HEADER MEMBRANE PROTEIN 26-JUL-22 8DU3 TITLE CRYSTAL STRUCTURE OF A2AAR-STAR2-BRIL IN COMPLEX WITH COMPOUND 21A COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A, SOLUBLE CYTOCHROME B562 CHIMERA, COMPND 3 SOLUBLE CYTOCHROME B562,ADENOSINE RECEPTOR A2A; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYTOCHROME B-562; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS GPCR, LCP, ANTAGONISTS, ALZHEIMER, PARKINSON, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR A.SHIRIAEVA,B.STAUCH,G.W.HAN,V.CHEREZOV REVDAT 2 24-AUG-22 8DU3 1 JRNL REVDAT 1 10-AUG-22 8DU3 0 JRNL AUTH R.BOLTEAU,R.DUROUX,A.LAVERSIN,B.VREULZ,A.SHIRIAEVA,B.STAUCH, JRNL AUTH 2 G.W.HAN,V.CHEREZOV,N.RENAULT,A.BARCZYK,S.RAVEZ,M.COEVOET, JRNL AUTH 3 P.MELNYK,M.LIBERELLE,S.YOUS JRNL TITL HIGH LIGAND EFFICIENCY QUINAZOLINE COMPOUNDS AS NOVEL A 2A JRNL TITL 2 ADENOSINE RECEPTOR ANTAGONISTS. JRNL REF EUR.J.MED.CHEM. V. 241 14620 2022 JRNL REFN ISSN 0223-5234 JRNL PMID 35933788 JRNL DOI 10.1016/J.EJMECH.2022.114620 REMARK 2 REMARK 2 RESOLUTION. 2.50 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.19.2_4158 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.83 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.9 REMARK 3 NUMBER OF REFLECTIONS : 17798 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.191 REMARK 3 R VALUE (WORKING SET) : 0.189 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.030 REMARK 3 FREE R VALUE TEST SET COUNT : 896 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 42.8300 - 4.5400 0.98 2959 154 0.1962 0.2314 REMARK 3 2 4.5400 - 3.6100 0.99 2829 153 0.1596 0.2099 REMARK 3 3 3.6100 - 3.1500 0.99 2831 159 0.1880 0.2113 REMARK 3 4 3.1500 - 2.8600 1.00 2779 158 0.1887 0.2413 REMARK 3 5 2.8600 - 2.6600 1.00 2796 147 0.2069 0.2603 REMARK 3 6 2.6600 - 2.5000 0.97 2708 125 0.2509 0.3231 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) : 0.240 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.140 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 52.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : NULL NULL REMARK 3 ANGLE : NULL NULL REMARK 3 CHIRALITY : NULL NULL REMARK 3 PLANARITY : NULL NULL REMARK 3 DIHEDRAL : NULL NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 208) REMARK 3 ORIGIN FOR THE GROUP (A): -24.1097 -5.5656 21.0910 REMARK 3 T TENSOR REMARK 3 T11: 0.2264 T22: 0.2790 REMARK 3 T33: 0.2187 T12: -0.0134 REMARK 3 T13: -0.0008 T23: 0.0241 REMARK 3 L TENSOR REMARK 3 L11: 0.3864 L22: 0.4540 REMARK 3 L33: 1.0119 L12: 0.2844 REMARK 3 L13: 0.2110 L23: 0.4907 REMARK 3 S TENSOR REMARK 3 S11: -0.0378 S12: -0.0484 S13: 0.0564 REMARK 3 S21: 0.0168 S22: 0.0391 S23: 0.0141 REMARK 3 S31: 0.0452 S32: -0.1378 S33: -0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1001 THROUGH 1106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.5139 -54.6974 20.0043 REMARK 3 T TENSOR REMARK 3 T11: 0.4832 T22: 0.3772 REMARK 3 T33: 0.8574 T12: 0.0919 REMARK 3 T13: -0.0263 T23: -0.0205 REMARK 3 L TENSOR REMARK 3 L11: 0.1704 L22: 0.4856 REMARK 3 L33: 0.4169 L12: -0.1583 REMARK 3 L13: 0.0146 L23: -0.1166 REMARK 3 S TENSOR REMARK 3 S11: 0.1268 S12: -0.1769 S13: 0.4208 REMARK 3 S21: -0.2746 S22: 0.0516 S23: -0.0045 REMARK 3 S31: -0.2581 S32: -0.0344 S33: 0.3050 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 219 THROUGH 306) REMARK 3 ORIGIN FOR THE GROUP (A): -18.0304 -10.6190 11.0892 REMARK 3 T TENSOR REMARK 3 T11: 0.2910 T22: 0.2532 REMARK 3 T33: 0.2320 T12: -0.0006 REMARK 3 T13: 0.0332 T23: -0.0128 REMARK 3 L TENSOR REMARK 3 L11: 0.3080 L22: 0.1209 REMARK 3 L33: 0.7113 L12: -0.0875 REMARK 3 L13: 0.2799 L23: -0.2135 REMARK 3 S TENSOR REMARK 3 S11: -0.0060 S12: 0.0344 S13: 0.0081 REMARK 3 S21: -0.3349 S22: 0.0145 S23: -0.1387 REMARK 3 S31: 0.0475 S32: 0.0522 S33: 0.0001 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 8DU3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JUL-22. REMARK 100 THE DEPOSITION ID IS D_1000267352. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-NOV-19 REMARK 200 TEMPERATURE (KELVIN) : 123 REMARK 200 PH : 4.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : HKL-2000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 19347 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 5.800 REMARK 200 R MERGE (I) : 0.15600 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 86.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.20 REMARK 200 R MERGE FOR SHELL (I) : 1.02000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.600 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 4EIY REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 51.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM CITRATE PH 4.5, SODIUM REMARK 280 THIOCYANATE, PEG 400, 2,4-HEXANEDIOL, LIPIDIC CUBIC PHASE, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.50000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 70.50000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.80000 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.90000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.80000 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.90000 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.50000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.80000 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.90000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.50000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.80000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.90000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 300 REMARK: THE AUTHOR STATES THAT THE BIOLOGICAL UNIT OF THIS PROTEIN REMARK 300 IS UNKNOWN. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 7450 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21520 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 22.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A -24 REMARK 465 LYS A -23 REMARK 465 THR A -22 REMARK 465 ILE A -21 REMARK 465 ILE A -20 REMARK 465 ALA A -19 REMARK 465 LEU A -18 REMARK 465 SER A -17 REMARK 465 TYR A -16 REMARK 465 ILE A -15 REMARK 465 PHE A -14 REMARK 465 CYS A -13 REMARK 465 LEU A -12 REMARK 465 VAL A -11 REMARK 465 PHE A -10 REMARK 465 ALA A -9 REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 GLY A -1 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 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 ARG A 199 NH1 NH2 REMARK 470 ARG A 206 CD NE CZ NH1 NH2 REMARK 470 LYS A1042 CG CD CE NZ REMARK 470 MET A1058 CG SD CE REMARK 470 LYS A1059 CG CD CE NZ REMARK 470 LYS A1104 CG CD CE NZ REMARK 470 ARG A 220 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 293 CG CD NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -51.88 -130.00 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 3005 REMARK 610 OLC A 3006 REMARK 610 OLC A 3007 REMARK 610 OLC A 3008 REMARK 610 OLA A 3009 REMARK 610 OLA A 3011 REMARK 610 OLA A 3012 REMARK 610 OLA A 3015 REMARK 610 OLA A 3016 REMARK 610 OLA A 3017 REMARK 610 OLA A 3018 REMARK 610 OLA A 3020 REMARK 610 OLA A 3022 REMARK 610 OLA A 3023 REMARK 610 OLA A 3025 DBREF 8DU3 A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 8DU3 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 8DU3 A 219 316 UNP P29274 AA2AR_HUMAN 219 316 SEQADV 8DU3 MET A -24 UNP P29274 INITIATING METHIONINE SEQADV 8DU3 LYS A -23 UNP P29274 EXPRESSION TAG SEQADV 8DU3 THR A -22 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ILE A -21 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ILE A -20 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ALA A -19 UNP P29274 EXPRESSION TAG SEQADV 8DU3 LEU A -18 UNP P29274 EXPRESSION TAG SEQADV 8DU3 SER A -17 UNP P29274 EXPRESSION TAG SEQADV 8DU3 TYR A -16 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ILE A -15 UNP P29274 EXPRESSION TAG SEQADV 8DU3 PHE A -14 UNP P29274 EXPRESSION TAG SEQADV 8DU3 CYS A -13 UNP P29274 EXPRESSION TAG SEQADV 8DU3 LEU A -12 UNP P29274 EXPRESSION TAG SEQADV 8DU3 VAL A -11 UNP P29274 EXPRESSION TAG SEQADV 8DU3 PHE A -10 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 8DU3 TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 8DU3 LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 8DU3 GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 8DU3 ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 8DU3 PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 8DU3 LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 8DU3 ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 8DU3 ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 8DU3 ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 8DU3 ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 8DU3 ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 8DU3 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 8DU3 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 8DU3 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 8DU3 ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 8DU3 ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 8DU3 ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 8DU3 HIS A 317 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 318 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 8DU3 HIS A 326 UNP P29274 EXPRESSION TAG SEQRES 1 A 447 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 447 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO SEQRES 3 A 447 PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU LEU SEQRES 4 A 447 ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL SEQRES 5 A 447 CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL SEQRES 6 A 447 THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE SEQRES 7 A 447 LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SEQRES 8 A 447 SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE SEQRES 9 A 447 ILE ALA CYS PHE VAL LEU VAL LEU ALA GLN SER SER ILE SEQRES 10 A 447 PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA SEQRES 11 A 447 ILE ALA ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY SEQRES 12 A 447 THR ARG ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SEQRES 13 A 447 SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN SEQRES 14 A 447 ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SER GLN SEQRES 15 A 447 GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP SEQRES 16 A 447 VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE SEQRES 17 A 447 ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL SEQRES 18 A 447 TYR LEU ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA SEQRES 19 A 447 ASP LEU GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU SEQRES 20 A 447 LYS VAL ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS SEQRES 21 A 447 ASP ALA LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA SEQRES 22 A 447 GLN LYS ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO SEQRES 23 A 447 ASP SER PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP SEQRES 24 A 447 ILE LEU VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA SEQRES 25 A 447 ASN GLU GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU SEQRES 26 A 447 GLN LEU LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR SEQRES 27 A 447 LEU GLU ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS SEQRES 28 A 447 ALA ALA LYS SER ALA ALA ILE ILE ALA GLY LEU PHE ALA SEQRES 29 A 447 LEU CYS TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR SEQRES 30 A 447 PHE PHE CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU SEQRES 31 A 447 MET TYR LEU ALA ILE VAL LEU ALA HIS THR ASN SER VAL SEQRES 32 A 447 VAL ASN PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE SEQRES 33 A 447 ARG GLN THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU SEQRES 34 A 447 ARG GLN GLN GLU PRO PHE LYS ALA HIS HIS HIS HIS HIS SEQRES 35 A 447 HIS HIS HIS HIS HIS HET TKO A3001 17 HET CLR A3002 28 HET CLR A3003 28 HET CLR A3004 28 HET OLC A3005 23 HET OLC A3006 16 HET OLC A3007 21 HET OLC A3008 20 HET OLA A3009 18 HET OLA A3010 20 HET OLA A3011 11 HET OLA A3012 9 HET OLA A3013 20 HET OLA A3014 20 HET OLA A3015 11 HET OLA A3016 8 HET OLA A3017 7 HET OLA A3018 11 HET OLA A3019 20 HET OLA A3020 11 HET OLA A3021 20 HET OLA A3022 17 HET OLA A3023 13 HET OLA A3024 20 HET OLA A3025 14 HETNAM TKO (4M)-6-BROMO-4-(FURAN-2-YL)QUINAZOLIN-2-AMINE HETNAM CLR CHOLESTEROL HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM OLA OLEIC ACID HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 TKO C12 H8 BR N3 O FORMUL 3 CLR 3(C27 H46 O) FORMUL 6 OLC 4(C21 H40 O4) FORMUL 10 OLA 17(C18 H34 O2) FORMUL 27 HOH *51(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 THR A 68 1 11 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ARG A 111 VAL A 116 1 6 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLN A 157 1 8 HELIX 10 AB1 LEU A 167 VAL A 172 1 6 HELIX 11 AB2 PRO A 173 TYR A 179 1 7 HELIX 12 AB3 VAL A 186 LYS A 1019 1 42 HELIX 13 AB4 ASN A 1022 ALA A 1043 1 22 HELIX 14 AB5 MET A 1058 GLY A 1082 1 25 HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11 HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9 HELIX 17 AB8 TYR A 1101 CYS A 259 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 HIS A 306 1 15 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 CRYST1 39.600 179.800 141.000 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 0.025253 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005562 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007092 0.00000 ATOM 1 N ALA A 0 -22.589 22.249 1.084 1.00 86.80 N ANISOU 1 N ALA A 0 13045 9632 10304 -602 -1113 845 N ATOM 2 CA ALA A 0 -23.707 21.534 0.404 1.00 88.12 C ANISOU 2 CA ALA A 0 13158 9847 10476 -534 -1163 872 C ATOM 3 C ALA A 0 -24.813 21.200 1.403 1.00 98.75 C ANISOU 3 C ALA A 0 14362 11247 11910 -356 -1190 833 C ATOM 4 O ALA A 0 -24.558 21.121 2.605 1.00102.85 O ANISOU 4 O ALA A 0 14789 11804 12487 -308 -1137 780 O ATOM 5 CB ALA A 0 -23.197 20.270 -0.263 1.00 81.37 C ANISOU 5 CB ALA A 0 12222 9103 9591 -644 -1073 873 C ATOM 6 N PRO A 1 -26.036 21.002 0.915 1.00 97.05 N ANISOU 6 N PRO A 1 14128 11042 11705 -263 -1270 855 N ATOM 7 CA PRO A 1 -27.147 20.672 1.817 1.00 93.35 C ANISOU 7 CA PRO A 1 13519 10636 11315 -100 -1295 811 C ATOM 8 C PRO A 1 -26.852 19.408 2.603 1.00 91.99 C ANISOU 8 C PRO A 1 13166 10599 11185 -110 -1178 763 C ATOM 9 O PRO A 1 -26.360 18.418 2.040 1.00 85.83 O ANISOU 9 O PRO A 1 12342 9892 10376 -209 -1107 774 O ATOM 10 CB PRO A 1 -28.336 20.472 0.863 1.00 89.41 C ANISOU 10 CB PRO A 1 13030 10143 10799 -39 -1386 847 C ATOM 11 CG PRO A 1 -27.969 21.215 -0.373 1.00 80.22 C ANISOU 11 CG PRO A 1 12057 8870 9553 -135 -1449 913 C ATOM 12 CD PRO A 1 -26.477 21.098 -0.488 1.00 88.95 C ANISOU 12 CD PRO A 1 13208 9974 10613 -304 -1345 917 C ATOM 13 N PRO A 2 -27.133 19.395 3.911 1.00 99.61 N ANISOU 13 N PRO A 2 14027 11601 12218 -10 -1157 708 N ATOM 14 CA PRO A 2 -26.886 18.172 4.691 1.00 93.67 C ANISOU 14 CA PRO A 2 13113 10975 11504 -18 -1053 665 C ATOM 15 C PRO A 2 -27.836 17.035 4.355 1.00 78.31 C ANISOU 15 C PRO A 2 11054 9131 9569 22 -1051 665 C ATOM 16 O PRO A 2 -27.497 15.873 4.611 1.00 76.66 O ANISOU 16 O PRO A 2 10739 9019 9370 -22 -963 646 O ATOM 17 CB PRO A 2 -27.061 18.639 6.143 1.00 96.89 C ANISOU 17 CB PRO A 2 13460 11382 11973 84 -1049 610 C ATOM 18 CG PRO A 2 -27.976 19.814 6.054 1.00 95.04 C ANISOU 18 CG PRO A 2 13308 11053 11749 192 -1167 616 C ATOM 19 CD PRO A 2 -27.665 20.488 4.746 1.00 93.67 C ANISOU 19 CD PRO A 2 13306 10777 11509 112 -1228 680 C ATOM 20 N ILE A 3 -29.006 17.326 3.781 1.00 76.25 N ANISOU 20 N ILE A 3 10814 8850 9305 103 -1147 684 N ATOM 21 CA ILE A 3 -29.965 16.274 3.465 1.00 69.78 C ANISOU 21 CA ILE A 3 9886 8132 8496 140 -1148 680 C ATOM 22 C ILE A 3 -29.438 15.341 2.381 1.00 68.21 C ANISOU 22 C ILE A 3 9698 7974 8245 13 -1096 719 C ATOM 23 O ILE A 3 -29.876 14.189 2.294 1.00 66.93 O ANISOU 23 O ILE A 3 9427 7912 8091 11 -1056 708 O ATOM 24 CB ILE A 3 -31.311 16.904 3.052 1.00 66.46 C ANISOU 24 CB ILE A 3 9492 7678 8083 257 -1272 688 C ATOM 25 CG1 ILE A 3 -32.387 15.831 2.851 1.00 68.43 C ANISOU 25 CG1 ILE A 3 9612 8044 8345 302 -1271 672 C ATOM 26 CG2 ILE A 3 -31.150 17.743 1.788 1.00 73.34 C ANISOU 26 CG2 ILE A 3 10537 8438 8892 208 -1356 751 C ATOM 27 CD1 ILE A 3 -32.741 15.074 4.116 1.00 79.27 C ANISOU 27 CD1 ILE A 3 10823 9524 9774 359 -1203 608 C ATOM 28 N MET A 4 -28.504 15.807 1.550 1.00 68.01 N ANISOU 28 N MET A 4 9802 7875 8163 -99 -1094 760 N ATOM 29 CA MET A 4 -27.982 14.974 0.473 1.00 61.76 C ANISOU 29 CA MET A 4 9025 7123 7317 -224 -1046 792 C ATOM 30 C MET A 4 -26.994 13.940 1.000 1.00 56.34 C ANISOU 30 C MET A 4 8243 6518 6645 -299 -922 757 C ATOM 31 O MET A 4 -27.131 12.744 0.722 1.00 51.84 O ANISOU 31 O MET A 4 7585 6036 6074 -328 -873 751 O ATOM 32 CB MET A 4 -27.318 15.851 -0.589 1.00 71.05 C ANISOU 32 CB MET A 4 10375 8198 8423 -326 -1085 843 C ATOM 33 CG MET A 4 -28.255 16.856 -1.232 1.00 65.69 C ANISOU 33 CG MET A 4 9810 7428 7721 -256 -1218 884 C ATOM 34 SD MET A 4 -27.394 17.980 -2.349 1.00 68.44 S ANISOU 34 SD MET A 4 10384 7643 7979 -386 -1263 946 S ATOM 35 CE MET A 4 -26.803 16.844 -3.604 1.00 57.33 C ANISOU 35 CE MET A 4 8967 6313 6504 -547 -1188 973 C ATOM 36 N GLY A 5 -25.987 14.385 1.755 1.00 57.19 N ANISOU 36 N GLY A 5 8370 6594 6764 -331 -874 732 N ATOM 37 CA GLY A 5 -25.046 13.446 2.338 1.00 53.37 C ANISOU 37 CA GLY A 5 7794 6186 6298 -389 -765 694 C ATOM 38 C GLY A 5 -25.694 12.509 3.336 1.00 51.07 C ANISOU 38 C GLY A 5 7354 5986 6066 -300 -732 654 C ATOM 39 O GLY A 5 -25.271 11.359 3.482 1.00 45.87 O ANISOU 39 O GLY A 5 6610 5405 5413 -342 -656 633 O ATOM 40 N SER A 6 -26.724 12.982 4.038 1.00 48.31 N ANISOU 40 N SER A 6 6972 5626 5756 -177 -790 640 