 -7.365 67.441 56.670 1.00 42.65 C ANISOU 2456 C ALA A 232 5818 4388 5997 -852 45 -60 C ATOM 2457 O ALA A 232 -7.232 68.618 56.299 1.00 40.83 O ANISOU 2457 O ALA A 232 5504 4312 5697 -801 47 -105 O ATOM 2458 CB ALA A 232 -7.931 65.785 54.852 1.00 40.45 C ANISOU 2458 CB ALA A 232 5684 3804 5882 -914 -327 -200 C ATOM 2459 N LYS A 233 -7.993 67.130 57.814 1.00 44.03 N ANISOU 2459 N LYS A 233 5947 4494 6287 -950 208 63 N ATOM 2460 CA LYS A 233 -8.451 68.210 58.694 1.00 42.96 C ANISOU 2460 CA LYS A 233 5681 4477 6167 -975 406 138 C ATOM 2461 C LYS A 233 -7.272 69.016 59.241 1.00 37.75 C ANISOU 2461 C LYS A 233 5118 3989 5237 -835 477 130 C ATOM 2462 O LYS A 233 -7.344 70.247 59.364 1.00 35.25 O ANISOU 2462 O LYS A 233 4706 3810 4876 -810 541 117 O ATOM 2463 CB LYS A 233 -9.275 67.651 59.854 1.00 47.65 C ANISOU 2463 CB LYS A 233 6254 4946 6906 -1086 612 283 C ATOM 2464 CG LYS A 233 -10.642 67.117 59.470 1.00 57.18 C ANISOU 2464 CG LYS A 233 7276 5985 8465 -1254 580 317 C ATOM 2465 CD LYS A 233 -11.360 66.617 60.725 1.00 66.19 C ANISOU 2465 CD LYS A 233 8401 7004 9744 -1354 855 487 C ATOM 2466 CE LYS A 233 -12.757 66.136 60.426 1.00 74.84 C ANISOU 2466 CE LYS A 233 9257 7921 11256 -1536 848 542 C ATOM 2467 NZ LYS A 233 -13.428 65.607 61.653 1.00 78.70 N ANISOU 2467 NZ LYS A 233 9736 8276 11892 -1632 1166 729 N ATOM 2468 N SER A 234 -6.181 68.337 59.582 1.00 37.38 N ANISOU 2468 N SER A 234 5255 3920 5028 -744 449 138 N ATOM 2469 CA SER A 234 -4.999 69.043 60.076 1.00 30.82 C ANISOU 2469 CA SER A 234 4498 3230 3983 -616 469 129 C ATOM 2470 C SER A 234 -4.497 70.043 59.057 1.00 39.50 C ANISOU 2470 C SER A 234 5502 4472 5034 -547 377 25 C ATOM 2471 O SER A 234 -4.246 71.211 59.384 1.00 41.56 O ANISOU 2471 O SER A 234 5707 4865 5220 -514 429 22 O ATOM 2472 CB SER A 234 -3.910 68.023 60.418 1.00 32.87 C ANISOU 2472 CB SER A 234 4941 3417 4130 -523 407 149 C ATOM 2473 OG SER A 234 -4.397 67.213 61.468 1.00 39.76 O ANISOU 2473 OG SER A 234 5927 4154 5024 -587 512 263 O ATOM 2474 N LEU A 235 -4.360 69.596 57.799 1.00 38.03 N ANISOU 2474 N LEU A 235 5324 4245 4882 -521 242 -60 N ATOM 2475 CA LEU A 235 -3.830 70.446 56.744 1.00 36.23 C ANISOU 2475 CA LEU A 235 5048 4130 4587 -443 176 -148 C ATOM 2476 C LEU A 235 -4.783 71.586 56.396 1.00 36.78 C ANISOU 2476 C LEU A 235 4968 4273 4734 -514 186 -165 C ATOM 2477 O LEU A 235 -4.334 72.671 56.005 1.00 38.02 O ANISOU 2477 O LEU A 235 5076 4554 4815 -456 191 -200 O ATOM 2478 CB LEU A 235 -3.531 69.590 55.509 1.00 37.02 C ANISOU 2478 CB LEU A 235 5255 4137 4675 -385 48 -232 C ATOM 2479 CG LEU A 235 -2.440 68.553 55.783 1.00 42.38 C ANISOU 2479 CG LEU A 235 6074 4749 5280 -281 45 -221 C ATOM 2480 CD1 LEU A 235 -2.353 67.570 54.624 1.00 43.63 C ANISOU 2480 CD1 LEU A 235 6371 4774 5432 -228 -66 -307 C ATOM 2481 CD2 LEU A 235 -1.101 69.247 56.012 1.00 43.80 C ANISOU 2481 CD2 LEU A 235 6224 5066 5352 -152 100 -215 C ATOM 2482 N ALA A 236 -6.088 71.359 56.513 1.00 33.37 N ANISOU 2482 N ALA A 236 4450 3753 4477 -637 190 -135 N ATOM 2483 CA ALA A 236 -7.061 72.416 56.259 1.00 35.07 C ANISOU 2483 CA ALA A 236 4498 4022 4805 -696 198 -142 C ATOM 2484 C ALA A 236 -7.020 73.504 57.341 1.00 41.11 C ANISOU 2484 C ALA A 236 5200 4904 5517 -684 373 -84 C ATOM 2485 O ALA A 236 -7.329 74.670 57.060 1.00 40.00 O ANISOU 2485 O ALA A 236 4954 4851 5392 -676 379 -108 O ATOM 2486 CB ALA A 236 -8.465 71.795 56.172 1.00 35.49 C ANISOU 2486 CB ALA A 236 4440 3927 5119 -834 157 -112 C ATOM 2487 N ILE A 237 -6.670 73.141 58.584 1.00 38.11 N ANISOU 2487 N ILE A 237 4910 4509 5062 -676 504 -9 N ATOM 2488 CA ILE A 237 -6.492 74.138 59.639 1.00 37.51 C ANISOU 2488 CA ILE A 237 4844 4525 4884 -643 647 33 C ATOM 2489 C ILE A 237 -5.404 75.129 59.251 1.00 37.75 C ANISOU 2489 C ILE A 237 4888 4688 4769 -547 571 -32 C ATOM 2490 O ILE A 237 -5.524 76.325 59.518 1.00 37.59 O ANISOU 2490 O ILE A 237 4812 4750 4720 -534 627 -38 O ATOM 2491 CB ILE A 237 -6.165 73.458 60.987 1.00 38.39 C ANISOU 2491 CB ILE A 237 5121 4572 4891 -631 761 120 C ATOM 2492 CG1 ILE A 237 -7.381 72.726 61.535 1.00 45.27 C ANISOU 2492 CG1 ILE A 237 5964 5311 5925 -737 910 211 C ATOM 2493 CG2 ILE A 237 -5.726 74.489 62.050 1.00 40.10 C ANISOU 2493 CG2 ILE A 237 5423 4872 4940 -569 856 141 C ATOM 2494 CD1 ILE A 237 -7.041 71.809 62.764 1.00 47.44 C ANISOU 2494 CD1 ILE A 237 6457 5487 6080 -723 1018 311 C ATOM 2495 N ILE A 238 -4.314 74.629 58.649 1.00 30.68 N ANISOU 2495 N ILE A 238 4062 3800 3793 -476 458 -73 N ATOM 2496 CA ILE A 238 -3.244 75.478 58.131 1.00 34.69 C ANISOU 2496 CA ILE A 238 4554 4416 4212 -392 402 -122 C ATOM 2497 C ILE A 238 -3.803 76.505 57.141 1.00 37.89 C ANISOU 2497 C ILE A 238 4847 4881 4669 -410 377 -171 C ATOM 2498 O ILE A 238 -3.447 77.691 57.179 1.00 33.38 O ANISOU 2498 O ILE A 238 4230 4400 4053 -383 396 -181 O ATOM 2499 CB ILE A 238 -2.155 74.609 57.464 1.00 37.80 C ANISOU 2499 CB ILE A 238 5019 4782 4561 -308 319 -152 C ATOM 2500 CG1 ILE A 238 -1.657 73.527 58.442 1.00 47.12 C ANISOU 2500 CG1 ILE A 238 6315 5884 5705 -283 321 -99 C ATOM 2501 CG2 ILE A 238 -1.002 75.477 56.884 1.00 35.96 C ANISOU 2501 CG2 ILE A 238 4738 4649 4274 -221 300 -185 C ATOM 2502 CD1 ILE A 238 -0.519 73.926 59.292 1.00 49.28 C ANISOU 2502 CD1 ILE A 238 6619 6209 5896 -211 303 -72 C ATOM 2503 N VAL A 239 -4.631 76.048 56.197 1.00 34.39 N ANISOU 2503 N VAL A 239 4376 4372 4318 -452 306 -203 N ATOM 2504 CA VAL A 239 -5.210 76.968 55.216 1.00 34.04 C ANISOU 2504 CA VAL A 239 4252 4364 4318 -460 247 -246 C ATOM 2505 C VAL A 239 -6.075 78.008 55.918 1.00 34.93 C ANISOU 2505 C VAL A 239 4243 4517 4511 -510 335 -212 C ATOM 2506 O VAL A 239 -6.046 79.200 55.569 1.00 33.23 O ANISOU 2506 O VAL A 239 3978 4375 4272 -482 331 -232 O ATOM 2507 CB VAL A 239 -6.007 76.195 54.149 1.00 37.04 C ANISOU 2507 CB VAL A 239 4649 4634 4789 -498 106 -290 C ATOM 2508 CG1 VAL A 239 -6.682 77.194 53.145 1.00 37.29 C ANISOU 2508 CG1 VAL A 239 4618 4688 4862 -499 8 -331 C ATOM 2509 CG2 VAL A 239 -5.097 75.195 53.446 1.00 31.76 C ANISOU 2509 CG2 VAL A 239 4141 3913 4012 -424 38 -334 C ATOM 2510 N GLY A 240 -6.824 77.580 56.939 1.00 34.88 N ANISOU 2510 N GLY A 240 4201 4454 4597 -573 438 -154 N ATOM 2511 CA GLY A 240 -7.743 78.490 57.620 1.00 36.56 C ANISOU 2511 CA GLY A 240 4304 4685 4902 -605 561 -119 C ATOM 2512 C GLY A 240 -7.013 79.548 58.429 1.00 39.29 C ANISOU 2512 C GLY A 240 4713 5122 5094 -544 651 -115 C ATOM 2513 O GLY A 240 -7.428 80.714 58.463 1.00 33.47 O ANISOU 2513 O GLY A 240 3903 4429 4385 -531 692 -126 O ATOM 2514 N LEU A 241 -5.878 79.178 59.041 1.00 34.31 N ANISOU 2514 N LEU A 241 4222 4509 4308 -501 651 -104 N ATOM 2515 CA LEU A 241 -5.060 80.167 59.752 1.00 33.14 C ANISOU 2515 CA LEU A 241 4144 4427 4023 -447 674 -111 C ATOM 2516 C LEU A 241 -4.338 81.121 58.788 1.00 35.35 C ANISOU 2516 C LEU A 241 4368 4786 4280 -409 573 -163 C ATOM 2517 O LEU A 241 -4.141 82.287 59.120 1.00 34.78 O ANISOU 2517 O LEU A 241 4293 4756 4166 -390 590 -175 O ATOM 2518 CB LEU A 241 -4.050 79.456 60.657 1.00 34.62 C ANISOU 2518 CB LEU A 241 4486 4589 4079 -410 655 -82 C ATOM 2519 CG LEU A 241 -4.700 78.760 61.879 1.00 38.89 C ANISOU 2519 CG LEU A 241 5142 5044 4590 -435 792 -13 C ATOM 2520 CD1 LEU A 241 -3.691 77.885 62.621 1.00 43.37 C ANISOU 2520 CD1 LEU A 241 5885 5567 5027 -391 730 19 C ATOM 2521 CD2 LEU A 241 -5.271 79.824 62.799 1.00 42.98 C ANISOU 2521 CD2 LEU A 241 5705 5569 5056 -424 930 -1 C ATOM 2522 N PHE A 242 -3.918 80.644 57.617 1.00 30.08 N ANISOU 2522 N PHE A 242 3678 4123 3629 -392 480 -191 N ATOM 2523 CA PHE A 242 -3.401 81.555 56.586 1.00 28.35 C ANISOU 2523 CA PHE A 242 3418 3962 3393 -357 426 -224 C ATOM 2524 C PHE A 242 -4.453 82.619 56.244 1.00 33.14 C ANISOU 2524 C PHE A 242 3944 4580 4069 -382 437 -236 C ATOM 2525 O PHE A 242 -4.161 83.816 56.239 1.00 31.46 O ANISOU 2525 O PHE A 242 3711 4411 3830 -364 447 -242 O ATOM 2526 CB PHE A 242 -2.984 80.762 55.341 1.00 29.20 C ANISOU 2526 CB PHE A 242 3560 4048 3487 -322 358 -249 C ATOM 2527 CG PHE A 242 -2.385 81.608 54.241 1.00 31.08 C ANISOU 2527 CG PHE A 242 3794 4331 3685 -274 341 -267 C ATOM 2528 CD1 PHE A 242 -3.206 82.235 53.315 1.00 32.55 C ANISOU 2528 CD1 PHE A 242 3968 4510 3890 -282 297 -287 C ATOM 2529 CD2 PHE A 242 -1.011 81.825 54.175 1.00 29.03 C ANISOU 2529 CD2 PHE A 242 3535 4109 3385 -219 373 -251 C ATOM 2530 CE1 PHE A 242 -2.667 83.058 52.313 1.00 35.16 C ANISOU 2530 CE1 PHE A 242 4329 4869 4161 -234 300 -289 C ATOM 2531 CE2 PHE A 242 -0.468 82.642 53.164 1.00 30.25 C ANISOU 2531 CE2 PHE A 242 3685 4293 3516 -179 400 -248 C ATOM 2532 CZ PHE A 242 -1.308 83.251 52.245 1.00 34.34 C ANISOU 2532 CZ PHE A 242 4232 4802 4015 -186 371 -265 C ATOM 2533 N ALA A 243 -5.702 82.201 56.016 1.00 32.69 N ANISOU 2533 N ALA A 243 3826 4468 4126 -426 429 -235 N ATOM 2534 CA ALA A 243 -6.762 83.162 55.686 1.00 34.02 C ANISOU 2534 CA ALA A 243 3892 4634 4400 -439 423 -242 C ATOM 2535 C ALA A 243 -7.016 84.144 56.838 1.00 36.82 C ANISOU 2535 C ALA A 243 4224 5012 4755 -432 553 -222 C ATOM 2536 O ALA A 243 -7.174 85.351 56.614 1.00 35.17 O ANISOU 2536 O ALA A 243 3979 4828 4557 -407 548 -236 O ATOM 2537 CB ALA A 243 -8.046 82.403 55.329 1.00 31.10 C ANISOU 2537 CB ALA A 243 3429 4181 4208 -494 371 -237 C ATOM 2538 N ALEU A 244 -7.053 83.641 58.078 0.50 35.21 N ANISOU 2538 N ALEU A 244 4072 4783 4523 -445 672 -189 N ATOM 2539 N BLEU A 244 -7.051 83.641 58.076 0.50 35.23 N ANISOU 2539 N BLEU A 244 4074 4785 4525 -445 672 -189 N ATOM 2540 CA ALEU A 244 -7.301 84.501 59.230 0.50 34.25 C ANISOU 2540 CA ALEU A 244 3990 4662 4363 -422 809 -176 C ATOM 2541 CA BLEU A 244 -7.302 84.501 59.226 0.50 34.24 C ANISOU 2541 CA BLEU A 244 3988 4660 4362 -422 809 -176 C ATOM 2542 C ALEU A 244 -6.194 85.537 59.396 0.50 35.31 C ANISOU 2542 C ALEU A 244 4213 4846 4357 -379 754 -209 C ATOM 2543 C BLEU A 244 -6.194 85.535 59.402 0.50 35.32 C ANISOU 2543 C BLEU A 244 4215 4848 4359 -379 755 -208 C ATOM 2544 O ALEU A 244 -6.460 86.682 59.778 0.50 35.57 O ANISOU 2544 O ALEU A 244 4255 4879 4382 -352 806 -224 O ATOM 2545 O BLEU A 244 -6.459 86.675 59.798 0.50 35.57 O ANISOU 2545 O BLEU A 244 4257 4879 4381 -351 807 -224 O ATOM 2546 CB ALEU A 244 -7.436 83.653 60.500 0.50 35.18 C ANISOU 2546 CB ALEU A 244 4211 4727 4429 -432 947 -128 C ATOM 2547 CB BLEU A 244 -7.449 83.651 60.491 0.50 35.21 C ANISOU 2547 CB BLEU A 244 4212 4730 4434 -433 947 -127 C ATOM 2548 CG ALEU A 244 -7.604 84.413 61.823 0.50 36.57 C ANISOU 2548 CG ALEU A 244 4511 4882 4503 -387 1107 -116 C ATOM 2549 CG BLEU A 244 -8.829 83.094 60.832 0.50 42.92 C ANISOU 2549 CG BLEU A 244 5089 5633 5585 -474 1104 -73 C ATOM 2550 CD1ALEU A 244 -9.012 85.016 61.912 0.50 41.30 C ANISOU 2550 CD1ALEU A 244 4975 5446 5270 -381 1270 -98 C ATOM 2551 CD1BLEU A 244 -8.761 82.294 62.130 0.50 44.15 C ANISOU 2551 CD1BLEU A 244 5406 5729 5639 -475 1262 -11 C ATOM 2552 CD2ALEU A 244 -7.335 83.503 63.017 0.50 36.19 C ANISOU 2552 CD2ALEU A 244 4651 4778 4321 -381 1203 -66 C ATOM 2553 CD2BLEU A 244 -9.863 84.225 60.961 0.50 41.37 C ANISOU 2553 CD2BLEU A 244 4776 5428 5514 -447 1223 -74 C ATOM 2554 N CYS A 245 -4.943 85.157 59.122 1.00 29.90 N ANISOU 2554 N CYS A 245 3585 4191 3585 -372 651 -217 N ATOM 2555 CA CYS A 245 -3.837 86.101 59.314 1.00 31.66 C ANISOU 2555 CA CYS A 245 3860 4442 3726 -347 587 -237 C ATOM 2556 C CYS A 245 -3.699 87.116 58.169 1.00 33.92 C ANISOU 2556 C CYS A 245 4062 4761 4064 -343 531 -255 C ATOM 2557 O CYS A 245 -3.160 88.203 58.396 1.00 33.37 O ANISOU 2557 O CYS A 245 4016 4695 3970 -335 505 -268 O ATOM 2558 CB CYS A 245 -2.506 85.348 59.465 1.00 29.76 C ANISOU 2558 CB CYS A 245 3673 4210 3425 -336 502 -227 C ATOM 2559 SG CYS A 245 -2.401 84.428 61.070 1.00 33.41 S ANISOU 2559 SG CYS A 245 4306 4613 3775 -325 533 -200 S ATOM 2560 N TRP A 246 -4.088 86.772 56.936 1.00 30.64 N ANISOU 2560 N TRP A 246 3578 4355 3709 -346 497 -254 N ATOM 2561 CA TRP A 246 -3.886 87.675 55.791 1.00 29.55 C ANISOU 2561 CA TRP A 246 3408 4235 3585 -331 448 -258 C ATOM 2562 C TRP A 246 -5.127 88.471 55.404 1.00 34.02 C ANISOU 2562 C TRP A 246 3919 4778 4230 -325 445 -267 C ATOM 2563 O TRP A 246 -4.995 89.554 54.818 1.00 31.95 O ANISOU 2563 O TRP A 246 3656 4516 3966 -308 417 -265 O ATOM 2564 CB TRP A 246 -3.394 86.892 54.552 1.00 30.25 C ANISOU 2564 CB TRP A 246 3515 4330 3649 -313 398 -254 C ATOM 2565 CG TRP A 246 -1.935 86.583 54.682 1.00 30.98 C ANISOU 2565 CG TRP A 246 3630 4445 3697 -296 410 -237 C ATOM 2566 CD1 TRP A 246 -1.364 85.419 55.141 1.00 30.30 C ANISOU 2566 CD1 TRP A 246 3567 4354 3592 -288 409 -233 C ATOM 2567 CD2 TRP A 246 -0.859 87.489 54.433 1.00 31.15 C ANISOU 2567 CD2 TRP A 246 3630 4482 3723 -288 422 -214 C ATOM 2568 NE1 TRP A 246 0.005 85.545 55.155 1.00 34.58 N ANISOU 2568 NE1 TRP A 246 4088 4912 4140 -264 410 -211 N ATOM 2569 CE2 TRP A 246 0.343 86.808 54.734 1.00 31.00 C ANISOU 2569 CE2 TRP A 246 3595 4471 3714 -272 423 -196 C ATOM 2570 CE3 TRP A 246 -0.794 88.801 53.963 1.00 29.77 C ANISOU 2570 CE3 TRP A 246 3440 4304 3566 -293 430 -199 C ATOM 2571 CZ2 TRP A 246 1.601 87.420 54.617 1.00 30.91 C ANISOU 2571 CZ2 TRP A 246 3519 4461 3762 -269 435 -162 C ATOM 2572 CZ3 TRP A 246 0.454 89.417 53.852 1.00 29.99 C ANISOU 2572 CZ3 TRP A 246 3427 4331 3636 -299 452 -162 C ATOM 2573 CH2 TRP A 246 1.636 88.714 54.148 1.00 30.06 C ANISOU 2573 CH2 TRP A 246 3390 4347 3685 -290 456 -142 C ATOM 2574 N LEU A 247 -6.332 87.961 55.674 1.00 29.39 N ANISOU 2574 N LEU A 247 3271 4160 3737 -339 473 -267 N ATOM 2575 CA LEU A 247 -7.523 88.681 55.219 1.00 31.07 C ANISOU 2575 CA LEU A 247 3393 4340 4072 -324 449 -271 C ATOM 2576 C LEU A 247 -7.671 90.090 55.798 1.00 35.68 C ANISOU 2576 C LEU A 247 3978 4918 4662 -291 514 -277 C ATOM 2577 O LEU A 247 -8.164 90.969 55.073 1.00 37.08 O ANISOU 2577 O LEU A 247 4114 5074 4900 -262 453 -279 O ATOM 2578 CB LEU A 247 -8.784 87.861 55.536 1.00 31.27 C ANISOU 2578 CB LEU A 247 3307 4317 4258 -352 485 -258 C ATOM 2579 CG LEU A 247 -9.117 86.762 54.519 1.00 42.28 C ANISOU 2579 CG LEU A 247 4673 5676 5714 -383 346 -264 C ATOM 2580 CD1 LEU A 247 -10.391 86.016 54.904 1.00 44.96 C ANISOU 2580 CD1 LEU A 247 4867 5947 6270 -431 378 -241 C ATOM 2581 CD2 LEU A 247 -9.264 87.362 53.150 1.00 50.25 C ANISOU 2581 CD2 LEU A 247 5700 