N ATOM 41 CA SER A 6 -27.431 12.121 4.975 1.00 47.87 C ANISOU 41 CA SER A 6 6778 5661 5750 -99 -761 601 C ATOM 42 C SER A 6 -28.336 11.130 4.255 1.00 41.21 C ANISOU 42 C SER A 6 5876 4889 4895 -95 -770 616 C ATOM 43 O SER A 6 -28.603 10.047 4.785 1.00 42.69 O ANISOU 43 O SER A 6 5953 5163 5105 -82 -718 589 O ATOM 44 CB SER A 6 -28.243 12.969 5.957 1.00 52.36 C ANISOU 44 CB SER A 6 7326 6204 6363 26 -816 572 C ATOM 45 OG SER A 6 -29.255 13.701 5.291 1.00 57.60 O ANISOU 45 OG SER A 6 8046 6821 7017 91 -918 595 O ATOM 46 N SER A 7 -28.811 11.475 3.056 1.00 43.56 N ANISOU 46 N SER A 7 6249 5149 5153 -110 -837 658 N ATOM 47 CA SER A 7 -29.627 10.541 2.286 1.00 48.08 C ANISOU 47 CA SER A 7 6769 5789 5708 -115 -847 673 C ATOM 48 C SER A 7 -28.830 9.302 1.900 1.00 42.96 C ANISOU 48 C SER A 7 6083 5201 5039 -223 -756 673 C ATOM 49 O SER A 7 -29.350 8.181 1.943 1.00 40.81 O ANISOU 49 O SER A 7 5718 5012 4776 -217 -724 660 O ATOM 50 CB SER A 7 -30.175 11.228 1.035 1.00 42.70 C ANISOU 50 CB SER A 7 6191 5051 4984 -117 -940 721 C ATOM 51 OG SER A 7 -31.203 12.142 1.367 1.00 55.26 O ANISOU 51 OG SER A 7 7791 6604 6601 5 -1034 712 O ATOM 52 N VAL A 8 -27.569 9.485 1.504 1.00 37.13 N ANISOU 52 N VAL A 8 5417 4422 4269 -323 -715 685 N ATOM 53 CA VAL A 8 -26.712 8.339 1.208 1.00 43.96 C ANISOU 53 CA VAL A 8 6242 5344 5119 -419 -628 674 C ATOM 54 C VAL A 8 -26.517 7.490 2.458 1.00 42.79 C ANISOU 54 C VAL A 8 5980 5259 5018 -383 -560 627 C ATOM 55 O VAL A 8 -26.672 6.264 2.431 1.00 42.71 O ANISOU 55 O VAL A 8 5895 5321 5014 -399 -515 615 O ATOM 56 CB VAL A 8 -25.366 8.814 0.634 1.00 40.97 C ANISOU 56 CB VAL A 8 5957 4914 4698 -531 -597 684 C ATOM 57 CG1 VAL A 8 -24.408 7.650 0.502 1.00 39.93 C ANISOU 57 CG1 VAL A 8 5770 4845 4558 -616 -505 657 C ATOM 58 CG2 VAL A 8 -25.575 9.493 -0.709 1.00 44.39 C ANISOU 58 CG2 VAL A 8 6508 5289 5071 -584 -661 735 C ATOM 59 N TYR A 9 -26.172 8.134 3.575 1.00 43.45 N ANISOU 59 N TYR A 9 6059 5314 5136 -335 -553 601 N ATOM 60 CA TYR A 9 -25.974 7.397 4.817 1.00 37.45 C ANISOU 60 CA TYR A 9 5201 4610 4418 -301 -494 559 C ATOM 61 C TYR A 9 -27.245 6.664 5.230 1.00 30.76 C ANISOU 61 C TYR A 9 4262 3830 3594 -228 -506 548 C ATOM 62 O TYR A 9 -27.198 5.485 5.600 1.00 32.64 O ANISOU 62 O TYR A 9 4426 4134 3843 -242 -452 529 O ATOM 63 CB TYR A 9 -25.511 8.356 5.916 1.00 43.04 C ANISOU 63 CB TYR A 9 5925 5273 5156 -258 -496 534 C ATOM 64 CG TYR A 9 -25.628 7.799 7.317 1.00 33.40 C ANISOU 64 CG TYR A 9 4607 4105 3978 -199 -456 493 C ATOM 65 CD1 TYR A 9 -24.747 6.829 7.779 1.00 30.90 C ANISOU 65 CD1 TYR A 9 4241 3833 3668 -243 -383 468 C ATOM 66 CD2 TYR A 9 -26.615 8.250 8.180 1.00 38.48 C ANISOU 66 CD2 TYR A 9 5212 4756 4655 -99 -494 475 C ATOM 67 CE1 TYR A 9 -24.856 6.320 9.058 1.00 31.00 C ANISOU 67 CE1 TYR A 9 4175 3889 3713 -193 -352 434 C ATOM 68 CE2 TYR A 9 -26.729 7.749 9.459 1.00 39.64 C ANISOU 68 CE2 TYR A 9 5274 4953 4833 -55 -456 437 C ATOM 69 CZ TYR A 9 -25.850 6.785 9.892 1.00 32.63 C ANISOU 69 CZ TYR A 9 4348 4103 3947 -104 -386 420 C ATOM 70 OH TYR A 9 -25.970 6.290 11.168 1.00 38.09 O ANISOU 70 OH TYR A 9 4967 4841 4665 -63 -354 387 O ATOM 71 N ILE A 10 -28.395 7.337 5.149 1.00 34.95 N ANISOU 71 N ILE A 10 4799 4347 4132 -152 -580 557 N ATOM 72 CA ILE A 10 -29.651 6.713 5.556 1.00 37.99 C ANISOU 72 CA ILE A 10 5091 4806 4538 -85 -591 539 C ATOM 73 C ILE A 10 -30.003 5.559 4.625 1.00 38.55 C ANISOU 73 C ILE A 10 5133 4934 4580 -140 -573 556 C ATOM 74 O ILE A 10 -30.425 4.487 5.076 1.00 32.22 O ANISOU 74 O ILE A 10 4247 4206 3788 -136 -532 535 O ATOM 75 CB ILE A 10 -30.775 7.766 5.606 1.00 36.13 C ANISOU 75 CB ILE A 10 4867 4544 4315 13 -680 537 C ATOM 76 CG1 ILE A 10 -30.543 8.725 6.779 1.00 39.32 C ANISOU 76 CG1 ILE A 10 5278 4907 4756 78 -689 506 C ATOM 77 CG2 ILE A 10 -32.143 7.092 5.719 1.00 32.34 C ANISOU 77 CG2 ILE A 10 4292 4151 3846 68 -698 516 C ATOM 78 CD1 ILE A 10 -31.452 9.941 6.782 1.00 39.04 C ANISOU 78 CD1 ILE A 10 5274 4825 4735 176 -783 501 C ATOM 79 N THR A 11 -29.833 5.753 3.315 1.00 38.69 N ANISOU 79 N THR A 11 5225 4917 4557 -197 -602 595 N ATOM 80 CA THR A 11 -30.158 4.695 2.364 1.00 39.90 C ANISOU 80 CA THR A 11 5355 5124 4680 -254 -586 611 C ATOM 81 C THR A 11 -29.287 3.465 2.593 1.00 39.40 C ANISOU 81 C THR A 11 5251 5102 4618 -323 -496 593 C ATOM 82 O THR A 11 -29.764 2.328 2.495 1.00 35.49 O ANISOU 82 O THR A 11 4693 4672 4119 -338 -467 585 O ATOM 83 CB THR A 11 -29.996 5.209 0.933 1.00 35.92 C ANISOU 83 CB THR A 11 4950 4570 4128 -311 -631 656 C ATOM 84 OG1 THR A 11 -30.755 6.411 0.765 1.00 40.42 O ANISOU 84 OG1 THR A 11 5571 5088 4697 -239 -724 673 O ATOM 85 CG2 THR A 11 -30.488 4.183 -0.063 1.00 38.16 C ANISOU 85 CG2 THR A 11 5207 4911 4380 -361 -623 671 C ATOM 86 N VAL A 12 -28.005 3.670 2.897 1.00 40.96 N ANISOU 86 N VAL A 12 5481 5262 4819 -365 -453 583 N ATOM 87 CA VAL A 12 -27.122 2.539 3.157 1.00 38.33 C ANISOU 87 CA VAL A 12 5108 4964 4489 -420 -375 559 C ATOM 88 C VAL A 12 -27.513 1.845 4.456 1.00 33.76 C ANISOU 88 C VAL A 12 4444 4435 3948 -363 -345 527 C ATOM 89 O VAL A 12 -27.518 0.611 4.538 1.00 35.15 O ANISOU 89 O VAL A 12 4572 4661 4124 -389 -301 514 O ATOM 90 CB VAL A 12 -25.656 3.007 3.181 1.00 41.99 C ANISOU 90 CB VAL A 12 5624 5382 4948 -475 -341 548 C ATOM 91 CG1 VAL A 12 -24.745 1.887 3.677 1.00 40.23 C ANISOU 91 CG1 VAL A 12 5350 5198 4739 -509 -267 513 C ATOM 92 CG2 VAL A 12 -25.231 3.479 1.798 1.00 32.33 C ANISOU 92 CG2 VAL A 12 4487 4122 3676 -556 -359 578 C ATOM 93 N GLU A 13 -27.844 2.622 5.491 1.00 34.50 N ANISOU 93 N GLU A 13 4522 4514 4071 -288 -368 512 N ATOM 94 CA GLU A 13 -28.265 2.029 6.757 1.00 29.76 C ANISOU 94 CA GLU A 13 3845 3963 3501 -239 -341 481 C ATOM 95 C GLU A 13 -29.494 1.148 6.572 1.00 29.14 C ANISOU 95 C GLU A 13 3706 3952 3413 -227 -347 481 C ATOM 96 O GLU A 13 -29.560 0.038 7.113 1.00 31.22 O ANISOU 96 O GLU A 13 3919 4263 3679 -242 -301 464 O ATOM 97 CB GLU A 13 -28.548 3.127 7.783 1.00 31.05 C ANISOU 97 CB GLU A 13 4003 4102 3694 -160 -372 463 C ATOM 98 CG GLU A 13 -27.314 3.863 8.282 1.00 34.95 C ANISOU 98 CG GLU A 13 4542 4539 4199 -170 -354 453 C ATOM 99 CD GLU A 13 -26.583 3.108 9.382 1.00 41.46 C ANISOU 99 CD GLU A 13 5321 5391 5042 -177 -294 422 C ATOM 100 OE1 GLU A 13 -26.433 1.873 9.264 1.00 41.40 O ANISOU 100 OE1 GLU A 13 5281 5424 5024 -216 -254 419 O ATOM 101 OE2 GLU A 13 -26.162 3.750 10.369 1.00 37.64 O ANISOU 101 OE2 GLU A 13 4837 4885 4579 -143 -289 400 O ATOM 102 N LEU A 14 -30.480 1.625 5.808 1.00 28.87 N ANISOU 102 N LEU A 14 3681 3922 3365 -203 -405 499 N ATOM 103 CA LEU A 14 -31.700 0.849 5.609 1.00 31.98 C ANISOU 103 CA LEU A 14 4013 4388 3750 -194 -413 494 C ATOM 104 C LEU A 14 -31.428 -0.420 4.811 1.00 30.99 C ANISOU 104 C LEU A 14 3886 4291 3595 -276 -370 507 C ATOM 105 O LEU A 14 -32.035 -1.465 5.070 1.00 27.81 O ANISOU 105 O LEU A 14 3426 3951 3188 -288 -342 492 O ATOM 106 CB LEU A 14 -32.753 1.704 4.911 1.00 36.64 C ANISOU 106 CB LEU A 14 4615 4975 4332 -145 -492 507 C ATOM 107 CG LEU A 14 -33.304 2.869 5.732 1.00 41.25 C ANISOU 107 CG LEU A 14 5186 5542 4946 -48 -542 484 C ATOM 108 CD1 LEU A 14 -34.117 3.805 4.848 1.00 41.68 C ANISOU 108 CD1 LEU A 14 5276 5571 4990 -1 -632 502 C ATOM 109 CD2 LEU A 14 -34.145 2.352 6.892 1.00 39.54 C ANISOU 109 CD2 LEU A 14 4871 5404 4750 -3 -518 439 C ATOM 110 N ALA A 15 -30.528 -0.349 3.829 1.00 29.35 N ANISOU 110 N ALA A 15 3744 4041 3367 -339 -364 531 N ATOM 111 CA ALA A 15 -30.162 -1.550 3.087 1.00 29.87 C ANISOU 111 CA ALA A 15 3810 4132 3409 -417 -320 536 C ATOM 112 C ALA A 15 -29.515 -2.579 4.007 1.00 34.00 C ANISOU 112 C ALA A 15 4297 4673 3948 -433 -255 508 C ATOM 113 O ALA A 15 -29.785 -3.781 3.894 1.00 30.02 O ANISOU 113 O ALA A 15 3762 4211 3433 -466 -224 501 O ATOM 114 CB ALA A 15 -29.226 -1.185 1.934 1.00 29.59 C ANISOU 114 CB ALA A 15 3849 4048 3345 -483 -322 559 C ATOM 115 N ILE A 16 -28.667 -2.123 4.932 1.00 31.23 N ANISOU 115 N ILE A 16 3955 4289 3623 -408 -238 491 N ATOM 116 CA ILE A 16 -28.037 -3.030 5.887 1.00 32.43 C ANISOU 116 CA ILE A 16 4078 4453 3791 -414 -185 464 C ATOM 117 C ILE A 16 -29.080 -3.648 6.809 1.00 35.90 C ANISOU 117 C ILE A 16 4458 4946 4238 -378 -180 451 C ATOM 118 O ILE A 16 -29.033 -4.848 7.107 1.00 34.89 O ANISOU 118 O ILE A 16 4309 4843 4102 -406 -142 440 O ATOM 119 CB ILE A 16 -26.956 -2.283 6.689 1.00 30.17 C ANISOU 119 CB ILE A 16 3812 4123 3529 -391 -175 448 C ATOM 120 CG1 ILE A 16 -25.801 -1.883 5.775 1.00 36.80 C ANISOU 120 CG1 ILE A 16 4707 4920 4355 -446 -167 453 C ATOM 121 CG2 ILE A 16 -26.455 -3.139 7.839 1.00 31.93 C ANISOU 121 CG2 ILE A 16 4003 4361 3769 -381 -133 420 C ATOM 122 CD1 ILE A 16 -24.951 -0.778 6.342 1.00 39.91 C ANISOU 122 CD1 ILE A 16 5130 5269 4766 -427 -172 442 C ATOM 123 N ALA A 17 -30.025 -2.838 7.293 1.00 35.18 N ANISOU 123 N ALA A 17 4340 4869 4156 -318 -217 448 N ATOM 124 CA ALA A 17 -31.058 -3.366 8.176 1.00 40.44 C ANISOU 124 CA ALA A 17 4944 5596 4824 -291 -208 428 C ATOM 125 C ALA A 17 -31.824 -4.500 7.507 1.00 37.24 C ANISOU 125 C ALA A 17 4516 5243 4390 -339 -196 434 C ATOM 126 O ALA A 17 -32.066 -5.544 8.123 1.00 39.13 O ANISOU 126 O ALA A 17 4727 5520 4620 -362 -160 419 O ATOM 127 CB ALA A 17 -32.010 -2.246 8.595 1.00 29.63 C ANISOU 127 CB ALA A 17 3546 4242 3470 -218 -256 416 C ATOM 128 N VAL A 18 -32.204 -4.318 6.240 1.00 39.13 N ANISOU 128 N VAL A 18 4772 5485 4611 -360 -227 455 N ATOM 129 CA VAL A 18 -32.947 -5.352 5.525 1.00 38.00 C ANISOU 129 CA VAL A 18 4607 5393 4439 -409 -218 460 C ATOM 130 C VAL A 18 -32.145 -6.646 5.478 1.00 35.16 C ANISOU 130 C VAL A 18 4267 5024 4068 -473 -163 458 C ATOM 131 O VAL A 18 -32.665 -7.732 5.759 1.00 34.38 O ANISOU 131 O VAL A 18 4141 4969 3954 -503 -135 447 O ATOM 132 CB VAL A 18 -33.310 -4.865 4.111 1.00 37.64 C ANISOU 132 CB VAL A 18 4586 5342 4372 -422 -264 486 C ATOM 133 CG1 VAL A 18 -33.880 -6.005 3.283 1.00 41.44 C ANISOU 133 CG1 VAL A 18 5052 5872 4821 -484 -248 490 C ATOM 134 CG2 VAL A 18 -34.300 -3.719 4.190 1.00 39.45 C ANISOU 134 CG2 VAL A 18 4792 5587 4611 -350 -327 482 C ATOM 135 N LEU A 19 -30.865 -6.551 5.114 1.00 34.09 N ANISOU 135 N LEU A 19 4180 4833 3939 -496 -148 465 N ATOM 136 CA LEU A 19 -30.036 -7.748 5.024 1.00 34.92 C ANISOU 136 CA LEU A 19 4304 4926 4038 -548 -102 456 C ATOM 137 C LEU A 19 -29.807 -8.368 6.398 1.00 39.68 C ANISOU 137 C LEU A 19 4890 5530 4655 -529 -71 435 C ATOM 138 O LEU A 19 -29.786 -9.597 6.535 1.00 36.93 O ANISOU 138 O LEU A 19 4545 5194 4295 -565 -41 427 O ATOM 139 CB LEU A 19 -28.706 -7.407 4.354 1.00 37.51 C ANISOU 139 CB LEU A 19 4680 5203 4371 -574 -93 458 C ATOM 140 CG LEU A 19 -28.797 -6.940 2.898 1.00 41.83 C ANISOU 140 CG LEU A 19 5257 5745 4894 -612 -118 480 C ATOM 141 CD1 LEU A 19 -27.447 -6.425 2.424 1.00 44.20 C ANISOU 141 CD1 LEU A 19 5602 5997 5195 -640 -107 476 C ATOM 142 CD2 LEU A 19 -29.288 -8.062 1.987 1.00 37.77 C ANISOU 142 CD2 LEU A 19 4736 5265 4349 -670 -104 484 C ATOM 143 N ALA A 20 -29.638 -7.535 7.429 1.00 38.93 N ANISOU 143 N ALA A 20 4786 5423 4585 -474 -80 426 N ATOM 144 CA ALA A 20 -29.421 -8.058 8.775 1.00 36.75 C ANISOU 144 CA ALA A 20 4498 5149 4318 -456 -55 408 C ATOM 145 C ALA A 20 -30.632 -8.840 9.266 1.00 37.06 C ANISOU 145 C ALA A 20 4502 5245 4334 -470 -45 402 C ATOM 146 O ALA A 20 -30.488 -9.864 9.945 1.00 37.18 O ANISOU 146 O ALA A 20 4526 5263 4339 -493 -17 394 O ATOM 147 CB ALA A 20 -29.107 -6.914 9.738 1.00 34.42 C ANISOU 147 CB ALA A 20 4196 4833 4049 -397 -69 397 C ATOM 148 N ILE A 21 -31.835 -8.368 8.937 1.00 33.39 N ANISOU 148 N ILE A 21 3999 4828 3859 -459 -71 405 N ATOM 149 CA ILE A 21 -33.051 -9.052 9.366 1.00 39.03 C ANISOU 149 CA ILE A 21 4670 5610 4548 -479 -59 392 C ATOM 150 C ILE A 21 -33.250 -10.335 8.567 1.00 40.40 C ANISOU 150 C ILE A 21 4860 5799 4691 -550 -38 401 C ATOM 151 O ILE A 21 -33.522 -11.402 9.130 1.00 36.47 O ANISOU 151 O ILE A 21 4365 5322 4171 -590 -8 393 O ATOM 152 CB ILE A 21 -34.264 -8.113 9.232 1.00 37.27 C ANISOU 152 CB ILE A 21 4393 5440 4326 -437 -97 382 C ATOM 153 CG1 ILE A 21 -34.116 -6.920 10.177 1.00 34.47 C ANISOU 153 CG1 ILE A 21 4023 5071 4003 -365 -116 367 C ATOM 154 CG2 ILE A 21 -35.553 -8.867 9.522 1.00 37.69 C ANISOU 154 CG2 ILE A 21 4395 5578 4349 -470 -83 362 C ATOM 155 CD1 ILE A 21 -35.053 -5.767 9.864 1.00 36.53 C ANISOU 155 CD1 ILE A 21 4244 5361 4274 -307 -167 356 C ATOM 156 N LEU A 22 -33.119 -10.251 7.242 1.00 40.24 N ANISOU 156 N LEU A 22 4857 5766 4666 -572 -53 418 N ATOM 157 CA LEU A 22 -33.354 -11.417 6.398 1.00 38.37 C ANISOU 157 CA LEU A 22 4635 5546 4400 -641 -34 424 C ATOM 158 C LEU A 22 -32.393 -12.547 6.740 1.00 36.71 C ANISOU 158 C LEU A 22 4470 5291 4187 -675 3 419 C ATOM 159 O LEU A 22 -32.813 -13.678 7.011 1.00 36.26 O ANISOU 159 O LEU A 22 4418 5253 4104 -720 27 413 O ATOM 160 CB LEU A 22 -33.220 -11.031 4.925 1.00 41.63 C ANISOU 160 CB LEU A 22 5063 5947 4807 -658 -58 442 C ATOM 161 CG LEU A 22 -34.355 -10.197 4.326 1.00 44.32 C ANISOU 161 CG LEU A 22 5364 6336 5138 -635 -103 448 C ATOM 162 CD1 LEU A 22 -33.969 -9.691 2.945 1.00 40.15 C ANISOU 162 CD1 LEU A 22 4872 5780 4603 -650 -130 472 C ATOM 163 CD2 LEU A 22 -35.639 -11.012 4.259 1.00 40.35 C ANISOU 163 CD2 LEU A 22 4817 5910 4603 -673 -95 436 C ATOM 164 N GLY A 23 -31.092 -12.259 6.733 1.00 37.62 N ANISOU 164 N GLY A 23 4620 5345 4327 -654 5 419 N ATOM 165 CA GLY A 23 -30.116 -13.316 6.937 1.00 34.12 C ANISOU 165 CA GLY A 23 4220 4859 3886 -678 32 409 C ATOM 166 C GLY A 23 -30.244 -13.973 8.296 1.00 33.03 C ANISOU 166 C GLY A 23 4088 4720 3741 -671 48 399 C ATOM 167 O GLY A 23 -30.209 -15.200 8.411 1.00 31.97 O ANISOU 167 O GLY A 23 3986 4575 3588 -711 67 395 O ATOM 168 N ASN A 24 -30.404 -13.167 9.344 1.00 35.22 N ANISOU 168 N ASN A 24 4342 5008 4033 -624 39 396 N ATOM 169 CA ASN A 24 -30.409 -13.717 10.693 1.00 38.32 C ANISOU 169 CA ASN A 24 4747 5397 4417 -619 54 387 C ATOM 170 C ASN A 24 -31.747 -14.343 11.056 1.00 34.54 C ANISOU 170 C ASN A 24 4248 4978 3898 -663 66 386 C ATOM 171 O ASN A 24 -31.788 -15.265 11.878 1.00 32.89 O ANISOU 171 O ASN A 24 4071 4762 3665 -692 84 384 O ATOM 172 CB ASN A 24 -30.030 -12.631 11.697 1.00 34.29 C ANISOU 172 CB ASN A 24 4219 4877 3933 -557 42 379 C ATOM 173 CG ASN A 24 -28.565 -12.278 11.622 1.00 31.27 C ANISOU 173 CG ASN A 24 3865 4434 3583 -524 37 374 C ATOM 174 OD1 ASN A 24 -27.709 -13.054 12.046 1.00 33.69 O ANISOU 174 OD1 ASN A 24 4208 4700 3890 -526 46 365 O ATOM 175 ND2 ASN A 24 -28.263 -11.115 11.064 1.00 34.56 N ANISOU 175 ND2 ASN A 24 4266 4843 4024 -496 20 375 N ATOM 176 N VAL A 25 -32.846 -13.872 10.463 1.00 35.91 N ANISOU 176 N VAL A 25 4370 5212 4060 -672 56 386 N ATOM 177 CA VAL A 25 -34.108 -14.586 10.619 1.00 41.30 C ANISOU 177 CA VAL A 25 5030 5961 4701 -727 72 379 C ATOM 178 C VAL A 25 -33.988 -15.986 10.038 1.00 36.03 C ANISOU 178 C VAL A 25 4413 5272 4005 -797 93 387 C ATOM 179 O VAL A 25 -34.611 -16.932 10.533 1.00 43.53 O ANISOU 179 O VAL A 25 5378 6248 4915 -854 115 382 O ATOM 180 CB VAL A 25 -35.260 -13.798 9.966 1.00 38.20 C ANISOU 180 CB VAL A 25 4568 5641 4306 -716 51 371 C ATOM 181 CG1 VAL A 25 -36.485 -14.688 9.798 1.00 35.79 C ANISOU 181 CG1 VAL A 25 4237 5408 3953 -787 70 360 C ATOM 182 CG2 VAL A 25 -35.601 -12.579 10.806 1.00 37.53 C ANISOU 182 CG2 VAL A 25 4433 5585 4243 -649 33 354 C ATOM 183 N LEU A 26 -33.175 -16.147 8.993 1.00 39.05 N ANISOU 183 N LEU A 26 4826 5607 4404 -799 87 396 N ATOM 184 CA LEU A 26 -32.983 -17.463 8.397 1.00 40.96 C ANISOU 184 CA LEU A 26 5118 5823 4622 -861 104 399 C ATOM 185 C LEU A 26 -32.175 -18.371 9.316 1.00 40.01 C ANISOU 185 C LEU A 26 5064 5641 4499 -864 116 396 C ATOM 186 O LEU A 26 -32.441 -19.576 9.397 1.00 44.09 O ANISOU 186 O LEU A 26 5624 6146 4981 -922 132 396 O ATOM 187 CB LEU A 26 -32.294 -17.317 7.042 1.00 43.74 C ANISOU 187 CB LEU A 26 5481 6145 4993 -860 95 403 C ATOM 188 CG LEU A 26 -32.479 -18.468 6.054 1.00 56.35 C ANISOU 188 CG LEU A 26 7108 7741 6563 -929 110 402 C ATOM 189 CD1 LEU A 26 -33.916 -18.520 5.565 1.00 49.33 C ANISOU 189 CD1 LEU A 26 6174 6931 5638 -976 111 405 C ATOM 190 CD2 LEU A 26 -31.512 -18.322 4.887 1.00 65.42 C ANISOU 190 CD2 LEU A 26 8273 8852 7732 -924 105 400 C ATOM 191 N VAL A 27 -31.181 -17.815 10.012 1.00 39.00 N ANISOU 191 N VAL A 27 4946 5467 4403 -803 106 392 N ATOM 192 CA VAL A 27 -30.401 -18.610 10.960 1.00 37.16 C ANISOU 192 CA VAL A 27 4775 5176 4168 -796 108 388 C ATOM 193 C VAL A 27 -31.310 -19.167 12.048 1.00 40.44 C ANISOU 193 C VAL A 27 5206 5620 4539 -836 121 393 C ATOM 194 O VAL A 27 -31.244 -20.353 12.392 1.00 39.36 O ANISOU 194 O VAL A 27 5136 5447 4371 -879 128 396 O ATOM 195 CB VAL A 27 -29.258 -17.767 11.558 1.00 35.73 C ANISOU 195 CB VAL A 27 4591 4955 4029 -721 92 380 C ATOM 196 CG1 VAL A 27 -28.598 -18.495 12.733 1.00 34.23 C ANISOU 196 CG1 VAL A 27 4461 4713 3832 -707 88 377 C ATOM 197 CG2 VAL A 27 -28.224 -17.442 10.491 1.00 31.95 C ANISOU 197 CG2 VAL A 27 4110 4443 3585 -697 85 370 C ATOM 198 N CYS A 28 -32.178 -18.317 12.603 1.00 37.66 N ANISOU 198 N CYS A 28 4794 5333 4181 -826 124 390 N ATOM 199 CA CYS A 28 -33.087 -18.767 13.652 1.00 39.18 C ANISOU 199 CA CYS A 28 4993 5567 4326 -873 142 387 C ATOM 200 C CYS A 28 -34.080 -19.792 13.118 1.00 46.13 C ANISOU 200 C CYS A 28 5886 6485 5158 -963 162 388 C ATOM 201 O CYS A 28 -34.375 -20.788 13.788 1.00 43.91 O ANISOU 201 O CYS A 28 5660 6194 4829 -1024 178 391 O ATOM 202 CB CYS A 28 -33.829 -17.573 14.252 1.00 41.82 C ANISOU 202 CB CYS A 28 5249 5974 4668 -840 141 373 C ATOM 203 SG CYS A 28 -32.773 -16.376 15.097 1.00 37.43 S ANISOU 203 SG CYS A 28 4682 5378 4162 -744 121 369 S ATOM 204 N TRP A 29 -34.607 -19.561 11.913 1.00 50.07 N ANISOU 204 N TRP A 29 6337 7024 5661 -977 161 385 N ATOM 205 CA TRP A 29 -35.555 -20.503 11.329 1.00 52.85 C ANISOU 205 CA TRP A 29 6696 7418 5967 -1064 181 383 C ATOM 206 C TRP A 29 -34.889 -21.835 11.007 1.00 46.92 C ANISOU 206 C TRP A 29 6040 6588 5200 -1107 186 394 C ATOM 207 O TRP A 29 -35.554 -22.877 11.013 1.00 46.30 O ANISOU 207 O TRP A 29 5999 6523 5071 -1191 206 393 O ATOM 208 CB TRP A 29 -36.185 -19.890 10.077 1.00 52.16 C ANISOU 208 CB TRP A 29 6537 7389 5891 -1060 171 378 C ATOM 209 CG TRP A 29 -37.410 -20.611 9.587 1.00 70.80 C ANISOU 209 CG TRP A 29 8879 9821 8202 -1147 190 368 C ATOM 210 CD1 TRP A 29 -37.542 -21.295 8.414 1.00 72.95 C ANISOU 210 CD1 TRP A 29 9169 10090 8460 -1197 194 372 C ATOM 211 CD2 TRP A 29 -38.674 -20.718 10.258 1.00 77.44 C ANISOU 211 CD2 TRP A 29 9674 10752 8997 -1200 211 346 C ATOM 212 NE1 TRP A 29 -38.808 -21.819 8.310 1.00 77.28 N ANISOU 212 NE1 TRP A 29 9687 10720 8958 -1277 215 357 N ATOM 213 CE2 TRP A 29 -39.522 -21.482 9.430 1.00 90.91 C ANISOU 213 CE2 TRP A 29 11372 12506 10662 -1282 226 339 C ATOM 214 CE3 TRP A 29 -39.170 -20.245 11.476 1.00 76.90 C ANISOU 214 CE3 TRP A 29 9569 10733 8916 -1190 220 328 C ATOM 215 CZ2 TRP A 29 -40.837 -21.783 9.782 1.00 93.03 C ANISOU 215 CZ2 TRP A 29 11594 12874 10878 -1355 250 311 C ATOM 216 CZ3 TRP A 29 -40.477 -20.546 11.824 1.00 80.67 C ANISOU 216 CZ3 TRP A 29 9999 11310 9340 -1263 245 299 C ATOM 217 CH2 TRP A 29 -41.295 -21.306 10.980 1.00 82.41 C ANISOU 217 CH2 TRP A 29 10210 11580 9521 -1345 260 290 C ATOM 218 N ALA A 30 -33.581 -21.828 10.740 1.00 43.61 N ANISOU 218 N ALA A 30 5660 6087 4822 -1052 168 399 N ATOM 219 CA ALA A 30 -32.876 -23.080 10.486 1.00 40.97 C ANISOU 219 CA ALA A 30 5416 5674 4479 -1080 168 401 C ATOM 220 C ALA A 30 -32.684 -23.876 11.771 1.00 46.16 C ANISOU 220 C ALA A 30 6153 6282 5104 -1098 167 407 C ATOM 221 O ALA A 30 -32.871 -25.099 11.784 1.00 45.40 O ANISOU 221 O ALA A 30 6132 6150 4967 -1162 175 411 O ATOM 222 CB ALA A 30 -31.527 -22.797 9.827 1.00 41.56 C ANISOU 222 CB ALA A 30 5499 5686 4607 -1013 149 393 C ATOM 223 N VAL A 31 -32.310 -23.203 12.861 1.00 46.33 N ANISOU 223 N VAL A 31 6165 6297 5141 -1044 157 409 N ATOM 224 CA VAL A 31 -32.111 -23.903 14.127 1.00 47.36 C ANISOU 224 CA VAL A 31 6376 6381 5237 -1061 152 417 C ATOM 225 C VAL A 31 -33.441 -24.382 14.696 1.00 45.91 C ANISOU 225 C VAL A 31 6201 6259 4985 -1157 180 421 C ATOM 226 O VAL A 31 -33.493 -25.406 15.387 1.00 51.01 O ANISOU 226 O VAL A 31 6940 6862 5581 -1212 181 432 O ATOM 227 CB VAL A 31 -31.366 -22.996 15.125 1.00 45.30 C ANISOU 227 CB VAL A 31 6098 6105 5010 -980 134 416 C ATOM 228 CG1 VAL A 31 -31.306 -23.644 16.501 1.00 45.07 C ANISOU 228 CG1 VAL A 31 6150 6039 4937 -1004 128 427 C ATOM 229 CG2 VAL A 31 -29.963 -22.692 14.622 1.00 45.95 C ANISOU 229 CG2 VAL A 31 6183 6124 5154 -897 107 406 C ATOM 230 N TRP A 32 -34.532 -23.664 14.421 1.00 46.93 N ANISOU 230 N TRP A 32 6235 6490 5105 -1180 201 410 N ATOM 231 CA TRP A 32 -35.832 -24.083 14.933 1.00 55.03 C ANISOU 231 CA TRP A 32 7254 7590 6063 -1276 232 403 C ATOM 232 C TRP A 32 -36.285 -25.391 14.295 1.00 56.22 C ANISOU 232 C TRP A 32 7469 7725 6166 -1373 248 408 C ATOM 233 O TRP A 32 -36.855 -26.254 14.973 1.00 65.88 O ANISOU 233 O TRP A 32 8756 8952 7323 -1462 267 411 O ATOM 234 CB TRP A 32 -36.869 -22.987 14.689 1.00 54.84 C ANISOU 234 CB TRP A 32 7105 7685 6049 -1267 245 380 C ATOM 235 CG TRP A 32 -38.255 -23.360 15.125 1.00 60.78 C ANISOU 235 CG TRP A 32 7830 8532 6732 -1367 280 361 C ATOM 236 CD1 TRP A 32 -39.191 -24.034 14.394 1.00 63.84 C ANISOU 236 CD1 TRP A 32 8206 8972 7077 -1455 302 350 C ATOM 237 CD2 TRP A 32 -38.864 -23.077 16.390 1.00 75.34 C ANISOU 237 CD2 TRP A 32 9652 10437 8538 -1394 300 343 C ATOM 238 NE1 TRP A 32 -40.343 -24.189 15.126 1.00 67.92 N ANISOU 238 NE1 TRP A 32 8692 9582 7532 -1537 335 325 N ATOM 239 CE2 TRP A 32 -40.168 -23.611 16.356 1.00 74.63 C ANISOU 239 CE2 TRP A 32 9534 10440 8383 -1503 335 319 C ATOM 240 CE3 TRP A 32 -38.432 -22.425 17.550 1.00 80.09 C ANISOU 240 CE3 TRP A 32 10251 11027 9152 -1342 292 341 C ATOM 241 CZ2 TRP A 32 -41.044 -23.513 17.435 1.00 78.81 C ANISOU 241 CZ2 TRP A 32 10032 11054 8857 -1563 365 291 C ATOM 242 CZ3 TRP A 32 -39.304 -22.328 18.621 1.00 81.79 C ANISOU 242 CZ3 TRP A 32 10438 11323 9314 -1398 321 316 C ATOM 243 CH2 TRP A 32 -40.595 -22.868 18.555 1.00 79.53 C ANISOU 243 CH2 TRP A 32 10124 11132 8963 -1509 358 290 C ATOM 244 N LEU A 33 -36.039 -25.560 12.997 1.00 50.25 N ANISOU 244 N LEU A 33 6703 6951 5438 -1362 241 407 N ATOM 245 CA LEU A 33 -36.551 -26.708 12.259 1.00 55.90 C ANISOU 245 CA LEU A 33 7468 7661 6111 -1454 257 407 C ATOM 246 C LEU A 33 -35.642 -27.928 12.367 1.00 57.32 C ANISOU 246 C LEU A 33 7780 7718 6280 -1466 241 421 C ATOM 247 O LEU A 33 -36.106 -29.022 12.701 1.00 73.23 O ANISOU 247 O LEU A 33 9880 9712 8233 -1558 254 428 O ATOM 248 CB LEU A 33 -36.739 -26.336 10.785 1.00 55.40 C ANISOU 248 CB LEU A 33 7333 7637 6079 -1441 256 398 C ATOM 249 CG LEU A 33 -37.771 -25.253 10.475 1.00 62.38 C ANISOU 249 CG LEU A 33 8091 8642 6968 -1434 265 382 C ATOM 250 CD1 LEU A 33 -37.682 -24.854 9.010 1.00 65.16 C ANISOU 250 CD1 LEU A 33 8392 9009 7355 -1406 252 379 C ATOM 251 CD2 LEU A 33 -39.177 -25.721 10.818 1.00 60.53 C ANISOU 251 CD2 LEU A 33 7834 8500 6664 -1539 297 365 C ATOM 252 N ASN A 34 -34.354 -27.762 12.081 1.00 47.33 N ANISOU 252 N ASN A 34 6537 6373 5074 -1375 210 423 N ATOM 253 CA ASN A 34 -33.442 -28.893 12.010 1.00 49.02 C ANISOU 253 CA ASN A 34 6866 6471 5287 -1371 188 427 C ATOM 254 C ASN A 34 -32.946 -29.270 13.402 1.00 58.08 C ANISOU 254 C ASN A 34 8105 7551 6414 -1356 166 441 C ATOM 255 O ASN A 34 -32.411 -28.428 14.131 1.00 57.62 O ANISOU 255 O ASN A 34 8014 7494 6387 -1282 151 443 O ATOM 256 CB ASN A 34 -32.266 -28.556 11.094 1.00 51.09 C ANISOU 256 CB ASN A 34 7105 6688 5621 -1281 165 412 C ATOM 257 CG ASN A 34 -31.376 -29.750 10.823 1.00 52.13 C ANISOU 257 CG ASN A 34 7343 6708 5756 -1273 141 404 C ATOM 258 OD1 ASN A 34 -31.611 -30.845 11.334 1.00 56.32 O ANISOU 258 OD1 ASN A 34 7978 7185 6236 -1332 136 414 O ATOM 259 ND2 ASN A 34 -30.346 -29.546 10.010 1.00 45.02 N ANISOU 259 ND2 ASN A 34 6421 5773 4913 -1203 124 382 N ATOM 260 N SER A 35 -33.123 -30.544 13.766 1.00 59.90 N ANISOU 260 N SER A 35 8455 7717 6586 -1429 162 453 N ATOM 261 CA SER A 35 -32.704 -31.028 15.077 1.00 63.40 C ANISOU 261 CA SER A 35 9004 8088 6997 -1426 136 471 C ATOM 262 C SER A 35 -31.199 -31.240 15.177 1.00 62.92 C ANISOU 262 C SER A 35 9002 7915 6988 -1319 84 465 C ATOM 263 O SER A 35 -30.658 -31.205 16.288 1.00 59.19 O ANISOU 263 O SER A 35 8584 7396 6510 -1279 54 477 O ATOM 264 CB SER A 35 -33.421 -32.338 15.412 1.00 69.65 C ANISOU 264 CB SER A 35 9917 8843 7702 -1548 146 486 C ATOM 265 OG SER A 35 -34.802 -32.119 15.634 1.00 89.87 O ANISOU 265 OG SER A 35 12425 11517 10206 -1651 195 486 O ATOM 266 N ASN A 36 -30.513 -31.468 14.054 1.00 49.43 N ANISOU 266 N ASN A 36 7285 6167 5329 -1272 71 444 N ATOM 267 CA ASN A 36 -29.061 -31.586 14.093 1.00 57.63 C ANISOU 267 CA ASN A 36 8360 7115 6423 -1164 22 426 C ATOM 268 C ASN A 36 -28.390 -30.261 14.430 1.00 60.24 C ANISOU 268 C ASN A 36 8593 7484 6811 -1068 15 417 C ATOM 269 O ASN A 36 -27.234 -30.259 14.868 1.00 62.49 O ANISOU 269 O ASN A 36 8909 7703 7132 -980 -27 404 O ATOM 270 CB ASN A 36 -28.531 -32.104 12.756 1.00 60.84 C ANISOU 270 CB ASN A 36 8766 7483 6866 -1144 17 396 C ATOM 271 CG ASN A 36 -29.049 -33.488 12.419 1.00 64.60 C ANISOU 271 CG ASN A 36 9352 7904 7289 -1232 19 401 C ATOM 272 OD1 ASN A 36 -29.624 -34.173 13.265 1.00 74.27 O ANISOU 272 OD1 ASN A 36 10672 9098 8448 -1302 15 428 O ATOM 273 ND2 ASN A 36 -28.839 -33.909 11.177 1.00 64.10 N ANISOU 273 ND2 ASN A 36 9278 7827 7250 -1234 25 374 N ATOM 274 N LEU A 37 -29.082 -29.141 14.228 1.00 54.27 N ANISOU 274 N LEU A 37 7722 6832 6064 -1080 51 420 N ATOM 275 CA LEU A 37 -28.563 -27.831 14.594 1.00 59.63 C ANISOU 275 CA LEU A 37 8314 7550 6792 -998 46 413 C ATOM 276 C LEU A 37 -28.931 -27.424 16.013 1.00 56.56 C ANISOU 276 C LEU A 37 7935 7185 6371 -1006 46 433 C ATOM 277 O LEU A 37 -28.461 -26.382 16.483 1.00 53.29 O ANISOU 277 O LEU A 37 7460 6795 5994 -937 38 427 O ATOM 278 CB LEU A 37 -29.079 -26.767 13.618 1.00 53.36 C ANISOU 278 CB LEU A 37 7397 6849 6028 -1000 78 405 C ATOM 279 CG LEU A 37 -28.659 -26.935 12.157 1.00 50.69 C ANISOU 279 CG LEU A 37 7035 6502 5725 -990 80 383 C ATOM 280 CD1 LEU A 37 -29.362 -25.910 11.287 1.00 52.25 C ANISOU 280 CD1 LEU A 37 7123 6792 5936 -1004 108 384 C ATOM 281 CD2 LEU A 37 -27.151 -26.816 12.007 1.00 47.72 C ANISOU 281 CD2 LEU A 37 6664 6062 5405 -897 49 356 C ATOM 282 N GLN A 38 -29.752 -28.212 16.703 1.00 58.37 N ANISOU 282 N GLN A 38 8240 7410 6529 -1092 55 454 N ATOM 283 CA GLN A 38 -30.188 -27.887 18.059 1.00 59.70 C ANISOU 283 CA GLN A 38 8420 7607 6655 -1115 60 470 C ATOM 284 C GLN A 38 -29.162 -28.439 19.040 1.00 52.99 C ANISOU 284 C GLN A 38 7678 6655 5799 -1066 10 480 C ATOM 285 O GLN A 38 -29.204 -29.614 19.411 1.00 64.26 O ANISOU 285 O GLN A 38 9231 8010 7175 -1117 -9 496 O ATOM 286 CB GLN A 38 -31.582 -28.445 18.320 1.00 52.05 C ANISOU 286 CB GLN A 38 7478 6691 5605 -1243 98 484 C ATOM 287 CG GLN A 38 -32.670 -27.731 17.536 1.00 57.93 C ANISOU 287 CG GLN A 38 8101 7554 6355 -1283 144 470 C ATOM 288 CD GLN A 38 -33.971 -28.499 17.516 1.00 62.71 C ANISOU 288 CD GLN A 38 8736 8210 6883 -1415 181 473 C ATOM 289 OE1 GLN A 38 -34.045 -29.633 17.989 1.00 59.51 O ANISOU 289 OE1 GLN A 38 8453 7743 6418 -1485 174 490 O ATOM 290 NE2 GLN A 38 -35.008 -27.887 16.960 1.00 67.69 N ANISOU 290 NE2 GLN A 38 9256 8953 7511 -1451 217 456 N ATOM 291 N ASN A 39 -28.225 -27.587 19.447 1.00 55.79 N ANISOU 291 N ASN A 39 7988 7002 6206 -967 -14 468 N ATOM 292 CA ASN A 39 -27.234 -27.934 20.452 1.00 50.98 C ANISOU 292 CA ASN A 39 7466 6310 5596 -909 -65 473 C ATOM 293 C ASN A 39 -26.840 -26.661 21.185 1.00 51.55 C ANISOU 293 C ASN A 39 7457 6428 5701 -841 -67 465 C ATOM 294 O ASN A 39 -27.217 -25.554 20.793 1.00 53.02 O ANISOU 294 O ASN A 39 7527 6698 5920 -830 -32 454 O ATOM 295 CB ASN A 39 -26.012 -28.617 19.830 1.00 46.49 C ANISOU 295 CB ASN A 39 6948 5644 5072 -835 -113 452 C ATOM 296 CG ASN A 39 -25.458 -27.853 18.650 1.00 56.46 C ANISOU 296 CG ASN A 39 8099 6943 6411 -772 -100 418 C ATOM 297 OD1 ASN A 39 -24.805 -26.823 18.814 1.00 53.39 O ANISOU 297 OD1 ASN A 39 7634 6582 6071 -698 -105 401 O ATOM 298 ND2 ASN A 39 -25.712 -28.357 17.447 1.00 57.90 N ANISOU 298 ND2 ASN A 39 8276 7123 6600 -806 -82 408 N ATOM 299 N VAL A 40 -26.069 -26.829 22.261 1.00 56.48 N ANISOU 299 N VAL A 40 8150 6993 6317 -795 -111 471 N ATOM 300 CA VAL A 40 -25.729 -25.688 23.106 1.00 52.18 C ANISOU 300 CA VAL A 40 7540 6491 5795 -739 -112 464 C ATOM 301 C VAL A 40 -24.968 -24.641 22.304 1.00 44.92 C ANISOU 301 C VAL A 40 6508 5600 4960 -652 -109 432 C ATOM 302 O VAL A 40 -25.230 -23.437 22.423 1.00 40.34 O ANISOU 302 O VAL A 40 5831 5093 4403 -636 -82 424 O ATOM 303 CB VAL A 40 -24.930 -26.151 24.339 1.00 49.64 C ANISOU 303 CB VAL A 40 7321 6094 5448 -701 -168 475 C ATOM 304 CG1 VAL A 40 -24.478 -24.951 25.153 1.00 46.72 C ANISOU 304 CG1 VAL A 40 6879 5766 5106 -638 -170 463 C ATOM 305 CG2 VAL A 40 -25.774 -27.091 25.188 1.00 44.80 C ANISOU 305 CG2 VAL A 40 6824 5457 4740 -802 -167 511 C ATOM 306 N THR A 41 -24.027 -25.080 21.467 1.00 42.36 N ANISOU 306 N THR A 41 6196 5218 4679 -598 -137 409 N ATOM 307 CA THR A 41 -23.265 -24.138 20.655 1.00 42.11 C ANISOU 307 CA THR A 41 6064 5215 4722 -528 -131 375 C ATOM 308 C THR A 41 -24.195 -23.221 19.868 1.00 44.06 C ANISOU 308 C THR A 41 6210 5551 4980 -568 -78 378 C ATOM 309 O THR A 41 -24.056 -21.993 19.906 1.00 40.73 O ANISOU 309 O THR A 41 5702 5179 4593 -531 -64 367 O ATOM 310 CB THR A 41 -22.335 -24.898 19.707 1.00 46.91 C ANISOU 310 CB THR A 41 6699 5760 5365 -486 -158 345 C ATOM 311 OG1 THR A 41 -21.679 -25.955 20.418 1.00 54.09 O ANISOU 311 OG1 THR A 41 7719 6578 6253 -456 -214 344 O ATOM 312 CG2 THR A 41 -21.287 -23.961 19.124 1.00 44.46 C ANISOU 312 CG2 THR A 41 6297 5471 5124 -409 -160 303 C ATOM 313 N ASN A 42 -25.166 -23.804 19.163 1.00 43.51 N ANISOU 313 N ASN A 42 6152 5499 4879 -644 -51 392 N ATOM 314 CA ASN A 42 -26.046 -23.029 18.299 1.00 37.85 C ANISOU 314 CA ASN A 42 5343 4864 4173 -679 -9 393 C ATOM 315 C ASN A 42 -27.094 -22.233 19.064 1.00 41.40 C ANISOU 315 C ASN A 42 5744 5392 4595 -712 19 407 C ATOM 316 O ASN A 42 -27.747 -21.372 18.465 1.00 37.21 O ANISOU 316 O ASN A 42 5127 4931 4080 -721 45 403 O ATOM 317 CB ASN A 42 -26.739 -23.951 17.294 1.00 42.32 C ANISOU 317 CB ASN A 42 5936 5429 4713 -750 9 399 C ATOM 318 CG ASN A 42 -25.804 -24.420 16.200 1.00 43.08 C ANISOU 318 CG ASN A 42 6045 5473 4850 -715 -7 375 C ATOM 319 OD1 ASN A 42 -24.684 -23.926 16.069 1.00 40.96 O ANISOU 319 OD1 ASN A 42 5747 5183 4632 -639 -27 350 O ATOM 320 ND2 ASN A 42 -26.264 -25.369 15.397 1.00 47.54 N ANISOU 320 ND2 ASN A 42 6648 6022 5391 -773 3 378 N ATOM 321 N TYR A 43 -27.280 -22.494 20.360 1.00 40.63 N ANISOU 321 N TYR A 43 5700 5284 4454 -731 11 420 N ATOM 322 CA TYR A 43 -28.156 -21.635 21.149 1.00 41.61 C ANISOU 322 CA TYR A 43 5768 5488 4556 -754 37 423 C ATOM 323 C TYR A 43 -27.512 -20.277 21.393 1.00 37.62 C ANISOU 323 C TYR A 43 5186 5003 4105 -670 30 405 C ATOM 324 O TYR A 43 -28.214 -19.265 21.481 1.00 41.58 O ANISOU 324 O TYR A 43 5607 5578 4615 -670 53 398 O ATOM 325 CB TYR A 43 -28.512 -22.311 22.473 1.00 46.41 C ANISOU 325 CB TYR A 43 6459 6081 5094 -806 33 440 C ATOM 326 CG TYR A 43 -29.176 -23.664 22.308 1.00 60.62 C ANISOU 326 CG TYR A 43 8347 7855 6831 -901 41 459 C ATOM 327 CD1 TYR A 43 -29.882 -23.980 21.152 1.00 52.84 C ANISOU 327 CD1 TYR A 43 7333 6901 5843 -951 67 456 C ATOM 328 CD2 TYR A 43 -29.092 -24.625 23.306 1.00 58.04 C ANISOU 328 CD2 TYR A 43 8138 7471 6442 -943 21 479 C ATOM 329 CE1 TYR A 43 -30.484 -25.212 20.998 1.00 57.67 C ANISOU 329 CE1 TYR A 43 8028 7489 6396 -1043 75 471 C ATOM 330 CE2 TYR A 43 -29.689 -25.862 23.158 1.00 58.64 C ANISOU 330 CE2 TYR A 43 8307 7518 6456 -1036 27 497 C ATOM 331 CZ TYR A 43 -30.384 -26.150 22.002 1.00 64.52 C ANISOU 331 CZ TYR A 43 9017 8296 7201 -1086 56 491 C ATOM 332 OH TYR A 43 -30.983 -27.379 21.849 1.00 60.27 O ANISOU 332 OH TYR A 43 8573 7729 6600 -1184 64 507 O ATOM 333 N PHE A 44 -26.181 -20.234 21.496 1.00 36.17 N ANISOU 333 N PHE A 44 5025 4757 3961 -597 -4 395 N ATOM 334 CA PHE A 44 -25.491 -18.951 21.532 1.00 37.47 C ANISOU 334 CA PHE A 44 5117 4940 4181 -523 -9 375 C ATOM 335 C PHE A 44 -25.458 -18.307 20.152 1.00 37.30 C ANISOU 335 C PHE A 44 5024 4942 4205 -508 5 363 C ATOM 336 O PHE A 44 -25.452 -17.074 20.045 1.00 34.24 O ANISOU 336 O PHE A 44 4565 4594 3851 -475 13 352 O ATOM 337 CB PHE A 44 -24.073 -19.130 22.076 1.00 41.21 C ANISOU 337 CB PHE A 44 5633 5347 4679 -455 -50 361 C ATOM 338 CG PHE A 44 -24.027 -19.543 23.522 1.00 42.05 C ANISOU 338 CG PHE A 44 5807 5430 4740 -460 -70 374 C ATOM 339 CD1 PHE A 44 -24.344 -18.640 24.524 1.00 44.07 C ANISOU 339 CD1 PHE A 44 6027 5733 4986 -454 -59 373 C ATOM 340 CD2 PHE A 44 -23.666 -20.832 23.880 1.00 37.44 C ANISOU 340 CD2 PHE A 44 5329 4775 4122 -472 -104 386 C ATOM 341 CE1 PHE A 44 -24.306 -19.017 25.857 1.00 50.27 C ANISOU 341 CE1 PHE A 44 6877 6499 5723 -466 -77 385 C ATOM 342 CE2 PHE A 44 -23.623 -21.213 25.209 1.00 39.71 C ANISOU 342 CE2 PHE A 44 5689 5037 4361 -481 -127 401 C ATOM 343 CZ PHE A 44 -23.945 -20.307 26.198 1.00 38.60 C ANISOU 343 CZ PHE A 44 5510 4950 4208 -481 -112 402 C ATOM 344 N VAL A 45 -25.440 -19.119 19.091 1.00 36.33 N ANISOU 344 N VAL A 45 4925 4795 4082 -535 6 364 N ATOM 345 CA VAL A 45 -25.545 -18.580 17.737 1.00 31.56 C ANISOU 345 CA VAL A 45 4261 4220 3512 -536 21 356 C ATOM 346 C VAL A 45 -26.893 -17.899 17.541 1.00 35.74 C ANISOU 346 C VAL A 45 4730 4826 4025 -575 48 367 C ATOM 347 O VAL A 45 -26.984 -16.830 16.924 1.00 35.63 O ANISOU 347 O VAL A 45 4650 4846 4042 -551 53 361 O ATOM 348 CB VAL A 45 -25.324 -19.699 16.702 1.00 32.51 C ANISOU 348 CB VAL A 45 4423 4299 3628 -565 18 352 C ATOM 349 CG1 VAL A 45 -25.604 -19.196 15.300 1.00 30.98 C ANISOU 349 CG1 VAL A 45 4172 4143 3457 -580 36 348 C ATOM 350 CG2 VAL A 45 -23.911 -20.243 16.801 1.00 30.28 C ANISOU 350 CG2 VAL A 45 4187 3946 3371 -511 -13 329 C ATOM 351 N VAL A 46 -27.962 -18.510 18.056 1.00 34.31 N ANISOU 351 N VAL A 46 4571 4674 3791 -636 63 381 N ATOM 352 CA VAL A 46 -29.285 -17.900 17.959 1.00 34.88 C ANISOU 352 CA VAL A 46 4578 4829 3846 -670 87 382 C ATOM 353 C VAL A 46 -29.328 -16.602 18.753 1.00 33.75 C ANISOU 353 C VAL A 46 4377 4723 3724 -620 85 370 C ATOM 354 O VAL A 46 -29.846 -15.583 18.280 1.00 34.44 O ANISOU 354 O VAL A 46 4393 4859 3833 -600 89 362 O ATOM 355 CB VAL A 46 -30.362 -18.894 18.430 1.00 36.00 C ANISOU 355 CB VAL A 46 4757 5000 3921 -756 107 392 C ATOM 356 CG1 VAL A 46 -31.688 -18.182 18.662 1.00 40.08 C ANISOU 356 CG1 VAL A 46 5196 5614 4417 -783 130 380 C ATOM 357 CG2 VAL A 46 -30.523 -20.010 17.406 1.00 41.54 C ANISOU 357 CG2 VAL A 46 5501 5676 4604 -810 111 400 C ATOM 358 N SER A 47 -28.783 -16.614 19.971 1.00 33.23 N ANISOU 358 N SER A 47 4345 4630 3649 -597 75 369 N ATOM 359 CA SER A 47 -28.715 -15.387 20.758 1.00 38.54 C ANISOU 359 CA SER A 47 4968 5332 4344 -547 73 354 C ATOM 360 C SER A 47 -27.942 -14.308 20.012 1.00 33.66 C ANISOU 360 C SER A 47 4305 4698 3787 -481 60 344 C ATOM 361 O SER A 47 -28.320 -13.131 20.033 1.00 31.22 O ANISOU 361 O SER A 47 3934 4428 3499 -451 61 333 O ATOM 362 CB SER A 47 -28.071 -15.673 22.115 1.00 32.82 C ANISOU 362 CB SER A 47 4297 4573 3601 -532 61 355 C ATOM 363 OG SER A 47 -27.941 -14.488 22.882 1.00 37.61 O ANISOU 363 OG SER A 47 4857 5206 4229 -484 60 339 O ATOM 364 N LEU A 48 -26.855 -14.693 19.342 1.00 37.02 N ANISOU 364 N LEU A 48 4764 5065 4238 -462 45 345 N ATOM 365 CA LEU A 48 -26.105 -13.743 