6672 6722 -350 180 -282 C ATOM 2582 N PRO A 248 -7.329 90.370 57.059 1.00 34.84 N ANISOU 2582 N PRO A 248 3940 4810 4488 -285 620 -284 N ATOM 2583 CA PRO A 248 -7.541 91.744 57.562 1.00 34.85 C ANISOU 2583 CA PRO A 248 3970 4781 4489 -243 671 -303 C ATOM 2584 C PRO A 248 -6.851 92.808 56.725 1.00 32.93 C ANISOU 2584 C PRO A 248 3756 4541 4214 -237 569 -307 C ATOM 2585 O PRO A 248 -7.456 93.834 56.410 1.00 34.80 O ANISOU 2585 O PRO A 248 3964 4741 4518 -199 559 -312 O ATOM 2586 CB PRO A 248 -6.984 91.673 58.999 1.00 37.31 C ANISOU 2586 CB PRO A 248 4421 5079 4676 -239 758 -318 C ATOM 2587 CG PRO A 248 -7.320 90.231 59.430 1.00 39.31 C ANISOU 2587 CG PRO A 248 4661 5338 4938 -264 829 -290 C ATOM 2588 CD PRO A 248 -6.936 89.448 58.154 1.00 37.17 C ANISOU 2588 CD PRO A 248 4312 5106 4703 -304 697 -277 C ATOM 2589 N LEU A 249 -5.594 92.579 56.360 1.00 30.86 N ANISOU 2589 N LEU A 249 3545 4311 3868 -270 505 -296 N ATOM 2590 CA LEU A 249 -4.856 93.512 55.514 1.00 31.40 C ANISOU 2590 CA LEU A 249 3636 4373 3923 -274 441 -279 C ATOM 2591 C LEU A 249 -5.528 93.677 54.158 1.00 37.97 C ANISOU 2591 C LEU A 249 4433 5195 4798 -247 384 -257 C ATOM 2592 O LEU A 249 -5.649 94.793 53.646 1.00 37.33 O ANISOU 2592 O LEU A 249 4373 5075 4736 -225 354 -243 O ATOM 2593 CB LEU A 249 -3.437 92.990 55.346 1.00 34.98 C ANISOU 2593 CB LEU A 249 4111 4859 4322 -309 418 -257 C ATOM 2594 CG LEU A 249 -2.184 93.836 55.164 1.00 42.89 C ANISOU 2594 CG LEU A 249 5125 5840 5329 -338 393 -231 C ATOM 2595 CD1 LEU A 249 -2.262 95.162 55.885 1.00 34.85 C ANISOU 2595 CD1 LEU A 249 4150 4758 4332 -345 373 -255 C ATOM 2596 CD2 LEU A 249 -0.965 93.033 55.618 1.00 34.64 C ANISOU 2596 CD2 LEU A 249 4064 4820 4277 -366 376 -220 C ATOM 2597 N HIS A 250 -5.933 92.558 53.530 1.00 34.95 N ANISOU 2597 N HIS A 250 4023 4832 4424 -247 345 -254 N ATOM 2598 CA HIS A 250 -6.629 92.656 52.252 1.00 31.97 C ANISOU 2598 CA HIS A 250 3650 4425 4074 -215 244 -242 C ATOM 2599 C HIS A 250 -7.920 93.461 52.387 1.00 33.90 C ANISOU 2599 C HIS A 250 3813 4618 4449 -178 214 -251 C ATOM 2600 O HIS A 250 -8.249 94.282 51.523 1.00 31.48 O ANISOU 2600 O HIS A 250 3537 4268 4155 -138 126 -234 O ATOM 2601 CB HIS A 250 -6.930 91.244 51.701 1.00 26.34 C ANISOU 2601 CB HIS A 250 2935 3715 3357 -224 178 -253 C ATOM 2602 CG HIS A 250 -5.717 90.551 51.138 1.00 31.08 C ANISOU 2602 CG HIS A 250 3638 4344 3825 -226 195 -240 C ATOM 2603 ND1 HIS A 250 -5.029 91.036 50.048 1.00 28.99 N ANISOU 2603 ND1 HIS A 250 3487 4069 3459 -191 187 -209 N ATOM 2604 CD2 HIS A 250 -5.066 89.424 51.523 1.00 32.12 C ANISOU 2604 CD2 HIS A 250 3779 4506 3919 -246 240 -248 C ATOM 2605 CE1 HIS A 250 -4.005 90.232 49.774 1.00 30.23 C ANISOU 2605 CE1 HIS A 250 3704 4250 3532 -185 245 -199 C ATOM 2606 NE2 HIS A 250 -4.006 89.248 50.661 1.00 30.50 N ANISOU 2606 NE2 HIS A 250 3672 4310 3608 -217 264 -226 N ATOM 2607 N ILE A 251 -8.677 93.217 53.449 1.00 27.87 N ANISOU 2607 N ILE A 251 2950 3849 3790 -182 296 -271 N ATOM 2608 CA ILE A 251 -9.967 93.890 53.623 1.00 32.60 C ANISOU 2608 CA ILE A 251 3437 4393 4558 -133 300 -274 C ATOM 2609 C ILE A 251 -9.779 95.384 53.866 1.00 33.83 C ANISOU 2609 C ILE A 251 3650 4515 4689 -87 335 -279 C ATOM 2610 O ILE A 251 -10.560 96.205 53.363 1.00 31.42 O ANISOU 2610 O ILE A 251 3297 4152 4489 -29 268 -271 O ATOM 2611 CB ILE A 251 -10.753 93.216 54.756 1.00 32.87 C ANISOU 2611 CB ILE A 251 3358 4421 4711 -143 440 -280 C ATOM 2612 CG1 ILE A 251 -11.244 91.837 54.253 1.00 34.38 C ANISOU 2612 CG1 ILE A 251 3460 4608 4995 -191 359 -268 C ATOM 2613 CG2 ILE A 251 -11.969 94.110 55.216 1.00 29.73 C ANISOU 2613 CG2 ILE A 251 2834 3958 4502 -72 522 -279 C ATOM 2614 CD1 ILE A 251 -11.798 90.971 55.351 1.00 42.49 C ANISOU 2614 CD1 ILE A 251 4397 5624 6123 -222 521 -254 C ATOM 2615 N ILE A 252 -8.744 95.763 54.641 1.00 29.72 N ANISOU 2615 N ILE A 252 3237 4013 4044 -111 418 -292 N ATOM 2616 CA ILE A 252 -8.387 97.180 54.796 1.00 31.26 C ANISOU 2616 CA ILE A 252 3513 4155 4210 -83 422 -299 C ATOM 2617 C ILE A 252 -8.099 97.832 53.439 1.00 32.99 C ANISOU 2617 C ILE A 252 3778 4349 4409 -76 302 -257 C ATOM 2618 O ILE A 252 -8.591 98.932 53.150 1.00 32.59 O ANISOU 2618 O ILE A 252 3740 4228 4416 -23 266 -250 O ATOM 2619 CB ILE A 252 -7.189 97.333 55.749 1.00 32.46 C ANISOU 2619 CB ILE A 252 3775 4315 4242 -129 472 -321 C ATOM 2620 CG1 ILE A 252 -7.617 96.959 57.187 1.00 33.95 C ANISOU 2620 CG1 ILE A 252 3987 4496 4416 -106 598 -362 C ATOM 2621 CG2 ILE A 252 -6.677 98.741 55.709 1.00 29.85 C ANISOU 2621 CG2 ILE A 252 3531 3913 3897 -124 437 -323 C ATOM 2622 CD1 ILE A 252 -6.476 96.880 58.191 1.00 38.27 C ANISOU 2622 CD1 ILE A 252 4669 5041 4831 -147 600 -390 C ATOM 2623 N ASN A 253 -7.288 97.172 52.591 1.00 31.23 N ANISOU 2623 N ASN A 253 3602 4169 4094 -119 254 -224 N ATOM 2624 CA ASN A 253 -7.040 97.681 51.235 1.00 32.05 C ANISOU 2624 CA ASN A 253 3792 4238 4146 -100 169 -173 C ATOM 2625 C ASN A 253 -8.329 97.864 50.439 1.00 34.54 C ANISOU 2625 C ASN A 253 4080 4501 4542 -30 42 -168 C ATOM 2626 O ASN A 253 -8.459 98.837 49.695 1.00 35.33 O ANISOU 2626 O ASN A 253 4261 4534 4631 14 -28 -131 O ATOM 2627 CB ASN A 253 -6.057 96.759 50.489 1.00 27.75 C ANISOU 2627 CB ASN A 253 3315 3743 3485 -135 178 -141 C ATOM 2628 CG ASN A 253 -4.603 96.869 51.060 1.00 33.35 C ANISOU 2628 CG ASN A 253 4038 4480 4155 -198 280 -124 C ATOM 2629 OD1 ASN A 253 -4.281 97.830 51.792 1.00 32.20 O ANISOU 2629 OD1 ASN A 253 3887 4295 4051 -222 307 -131 O ATOM 2630 ND2 ASN A 253 -3.743 95.883 50.744 1.00 26.31 N ANISOU 2630 ND2 ASN A 253 3159 3639 3201 -220 321 -106 N ATOM 2631 N CYS A 254 -9.305 96.954 50.580 1.00 30.14 N ANISOU 2631 N CYS A 254 3404 3958 4087 -19 -5 -198 N ATOM 2632 CA CYS A 254 -10.581 97.161 49.894 1.00 29.80 C ANISOU 2632 CA CYS A 254 3296 3848 4179 45 -163 -194 C ATOM 2633 C CYS A 254 -11.280 98.440 50.367 1.00 35.08 C ANISOU 2633 C CYS A 254 3898 4450 4982 112 -138 -196 C ATOM 2634 O CYS A 254 -11.873 99.163 49.551 1.00 36.00 O ANISOU 2634 O CYS A 254 4039 4488 5152 180 -283 -171 O ATOM 2635 CB CYS A 254 -11.498 95.941 50.091 1.00 32.79 C ANISOU 2635 CB CYS A 254 3517 4238 4704 26 -212 -221 C ATOM 2636 SG CYS A 254 -10.915 94.479 49.181 1.00 37.00 S ANISOU 2636 SG CYS A 254 4166 4803 5088 -25 -315 -226 S ATOM 2637 N PHE A 255 -11.257 98.729 51.680 1.00 31.52 N ANISOU 2637 N PHE A 255 3385 4013 4578 107 38 -227 N ATOM 2638 CA PHE A 255 -11.862 99.984 52.160 1.00 35.21 C ANISOU 2638 CA PHE A 255 3822 4402 5156 188 84 -238 C ATOM 2639 C PHE A 255 -11.115 101.194 51.609 1.00 36.83 C ANISOU 2639 C PHE A 255 4198 4550 5246 198 33 -209 C ATOM 2640 O PHE A 255 -11.731 102.165 51.137 1.00 38.65 O ANISOU 2640 O PHE A 255 4436 4690 5559 279 -53 -189 O ATOM 2641 CB PHE A 255 -11.898 100.049 53.703 1.00 36.04 C ANISOU 2641 CB PHE A 255 3896 4516 5283 194 297 -285 C ATOM 2642 CG PHE A 255 -13.096 99.358 54.297 1.00 38.07 C ANISOU 2642 CG PHE A 255 3956 4773 5736 229 391 -295 C ATOM 2643 CD1 PHE A 255 -14.286 100.058 54.495 1.00 41.61 C ANISOU 2643 CD1 PHE A 255 4268 5138 6403 337 433 -296 C ATOM 2644 CD2 PHE A 255 -13.059 97.996 54.567 1.00 37.91 C ANISOU 2644 CD2 PHE A 255 3871 4820 5712 158 437 -292 C ATOM 2645 CE1 PHE A 255 -15.419 99.419 54.995 1.00 41.69 C ANISOU 2645 CE1 PHE A 255 4057 5135 6647 368 544 -287 C ATOM 2646 CE2 PHE A 255 -14.178 97.346 55.096 1.00 39.99 C ANISOU 2646 CE2 PHE A 255 3938 5067 6190 179 543 -284 C ATOM 2647 CZ PHE A 255 -15.363 98.048 55.287 1.00 43.72 C ANISOU 2647 CZ PHE A 255 4250 5458 6903 280 602 -277 C ATOM 2648 N THR A 256 -9.783 101.170 51.696 1.00 31.58 N ANISOU 2648 N THR A 256 3659 3923 4415 118 88 -198 N ATOM 2649 CA THR A 256 -8.992 102.265 51.149 1.00 32.84 C ANISOU 2649 CA THR A 256 3967 4017 4494 107 60 -153 C ATOM 2650 C THR A 256 -9.340 102.503 49.684 1.00 34.66 C ANISOU 2650 C THR A 256 4273 4197 4699 156 -89 -88 C ATOM 2651 O THR A 256 -9.595 103.640 49.271 1.00 36.84 O ANISOU 2651 O THR A 256 4624 4371 5001 212 -148 -55 O ATOM 2652 CB THR A 256 -7.513 101.946 51.308 1.00 30.98 C ANISOU 2652 CB THR A 256 3804 3833 4134 4 133 -135 C ATOM 2653 OG1 THR A 256 -7.252 101.752 52.702 1.00 35.20 O ANISOU 2653 OG1 THR A 256 4299 4394 4680 -29 226 -200 O ATOM 2654 CG2 THR A 256 -6.629 103.104 50.728 1.00 32.19 C ANISOU 2654 CG2 THR A 256 4088 3900 4243 -26 127 -69 C ATOM 2655 N PHE A 257 -9.422 101.422 48.899 1.00 32.66 N ANISOU 2655 N PHE A 257 4024 3997 4387 146 -167 -74 N ATOM 2656 CA PHE A 257 -9.610 101.526 47.451 1.00 34.56 C ANISOU 2656 CA PHE A 257 4408 4181 4543 195 -323 -15 C ATOM 2657 C PHE A 257 -11.048 101.873 47.081 1.00 37.80 C ANISOU 2657 C PHE A 257 4746 4510 5107 296 -512 -24 C ATOM 2658 O PHE A 257 -11.282 102.752 46.255 1.00 37.37 O ANISOU 2658 O PHE A 257 4822 4355 5021 364 -632 28 O ATOM 2659 CB PHE A 257 -9.207 100.201 46.785 1.00 32.06 C ANISOU 2659 CB PHE A 257 4155 3931 4097 161 -351 -13 C ATOM 2660 CG PHE A 257 -9.275 100.225 45.291 1.00 33.94 C ANISOU 2660 CG PHE A 257 4611 4099 4185 221 -502 42 C ATOM 2661 CD1 PHE A 257 -8.493 101.118 44.552 1.00 33.98 C ANISOU 2661 CD1 PHE A 257 4830 4040 4042 235 -443 128 C ATOM 2662 CD2 PHE A 257 -10.096 99.335 44.610 1.00 37.10 C ANISOU 2662 CD2 PHE A 257 5028 4481 4587 262 -704 12 C ATOM 2663 CE1 PHE A 257 -8.554 101.140 43.170 1.00 39.37 C ANISOU 2663 CE1 PHE A 257 5770 4643 4545 305 -565 186 C ATOM 2664 CE2 PHE A 257 -10.153 99.335 43.212 1.00 44.51 C ANISOU 2664 CE2 PHE A 257 6231 5335 5345 330 -870 55 C ATOM 2665 CZ PHE A 257 -9.393 100.252 42.488 1.00 42.80 C ANISOU 2665 CZ PHE A 257 6259 5058 4946 361 -791 144 C ATOM 2666 N PHE A 258 -12.028 101.161 47.639 1.00 32.73 N ANISOU 2666 N PHE A 258 3892 3897 4647 308 -547 -79 N ATOM 2667 CA PHE A 258 -13.406 101.293 47.183 1.00 36.08 C ANISOU 2667 CA PHE A 258 4202 4239 5269 399 -756 -81 C ATOM 2668 C PHE A 258 -14.188 102.391 47.901 1.00 40.28 C ANISOU 2668 C PHE A 258 4594 4699 6010 482 -705 -92 C ATOM 2669 O PHE A 258 -15.249 102.792 47.416 1.00 40.65 O ANISOU 2669 O PHE A 258 4557 4652 6236 577 -891 -78 O ATOM 2670 CB PHE A 258 -14.171 99.982 47.367 1.00 36.81 C ANISOU 2670 CB PHE A 258 4097 4371 5518 368 -823 -122 C ATOM 2671 CG PHE A 258 -13.772 98.880 46.416 1.00 34.81 C ANISOU 2671 CG PHE A 258 3988 4141 5096 322 -962 -121 C ATOM 2672 CD1 PHE A 258 -13.896 99.039 45.041 1.00 40.10 C ANISOU 2672 CD1 PHE A 258 4867 4725 5644 380 -1213 -89 C ATOM 2673 CD2 PHE A 258 -13.310 97.668 46.911 1.00 34.45 C ANISOU 2673 CD2 PHE A 258 3894 4188 5006 233 -845 -154 C ATOM 2674 CE1 PHE A 258 -13.568 98.003 44.157 1.00 42.59 C ANISOU 2674 CE1 PHE A 258 5359 5043 5782 356 -1340 -99 C ATOM 2675 CE2 PHE A 258 -12.957 96.619 46.045 1.00 35.78 C ANISOU 2675 CE2 PHE A 258 4211 4364 5020 203 -967 -162 C ATOM 2676 CZ PHE A 258 -13.093 96.791 44.654 1.00 40.43 C ANISOU 2676 CZ PHE A 258 5025 4862 5475 268 -1213 -139 C ATOM 2677 N CYS A 259 -13.723 102.896 49.041 1.00 35.88 N ANISOU 2677 N CYS A 259 4020 4169 5446 461 -473 -120 N ATOM 2678 CA CYS A 259 -14.460 103.934 49.770 1.00 41.06 C ANISOU 2678 CA CYS A 259 4576 4742 6284 558 -399 -140 C ATOM 2679 C CYS A 259 -13.612 105.198 49.921 1.00 49.02 C ANISOU 2679 C CYS A 259 5784 5687 7154 561 -326 -127 C ATOM 2680 O CYS A 259 -13.087 105.478 51.012 1.00 45.02 O ANISOU 2680 O CYS A 259 5305 5195 6604 529 -140 -172 O ATOM 2681 CB CYS A 259 -14.916 103.435 51.144 1.00 37.27 C ANISOU 2681 CB CYS A 259 3906 4311 5943 557 -181 -198 C ATOM 2682 SG CYS A 259 -15.989 104.663 51.994 1.00 46.76 S ANISOU 2682 SG CYS A 259 4986 5392 7387 715 -58 -225 S ATOM 2683 N PRO A 260 -13.493 106.008 48.865 1.00 55.33 N ANISOU 2683 N PRO A 260 6741 6395 7888 601 -481 -64 N ATOM 2684 CA PRO A 260 -12.789 107.300 49.000 1.00 61.89 C ANISOU 2684 CA PRO A 260 7748 7133 8635 602 -418 -42 C ATOM 2685 C PRO A 260 -13.426 108.261 50.004 1.00 60.07 C ANISOU 2685 C PRO A 260 7447 6811 8566 699 -323 -97 C ATOM 2686 O PRO A 260 -12.756 109.201 50.447 1.00 65.07 O ANISOU 2686 O PRO A 260 8221 7370 9132 678 -243 -105 O ATOM 2687 CB PRO A 260 -12.835 107.871 47.575 1.00 66.45 C ANISOU 2687 CB PRO A 260 8499 7612 9137 651 -617 50 C ATOM 2688 CG PRO A 260 -14.079 107.240 46.978 1.00 66.95 C ANISOU 2688 CG PRO A 260 8421 7672 9345 739 -822 47 C ATOM 2689 CD PRO A 260 -14.093 105.838 47.532 1.00 59.31 C ANISOU 2689 CD PRO A 260 7283 6848 8405 659 -738 -11 C ATOM 2690 N ASP A 261 -14.692 108.072 50.367 1.00 56.22 N ANISOU 2690 N ASP A 261 6747 6310 8305 807 -326 -133 N ATOM 2691 CA ASP A 261 -15.344 108.893 51.383 1.00 57.95 C ANISOU 2691 CA ASP A 261 6896 6440 8680 922 -186 -189 C ATOM 2692 C ASP A 261 -15.018 108.465 52.810 1.00 52.94 C ANISOU 2692 C ASP A 261 6243 5874 7996 878 69 -268 C ATOM 2693 O ASP A 261 -15.391 109.170 53.752 1.00 55.90 O ANISOU 2693 O ASP A 261 6631 6166 8441 976 220 -325 O ATOM 2694 CB ASP A 261 -16.862 108.848 51.189 1.00 67.95 C ANISOU 2694 CB ASP A 261 7912 7653 10252 1069 -265 -182 C ATOM 2695 CG ASP A 261 -17.325 109.690 50.022 1.00 80.38 C ANISOU 2695 CG ASP A 261 9542 9098 11899 1167 -523 -116 C ATOM 2696 OD1 ASP A 261 -16.790 110.807 49.855 1.00 84.90 O ANISOU 2696 OD1 ASP A 261 10332 9567 12357 1187 -539 -96 O ATOM 2697 OD2 ASP A 261 -18.224 109.239 49.274 1.00 86.86 O ANISOU 2697 OD2 ASP A 261 10200 9906 12897 1222 -728 -82 O ATOM 2698 N CYS A 262 -14.389 107.309 52.991 1.00 50.61 N ANISOU 2698 N CYS A 262 5935 5716 7579 751 117 -275 N ATOM 2699 CA CYS A 262 -14.028 106.791 54.302 1.00 47.39 C ANISOU 2699 CA CYS A 262 5541 5371 7094 706 331 -341 C ATOM 2700 C CYS A 262 -12.673 107.346 54.716 1.00 49.01 C ANISOU 2700 C CYS A 262 5986 5553 7084 616 352 -366 C ATOM 2701 O CYS A 262 -11.762 107.461 53.890 1.00 53.92 O ANISOU 2701 O CYS A 262 6706 6185 7596 521 229 -314 O ATOM 2702 CB CYS A 262 -13.972 105.264 54.275 1.00 40.88 C ANISOU 2702 CB CYS A 262 4593 4688 6251 614 349 -329 C ATOM 2703 SG CYS A 262 -15.564 104.453 53.964 1.00 48.01 S ANISOU 2703 SG CYS A 262 5177 5603 7462 690 322 -303 S ATOM 2704 N SER A 263 -12.553 107.717 55.987 1.00 41.39 N ANISOU 2704 N SER A 263 5122 4537 6067 650 507 -443 N ATOM 2705 CA SER A 263 -11.232 107.996 56.529 1.00 39.23 C ANISOU 2705 CA SER A 263 5055 4244 5606 543 496 -478 C ATOM 2706 C SER A 263 -10.383 106.747 56.404 1.00 36.73 C ANISOU 2706 C SER A 263 4699 4074 