18.530 1.00 32.35 C ANISOU 365 CA LEU A 48 4135 4461 3697 -416 36 334 C ATOM 366 C LEU A 48 -26.946 -13.244 17.361 1.00 28.12 C ANISOU 366 C LEU A 48 3553 3964 3167 -437 45 340 C ATOM 367 O LEU A 48 -26.970 -12.043 17.071 1.00 32.16 O ANISOU 367 O LEU A 48 4020 4492 3706 -404 39 334 O ATOM 368 CB LEU A 48 -24.817 -14.401 18.036 1.00 27.03 C ANISOU 368 CB LEU A 48 3502 3726 3043 -400 22 324 C ATOM 369 CG LEU A 48 -23.801 -13.533 17.295 1.00 34.92 C ANISOU 369 CG LEU A 48 4473 4709 4088 -362 16 305 C ATOM 370 CD1 LEU A 48 -23.258 -12.440 18.193 1.00 37.50 C ANISOU 370 CD1 LEU A 48 4776 5038 4437 -312 8 291 C ATOM 371 CD2 LEU A 48 -22.667 -14.404 16.764 1.00 40.96 C ANISOU 371 CD2 LEU A 48 5272 5425 4865 -355 6 286 C ATOM 372 N ALA A 49 -27.653 -14.150 16.684 1.00 34.37 N ANISOU 372 N ALA A 49 4358 4771 3931 -491 55 352 N ATOM 373 CA ALA A 49 -28.508 -13.741 15.575 1.00 31.44 C ANISOU 373 CA ALA A 49 3943 4442 3560 -512 60 357 C ATOM 374 C ALA A 49 -29.640 -12.837 16.052 1.00 32.95 C ANISOU 374 C ALA A 49 4077 4698 3745 -501 61 352 C ATOM 375 O ALA A 49 -30.011 -11.882 15.361 1.00 33.32 O ANISOU 375 O ALA A 49 4080 4769 3812 -479 50 351 O ATOM 376 CB ALA A 49 -29.062 -14.976 14.866 1.00 33.26 C ANISOU 376 CB ALA A 49 4201 4678 3757 -577 72 368 C ATOM 377 N ALA A 50 -30.203 -13.120 17.230 1.00 31.47 N ANISOU 377 N ALA A 50 3890 4539 3527 -517 73 346 N ATOM 378 CA ALA A 50 -31.245 -12.253 17.774 1.00 35.79 C ANISOU 378 CA ALA A 50 4375 5154 4069 -503 76 329 C ATOM 379 C ALA A 50 -30.734 -10.829 17.962 1.00 35.31 C ANISOU 379 C ALA A 50 4283 5080 4054 -430 57 318 C ATOM 380 O ALA A 50 -31.439 -9.860 17.651 1.00 31.83 O ANISOU 380 O ALA A 50 3789 4679 3628 -402 45 307 O ATOM 381 CB ALA A 50 -31.759 -12.815 19.098 1.00 38.68 C ANISOU 381 CB ALA A 50 4753 5552 4391 -538 96 320 C ATOM 382 N ALA A 51 -29.508 -10.681 18.472 1.00 31.29 N ANISOU 382 N ALA A 51 3808 4514 3565 -397 50 319 N ATOM 383 CA ALA A 51 -28.930 -9.350 18.624 1.00 32.41 C ANISOU 383 CA ALA A 51 3928 4638 3748 -334 34 307 C ATOM 384 C ALA A 51 -28.794 -8.653 17.276 1.00 32.98 C ANISOU 384 C ALA A 51 3988 4696 3849 -320 17 316 C ATOM 385 O ALA A 51 -29.017 -7.441 17.170 1.00 30.47 O ANISOU 385 O ALA A 51 3639 4385 3554 -279 0 308 O ATOM 386 CB ALA A 51 -27.571 -9.445 19.319 1.00 30.97 C ANISOU 386 CB ALA A 51 3787 4401 3581 -309 30 303 C ATOM 387 N ASP A 52 -28.430 -9.400 16.231 1.00 29.18 N ANISOU 387 N ASP A 52 3534 4189 3363 -354 19 331 N ATOM 388 CA ASP A 52 -28.280 -8.788 14.916 1.00 31.86 C ANISOU 388 CA ASP A 52 3868 4515 3721 -351 4 340 C ATOM 389 C ASP A 52 -29.630 -8.414 14.313 1.00 35.23 C ANISOU 389 C ASP A 52 4254 4994 4136 -358 -7 345 C ATOM 390 O ASP A 52 -29.733 -7.403 13.608 1.00 26.58 O ANISOU 390 O ASP A 52 3146 3893 3059 -332 -31 349 O ATOM 391 CB ASP A 52 -27.506 -9.727 13.991 1.00 30.23 C ANISOU 391 CB ASP A 52 3700 4275 3511 -389 13 348 C ATOM 392 CG ASP A 52 -26.057 -9.899 14.418 1.00 40.84 C ANISOU 392 CG ASP A 52 5076 5568 4874 -370 16 334 C ATOM 393 OD1 ASP A 52 -25.511 -8.975 15.062 1.00 36.67 O ANISOU 393 OD1 ASP A 52 4540 5026 4368 -329 9 322 O ATOM 394 OD2 ASP A 52 -25.464 -10.956 14.110 1.00 43.75 O ANISOU 394 OD2 ASP A 52 5476 5911 5235 -395 25 331 O ATOM 395 N ILE A 53 -30.675 -9.202 14.581 1.00 34.63 N ANISOU 395 N ILE A 53 4159 4970 4029 -392 7 342 N ATOM 396 CA ILE A 53 -32.014 -8.824 14.141 1.00 31.04 C ANISOU 396 CA ILE A 53 3654 4579 3563 -393 -6 337 C ATOM 397 C ILE A 53 -32.418 -7.494 14.763 1.00 29.97 C ANISOU 397 C ILE A 53 3475 4462 3450 -329 -28 316 C ATOM 398 O ILE A 53 -32.965 -6.613 14.087 1.00 28.77 O ANISOU 398 O ILE A 53 3296 4325 3311 -297 -59 315 O ATOM 399 CB ILE A 53 -33.020 -9.940 14.481 1.00 36.55 C ANISOU 399 CB ILE A 53 4335 5335 4218 -450 19 329 C ATOM 400 CG1 ILE A 53 -32.834 -11.127 13.533 1.00 38.43 C ANISOU 400 CG1 ILE A 53 4612 5555 4434 -512 32 349 C ATOM 401 CG2 ILE A 53 -34.447 -9.415 14.413 1.00 34.39 C ANISOU 401 CG2 ILE A 53 3991 5142 3933 -440 7 307 C ATOM 402 CD1 ILE A 53 -33.542 -12.393 13.989 1.00 39.09 C ANISOU 402 CD1 ILE A 53 4704 5677 4471 -579 61 344 C ATOM 403 N LEU A 54 -32.148 -7.323 16.059 1.00 33.80 N ANISOU 403 N LEU A 54 3958 4946 3939 -307 -15 299 N ATOM 404 CA LEU A 54 -32.511 -6.087 16.739 1.00 34.05 C ANISOU 404 CA LEU A 54 3950 4996 3992 -246 -33 274 C ATOM 405 C LEU A 54 -31.695 -4.898 16.251 1.00 33.59 C ANISOU 405 C LEU A 54 3914 4876 3972 -195 -64 283 C ATOM 406 O LEU A 54 -32.115 -3.753 16.449 1.00 34.83 O ANISOU 406 O LEU A 54 4043 5041 4150 -140 -90 265 O ATOM 407 CB LEU A 54 -32.344 -6.255 18.250 1.00 32.66 C ANISOU 407 CB LEU A 54 3771 4832 3805 -242 -9 253 C ATOM 408 CG LEU A 54 -33.316 -7.235 18.915 1.00 32.86 C ANISOU 408 CG LEU A 54 3772 4927 3784 -296 21 238 C ATOM 409 CD1 LEU A 54 -32.889 -7.554 20.340 1.00 32.82 C ANISOU 409 CD1 LEU A 54 3789 4918 3762 -305 44 227 C ATOM 410 CD2 LEU A 54 -34.730 -6.674 18.903 1.00 39.25 C ANISOU 410 CD2 LEU A 54 4505 5820 4588 -278 11 203 C ATOM 411 N VAL A 55 -30.544 -5.132 15.619 1.00 33.21 N ANISOU 411 N VAL A 55 3917 4768 3933 -215 -61 306 N ATOM 412 CA VAL A 55 -29.787 -4.016 15.062 1.00 30.71 C ANISOU 412 CA VAL A 55 3627 4396 3645 -182 -86 314 C ATOM 413 C VAL A 55 -30.536 -3.407 13.884 1.00 26.05 C ANISOU 413 C VAL A 55 3028 3814 3056 -173 -122 327 C ATOM 414 O VAL A 55 -30.562 -2.182 13.713 1.00 31.24 O ANISOU 414 O VAL A 55 3692 4446 3734 -128 -156 325 O ATOM 415 CB VAL A 55 -28.370 -4.466 14.663 1.00 34.30 C ANISOU 415 CB VAL A 55 4131 4796 4105 -213 -70 327 C ATOM 416 CG1 VAL A 55 -27.700 -3.415 13.784 1.00 31.23 C ANISOU 416 CG1 VAL A 55 3773 4359 3735 -203 -94 337 C ATOM 417 CG2 VAL A 55 -27.530 -4.722 15.903 1.00 27.21 C ANISOU 417 CG2 VAL A 55 3243 3882 3213 -202 -49 310 C ATOM 418 N GLY A 56 -31.159 -4.243 13.059 1.00 23.50 N ANISOU 418 N GLY A 56 2697 3524 2709 -215 -118 340 N ATOM 419 CA GLY A 56 -31.925 -3.752 11.933 1.00 28.56 C ANISOU 419 CA GLY A 56 3329 4177 3346 -208 -156 352 C ATOM 420 C GLY A 56 -33.268 -3.174 12.327 1.00 27.86 C ANISOU 420 C GLY A 56 3181 4147 3259 -159 -184 326 C ATOM 421 O GLY A 56 -33.707 -2.167 11.766 1.00 30.58 O ANISOU 421 O GLY A 56 3522 4481 3615 -115 -232 328 O ATOM 422 N VAL A 57 -33.930 -3.799 13.299 1.00 30.54 N ANISOU 422 N VAL A 57 3472 4547 3584 -168 -156 299 N ATOM 423 CA VAL A 57 -35.277 -3.376 13.660 1.00 31.81 C ANISOU 423 CA VAL A 57 3563 4781 3743 -129 -176 263 C ATOM 424 C VAL A 57 -35.256 -2.135 14.549 1.00 29.75 C ANISOU 424 C VAL A 57 3286 4507 3513 -52 -199 234 C ATOM 425 O VAL A 57 -36.196 -1.333 14.511 1.00 34.96 O ANISOU 425 O VAL A 57 3899 5201 4184 5 -238 206 O ATOM 426 CB VAL A 57 -36.026 -4.538 14.338 1.00 41.05 C ANISOU 426 CB VAL A 57 4689 6030 4878 -180 -133 240 C ATOM 427 CG1 VAL A 57 -37.382 -4.081 14.854 1.00 39.70 C ANISOU 427 CG1 VAL A 57 4434 5947 4704 -142 -148 190 C ATOM 428 CG2 VAL A 57 -36.196 -5.696 13.371 1.00 30.73 C ANISOU 428 CG2 VAL A 57 3397 4738 3540 -253 -117 266 C ATOM 429 N LEU A 58 -34.203 -1.941 15.345 1.00 31.39 N ANISOU 429 N LEU A 58 3529 4664 3735 -47 -177 237 N ATOM 430 CA LEU A 58 -34.188 -0.849 16.313 1.00 32.81 C ANISOU 430 CA LEU A 58 3691 4834 3941 20 -192 205 C ATOM 431 C LEU A 58 -32.922 -0.004 16.243 1.00 30.05 C ANISOU 431 C LEU A 58 3406 4393 3618 42 -205 225 C ATOM 432 O LEU A 58 -33.003 1.226 16.150 1.00 32.94 O ANISOU 432 O LEU A 58 3781 4727 4010 102 -247 215 O ATOM 433 CB LEU A 58 -34.347 -1.400 17.732 1.00 36.18 C ANISOU 433 CB LEU A 58 4084 5312 4353 4 -148 173 C ATOM 434 CG LEU A 58 -35.678 -2.075 18.066 1.00 35.34 C ANISOU 434 CG LEU A 58 3906 5307 4216 -20 -130 140 C ATOM 435 CD1 LEU A 58 -35.622 -2.659 19.469 1.00 37.06 C ANISOU 435 CD1 LEU A 58 4110 5562 4410 -51 -82 116 C ATOM 436 CD2 LEU A 58 -36.838 -1.101 17.936 1.00 36.39 C ANISOU 436 CD2 LEU A 58 3973 5489 4364 48 -173 97 C ATOM 437 N ALA A 59 -31.749 -0.640 16.297 1.00 26.29 N ANISOU 437 N ALA A 59 2976 3877 3137 -5 -172 248 N ATOM 438 CA ALA A 59 -30.511 0.125 16.419 1.00 31.16 C ANISOU 438 CA ALA A 59 3644 4420 3776 10 -177 257 C ATOM 439 C ALA A 59 -30.290 1.037 15.217 1.00 30.89 C ANISOU 439 C ALA A 59 3654 4330 3753 22 -219 280 C ATOM 440 O ALA A 59 -29.902 2.200 15.378 1.00 32.57 O ANISOU 440 O ALA A 59 3895 4495 3987 61 -245 274 O ATOM 441 CB ALA A 59 -29.321 -0.817 16.595 1.00 32.78 C ANISOU 441 CB ALA A 59 3882 4600 3972 -42 -137 271 C ATOM 442 N ILE A 60 -30.518 0.533 14.007 1.00 31.35 N ANISOU 442 N ILE A 60 3726 4392 3794 -16 -228 308 N ATOM 443 CA ILE A 60 -30.287 1.321 12.796 1.00 31.55 C ANISOU 443 CA ILE A 60 3804 4364 3820 -18 -269 335 C ATOM 444 C ILE A 60 -31.326 2.435 12.710 1.00 25.59 C ANISOU 444 C ILE A 60 3033 3611 3077 53 -328 323 C ATOM 445 O ILE A 60 -30.964 3.587 12.430 1.00 26.65 O ANISOU 445 O ILE A 60 3219 3682 3225 81 -366 331 O ATOM 446 CB ILE A 60 -30.296 0.432 11.542 1.00 27.42 C ANISOU 446 CB ILE A 60 3297 3851 3271 -80 -262 365 C ATOM 447 CG1 ILE A 60 -28.943 -0.278 11.407 1.00 31.51 C ANISOU 447 CG1 ILE A 60 3851 4339 3783 -141 -217 375 C ATOM 448 CG2 ILE A 60 -30.589 1.260 10.303 1.00 26.26 C ANISOU 448 CG2 ILE A 60 3191 3669 3117 -74 -316 391 C ATOM 449 CD1 ILE A 60 -28.900 -1.367 10.342 1.00 31.96 C ANISOU 449 CD1 ILE A 60 3917 4413 3814 -206 -199 396 C ATOM 450 N PRO A 61 -32.614 2.156 12.920 1.00 28.93 N ANISOU 450 N PRO A 61 3390 4105 3497 82 -340 300 N ATOM 451 CA PRO A 61 -33.562 3.268 13.101 1.00 35.60 C ANISOU 451 CA PRO A 61 4210 4956 4361 166 -397 273 C ATOM 452 C PRO A 61 -33.104 4.271 14.148 1.00 30.68 C ANISOU 452 C PRO A 61 3599 4293 3766 218 -402 246 C ATOM 453 O PRO A 61 -33.228 5.481 13.932 1.00 30.77 O ANISOU 453 O PRO A 61 3643 4253 3795 276 -457 243 O ATOM 454 CB PRO A 61 -34.856 2.553 13.508 1.00 35.64 C ANISOU 454 CB PRO A 61 4124 5063 4354 176 -386 237 C ATOM 455 CG PRO A 61 -34.764 1.219 12.837 1.00 29.61 C ANISOU 455 CG PRO A 61 3362 4330 3559 93 -348 266 C ATOM 456 CD PRO A 61 -33.301 0.855 12.815 1.00 31.34 C ANISOU 456 CD PRO A 61 3645 4486 3777 38 -309 297 C ATOM 457 N PHE A 62 -32.564 3.803 15.276 1.00 32.51 N ANISOU 457 N PHE A 62 3809 4542 4000 199 -347 228 N ATOM 458 CA PHE A 62 -32.050 4.725 16.283 1.00 31.07 C ANISOU 458 CA PHE A 62 3640 4324 3843 243 -348 202 C ATOM 459 C PHE A 62 -30.891 5.546 15.728 1.00 32.67 C ANISOU 459 C PHE A 62 3930 4429 4054 231 -366 232 C ATOM 460 O PHE A 62 -30.837 6.768 15.908 1.00 30.72 O ANISOU 460 O PHE A 62 3714 4130 3827 283 -405 220 O ATOM 461 CB PHE A 62 -31.613 3.957 17.534 1.00 31.27 C ANISOU 461 CB PHE A 62 3633 4387 3862 215 -287 181 C ATOM 462 CG PHE A 62 -32.750 3.358 18.324 1.00 35.93 C ANISOU 462 CG PHE A 62 4140 5071 4440 226 -268 142 C ATOM 463 CD1 PHE A 62 -34.074 3.581 17.968 1.00 40.66 C ANISOU 463 CD1 PHE A 62 4687 5723 5039 266 -303 118 C ATOM 464 CD2 PHE A 62 -32.488 2.573 19.433 1.00 33.99 C ANISOU 464 CD2 PHE A 62 3871 4863 4179 193 -215 127 C ATOM 465 CE1 PHE A 62 -35.110 3.025 18.704 1.00 38.67 C ANISOU 465 CE1 PHE A 62 4354 5568 4772 266 -279 75 C ATOM 466 CE2 PHE A 62 -33.517 2.016 20.171 1.00 35.01 C ANISOU 466 CE2 PHE A 62 3931 5082 4289 189 -193 90 C ATOM 467 CZ PHE A 62 -34.828 2.242 19.806 1.00 38.93 C ANISOU 467 CZ PHE A 62 4369 5637 4785 222 -222 61 C ATOM 468 N ALA A 63 -29.951 4.885 15.045 1.00 35.26 N ANISOU 468 N ALA A 63 4300 4732 4364 158 -338 268 N ATOM 469 CA ALA A 63 -28.783 5.587 14.517 1.00 27.06 C ANISOU 469 CA ALA A 63 3342 3613 3327 131 -346 291 C ATOM 470 C ALA A 63 -29.183 6.634 13.486 1.00 32.49 C ANISOU 470 C ALA A 63 4085 4246 4013 156 -412 313 C ATOM 471 O ALA A 63 -28.617 7.733 13.453 1.00 30.61 O ANISOU 471 O ALA A 63 3911 3937 3784 168 -438 316 O ATOM 472 CB ALA A 63 -27.807 4.585 13.906 1.00 33.13 C ANISOU 472 CB ALA A 63 4134 4380 4076 48 -302 316 C ATOM 473 N ILE A 64 -30.146 6.309 12.624 1.00 32.28 N ANISOU 473 N ILE A 64 4042 4249 3972 160 -443 329 N ATOM 474 CA ILE A 64 -30.639 7.296 11.670 1.00 32.84 C ANISOU 474 CA ILE A 64 4169 4270 4040 193 -516 349 C ATOM 475 C ILE A 64 -31.234 8.487 12.409 1.00 34.23 C ANISOU 475 C ILE A 64 4339 4421 4245 288 -566 315 C ATOM 476 O ILE A 64 -31.088 9.640 11.984 1.00 33.67 O ANISOU 476 O ILE A 64 4346 4271 4178 315 -622 328 O ATOM 477 CB ILE A 64 -31.658 6.646 10.716 1.00 34.25 C ANISOU 477 CB ILE A 64 4317 4499 4199 187 -541 366 C ATOM 478 CG1 ILE A 64 -30.946 5.672 9.772 1.00 34.35 C ANISOU 478 CG1 ILE A 64 4358 4514 4180 90 -501 403 C ATOM 479 CG2 ILE A 64 -32.412 7.716 9.932 1.00 33.70 C ANISOU 479 CG2 ILE A 64 4292 4385 4128 245 -631 378 C ATOM 480 CD1 ILE A 64 -31.870 4.652 9.132 1.00 34.67 C ANISOU 480 CD1 ILE A 64 4348 4626 4201 70 -500 410 C ATOM 481 N THR A 65 -31.900 8.229 13.537 1.00 31.38 N ANISOU 481 N THR A 65 3891 4127 3903 337 -547 268 N ATOM 482 CA THR A 65 -32.547 9.301 14.287 1.00 31.15 C ANISOU 482 CA THR A 65 3844 4088 3905 433 -592 224 C ATOM 483 C THR A 65 -31.520 10.238 14.914 1.00 32.99 C ANISOU 483 C THR A 65 4139 4243 4154 438 -586 218 C ATOM 484 O THR A 65 -31.637 11.464 14.804 1.00 31.82 O ANISOU 484 O THR A 65 4046 4025 4020 494 -646 212 O ATOM 485 CB THR A 65 -33.461 8.703 15.361 1.00 34.63 C ANISOU 485 CB THR A 65 4172 4631 4355 468 -561 169 C ATOM 486 OG1 THR A 65 -34.484 7.913 14.742 1.00 35.44 O ANISOU 486 OG1 THR A 65 4217 4808 4440 462 -570 170 O ATOM 487 CG2 THR A 65 -34.118 9.790 16.177 1.00 40.97 C ANISOU 487 CG2 THR A 65 4947 5431 5190 568 -604 113 C ATOM 488 N ILE A 66 -30.500 9.684 15.576 1.00 32.20 N ANISOU 488 N ILE A 66 4033 4152 4050 381 -517 217 N ATOM 489 CA ILE A 66 -29.531 10.523 16.273 1.00 37.71 C ANISOU 489 CA ILE A 66 4778 4788 4761 383 -507 205 C ATOM 490 C ILE A 66 -28.612 11.278 15.325 1.00 38.25 C ANISOU 490 C ILE A 66 4958 4760 4817 339 -532 245 C ATOM 491 O ILE A 66 -27.928 12.210 15.759 1.00 47.19 O ANISOU 491 O ILE A 66 6142 5829 5959 346 -538 234 O ATOM 492 CB ILE A 66 -28.675 9.699 17.260 1.00 42.71 C ANISOU 492 CB ILE A 66 5372 5462 5392 336 -430 190 C ATOM 493 CG1 ILE A 66 -27.858 8.640 16.518 1.00 35.11 C ANISOU 493 CG1 ILE A 66 4428 4509 4405 246 -388 228 C ATOM 494 CG2 ILE A 66 -29.560 9.060 18.328 1.00 44.52 C ANISOU 494 CG2 ILE A 66 5504 5783 5630 373 -405 148 C ATOM 495 CD1 ILE A 66 -27.309 7.546 17.420 1.00 44.00 C ANISOU 495 CD1 ILE A 66 5504 5690 5526 211 -323 213 C ATOM 496 N SER A 67 -28.576 10.908 14.042 1.00 39.78 N ANISOU 496 N SER A 67 5191 4941 4984 288 -546 289 N ATOM 497 CA SER A 67 -27.775 11.654 13.078 1.00 39.85 C ANISOU 497 CA SER A 67 5310 4859 4971 237 -572 327 C ATOM 498 C SER A 67 -28.419 12.981 12.699 1.00 37.11 C ANISOU 498 C SER A 67 5033 4437 4631 304 -660 333 C ATOM 499 O SER A 67 -27.716 13.887 12.242 1.00 39.06 O ANISOU 499 O SER A 67 5383 4594 4862 272 -685 355 O ATOM 500 CB SER A 67 -27.541 10.820 11.814 1.00 38.07 C ANISOU 500 CB SER A 67 5106 4649 4710 157 -558 371 C ATOM 501 OG SER A 67 -28.743 10.618 11.090 1.00 36.78 O ANISOU 501 OG SER A 67 4923 4512 4540 194 -607 386 O ATOM 502 N THR A 68 -29.733 13.117 12.885 1.00 34.62 N ANISOU 502 N THR A 68 4664 4155 4336 396 -709 309 N ATOM 503 CA THR A 68 -30.416 14.367 12.580 1.00 43.70 C ANISOU 503 CA THR A 68 5876 5233 5496 477 -802 307 C ATOM 504 C THR A 68 -30.148 15.450 13.618 1.00 41.90 C ANISOU 504 C THR A 68 5673 4951 5297 532 -815 267 C ATOM 505 O THR A 68 -30.257 16.637 13.295 1.00 45.86 O ANISOU 505 O THR A 68 6267 5358 5802 575 -888 275 O ATOM 506 CB THR A 68 -31.928 14.132 12.471 1.00 45.79 C ANISOU 506 CB THR A 68 6062 5563 5775 564 -852 282 C ATOM 507 OG1 THR A 68 -32.444 13.701 13.738 1.00 45.18 O ANISOU 507 OG1 THR A 68 5867 5573 5727 613 -811 222 O ATOM 508 CG2 THR A 68 -32.237 13.082 11.411 1.00 42.68 C ANISOU 508 CG2 THR A 68 5645 5221 5349 508 -842 320 C ATOM 509 N GLY A 69 -29.802 15.077 14.847 1.00 41.59 N ANISOU 509 N GLY A 69 5560 4964 5277 532 -749 227 N ATOM 510 CA GLY A 69 -29.634 16.064 15.896 1.00 39.75 C ANISOU 510 CA GLY A 69 5341 4690 5074 588 -759 183 C ATOM 511 C GLY A 69 -30.937 16.648 16.391 1.00 42.33 C ANISOU 511 C GLY A 69 5616 5034 5433 712 -820 131 C ATOM 512 O GLY A 69 -30.960 17.789 16.866 1.00 47.20 O ANISOU 512 O GLY A 69 6278 5583 6072 774 -863 102 O ATOM 513 N PHE A 70 -32.026 15.891 16.297 1.00 41.89 N ANISOU 513 N PHE A 70 5464 5070 5381 749 -825 114 N ATOM 514 CA PHE A 70 -33.339 16.408 16.652 1.00 42.98 C ANISOU 514 CA PHE A 70 5544 5238 5549 868 -887 57 C ATOM 515 C PHE A 70 -33.426 16.695 18.147 1.00 41.11 C ANISOU 515 C PHE A 70 5239 5039 5343 919 -853 -15 C ATOM 516 O PHE A 70 -32.767 16.052 18.968 1.00 37.81 O ANISOU 516 O PHE A 70 4779 4668 4918 860 -771 -22 O ATOM 517 CB PHE A 70 -34.426 15.411 16.248 1.00 40.94 C ANISOU 517 CB PHE A 70 5188 5087 5282 880 -887 49 C ATOM 518 CG PHE A 70 -34.627 14.297 17.236 1.00 45.07 C ANISOU 518 CG PHE A 70 5588 5732 5804 851 -802 11 C ATOM 519 CD1 PHE A 70 -33.636 13.355 17.455 1.00 42.80 C ANISOU 519 CD1 PHE A 70 5301 5467 5495 748 -717 44 C ATOM 520 CD2 PHE A 70 -35.814 14.188 17.941 1.00 49.95 C ANISOU 520 CD2 PHE A 70 6093 6444 6441 925 -809 -61 C ATOM 521 CE1 PHE A 70 -33.824 12.329 18.365 1.00 40.70 C ANISOU 521 CE1 PHE A 70 4936 5304 5224 720 -645 13 C ATOM 522 CE2 PHE A 70 -36.008 13.165 18.848 1.00 46.47 C ANISOU 522 CE2 PHE A 70 5551 6114 5991 888 -730 -94 C ATOM 523 CZ PHE A 70 -35.012 12.235 19.061 1.00 43.68 C ANISOU 523 CZ PHE A 70 5210 5771 5613 785 -650 -53 C ATOM 524 N CYS A 71 -34.255 17.676 18.493 1.00 35.65 N ANISOU 524 N CYS A 71 4537 4326 4682 1031 -921 -70 N ATOM 525 CA CYS A 71 -34.451 18.034 19.891 1.00 45.84 C ANISOU 525 CA CYS A 71 5760 5655 6002 1087 -896 -146 C ATOM 526 C CYS A 71 -35.118 16.893 20.649 1.00 39.53 C ANISOU 526 C CYS A 71 4817 5005 5199 1076 -829 -191 C ATOM 527 O CYS A 71 -36.092 16.300 20.181 1.00 38.26 O ANISOU 527 O CYS A 71 4587 4919 5031 1095 -846 -200 O ATOM 528 CB CYS A 71 -35.305 19.297 19.998 1.00 43.26 C ANISOU 528 CB CYS A 71 5449 5278 5711 1218 -990 -203 C ATOM 529 SG CYS A 71 -34.580 20.757 19.219 1.00 48.28 S ANISOU 529 SG CYS A 71 6272 5725 6348 1235 -1077 -155 S ATOM 530 N ALA A 72 -34.597 16.599 21.838 1.00 41.62 N ANISOU 530 N ALA A 72 5039 5311 5463 1041 -755 -220 N ATOM 531 CA ALA A 72 -35.153 15.533 22.657 1.00 42.43 C ANISOU 531 CA ALA A 72 5018 5550 5554 1018 -688 -261 C ATOM 532 C ALA A 72 -34.682 15.701 24.093 1.00 41.93 C ANISOU 532 C ALA A 72 4925 5509 5498 1013 -633 -308 C ATOM 533 O ALA A 72 -33.699 16.394 24.369 1.00 44.22 O ANISOU 533 O ALA A 72 5293 5713 5797 1001 -631 -294 O ATOM 534 CB ALA A 72 -34.752 14.151 22.130 1.00 43.88 C ANISOU 534 CB ALA A 72 5193 5779 5701 912 -631 -199 C ATOM 535 N ALA A 73 -35.405 15.054 25.003 1.00 41.89 N ANISOU 535 N ALA A 73 4808 5623 5485 1015 -587 -366 N ATOM 536 CA ALA A 73 -34.958 14.971 26.385 1.00 41.35 C ANISOU 536 CA ALA A 73 4707 5593 5413 992 -525 -405 C ATOM 537 C ALA A 73 -33.655 14.187 26.457 1.00 35.89 C ANISOU 537 C ALA A 73 4067 4878 4693 885 -463 -338 C ATOM 538 O ALA A 73 -33.491 13.161 25.791 1.00 42.06 O ANISOU 538 O ALA A 73 4851 5681 5448 818 -439 -284 O ATOM 539 CB ALA A 73 -36.026 14.303 27.250 1.00 40.85 C ANISOU 539 CB ALA A 73 4517 5671 5335 998 -485 -476 C ATOM 540 N CYS A 74 -32.723 14.673 27.279 1.00 39.01 N ANISOU 540 N CYS A 74 4500 5229 5093 873 -438 -347 N ATOM 541 CA CYS A 74 -31.374 14.117 27.266 1.00 38.72 C ANISOU 541 CA CYS A 74 4521 5157 5035 783 -393 -288 C ATOM 542 C CYS A 74 -31.374 12.629 27.598 1.00 35.68 C ANISOU 542 C CYS A 74 4080 4863 4614 709 -329 -270 C ATOM 543 O CYS A 74 -30.644 11.849 26.975 1.00 40.31 O ANISOU 543 O CYS A 74 4706 5431 5181 641 -309 -209 O ATOM 544 CB CYS A 74 -30.480 14.879 28.242 1.00 40.67 C ANISOU 544 CB CYS A 74 4802 5358 5292 786 -376 -313 C ATOM 545 SG CYS A 74 -28.746 14.374 28.168 1.00 49.35 S ANISOU 545 SG CYS A 74 5972 6409 6369 687 -330 -251 S ATOM 546 N HIS A 75 -32.180 12.212 28.576 1.00 38.54 N ANISOU 546 N HIS A 75 4356 5324 4963 719 -298 -325 N ATOM 547 CA HIS A 75 -32.175 10.806 28.964 1.00 38.51 C ANISOU 547 CA HIS A 75 4313 5401 4919 643 -240 -307 C ATOM 548 C HIS A 75 -32.865 9.934 27.925 1.00 38.25 C ANISOU 548 C HIS A 75 4258 5405 4869 618 -247 -274 C ATOM 549 O HIS A 75 -32.479 8.776 27.737 1.00 33.17 O ANISOU 549 O HIS A 75 3625 4783 4197 544 -211 -229 O ATOM 550 CB HIS A 75 -32.827 10.636 30.334 1.00 36.95 C ANISOU 550 CB HIS A 75 4037 5299 4703 648 -202 -376 C ATOM 551 CG HIS A 75 -31.939 11.041 31.466 1.00 45.22 C ANISOU 551 CG HIS A 75 5108 6323 5749 639 -176 -395 C ATOM 552 ND1 HIS A 75 -31.763 12.356 31.841 1.00 49.07 N ANISOU 552 ND1 HIS A 75 5614 6758 6271 704 -204 -436 N ATOM 553 CD2 HIS A 75 -31.153 10.307 32.289 1.00 50.03 C ANISOU 553 CD2 HIS A 75 5731 6953 6326 575 -127 -377 C ATOM 554 CE1 HIS A 75 -30.917 12.414 32.853 1.00 44.60 C ANISOU 554 CE1 HIS A 75 5067 6187 5694 676 -171 -445 C ATOM 555 NE2 HIS A 75 -30.532 11.184 33.145 1.00 56.56 N ANISOU 555 NE2 HIS A 75 6578 7746 7168 599 -126 -409 N ATOM 556 N GLY A 76 -33.883 10.465 27.248 1.00 34.84 N ANISOU 556 N GLY A 76 3798 4981 4458 680 -297 -298 N ATOM 557 CA GLY A 76 -34.449 9.749 26.120 1.00 34.31 C ANISOU 557 CA GLY A 76 3719 4938 4378 658 -312 -262 C ATOM 558 C GLY A 76 -33.468 9.640 24.969 1.00 38.71 C ANISOU 558 C GLY A 76 4367 5403 4936 619 -328 -183 C ATOM 559 O GLY A 76 -33.441 8.633 24.256 1.00 38.85 O ANISOU 559 O GLY A 76 4390 5441 4931 560 -311 -138 O ATOM 560 N CYS A 77 -32.649 10.677 24.771 1.00 36.98 N ANISOU 560 N CYS A 77 4223 5085 4742 646 -359 -168 N ATOM 561 CA CYS A 77 -31.602 10.619 23.757 1.00 37.02 C ANISOU 561 CA CYS A 77 4317 5007 4743 597 -368 -99 C ATOM 562 C CYS A 77 -30.526 9.610 24.141 1.00 33.23 C ANISOU 562 C CYS A 77 3851 4538 4239 514 -305 -68 C ATOM 563 O CYS A 77 -29.976 8.921 23.275 1.00 30.56 O ANISOU 563 O CYS A 77 3548 4178 3884 456 -295 -16 O ATOM 564 CB CYS A 77 -30.998 12.012 23.560 1.00 40.53 C ANISOU 564 CB CYS A 77 4840 5346 5215 638 -412 -98 C ATOM 565 SG CYS A 77 -29.634 12.103 22.369 1.00 41.18 S ANISOU 565 SG CYS A 77 5034 5327 5285 568 -419 -23 S ATOM 566 N LEU A 78 -30.218 9.506 25.437 1.00 37.88 N ANISOU 566 N LEU A 78 4412 5159 4823 508 -266 -101 N ATOM 567 CA LEU A 78 -29.230 8.532 25.894 1.00 33.65 C ANISOU 567 CA LEU A 78 3889 4634 4263 438 -214 -76 C ATOM 568 C LEU A 78 -29.622 7.117 25.499 1.00 31.24 C ANISOU 568 C LEU A 78 3556 4388 3927 385 -188 -48 C ATOM 569 O LEU A 78 -28.771 6.324 25.075 1.00 31.68 O ANISOU 569 O LEU A 78 3646 4422 3968 328 -168 -6 O ATOM 570 CB LEU A 78 -29.068 8.614 27.411 1.00 40.21 C ANISOU 570 CB LEU A 78 4689 5503 5088 445 -182 -121 C ATOM 571 CG LEU A 78 -27.951 9.499 27.958 1.00 37.82 C ANISOU 571 CG LEU A 78 4432 5136 4801 454 -182 -131 C ATOM 572 CD1 LEU A 78 -28.065 9.592 29.472 1.00 39.05 C ANISOU 572 CD1 LEU A 78 4547 5343 4949 468 -154 -182 C ATOM 573 CD2 LEU A 78 -26.588 8.962 27.551 1.00 36.50 C ANISOU 573 CD2 LEU A 78 4319 4926 4624 393 -164 -85 C ATOM 574 N PHE A 79 -30.903 6.775 25.646 1.00 33.62 N ANISOU 574 N PHE A 79 3791 4765 4217 400 -187 -76 N ATOM 575 CA PHE A 79 -31.324 5.399 25.410 1.00 37.17 C ANISOU 575 CA PHE A 79 4215 5276 4633 342 -158 -55 C ATOM 576 C PHE A 79 -31.131 5.007 23.951 1.00 30.80 C ANISOU 576 C PHE A 79 3447 4431 3826 314 -177 -1 C ATOM 577 O PHE A 79 -30.508 3.984 23.651 1.00 34.94 O ANISOU 577 O PHE A 79 3997 4948 4329 253 -150 37 O ATOM 578 CB PHE A 79 -32.781 5.200 25.827 1.00 33.64 C ANISOU 578 CB PHE A 79 3684 4925 4171 359 -153 -103 C ATOM 579 CG PHE A 79 -33.265 3.790 25.641 1.00 37.27 C ANISOU 579 CG PHE A 79 4120 5449 4590 291 -120 -85 C ATOM 580 CD1 PHE A 79 -33.000 2.823 26.597 1.00 35.45 C ANISOU 580 CD1 PHE A 79 3889 5257 4322 231 -71 -84 C ATOM 581 CD2 PHE A 79 -33.963 3.423 24.503 1.00 38.14 C ANISOU 581 CD2 PHE A 79 4216 5578 4696 282 -140 -66 C ATOM 582 CE1 PHE A 79 -33.431 1.523 26.423 1.00 40.51 C ANISOU 582 CE1 PHE A 79 4521 5950 4923 163 -43 -66 C ATOM 583 CE2 PHE A 79 -34.396 2.123 24.329 1.00 36.32 C ANISOU 583 CE2 PHE A 79 3968 5405 4426 214 -108 -51 C ATOM 584 CZ PHE A 79 -34.131 1.175 25.289 1.00 36.96 C ANISOU 584 CZ PHE A 79 4054 5519 4470 153 -59 -50 C ATOM 585 N ILE A 80 -31.661 5.808 23.022 1.00 31.63 N ANISOU 585 N ILE A 80 3558 4509 3952 359 -226 0 N ATOM 586 CA ILE A 80 -31.500 5.468 21.613 1.00 39.73 C ANISOU 586 CA ILE A 80 4623 5499 4973 329 -245 50 C ATOM 587 C ILE A 80 -30.038 5.531 21.197 1.00 29.17 C ANISOU 587 C ILE A 80 3362 4082 3639 290 -237 91 C ATOM 588 O ILE A 80 -29.653 4.901 20.206 1.00 36.62 O ANISOU 588 O ILE A 80 4336 5007 4569 241 -233 132 O ATOM 589 CB ILE A 80 -32.359 6.377 20.712 1.00 38.33 C ANISOU 589 CB ILE A 80 4445 5304 4814 388 -308 45 C ATOM 590 CG1 ILE A 80 -31.914 7.834 20.812 1.00 36.85 C ANISOU 590 CG1 ILE A 80 4306 5036 4657 446 -349 34 C ATOM 591 CG2 ILE A 80 -33.824 6.258 21.088 1.00 36.75 C ANISOU 591 CG2 ILE A 80 4157 5197 4611 427 -317 -5 C ATOM 592 CD1 ILE A 80 -32.598 8.741 19.802 1.00 38.86 C ANISOU 592 CD1 ILE A 80 4585 5252 4928 503 -422 38 C ATOM 593 N ALA A 81 -29.211 6.276 21.932 1.00 27.29 N ANISOU 593 N ALA A 81 3151 3801 3417 307 -233 75 N ATOM 594 CA ALA A 81 -27.786 6.328 21.631 1.00 34.02 C ANISOU 594 CA ALA A 81 4066 4590 4270 266 -220 103 C ATOM 595 C ALA A 81 -27.051 5.110 22.178 1.00 31.86 C ANISOU 595 C ALA A 81 3783 4345 3976 212 -171 111 C ATOM 596 O ALA A 81 -26.113 4.613 21.545 1.00 36.05 O ANISOU 596 O ALA A 81 4350 4846 4499 165 -158 139 O ATOM 597 CB ALA A 81 -27.180 7.611 22.199 1.00 31.46 C ANISOU 597 CB ALA A 81 3775 4210 3968 301 -235 80 C ATOM 598 N CYS A 82 -27.469 4.607 23.338 1.00 30.72 N ANISOU 598 N CYS A 82 3594 4259 3820 218 -145 84 N ATOM 599 CA CYS A 82 -26.749 3.537 24.014 1.00 32.05 C ANISOU 599 CA CYS A 82 3764 4447 3967 175 -107 90 C ATOM 600 C CYS A 82 -27.278 2.148 23.694 1.00 27.80 C ANISOU 600 C CYS A 82 3209 3955 3400 131 -88 111 C ATOM 601 O CYS A 82 -26.610 1.162 24.022 1.00 30.86 O ANISOU 601 O CYS A 82 3613 4344 3769 93 -64 123 O ATOM 602 CB CYS A 82 -26.798 3.746 25.533 1.00 34.69 C ANISOU 602 CB CYS A 82 4071 4812 4297 197 -90 52 C ATOM 603 SG CYS A 82 -25.802 5.135 26.121 1.00 29.75 S ANISOU 603 SG CYS A 82 3475 4129 3700 233 -101 26 S ATOM 604 N PHE A 83 -28.449 2.035 23.066 1.00 31.68 N ANISOU 604 N PHE A 83 3671 4482 3886 136 -101 113 N ATOM 605 CA PHE A 83 -29.021 0.712 22.848 1.00 34.97 C ANISOU 605 CA PHE A 83 4070 4947 4270 88 -79 129 C ATOM 606 C PHE A 83 -28.121 -0.155 21.976 1.00 31.95 C ANISOU 606 C PHE A 83 3733 4525 3880 40 -71 168 C ATOM 607 O PHE A 83 -28.066 -1.376 22.167 1.00 24.42 O ANISOU 607 O PHE A 83 2786 3593 2900 -4 -47 180 O ATOM 608 CB PHE A 83 -30.409 0.827 22.223 1.00 35.61 C ANISOU 608 CB PHE A 83 4106 5075 4347 102 -98 120 C ATOM 609 CG PHE A 83 -31.113 -0.492 22.089 1.00 34.75 C ANISOU 609 CG PHE A 83 3977 5026 4202 47 -73 129 C ATOM 610 CD1 PHE A 83 -31.547 -1.173 23.214 1.00 35.63 C ANISOU 610 CD1 PHE A 83 4060 5195 4281 20 -41 107 C ATOM 611 CD2 PHE A 83 -31.329 -1.058 20.846 1.00 32.50 C ANISOU 611 CD2 PHE A 83 3703 4737 3909 16 -82 160 C ATOM 612 CE1 PHE A 83 -32.187 -2.390 23.101 1.00 40.05 C ANISOU 612 CE1 PHE A 83 4609 5805 4802 -39 -17 116 C ATOM 613 CE2 PHE A 83 -31.972 -2.277 20.727 1.00 33.61 C ANISOU 613 CE2 PHE A 83 3827 4929 4014 -39 -58 167 C ATOM 614 CZ PHE A 83 -32.399 -2.944 21.857 1.00 31.14 C ANISOU 614 CZ PHE A 83 3492 4671 3670 -68 -25 145 C ATOM 615 N VAL A 84 -27.411 0.447 21.018 1.00 29.52 N ANISOU 615 N VAL A 84 3461 4161 3594 44 -91 186 N ATOM 616 CA VAL A 84 -26.493 -0.332 20.193 1.00 29.59 C ANISOU 616 CA VAL A 84 3509 4138 3597 -1 -80 213 C ATOM 617 C VAL A 84 -25.354 -0.884 21.040 1.00 29.85 C ANISOU 617 C VAL A 84 3560 4155 3625 -14 -58 205 C ATOM 618 O VAL A 84 -24.794 -1.942 20.728 1.00 23.66 O ANISOU 618 O VAL A 84 2795 3364 2828 -50 -44 218 O ATOM 619 CB VAL A 84 -25.969 0.520 19.022 1.00 33.86 C ANISOU 619 CB VAL A 84 4084 4626 4155 -2 -104 229 C ATOM 620 CG1 VAL A 84 -25.062 1.635 19.527 1.00 33.02 C ANISOU 620 CG1 VAL A 84 4000 4475 4070 24 -111 211 C ATOM 621 CG2 VAL A 84 -25.238 -0.354 18.011 1.00 33.93 C ANISOU 621 CG2 VAL A 84 4122 4616 4153 -55 -91 251 C ATOM 622 N LEU A 85 -24.994 -0.190 22.124 1.00 26.61 N ANISOU 622 N LEU A 85 3144 3740 3226 18 -57 180 N ATOM 623 CA LEU A 85 -23.983 -0.721 23.030 1.00 26.28 C ANISOU 623 CA LEU A 85 3118 3690 3178 10 -41 170 C ATOM 624 C LEU A 85 -24.475 -1.979 23.732 1.00 29.23 C ANISOU 624 C LEU A 85 3485 4103 3519 -13 -24 174 C ATOM 625 O LEU A 85 -23.678 -2.884 24.011 1.00 29.74 O ANISOU 625 O LEU A 85 3575 4153 3570 -31 -17 179 O ATOM 626 CB LEU A 85 -23.589 0.343 24.053 1.00 29.31 C ANISOU 626 CB LEU A 85 3496 4064 3578 48 -45 140 C ATOM 627 CG LEU A 85 -23.091 1.663 23.458 1.00 31.60 C ANISOU 627 CG LEU A 85 3802 4308 3895 66 -63 134 C ATOM 628 CD1 LEU A 85 -22.810 2.675 24.554 1.00 26.68 C ANISOU 628 CD1 LEU A 85 3173 3678 3285 102 -65 103 C ATOM 629 CD2 LEU A 85 -21.852 1.440 22.602 1.00 28.80 C ANISOU 629 CD2 LEU A 85 3480 3915 3546 33 -59 144 C ATOM 630 N VAL A 86 -25.777 -2.054 24.021 1.00 27.00 N ANISOU 630 N VAL A 86 3170 3870 3219 -14 -20 170 N ATOM 631 CA VAL A 86 -26.346 -3.258 24.623 1.00 24.50 C ANISOU 631 CA VAL A 86 2854 3593 2862 -51 -1 175 C ATOM 632 C VAL A 86 -26.212 -4.438 23.669 1.00 29.70 C ANISOU 632 C VAL A 86 3540 4237 3506 -94 3 205 C ATOM 633 O VAL A 86 -25.808 -5.538 24.062 1.00 29.38 O ANISOU 633 O VAL A 86 3534 4189 3441 -122 11 215 O ATOM 634 CB VAL A 86 -27.818 -3.022 25.009 1.00 29.29 C ANISOU 634 CB VAL A 86 3412 4267 3452 -49 7 156 C ATOM 635 CG1 VAL A 86 -28.458 -4.324 25.500 1.00 26.93 C ANISOU 635 CG1 VAL A 86 3118 4012 3103 -105 30 163 C ATOM 636 CG2 VAL A 86 -27.936 -1.928 26.058 1.00 25.00 C ANISOU 636 CG2 VAL A 86 2840 3739 2921 -6 5 120 C ATOM 637 N LEU A 87 -26.558 -4.226 22.397 1.00 28.12 N ANISOU 637 N LEU A 87 3332 4033 3321 -99 -6 218 N ATOM 638 CA LEU A 87 -26.520 -5.319 21.432 1.00 27.95 C ANISOU 638 CA LEU A 87 3333 4002 3284 -142 -2 243 C ATOM 639 C LEU A 87 -25.090 -5.758 21.152 1.00 26.48 C ANISOU 639 C LEU A 87 3188 3762 3110 -147 -4 247 C ATOM 640 O LEU A 87 -24.821 -6.955 20.992 1.00 31.07 O ANISOU 640 O LEU A 87 3799 4332 3673 -178 3 258 O ATOM 641 CB LEU A 87 -27.217 -4.899 20.138 1.00 28.61 C ANISOU 641 CB LEU A 87 3397 4095 3378 -146 -14 254 C ATOM 642 CG LEU A 87 -28.684 -4.486 20.282 1.00 29.86 C ANISOU 642 CG LEU A 87 3506 4313 3527 -136 -18 242 C ATOM 643 CD1 LEU A 87 -29.236 -3.986 18.953 1.00 32.52 C ANISOU 643 CD1 LEU A 87 3829 4651 3875 -130 -40 254 C ATOM 644 CD2 LEU A 87 -29.524 -5.639 20.822 1.00 27.64 C ANISOU 644 CD2 LEU A 87 3214 4085 3203 -182 6 240 C ATOM 645 N ALA A 88 -24.157 -4.807 21.084 1.00 23.33 N ANISOU 645 N ALA A 88 2792 3330 2742 -117 -13 235 N ATOM 646 CA ALA A 88 -22.758 -5.173 20.892 1.00 25.23 C ANISOU 646 CA ALA A 88 3062 3532 2994 -119 -14 227 C ATOM 647 C ALA A 88 -22.240 -5.980 22.075 1.00 34.12 C ANISOU 647 C ALA A 88 4207 4653 4103 -112 -13 218 C ATOM 648 O ALA A 88 -21.517 -6.968 21.894 1.00 31.13 O ANISOU 648 O ALA A 88 3856 4253 3720 -124 -15 217 O ATOM 649 CB ALA A 88 -21.911 -3.919 20.681 1.00 25.07 C ANISOU 649 CB ALA A 88 3037 3484 3003 -96 -22 211 C ATOM 650 N GLN A 89 -22.601 -5.580 23.296 1.00 28.74 N ANISOU 650 N GLN A 89 3514 3993 3413 -92 -12 208 N ATOM 651 CA GLN A 89 -22.140 -6.317 24.467 1.00 29.48 C ANISOU 651 CA GLN A 89 3635 4083 3485 -89 -15 202 C ATOM 652 C GLN A 89 -22.737 -7.716 24.502 1.00 28.03 C ANISOU 652 C GLN A 89 3482 3906 3263 -128 -10 224 C ATOM 653 O GLN A 89 -22.059 -8.678 24.879 1.00 29.86 O ANISOU 653 O GLN A 89 3755 4110 3479 -131 -22 226 O ATOM 654 CB GLN A 89 -22.492 -5.552 25.741 1.00 30.98 C ANISOU 654 CB GLN A 89 3805 4298 3667 -66 -12 186 C ATOM 655 CG GLN A 89 -21.661 -5.961 26.937 1.00 29.70 C ANISOU 655 CG GLN A 89 3671 4123 3490 -53 -22 175 C ATOM 656 CD GLN A 89 -20.190 -5.670 26.735 1.00 28.54 C ANISOU 656 CD GLN A 89 3531 3939 3374 -24 -37 155 C ATOM 657 OE1 GLN A 89 -19.822 -4.620 26.213 1.00 31.93 O ANISOU 657 OE1 GLN A 89 3935 4360 3835 -8 -35 141 O ATOM 658 NE2 GLN A 89 -19.339 -6.607 27.134 1.00 40.21 N ANISOU 658 NE2 GLN A 89 5045 5394 4841 -18 -54 152 N ATOM 659 N SER A 90 -24.007 -7.848 24.114 1.00 32.09 N ANISOU 659 N SER A 90 3978 4457 3759 -159 3 238 N ATOM 660 CA SER A 90 -24.614 -9.169 24.024 1.00 30.30 C ANISOU 660 CA SER A 90 3782 4237 3492 -208 11 258 C ATOM 661 C SER A 90 -23.835 -10.053 23.058 1.00 27.33 C ANISOU 661 C SER A 90 3443 3816 3126 -218 1 267 C ATOM 662 O SER A 90 -23.562 -11.223 23.355 1.00 26.03 O ANISOU 662 O SER A 90 3329 3625 2935 -237 -6 276 O ATOM 663 CB SER A 90 -26.076 -9.031 23.593 1.00 28.65 C ANISOU 663 CB SER A 90 3536 4084 3268 -239 28 264 C ATOM 664 OG SER A 90 -26.755 -10.276 23.617 1.00 32.34 O ANISOU 664 OG SER A 90 4033 4565 3689 -296 39 280 O ATOM 665 N SER A 91 -23.440 -9.500 21.909 1.00 29.54 N ANISOU 665 N SER A 91 3700 4084 3441 -206 -1 263 N ATOM 666 CA SER A 91 -22.683 -10.277 20.932 1.00 28.29 C ANISOU 666 CA SER A 91 3568 3889 3292 -218 -6 264 C ATOM 667 C SER A 91 -21.354 -10.746 21.510 1.00 27.27 C ANISOU 667 C SER A 91 3471 3719 3172 -187 -24 244 C ATOM 668 O SER A 91 -20.923 -11.876 21.255 1.00 29.05 O ANISOU 668 O SER A 91 3736 3915 3388 -197 -34 244 O ATOM 669 CB SER A 91 -22.448 -9.445 19.670 1.00 31.40 C ANISOU 669 CB SER A 91 3931 4281 3717 -216 -3 259 C ATOM 670 OG SER A 91 -23.669 -8.995 19.114 1.00 29.03 O ANISOU 670 OG SER A 91 3604 4017 3410 -236 5 276 O ATOM 671 N ILE A 92 -20.684 -9.889 22.284 1.00 28.69 N ANISOU 671 N ILE A 92 3634 3897 3369 -148 -32 224 N ATOM 672 CA ILE A 92 -19.393 -10.255 22.862 1.00 26.37 C ANISOU 672 CA ILE A 92 3363 3572 3084 -114 -54 199 C ATOM 673 C ILE A 92 -19.549 -11.422 23.828 1.00 27.92 C ANISOU 673 C ILE A 92 3614 3751 3242 -118 -71 213 C ATOM 674 O ILE A 92 -18.738 -12.354 23.832 1.00 28.78 O ANISOU 674 O ILE A 92 3761 3822 3350 -103 -95 201 O ATOM 675 CB ILE A 92 -18.751 -9.032 23.544 1.00 30.41 C ANISOU 675 CB ILE A 92 3844 4092 3618 -76 -57 175 C ATOM 676 CG1 ILE A 92 -18.236 -8.053 22.483 1.00 31.91 C ANISOU 676 CG1 ILE A 92 3998 4283 3844 -76 -46 157 C ATOM 677 CG2 ILE A 92 -17.615 -9.462 24.472 1.00 31.43 C ANISOU 677 CG2 ILE A 92 3996 4198 3747 -39 -83 150 C ATOM 678 CD1 ILE A 92 -18.011 -6.646 22.995 1.00 39.29 C ANISOU 678 CD1 ILE A 92 4904 5229 4797 -53 -43 141 C ATOM 679 N PHE A 93 -20.588 -11.391 24.665 1.00 32.58 N ANISOU 679 N PHE A 93 4212 4368 3798 -141 -61 234 N ATOM 680 CA PHE A 93 -20.828 -12.511 25.569 1.00 29.08 C ANISOU 680 CA PHE A 93 3832 3908 3309 -161 -75 251 C ATOM 681 C PHE A 93 -21.114 -13.792 24.794 1.00 30.70 C ANISOU 681 C PHE A 93 4084 4087 3495 -198 -77 269 C ATOM 682 O PHE A 93 -20.607 -14.864 25.145 1.00 36.72 O ANISOU 682 O PHE A 93 4912 4804 4237 -193 -106 272 O ATOM 683 CB PHE A 93 -21.985 -12.187 26.515 1.00 34.71 C ANISOU 683 CB PHE A 93 4538 4668 3983 -192 -55 265 C ATOM 684 CG PHE A 93 -21.658 -11.139 27.553 1.00 37.87 C ANISOU 684 CG PHE A 93 4909 5086 4392 -156 -57 245 C ATOM 685 CD1 PHE A 93 -20.430 -11.131 28.199 1.00 44.12 C ANISOU 685 CD1 PHE A 93 5722 5845 5195 -111 -87 228 C ATOM 686 CD2 PHE A 93 -22.584 -10.162 27.882 1.00 34.93 C ANISOU 686 CD2 PHE A 93 4487 4767 4018 -165 -32 240 C ATOM 687 CE1 PHE A 93 -20.132 -10.169 29.150 1.00 48.38 C ANISOU 687 CE1 PHE A 93 6236 6405 5742 -81 -88 208 C ATOM 688 CE2 PHE A 93 -22.293 -9.197 28.831 1.00 41.94 C ANISOU 688 CE2 PHE A 93 5350 5672 4914 -132 -33 219 C ATOM 689 CZ PHE A 93 -21.065 -9.201 29.467 1.00 38.36 C ANISOU 689 CZ PHE A 93 4921 5184 4469 -93 -60 205 C ATOM 690 N SER A 94 -21.921 -13.706 23.734 1.00 25.88 N ANISOU 690 N SER A 94 3444 3502 2889 -234 -52 280 N ATOM 691 CA SER A 94 -22.214 -14.897 22.942 