5183 402 472 -451 C ATOM 2707 O SER A 263 -10.889 105.631 56.526 1.00 39.18 O ANISOU 2707 O SER A 263 4873 4487 5526 406 540 -447 O ATOM 2708 CB SER A 263 -11.304 108.419 57.994 1.00 43.83 C ANISOU 2708 CB SER A 263 5788 4742 6121 613 647 -579 C ATOM 2709 OG SER A 263 -11.915 109.680 58.105 1.00 57.86 O ANISOU 2709 OG SER A 263 7641 6362 7982 745 667 -610 O ATOM 2710 N HIS A 264 -9.093 106.946 56.153 1.00 37.51 N ANISOU 2710 N HIS A 264 4906 4168 5178 280 381 -429 N ATOM 2711 CA HIS A 264 -8.164 105.844 56.006 1.00 39.13 C ANISOU 2711 CA HIS A 264 5074 4496 5296 157 359 -400 C ATOM 2712 C HIS A 264 -8.053 105.126 57.347 1.00 38.44 C ANISOU 2712 C HIS A 264 5026 4451 5129 152 458 -474 C ATOM 2713 O HIS A 264 -8.116 105.762 58.398 1.00 36.19 O ANISOU 2713 O HIS A 264 4882 4071 4798 203 509 -548 O ATOM 2714 CB HIS A 264 -6.795 106.387 55.548 1.00 36.43 C ANISOU 2714 CB HIS A 264 4822 4108 4912 39 264 -354 C ATOM 2715 CG HIS A 264 -5.840 105.327 55.090 1.00 38.34 C ANISOU 2715 CG HIS A 264 4998 4467 5102 -70 247 -302 C ATOM 2716 ND1 HIS A 264 -5.276 104.412 55.956 1.00 31.73 N ANISOU 2716 ND1 HIS A 264 4149 3703 4202 -123 274 -345 N ATOM 2717 CD2 HIS A 264 -5.321 105.056 53.862 1.00 37.60 C ANISOU 2717 CD2 HIS A 264 4868 4415 5002 -123 217 -209 C ATOM 2718 CE1 HIS A 264 -4.469 103.607 55.277 1.00 35.38 C ANISOU 2718 CE1 HIS A 264 4543 4252 4647 -201 258 -283 C ATOM 2719 NE2 HIS A 264 -4.470 103.982 54.011 1.00 37.54 N ANISOU 2719 NE2 HIS A 264 4806 4508 4948 -201 239 -202 N ATOM 2720 N ALA A 265 -7.924 103.799 57.315 1.00 38.05 N ANISOU 2720 N ALA A 265 4882 4529 5046 103 485 -454 N ATOM 2721 CA ALA A 265 -7.678 103.061 58.551 1.00 37.39 C ANISOU 2721 CA ALA A 265 4867 4479 4861 90 567 -508 C ATOM 2722 C ALA A 265 -6.525 103.713 59.303 1.00 35.14 C ANISOU 2722 C ALA A 265 4768 4109 4474 32 484 -556 C ATOM 2723 O ALA A 265 -5.531 104.098 58.686 1.00 35.23 O ANISOU 2723 O ALA A 265 4776 4102 4509 -60 361 -517 O ATOM 2724 CB ALA A 265 -7.325 101.592 58.272 1.00 35.08 C ANISOU 2724 CB ALA A 265 4471 4319 4539 17 562 -468 C ATOM 2725 N PRO A 266 -6.606 103.841 60.616 1.00 38.13 N ANISOU 2725 N PRO A 266 5318 4421 4747 83 543 -636 N ATOM 2726 CA PRO A 266 -5.535 104.536 61.334 1.00 39.05 C ANISOU 2726 CA PRO A 266 5634 4426 4777 29 408 -693 C ATOM 2727 C PRO A 266 -4.251 103.718 61.317 1.00 41.32 C ANISOU 2727 C PRO A 266 5883 4782 5035 -99 278 -663 C ATOM 2728 O PRO A 266 -4.244 102.500 61.112 1.00 37.99 O ANISOU 2728 O PRO A 266 5344 4489 4602 -122 325 -621 O ATOM 2729 CB PRO A 266 -6.088 104.709 62.755 1.00 42.64 C ANISOU 2729 CB PRO A 266 6324 4790 5087 143 518 -790 C ATOM 2730 CG PRO A 266 -7.162 103.650 62.891 1.00 47.54 C ANISOU 2730 CG PRO A 266 6832 5519 5712 220 734 -760 C ATOM 2731 CD PRO A 266 -7.697 103.382 61.492 1.00 41.55 C ANISOU 2731 CD PRO A 266 5785 4860 5141 197 741 -672 C ATOM 2732 N LEU A 267 -3.150 104.436 61.524 1.00 40.38 N ANISOU 2732 N LEU A 267 5852 4558 4930 -183 102 -684 N ATOM 2733 CA LEU A 267 -1.817 103.851 61.427 1.00 45.50 C ANISOU 2733 CA LEU A 267 6424 5245 5617 -308 -43 -646 C ATOM 2734 C LEU A 267 -1.620 102.686 62.401 1.00 40.76 C ANISOU 2734 C LEU A 267 5901 4703 4882 -293 -50 -681 C ATOM 2735 O LEU A 267 -1.026 101.656 62.040 1.00 39.98 O ANISOU 2735 O LEU A 267 5659 4712 4820 -351 -72 -624 O ATOM 2736 CB LEU A 267 -0.794 104.963 61.667 1.00 51.36 C ANISOU 2736 CB LEU A 267 7254 5825 6437 -396 -244 -672 C ATOM 2737 CG LEU A 267 0.674 104.755 61.335 1.00 65.02 C ANISOU 2737 CG LEU A 267 8840 7550 8313 -542 -405 -611 C ATOM 2738 CD1 LEU A 267 1.300 106.075 60.957 1.00 68.13 C ANISOU 2738 CD1 LEU A 267 9229 7786 8872 -632 -523 -588 C ATOM 2739 CD2 LEU A 267 1.358 104.205 62.559 1.00 71.82 C ANISOU 2739 CD2 LEU A 267 9828 8372 9088 -560 -573 -680 C ATOM 2740 N TRP A 268 -2.085 102.830 63.649 1.00 35.90 N ANISOU 2740 N TRP A 268 5537 4006 4099 -205 -26 -772 N ATOM 2741 CA TRP A 268 -1.939 101.721 64.602 1.00 37.68 C ANISOU 2741 CA TRP A 268 5880 4271 4167 -180 -23 -795 C ATOM 2742 C TRP A 268 -2.631 100.458 64.093 1.00 38.34 C ANISOU 2742 C TRP A 268 5782 4518 4266 -156 168 -723 C ATOM 2743 O TRP A 268 -2.134 99.333 64.297 1.00 37.40 O ANISOU 2743 O TRP A 268 5634 4470 4106 -189 131 -694 O ATOM 2744 CB TRP A 268 -2.469 102.113 65.994 1.00 40.02 C ANISOU 2744 CB TRP A 268 6526 4437 4242 -65 24 -897 C ATOM 2745 CG TRP A 268 -3.996 102.305 66.106 1.00 41.37 C ANISOU 2745 CG TRP A 268 6735 4613 4370 76 323 -908 C ATOM 2746 CD1 TRP A 268 -4.680 103.485 66.072 1.00 46.11 C ANISOU 2746 CD1 TRP A 268 7409 5111 5000 157 400 -954 C ATOM 2747 CD2 TRP A 268 -4.991 101.278 66.311 1.00 44.37 C ANISOU 2747 CD2 TRP A 268 7065 5090 4702 152 581 -867 C ATOM 2748 NE1 TRP A 268 -6.034 103.264 66.261 1.00 43.14 N ANISOU 2748 NE1 TRP A 268 7018 4764 4609 288 696 -945 N ATOM 2749 CE2 TRP A 268 -6.248 101.916 66.380 1.00 46.18 C ANISOU 2749 CE2 TRP A 268 7313 5271 4962 277 812 -886 C ATOM 2750 CE3 TRP A 268 -4.939 99.885 66.429 1.00 50.23 C ANISOU 2750 CE3 TRP A 268 7739 5941 5405 124 639 -810 C ATOM 2751 CZ2 TRP A 268 -7.441 101.207 66.549 1.00 54.16 C ANISOU 2751 CZ2 TRP A 268 8243 6341 5996 364 1103 -843 C ATOM 2752 CZ3 TRP A 268 -6.132 99.177 66.592 1.00 52.60 C ANISOU 2752 CZ3 TRP A 268 7983 6295 5708 203 923 -768 C ATOM 2753 CH2 TRP A 268 -7.364 99.847 66.669 1.00 54.70 C ANISOU 2753 CH2 TRP A 268 8243 6511 6031 318 1155 -783 C ATOM 2754 N LEU A 269 -3.749 100.618 63.391 1.00 33.91 N ANISOU 2754 N LEU A 269 5090 4006 3786 -101 346 -693 N ATOM 2755 CA LEU A 269 -4.437 99.444 62.875 1.00 33.73 C ANISOU 2755 CA LEU A 269 4892 4115 3808 -89 491 -630 C ATOM 2756 C LEU A 269 -3.727 98.877 61.647 1.00 35.47 C ANISOU 2756 C LEU A 269 4893 4437 4147 -185 399 -556 C ATOM 2757 O LEU A 269 -3.673 97.656 61.488 1.00 33.43 O ANISOU 2757 O LEU A 269 4552 4269 3881 -205 430 -518 O ATOM 2758 CB LEU A 269 -5.896 99.792 62.578 1.00 39.42 C ANISOU 2758 CB LEU A 269 5535 4835 4609 5 681 -623 C ATOM 2759 CG LEU A 269 -6.700 98.622 62.003 1.00 45.27 C ANISOU 2759 CG LEU A 269 6073 5686 5440 6 801 -560 C ATOM 2760 CD1 LEU A 269 -6.783 97.486 63.037 1.00 42.35 C ANISOU 2760 CD1 LEU A 269 5806 5337 4950 20 908 -559 C ATOM 2761 CD2 LEU A 269 -8.096 99.077 61.560 1.00 46.83 C ANISOU 2761 CD2 LEU A 269 6140 5867 5788 90 936 -546 C ATOM 2762 N MET A 270 -3.160 99.731 60.768 1.00 32.18 N ANISOU 2762 N MET A 270 4400 3993 3834 -238 299 -530 N ATOM 2763 CA MET A 270 -2.339 99.202 59.681 1.00 34.17 C ANISOU 2763 CA MET A 270 4487 4323 4174 -317 242 -456 C ATOM 2764 C MET A 270 -1.220 98.307 60.219 1.00 36.49 C ANISOU 2764 C MET A 270 4786 4644 4435 -371 149 -452 C ATOM 2765 O MET A 270 -0.978 97.222 59.689 1.00 32.23 O ANISOU 2765 O MET A 270 4134 4197 3914 -388 177 -406 O ATOM 2766 CB MET A 270 -1.695 100.329 58.844 1.00 34.36 C ANISOU 2766 CB MET A 270 4465 4283 4306 -373 167 -417 C ATOM 2767 CG MET A 270 -2.645 101.310 58.132 1.00 32.40 C ANISOU 2767 CG MET A 270 4215 3992 4105 -320 224 -405 C ATOM 2768 SD MET A 270 -3.841 100.481 57.137 1.00 33.21 S ANISOU 2768 SD MET A 270 4196 4201 4220 -255 328 -363 S ATOM 2769 CE MET A 270 -2.783 99.553 55.977 1.00 29.54 C ANISOU 2769 CE MET A 270 3626 3827 3772 -328 306 -278 C ATOM 2770 N TYR A 271 -0.485 98.782 61.243 1.00 26.31 N ANISOU 2770 N TYR A 271 3634 3258 3106 -395 12 -504 N ATOM 2771 CA TYR A 271 0.682 98.037 61.702 1.00 32.73 C ANISOU 2771 CA TYR A 271 4433 4076 3926 -446 -126 -495 C ATOM 2772 C TYR A 271 0.270 96.788 62.461 1.00 34.17 C ANISOU 2772 C TYR A 271 4706 4313 3964 -391 -67 -510 C ATOM 2773 O TYR A 271 0.970 95.765 62.401 1.00 33.45 O ANISOU 2773 O TYR A 271 4538 4276 3897 -415 -120 -474 O ATOM 2774 CB TYR A 271 1.594 98.951 62.523 1.00 35.46 C ANISOU 2774 CB TYR A 271 4900 4277 4295 -495 -343 -547 C ATOM 2775 CG TYR A 271 2.398 99.778 61.557 1.00 44.72 C ANISOU 2775 CG TYR A 271 5896 5412 5683 -587 -404 -489 C ATOM 2776 CD1 TYR A 271 3.447 99.199 60.848 1.00 48.03 C ANISOU 2776 CD1 TYR A 271 6097 5885 6266 -653 -431 -406 C ATOM 2777 CD2 TYR A 271 2.057 101.096 61.261 1.00 49.85 C ANISOU 2777 CD2 TYR A 271 6591 5970 6380 -597 -394 -502 C ATOM 2778 CE1 TYR A 271 4.178 99.918 59.922 1.00 47.22 C ANISOU 2778 CE1 TYR A 271 5829 5742 6371 -735 -432 -331 C ATOM 2779 CE2 TYR A 271 2.788 101.834 60.323 1.00 51.04 C ANISOU 2779 CE2 TYR A 271 6587 6076 6732 -687 -420 -427 C ATOM 2780 CZ TYR A 271 3.853 101.227 59.658 1.00 51.01 C ANISOU 2780 CZ TYR A 271 6367 6126 6890 -758 -426 -337 C ATOM 2781 OH TYR A 271 4.604 101.906 58.728 1.00 46.05 O ANISOU 2781 OH TYR A 271 5582 5445 6470 -844 -405 -244 O ATOM 2782 N LEU A 272 -0.891 96.827 63.115 1.00 32.11 N ANISOU 2782 N LEU A 272 4596 4035 3571 -311 68 -552 N ATOM 2783 CA LEU A 272 -1.396 95.622 63.759 1.00 34.44 C ANISOU 2783 CA LEU A 272 4969 4373 3742 -262 171 -545 C ATOM 2784 C LEU A 272 -1.749 94.563 62.714 1.00 35.77 C ANISOU 2784 C LEU A 272 4922 4664 4006 -280 277 -476 C ATOM 2785 O LEU A 272 -1.471 93.378 62.899 1.00 32.75 O ANISOU 2785 O LEU A 272 4532 4323 3587 -286 272 -448 O ATOM 2786 CB LEU A 272 -2.609 95.975 64.631 1.00 35.97 C ANISOU 2786 CB LEU A 272 5354 4508 3805 -168 345 -590 C ATOM 2787 CG LEU A 272 -3.249 94.781 65.338 1.00 48.64 C ANISOU 2787 CG LEU A 272 7050 6138 5293 -118 504 -565 C ATOM 2788 CD1 LEU A 272 -2.242 94.208 66.337 1.00 49.13 C ANISOU 2788 CD1 LEU A 272 7321 6149 5199 -124 339 -580 C ATOM 2789 CD2 LEU A 272 -4.577 95.201 66.030 1.00 53.86 C ANISOU 2789 CD2 LEU A 272 7849 6739 5875 -16 750 -589 C ATOM 2790 N ALA A 273 -2.347 94.978 61.597 1.00 30.69 N ANISOU 2790 N ALA A 273 4123 4061 3475 -284 351 -451 N ATOM 2791 CA ALA A 273 -2.639 94.034 60.521 1.00 30.54 C ANISOU 2791 CA ALA A 273 3934 4135 3534 -299 409 -397 C ATOM 2792 C ALA A 273 -1.356 93.495 59.896 1.00 30.40 C ANISOU 2792 C ALA A 273 3826 4158 3567 -351 305 -359 C ATOM 2793 O ALA A 273 -1.317 92.345 59.468 1.00 29.04 O ANISOU 2793 O ALA A 273 3589 4044 3402 -352 332 -329 O ATOM 2794 CB ALA A 273 -3.503 94.694 59.438 1.00 27.06 C ANISOU 2794 CB ALA A 273 3384 3706 3190 -283 465 -382 C ATOM 2795 N ILE A 274 -0.319 94.331 59.773 1.00 30.07 N ANISOU 2795 N ILE A 274 3766 4074 3584 -393 196 -356 N ATOM 2796 CA ILE A 274 0.947 93.861 59.222 1.00 29.04 C ANISOU 2796 CA ILE A 274 3520 3970 3544 -434 127 -308 C ATOM 2797 C ILE A 274 1.578 92.811 60.155 1.00 30.71 C ANISOU 2797 C ILE A 274 3781 4181 3707 -427 45 -318 C ATOM 2798 O ILE A 274 2.039 91.762 59.704 1.00 32.14 O ANISOU 2798 O ILE A 274 3876 4414 3923 -420 60 -280 O ATOM 2799 CB ILE A 274 1.889 95.061 58.977 1.00 33.32 C ANISOU 2799 CB ILE A 274 4009 4444 4208 -492 38 -291 C ATOM 2800 CG1 ILE A 274 1.368 95.958 57.816 1.00 33.88 C ANISOU 2800 CG1 ILE A 274 4032 4514 4326 -493 131 -257 C ATOM 2801 CG2 ILE A 274 3.347 94.595 58.748 1.00 31.81 C ANISOU 2801 CG2 ILE A 274 3679 4253 4153 -534 -37 -239 C ATOM 2802 CD1 ILE A 274 2.090 97.302 57.718 1.00 30.78 C ANISOU 2802 CD1 ILE A 274 3620 4025 4051 -555 58 -239 C ATOM 2803 N AVAL A 275 1.618 93.103 61.461 0.50 29.82 N ANISOU 2803 N AVAL A 275 3835 3994 3500 -417 -51 -369 N ATOM 2804 N BVAL A 275 1.620 93.081 61.464 0.50 29.88 N ANISOU 2804 N BVAL A 275 3843 4003 3507 -417 -51 -368 N ATOM 2805 CA AVAL A 275 2.148 92.162 62.451 0.50 30.77 C ANISOU 2805 CA AVAL A 275 4056 4092 3541 -398 -154 -377 C ATOM 2806 CA BVAL A 275 2.221 92.093 62.365 0.50 30.61 C ANISOU 2806 CA BVAL A 275 4017 4078 3534 -401 -155 -371 C ATOM 2807 C AVAL A 275 1.378 90.846 62.415 0.50 31.22 C ANISOU 2807 C AVAL A 275 4134 4215 3515 -357 -15 -353 C ATOM 2808 C BVAL A 275 1.381 90.818 62.422 0.50 31.17 C ANISOU 2808 C BVAL A 275 4128 4209 3507 -356 -15 -353 C ATOM 2809 O AVAL A 275 1.968 89.761 62.473 0.50 29.49 O ANISOU 2809 O AVAL A 275 3886 4014 3305 -348 -63 -324 O ATOM 2810 O BVAL A 275 1.931 89.720 62.543 0.50 28.82 O ANISOU 2810 O BVAL A 275 3813 3927 3210 -345 -61 -325 O ATOM 2811 CB AVAL A 275 2.113 92.800 63.855 0.50 32.14 C ANISOU 2811 CB AVAL A 275 4482 4155 3573 -377 -272 -443 C ATOM 2812 CB BVAL A 275 2.466 92.674 63.775 0.50 32.60 C ANISOU 2812 CB BVAL A 275 4502 4217 3669 -389 -315 -433 C ATOM 2813 CG1AVAL A 275 2.262 91.732 64.946 0.50 26.86 C ANISOU 2813 CG1AVAL A 275 3997 3458 2751 -331 -335 -447 C ATOM 2814 CG1BVAL A 275 3.445 93.856 63.726 0.50 31.31 C ANISOU 2814 CG1BVAL A 275 4282 3968 3646 -452 -504 -450 C ATOM 2815 CG2AVAL A 275 3.205 93.865 63.982 0.50 31.46 C ANISOU 2815 CG2AVAL A 275 4369 3978 3608 -436 -492 -465 C ATOM 2816 CG2BVAL A 275 1.173 93.046 64.457 0.50 31.83 C ANISOU 2816 CG2BVAL A 275 4614 4087 3394 -331 -171 -479 C ATOM 2817 N LEU A 276 0.052 90.919 62.302 1.00 30.94 N ANISOU 2817 N LEU A 276 4132 4200 3424 -332 155 -362 N ATOM 2818 CA LEU A 276 -0.766 89.702 62.246 1.00 31.86 C ANISOU 2818 CA LEU A 276 4245 4357 3502 -310 286 -333 C ATOM 2819 C LEU A 276 -0.407 88.836 61.035 1.00 36.03 C ANISOU 2819 C LEU A 276 4602 4954 4136 -329 286 -293 C ATOM 2820 O LEU A 276 -0.246 87.611 61.161 1.00 33.19 O ANISOU 2820 O LEU A 276 4256 4603 3753 -318 288 -269 O ATOM 2821 CB LEU A 276 -2.255 90.068 62.231 1.00 33.78 C ANISOU 2821 CB LEU A 276 4497 4598 3741 -288 460 -342 C ATOM 2822 CG LEU A 276 -3.273 88.910 62.140 1.00 41.89 C ANISOU 2822 CG LEU A 276 5484 5646 4787 -283 602 -306 C ATOM 2823 CD1 LEU A 276 -3.187 87.926 63.335 1.00 40.94 C ANISOU 2823 CD1 LEU A 276 5538 5480 4536 -263 639 -285 C ATOM 2824 CD2 LEU A 276 -4.699 89.443 62.038 1.00 47.67 C ANISOU 2824 CD2 LEU A 276 6160 6364 5587 -262 759 -309 C ATOM 2825 N SER A 277 -0.246 89.450 59.854 1.00 32.31 N ANISOU 2825 N SER A 277 3998 4516 3764 -347 289 -284 N ATOM 2826 CA SER A 277 0.136 88.675 58.678 1.00 29.09 C ANISOU 2826 CA SER A 277 3478 4155 3420 -345 304 -251 C ATOM 2827 C SER A 277 1.485 88.002 58.904 1.00 30.50 C ANISOU 2827 C SER A 277 3628 4328 3631 -337 219 -229 C ATOM 2828 O SER A 277 1.698 86.870 58.461 1.00 31.35 O ANISOU 2828 O SER A 277 3707 4456 3747 -312 241 -210 O ATOM 2829 CB SER A 277 0.181 89.566 57.401 1.00 27.17 C ANISOU 2829 CB SER A 277 3147 3930 3246 -353 332 -235 C ATOM 2830 OG SER A 277 1.339 90.402 57.359 1.00 27.35 O ANISOU 2830 OG SER A 277 3118 3930 3343 -378 273 -216 O ATOM 2831 N HIS A 278 2.420 88.688 59.586 1.00 27.85 N ANISOU 2831 N HIS A 278 3296 3951 3333 -355 102 -234 N ATOM 2832 CA HIS A 278 3.731 