1.00 30.93 C ANISOU 691 CA SER A 94 4124 4118 3509 -273 -52 295 C ATOM 692 C SER A 94 -20.967 -15.415 22.234 1.00 34.38 C ANISOU 692 C SER A 94 4580 4505 3979 -239 -75 272 C ATOM 693 O SER A 94 -20.755 -16.630 22.152 1.00 36.25 O ANISOU 693 O SER A 94 4879 4698 4197 -249 -94 276 O ATOM 694 CB SER A 94 -23.319 -14.599 21.929 1.00 30.90 C ANISOU 694 CB SER A 94 4077 4158 3505 -317 -21 307 C ATOM 695 OG SER A 94 -24.560 -14.389 22.583 1.00 33.74 O ANISOU 695 OG SER A 94 4422 4568 3828 -354 -2 321 O ATOM 696 N LEU A 95 -20.128 -14.513 21.716 1.00 31.17 N ANISOU 696 N LEU A 95 4121 4103 3618 -200 -74 244 N ATOM 697 CA LEU A 95 -18.903 -14.952 21.055 1.00 35.64 C ANISOU 697 CA LEU A 95 4694 4634 4214 -169 -93 211 C ATOM 698 C LEU A 95 -17.958 -15.623 22.043 1.00 36.27 C ANISOU 698 C LEU A 95 4821 4671 4289 -122 -134 193 C ATOM 699 O LEU A 95 -17.329 -16.638 21.722 1.00 41.23 O ANISOU 699 O LEU A 95 5489 5257 4921 -106 -159 175 O ATOM 700 CB LEU A 95 -18.214 -13.768 20.378 1.00 31.31 C ANISOU 700 CB LEU A 95 4081 4108 3709 -149 -80 182 C ATOM 701 CG LEU A 95 -18.954 -13.167 19.182 1.00 31.02 C ANISOU 701 CG LEU A 95 4006 4101 3678 -190 -49 197 C ATOM 702 CD1 LEU A 95 -18.344 -11.828 18.799 1.00 34.71 C ANISOU 702 CD1 LEU A 95 4423 4588 4179 -174 -39 174 C ATOM 703 CD2 LEU A 95 -18.937 -14.120 18.004 1.00 30.71 C ANISOU 703 CD2 LEU A 95 3985 4047 3638 -220 -45 194 C ATOM 704 N LEU A 96 -17.846 -15.071 23.251 1.00 31.82 N ANISOU 704 N LEU A 96 4256 4117 3716 -98 -144 195 N ATOM 705 CA LEU A 96 -16.988 -15.684 24.257 1.00 37.57 C ANISOU 705 CA LEU A 96 5034 4806 4435 -53 -189 180 C ATOM 706 C LEU A 96 -17.545 -17.030 24.705 1.00 41.17 C ANISOU 706 C LEU A 96 5581 5220 4841 -80 -211 212 C ATOM 707 O LEU A 96 -16.790 -17.993 24.881 1.00 37.99 O ANISOU 707 O LEU A 96 5235 4764 4436 -46 -255 198 O ATOM 708 CB LEU A 96 -16.827 -14.734 25.444 1.00 42.10 C ANISOU 708 CB LEU A 96 5586 5405 5006 -28 -193 176 C ATOM 709 CG LEU A 96 -15.874 -15.161 26.560 1.00 51.92 C ANISOU 709 CG LEU A 96 6872 6615 6239 25 -243 159 C ATOM 710 CD1 LEU A 96 -14.502 -15.512 26.010 1.00 43.75 C ANISOU 710 CD1 LEU A 96 5825 5553 5244 81 -275 108 C ATOM 711 CD2 LEU A 96 -15.765 -14.054 27.602 1.00 46.63 C ANISOU 711 CD2 LEU A 96 6169 5980 5570 42 -238 152 C ATOM 712 N ALA A 97 -18.865 -17.121 24.886 1.00 39.68 N ANISOU 712 N ALA A 97 5410 5056 4612 -144 -182 253 N ATOM 713 CA ALA A 97 -19.467 -18.394 25.269 1.00 36.99 C ANISOU 713 CA ALA A 97 5161 4677 4217 -187 -198 285 C ATOM 714 C ALA A 97 -19.229 -19.457 24.204 1.00 36.56 C ANISOU 714 C ALA A 97 5144 4577 4172 -193 -210 278 C ATOM 715 O ALA A 97 -18.939 -20.615 24.525 1.00 35.10 O ANISOU 715 O ALA A 97 5048 4329 3961 -186 -250 284 O ATOM 716 CB ALA A 97 -20.964 -18.216 25.516 1.00 34.21 C ANISOU 716 CB ALA A 97 4804 4375 3820 -264 -156 320 C ATOM 717 N ILE A 98 -19.357 -19.085 22.929 1.00 39.84 N ANISOU 717 N ILE A 98 5497 5021 4622 -205 -179 265 N ATOM 718 CA ILE A 98 -19.111 -20.040 21.853 1.00 36.36 C ANISOU 718 CA ILE A 98 5084 4542 4191 -212 -186 253 C ATOM 719 C ILE A 98 -17.677 -20.548 21.919 1.00 32.68 C ANISOU 719 C ILE A 98 4641 4022 3755 -136 -236 209 C ATOM 720 O ILE A 98 -17.421 -21.750 21.784 1.00 39.77 O ANISOU 720 O ILE A 98 5612 4859 4640 -129 -269 204 O ATOM 721 CB ILE A 98 -19.429 -19.396 20.490 1.00 29.98 C ANISOU 721 CB ILE A 98 4198 3779 3413 -238 -144 244 C ATOM 722 CG1 ILE A 98 -20.940 -19.190 20.348 1.00 32.72 C ANISOU 722 CG1 ILE A 98 4533 4175 3726 -312 -104 284 C ATOM 723 CG2 ILE A 98 -18.910 -20.258 19.355 1.00 32.08 C ANISOU 723 CG2 ILE A 98 4480 4010 3698 -234 -152 218 C ATOM 724 CD1 ILE A 98 -21.333 -18.184 19.284 1.00 28.03 C ANISOU 724 CD1 ILE A 98 3855 3635 3159 -328 -68 280 C ATOM 725 N ALA A 99 -16.722 -19.645 22.148 1.00 39.43 N ANISOU 725 N ALA A 99 5436 4898 4649 -79 -244 173 N ATOM 726 CA ALA A 99 -15.328 -20.057 22.265 1.00 34.85 C ANISOU 726 CA ALA A 99 4864 4278 4098 -2 -293 122 C ATOM 727 C ALA A 99 -15.142 -21.010 23.438 1.00 37.11 C ANISOU 727 C ALA A 99 5250 4502 4348 27 -351 137 C ATOM 728 O ALA A 99 -14.561 -22.092 23.290 1.00 35.68 O ANISOU 728 O ALA A 99 5127 4260 4168 63 -397 115 O ATOM 729 CB ALA A 99 -14.431 -18.828 22.419 1.00 35.03 C ANISOU 729 CB ALA A 99 4803 4345 4162 43 -287 81 C ATOM 730 N ILE A 100 -15.645 -20.628 24.615 1.00 38.22 N ANISOU 730 N ILE A 100 5414 4655 4452 10 -352 173 N ATOM 731 CA ILE A 100 -15.485 -21.466 25.800 1.00 36.18 C ANISOU 731 CA ILE A 100 5258 4339 4151 31 -409 192 C ATOM 732 C ILE A 100 -16.186 -22.804 25.604 1.00 39.68 C ANISOU 732 C ILE A 100 5806 4723 4549 -19 -422 227 C ATOM 733 O ILE A 100 -15.713 -23.846 26.073 1.00 34.14 O ANISOU 733 O ILE A 100 5201 3945 3825 15 -485 226 O ATOM 734 CB ILE A 100 -16.007 -20.728 27.045 1.00 34.62 C ANISOU 734 CB ILE A 100 5060 4177 3917 7 -397 224 C ATOM 735 CG1 ILE A 100 -15.121 -19.515 27.347 1.00 30.83 C ANISOU 735 CG1 ILE A 100 4492 3742 3482 66 -396 184 C ATOM 736 CG2 ILE A 100 -16.064 -21.676 28.238 1.00 32.61 C ANISOU 736 CG2 ILE A 100 4928 3862 3603 5 -451 255 C ATOM 737 CD1 ILE A 100 -15.720 -18.549 28.344 1.00 41.73 C ANISOU 737 CD1 ILE A 100 5848 5172 4837 38 -369 208 C ATOM 738 N ASP A 101 -17.326 -22.796 24.913 1.00 37.99 N ANISOU 738 N ASP A 101 5577 4540 4316 -100 -367 257 N ATOM 739 CA ASP A 101 -18.018 -24.044 24.617 1.00 40.22 C ANISOU 739 CA ASP A 101 5955 4772 4556 -157 -373 287 C ATOM 740 C ASP A 101 -17.143 -24.979 23.790 1.00 46.64 C ANISOU 740 C ASP A 101 6800 5519 5401 -105 -414 248 C ATOM 741 O ASP A 101 -17.091 -26.186 24.052 1.00 40.44 O ANISOU 741 O ASP A 101 6129 4654 4583 -105 -461 260 O ATOM 742 CB ASP A 101 -19.324 -23.744 23.885 1.00 40.62 C ANISOU 742 CB ASP A 101 5962 4882 4590 -248 -304 314 C ATOM 743 CG ASP A 101 -20.115 -24.990 23.584 1.00 44.08 C ANISOU 743 CG ASP A 101 6494 5276 4979 -319 -304 344 C ATOM 744 OD1 ASP A 101 -20.758 -25.522 24.512 1.00 54.14 O ANISOU 744 OD1 ASP A 101 7856 6529 6187 -373 -313 383 O ATOM 745 OD2 ASP A 101 -20.090 -25.440 22.421 1.00 44.89 O ANISOU 745 OD2 ASP A 101 6587 5366 5104 -327 -294 328 O ATOM 746 N ARG A 102 -16.444 -24.439 22.787 1.00 46.05 N ANISOU 746 N ARG A 102 6630 5477 5389 -63 -397 198 N ATOM 747 CA ARG A 102 -15.608 -25.278 21.935 1.00 39.03 C ANISOU 747 CA ARG A 102 5758 4538 4534 -14 -430 149 C ATOM 748 C ARG A 102 -14.344 -25.734 22.653 1.00 43.57 C ANISOU 748 C ARG A 102 6375 5055 5126 86 -509 108 C ATOM 749 O ARG A 102 -13.819 -26.812 22.350 1.00 42.83 O ANISOU 749 O ARG A 102 6343 4890 5038 127 -558 79 O ATOM 750 CB ARG A 102 -15.251 -24.530 20.648 1.00 39.51 C ANISOU 750 CB ARG A 102 5702 4660 4651 -9 -384 104 C ATOM 751 CG ARG A 102 -16.403 -24.387 19.652 1.00 35.20 C ANISOU 751 CG ARG A 102 5128 4155 4090 -100 -320 136 C ATOM 752 CD ARG A 102 -16.934 -25.748 19.197 1.00 44.54 C ANISOU 752 CD ARG A 102 6403 5278 5242 -141 -332 153 C ATOM 753 NE ARG A 102 -17.922 -26.290 20.125 1.00 58.46 N ANISOU 753 NE ARG A 102 8260 7012 6939 -199 -339 213 N ATOM 754 CZ ARG A 102 -18.236 -27.574 20.230 1.00 46.83 C ANISOU 754 CZ ARG A 102 6903 5465 5426 -227 -368 233 C ATOM 755 NH1 ARG A 102 -17.652 -28.495 19.480 1.00 60.04 N ANISOU 755 NH1 ARG A 102 8613 7079 7120 -194 -398 195 N ATOM 756 NH2 ARG A 102 -19.154 -27.947 21.119 1.00 50.70 N ANISOU 756 NH2 ARG A 102 7475 5939 5850 -292 -368 288 N ATOM 757 N TYR A 103 -13.839 -24.942 23.601 1.00 37.01 N ANISOU 757 N TYR A 103 5509 4250 4301 130 -525 101 N ATOM 758 CA TYR A 103 -12.676 -25.383 24.364 1.00 44.06 C ANISOU 758 CA TYR A 103 6444 5091 5205 226 -606 63 C ATOM 759 C TYR A 103 -13.032 -26.547 25.281 1.00 48.34 C ANISOU 759 C TYR A 103 7139 5541 5685 219 -667 110 C ATOM 760 O TYR A 103 -12.271 -27.515 25.388 1.00 47.81 O ANISOU 760 O TYR A 103 7144 5397 5624 289 -743 79 O ATOM 761 CB TYR A 103 -12.098 -24.225 25.174 1.00 47.11 C ANISOU 761 CB TYR A 103 6758 5533 5609 267 -607 46 C ATOM 762 CG TYR A 103 -10.917 -24.633 26.023 1.00 51.20 C ANISOU 762 CG TYR A 103 7313 6004 6135 368 -694 6 C ATOM 763 CD1 TYR A 103 -9.688 -24.918 25.443 1.00 51.08 C ANISOU 763 CD1 TYR A 103 7254 5979 6174 456 -734 -77 C ATOM 764 CD2 TYR A 103 -11.032 -24.742 27.401 1.00 48.44 C ANISOU 764 CD2 TYR A 103 7043 5624 5738 376 -739 46 C ATOM 765 CE1 TYR A 103 -8.605 -25.294 26.212 1.00 50.78 C ANISOU 765 CE1 TYR A 103 7246 5902 6145 556 -820 -120 C ATOM 766 CE2 TYR A 103 -9.955 -25.119 28.179 1.00 57.86 C ANISOU 766 CE2 TYR A 103 8274 6774 6937 473 -826 9 C ATOM 767 CZ TYR A 103 -8.744 -25.395 27.580 1.00 57.67 C ANISOU 767 CZ TYR A 103 8202 6741 6970 566 -868 -75 C ATOM 768 OH TYR A 103 -7.667 -25.770 28.352 1.00 58.65 O ANISOU 768 OH TYR A 103 8357 6825 7101 669 -961 -117 O ATOM 769 N ILE A 104 -14.184 -26.472 25.949 1.00 44.28 N ANISOU 769 N ILE A 104 6679 5036 5110 132 -638 180 N ATOM 770 CA ILE A 104 -14.626 -27.583 26.784 1.00 43.45 C ANISOU 770 CA ILE A 104 6729 4845 4934 103 -689 230 C ATOM 771 C ILE A 104 -14.835 -28.827 25.933 1.00 50.07 C ANISOU 771 C ILE A 104 7648 5612 5765 84 -705 229 C ATOM 772 O ILE A 104 -14.494 -29.945 26.341 1.00 39.18 O ANISOU 772 O ILE A 104 6396 4132 4357 117 -781 233 O ATOM 773 CB ILE A 104 -15.907 -27.196 27.547 1.00 42.42 C ANISOU 773 CB ILE A 104 6624 4756 4736 -3 -639 298 C ATOM 774 CG1 ILE A 104 -15.626 -26.036 28.508 1.00 41.32 C ANISOU 774 CG1 ILE A 104 6419 4679 4603 24 -632 295 C ATOM 775 CG2 ILE A 104 -16.459 -28.397 28.304 1.00 48.03 C ANISOU 775 CG2 ILE A 104 7505 5381 5364 -56 -682 351 C ATOM 776 CD1 ILE A 104 -16.878 -25.353 29.025 1.00 39.52 C ANISOU 776 CD1 ILE A 104 6169 4520 4326 -75 -565 343 C ATOM 777 N ALA A 105 -15.389 -28.651 24.732 1.00 45.72 N ANISOU 777 N ALA A 105 7028 5107 5237 31 -638 222 N ATOM 778 CA ALA A 105 -15.665 -29.792 23.867 1.00 43.35 C ANISOU 778 CA ALA A 105 6799 4745 4928 2 -645 220 C ATOM 779 C ALA A 105 -14.388 -30.557 23.542 1.00 49.82 C ANISOU 779 C ALA A 105 7648 5489 5792 114 -722 155 C ATOM 780 O ALA A 105 -14.347 -31.789 23.637 1.00 58.07 O ANISOU 780 O ALA A 105 8822 6433 6808 124 -780 162 O ATOM 781 CB ALA A 105 -16.353 -29.320 22.585 1.00 43.03 C ANISOU 781 CB ALA A 105 6659 4778 4911 -64 -561 216 C ATOM 782 N ILE A 106 -13.330 -29.843 23.164 1.00 48.95 N ANISOU 782 N ILE A 106 7419 5427 5751 199 -724 86 N ATOM 783 CA ILE A 106 -12.101 -30.503 22.738 1.00 48.46 C ANISOU 783 CA ILE A 106 7361 5313 5738 306 -791 8 C ATOM 784 C ILE A 106 -11.189 -30.845 23.916 1.00 50.45 C ANISOU 784 C ILE A 106 7683 5502 5984 406 -889 -8 C ATOM 785 O ILE A 106 -10.426 -31.814 23.840 1.00 53.41 O ANISOU 785 O ILE A 106 8123 5794 6374 490 -968 -54 O ATOM 786 CB ILE A 106 -11.366 -29.626 21.711 1.00 51.01 C ANISOU 786 CB ILE A 106 7524 5725 6135 343 -745 -67 C ATOM 787 CG1 ILE A 106 -10.314 -30.451 20.970 1.00 57.74 C ANISOU 787 CG1 ILE A 106 8374 6530 7034 432 -797 -155 C ATOM 788 CG2 ILE A 106 -10.710 -28.431 22.394 1.00 46.72 C ANISOU 788 CG2 ILE A 106 6885 5250 5616 389 -742 -88 C ATOM 789 CD1 ILE A 106 -9.670 -29.718 19.823 1.00 64.49 C ANISOU 789 CD1 ILE A 106 9078 7473 7952 447 -744 -232 C ATOM 790 N ALA A 107 -11.252 -30.078 25.007 1.00 51.47 N ANISOU 790 N ALA A 107 7801 5667 6090 402 -890 26 N ATOM 791 CA ALA A 107 -10.351 -30.304 26.134 1.00 51.83 C ANISOU 791 CA ALA A 107 7903 5661 6128 498 -985 8 C ATOM 792 C ALA A 107 -10.812 -31.463 27.011 1.00 54.81 C ANISOU 792 C ALA A 107 8470 5924 6431 477 -1055 71 C ATOM 793 O ALA A 107 -9.987 -32.265 27.464 1.00 62.51 O ANISOU 793 O ALA A 107 9531 6811 7407 573 -1157 42 O ATOM 794 CB ALA A 107 -10.228 -29.033 26.974 1.00 49.03 C ANISOU 794 CB ALA A 107 7465 5389 5774 497 -958 19 C ATOM 795 N ILE A 108 -12.111 -31.557 27.277 1.00 56.78 N ANISOU 795 N ILE A 108 8788 6172 6613 354 -1005 153 N ATOM 796 CA ILE A 108 -12.661 -32.639 28.091 1.00 53.66 C ANISOU 796 CA ILE A 108 8582 5671 6135 310 -1061 217 C ATOM 797 C ILE A 108 -13.902 -33.198 27.404 1.00 57.20 C ANISOU 797 C ILE A 108 9085 6108 6542 185 -999 264 C ATOM 798 O ILE A 108 -15.020 -33.046 27.919 1.00 59.57 O ANISOU 798 O ILE A 108 9427 6434 6774 70 -950 332 O ATOM 799 CB ILE A 108 -12.982 -32.160 29.515 1.00 59.07 C ANISOU 799 CB ILE A 108 9314 6374 6758 274 -1071 274 C ATOM 800 CG1 ILE A 108 -13.791 -30.860 29.481 1.00 55.42 C ANISOU 800 CG1 ILE A 108 8722 6040 6296 188 -961 297 C ATOM 801 CG2 ILE A 108 -11.696 -31.963 30.302 1.00 65.80 C ANISOU 801 CG2 ILE A 108 10158 7207 7638 404 -1160 230 C ATOM 802 CD1 ILE A 108 -14.323 -30.440 30.835 1.00 69.26 C ANISOU 802 CD1 ILE A 108 10523 7814 7978 130 -958 354 C ATOM 803 N PRO A 109 -13.756 -33.862 26.255 1.00 54.92 N ANISOU 803 N PRO A 109 8795 5784 6289 202 -999 226 N ATOM 804 CA PRO A 109 -14.945 -34.342 25.533 1.00 55.80 C ANISOU 804 CA PRO A 109 8945 5893 6362 80 -934 266 C ATOM 805 C PRO A 109 -15.776 -35.342 26.314 1.00 64.25 C ANISOU 805 C PRO A 109 10205 6871 7334 -8 -966 340 C ATOM 806 O PRO A 109 -16.984 -35.453 26.068 1.00 63.63 O ANISOU 806 O PRO A 109 10148 6822 7205 -138 -897 387 O ATOM 807 CB PRO A 109 -14.352 -34.974 24.265 1.00 54.25 C ANISOU 807 CB PRO A 109 8726 5660 6227 140 -950 199 C ATOM 808 CG PRO A 109 -12.941 -35.306 24.621 1.00 54.14 C ANISOU 808 CG PRO A 109 8733 5582 6257 290 -1053 136 C ATOM 809 CD PRO A 109 -12.503 -34.237 25.579 1.00 57.55 C ANISOU 809 CD PRO A 109 9090 6080 6697 331 -1058 138 C ATOM 810 N LEU A 110 -15.173 -36.080 27.248 1.00 76.04 N ANISOU 810 N LEU A 110 11839 8257 8795 54 -1070 349 N ATOM 811 CA LEU A 110 -15.929 -37.090 27.979 1.00 71.08 C ANISOU 811 CA LEU A 110 11410 7532 8065 -37 -1104 420 C ATOM 812 C LEU A 110 -16.866 -36.465 29.004 1.00 70.19 C ANISOU 812 C LEU A 110 11307 7485 7876 -150 -1052 488 C ATOM 813 O LEU A 110 -17.899 -37.056 29.336 1.00 73.24 O ANISOU 813 O LEU A 110 11814 7840 8174 -279 -1031 549 O ATOM 814 CB LEU A 110 -14.972 -38.070 28.657 1.00 84.71 C ANISOU 814 CB LEU A 110 13294 9115 9778 69 -1241 410 C ATOM 815 CG LEU A 110 -14.133 -38.934 27.711 1.00 81.08 C ANISOU 815 CG LEU A 110 12857 8569 9381 176 -1304 342 C ATOM 816 CD1 LEU A 110 -13.188 -39.830 28.498 1.00 78.43 C ANISOU 816 CD1 LEU A 110 12677 8093 9029 291 -1449 330 C ATOM 817 CD2 LEU A 110 -15.024 -39.765 26.797 1.00 76.76 C ANISOU 817 CD2 LEU A 110 12378 7982 8806 73 -1260 361 C ATOM 818 N ARG A 111 -16.535 -35.278 29.509 1.00 77.66 N ANISOU 818 N ARG A 111 12129 8525 8853 -109 -1029 475 N ATOM 819 CA ARG A 111 -17.359 -34.594 30.495 1.00 81.48 C ANISOU 819 CA ARG A 111 12608 9081 9271 -206 -978 528 C ATOM 820 C ARG A 111 -18.156 -33.439 29.900 1.00 84.06 C ANISOU 820 C ARG A 111 12759 9553 9628 -275 -859 522 C ATOM 821 O ARG A 111 -18.713 -32.633 30.652 1.00 79.87 O ANISOU 821 O ARG A 111 12184 9101 9062 -333 -813 549 O ATOM 822 CB ARG A 111 -16.485 -34.078 31.640 1.00 87.46 C ANISOU 822 CB ARG A 111 13363 9836 10031 -118 -1042 521 C ATOM 823 CG ARG A 111 -15.438 -35.078 32.123 1.00 98.26 C ANISOU 823 CG ARG A 111 14877 11067 11392 -11 -1175 510 C ATOM 824 CD ARG A 111 -14.836 -34.681 33.472 1.00112.26 C ANISOU 824 CD ARG A 111 16682 12834 13137 44 -1239 521 C ATOM 825 NE ARG A 111 -15.826 -34.037 34.329 1.00115.79 N ANISOU 825 NE ARG A 111 17125 13358 13510 -79 -1170 577 N ATOM 826 CZ ARG A 111 -15.784 -32.772 34.729 1.00112.21 C ANISOU 826 CZ ARG A 111 16534 13019 13083 -72 -1118 564 C ATOM 827 NH1 ARG A 111 -14.730 -32.004 34.500 1.00111.01 N ANISOU 827 NH1 ARG A 111 16248 12911 13020 52 -1135 501 N ATOM 828 NH2 ARG A 111 -16.827 -32.265 35.381 1.00100.62 N ANISOU 828 NH2 ARG A 111 15062 11623 11547 -194 -1047 609 N ATOM 829 N TYR A 112 -18.232 -33.344 28.571 1.00 66.02 N ANISOU 829 N TYR A 112 10378 7304 7405 -269 -811 487 N ATOM 830 CA TYR A 112 -18.898 -32.208 27.942 1.00 64.79 C ANISOU 830 CA TYR A 112 10055 7280 7283 -319 -708 478 C ATOM 831 C TYR A 112 -20.413 -32.293 28.103 1.00 65.87 C ANISOU 831 C TYR A 112 10223 7463 7340 -474 -636 531 C ATOM 832 O TYR A 112 -21.047 -31.372 28.629 1.00 67.00 O ANISOU 832 O TYR A 112 10293 7701 7463 -526 -581 547 O ATOM 833 CB TYR A 112 -18.519 -32.133 26.461 1.00 59.02 C ANISOU 833 CB TYR A 112 9222 6569 6634 -271 -683 425 C ATOM 834 CG TYR A 112 -19.268 -31.063 25.696 1.00 50.13 C ANISOU 834 CG TYR A 112 7943 5568 5538 -328 -583 420 C ATOM 835 CD1 TYR A 112 -18.768 -29.771 25.599 1.00 50.15 C ANISOU 835 CD1 TYR A 112 7798 5654 5602 -267 -556 387 C ATOM 836 CD2 TYR A 112 -20.477 -31.345 25.075 1.00 60.22 C ANISOU 836 CD2 TYR A 112 9226 6877 6778 -442 -521 447 C ATOM 837 CE1 TYR A 112 -19.451 -28.792 24.904 1.00 50.40 C ANISOU 837 CE1 TYR A 112 7701 5791 5659 -315 -474 384 C ATOM 838 CE2 TYR A 112 -21.168 -30.373 24.380 1.00 60.74 C ANISOU 838 CE2 TYR A 112 9154 7053 6870 -486 -439 442 C ATOM 839 CZ TYR A 112 -20.650 -29.099 24.296 1.00 58.13 C ANISOU 839 CZ TYR A 112 8687 6798 6602 -420 -419 412 C ATOM 840 OH TYR A 112 -21.336 -28.128 23.601 1.00 52.45 O ANISOU 840 OH TYR A 112 7842 6180 5907 -460 -346 408 O ATOM 841 N ASN A 113 -21.012 -33.396 27.646 1.00 72.90 N ANISOU 841 N ASN A 113 11221 8292 8185 -550 -636 552 N ATOM 842 CA ASN A 113 -22.470 -33.494 27.631 1.00 78.25 C ANISOU 842 CA ASN A 113 11913 9027 8791 -703 -562 592 C ATOM 843 C ASN A 113 -23.064 -33.387 29.029 1.00 73.70 C ANISOU 843 C ASN A 113 11410 8467 8124 -783 -558 637 C ATOM 844 O ASN A 113 -24.180 -32.881 29.190 1.00 70.03 O ANISOU 844 O ASN A 113 10889 8102 7619 -889 -481 654 O ATOM 845 CB ASN A 113 -22.899 -34.804 26.972 1.00 79.93 C ANISOU 845 CB ASN A 113 12247 9157 8965 -770 -572 605 C ATOM 846 CG ASN A 113 -22.773 -34.762 25.462 1.00 92.89 C ANISOU 846 CG ASN A 113 13789 10822 10682 -737 -540 563 C ATOM 847 OD1 ASN A 113 -23.002 -33.725 24.836 1.00 82.89 O ANISOU 847 OD1 ASN A 113 12361 9666 9468 -730 -476 540 O ATOM 848 ND2 ASN A 113 -22.406 -35.891 24.868 1.00 92.65 N ANISOU 848 ND2 ASN A 113 13859 10687 10655 -717 -587 551 N ATOM 849 N GLY A 114 -22.346 -33.864 30.048 1.00 63.04 N ANISOU 849 N GLY A 114 10186 7025 6740 -736 -642 655 N ATOM 850 CA GLY A 114 -22.821 -33.703 31.410 1.00 67.42 C ANISOU 850 CA GLY A 114 10808 7599 7208 -810 -640 695 C ATOM 851 C GLY A 114 -22.609 -32.309 31.954 1.00 67.37 C ANISOU 851 C GLY A 114 10658 7698 7240 -761 -609 676 C ATOM 852 O GLY A 114 -23.413 -31.827 32.759 1.00 74.74 O ANISOU 852 O GLY A 114 11579 8707 8113 -850 -561 698 O ATOM 853 N LEU A 115 -21.539 -31.639 31.525 1.00 65.92 N ANISOU 853 N LEU A 115 10365 7525 7156 -624 -634 631 N ATOM 854 CA LEU A 115 -21.234 -30.300 32.019 1.00 64.54 C ANISOU 854 CA LEU A 115 10058 7442 7021 -571 -609 609 C ATOM 855 C LEU A 115 -22.070 -29.243 31.305 1.00 64.60 C ANISOU 855 C LEU A 115 9899 7579 7066 -616 -509 591 C ATOM 856 O LEU A 115 -22.780 -28.460 31.944 1.00 62.59 O ANISOU 856 O LEU A 115 9589 7413 6781 -675 -457 601 O ATOM 857 CB LEU A 115 -19.738 -30.018 31.846 1.00 63.71 C ANISOU 857 CB LEU A 115 9905 7298 7002 -413 -676 564 C ATOM 858 CG LEU A 115 -19.230 -28.617 32.193 1.00 70.12 C ANISOU 858 CG LEU A 115 10573 8198 7870 -345 -654 532 C ATOM 859 CD1 LEU A 115 -19.592 -28.238 33.618 1.00 78.81 C ANISOU 859 CD1 LEU A 115 11716 9329 8899 -394 -654 564 C ATOM 860 CD2 LEU A 115 -17.723 -28.548 31.989 1.00 68.75 C ANISOU 860 CD2 LEU A 115 10369 7980 7773 -198 -726 483 C ATOM 861 N VAL A 116 -22.001 -29.211 29.978 1.00 62.64 N ANISOU 861 N VAL A 116 9573 7343 6884 -589 -484 563 N ATOM 862 CA VAL A 116 -22.654 -28.187 29.171 1.00 59.69 C ANISOU 862 CA VAL A 116 9041 7083 6555 -613 -401 543 C ATOM 863 C VAL A 116 -23.975 -28.754 28.669 1.00 55.71 C ANISOU 863 C VAL A 116 8565 6606 5997 -741 -346 567 C ATOM 864 O VAL A 116 -23.999 -29.576 27.746 1.00 63.60 O ANISOU 864 O VAL A 116 9605 7555 7004 -754 -353 564 O ATOM 865 CB VAL A 116 -21.761 -27.740 28.006 1.00 60.83 C ANISOU 865 CB VAL A 116 9080 7231 6801 -512 -406 496 C ATOM 866 CG1 VAL A 116 -22.477 -26.721 27.146 1.00 53.83 C ANISOU 866 CG1 VAL A 116 8047 6453 5954 -542 -327 482 C ATOM 867 CG2 VAL A 116 -20.448 -27.173 28.525 1.00 50.92 C ANISOU 867 CG2 VAL A 116 7792 5958 5597 -392 -458 466 C ATOM 868 N THR A 117 -25.077 -28.308 29.264 1.00 57.25 N ANISOU 868 N THR A 117 8732 6884 6135 -836 -290 584 N ATOM 869 CA THR A 117 -26.416 -28.743 28.895 1.00 56.08 C ANISOU 869 CA THR A 117 8596 6783 5929 -966 -232 600 C ATOM 870 C THR A 117 -27.223 -27.556 28.381 1.00 54.25 C ANISOU 870 C THR A 117 8196 6683 5733 -984 -157 575 C ATOM 871 O THR A 117 -26.780 -26.405 28.419 1.00 55.51 O ANISOU 871 O THR A 117 8245 6892 5955 -904 -151 552 O ATOM 872 CB THR A 117 -27.137 -29.393 30.084 1.00 62.47 C ANISOU 872 CB THR A 117 9531 7581 6625 -1082 -230 636 C ATOM 873 OG1 THR A 117 -27.302 -28.430 31.133 1.00 63.36 O ANISOU 873 OG1 THR A 117 9586 7769 6720 -1083 -210 632 O ATOM 874 CG2 THR A 117 -26.345 -30.585 30.609 1.00 60.62 C ANISOU 874 CG2 THR A 117 9479 7205 6350 -1062 -314 665 C ATOM 875 N GLY A 118 -28.430 -27.854 27.899 1.00 61.81 N ANISOU 875 N GLY A 118 9140 7697 6648 -1092 -103 580 N ATOM 876 CA GLY A 118 -29.268 -26.810 27.333 1.00 58.64 C ANISOU 876 CA GLY A 118 8584 7419 6279 -1107 -39 554 C ATOM 877 C GLY A 118 -29.857 -25.886 28.383 1.00 59.81 C ANISOU 877 C GLY A 118 8668 7659 6396 -1135 -5 545 C ATOM 878 O GLY A 118 -29.940 -24.673 28.176 1.00 64.41 O ANISOU 878 O GLY A 118 9119 8319 7036 -1081 20 518 O ATOM 879 N THR A 119 -30.278 -26.444 29.521 1.00 60.82 N ANISOU 879 N THR A 119 8895 7780 6433 -1222 -4 566 N ATOM 880 CA THR A 119 -30.861 -25.614 30.571 1.00 67.16 C ANISOU 880 CA THR A 119 9641 8676 7200 -1256 31 552 C ATOM 881 C THR A 119 -29.836 -24.633 31.125 1.00 56.92 C ANISOU 881 C THR A 119 8296 7368 5964 -1136 -2 540 C ATOM 882 O THR A 119 -30.156 -23.466 31.380 1.00 59.40 O ANISOU 882 O THR A 119 8492 7772 6306 -1111 31 511 O ATOM 883 CB THR A 119 -31.419 -26.492 31.692 1.00 64.51 C ANISOU 883 CB THR A 119 9436 8327 6746 -1380 35 577 C ATOM 884 OG1 THR A 119 -30.391 -27.364 32.181 1.00 75.01 O ANISOU 884 OG1 THR A 119 10920 9524 8055 -1348 -37 613 O ATOM 885 CG2 THR A 119 -32.590 -27.320 31.186 1.00 71.78 C ANISOU 885 CG2 THR A 119 10387 9284 7601 -1515 80 581 C ATOM 886 N ARG A 120 -28.597 -25.088 31.315 1.00 53.90 N ANISOU 886 N ARG A 120 8001 6876 5603 -1060 -69 558 N ATOM 887 CA ARG A 120 -27.547 -24.187 31.773 1.00 58.09 C ANISOU 887 CA ARG A 120 8483 7395 6192 -945 -102 543 C ATOM 888 C ARG A 120 -27.216 -23.136 30.724 1.00 59.15 C ANISOU 888 C ARG A 120 8474 7570 6429 -854 -85 510 C ATOM 889 O ARG A 120 -26.898 -21.993 31.073 1.00 56.95 O ANISOU 889 O ARG A 120 8109 7337 6194 -792 -79 488 O ATOM 890 CB ARG A 120 -26.304 -24.991 32.142 1.00 60.70 C ANISOU 890 CB ARG A 120 8939 7602 6523 -882 -182 564 C ATOM 891 CG ARG A 120 -26.501 -25.823 33.390 1.00 68.62 C ANISOU 891 CG ARG A 120 10090 8561 7422 -960 -208 598 C ATOM 892 CD ARG A 120 -25.487 -26.936 33.509 1.00 65.57 C ANISOU 892 CD ARG A 120 9851 8037 7025 -913 -293 623 C ATOM 893 NE ARG A 120 -25.549 -27.547 34.830 1.00 65.00 N ANISOU 893 NE ARG A 120 9921 7921 6855 -975 -328 657 N ATOM 894 CZ ARG A 120 -24.816 -28.581 35.216 1.00 76.49 C ANISOU 894 CZ ARG A 120 11533 9254 8276 -951 -409 685 C ATOM 895 NH1 ARG A 120 -23.975 -29.180 34.388 1.00 70.85 N ANISOU 895 NH1 ARG A 120 10852 8448 7618 -865 -463 678 N ATOM 896 NH2 ARG A 120 -24.926 -29.022 36.465 1.00 92.48 N ANISOU 896 NH2 ARG A 120 13686 11245 10205 -1013 -438 718 N ATOM 897 N ALA A 121 -27.291 -23.497 29.441 1.00 53.16 N ANISOU 897 N ALA A 121 7696 6796 5708 -851 -78 507 N ATOM 898 CA ALA A 121 -27.042 -22.521 28.386 1.00 52.25 C ANISOU 898 CA ALA A 121 7453 6719 5681 -778 -62 479 C ATOM 899 C ALA A 121 -28.103 -21.428 28.386 1.00 46.55 C ANISOU 899 C ALA A 121 6612 6113 4962 -809 -4 459 C ATOM 900 O ALA A 121 -27.781 -20.242 28.252 1.00 44.94 O ANISOU 900 O ALA A 121 6310 5946 4819 -738 1 436 O ATOM 901 CB ALA A 121 -26.992 -23.221 27.027 1.00 47.93 C ANISOU 901 CB ALA A 121 6917 6134 5161 -782 -64 481 C ATOM 902 N ALA A 122 -29.375 -21.808 28.541 1.00 48.36 N ANISOU 902 N ALA A 122 6847 6401 5125 -915 37 464 N ATOM 903 CA ALA A 122 -30.450 -20.822 28.523 1.00 50.87 C ANISOU 903 CA ALA A 122 7047 6835 5446 -941 88 436 C ATOM 904 C ALA A 122 -30.335 -19.842 29.683 1.00 47.73 C ANISOU 904 C ALA A 122 6608 6480 5047 -908 92 418 C ATOM 905 O ALA A 122 -30.680 -18.664 29.536 1.00 43.49 O ANISOU 905 O ALA A 122 5957 6015 4552 -869 115 388 O ATOM 906 CB ALA A 122 -31.807 -21.524 28.561 1.00 47.50 C ANISOU 906 CB ALA A 122 6638 6469 4940 -1068 131 437 C ATOM 907 N GLY A 123 -29.862 -20.306 30.840 1.00 44.67 N ANISOU 907 N GLY A 123 6315 6048 4610 -923 67 436 N ATOM 908 CA GLY A 123 -29.701 -19.407 31.970 1.00 40.13 C ANISOU 908 CA GLY A 123 5705 5510 4031 -894 69 418 C ATOM 909 C GLY A 123 -28.532 -18.460 31.791 1.00 44.05 C ANISOU 909 C GLY A 123 6149 5975 4615 -770 38 405 C ATOM 910 O GLY A 123 -28.613 -17.283 32.154 1.00 46.24 O ANISOU 910 O GLY A 123 6338 6308 4921 -730 54 376 O ATOM 911 N ILE A 124 -27.427 -18.959 31.236 1.00 45.04 N ANISOU 911 N ILE A 124 6326 6008 4779 -710 -8 420 N ATOM 912 CA ILE A 124 -26.289 -18.095 30.943 1.00 43.14 C ANISOU 912 CA ILE A 124 6031 5742 4619 -600 -35 402 C ATOM 913 C ILE A 124 -26.684 -17.027 29.932 1.00 40.38 C ANISOU 913 C ILE A 124 5559 5450 4333 -569 -2 377 C ATOM 914 O ILE A 124 -26.298 -15.859 30.057 1.00 40.00 O ANISOU 914 O ILE A 124 5438 5426 4333 -507 -1 354 O ATOM 915 CB ILE A 124 -25.100 -18.937 30.444 1.00 48.47 C ANISOU 915 CB ILE A 124 6779 6316 5320 -549 -88 415 C ATOM 916 CG1 ILE A 124 -24.573 -19.818 31.577 1.00 51.94 C ANISOU 916 CG1 ILE A 124 7341 6691 5702 -559 -134 437 C ATOM 917 CG2 ILE A 124 -23.999 -18.036 29.895 1.00 45.77 C ANISOU 917 CG2 ILE A 124 6365 5961 5065 -447 -106 388 C ATOM 918 CD1 ILE A 124 -23.666 -20.937 31.113 1.00 55.23 C ANISOU 918 CD1 ILE A 124 7849 7007 6128 -524 -188 449 C ATOM 919 N ILE A 125 -27.464 -17.409 28.918 1.00 41.68 N ANISOU 919 N ILE A 125 5704 5636 4495 -615 22 383 N ATOM 920 CA ILE A 125 -27.892 -16.450 27.903 1.00 41.95 C ANISOU 920 CA ILE A 125 5631 5723 4584 -588 46 363 C ATOM 921 C ILE A 125 -28.740 -15.353 28.532 1.00 40.20 C ANISOU 921 C ILE A 125 5328 5590 4357 -592 77 336 C ATOM 922 O ILE A 125 -28.578 -14.166 28.221 1.00 31.64 O ANISOU 922 O ILE A 125 4165 4529 3330 -530 78 314 O ATOM 923 CB ILE A 125 -28.646 -17.174 26.772 1.00 46.41 C ANISOU 923 CB ILE A 125 6197 6298 5136 -644 64 373 C ATOM 924 CG1 ILE A 125 -27.671 -18.011 25.938 1.00 40.13 C ANISOU 924 CG1 ILE A 125 5463 5416 4367 -618 32 389 C ATOM 925 CG2 ILE A 125 -29.391 -16.170 25.895 1.00 45.23 C ANISOU 925 CG2 ILE A 125 5938 6219 5026 -630 89 353 C ATOM 926 CD1 ILE A 125 -28.347 -19.011 25.013 1.00 45.38 C ANISOU 926 CD1 ILE A 125 6159 6078 5006 -686 46 403 C ATOM 927 N ALA A 126 -29.658 -15.729 29.425 1.00 39.14 N ANISOU 927 N ALA A 126 5214 5506 4153 -668 102 334 N ATOM 928 CA ALA A 126 -30.486 -14.733 30.096 1.00 37.58 C ANISOU 928 CA ALA A 126 4934 5397 3946 -674 132 299 C ATOM 929 C ALA A 126 -29.638 -13.795 30.948 1.00 38.82 C ANISOU 929 C ALA A 126 5076 5539 4134 -602 114 284 C ATOM 930 O ALA A 126 -29.851 -12.576 30.944 1.00 32.55 O ANISOU 930 O ALA A 126 4195 4791 3382 -553 125 253 O ATOM 931 CB ALA A 126 -31.545 -15.427 30.953 1.00 35.00 C ANISOU 931 CB ALA A 126 4639 5130 3530 -780 165 295 C ATOM 932 N ILE A 127 -28.670 -14.345 31.685 1.00 36.12 N ANISOU 932 N ILE A 127 4821 5132 3772 -592 84 305 N ATOM 933 CA ILE A 127 -27.815 -13.517 32.531 1.00 37.92 C ANISOU 933 CA ILE A 127 5038 5345 4025 -527 65 290 C ATOM 934 C ILE A 127 -26.987 -12.565 31.680 1.00 34.74 C ANISOU 934 C ILE A 127 4576 4915 3709 -436 47 278 C ATOM 935 O ILE A 127 -26.789 -11.398 32.040 1.00 35.46 O ANISOU 935 O ILE A 127 4608 5030 3834 -386 51 250 O ATOM 936 CB ILE A 127 -26.921 -14.405 33.417 1.00 42.30 C ANISOU 936 CB ILE A 127 5703 5831 4537 -534 27 316 C ATOM 937 CG1 ILE A 127 -27.767 -15.121 34.472 1.00 44.38 C ANISOU 937 CG1 ILE A 127 6027 6129 4705 -632 47 326 C ATOM 938 CG2 ILE A 127 -25.828 -13.573 34.082 1.00 37.40 C ANISOU 938 CG2 ILE A 127 5068 5188 3953 -455 0 300 C ATOM 939 CD1 ILE A 127 -27.071 -16.297 35.127 1.00 46.49 C ANISOU 939 CD1 ILE A 127 6428 6317 4918 -655 4 363 C ATOM 940 N CYS A 128 -26.488 -13.047 30.540 1.00 36.29 N ANISOU 940 N CYS A 128 4789 5060 3939 -417 30 295 N ATOM 941 CA CYS A 128 -25.666 -12.202 29.681 1.00 36.32 C ANISOU 941 CA CYS A 128 4744 5038 4018 -343 16 282 C ATOM 942 C CYS A 128 -26.468 -11.049 29.093 1.00 34.50 C ANISOU 942 C CYS A 128 4420 4865 3822 -329 41 260 C ATOM 943 O CYS A 128 -25.923 -9.958 28.889 1.00 27.91 O ANISOU 943 O CYS A 128 3541 4024 3039 -270 34 242 O ATOM 944 CB CYS A 128 -25.039 -13.045 28.574 1.00 36.93 C ANISOU 944 CB CYS A 128 4859 5055 4116 -337 -4 300 C ATOM 945 SG CYS A 128 -23.720 -14.132 29.170 1.00 40.27 S ANISOU 945 SG CYS A 128 5383 5394 4522 -315 -51 313 S ATOM 946 N TRP A 129 -27.757 -11.259 28.826 1.00 35.07 N ANISOU 946 N TRP A 129 4465 4995 3865 -383 69 259 N ATOM 947 CA TRP A 129 -28.582 -10.165 28.325 1.00 34.51 C ANISOU 947 CA TRP A 129 4306 4982 3826 -362 85 235 C ATOM 948 C TRP A 129 -28.835 -9.124 29.409 1.00 36.16 C ANISOU 948 C TRP A 129 4470 5236 4035 -335 95 201 C ATOM 949 O TRP A 129 -28.802 -7.918 29.137 1.00 36.84 O ANISOU 949 O TRP A 129 4498 5330 4168 -279 89 178 O ATOM 950 CB TRP A 129 -29.899 -10.710 27.781 1.00 36.95 C ANISOU 950 CB TRP A 129 4591 5347 4100 -425 109 235 C ATOM 951 CG TRP A 129 -29.825 -11.124 26.346 1.00 34.35 C ANISOU 951 CG TRP A 129 4267 4989 3796 -428 101 256 C ATOM 952 CD1 TRP A 129 -29.699 -12.393 25.861 1.00 36.26 C ANISOU 952 CD1 TRP A 129 4571 5195 4011 -477 99 284 C ATOM 953 CD2 TRP A 129 -29.876 -10.261 25.205 1.00 36.37 C ANISOU 953 CD2 TRP A 129 4468 5246 4105 -384 91 251 C ATOM 954 NE1 TRP A 129 -29.669 -12.373 24.487 1.00 33.57 N ANISOU 954 NE1 TRP A 129 4212 4840 3705 -466 93 293 N ATOM 955 CE2 TRP A 129 -29.776 -11.076 24.060 1.00 36.83 C ANISOU 955 CE2 TRP A 129 4554 5274 4164 -411 87 275 C ATOM 956 CE3 TRP A 129 -29.996 -8.878 25.040 1.00 28.18 C ANISOU 956 CE3 TRP A 129 3368 4228 3112 -324 83 228 C ATOM 957 CZ2 TRP A 129 -29.793 -10.554 22.768 1.00 37.96 C ANISOU 957 CZ2 TRP A 129 4664 5412 4348 -386 77 278 C ATOM 958 CZ3 TRP A 129 -30.011 -8.360 23.758 1.00 33.42 C ANISOU 958 CZ3 TRP A 129 4004 4879 3815 -298 68 234 C ATOM 959 CH2 TRP A 129 -29.913 -9.197 22.638 1.00 40.83 C ANISOU 959 CH2 TRP A 129 4972 5794 4750 -331 66 259 C ATOM 960 N VAL A 130 -29.088 -9.566 30.644 1.00 33.65 N ANISOU 960 N VAL A 130 4181 4943 3659 -378 108 195 N ATOM 961 CA VAL A 130 -29.254 -8.623 31.748 1.00 32.20 C ANISOU 961 CA VAL A 130 3959 4804 3473 -355 118 160 C ATOM 962 C VAL A 130 -27.984 -7.803 31.935 1.00 36.28 C ANISOU 962 C VAL A 130 4480 5264 4040 -280 91 156 C ATOM 963 O VAL A 130 -28.030 -6.577 32.089 1.00 31.44 O ANISOU 963 O VAL A 130 3811 4672 3465 -231 92 124 O ATOM 964 CB VAL A 130 -29.638 -9.370 33.039 1.00 40.13 C ANISOU 964 CB VAL A 130 5009 5841 4399 -426 136 159 C ATOM 965 CG1 VAL A 130 -29.572 -8.437 34.237 1.00 33.76 C ANISOU 965 CG1 VAL A 130 4170 5069 3588 -400 143 122 C ATOM 966 CG2 VAL A 130 -31.029 -9.970 32.915 1.00 37.41 C ANISOU 966 CG2 VAL A 130 4643 5571 4002 -507 170 149 C ATOM 967 N LEU A 131 -26.827 -8.469 31.925 1.00 33.87 N ANISOU 967 N LEU A 131 4243 4890 3737 -270 65 184 N ATOM 968 CA LEU A 131 -25.566 -7.749 32.058 1.00 29.32 C ANISOU 968 CA LEU A 131 3668 4266 3207 -204 40 175 C ATOM 969 C LEU A 131 -25.300 -6.852 30.856 1.00 30.67 C ANISOU 969 C LEU A 131 3791 4419 3444 -156 34 168 C ATOM 970 O LEU A 131 -24.661 -5.802 30.999 1.00 32.88 O ANISOU 970 O LEU A 131 4046 4684 3763 -106 25 147 O ATOM 971 CB LEU A 131 -24.420 -8.739 32.246 1.00 36.12 C ANISOU 971 CB LEU A 131 4607 5062 4055 -202 10 199 C ATOM 972 CG LEU A 131 -24.462 -9.558 33.536 1.00 43.19 C ANISOU 972 CG LEU A 131 5568 5961 4883 -243 4 210 C ATOM 973 CD1 LEU A 131 -23.416 -10.661 33.496 1.00 44.63 C ANISOU 973 CD1 LEU A 131 5833 6071 5054 -235 -36 236 C ATOM 974 CD2 LEU A 131 -24.249 -8.661 34.743 1.00 36.68 C ANISOU 974 CD2 LEU A 131 4722 5164 4053 -219 6 182 C ATOM 975 N SER A 132 -25.775 -7.243 29.669 1.00 31.40 N ANISOU 975 N SER A 132 3876 4510 3546 -176 38 185 N ATOM 976 CA SER A 132 -25.582 -6.414 28.482 1.00 31.52 C ANISOU 976 CA SER A 132 3854 4507 3616 -139 31 181 C ATOM 977 C SER A 132 -26.350 -5.103 28.600 1.00 33.65 C ANISOU 977 C SER A 132 4060 4819 3907 -109 38 152 C ATOM 978 O SER A 132 -25.841 -4.040 28.218 1.00 24.59 O ANISOU 978 O SER A 132 2893 3645 2804 -63 26 140 O ATOM 979 CB SER A 132 -26.013 -7.183 27.230 1.00 34.83 C ANISOU 979 CB SER A 132 4281 4921 4033 -172 33 206 C ATOM 980 OG SER A 132 -25.136 -8.268 26.966 1.00 31.94 O ANISOU 980 OG SER A 132 3973 4504 3659 -186 21 227 O ATOM 981 N PHE A 133 -27.575 -5.157 29.130 1.00 32.15 N ANISOU 981 N PHE A 133 3838 4694 3684 -135 58 136 N ATOM 982 CA PHE A 133 -28.319 -3.930 29.385 1.00 32.28 C ANISOU 982 CA PHE A 133 3790 4753 3720 -99 62 98 C ATOM 983 C PHE A 133 -27.626 -3.083 30.447 1.00 34.77 C ANISOU 983 C PHE A 133 4107 5057 4049 -60 58 73 C ATOM 984 O PHE A 133 -27.472 -1.866 30.281 1.00 36.31 O ANISOU 984 O PHE A 133 4273 5237 4286 -8 45 51 O ATOM 985 CB PHE A 133 -29.753 -4.261 29.802 1.00 31.18 C ANISOU 985 CB PHE A 133 3610 4698 3538 -140 87 76 C ATOM 986 CG PHE A 133 -30.684 -4.493 28.642 1.00 33.66 C ANISOU 986 CG PHE A 133 3892 5040 3856 -156 87 82 C ATOM 987 CD1 PHE A 133 -31.383 -3.438 28.080 1.00 31.92 C ANISOU 987 CD1 PHE A 133 3610 4846 3672 -108 74 55 C ATOM 988 CD2 PHE A 133 -30.862 -5.763 28.115 1.00 32.68 C ANISOU 988 CD2 PHE A 133 3803 4915 3699 -217 96 114 C ATOM 989 CE1 PHE A 133 -32.239 -3.643 27.018 1.00 31.91 C ANISOU 989 CE1 PHE A 133 3580 4873 3673 -120 69 60 C ATOM 990 CE2 PHE A 133 -31.720 -5.971 27.050 1.00 33.99 C ANISOU 990 CE2 PHE A 133 3938 5111 3867 -234 97 118 C ATOM 991 CZ PHE A 133 -32.407 -4.908 26.502 1.00 32.01 C ANISOU 991 CZ PHE A 133 3621 4889 3651 -185 82 91 C ATOM 992 N ALA A 134 -27.185 -3.714 31.538 1.00 30.64 N ANISOU 992 N ALA A 134 3620 4534 3487 -86 65 76 N ATOM 993 CA ALA A 134 -26.501 -2.980 32.600 1.00 34.00 C ANISOU 993 CA ALA A 134 4049 4951 3919 -54 61 51 C ATOM 994 C ALA A 134 -25.252 -2.284 32.071 1.00 32.77 C ANISOU 994 C ALA A 134 3906 4729 3816 -5 37 56 C ATOM 995 O ALA A 134 -25.057 -1.083 32.286 1.00 31.86 O ANISOU 995 O ALA A 134 3765 4609 3733 37 32 27 O ATOM 996 CB ALA A 134 -26.143 -3.932 33.743 1.00 30.67 C ANISOU 996 CB ALA A 134 3678 4533 3441 -95 65 62 C ATOM 997 N ILE A 135 -24.389 -3.027 31.377 1.00 28.29 N ANISOU 997 N ILE A 135 3380 4113 3255 -14 23 86 N ATOM 998 CA ILE A 135 -23.172 -2.431 30.832 1.00 31.62 C ANISOU 998 CA ILE A 135 3811 4481 3721 21 5 84 C ATOM 999 C ILE A 135 -23.521 -1.378 29.786 1.00 30.66 C ANISOU 999 C ILE A 135 3657 4350 3642 46 2 78 C ATOM 1000 O ILE A 135 -23.011 -0.251 29.817 1.00 31.57 O ANISOU 1000 O ILE A 135 3762 4443 3789 79 -6 58 O ATOM 1001 CB ILE A 135 -22.255 -3.525 30.254 1.00 28.58 C ANISOU 1001 CB ILE A 135 3471 4055 3334 5 -8 110 C ATOM 1002 CG1 ILE A 135 -21.672 -4.379 31.380 1.00 27.26 C ANISOU 1002 CG1 ILE A 135 3345 3882 3129 -4 -18 113 C ATOM 1003 CG2 ILE A 135 -21.134 -2.909 29.435 1.00 26.53 C ANISOU 1003 CG2 ILE A 135 3210 3752 3119 32 -21 103 C ATOM 1004 CD1 ILE A 135 -21.099 -5.703 30.915 1.00 35.97 C ANISOU 1004 CD1 ILE A 135 4497 4950 4218 -21 -35 138 C ATOM 1005 N GLY A 136 -24.414 -1.722 28.856 1.00 32.41 N ANISOU 1005 N GLY A 136 3866 4587 3861 27 5 96 N ATOM 1006 CA GLY A 136 -24.701 -0.828 27.748 1.00 29.48 C ANISOU 1006 CA GLY A 136 3475 4199 3526 49 -6 97 C ATOM 1007 C GLY A 136 -25.400 0.452 28.158 1.00 31.04 C ANISOU 1007 C GLY A 136 3634 4417 