88.076 59.828 1.00 26.67 C ANISOU 2832 CA HIS A 278 3085 3784 3264 -344 -8 -208 C ATOM 2833 C HIS A 278 3.644 86.929 60.831 1.00 31.49 C ANISOU 2833 C HIS A 278 3825 4370 3770 -308 -64 -214 C ATOM 2834 O HIS A 278 4.448 85.981 60.755 1.00 30.39 O ANISOU 2834 O HIS A 278 3629 4227 3690 -275 -114 -186 O ATOM 2835 CB HIS A 278 4.727 89.115 60.368 1.00 26.89 C ANISOU 2835 CB HIS A 278 3075 3748 3394 -383 -168 -213 C ATOM 2836 CG HIS A 278 5.040 90.191 59.385 1.00 29.90 C ANISOU 2836 CG HIS A 278 3316 4132 3911 -426 -112 -185 C ATOM 2837 ND1 HIS A 278 5.767 91.314 59.715 1.00 31.21 N ANISOU 2837 ND1 HIS A 278 3435 4226 4199 -483 -239 -186 N ATOM 2838 CD2 HIS A 278 4.769 90.289 58.059 1.00 32.79 C ANISOU 2838 CD2 HIS A 278 3599 4550 4310 -419 51 -149 C ATOM 2839 CE1 HIS A 278 5.907 92.075 58.635 1.00 32.14 C ANISOU 2839 CE1 HIS A 278 3433 4352 4426 -514 -130 -142 C ATOM 2840 NE2 HIS A 278 5.312 91.478 57.620 1.00 31.30 N ANISOU 2840 NE2 HIS A 278 3318 4322 4252 -469 48 -119 N ATOM 2841 N THR A 279 2.735 87.023 61.814 1.00 31.31 N ANISOU 2841 N THR A 279 3985 4315 3595 -305 -46 -244 N ATOM 2842 CA THR A 279 2.609 85.930 62.787 1.00 34.27 C ANISOU 2842 CA THR A 279 4520 4652 3849 -269 -73 -234 C ATOM 2843 C THR A 279 2.194 84.622 62.121 1.00 31.57 C ANISOU 2843 C THR A 279 4126 4346 3524 -253 39 -201 C ATOM 2844 O THR A 279 2.408 83.551 62.701 1.00 34.23 O ANISOU 2844 O THR A 279 4556 4645 3805 -222 0 -178 O ATOM 2845 CB THR A 279 1.608 86.253 63.910 1.00 36.40 C ANISOU 2845 CB THR A 279 5017 4871 3942 -258 -7 -258 C ATOM 2846 OG1 THR A 279 0.274 86.223 63.399 1.00 49.62 O ANISOU 2846 OG1 THR A 279 6649 6585 5619 -271 198 -253 O ATOM 2847 CG2 THR A 279 1.895 87.598 64.509 1.00 30.14 C ANISOU 2847 CG2 THR A 279 4313 4026 3114 -267 -115 -305 C ATOM 2848 N ASN A 280 1.635 84.676 60.908 1.00 30.32 N ANISOU 2848 N ASN A 280 3842 4243 3435 -270 155 -202 N ATOM 2849 CA ASN A 280 1.336 83.430 60.205 1.00 33.18 C ANISOU 2849 CA ASN A 280 4173 4617 3818 -254 220 -183 C ATOM 2850 C ASN A 280 2.584 82.577 60.001 1.00 34.30 C ANISOU 2850 C ASN A 280 4266 4748 4020 -206 140 -161 C ATOM 2851 O ASN A 280 2.492 81.346 59.932 1.00 34.76 O ANISOU 2851 O ASN A 280 4367 4780 4061 -179 157 -147 O ATOM 2852 CB ASN A 280 0.702 83.688 58.839 1.00 33.80 C ANISOU 2852 CB ASN A 280 4152 4738 3953 -269 305 -195 C ATOM 2853 CG ASN A 280 0.251 82.388 58.179 1.00 33.40 C ANISOU 2853 CG ASN A 280 4111 4671 3909 -257 343 -191 C ATOM 2854 OD1 ASN A 280 -0.649 81.696 58.689 1.00 37.45 O ANISOU 2854 OD1 ASN A 280 4688 5145 4395 -281 381 -183 O ATOM 2855 ND2 ASN A 280 0.912 82.024 57.104 1.00 29.01 N ANISOU 2855 ND2 ASN A 280 3505 4127 3389 -216 341 -192 N ATOM 2856 N SER A 281 3.743 83.197 59.885 1.00 29.13 N ANISOU 2856 N SER A 281 3508 4099 3460 -194 56 -154 N ATOM 2857 CA SER A 281 4.978 82.443 59.689 1.00 30.47 C ANISOU 2857 CA SER A 281 3590 4251 3735 -136 -8 -125 C ATOM 2858 C SER A 281 5.487 81.766 60.958 1.00 34.04 C ANISOU 2858 C SER A 281 4148 4637 4149 -104 -164 -112 C ATOM 2859 O SER A 281 6.547 81.135 60.905 1.00 33.10 O ANISOU 2859 O SER A 281 3943 4490 4142 -45 -244 -85 O ATOM 2860 CB SER A 281 6.079 83.352 59.104 1.00 30.47 C ANISOU 2860 CB SER A 281 3403 4266 3908 -139 -29 -106 C ATOM 2861 OG SER A 281 5.655 83.850 57.825 1.00 32.72 O ANISOU 2861 OG SER A 281 3629 4600 4204 -151 129 -106 O ATOM 2862 N VAL A 282 4.770 81.873 62.085 1.00 31.82 N ANISOU 2862 N VAL A 282 4061 4319 3711 -128 -201 -124 N ATOM 2863 CA VAL A 282 5.178 81.228 63.335 1.00 34.85 C ANISOU 2863 CA VAL A 282 4611 4622 4008 -88 -352 -105 C ATOM 2864 C VAL A 282 4.321 79.989 63.589 1.00 35.64 C ANISOU 2864 C VAL A 282 4865 4690 3986 -73 -246 -79 C ATOM 2865 O VAL A 282 4.752 79.056 64.280 1.00 35.00 O ANISOU 2865 O VAL A 282 4903 4538 3857 -21 -346 -46 O ATOM 2866 CB VAL A 282 5.048 82.204 64.531 1.00 35.82 C ANISOU 2866 CB VAL A 282 4911 4695 4004 -111 -465 -132 C ATOM 2867 CG1 VAL A 282 5.409 81.516 65.882 1.00 37.47 C ANISOU 2867 CG1 VAL A 282 5368 4800 4070 -56 -636 -110 C ATOM 2868 CG2 VAL A 282 5.866 83.472 64.313 1.00 31.75 C ANISOU 2868 CG2 VAL A 282 4247 4187 3631 -143 -592 -158 C ATOM 2869 N VAL A 283 3.088 79.978 63.070 1.00 32.51 N ANISOU 2869 N VAL A 283 4469 4330 3555 -120 -57 -88 N ATOM 2870 CA VAL A 283 2.091 79.051 63.629 1.00 35.39 C ANISOU 2870 CA VAL A 283 4998 4638 3810 -132 49 -54 C ATOM 2871 C VAL A 283 2.178 77.608 63.069 1.00 30.82 C ANISOU 2871 C VAL A 283 4399 4024 3288 -107 68 -28 C ATOM 2872 O VAL A 283 1.862 76.657 63.794 1.00 37.72 O ANISOU 2872 O VAL A 283 5435 4815 4080 -99 87 18 O ATOM 2873 CB VAL A 283 0.655 79.606 63.462 1.00 40.16 C ANISOU 2873 CB VAL A 283 5595 5268 4394 -197 233 -65 C ATOM 2874 CG1 VAL A 283 0.507 80.967 64.117 1.00 42.59 C ANISOU 2874 CG1 VAL A 283 5964 5588 4628 -205 230 -94 C ATOM 2875 CG2 VAL A 283 0.233 79.650 62.011 1.00 37.47 C ANISOU 2875 CG2 VAL A 283 5062 4988 4186 -229 299 -92 C ATOM 2876 N ASN A 284 2.575 77.400 61.812 1.00 29.55 N ANISOU 2876 N ASN A 284 4073 3905 3250 -88 74 -53 N ATOM 2877 CA ASN A 284 2.519 76.043 61.253 1.00 31.64 C ANISOU 2877 CA ASN A 284 4355 4116 3550 -59 100 -41 C ATOM 2878 C ASN A 284 3.308 75.014 62.057 1.00 32.50 C ANISOU 2878 C ASN A 284 4579 4138 3630 12 -9 2 C ATOM 2879 O ASN A 284 2.761 73.928 62.311 1.00 33.83 O ANISOU 2879 O ASN A 284 4872 4222 3759 2 31 35 O ATOM 2880 CB ASN A 284 2.964 76.030 59.782 1.00 30.09 C ANISOU 2880 CB ASN A 284 4011 3964 3457 -21 127 -81 C ATOM 2881 CG ASN A 284 2.026 76.833 58.895 1.00 38.35 C ANISOU 2881 CG ASN A 284 4989 5070 4513 -85 218 -119 C ATOM 2882 OD1 ASN A 284 0.900 77.164 59.317 1.00 37.03 O ANISOU 2882 OD1 ASN A 284 4860 4901 4310 -161 269 -115 O ATOM 2883 ND2 ASN A 284 2.467 77.143 57.674 1.00 36.14 N ANISOU 2883 ND2 ASN A 284 4616 4832 4285 -46 247 -148 N ATOM 2884 N PRO A 285 4.556 75.267 62.493 1.00 32.84 N ANISOU 2884 N PRO A 285 4587 4180 3713 81 -159 11 N ATOM 2885 CA PRO A 285 5.236 74.268 63.349 1.00 33.81 C ANISOU 2885 CA PRO A 285 4840 4202 3805 158 -295 59 C ATOM 2886 C PRO A 285 4.397 73.825 64.553 1.00 35.46 C ANISOU 2886 C PRO A 285 5317 4326 3830 122 -272 108 C ATOM 2887 O PRO A 285 4.486 72.660 64.949 1.00 33.88 O ANISOU 2887 O PRO A 285 5256 4025 3593 166 -305 156 O ATOM 2888 CB PRO A 285 6.518 74.998 63.789 1.00 35.98 C ANISOU 2888 CB PRO A 285 5021 4487 4161 211 -492 57 C ATOM 2889 CG PRO A 285 6.810 75.971 62.620 1.00 33.87 C ANISOU 2889 CG PRO A 285 4498 4325 4044 187 -412 14 C ATOM 2890 CD PRO A 285 5.415 76.442 62.243 1.00 32.67 C ANISOU 2890 CD PRO A 285 4396 4228 3788 91 -232 -14 C ATOM 2891 N PHE A 286 3.574 74.710 65.142 1.00 35.16 N ANISOU 2891 N PHE A 286 5368 4314 3676 53 -193 105 N ATOM 2892 CA PHE A 286 2.758 74.297 66.293 1.00 38.94 C ANISOU 2892 CA PHE A 286 6120 4702 3975 31 -114 166 C ATOM 2893 C PHE A 286 1.633 73.364 65.872 1.00 34.79 C ANISOU 2893 C PHE A 286 5602 4133 3486 -33 82 201 C ATOM 2894 O PHE A 286 1.286 72.437 66.622 1.00 36.91 O ANISOU 2894 O PHE A 286 6075 4287 3663 -31 130 276 O ATOM 2895 CB PHE A 286 2.178 75.516 67.023 1.00 33.54 C ANISOU 2895 CB PHE A 286 5539 4045 3161 -7 -48 150 C ATOM 2896 CG PHE A 286 3.195 76.249 67.820 1.00 42.56 C ANISOU 2896 CG PHE A 286 6782 5169 4221 53 -278 128 C ATOM 2897 CD1 PHE A 286 4.008 77.203 67.214 1.00 44.30 C ANISOU 2897 CD1 PHE A 286 6780 5469 4582 53 -411 65 C ATOM 2898 CD2 PHE A 286 3.379 75.959 69.154 1.00 41.39 C ANISOU 2898 CD2 PHE A 286 6959 4905 3861 109 -377 173 C ATOM 2899 CE1 PHE A 286 4.974 77.873 67.955 1.00 45.71 C ANISOU 2899 CE1 PHE A 286 7033 5607 4726 94 -662 43 C ATOM 2900 CE2 PHE A 286 4.342 76.617 69.891 1.00 46.78 C ANISOU 2900 CE2 PHE A 286 7754 5548 4473 164 -647 144 C ATOM 2901 CZ PHE A 286 5.140 77.577 69.289 1.00 45.05 C ANISOU 2901 CZ PHE A 286 7281 5405 4432 150 -801 76 C ATOM 2902 N ILE A 287 1.033 73.620 64.694 1.00 35.26 N ANISOU 2902 N ILE A 287 5451 4265 3681 -94 184 152 N ATOM 2903 CA ILE A 287 -0.010 72.737 64.170 1.00 37.41 C ANISOU 2903 CA ILE A 287 5701 4480 4033 -165 317 174 C ATOM 2904 C ILE A 287 0.564 71.357 63.880 1.00 39.18 C ANISOU 2904 C ILE A 287 5978 4611 4300 -113 233 193 C ATOM 2905 O ILE A 287 -0.027 70.332 64.248 1.00 40.58 O ANISOU 2905 O ILE A 287 6281 4668 4470 -150 300 256 O ATOM 2906 CB ILE A 287 -0.669 73.344 62.920 1.00 38.70 C ANISOU 2906 CB ILE A 287 5650 4728 4328 -226 379 108 C ATOM 2907 CG1 ILE A 287 -1.293 74.711 63.241 1.00 42.47 C ANISOU 2907 CG1 ILE A 287 6078 5283 4775 -269 467 94 C ATOM 2908 CG2 ILE A 287 -1.709 72.370 62.327 1.00 37.67 C ANISOU 2908 CG2 ILE A 287 5491 4512 4310 -304 456 122 C ATOM 2909 CD1 ILE A 287 -2.439 74.619 64.199 1.00 48.84 C ANISOU 2909 CD1 ILE A 287 6996 6020 5540 -327 645 163 C ATOM 2910 N TYR A 288 1.732 71.299 63.228 1.00 34.89 N ANISOU 2910 N TYR A 288 5337 4105 3813 -21 99 145 N ATOM 2911 CA TYR A 288 2.345 69.984 63.014 1.00 35.60 C ANISOU 2911 CA TYR A 288 5490 4093 3944 54 23 161 C ATOM 2912 C TYR A 288 2.617 69.277 64.342 1.00 36.71 C ANISOU 2912 C TYR A 288 5860 4116 3970 95 -43 249 C ATOM 2913 O TYR A 288 2.396 68.068 64.455 1.00 38.01 O ANISOU 2913 O TYR A 288 6151 4153 4140 99 -30 296 O ATOM 2914 CB TYR A 288 3.646 70.081 62.207 1.00 35.54 C ANISOU 2914 CB TYR A 288 5333 4139 4032 170 -80 108 C ATOM 2915 CG TYR A 288 3.530 70.823 60.893 1.00 35.42 C ANISOU 2915 CG TYR A 288 5133 4230 4096 151 -8 32 C ATOM 2916 CD1 TYR A 288 2.393 70.695 60.089 1.00 35.72 C ANISOU 2916 CD1 TYR A 288 5164 4260 4149 66 89 -3 C ATOM 2917 CD2 TYR A 288 4.543 71.673 60.473 1.00 37.24 C ANISOU 2917 CD2 TYR A 288 5202 4553 4394 217 -46 3 C ATOM 2918 CE1 TYR A 288 2.286 71.397 58.884 1.00 42.01 C ANISOU 2918 CE1 TYR A 288 5834 5139 4988 60 133 -70 C ATOM 2919 CE2 TYR A 288 4.443 72.390 59.267 1.00 34.18 C ANISOU 2919 CE2 TYR A 288 4679 4252 4057 205 40 -52 C ATOM 2920 CZ TYR A 288 3.307 72.251 58.494 1.00 37.10 C ANISOU 2920 CZ TYR A 288 5085 4613 4400 132 123 -90 C ATOM 2921 OH TYR A 288 3.182 72.955 57.332 1.00 34.35 O ANISOU 2921 OH TYR A 288 4648 4334 4071 130 185 -141 O ATOM 2922 N ALA A 289 3.093 70.012 65.359 1.00 38.20 N ANISOU 2922 N ALA A 289 6136 4331 4048 129 -129 273 N ATOM 2923 CA ALA A 289 3.436 69.367 66.629 1.00 38.10 C ANISOU 2923 CA ALA A 289 6390 4192 3893 188 -226 357 C ATOM 2924 C ALA A 289 2.191 68.849 67.334 1.00 40.64 C ANISOU 2924 C ALA A 289 6928 4413 4099 102 -36 441 C ATOM 2925 O ALA A 289 2.219 67.773 67.934 1.00 43.50 O ANISOU 2925 O ALA A 289 7501 4632 4395 133 -52 523 O ATOM 2926 CB ALA A 289 4.183 70.331 67.562 1.00 37.74 C ANISOU 2926 CB ALA A 289 6425 4177 3736 243 -395 353 C ATOM 2927 N TYR A 290 1.085 69.600 67.276 1.00 39.58 N ANISOU 2927 N TYR A 290 6739 4341 3960 -3 159 432 N ATOM 2928 CA TYR A 290 -0.086 69.161 68.027 1.00 42.17 C ANISOU 2928 CA TYR A 290 7251 4564 4209 -81 378 530 C ATOM 2929 C TYR A 290 -0.881 68.109 67.280 1.00 45.32 C ANISOU 2929 C TYR A 290 7556 4880 4781 -170 490 555 C ATOM 2930 O TYR A 290 -1.485 67.254 67.916 1.00 46.08 O ANISOU 2930 O TYR A 290 7830 4833 4845 -213 616 661 O ATOM 2931 CB TYR A 290 -0.988 70.348 68.376 1.00 45.42 C ANISOU 2931 CB TYR A 290 7640 5049 4566 -144 562 523 C ATOM 2932 CG TYR A 290 -0.533 71.015 69.638 1.00 55.91 C ANISOU 2932 CG TYR A 290 9237 6361 5645 -65 506 546 C ATOM 2933 CD1 TYR A 290 -0.860 70.475 70.880 1.00 66.30 C ANISOU 2933 CD1 TYR A 290 10903 7533 6756 -40 617 660 C ATOM 2934 CD2 TYR A 290 0.261 72.154 69.605 1.00 62.92 C ANISOU 2934 CD2 TYR A 290 10060 7354 6494 -11 329 457 C ATOM 2935 CE1 TYR A 290 -0.431 71.062 72.047 1.00 70.36 C ANISOU 2935 CE1 TYR A 290 11725 8008 7000 47 541 674 C ATOM 2936 CE2 TYR A 290 0.692 72.758 70.777 1.00 72.02 C ANISOU 2936 CE2 TYR A 290 11490 8464 7410 61 233 467 C ATOM 2937 CZ TYR A 290 0.343 72.204 71.998 1.00 76.35 C ANISOU 2937 CZ TYR A 290 12417 8868 7724 97 330 570 C ATOM 2938 OH TYR A 290 0.768 72.782 73.182 1.00 83.04 O ANISOU 2938 OH TYR A 290 13605 9651 8296 184 213 573 O ATOM 2939 N ARG A 291 -0.878 68.129 65.942 1.00 41.69 N ANISOU 2939 N ARG A 291 6847 4492 4503 -196 439 463 N ATOM 2940 CA ARG A 291 -1.822 67.316 65.189 1.00 45.35 C ANISOU 2940 CA ARG A 291 7221 4870 5139 -300 527 469 C ATOM 2941 C ARG A 291 -1.220 66.103 64.494 1.00 46.68 C ANISOU 2941 C ARG A 291 7413 4940 5383 -248 389 443 C ATOM 2942 O ARG A 291 -1.984 65.228 64.080 1.00 49.46 O ANISOU 2942 O ARG A 291 7760 5171 5864 -336 437 462 O ATOM 2943 CB ARG A 291 -2.521 68.166 64.117 1.00 43.08 C ANISOU 2943 CB ARG A 291 6677 4697 4996 -376 568 382 C ATOM 2944 CG ARG A 291 -3.229 69.414 64.629 1.00 49.52 C ANISOU 2944 CG ARG A 291 7434 5605 5777 -424 714 395 C ATOM 2945 CD ARG A 291 -4.704 69.174 64.887 1.00 55.43 C ANISOU 2945 CD ARG A 291 8140 6264 6658 -555 927 473 C ATOM 2946 NE ARG A 291 -5.318 68.290 63.905 1.00 61.39 N ANISOU 2946 NE ARG A 291 8769 6926 7633 -645 884 455 N ATOM 2947 CZ ARG A 291 -6.571 67.847 63.991 1.00 65.71 C ANISOU 2947 CZ ARG A 291 9239 7358 8372 -776 1030 528 C ATOM 2948 NH1 ARG A 291 -7.320 68.222 65.014 1.00 65.38 N ANISOU 2948 NH1 ARG A 291 9231 7291 8320 -818 1274 631 N ATOM 2949 NH2 ARG A 291 -7.076 67.033 63.061 1.00 61.33 N ANISOU 2949 NH2 ARG A 291 8577 6697 8027 -863 934 499 N ATOM 2950 N ILE A 292 0.100 66.033 64.308 1.00 44.99 N ANISOU 2950 N ILE A 292 7209 4764 5121 -108 220 396 N ATOM 2951 CA ILE A 292 0.701 64.988 63.472 1.00 46.81 C ANISOU 2951 CA ILE A 292 7438 4910 5436 -34 111 351 C ATOM 2952 C ILE A 292 1.768 64.274 64.286 1.00 46.56 C ANISOU 2952 C ILE A 292 7584 4787 5321 98 -13 412 C ATOM 2953 O ILE A 292 2.836 64.845 64.555 1.00 44.64 O ANISOU 2953 O ILE A 292 7302 4629 5032 210 -131 394 O ATOM 2954 CB ILE A 292 1.303 65.529 62.162 1.00 48.19 C ANISOU 2954 CB ILE A 292 7416 5207 5686 33 48 228 C ATOM 2955 CG1 ILE A 292 0.310 66.367 61.365 1.00 44.42 C ANISOU 2955 CG1 ILE A 292 6782 4824 5273 -82 134 168 C ATOM 2956 CG2 ILE A 292 1.772 64.348 61.259 1.00 44.70 C ANISOU 2956 CG2 ILE A 292 7017 4648 5319 118 -24 178 C ATOM 2957 CD1 ILE A 292 0.943 66.987 60.118 1.00 41.64 C ANISOU 2957 CD1 ILE A 292 6281 4587 4955 -5 89 60 C ATOM 2958 N ARG A 293 1.507 63.007 64.631 1.00 44.46 N ANISOU 2958 N ARG A 293 7501 4333 5059 86 -6 485 N ATOM 2959 CA ARG A 293 2.340 62.307 65.607 1.00 49.63 C ANISOU 2959 CA ARG A 293 8371 4873 5613 203 -122 569 C ATOM 2960 C ARG A 293 3.792 62.184 65.147 1.00 47.46 C ANISOU 2960 C ARG A 293 8007 4631 5394 387 -311 504 C ATOM 2961 O ARG A 293 4.723 62.346 65.952 1.00 43.58 O ANISOU 2961 O ARG A 293 7588 4140 4831 500 -459 545 O ATOM 2962 CB ARG A 293 1.755 60.919 65.904 1.00 54.07 C ANISOU 2962 CB ARG A 293 9142 5209 6195 152 -70 661 C ATOM 2963 CG ARG A 293 2.569 60.109 66.930 1.00 63.96 C ANISOU 2963 CG ARG A 293 10657 6314 7329 280 -200 762 C ATOM 2964 CD ARG A 293 1.837 58.828 67.361 1.00 79.95 C ANISOU 2964 CD ARG A 293 12917 8100 9359 203 -110 879 C ATOM 2965 NE ARG A 293 0.650 59.142 68.157 1.00 92.51 N ANISOU 2965 NE ARG A 293 14610 9665 10874 45 115 987 N ATOM 2966 CZ ARG A 293 0.593 59.055 69.482 1.00103.04 C ANISOU 2966 CZ ARG A 293 16233 10909 12008 64 171 1126 C ATOM 2967 NH1 ARG A 293 -0.524 59.373 70.123 1.00106.05 N ANISOU 2967 NH1 ARG A 293 16693 11265 12335 -70 430 1224 N ATOM 2968 NH2 ARG A 293 1.650 58.635 70.167 1.00107.64 N ANISOU 2968 NH2 ARG A 293 17037 11412 12449 228 -28 1173 N ATOM 2969 N GLU A 294 4.009 61.893 63.864 1.00 48.78 N ANISOU 2969 N GLU A 294 8026 4813 5697 427 -310 406 N ATOM 2970 CA GLU A 294 5.374 61.685 63.383 1.00 52.17 C ANISOU 2970 CA GLU A 294 8359 5253 6209 616 -437 355 C ATOM 2971 C GLU A 294 6.211 62.966 63.478 1.00 47.03 C ANISOU 2971 C GLU A 294 7512 4783 5575 674 -500 325 C ATOM 2972 O GLU A 294 7.406 62.900 63.797 1.00 44.09 O ANISOU 2972 O GLU A 294 7094 4399 5261 822 -650 342 O ATOM 2973 CB GLU A 294 5.350 61.142 61.954 1.00 54.08 C ANISOU 2973 CB GLU A 294 8525 5461 6561 655 -381 253 C ATOM 2974 CG GLU A 294 6.686 60.592 61.478 1.00 60.55 C ANISOU 2974 CG GLU A 294 9290 6234 7480 873 -462 216 C ATOM 2975 CD GLU A 294 7.059 59.273 62.128 1.00 67.70 C ANISOU 2975 CD GLU A 294 10402 6931 8389 970 -569 289 C ATOM 2976 OE1 GLU A 294 8.262 58.943 62.158 1.00 66.59 O ANISOU 2976 OE1 GLU A 294 10208 6755 8339 1162 -670 293 O ATOM 2977 OE2 GLU A 294 6.148 58.558 62.599 1.00 70.80 O ANISOU 2977 OE2 GLU A 294 11001 7185 8715 857 -548 349 O ATOM 2978 N PHE A 295 5.608 64.141 63.236 1.00 44.29 N ANISOU 2978 N PHE A 295 7040 4588 5200 558 -403 285 N ATOM 2979 CA PHE A 295 6.323 65.400 63.483 1.00 42.16 C ANISOU 2979 CA PHE A 295 6612 4465 4942 589 -474 269 C ATOM 2980 C PHE A 295 6.603 65.598 64.966 1.00 44.10 C ANISOU 2980 C PHE A 295 7023 4669 5065 604 -616 351 C ATOM 2981 O PHE A 295 7.723 65.955 65.358 1.00 46.99 O ANISOU 2981 O PHE A 295 7316 5054 5485 707 -798 358 O ATOM 2982 CB PHE A 295 5.532 66.596 62.947 1.00 42.25 C ANISOU 2982 CB PHE A 295 6489 4627 4938 461 -340 213 C ATOM 2983 CG PHE A 295 5.815 66.914 61.496 1.00 42.64 C ANISOU 2983 CG PHE A 295 6335 4762 5105 498 -265 124 C ATOM 2984 CD1 PHE A 295 7.040 67.425 61.116 1.00 44.69 C ANISOU 2984 CD1 PHE A 295 6407 5093 5480 612 -316 100 C ATOM 2985 CD2 PHE A 295 4.856 66.692 60.518 1.00 42.33 C ANISOU 2985 CD2 PHE A 295 6303 4713 5067 421 -146 70 C ATOM 2986 CE1 PHE A 295 7.313 67.720 59.771 1.00 47.38 C ANISOU 2986 CE1 PHE A 295 6595 5501 5909 657 -204 31 C ATOM 2987 CE2 PHE A 295 5.115 66.988 59.177 1.00 46.13 C ANISOU 2987 CE2 PHE A 295 6658 5256 5611 470 -78 -12 C ATOM 2988 CZ PHE A 295 6.343 67.500 58.803 1.00 46.17 C ANISOU 2988 CZ PHE A 295 6503 5337 5702 592 -85 -27 C ATOM 2989 N ARG A 296 5.582 65.396 65.806 1.00 41.84 N ANISOU 2989 N ARG A 296 6966 4313 4617 501 -537 419 N ATOM 2990 CA ARG A 296 5.733 65.591 67.242 1.00 45.54 C ANISOU 2990 CA ARG A 296 7669 4724 4910 521 -648 500 C ATOM 2991 C ARG A 296 6.834 64.705 67.796 1.00 47.55 C ANISOU 2991 C ARG A 296 8046 4845 5176 677 -880 552 C ATOM 2992 O ARG A 296 7.681 65.156 68.579 1.00 45.12 O ANISOU 2992 O ARG A 296 7788 4532 4823 759 -1102 570 O ATOM 2993 CB ARG A 296 4.397 65.309 67.933 1.00 49.29 C ANISOU 2993 CB ARG A 296 8386 5118 5224 398 -455 580 C ATOM 2994 CG ARG A 296 4.443 65.303 69.435 1.00 57.44 C ANISOU 2994 CG ARG A 296 9753 6050 6023 433 -526 678 C ATOM 2995 CD ARG A 296 3.036 65.339 70.023 1.00 58.47 C ANISOU 2995 CD ARG A 296 10071 6132 6013 303 -252 755 C ATOM 2996 NE ARG A 296 2.269 64.116 69.797 1.00 49.55 N ANISOU 2996 NE ARG A 296 9012 4864 4952 234 -94 827 N ATOM 2997 CZ ARG A 296 1.217 64.010 68.987 1.00 52.86 C ANISOU 2997 CZ ARG A 296 9256 5303 5524 98 112 805 C ATOM 2998 NH1 ARG A 296 0.781 65.048 68.263 1.00 51.06 N ANISOU 2998 NH1 ARG A 296 8770 5239 5389 26 193 713 N ATOM 2999 NH2 ARG A 296 0.595 62.844 68.899 1.00 56.31 N ANISOU 2999 NH2 ARG A 296 9781 5580 6035 33 216 878 N ATOM 3000 N GLN A 297 6.855 63.440 67.391 1.00 46.38 N ANISOU 3000 N GLN A 297 7949 4572 5101 725 -858 575 N ATOM 3001 CA GLN A 297 7.874 62.546 67.930 1.00 51.78 C ANISOU 3001 CA GLN A 297 8757 5112 5807 887 -1083 631 C ATOM 3002 C GLN A 297 9.263 62.924 67.432 1.00 50.46 C ANISOU 3002 C GLN A 297 8305 5017 5851 1032 -1266 569 C ATOM 3003 O GLN A 297 10.246 62.808 68.171 1.00 49.62 O ANISOU 3003 O GLN A 297 8248 4839 5768 1158 -1526 613 O ATOM 3004 CB GLN A 297 7.541 61.103 67.578 1.00 57.66 C ANISOU 3004 CB GLN A 297 9629 5689 6590 907 -1007 666 C ATOM 3005 CG GLN A 297 6.252 60.592 68.214 1.00 70.91 C ANISOU 3005 CG GLN A 297 11592 7253 8100 765 -837 759 C ATOM 3006 CD GLN A 297 5.912 59.169 67.774 1.00 83.30 C ANISOU 3006 CD GLN A 297 13268 8638 9745 766 -774 788 C ATOM 3007 OE1 GLN A 297 6.258 58.748 66.661 1.00 86.61 O ANISOU 3007 OE1 GLN A 297 13516 9058 10335 825 -776 700 O ATOM 3008 NE2 GLN A 297 5.234 58.425 68.643 1.00 84.06 N ANISOU 3008 NE2 GLN A 297 13668 8560 9710 703 -707 914 N ATOM 3009 N THR A 298 9.369 63.400 66.188 1.00 44.75 N ANISOU 3009 N THR A 298 7282 4426 5295 1018 -1135 475 N ATOM 3010 CA THR A 298 10.680 63.776 65.680 1.00 45.46 C ANISOU 3010 CA THR A 298 7078 4577 5618 1153 -1255 433 C ATOM 3011 C THR A 298 11.162 65.064 66.335 1.00 48.37 C ANISOU 3011 C THR A 298 7346 5043 5990 1124 -1418 433 C ATOM 3012 O THR A 298 12.339 65.179 66.692 1.00 49.93 O ANISOU 3012 O THR A 298 7419 5207 6344 1243 -1658 452 O ATOM 3013 CB THR A 298 10.622 63.918 64.156 1.00 49.31 C ANISOU 3013 CB THR A 298 7322 5161 6251 1152 -1034 343 C ATOM 3014 OG1 THR A 298 10.079 62.707 63.605 1.00 47.14 O ANISOU 3014 OG1 THR A 298 7195 4769 5947 1169 -914 333 O ATOM 3015 CG2 THR A 298 12.016 64.167 63.591 1.00 46.18 C ANISOU 3015 CG2 THR A 298 6618 4803 6124 1309 -1100 319 C ATOM 3016 N PHE A 299 10.268 66.043 66.493 1.00 42.91 N ANISOU 3016 N PHE A 299 6700 4457 5147 969 -1305 410 N ATOM 3017 CA PHE A 299 10.604 67.245 67.256 1.00 44.59 C ANISOU 3017 CA PHE A 299 6894 4732 5318 934 -1473 406 C ATOM 3018 C PHE A 299 11.163 66.894 68.626 1.00 49.49 C ANISOU 3018 C PHE A 299 7767 5207 5828 1020 -1779 478 C ATOM 3019 O PHE A 299 12.209 67.414 69.037 1.00 53.87 O ANISOU 3019 O PHE A 299 8209 5751 6509 1090 -2058 475 O ATOM 3020 CB PHE A 299 9.374 68.141 67.426 1.00 44.66 C ANISOU 3020 CB PHE A 299 7011 4832 5126 770 -1291 384 C ATOM 3021 CG PHE A 299 8.905 68.798 66.171 1.00 43.59 C ANISOU 3021 CG PHE A 299 6623 4843 5096 685 -1058 310 C ATOM 3022 CD1 PHE A 299 9.638 68.722 64.985 1.00 46.42 C ANISOU 3022 CD1 PHE A 299 6692 5255 5691 755 -1011 266 C ATOM 3023 CD2 PHE A 299 7.716 69.490 66.171 1.00 39.57 C ANISOU 3023 CD2 PHE A 299 6181 4408 4446 547 -876 289 C ATOM 3024 CE1 PHE A 299 9.178 69.341 63.829 1.00 41.81 C ANISOU 3024 CE1 PHE A 299 5930 4792 5163 685 -800 203 C ATOM 3025 CE2 PHE A 299 7.261 70.111 65.027 1.00 42.41 C ANISOU 3025 CE2 PHE A 299 6331 4890 4893 476 -693 225 C ATOM 3026 CZ PHE A 299 7.995 70.029 63.848 1.00 43.28 C ANISOU 3026 CZ PHE A 299 6192 5048 5204 544 -663 182 C ATOM 3027 N AARG A 300 10.467 66.011 69.349 0.50 48.89 N ANISOU 3027 N AARG A 300 8048 5006 5524 1013 -1742 549 N ATOM 3028 N BARG A 300 10.467 66.018 69.355 0.50 48.88 N ANISOU 3028 N BARG A 300 8047 5005 5522 1013 -1742 549 N ATOM 3029 CA AARG A 300 10.905 65.610 70.682 0.50 52.79 C ANISOU 3029 CA AARG A 300 8861 5340 5856 1103 -2024 629 C ATOM 3030 CA BARG A 300 10.923 65.631 70.684 0.50 52.76 C ANISOU 3030 CA BARG A 300 8854 5338 5855 1103 -2029 628 C ATOM 3031 C AARG A 300 12.305 65.007 70.645 0.50 55.96 C ANISOU 3031 C AARG A 300 9110 5651 6502 1281 -2323 646 C ATOM 3032 C BARG A 300 12.320 65.025 70.635 0.50 55.95 C ANISOU 3032 C BARG A 300 9102 5652 6506 1281 -2325 644 C ATOM 3033 O AARG A 300 13.144 65.307 71.506 0.50 55.51 O ANISOU 3033 O AARG A 300 9122 5521 6449 1362 -2672 668 O ATOM 3034 O BARG A 300 13.171 65.333 71.482 0.50 55.52 O ANISOU 3034 O BARG A 300 9109 5525 6460 1363 -2675 666 O ATOM 3035 CB AARG A 300 9.902 64.613 71.274 0.50 55.52 C ANISOU 3035 CB AARG A 300 9598 5551 5945 1068 -1867 719 C ATOM 3036 CB BARG A 300 9.937 64.644 71.313 0.50 55.63 C ANISOU 3036 CB BARG A 300 9615 5564 5956 1071 -1881 719 C ATOM 3037 CG AARG A 300 10.055 64.348 72.770 0.50 59.24 C ANISOU 3037 CG AARG A 300 10512 5854 6143 1138 -2097 814 C ATOM 3038 CG BARG A 300 8.602 65.250 71.727 0.50 57.00 C ANISOU 3038 CG BARG A 300 9995 5786 5876 916 -1621 732 C ATOM 3039 CD AARG A 300 8.950 63.434 73.306 0.50 64.70 C ANISOU 3039 CD AARG A 300 11585 6413 6587 1082 -1864 920 C ATOM 3040 CD BARG A 300 7.859 64.323 72.701 0.50 67.37 C ANISOU 3040 CD BARG A 300 11755 6921 6922 910 -1528 856 C ATOM 3041 NE AARG A 300 7.634 63.779 72.784 0.50 68.90 N ANISOU 3041 NE AARG A 300 12047 7049 7084 910 -1473 898 N ATOM 3042 NE BARG A 300 6.766 63.594 72.059 0.50 68.34 N ANISOU 3042 NE BARG A 300 11850 7027 7089 800 -1196 884 N ATOM 3043 CZ AARG A 300 6.836 64.711 73.300 0.50 70.45 C ANISOU 3043 CZ AARG A 300 12376 7307 7084 813 -1318 897 C ATOM 3044 CZ BARG A 300 6.784 62.295 71.777 0.50 70.91 C ANISOU 3044 CZ BARG A 300 12228 7220 7495 839 -1175 936 C ATOM 3045 NH1AARG A 300 7.211 65.402 74.371 0.50 74.71 N ANISOU 3045 NH1AARG A 300 13171 7810 7406 870 -1520 908 N ATOM 3046 NH1BARG A 300 5.737 61.737 71.186 0.50 73.73 N ANISOU 3046 NH1BARG A 300 12550 7552 7910 718 -895 951 N ATOM 3047 NH2AARG A 300 5.659 64.951 72.741 0.50 66.76 N ANISOU 3047 NH2AARG A 300 11795 6925 6646 666 -974 880 N ATOM 3048 NH2BARG A 300 7.838 61.550 72.086 0.50 72.04 N ANISOU 3048 NH2BARG A 300 12456 7239 7679 999 -1449 972 N ATOM 3049 N LYS A 301 12.575 64.157 69.652 1.00 55.20 N ANISOU 3049 N LYS A 301 8809 5544 6621 1352 -2202 633 N ATOM 3050 CA LYS A 301 13.895 63.538 69.539 1.00 57.42 C ANISOU 3050 CA LYS A 301 8911 5733 7174 1541 -2444 651 C ATOM 3051 C LYS A 301 14.978 64.580 69.298 1.00 53.31 C ANISOU 3051 C LYS A 301 8010 5307 6940 1577 -2624 605 C ATOM 3052 O LYS A 301 16.045 64.523 69.908 1.00 60.69 O ANISOU 3052 O LYS A 301 8884 6143 8030 1700 -2976 640 O ATOM 3053 CB LYS A 301 13.878 62.511 68.404 1.00 64.98 C ANISOU 3053 CB LYS A 301 9732 6665 8292 1611 -2217 631 C ATOM 3054 CG LYS A 301 15.216 61.919 68.055 1.00 71.94 C ANISOU 3054 CG LYS A 301 10364 7467 9502 1820 -2384 639 C ATOM 3055 CD LYS A 301 15.052 60.746 67.093 1.00 75.60 C ANISOU 3055 CD LYS A 301 10821 7860 10043 1902 -2155 620 C ATOM 3056 N ILE A 302 14.707 65.549 68.420 1.00 52.24 N ANISOU 3056 N ILE A 302 7611 5346 6890 1467 -2398 532 N ATOM 3057 CA ILE A 302 15.702 66.551 68.060 1.00 55.87 C ANISOU 3057 CA ILE A 302 7680 5891 7659 1484 -2515 497 C ATOM 3058 C ILE A 302 16.033 67.427 69.260 1.00 59.53 C ANISOU 3058 C ILE A 302 8261 6314 8043 1445 -2874 509 C ATOM 3059 O ILE A 302 17.201 67.666 69.571 1.00 65.57 O ANISOU 3059 O ILE A 302 8818 7017 9079 1533 -3196 525 O ATOM 3060 CB ILE A 302 15.188 67.392 66.874 1.00 57.36 C ANISOU 3060 CB ILE A 302 7633 6261 7899 1364 -2170 426 C ATOM 3061 CG1 ILE A 302 15.133 66.564 65.585 1.00 54.22 C ANISOU 3061 CG1 ILE A 302 7097 5882 7623 1438 -1868 403 C ATOM 3062 CG2 ILE A 302 16.009 68.671 66.694 1.00 59.38 C ANISOU 3062 CG2 ILE A 302 7544 6601 8415 1331 -2280 402 C ATOM 3063 CD1 ILE A 302 14.443 67.312 64.425 1.00 49.01 C ANISOU 3063 CD1 ILE A 302 6300 5382 6939 1320 -1531 336 C ATOM 3064 N ILE A 303 15.008 67.916 69.955 1.00 60.49 N ANISOU 3064 N ILE A 303 8722 6456 7805 1319 -2828 501 N ATOM 3065 CA ILE A 303 15.231 68.813 71.087 1.00 63.57 C ANISOU 3065 CA ILE A 303 9290 6797 8066 1284 -3153 496 C ATOM 3066 C ILE A 303 15.989 68.100 72.207 1.00 68.37 C ANISOU 3066 C ILE A 303 10120 7218 8639 1406 -3532 549 C ATOM 3067 O ILE A 303 16.971 68.621 72.749 1.00 67.67 O ANISOU 3067 O ILE A 303 9902 7093 8718 1397 -3801 509 O ATOM 3068 CB ILE A 303 13.889 69.392 71.573 1.00 61.61 C ANISOU 3068 CB ILE A 303 9393 6600 7417 1142 -2952 476 C ATOM 3069 CG1 ILE A 303 13.369 70.410 70.553 1.00 58.71 C ANISOU 3069 CG1 ILE A 303 8743 6421 7142 1007 -2647 402 C ATOM 3070 CG2 ILE A 303 14.054 70.029 72.960 1.00 64.61 C ANISOU 3070 CG2 ILE A 303 10114 6871 7563 1147 -3302 479 C ATOM 3071 CD1 ILE A 303 11.836 70.500 70.438 1.00 55.36 C ANISOU 3071 CD1 ILE A 303 8541 6070 6425 884 -2279 392 C ATOM 3072 N ARG A 304 15.562 66.886 72.556 1.00 72.56 N ANISOU 3072 N ARG A 304 10955 7644 8970 1469 -3460 611 N ATOM 3073 CA ARG A 304 16.230 66.172 73.643 1.00 84.85 C ANISOU 3073 CA ARG A 304 12716 9049 10473 1536 -3709 630 C ATOM 3074 C ARG A 304 17.700 65.911 73.337 1.00 88.95 C ANISOU 3074 C ARG A 304 12832 9536 11428 1641 -3933 619 C ATOM 3075 O ARG A 304 18.535 65.922 74.250 1.00 90.36 O ANISOU 3075 O ARG A 304 13068 9613 11651 1664 -4236 603 O ATOM 3076 CB ARG A 304 15.522 64.848 73.926 1.00 89.54 C ANISOU 3076 CB ARG A 304 13667 9535 10820 1582 -3557 707 C ATOM 3077 CG ARG A 304 14.167 64.988 74.583 1.00 96.75 C ANISOU 3077 CG ARG A 304 15029 10437 11295 1473 -3342 734 C ATOM 3078 CD ARG A 304 13.369 63.709 74.415 1.00106.96 C ANISOU 3078 CD ARG A 304 16547 11646 12447 1492 -3096 820 C ATOM 3079 NE ARG A 304 12.184 63.683 75.266 1.00116.83 N ANISOU 3079 NE ARG A 304 18233 12852 13307 1391 -2883 861 N ATOM 3080 CZ ARG A 304 11.362 62.643 75.369 1.00123.11 C ANISOU 3080 CZ ARG A 304 19273 13554 13948 1369 -2647 943 C ATOM 3081 NH1 ARG A 304 11.583 61.540 74.660 1.00123.15 N ANISOU 3081 NH1 ARG A 304 19162 13494 14137 1443 -2617 984 N ATOM 3082 NH2 ARG A 304 10.306 62.712 76.170 1.00126.55 N ANISOU 3082 NH2 ARG A 304 20058 13954 14070 1273 -2421 982 N ATOM 3083 N SER A 305 18.039 65.691 72.069 1.00 88.57 N ANISOU 3083 N SER A 305 12379 9562 11710 1710 -3775 625 N ATOM 3084 CA SER A 305 19.388 65.286 71.695 1.00 90.97 C ANISOU 3084 CA SER A 305 12291 9832 12440 1826 -3900 630 C ATOM 3085 C SER A 305 20.305 66.471 71.413 1.00 94.93 C ANISOU 3085 C SER A 305 12366 10414 13288 1765 -4008 582 C ATOM 3086 O SER A 305 21.451 66.491 71.874 1.00102.04 O ANISOU 3086 O SER A 305 13097 11240 14432 1797 -4264 578 O ATOM 3087 CB SER A 305 19.333 64.374 70.470 1.00 90.99 C ANISOU 3087 CB SER A 305 12094 9851 12629 1950 -3623 657 C ATOM 3088 OG SER A 305 18.555 63.223 70.733 1.00 93.19 O ANISOU 3088 OG SER A 305 12762 10026 12621 1996 -3533 703 O ATOM 3089 N HIS A 306 19.826 67.458 70.654 1.00 94.12 N ANISOU 3089 N HIS A 306 12086 10449 13224 1672 -3814 548 N ATOM 3090 CA HIS A 306 20.666 68.533 70.137 1.00 96.38 C ANISOU 3090 CA HIS A 306 11922 10816 13883 1609 -3829 515 C ATOM 3091 C HIS A 306 20.387 69.871 70.806 1.00 97.02 C ANISOU 3091 C HIS A 306 12130 10924 13811 1443 -3980 460 C ATOM 3092 O HIS A 306 20.778 70.914 70.273 1.00 99.59 O ANISOU 3092 O HIS A 306 12125 11328 14388 1357 -3930 433 O ATOM 3093 CB HIS A 306 20.487 68.676 68.623 1.00 97.45 C ANISOU 3093 CB HIS A 306 11704 11082 14242 1638 -3460 516 C ATOM 3094 CG HIS A 306 20.482 67.376 67.884 1.00 98.38 C ANISOU 3094 CG HIS A 306 11784 11162 14433 1807 -3250 551 C ATOM 3095 ND1 HIS A 306 21.628 66.642 67.658 1.00103.05 N ANISOU 3095 ND1 HIS A 306 12118 11691 15346 1940 -3267 582 N ATOM 3096 CD2 HIS A 306 19.471 66.681 67.310 1.00 96.56 C ANISOU 3096 CD2 HIS A 306 11763 10944 13984 1847 -2986 548 C ATOM 3097 CE1 HIS A 306 21.320 65.547 66.984 1.00103.66 C ANISOU 3097 CE1 HIS A 306 12255 11732 15399 2080 -3045 598 C ATOM 3098 NE2 HIS A 306 20.018 65.548 66.758 1.00 99.56 N ANISOU 3098 NE2 HIS A 306 12019 11241 14568 2031 -2895 576 N ATOM 3099 N VAL A 307 19.705 69.872 71.947 1.00 97.79 N ANISOU 3099 N VAL A 307 12716 10947 13493 1398 -4129 445 N ATOM 3100 CA VAL A 307 19.418 71.120 72.648 1.00100.27 C ANISOU 3100 CA VAL A 307 13205 11262 13632 1260 -4258 382 C ATOM 3101 C VAL A 307 19.421 70.891 74.154 1.00104.60 C ANISOU 3101 C VAL A 307 14223 11643 13875 1267 -4535 364 C ATOM 3102 O VAL A 307 19.324 71.845 74.934 1.00109.22 O ANISOU 3102 O VAL A 307 15010 12177 14310 1178 -4684 304 O ATOM 3103 CB VAL A 307 18.075 71.724 72.191 1.00 94.08 C ANISOU 3103 CB VAL A 307 12565 10610 12570 1173 -3982 366 C ATOM 3104 N LEU A 308 19.536 69.633 74.577 1.00103.16 N ANISOU 3104 N LEU A 308 14237 11361 13599 1380 -4596 414 N ATOM 3105 CA LEU A 308 19.450 69.298 75.995 1.00101.90 C ANISOU 3105 CA LEU A 308 14567 11034 13117 1400 -4820 404 C ATOM 3106 C LEU A 308 20.582 68.365 76.447 1.00107.77 C ANISOU 3106 C LEU A 308 15251 11630 14067 1516 -5105 431 C ATOM 3107 O LEU A 308 21.196 67.654 75.646 1.00108.25 O ANISOU 3107 O LEU A 308 14959 11723 14449 1604 -5050 478 O ATOM 3108 CB LEU A 308 18.088 68.663 76.303 1.00 94.81 C ANISOU 3108 CB LEU A 308 14132 10138 11752 1404 -4561 446 C ATOM 3109 CG LEU A 308 16.869 69.507 76.716 1.00 87.40 C ANISOU 3109 CG LEU A 308 13538 9246 10424 1297 -4373 413 C ATOM 3110 CD1 LEU A 308 16.642 70.720 75.849 1.00 79.57 C ANISOU 3110 CD1 LEU A 308 12241 8414 9579 1196 -4243 367 C ATOM 3111 CD2 LEU A 308 15.612 68.645 76.697 1.00 88.04 C ANISOU 3111 CD2 LEU A 308 13944 9340 10167 1307 -4043 485 C TER 3112 LEU A 308 HETATM 3113 C1 ZMA A1201 1.656 103.752 56.472 1.00 48.75 C HETATM 3114 C2 ZMA A1201 1.420 105.116 56.336 1.00 53.24 C HETATM 3115 C3 ZMA A1201 0.232 105.531 55.725 1.00 56.65 C HETATM 3116 O4 ZMA A1201 -0.004 106.870 55.590 1.00 60.57 O HETATM 3117 C5 ZMA A1201 -0.706 104.594 55.257 1.00 41.49 C HETATM 3118 C6 ZMA A1201 -0.459 103.232 55.394 1.00 39.84 C HETATM 3119 C7 ZMA A1201 0.720 102.818 56.020 1.00 43.47 C HETATM 3120 C8 ZMA A1201 1.054 101.351 56.150 1.00 39.33 C HETATM 3121 C9 ZMA A1201 1.916 101.110 54.921 1.00 29.13 C HETATM 3122 N10 ZMA A1201 2.322 99.748 54.734 1.00 30.71 N HETATM 3123 C11 ZMA A1201 1.499 98.887 54.097 1.00 29.31 C HETATM 3124 N12 ZMA A1201 1.867 97.609 53.941 1.00 29.82 N HETATM 3125 N13 ZMA A1201 0.305 99.347 53.638 1.00 29.09 N HETATM 3126 C14 ZMA A1201 -0.556 98.509 53.016 1.00 32.32 C HETATM 3127 N15 ZMA A1201 -1.749 99.002 52.583 1.00 29.80 N HETATM 3128 N16 ZMA A1201 -0.178 97.230 52.834 1.00 29.38 N HETATM 3129 N17 ZMA A1201 -0.937 96.219 52.238 1.00 29.95 N HETATM 3130 C18 ZMA A1201 1.000 96.796 53.291 1.00 31.96 C HETATM 3131 N19 ZMA A1201 1.129 95.473 53.001 1.00 28.59 N HETATM 3132 C20 ZMA A1201 -0.052 95.197 52.366 1.00 29.36 C HETATM 3133 C21 ZMA A1201 -0.442 93.849 51.873 1.00 29.72 C HETATM 3134 C22 ZMA A1201 0.385 92.754 51.755 1.00 28.47 C HETATM 3135 C23 ZMA A1201 -0.495 91.766 51.286 1.00 30.63 C HETATM 3136 C24 ZMA A1201 -1.779 92.288 51.152 1.00 33.48 C HETATM 3137 O25 ZMA A1201 -1.734 93.612 51.547 1.00 35.33 O HETATM 3138 NA NA A1202 3.894 81.714 54.567 1.00 35.28 NA HETATM 3139 C1 CLR A1203 18.858 100.901 48.794 1.00 54.29 C HETATM 3140 C2 CLR A1203 18.386 102.336 48.546 1.00 55.97 C HETATM 3141 C3 CLR A1203 18.576 102.718 47.072 1.00 56.67 C HETATM 3142 C4 CLR A1203 17.769 101.752 46.200 1.00 51.62 C HETATM 3143 C5 CLR A1203 18.085 100.311 46.528 1.00 55.56 C HETATM 3144 C6 CLR A1203 18.355 99.453 45.524 1.00 57.42 C HETATM 3145 C7 CLR A1203 18.375 97.943 45.695 1.00 55.60 C HETATM 3146 C8 CLR A1203 18.141 97.470 47.129 1.00 55.04 C HETATM 3147 C9 CLR A1203 18.674 98.480 48.135 1.00 49.87 C HETATM 3148 C10 CLR A1203 18.070 99.871 47.973 1.00 51.53 C HETATM 3149 C11 CLR A1203 18.496 97.933 49.546 1.00 49.69 C HETATM 3150 C12 CLR A1203 19.243 96.609 49.744 1.00 52.98 C HETATM 3151 C13 CLR A1203 18.733 95.582 48.746 1.00 54.70 C HETATM 3152 C14 CLR A1203 18.907 96.172 47.358 1.00 55.23 C HETATM 3153 C15 CLR A1203 18.675 95.004 46.397 1.00 60.56 C HETATM 3154 C16 CLR A1203 19.198 93.790 47.180 1.00 59.99 C HETATM 3155 C17 CLR A1203 19.493 94.263 48.609 1.00 57.78 C HETATM 3156 C18 CLR A1203 17.269 95.270 49.004 1.00 52.94 C HETATM 3157 C19 CLR A1203 16.628 99.832 48.444 1.00 55.30 C HETATM 3158 C20 CLR A1203 19.168 93.157 49.608 1.00 60.83 C HETATM 3159 C21 CLR A1203 19.644 93.467 51.024 1.00 62.74 C HETATM 3160 C22 CLR A1203 19.789 91.842 49.143 1.00 59.79 C HETATM 3161 C23 CLR A1203 19.858 90.821 50.275 1.00 63.79 C HETATM 3162 C24 CLR A1203 20.721 89.639 49.851 1.00 73.94 C HETATM 3163 C25 CLR A1203 20.488 88.405 50.717 1.00 82.00 C HETATM 3164 C26 CLR A1203 21.371 87.255 50.254 1.00 86.82 C HETATM 3165 C27 CLR A1203 20.749 88.690 52.189 1.00 83.47 C HETATM 3166 O1 CLR A1203 18.156 104.077 46.807 1.00 56.24 O HETATM 3167 C1 CLR A1204 -11.787 101.059 57.429 1.00 46.95 C HETATM 3168 C2 CLR A1204 -11.728 102.593 57.373 1.00 52.36 C HETATM 3169 C3 CLR A1204 -13.101 103.234 57.646 1.00 55.57 C HETATM 3170 C4 CLR A1204 -13.637 102.804 59.007 1.00 48.06 C HETATM 3171 C5 CLR A1204 -13.564 101.289 59.156 1.00 51.79 C HETATM 3172 C6 CLR A1204 -14.640 100.618 59.629 1.00 55.41 C HETATM 3173 C7 CLR A1204 -14.570 99.236 60.247 1.00 56.26 C HETATM 3174 C8 CLR A1204 -13.242 98.518 59.966 1.00 57.30 C HETATM 3175 C9 CLR A1204 -12.514 99.053 58.731 1.00 52.14 C HETATM 3176 C10 CLR A1204 -12.284 100.564 58.791 1.00 54.03 C HETATM 3177 C11 CLR A1204 -11.204 98.292 58.512 1.00 51.95 C HETATM 3178 C12 CLR A1204 -11.379 96.767 58.453 1.00 54.11 C HETATM 3179 C13 CLR A1204 -12.108 96.236 59.680 1.00 56.14 C HETATM 3180 C14 CLR A1204 -13.424 97.007 59.760 1.00 58.00 C HETATM 3181 C15 CLR A1204 -14.249 96.235 60.782 1.00 58.86 C HETATM 3182 C16 CLR A1204 -13.815 94.774 60.571 1.00 59.13 C HETATM 3183 C17 CLR A1204 -12.584 94.783 59.650 1.00 58.04 C HETATM 3184 C18 CLR A1204 -11.311 96.472 60.960 1.00 57.06 C HETATM 3185 C19 CLR A1204 -11.260 100.897 59.874 1.00 57.22 C HETATM 3186 C20 CLR A1204 -11.613 93.656 60.041 1.00 60.30 C HETATM 3187 C21 CLR A1204 -10.399 93.543 59.130 1.00 60.81 C HETATM 3188 C22 CLR A1204 -12.363 92.333 59.970 1.00 58.28 C HETATM 3189 C23 CLR A1204 -11.544 91.132 60.424 1.00 63.09 C HETATM 3190 C24 CLR A1204 -11.545 90.080 59.324 1.00 68.60 C HETATM 3191 C25 CLR A1204 -11.649 88.637 59.814 1.00 70.63 C HETATM 3192 C26 CLR A1204 -11.105 87.712 58.731 1.00 65.93 C HETATM 3193 C27 CLR A1204 -10.944 88.387 61.143 1.00 70.83 C HETATM 3194 O1 CLR A1204 -13.030 104.667 57.587 1.00 55.73 O HETATM 3195 C1 CLR A1205 -17.090 98.500 49.508 1.00 46.55 C HETATM 3196 C2 CLR A1205 -17.219 100.018 49.509 1.00 45.75 C HETATM 3197 C3 CLR A1205 -18.260 100.484 50.513 1.00 48.34 C HETATM 3198 C4 CLR A1205 -17.820 100.057 51.916 1.00 48.71 C HETATM 3199 C5 CLR A1205 -17.609 98.555 51.904 1.00 51.04 C HETATM 3200 C6 CLR A1205 -18.245 97.778 52.803 1.00 51.57 C HETATM 3201 C7 CLR A1205 -17.897 96.320 53.073 1.00 54.23 C HETATM 3202 C8 CLR A1205 -16.726 95.818 52.227 1.00 49.15 C HETATM 3203 C9 CLR A1205 -16.770 96.443 50.834 1.00 45.73 C HETATM 3204 C10 CLR A1205 -16.678 97.968 50.864 1.00 47.43 C HETATM 3205 C11 CLR A1205 -15.704 95.844 49.915 1.00 52.92 C HETATM 3206 C12 CLR A1205 -15.774 94.323 49.789 1.00 50.66 C HETATM 3207 C13 CLR A1205 -15.663 93.724 51.186 1.00 51.28 C HETATM 3208 C14 CLR A1205 -16.779 94.304 52.054 1.00 49.15 C HETATM 3209 C15 CLR A1205 -16.801 93.459 53.320 1.00 51.82 C HETATM 3210 C16 CLR A1205 -16.384 92.076 52.801 1.00 54.35 C HETATM 3211 C17 CLR A1205 -15.929 92.228 51.341 1.00 54.79 C HETATM 3212 C18 CLR A1205 -14.282 94.070 51.748 1.00 44.45 C HETATM 3213 C19 CLR A1205 -15.268 98.457 51.191 1.00 49.18 C HETATM 3214 C20 CLR A1205 -14.784 91.242 51.057 1.00 60.92 C HETATM 3215 C21 CLR A1205 -14.320 91.213 49.611 1.00 57.11 C HETATM 3216 C22 CLR A1205 -15.227 89.829 51.432 1.00 69.38 C HETATM 3217 C23 CLR A1205 -14.117 88.800 51.250 1.00 71.00 C HETATM 3218 C24 CLR A1205 -14.670 87.498 50.691 1.00 72.58 C HETATM 3219 C25 CLR A1205 -14.899 86.458 51.783 1.00 74.80 C HETATM 3220 C26 CLR A1205 -14.702 85.048 51.231 1.00 77.54 C HETATM 3221 C27 CLR A1205 -14.010 86.692 52.997 1.00 72.46 C HETATM 3222 O1 CLR A1205 -18.413 101.911 50.399 1.00 47.73 O HETATM 3223 C10 OLC A1206 19.683 91.643 56.089 1.00 71.02 C HETATM 3224 C9 OLC A1206 19.212 92.880 56.259 1.00 67.97 C HETATM 3225 C11 OLC A1206 19.723 91.034 54.707 1.00 69.06 C HETATM 3226 C8 OLC A1206 18.694 93.686 55.091 1.00 61.84 C HETATM 3227 C24 OLC A1206 20.821 106.214 54.187 1.00101.32 C HETATM 3228 C7 OLC A1206 18.483 95.130 55.533 1.00 60.59 C HETATM 3229 C6 OLC A1206 17.620 95.949 54.574 1.00 58.63 C HETATM 3230 C5 OLC A1206 18.400 97.000 53.787 1.00 66.24 C HETATM 3231 C4 OLC A1206 18.273 98.390 54.410 1.00 72.07 C HETATM 3232 C3 OLC A1206 18.636 99.514 53.437 1.00 71.50 C HETATM 3233 C2 OLC A1206 18.858 100.822 54.194 1.00 75.06 C HETATM 3234 C21 OLC A1206 19.576 104.436 52.953 1.00 93.25 C HETATM 3235 C1 OLC A1206 19.091 101.998 53.265 1.00 82.25 C HETATM 3236 C22 OLC A1206 19.439 105.721 53.775 1.00 98.97 C HETATM 3237 O19 OLC A1206 18.928 101.893 52.058 1.00 83.64 O HETATM 3238 O25 OLC A1206 20.692 107.301 55.111 1.00105.09 O HETATM 3239 O23 OLC A1206 18.761 106.746 53.024 1.00100.84 O HETATM 3240 O20 OLC A1206 19.507 103.287 53.804 1.00 86.26 O HETATM 3241 C24 OLC A1207 18.130 98.344 41.684 1.00 95.25 C HETATM 3242 C4 OLC A1207 18.682 90.173 44.566 1.00 96.44 C HETATM 3243 C3 OLC A1207 18.959 91.323 43.610 1.00 98.26 C HETATM 3244 C2 OLC A1207 17.999 92.482 43.853 1.00101.53 C HETATM 3245 C21 OLC A1207 18.080 95.890 42.093 1.00102.98 C HETATM 3246 C1 OLC A1207 18.144 93.491 42.735 1.00104.43 C HETATM 3247 C22 OLC A1207 17.356 97.209 42.347 1.00 97.09 C HETATM 3248 O19 OLC A1207 18.839 93.228 41.764 1.00104.76 O HETATM 3249 O25 OLC A1207 17.337 99.539 41.682 1.00 93.50 O HETATM 3250 O23 OLC A1207 16.046 97.148 41.782 1.00 95.20 O HETATM 3251 O20 OLC A1207 17.489 94.796 42.805 1.00105.15 O HETATM 3252 C10 OLC A1208 16.924 82.730 52.892 1.00 70.91 C HETATM 3253 C9 OLC A1208 16.456 81.704 53.605 1.00 70.79 C HETATM 3254 C8 OLC A1208 15.754 80.547 52.928 1.00 69.59 C HETATM 3255 C24 OLC A1208 15.300 67.017 52.246 1.00 90.78 C HETATM 3256 C7 OLC A1208 16.013 79.270 53.718 1.00 67.09 C HETATM 3257 C6 OLC A1208 15.806 78.031 52.864 1.00 67.18 C HETATM 3258 C5 OLC A1208 16.041 76.765 53.672 1.00 70.56 C HETATM 3259 C4 OLC A1208 15.554 75.565 52.867 1.00 75.61 C HETATM 3260 C3 OLC A1208 16.106 74.267 53.433 1.00 81.32 C HETATM 3261 C2 OLC A1208 15.335 73.063 52.898 1.00 87.69 C HETATM 3262 C21 OLC A1208 15.770 69.337 53.101 1.00 95.44 C HETATM 3263 C1 OLC A1208 15.861 71.796 53.545 1.00 93.10 C HETATM 3264 C22 OLC A1208 14.700 68.284 52.855 1.00 93.72 C HETATM 3265 O19 OLC A1208 16.925 71.796 54.144 1.00 93.10 O HETATM 3266 O25 OLC A1208 14.263 66.184 51.708 1.00 90.37 O HETATM 3267 O23 OLC A1208 14.120 67.999 54.128 1.00 96.07 O HETATM 3268 O20 OLC A1208 15.110 70.551 53.451 1.00 96.80 O HETATM 3269 C9 OLC A1209 14.298 83.407 49.114 1.00 81.34 C HETATM 3270 C8 OLC A1209 13.730 82.055 49.473 1.00 81.01 C HETATM 3271 C24 OLC A1209 13.251 69.167 48.717 1.00 90.33 C HETATM 3272 C7 OLC A1209 14.020 81.088 48.335 1.00 81.94 C HETATM 3273 C6 OLC A1209 13.812 79.645 48.780 1.00 81.92 C HETATM 3274 C5 OLC A1209 14.324 78.690 47.710 1.00 78.93 C HETATM 3275 C4 OLC A1209 13.309 77.599 47.424 1.00 72.86 C HETATM 3276 C3 OLC A1209 13.354 76.511 48.481 1.00 69.29 C HETATM 3277 C2 OLC A1209 12.442 75.372 48.045 1.00 76.51 C HETATM 3278 C21 OLC A1209 13.131 71.679 48.790 1.00 85.19 C HETATM 3279 C1 OLC A1209 12.794 74.139 48.833 1.00 83.95 C HETATM 3280 C22 OLC A1209 12.531 70.409 48.198 1.00 88.08 C HETATM 3281 O19 OLC A1209 13.483 74.248 49.832 1.00 92.70 O HETATM 3282 O25 OLC A1209 12.806 68.006 47.998 1.00 92.15 O HETATM 3283 O23 OLC A1209 11.168 70.344 48.601 1.00 90.65 O HETATM 3284 O20 OLC A1209 12.361 72.818 48.407 1.00 81.85 O HETATM 3285 C10 OLC A1210 6.664 83.421 33.474 1.00 70.56 C HETATM 3286 C9 OLC A1210 7.603 84.086 34.140 1.00 69.83 C HETATM 3287 C8 OLC A1210 9.043 83.934 33.728 1.00 73.48 C HETATM 3288 C24 OLC A1210 12.034 96.778 34.210 1.00 78.86 C HETATM 3289 C7 OLC A1210 9.838 85.177 34.117 1.00 80.43 C HETATM 3290 C6 OLC A1210 9.445 86.402 33.293 1.00 82.40 C HETATM 3291 C5 OLC A1210 10.552 87.459 33.261 1.00 80.59 C HETATM 3292 C4 OLC A1210 10.145 88.685 32.451 1.00 78.96 C HETATM 3293 C3 OLC A1210 11.284 89.688 32.303 1.00 80.96 C HETATM 3294 C2 OLC A1210 11.312 90.714 33.431 1.00 84.48 C HETATM 3295 C21 OLC A1210 12.302 94.383 33.470 1.00 84.82 C HETATM 3296 C1 OLC A1210 12.216 91.864 33.035 1.00 88.64 C HETATM 3297 C22 OLC A1210 12.676 95.430 34.538 1.00 84.93 C HETATM 3298 O19 OLC A1210 12.773 91.816 31.953 1.00 93.77 O HETATM 3299 O25 OLC A1210 12.688 97.879 34.860 1.00 77.44 O HETATM 3300 O23 OLC A1210 12.242 95.022 35.842 1.00 90.67 O HETATM 3301 O20 OLC A1210 12.422 93.024 33.917 1.00 87.31 O HETATM 3302 C24 OLC A1211 17.082 103.582 58.306 1.00 89.14 C HETATM 3303 C7 OLC A1211 18.792 93.061 60.443 1.00 84.34 C HETATM 3304 C6 OLC A1211 17.749 93.166 61.549 1.00 83.99 C HETATM 3305 C5 OLC A1211 17.409 94.621 61.867 1.00 82.30 C HETATM 3306 C4 OLC A1211 16.550 95.256 60.782 1.00 76.86 C HETATM 3307 C3 OLC A1211 17.267 96.433 60.134 1.00 76.34 C HETATM 3308 C2 OLC A1211 16.312 97.590 59.863 1.00 77.89 C HETATM 3309 C21 OLC A1211 17.261 101.131 58.781 1.00 86.95 C HETATM 3310 C1 OLC A1211 17.082 98.667 59.149 1.00 83.83 C HETATM 3311 C22 OLC A1211 16.595 102.194 57.916 1.00 89.03 C HETATM 3312 O19 OLC A1211 18.249 98.480 58.871 1.00 90.66 O HETATM 3313 O25 OLC A1211 16.794 104.507 57.249 1.00 89.54 O HETATM 3314 O23 OLC A1211 16.975 101.970 56.559 1.00 93.70 O HETATM 3315 O20 OLC A1211 16.478 99.938 58.791 1.00 85.59 O HETATM 3316 C24 OLC A1212 23.159 101.123 62.149 1.00109.20 C HETATM 3317 C5 OLC A1212 23.297 92.572 61.983 1.00111.17 C HETATM 3318 C4 OLC A1212 22.948 92.789 63.451 1.00112.07 C HETATM 3319 C3 OLC A1212 23.251 94.216 63.902 1.00111.52 C HETATM 3320 C2 OLC A1212 22.387 95.247 63.182 1.00110.86 C HETATM 3321 C21 OLC A1212 22.676 99.096 63.574 1.00108.67 C HETATM 3322 C1 OLC A1212 22.639 96.611 63.787 1.00111.37 C HETATM 3323 C22 OLC A1212 22.068 100.222 62.737 1.00107.08 C HETATM 3324 O19 OLC A1212 23.218 96.716 64.857 1.00112.83 O HETATM 3325 O25 OLC A1212 23.912 101.792 63.174 1.00108.92 O HETATM 3326 O23 OLC A1212 21.286 99.658 61.676 1.00102.46 O HETATM 3327 O20 OLC A1212 22.214 97.825 63.105 1.00110.11 O HETATM 3328 C10 OLC A1213 0.257 93.160 69.932 1.00 72.61 C HETATM 3329 C9 OLC A1213 0.519 94.446 69.737 1.00 75.28 C HETATM 3330 C11 OLC A1213 0.999 92.104 69.157 1.00 77.48 C HETATM 3331 C8 OLC A1213 1.552 94.890 68.729 1.00 77.68 C HETATM 3332 C24 OLC A1213 5.742 105.139 62.876 1.00 88.91 C HETATM 3333 C7 OLC A1213 1.147 96.253 68.183 1.00 76.08 C HETATM 3334 C6 OLC A1213 2.055 96.673 67.040 1.00 71.63 C HETATM 3335 C5 OLC A1213 1.617 98.020 66.482 1.00 68.62 C HETATM 3336 C4 OLC A1213 1.615 99.083 67.574 1.00 72.29 C HETATM 3337 C3 OLC A1213 1.633 100.485 66.976 1.00 70.65 C HETATM 3338 C2 OLC A1213 2.802 100.604 66.013 1.00 72.05 C HETATM 3339 C21 OLC A1213 4.310 103.668 64.281 1.00 82.68 C HETATM 3340 C1 OLC A1213 2.786 101.955 65.344 1.00 79.09 C HETATM 3341 C22 OLC A1213 5.041 103.792 62.946 1.00 83.60 C HETATM 3342 O19 OLC A1213 1.882 102.743 65.561 1.00 86.13 O HETATM 3343 O25 OLC A1213 6.507 105.197 61.663 1.00 91.50 O HETATM 3344 O23 OLC A1213 6.014 102.745 62.802 1.00 80.26 O HETATM 3345 O20 OLC A1213 3.860 102.322 64.435 1.00 80.46 O HETATM 3346 C10 OLC A1214 24.253 89.684 56.474 1.00 76.76 C HETATM 3347 C9 OLC A1214 24.760 90.820 56.953 1.00 74.88 C HETATM 3348 C8 OLC A1214 24.152 92.152 56.577 1.00 74.90 C HETATM 3349 C24 OLC A1214 23.271 104.065 57.605 1.00 82.31 C HETATM 3350 C7 OLC A1214 24.409 93.163 57.690 1.00 72.91 C HETATM 3351 C6 OLC A1214 23.672 94.471 57.438 1.00 71.29 C HETATM 3352 C5 OLC A1214 22.343 94.492 58.182 1.00 74.05 C HETATM 3353 C4 OLC A1214 21.453 95.643 57.726 1.00 71.83 C HETATM 3354 C3 OLC A1214 22.124 96.985 57.952 1.00 71.61 C HETATM 3355 C2 OLC A1214 21.277 98.129 57.395 1.00 77.32 C HETATM 3356 C21 OLC A1214 22.596 101.714 57.279 1.00 84.55 C HETATM 3357 C1 OLC A1214 21.984 99.406 57.765 1.00 85.00 C HETATM 3358 C22 OLC A1214 22.077 103.133 57.443 1.00 85.45 C HETATM 3359 O19 OLC A1214 22.972 99.340 58.478 1.00 90.67 O HETATM 3360 O25 OLC A1214 22.849 105.420 57.427 1.00 81.52 O HETATM 3361 O23 OLC A1214 21.351 103.517 56.273 1.00 90.46 O HETATM 3362 O20 OLC A1214 21.568 100.722 57.297 1.00 84.97 O HETATM 3363 C1 OLA A1215 -4.293 107.286 69.565 1.00101.76 C HETATM 3364 O1 OLA A1215 -3.962 107.785 68.465 1.00106.38 O HETATM 3365 O2 OLA A1215 -5.221 107.823 70.212 1.00100.01 O HETATM 3366 C2 OLA A1215 -3.576 106.062 70.098 1.00 94.98 C HETATM 3367 C3 OLA A1215 -4.121 104.792 69.452 1.00 87.81 C HETATM 3368 C4 OLA A1215 -4.563 103.800 70.518 1.00 83.15 C HETATM 3369 C5 OLA A1215 -4.744 102.389 69.975 1.00 78.40 C HETATM 3370 C6 OLA A1215 -3.436 101.603 70.011 1.00 74.92 C HETATM 3371 C7 OLA A1215 -3.726 100.122 70.204 1.00 73.50 C HETATM 3372 C8 OLA A1215 -2.482 99.258 70.040 1.00 74.20 C HETATM 3373 C9 OLA A1215 -2.757 97.895 70.634 1.00 76.14 C HETATM 3374 C10 OLA A1215 -2.941 96.829 69.861 1.00 74.92 C HETATM 3375 C1 OLA A1216 0.687 104.538 68.167 1.00 95.54 C HETATM 3376 O1 OLA A1216 1.173 105.239 67.254 1.00 94.98 O HETATM 3377 O2 OLA A1216 -0.526 104.661 68.446 1.00 97.97 O HETATM 3378 C2 OLA A1216 1.551 103.557 68.923 1.00 92.20 C HETATM 3379 C3 OLA A1216 0.966 103.329 70.312 1.00 85.88 C HETATM 3380 C4 OLA A1216 1.098 101.868 70.727 1.00 82.64 C HETATM 3381 C5 OLA A1216 0.519 101.642 72.119 1.00 83.71 C HETATM 3382 C6 OLA A1216 0.977 100.305 72.690 1.00 83.79 C HETATM 3383 C7 OLA A1216 1.391 100.448 74.149 1.00 81.36 C HETATM 3384 C8 OLA A1216 2.344 99.332 74.558 1.00 77.12 C HETATM 3385 C9 OLA A1216 1.580 98.264 75.304 1.00 73.60 C HETATM 3386 C10 OLA A1216 1.812 96.979 75.051 1.00 67.44 C HETATM 3387 C11 OLA A1216 3.022 96.575 74.244 1.00 60.24 C HETATM 3388 C12 OLA A1216 3.249 95.075 74.384 1.00 53.00 C HETATM 3389 C13 OLA A1216 4.382 94.606 73.479 1.00 58.39 C HETATM 3390 C14 OLA A1216 4.416 93.086 73.388 1.00 57.23 C HETATM 3391 C1 OLA A1217 -11.485 102.947 63.729 1.00 90.60 C HETATM 3392 O1 OLA A1217 -11.663 103.900 62.941 1.00 88.35 O HETATM 3393 O2 OLA A1217 -10.945 103.168 64.833 1.00 95.99 O HETATM 3394 C2 OLA A1217 -11.908 101.548 63.353 1.00 88.40 C HETATM 3395 C3 OLA A1217 -11.997 100.670 64.596 1.00 85.29 C HETATM 3396 C4 OLA A1217 -11.333 99.328 64.326 1.00 82.48 C HETATM 3397 C5 OLA A1217 -11.992 98.209 65.117 1.00 80.76 C HETATM 3398 C6 OLA A1217 -11.226 96.912 64.893 1.00 83.03 C HETATM 3399 C7 OLA A1217 -11.011 96.136 66.188 1.00 82.48 C HETATM 3400 C8 OLA A1217 -9.584 95.610 66.288 1.00 80.02 C HETATM 3401 C1 OLA A1218 16.527 100.975 63.360 1.00108.90 C HETATM 3402 O1 OLA A1218 17.302 101.793 62.815 1.00113.57 O HETATM 3403 O2 OLA A1218 15.323 100.966 63.016 1.00107.85 O HETATM 3404 C2 OLA A1218 17.038 100.023 64.419 1.00102.62 C HETATM 3405 C3 OLA A1218 16.423 98.646 64.219 1.00 95.62 C HETATM 3406 C4 OLA A1218 17.475 97.558 64.392 1.00 94.19 C HETATM 3407 C5 OLA A1218 17.230 96.756 65.662 1.00 93.56 C HETATM 3408 C6 OLA A1218 18.483 96.005 66.091 1.00 95.42 C HETATM 3409 C7 OLA A1218 18.509 94.600 65.496 1.00 96.73 C HETATM 3410 C8 OLA A1218 19.351 93.656 66.349 1.00 97.12 C HETATM 3411 C9 OLA A1218 19.452 92.309 65.668 1.00 97.20 C HETATM 3412 C1 OLA A1219 14.595 100.432 69.419 1.00 95.89 C HETATM 3413 O1 OLA A1219 13.966 100.064 68.407 1.00 97.26 O HETATM 3414 O2 OLA A1219 14.941 101.634 69.517 1.00 97.33 O HETATM 3415 C2 OLA A1219 14.917 99.424 70.494 1.00 91.93 C HETATM 3416 C3 OLA A1219 14.114 98.165 70.203 1.00 88.22 C HETATM 3417 C4 OLA A1219 15.021 97.046 69.709 1.00 86.35 C HETATM 3418 C5 OLA A1219 15.679 96.314 70.871 1.00 84.01 C HETATM 3419 C6 OLA A1219 15.908 94.848 70.526 1.00 84.12 C HETATM 3420 C7 OLA A1219 14.712 93.979 70.908 1.00 84.85 C HETATM 3421 C1 OLA A1220 0.550 67.664 42.748 1.00 78.72 C HETATM 3422 O1 OLA A1220 1.011 66.579 42.330 1.00 84.68 O HETATM 3423 O2 OLA A1220 0.703 67.943 43.939 1.00 76.32 O HETATM 3424 C2 OLA A1220 -0.162 68.638 41.845 1.00 78.96 C HETATM 3425 C3 OLA A1220 0.463 70.020 42.008 1.00 76.32 C HETATM 3426 C4 OLA A1220 -0.538 71.127 41.700 1.00 70.97 C HETATM 3427 C5 OLA A1220 0.187 72.424 41.384 1.00 68.58 C HETATM 3428 C6 OLA A1220 -0.606 73.638 41.834 1.00 63.27 C HETATM 3429 C7 OLA A1220 0.346 74.736 42.294 1.00 61.73 C HETATM 3430 C1 OLA A1221 -15.120 100.970 40.815 1.00108.54 C HETATM 3431 O1 OLA A1221 -14.298 101.849 40.478 1.00111.14 O HETATM 3432 O2 OLA A1221 -15.193 100.653 42.018 1.00110.16 O HETATM 3433 C2 OLA A1221 -16.005 100.290 39.799 1.00104.06 C HETATM 3434 C3 OLA A1221 -16.613 99.059 40.456 1.00101.94 C HETATM 3435 C4 OLA A1221 -15.972 97.774 39.950 1.00 99.81 C HETATM 3436 C5 OLA A1221 -16.571 96.568 40.663 1.00 98.99 C HETATM 3437 C6 OLA A1221 -15.515 95.496 40.898 1.00 98.28 C HETATM 3438 C7 OLA A1221 -15.979 94.115 40.447 1.00 97.39 C HETATM 3439 C8 OLA A1221 -15.476 93.058 41.427 1.00 96.38 C HETATM 3440 C9 OLA A1221 -15.814 91.664 40.954 1.00 94.08 C HETATM 3441 C10 OLA A1221 -15.030 90.646 41.297 1.00 93.52 C HETATM 3442 C1 OLA A1222 -10.582 73.643 65.024 1.00114.12 C HETATM 3443 O1 OLA A1222 -10.994 73.153 63.951 1.00116.12 O HETATM 3444 O2 OLA A1222 -10.765 73.013 66.088 1.00114.51 O HETATM 3445 C2 OLA A1222 -9.871 74.976 65.036 1.00109.54 C HETATM 3446 C3 OLA A1222 -10.331 75.806 63.843 1.00103.68 C HETATM 3447 C4 OLA A1222 -9.150 76.497 63.171 1.00 97.22 C HETATM 3448 C5 OLA A1222 -9.563 77.109 61.838 1.00 92.13 C HETATM 3449 C6 OLA A1222 -9.423 78.626 61.867 1.00 90.81 C HETATM 3450 C7 OLA A1222 -10.763 79.304 61.608 1.00 89.24 C HETATM 3451 C8 OLA A1222 -10.743 80.067 60.289 1.00 88.81 C HETATM 3452 C9 OLA A1222 -11.988 80.916 60.180 1.00 89.80 C HETATM 3453 C10 OLA A1222 -12.238 81.588 59.060 1.00 87.28 C HETATM 3454 C11 OLA A1222 -11.483 81.256 57.795 1.00 83.84 C HETATM 3455 C1 OLA A1223 16.517 74.740 66.558 1.00 92.56 C HETATM 3456 O1 OLA A1223 17.247 75.548 65.941 1.00 96.47 O HETATM 3457 O2 OLA A1223 16.304 73.623 66.032 1.00 93.94 O HETATM 3458 C2 OLA A1223 15.943 75.112 67.916 1.00 85.54 C HETATM 3459 C3 OLA A1223 14.475 74.709 68.060 1.00 80.24 C HETATM 3460 C4 OLA A1223 13.759 75.480 69.175 1.00 74.32 C HETATM 3461 C5 OLA A1223 12.261 75.188 69.200 1.00 65.40 C HETATM 3462 C6 OLA A1223 11.461 76.470 69.406 1.00 55.61 C HETATM 3463 C7 OLA A1223 10.247 76.566 68.495 1.00 49.63 C HETATM 3464 C8 OLA A1223 9.751 77.994 68.494 1.00 48.37 C HETATM 3465 C9 OLA A1223 8.485 78.117 67.702 1.00 53.54 C HETATM 3466 C1 OLA A1224 12.843 91.947 38.110 1.00103.07 C HETATM 3467 O1 OLA A1224 12.259 92.964 37.678 1.00104.52 O HETATM 3468 O2 OLA A1224 13.676 92.072 39.034 1.00104.73 O HETATM 3469 C2 OLA A1224 12.546 90.586 37.526 1.00 98.15 C HETATM 3470 C3 OLA A1224 11.054 90.298 37.643 1.00 91.65 C HETATM 3471 C4 OLA A1224 10.809 88.881 38.147 1.00 86.48 C HETATM 3472 C5 OLA A1224 11.138 87.854 37.070 1.00 83.49 C HETATM 3473 C6 OLA A1224 11.189 86.447 37.654 1.00 81.13 C HETATM 3474 C7 OLA A1224 12.622 85.935 37.719 1.00 79.75 C HETATM 3475 C8 OLA A1224 12.760 84.829 38.760 1.00 81.25 C HETATM 3476 C9 OLA A1224 14.125 84.907 39.399 1.00 83.25 C HETATM 3477 C10 OLA A1224 14.466 84.040 40.349 1.00 84.55 C HETATM 3478 C11 OLA A1224 13.620 82.813 40.590 1.00 84.48 C HETATM 3479 C12 OLA A1224 14.515 81.655 41.017 1.00 83.13 C HETATM 3480 C13 OLA A1224 13.861 80.840 42.126 1.00 83.54 C HETATM 3481 C14 OLA A1224 14.326 79.389 42.084 1.00 85.54 C HETATM 3482 C15 OLA A1224 13.798 78.612 43.284 1.00 85.74 C HETATM 3483 C16 OLA A1224 14.437 77.230 43.363 1.00 84.51 C HETATM 3484 C17 OLA A1224 13.588 76.284 44.204 1.00 79.77 C HETATM 3485 C18 OLA A1224 14.066 74.844 44.057 1.00 76.50 C HETATM 3486 C1 OLA A1225 24.641 65.695 58.122 1.00 82.18 C HETATM 3487 O1 OLA A1225 25.314 64.872 58.773 1.00 85.15 O HETATM 3488 O2 OLA A1225 23.847 65.249 57.265 1.00 82.90 O HETATM 3489 C2 OLA A1225 24.788 67.180 58.370 1.00 75.23 C HETATM 3490 C3 OLA A1225 24.497 67.901 57.070 1.00 76.23 C HETATM 3491 C4 OLA A1225 23.274 68.798 57.177 1.00 83.18 C HETATM 3492 C5 OLA A1225 22.732 69.119 55.787 1.00 87.97 C HETATM 3493 C6 OLA A1225 21.858 70.370 55.804 1.00 93.09 C HETATM 3494 C7 OLA A1225 20.498 70.072 56.439 1.00 97.05 C HETATM 3495 C8 OLA A1225 19.504 71.221 56.274 1.00 96.25 C HETATM 3496 C9 OLA A1225 18.338 71.035 57.220 1.00 93.00 C HETATM 3497 C10 OLA A1225 17.775 72.080 57.831 1.00 90.89 C HETATM 3498 C11 OLA A1225 18.481 73.415 57.896 1.00 88.09 C HETATM 3499 C12 OLA A1225 17.607 74.527 57.324 1.00 84.67 C HETATM 3500 C13 OLA A1225 18.471 75.695 56.860 1.00 83.24 C HETATM 3501 C14 OLA A1225 17.917 77.029 57.341 1.00 84.21 C HETATM 3502 C15 OLA A1225 18.817 78.189 56.922 1.00 85.62 C HETATM 3503 C16 OLA A1225 18.560 79.451 57.746 1.00 82.48 C HETATM 3504 C17 OLA A1225 19.201 80.669 57.086 1.00 79.34 C HETATM 3505 C1 PEG A1226 5.091 69.283 35.862 1.00 94.24 C HETATM 3506 O1 PEG A1226 5.400 70.537 35.245 1.00 95.68 O HETATM 3507 C2 PEG A1226 6.285 68.819 36.686 1.00 94.52 C HETATM 3508 O2 PEG A1226 7.415 68.643 35.834 1.00 95.85 O HETATM 3509 C3 PEG A1226 8.580 68.304 36.576 1.00 97.41 C HETATM 3510 C4 PEG A1226 9.623 67.717 35.640 1.00 99.20 C HETATM 3511 O4 PEG A1226 10.902 67.839 36.265 1.00101.24 O HETATM 3512 C9 OLC A1227 23.518 88.587 46.212 1.00 80.01 C HETATM 3513 C8 OLC A1227 23.419 89.972 46.810 1.00 79.42 C HETATM 3514 C24 OLC A1227 22.955 103.277 44.623 1.00 93.63 C HETATM 3515 C7 OLC A1227 23.325 91.037 45.717 1.00 75.26 C HETATM 3516 C6 OLC A1227 23.555 92.413 46.327 1.00 70.40 C HETATM 3517 C5 OLC A1227 23.376 93.548 45.326 1.00 65.17 C HETATM 3518 C4 OLC A1227 23.290 94.883 46.070 1.00 62.13 C HETATM 3519 C3 OLC A1227 22.966 96.033 45.120 1.00 59.02 C HETATM 3520 C2 OLC A1227 22.739 97.307 45.913 1.00 59.92 C HETATM 3521 C21 OLC A1227 22.479 100.850 44.487 1.00 76.13 C HETATM 3522 C1 OLC A1227 22.486 98.448 44.974 1.00 68.30 C HETATM 3523 C22 OLC A1227 22.029 102.165 45.096 1.00 87.44 C HETATM 3524 O19 OLC A1227 22.394 98.245 43.782 1.00 78.12 O HETATM 3525 O25 OLC A1227 22.256 104.525 44.722 1.00 96.51 O HETATM 3526 O23 OLC A1227 20.706 102.456 44.637 1.00 92.12 O HETATM 3527 O20 OLC A1227 22.348 99.813 45.448 1.00 71.63 O HETATM 3528 O HOH A1301 2.741 56.748 48.699 1.00 86.11 O HETATM 3529 O HOH A1302 -17.884 25.011 50.545 1.00 73.84 O HETATM 3530 O HOH A1303 -6.964 56.473 50.100 1.00 60.73 O HETATM 3531 O HOH A1304 4.788 104.439 58.652 1.00 64.22 O HETATM 3532 O HOH A1305 -6.817 107.816 59.208 1.00 70.21 O HETATM 3533 O HOH A1306 -5.052 100.376 52.838 1.00 31.17 O HETATM 3534 O HOH A1307 5.388 74.182 56.690 1.00 33.71 O HETATM 3535 O HOH A1308 3.005 61.587 49.618 1.00 55.18 O HETATM 3536 O HOH A1309 6.215 108.915 48.751 1.00 41.28 O HETATM 3537 O HOH A1310 1.069 87.439 46.902 1.00 35.34 O HETATM 3538 O HOH A1311 8.100 92.996 54.070 1.00 32.07 O HETATM 3539 O HOH A1312 6.011 75.265 46.478 1.00 44.45 O HETATM 3540 O HOH A1313 6.334 77.816 49.522 1.00 36.99 O HETATM 3541 O HOH A1314 8.929 92.822 51.400 1.00 32.57 O HETATM 3542 O HOH A1315 2.426 83.496 55.429 1.00 34.77 O HETATM 3543 O HOH A1316 7.401 78.707 64.732 1.00 46.62 O HETATM 3544 O HOH A1317 4.637 107.276 69.193 1.00 51.62 O HETATM 3545 O HOH A1318 3.951 105.497 37.378 1.00 56.21 O HETATM 3546 O HOH A1319 -1.723 103.023 46.845 1.00 48.69 O HETATM 3547 O HOH A1320 3.343 93.990 53.581 1.00 41.52 O HETATM 3548 O HOH A1321 3.670 85.505 56.949 1.00 34.12 O HETATM 3549 O HOH A1322 4.560 97.158 53.948 1.00 42.19 O HETATM 3550 O HOH A1323 -13.577 29.763 56.695 1.00 72.90 O HETATM 3551 O HOH A1324 6.238 98.015 57.743 1.00 36.90 O HETATM 3552 O HOH A1325 -8.703 102.384 54.943 1.00 36.84 O HETATM 3553 O HOH A1326 4.749 103.126 34.954 1.00 79.85 O HETATM 3554 O HOH A1327 5.620 76.827 57.726 1.00 33.99 O HETATM 3555 O HOH A1328 -3.398 72.803 51.906 1.00 34.49 O HETATM 3556 O HOH A1329 -2.970 64.850 61.465 1.00 62.32 O HETATM 3557 O HOH A1330 -0.589 88.589 49.090 1.00 35.49 O HETATM 3558 O HOH A1331 -5.587 63.036 53.802 1.00 39.82 O HETATM 3559 O HOH A1332 2.746 80.232 56.021 1.00 34.02 O HETATM 3560 O HOH A1333 -7.121 53.777 42.736 1.00 65.38 O HETATM 3561 O HOH A1334 14.200 103.712 39.975 1.00 57.99 O HETATM 3562 O HOH A1335 -3.591 90.956 58.243 1.00 34.64 O HETATM 3563 O HOH A1336 4.023 79.010 59.900 1.00 31.14 O HETATM 3564 O HOH A1337 -18.182 103.882 48.429 1.00 69.09 O HETATM 3565 O HOH A1338 -3.604 62.059 54.239 1.00 52.53 O HETATM 3566 O HOH A1339 6.173 77.911 45.504 1.00 44.85 O HETATM 3567 O HOH A1340 0.054 54.228 44.770 1.00 64.61 O HETATM 3568 O HOH A1341 -9.278 55.989 49.385 1.00 61.93 O HETATM 3569 O HOH A1342 -2.010 72.664 54.392 1.00 40.10 O HETATM 3570 O HOH A1343 9.118 102.597 62.512 1.00 55.93 O HETATM 3571 O HOH A1344 -15.875 25.714 53.194 1.00 72.17 O HETATM 3572 O HOH A1345 1.080 106.598 52.152 1.00 48.35 O HETATM 3573 O HOH A1346 -1.037 78.931 58.140 1.00 34.67 O HETATM 3574 O HOH A1347 2.136 104.016 52.827 1.00 37.42 O HETATM 3575 O HOH A1348 -2.121 87.160 51.109 1.00 34.95 O HETATM 3576 O HOH A1349 -6.201 62.059 51.438 1.00 46.87 O HETATM 3577 O HOH A1350 -4.842 93.702 49.040 1.00 29.91 O HETATM 3578 O HOH A1351 4.619 85.847 53.740 1.00 38.71 O HETATM 3579 O HOH A1352 8.224 107.318 60.756 1.00103.34 O HETATM 3580 O HOH A1353 6.460 109.398 45.995 1.00 53.50 O HETATM 3581 O HOH A1354 0.965 53.663 41.965 1.00 97.01 O HETATM 3582 O HOH A1355 0.790 78.616 55.834 1.00 49.96 O HETATM 3583 O HOH A1356 -10.413 105.403 52.121 1.00 65.32 O HETATM 3584 O HOH A1357 9.030 60.683 37.701 1.00 71.69 O HETATM 3585 O HOH A1358 5.714 95.384 52.363 1.00 34.56 O HETATM 3586 O HOH A1359 -7.795 105.570 66.142 1.00 68.42 O HETATM 3587 O HOH A1360 -12.577 102.326 42.772 1.00 84.47 O HETATM 3588 O HOH A1361 1.414 113.472 43.498 1.00 77.31 O HETATM 3589 O HOH A1362 8.211 95.607 53.079 1.00 42.38 O HETATM 3590 O HOH A1363 -1.850 106.366 51.952 1.00 50.67 O HETATM 3591 O HOH A1364 3.102 58.213 35.226 1.00 69.48 O HETATM 3592 O HOH A1365 5.561 93.191 55.261 1.00 39.12 O HETATM 3593 O HOH A1366 -3.884 61.064 60.552 1.00 66.67 O HETATM 3594 O HOH A1367 -3.522 107.305 62.034 1.00 56.96 O HETATM 3595 O HOH A1368 -3.718 104.317 49.164 1.00 68.92 O HETATM 3596 O HOH A1369 -1.489 63.654 66.952 1.00 64.18 O HETATM 3597 O HOH A1370 8.426 101.529 36.078 1.00 62.63 O HETATM 3598 O HOH A1371 5.287 60.263 48.508 1.00 60.59 O HETATM 3599 O HOH A1372 15.515 58.162 59.042 1.00 60.31 O HETATM 3600 O HOH A1373 5.483 107.377 44.264 1.00 50.34 O HETATM 3601 O HOH A1374 -11.515 100.946 39.879 1.00 95.67 O HETATM 3602 O HOH A1375 4.988 99.879 56.081 1.00 42.34 O HETATM 3603 O AHOH A1376 -0.844 61.666 63.334 0.50 37.31 O HETATM 3604 O BHOH A1376 -1.908 61.957 64.429 0.50 42.49 O HETATM 3605 O HOH A1377 2.987 91.773 55.254 1.00 42.17 O HETATM 3606 O HOH A1378 -20.460 58.034 55.792 1.00 85.01 O HETATM 3607 O HOH A1379 5.537 101.902 54.279 1.00 35.02 O HETATM 3608 O HOH A1380 -15.028 107.214 57.678 1.00 79.45 O HETATM 3609 O HOH A1381 5.478 83.243 53.642 1.00 36.88 O HETATM 3610 O HOH A1382 1.629 60.881 62.221 1.00 55.82 O HETATM 3611 O HOH A1383 9.567 105.461 61.719 1.00 81.22 O HETATM 3612 O HOH A1384 -8.401 100.959 38.449 1.00 62.49 O HETATM 3613 O HOH A1385 -0.058 59.020 50.577 1.00 77.39 O HETATM 3614 O HOH A1386 -2.752 103.789 44.469 1.00 56.27 O HETATM 3615 O HOH A1387 -2.784 107.843 54.505 1.00 74.46 O HETATM 3616 O HOH A1388 -4.786 102.513 42.117 1.00 47.71 O HETATM 3617 O HOH A1389 -16.999 106.343 48.918 1.00 65.15 O HETATM 3618 O HOH A1390 -11.041 103.762 53.785 1.00 47.96 O HETATM 3619 O HOH A1391 -2.561 105.696 64.923 1.00 57.43 O HETATM 3620 O HOH A1392 -36.077 34.024 52.814 1.00 69.23 O HETATM 3621 O HOH A1393 8.149 108.906 57.062 1.00 90.84 O HETATM 3622 O HOH A1394 10.790 110.773 67.654 1.00 55.94 O HETATM 3623 O HOH A1395 -4.157 107.224 58.648 1.00 71.04 O HETATM 3624 O HOH A1396 -0.972 63.105 54.868 1.00 75.95 O HETATM 3625 O HOH A1397 -6.785 104.187 46.870 1.00 67.08 O HETATM 3626 O HOH A1398 -5.514 59.681 63.660 1.00 90.72 O HETATM 3627 O HOH A1399 4.885 58.297 49.514 1.00 89.25 O HETATM 3628 O HOH A1400 -3.346 59.872 63.766 1.00 83.13 O HETATM 3629 O HOH A1401 -1.646 62.448 60.881 1.00 75.64 O HETATM 3630 O HOH A1402 5.366 95.828 55.703 1.00 53.25 O HETATM 3631 O HOH A1403 11.144 67.802 74.401 1.00 51.42 O HETATM 3632 O HOH A1404 3.355 107.061 34.760 1.00 89.49 O HETATM 3633 O HOH A1405 12.627 104.924 63.015 1.00 91.62 O CONECT 417 3138 CONECT 550 1230 CONECT 566 1131 CONECT 586 1270 CONECT 700 3138 CONECT 1131 566 CONECT 1230 550 CONECT 1270 586 CONECT 2682 2703 CONECT 2703 2682 CONECT 3113 3114 3119 CONECT 3114 3113 3115 CONECT 3115 3114 3116 3117 CONECT 3116 3115 CONECT 3117 3115 3118 CONECT 3118 3117 3119 CONECT 3119 3113 3118 3120 CONECT 3120 3119 3121 CONECT 3121 3120 3122 CONECT 3122 3121 3123 CONECT 3123 3122 3124 3125 CONECT 3124 3123 3130 CONECT 3125 3123 3126 CONECT 3126 3125 3127 3128 CONECT 3127 3126 CONECT 3128 3126 3129 3130 CONECT 3129 3128 3132 CONECT 3130 3124 3128 3131 CONECT 3131 3130 3132 CONECT 3132 3129 3131 3133 CONECT 3133 3132 3134 3137 CONECT 3134 3133 3135 CONECT 3135 3134 3136 CONECT 3136 3135 3137 CONECT 3137 3133 3136 CONECT 3138 417 700 3542 3559 CONECT 3138 3609 CONECT 3139 3140 3148 CONECT 3140 3139 3141 CONECT 3141 3140 3142 3166 CONECT 3142 3141 3143 CONECT 3143 3142 3144 3148 CONECT 3144 3143 3145 CONECT 3145 3144 3146 CONECT 3146 3145 3147 3152 CONECT 3147 3146 3148 3149 CONECT 3148 3139 3143 3147 3157 CONECT 3149 3147 3150 CONECT 3150 3149 3151 CONECT 3151 3150 3152 3155 3156 CONECT 3152 3146 3151 3153 CONECT 3153 3152 3154 CONECT 3154 3153 3155 CONECT 3155 3151 3154 3158 CONECT 3156 3151 CONECT 3157 3148 CONECT 3158 3155 3159 3160 CONECT 3159 3158 CONECT 3160 3158 3161 CONECT 3161 3160 3162 CONECT 3162 3161 3163 CONECT 3163 3162 3164 3165 CONECT 3164 3163 CONECT 3165 3163 CONECT 3166 3141 CONECT 3167 3168 3176 CONECT 3168 3167 3169 CONECT 3169 3168 3170 3194 CONECT 3170 3169 3171 CONECT 3171 3170 3172 3176 CONECT 3172 3171 3173 CONECT 3173 3172 3174 CONECT 3174 3173 3175 3180 CONECT 3175 3174 3176 3177 CONECT 3176 3167 3171 3175 3185 CONECT 3177 3175 3178 CONECT 3178 3177 3179 CONECT 3179 3178 3180 3183 3184 CONECT 3180 3174 3179 3181 CONECT 3181 3180 3182 CONECT 3182 3181 3183 CONECT 3183 3179 3182 3186 CONECT 3184 3179 CONECT 3185 3176 CONECT 3186 3183 3187 3188 CONECT 3187 3186 CONECT 3188 3186 3189 CONECT 3189 3188 3190 CONECT 3190 3189 3191 CONECT 3191 3190 3192 3193 CONECT 3192 3191 CONECT 3193 3191 CONECT 3194 3169 CONECT 3195 3196 3204 CONECT 3196 3195 3197 CONECT 3197 3196 3198 3222 CONECT 3198 3197 3199 CONECT 3199 3198 3200 3204 CONECT 3200 3199 3201 CONECT 3201 3200 3202 CONECT 3202 3201 3203 3208 CONECT 3203 3202 3204 3205 CONECT 3204 3195 3199 3203 3213 CONECT 3205 3203 3206 CONECT 3206 3205 3207 CONECT 3207 3206 3208 3211 3212 CONECT 3208 3202 3207 3209 CONECT 3209 3208 3210 CONECT 3210 3209 3211 CONECT 3211 3207 3210 3214 CONECT 3212 3207 CONECT 3213 3204 CONECT 3214 3211 3215 3216 CONECT 3215 3214 CONECT 3216 3214 3217 CONECT 3217 3216 3218 CONECT 3218 3217 3219 CONECT 3219 3218 3220 3221 CONECT 3220 3219 CONECT 3221 3219 CONECT 3222 3197 CONECT 3223 3224 3225 CONECT 3224 3223 3226 CONECT 3225 3223 CONECT 3226 3224 3228 CONECT 3227 3236 3238 CONECT 3228 3226 3229 CONECT 3229 3228 3230 CONECT 3230 3229 3231 CONECT 3231 3230 3232 CONECT 3232 3231 3233 CONECT 3233 3232 3235 CONECT 3234 3236 3240 CONECT 3235 3233 3237 3240 CONECT 3236 3227 3234 3239 CONECT 3237 3235 CONECT 3238 3227 CONECT 3239 3236 CONECT 3240 3234 3235 CONECT 3241 3247 3249 CONECT 3242 3243 CONECT 3243 3242 3244 CONECT 3244 3243 3246 CONECT 3245 3247 3251 CONECT 3246 3244 3248 3251 CONECT 3247 3241 3245 3250 CONECT 3248 3246 CONECT 3249 3241 CONECT 3250 3247 CONECT 3251 3245 3246 CONECT 3252 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3256 CONECT 3255 3264 3266 CONECT 3256 3254 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3263 CONECT 3262 3264 3268 CONECT 3263 3261 3265 3268 CONECT 3264 3255 3262 3267 CONECT 3265 3263 CONECT 3266 3255 CONECT 3267 3264 CONECT 3268 3262 3263 CONECT 3269 3270 CONECT 3270 3269 3272 CONECT 3271 3280 3282 CONECT 3272 3270 3273 CONECT 3273 3272 3274 CONECT 3274 3273 3275 CONECT 3275 3274 3276 CONECT 3276 3275 3277 CONECT 3277 3276 3279 CONECT 3278 3280 3284 CONECT 3279 3277 3281 3284 CONECT 3280 3271 3278 3283 CONECT 3281 3279 CONECT 3282 3271 CONECT 3283 3280 CONECT 3284 3278 3279 CONECT 3285 3286 CONECT 3286 3285 3287 CONECT 3287 3286 3289 CONECT 3288 3297 3299 CONECT 3289 3287 3290 CONECT 3290 3289 3291 CONECT 3291 3290 3292 CONECT 3292 3291 3293 CONECT 3293 3292 3294 CONECT 3294 3293 3296 CONECT 3295 3297 3301 CONECT 3296 3294 3298 3301 CONECT 3297 3288 3295 3300 CONECT 3298 3296 CONECT 3299 3288 CONECT 3300 3297 CONECT 3301 3295 3296 CONECT 3302 3311 3313 CONECT 3303 3304 CONECT 3304 3303 3305 CONECT 3305 3304 3306 CONECT 3306 3305 3307 CONECT 3307 3306 3308 CONECT 3308 3307 3310 CONECT 3309 3311 3315 CONECT 3310 3308 3312 3315 CONECT 3311 3302 3309 3314 CONECT 3312 3310 CONECT 3313 3302 CONECT 3314 3311 CONECT 3315 3309 3310 CONECT 3316 3323 3325 CONECT 3317 3318 CONECT 3318 3317 3319 CONECT 3319 3318 3320 CONECT 3320 3319 3322 CONECT 3321 3323 3327 CONECT 3322 3320 3324 3327 CONECT 3323 3316 3321 3326 CONECT 3324 3322 CONECT 3325 3316 CONECT 3326 3323 CONECT 3327 3321 3322 CONECT 3328 3329 3330 CONECT 3329 3328 3331 CONECT 3330 3328 CONECT 3331 3329 3333 CONECT 3332 3341 3343 CONECT 3333 3331 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3340 CONECT 3339 3341 3345 CONECT 3340 3338 3342 3345 CONECT 3341 3332 3339 3344 CONECT 3342 3340 CONECT 3343 3332 CONECT 3344 3341 CONECT 3345 3339 3340 CONECT 3346 3347 CONECT 3347 3346 3348 CONECT 3348 3347 3350 CONECT 3349 3358 3360 CONECT 3350 3348 3351 CONECT 3351 3350 3352 CONECT 3352 3351 3353 CONECT 3353 3352 3354 CONECT 3354 3353 3355 CONECT 3355 3354 3357 CONECT 3356 3358 3362 CONECT 3357 3355 3359 3362 CONECT 3358 3349 3356 3361 CONECT 3359 3357 CONECT 3360 3349 CONECT 3361 3358 CONECT 3362 3356 3357 CONECT 3363 3364 3365 3366 CONECT 3364 3363 CONECT 3365 3363 CONECT 3366 3363 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 CONECT 3375 3376 3377 3378 CONECT 3376 3375 CONECT 3377 3375 CONECT 3378 3375 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 CONECT 3391 3392 3393 3394 CONECT 3392 3391 CONECT 3393 3391 CONECT 3394 3391 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 CONECT 3401 3402 3403 3404 CONECT 3402 3401 CONECT 3403 3401 CONECT 3404 3401 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 3408 CONECT 3408 3407 3409 CONECT 3409 3408 3410 CONECT 3410 3409 3411 CONECT 3411 3410 CONECT 3412 3413 3414 3415 CONECT 3413 3412 CONECT 3414 3412 CONECT 3415 3412 3416 CONECT 3416 3415 3417 CONECT 3417 3416 3418 CONECT 3418 3417 3419 CONECT 3419 3418 3420 CONECT 3420 3419 CONECT 3421 3422 3423 3424 CONECT 3422 3421 CONECT 3423 3421 CONECT 3424 3421 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 3428 CONECT 3428 3427 3429 CONECT 3429 3428 CONECT 3430 3431 3432 3433 CONECT 3431 3430 CONECT 3432 3430 CONECT 3433 3430 3434 CONECT 3434 3433 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3437 CONECT 3437 3436 3438 CONECT 3438 3437 3439 CONECT 3439 3438 3440 CONECT 3440 3439 3441 CONECT 3441 3440 CONECT 3442 3443 3444 3445 CONECT 3443 3442 CONECT 3444 3442 CONECT 3445 3442 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 3457 3458 CONECT 3456 3455 CONECT 3457 3455 CONECT 3458 3455 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 CONECT 3466 3467 3468 3469 CONECT 3467 3466 CONECT 3468 3466 CONECT 3469 3466 3470 CONECT 3470 3469 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 3482 CONECT 3482 3481 3483 CONECT 3483 3482 3484 CONECT 3484 3483 3485 CONECT 3485 3484 CONECT 3486 3487 3488 3489 CONECT 3487 3486 CONECT 3488 3486 CONECT 3489 3486 3490 CONECT 3490 3489 3491 CONECT 3491 3490 3492 CONECT 3492 3491 3493 CONECT 3493 3492 3494 CONECT 3494 3493 3495 CONECT 3495 3494 3496 CONECT 3496 3495 3497 CONECT 3497 3496 3498 CONECT 3498 3497 3499 CONECT 3499 3498 3500 CONECT 3500 3499 3501 CONECT 3501 3500 3502 CONECT 3502 3501 3503 CONECT 3503 3502 3504 CONECT 3504 3503 CONECT 3505 3506 3507 CONECT 3506 3505 CONECT 3507 3505 3508 CONECT 3508 3507 3509 CONECT 3509 3508 3510 CONECT 3510 3509 3511 CONECT 3511 3510 CONECT 3512 3513 CONECT 3513 3512 3515 CONECT 3514 3523 3525 CONECT 3515 3513 3516 CONECT 3516 3515 3517 CONECT 3517 3516 3518 CONECT 3518 3517 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3522 CONECT 3521 3523 3527 CONECT 3522 3520 3524 3527 CONECT 3523 3514 3521 3526 CONECT 3524 3522 CONECT 3525 3514 CONECT 3526 3523 CONECT 3527 3521 3522 CONECT 3542 3138 CONECT 3559 3138 CONECT 3609 3138 MASTER 550 0 27 18 2 0 39 6 3533 1 429 35 END