3741 89 -11 64 C ATOM 1008 O GLY A 136 -25.186 1.500 27.542 1.00 31.93 O ANISOU 1008 O GLY A 136 3749 4495 3888 120 -29 59 O ATOM 1009 N LEU A 137 -26.244 0.392 29.188 1.00 31.75 N ANISOU 1009 N LEU A 137 3694 4563 3805 88 4 39 N ATOM 1010 CA LEU A 137 -27.014 1.547 29.630 1.00 32.15 C ANISOU 1010 CA LEU A 137 3701 4642 3873 131 -1 -2 C ATOM 1011 C LEU A 137 -26.445 2.190 30.892 1.00 29.30 C ANISOU 1011 C LEU A 137 3342 4279 3513 153 5 -34 C ATOM 1012 O LEU A 137 -27.153 2.947 31.565 1.00 29.39 O ANISOU 1012 O LEU A 137 3313 4325 3527 181 8 -76 O ATOM 1013 CB LEU A 137 -28.472 1.149 29.859 1.00 37.88 C ANISOU 1013 CB LEU A 137 4378 5445 4570 115 14 -21 C ATOM 1014 CG LEU A 137 -29.189 0.536 28.652 1.00 36.49 C ANISOU 1014 CG LEU A 137 4192 5282 4389 92 9 5 C ATOM 1015 CD1 LEU A 137 -30.630 0.214 28.998 1.00 31.08 C ANISOU 1015 CD1 LEU A 137 3449 4685 3674 74 27 -26 C ATOM 1016 CD2 LEU A 137 -29.120 1.460 27.442 1.00 33.54 C ANISOU 1016 CD2 LEU A 137 3822 4861 4061 135 -24 14 C ATOM 1017 N THR A 138 -25.188 1.907 31.225 1.00 29.14 N ANISOU 1017 N THR A 138 3361 4220 3489 141 5 -20 N ATOM 1018 CA THR A 138 -24.554 2.566 32.364 1.00 32.26 C ANISOU 1018 CA THR A 138 3759 4610 3886 162 7 -50 C ATOM 1019 C THR A 138 -24.623 4.086 32.290 1.00 29.49 C ANISOU 1019 C THR A 138 3392 4237 3576 212 -6 -83 C ATOM 1020 O THR A 138 -24.811 4.718 33.343 1.00 29.66 O ANISOU 1020 O THR A 138 3393 4283 3594 232 1 -123 O ATOM 1021 CB THR A 138 -23.093 2.102 32.479 1.00 33.93 C ANISOU 1021 CB THR A 138 4015 4780 4096 148 1 -32 C ATOM 1022 OG1 THR A 138 -23.055 0.752 32.955 1.00 37.18 O ANISOU 1022 OG1 THR A 138 4449 5214 4465 110 10 -11 O ATOM 1023 CG2 THR A 138 -22.313 2.978 33.436 1.00 35.02 C ANISOU 1023 CG2 THR A 138 4156 4907 4244 173 -1 -65 C ATOM 1024 N PRO A 139 -24.480 4.729 31.128 1.00 30.28 N ANISOU 1024 N PRO A 139 3505 4288 3711 230 -27 -70 N ATOM 1025 CA PRO A 139 -24.604 6.195 31.099 1.00 32.53 C ANISOU 1025 CA PRO A 139 3786 4544 4030 278 -46 -100 C ATOM 1026 C PRO A 139 -25.920 6.705 31.657 1.00 32.34 C ANISOU 1026 C PRO A 139 3712 4570 4007 315 -46 -142 C ATOM 1027 O PRO A 139 -25.956 7.809 32.218 1.00 30.35 O ANISOU 1027 O PRO A 139 3452 4306 3774 356 -55 -183 O ATOM 1028 CB PRO A 139 -24.450 6.526 29.609 1.00 30.08 C ANISOU 1028 CB PRO A 139 3505 4178 3745 280 -70 -69 C ATOM 1029 CG PRO A 139 -23.596 5.427 29.077 1.00 30.33 C ANISOU 1029 CG PRO A 139 3564 4199 3762 231 -59 -31 C ATOM 1030 CD PRO A 139 -24.020 4.193 29.834 1.00 33.43 C ANISOU 1030 CD PRO A 139 3934 4651 4118 206 -36 -27 C ATOM 1031 N MET A 140 -27.007 5.941 31.526 1.00 29.13 N ANISOU 1031 N MET A 140 3268 4223 3578 300 -36 -140 N ATOM 1032 CA MET A 140 -28.284 6.366 32.085 1.00 30.05 C ANISOU 1032 CA MET A 140 3324 4402 3691 332 -34 -191 C ATOM 1033 C MET A 140 -28.317 6.284 33.606 1.00 32.83 C ANISOU 1033 C MET A 140 3653 4807 4014 320 -4 -231 C ATOM 1034 O MET A 140 -29.220 6.863 34.217 1.00 33.96 O ANISOU 1034 O MET A 140 3745 5000 4158 352 0 -287 O ATOM 1035 CB MET A 140 -29.417 5.529 31.494 1.00 32.49 C ANISOU 1035 CB MET A 140 3596 4768 3980 310 -29 -181 C ATOM 1036 CG MET A 140 -29.647 5.786 30.011 1.00 38.01 C ANISOU 1036 CG MET A 140 4308 5425 4708 331 -63 -152 C ATOM 1037 SD MET A 140 -30.943 4.759 29.300 1.00 50.81 S ANISOU 1037 SD MET A 140 5884 7119 6303 300 -57 -142 S ATOM 1038 CE MET A 140 -32.401 5.712 29.721 1.00 44.96 C ANISOU 1038 CE MET A 140 5060 6445 5576 367 -73 -220 C ATOM 1039 N LEU A 141 -27.367 5.594 34.230 1.00 35.53 N ANISOU 1039 N LEU A 141 4031 5141 4329 278 14 -209 N ATOM 1040 CA LEU A 141 -27.271 5.583 35.682 1.00 32.28 C ANISOU 1040 CA LEU A 141 3607 4772 3886 265 38 -244 C ATOM 1041 C LEU A 141 -26.505 6.783 36.227 1.00 37.16 C ANISOU 1041 C LEU A 141 4239 5348 4534 306 27 -275 C ATOM 1042 O LEU A 141 -26.286 6.854 37.443 1.00 35.28 O ANISOU 1042 O LEU A 141 3995 5139 4271 296 45 -304 O ATOM 1043 CB LEU A 141 -26.612 4.283 36.157 1.00 32.85 C ANISOU 1043 CB LEU A 141 3719 4852 3912 203 55 -205 C ATOM 1044 CG LEU A 141 -27.274 2.980 35.699 1.00 31.82 C ANISOU 1044 CG LEU A 141 3589 4757 3745 152 67 -172 C ATOM 1045 CD1 LEU A 141 -26.564 1.788 36.315 1.00 39.27 C ANISOU 1045 CD1 LEU A 141 4582 5697 4640 99 77 -139 C ATOM 1046 CD2 LEU A 141 -28.752 2.951 36.044 1.00 39.01 C ANISOU 1046 CD2 LEU A 141 4438 5753 4630 141 89 -213 C ATOM 1047 N GLY A 142 -26.093 7.719 35.368 1.00 29.11 N ANISOU 1047 N GLY A 142 3240 4258 3561 345 -1 -268 N ATOM 1048 CA GLY A 142 -25.475 8.948 35.831 1.00 25.83 C ANISOU 1048 CA GLY A 142 2840 3800 3173 382 -12 -302 C ATOM 1049 C GLY A 142 -24.208 9.343 35.100 1.00 28.76 C ANISOU 1049 C GLY A 142 3268 4089 3571 378 -31 -270 C ATOM 1050 O GLY A 142 -23.793 10.504 35.160 1.00 32.28 O ANISOU 1050 O GLY A 142 3734 4487 4044 408 -46 -295 O ATOM 1051 N TRP A 143 -23.571 8.394 34.417 1.00 31.79 N ANISOU 1051 N TRP A 143 3679 4457 3943 338 -29 -220 N ATOM 1052 CA TRP A 143 -22.324 8.669 33.704 1.00 30.01 C ANISOU 1052 CA TRP A 143 3501 4165 3737 324 -41 -196 C ATOM 1053 C TRP A 143 -22.654 9.192 32.306 1.00 30.00 C ANISOU 1053 C TRP A 143 3519 4114 3764 338 -66 -174 C ATOM 1054 O TRP A 143 -22.515 8.509 31.290 1.00 30.39 O ANISOU 1054 O TRP A 143 3583 4151 3811 311 -69 -134 O ATOM 1055 CB TRP A 143 -21.453 7.420 33.654 1.00 27.07 C ANISOU 1055 CB TRP A 143 3144 3800 3340 279 -30 -163 C ATOM 1056 CG TRP A 143 -20.015 7.697 33.327 1.00 30.63 C ANISOU 1056 CG TRP A 143 3630 4203 3804 263 -35 -158 C ATOM 1057 CD1 TRP A 143 -19.462 8.901 32.990 1.00 24.84 C ANISOU 1057 CD1 TRP A 143 2921 3419 3098 274 -46 -175 C ATOM 1058 CD2 TRP A 143 -18.943 6.747 33.312 1.00 26.98 C ANISOU 1058 CD2 TRP A 143 3183 3742 3327 232 -31 -141 C ATOM 1059 NE1 TRP A 143 -18.115 8.756 32.766 1.00 26.35 N ANISOU 1059 NE1 TRP A 143 3135 3588 3290 244 -44 -172 N ATOM 1060 CE2 TRP A 143 -17.771 7.444 32.957 1.00 23.76 C ANISOU 1060 CE2 TRP A 143 2798 3293 2939 223 -36 -154 C ATOM 1061 CE3 TRP A 143 -18.861 5.374 33.565 1.00 26.28 C ANISOU 1061 CE3 TRP A 143 3092 3683 3208 212 -26 -120 C ATOM 1062 CZ2 TRP A 143 -16.535 6.815 32.847 1.00 24.61 C ANISOU 1062 CZ2 TRP A 143 2915 3398 3040 199 -36 -153 C ATOM 1063 CZ3 TRP A 143 -17.632 4.752 33.453 1.00 27.35 C ANISOU 1063 CZ3 TRP A 143 3245 3807 3339 194 -31 -114 C ATOM 1064 CH2 TRP A 143 -16.486 5.473 33.099 1.00 30.52 C ANISOU 1064 CH2 TRP A 143 3657 4175 3763 190 -36 -134 C ATOM 1065 N ASN A 144 -23.103 10.444 32.273 1.00 31.90 N ANISOU 1065 N ASN A 144 3764 4325 4032 383 -87 -204 N ATOM 1066 CA ASN A 144 -23.513 11.075 31.029 1.00 35.78 C ANISOU 1066 CA ASN A 144 4282 4765 4548 403 -120 -185 C ATOM 1067 C ASN A 144 -23.221 12.569 31.106 1.00 32.86 C ANISOU 1067 C ASN A 144 3951 4330 4205 437 -144 -214 C ATOM 1068 O ASN A 144 -22.778 13.086 32.135 1.00 36.12 O ANISOU 1068 O ASN A 144 4362 4745 4619 445 -132 -251 O ATOM 1069 CB ASN A 144 -24.994 10.808 30.748 1.00 31.87 C ANISOU 1069 CB ASN A 144 3741 4315 4052 435 -131 -190 C ATOM 1070 CG ASN A 144 -25.899 11.326 31.850 1.00 30.13 C ANISOU 1070 CG ASN A 144 3471 4142 3835 483 -129 -250 C ATOM 1071 OD1 ASN A 144 -26.014 12.533 32.054 1.00 35.14 O ANISOU 1071 OD1 ASN A 144 4118 4739 4496 532 -152 -286 O ATOM 1072 ND2 ASN A 144 -26.555 10.414 32.558 1.00 34.73 N ANISOU 1072 ND2 ASN A 144 3998 4809 4389 467 -100 -264 N ATOM 1073 N ASN A 145 -23.475 13.263 29.996 1.00 33.06 N ANISOU 1073 N ASN A 145 4017 4294 4249 454 -181 -196 N ATOM 1074 CA ASN A 145 -23.276 14.701 29.896 1.00 36.36 C ANISOU 1074 CA ASN A 145 4489 4636 4691 484 -213 -217 C ATOM 1075 C ASN A 145 -24.586 15.477 29.989 1.00 36.86 C ANISOU 1075 C ASN A 145 4532 4696 4776 564 -251 -252 C ATOM 1076 O ASN A 145 -24.649 16.628 29.545 1.00 38.79 O ANISOU 1076 O ASN A 145 4833 4863 5042 598 -293 -259 O ATOM 1077 CB ASN A 145 -22.564 15.050 28.587 1.00 28.52 C ANISOU 1077 CB ASN A 145 3573 3566 3699 444 -233 -173 C ATOM 1078 CG ASN A 145 -21.187 14.435 28.488 1.00 38.32 C ANISOU 1078 CG ASN A 145 4831 4810 4921 369 -198 -152 C ATOM 1079 OD1 ASN A 145 -20.459 14.343 29.478 1.00 42.77 O ANISOU 1079 OD1 ASN A 145 5375 5397 5477 354 -169 -179 O ATOM 1080 ND2 ASN A 145 -20.820 14.006 27.287 1.00 49.49 N ANISOU 1080 ND2 ASN A 145 6277 6203 6325 322 -200 -109 N ATOM 1081 N CYS A 146 -25.637 14.870 30.546 1.00 31.59 N ANISOU 1081 N CYS A 146 3788 4112 4104 594 -238 -278 N ATOM 1082 CA CYS A 146 -26.909 15.578 30.657 1.00 31.64 C ANISOU 1082 CA CYS A 146 3762 4128 4133 674 -275 -323 C ATOM 1083 C CYS A 146 -26.814 16.754 31.619 1.00 33.67 C ANISOU 1083 C CYS A 146 4028 4355 4409 721 -284 -383 C ATOM 1084 O CYS A 146 -27.573 17.720 31.488 1.00 41.40 O ANISOU 1084 O CYS A 146 5013 5301 5416 795 -330 -420 O ATOM 1085 CB CYS A 146 -28.014 14.620 31.102 1.00 41.02 C ANISOU 1085 CB CYS A 146 4858 5425 5304 682 -251 -346 C ATOM 1086 SG CYS A 146 -28.431 13.341 29.889 1.00 40.83 S ANISOU 1086 SG CYS A 146 4819 5434 5260 639 -250 -284 S ATOM 1087 N GLY A 147 -25.897 16.695 32.585 1.00 43.51 N ANISOU 1087 N GLY A 147 5276 5613 5642 683 -244 -397 N ATOM 1088 CA GLY A 147 -25.735 17.796 33.518 1.00 47.15 C ANISOU 1088 CA GLY A 147 5748 6046 6119 721 -250 -455 C ATOM 1089 C GLY A 147 -25.100 19.027 32.910 1.00 47.09 C ANISOU 1089 C GLY A 147 5836 5922 6134 731 -290 -446 C ATOM 1090 O GLY A 147 -25.279 20.128 33.441 1.00 58.13 O ANISOU 1090 O GLY A 147 7252 7281 7554 783 -313 -497 O ATOM 1091 N GLN A 148 -24.370 18.868 31.804 1.00 48.50 N ANISOU 1091 N GLN A 148 6079 6044 6306 679 -299 -384 N ATOM 1092 CA GLN A 148 -23.685 19.968 31.128 1.00 46.94 C ANISOU 1092 CA GLN A 148 5984 5734 6118 668 -334 -368 C ATOM 1093 C GLN A 148 -24.144 20.023 29.675 1.00 43.55 C ANISOU 1093 C GLN A 148 5602 5252 5692 676 -382 -319 C ATOM 1094 O GLN A 148 -23.367 19.742 28.752 1.00 42.40 O ANISOU 1094 O GLN A 148 5510 5072 5529 608 -376 -266 O ATOM 1095 CB GLN A 148 -22.167 19.810 31.213 1.00 52.02 C ANISOU 1095 CB GLN A 148 6666 6359 6740 581 -296 -346 C ATOM 1096 CG GLN A 148 -21.615 19.793 32.634 1.00 64.93 C ANISOU 1096 CG GLN A 148 8261 8042 8369 571 -254 -393 C ATOM 1097 CD GLN A 148 -21.650 18.414 33.265 1.00 77.24 C ANISOU 1097 CD GLN A 148 9737 9707 9906 548 -208 -388 C ATOM 1098 OE1 GLN A 148 -21.762 17.402 32.572 1.00 71.62 O ANISOU 1098 OE1 GLN A 148 9006 9026 9181 520 -201 -343 O ATOM 1099 NE2 GLN A 148 -21.550 18.367 34.589 1.00 82.07 N ANISOU 1099 NE2 GLN A 148 10303 10371 10509 555 -180 -433 N ATOM 1100 N PRO A 149 -25.401 20.387 29.435 1.00 48.05 N ANISOU 1100 N PRO A 149 6154 5820 6284 758 -430 -340 N ATOM 1101 CA PRO A 149 -25.911 20.425 28.062 1.00 46.32 C ANISOU 1101 CA PRO A 149 5979 5554 6066 770 -481 -294 C ATOM 1102 C PRO A 149 -25.403 21.630 27.287 1.00 45.61 C ANISOU 1102 C PRO A 149 6016 5334 5979 764 -533 -271 C ATOM 1103 O PRO A 149 -25.139 22.698 27.843 1.00 49.99 O ANISOU 1103 O PRO A 149 6620 5827 6549 791 -551 -308 O ATOM 1104 CB PRO A 149 -27.430 20.501 28.259 1.00 53.83 C ANISOU 1104 CB PRO A 149 6859 6554 7040 870 -518 -339 C ATOM 1105 CG PRO A 149 -27.593 21.212 29.568 1.00 40.80 C ANISOU 1105 CG PRO A 149 5177 4916 5409 923 -511 -415 C ATOM 1106 CD PRO A 149 -26.428 20.772 30.421 1.00 46.18 C ANISOU 1106 CD PRO A 149 5849 5628 6069 845 -441 -412 C ATOM 1107 N LYS A 150 -25.273 21.440 25.975 1.00 46.28 N ANISOU 1107 N LYS A 150 6161 5376 6047 724 -559 -210 N ATOM 1108 CA LYS A 150 -24.872 22.516 25.069 1.00 48.51 C ANISOU 1108 CA LYS A 150 6576 5531 6323 708 -613 -179 C ATOM 1109 C LYS A 150 -26.110 23.347 24.756 1.00 50.78 C ANISOU 1109 C LYS A 150 6889 5767 6638 818 -699 -200 C ATOM 1110 O LYS A 150 -26.864 23.056 23.825 1.00 54.34 O ANISOU 1110 O LYS A 150 7339 6220 7086 845 -742 -169 O ATOM 1111 CB LYS A 150 -24.239 21.954 23.802 1.00 45.35 C ANISOU 1111 CB LYS A 150 6228 5112 5889 615 -604 -108 C ATOM 1112 CG LYS A 150 -22.970 21.149 24.037 1.00 44.35 C ANISOU 1112 CG LYS A 150 6078 5036 5738 511 -524 -94 C ATOM 1113 CD LYS A 150 -22.147 21.041 22.762 1.00 44.34 C ANISOU 1113 CD LYS A 150 6159 4987 5702 414 -522 -36 C ATOM 1114 CE LYS A 150 -21.016 20.029 22.895 1.00 62.02 C ANISOU 1114 CE LYS A 150 8352 7293 7919 321 -446 -28 C ATOM 1115 NZ LYS A 150 -19.876 20.540 23.707 1.00 67.82 N ANISOU 1115 NZ LYS A 150 9107 8013 8649 276 -410 -62 N ATOM 1116 N GLU A 151 -26.319 24.404 25.547 1.00 61.78 N ANISOU 1116 N GLU A 151 8304 7113 8058 887 -729 -256 N ATOM 1117 CA GLU A 151 -27.541 25.189 25.417 1.00 60.92 C ANISOU 1117 CA GLU A 151 8204 6962 7979 1009 -814 -292 C ATOM 1118 C GLU A 151 -27.524 26.068 24.173 1.00 58.47 C ANISOU 1118 C GLU A 151 8040 6518 7659 1013 -898 -243 C ATOM 1119 O GLU A 151 -28.582 26.323 23.585 1.00 60.06 O ANISOU 1119 O GLU A 151 8247 6697 7876 1100 -975 -246 O ATOM 1120 CB GLU A 151 -27.745 26.043 26.664 1.00 59.89 C ANISOU 1120 CB GLU A 151 8053 6822 7881 1082 -819 -374 C ATOM 1121 CG GLU A 151 -28.040 25.238 27.920 1.00 65.05 C ANISOU 1121 CG GLU A 151 8560 7613 8543 1095 -748 -431 C ATOM 1122 CD GLU A 151 -29.445 24.668 27.933 1.00 80.63 C ANISOU 1122 CD GLU A 151 10421 9682 10534 1178 -767 -466 C ATOM 1123 OE1 GLU A 151 -30.142 24.774 26.902 1.00 77.37 O ANISOU 1123 OE1 GLU A 151 10036 9235 10126 1222 -834 -440 O ATOM 1124 OE2 GLU A 151 -29.855 24.118 28.978 1.00 82.46 O ANISOU 1124 OE2 GLU A 151 10536 10025 10770 1195 -717 -521 O ATOM 1125 N GLY A 152 -26.347 26.538 23.756 1.00 58.66 N ANISOU 1125 N GLY A 152 8182 6452 7653 917 -887 -200 N ATOM 1126 CA GLY A 152 -26.275 27.321 22.534 1.00 55.81 C ANISOU 1126 CA GLY A 152 7972 5963 7272 903 -964 -147 C ATOM 1127 C GLY A 152 -26.771 26.549 21.328 1.00 62.33 C ANISOU 1127 C GLY A 152 8788 6818 8078 888 -988 -89 C ATOM 1128 O GLY A 152 -27.532 27.075 20.511 1.00 68.00 O ANISOU 1128 O GLY A 152 9573 7466 8798 951 -1079 -70 O ATOM 1129 N LYS A 153 -26.353 25.288 21.204 1.00 56.02 N ANISOU 1129 N LYS A 153 7906 6120 7258 807 -910 -61 N ATOM 1130 CA LYS A 153 -26.816 24.461 20.096 1.00 55.29 C ANISOU 1130 CA LYS A 153 7796 6066 7147 788 -925 -10 C ATOM 1131 C LYS A 153 -28.294 24.119 20.233 1.00 59.22 C ANISOU 1131 C LYS A 153 8191 6634 7676 906 -966 -45 C ATOM 1132 O LYS A 153 -28.996 23.994 19.223 1.00 54.00 O ANISOU 1132 O LYS A 153 7551 5961 7007 933 -1025 -12 O ATOM 1133 CB LYS A 153 -25.977 23.186 20.017 1.00 52.88 C ANISOU 1133 CB LYS A 153 7426 5852 6814 676 -830 20 C ATOM 1134 CG LYS A 153 -26.326 22.280 18.850 1.00 54.13 C ANISOU 1134 CG LYS A 153 7570 6048 6948 641 -836 74 C ATOM 1135 CD LYS A 153 -25.528 20.987 18.879 1.00 55.95 C ANISOU 1135 CD LYS A 153 7730 6371 7158 542 -743 93 C ATOM 1136 CE LYS A 153 -24.028 21.244 18.915 1.00 66.02 C ANISOU 1136 CE LYS A 153 9074 7605 8407 433 -694 105 C ATOM 1137 NZ LYS A 153 -23.243 20.036 18.522 1.00 57.35 N ANISOU 1137 NZ LYS A 153 7931 6578 7282 334 -622 132 N ATOM 1138 N ALA A 154 -28.785 23.966 21.466 1.00 53.61 N ANISOU 1138 N ALA A 154 7367 6003 7000 974 -937 -115 N ATOM 1139 CA ALA A 154 -30.197 23.659 21.664 1.00 56.13 C ANISOU 1139 CA ALA A 154 7579 6401 7347 1082 -971 -161 C ATOM 1140 C ALA A 154 -31.073 24.862 21.332 1.00 58.52 C ANISOU 1140 C ALA A 154 7947 6611 7675 1201 -1084 -188 C ATOM 1141 O ALA A 154 -32.166 24.706 20.775 1.00 47.23 O ANISOU 1141 O ALA A 154 6479 5211 6256 1275 -1144 -195 O ATOM 1142 CB ALA A 154 -30.433 23.194 23.100 1.00 47.48 C ANISOU 1142 CB ALA A 154 6349 5417 6274 1110 -904 -233 C ATOM 1143 N HIS A 155 -30.610 26.071 21.663 1.00 58.24 N ANISOU 1143 N HIS A 155 8015 6463 7651 1223 -1119 -206 N ATOM 1144 CA HIS A 155 -31.362 27.269 21.303 1.00 62.09 C ANISOU 1144 CA HIS A 155 8586 6844 8161 1337 -1236 -229 C ATOM 1145 C HIS A 155 -31.382 27.474 19.793 1.00 57.24 C ANISOU 1145 C HIS A 155 8097 6137 7515 1311 -1312 -149 C ATOM 1146 O HIS A 155 -32.423 27.819 19.222 1.00 62.34 O ANISOU 1146 O HIS A 155 8754 6757 8176 1413 -1408 -159 O ATOM 1147 CB HIS A 155 -30.770 28.493 22.003 1.00 58.27 C ANISOU 1147 CB HIS A 155 8197 6252 7692 1354 -1253 -263 C ATOM 1148 CG HIS A 155 -31.276 28.696 23.398 1.00 67.60 C ANISOU 1148 CG HIS A 155 9268 7501 8917 1442 -1230 -363 C ATOM 1149 ND1 HIS A 155 -32.531 29.198 23.667 1.00 85.47 N ANISOU 1149 ND1 HIS A 155 11478 9774 11222 1592 -1306 -437 N ATOM 1150 CD2 HIS A 155 -30.695 28.471 24.600 1.00 60.76 C ANISOU 1150 CD2 HIS A 155 8332 6698 8056 1402 -1141 -404 C ATOM 1151 CE1 HIS A 155 -32.703 29.270 24.975 1.00 93.76 C ANISOU 1151 CE1 HIS A 155 12430 10893 12301 1635 -1260 -522 C ATOM 1152 NE2 HIS A 155 -31.604 28.835 25.564 1.00 91.19 N ANISOU 1152 NE2 HIS A 155 12096 10599 11952 1520 -1161 -501 N ATOM 1153 N SER A 156 -30.244 27.259 19.128 1.00 56.99 N ANISOU 1153 N SER A 156 8157 6061 7437 1174 -1270 -73 N ATOM 1154 CA SER A 156 -30.184 27.467 17.684 1.00 63.93 C ANISOU 1154 CA SER A 156 9164 6851 8276 1134 -1337 5 C ATOM 1155 C SER A 156 -31.146 26.549 16.941 1.00 61.13 C ANISOU 1155 C SER A 156 8725 6584 7919 1166 -1359 23 C ATOM 1156 O SER A 156 -31.590 26.882 15.837 1.00 68.28 O ANISOU 1156 O SER A 156 9718 7420 8805 1190 -1448 66 O ATOM 1157 CB SER A 156 -28.758 27.245 17.182 1.00 62.71 C ANISOU 1157 CB SER A 156 9097 6660 8069 967 -1270 71 C ATOM 1158 OG SER A 156 -28.373 25.892 17.342 1.00 75.29 O ANISOU 1158 OG SER A 156 10570 8386 9652 888 -1166 81 O ATOM 1159 N GLN A 157 -31.468 25.392 17.516 1.00 62.38 N ANISOU 1159 N GLN A 157 8717 6892 8091 1163 -1282 -8 N ATOM 1160 CA GLN A 157 -32.418 24.460 16.927 1.00 61.37 C ANISOU 1160 CA GLN A 157 8496 6862 7962 1192 -1294 0 C ATOM 1161 C GLN A 157 -33.809 24.586 17.533 1.00 55.84 C ANISOU 1161 C GLN A 157 7680 6229 7308 1340 -1343 -83 C ATOM 1162 O GLN A 157 -34.680 23.761 17.239 1.00 59.71 O ANISOU 1162 O GLN A 157 8066 6821 7799 1367 -1344 -92 O ATOM 1163 CB GLN A 157 -31.913 23.023 17.078 1.00 66.14 C ANISOU 1163 CB GLN A 157 8997 7588 8545 1085 -1179 22 C ATOM 1164 CG GLN A 157 -30.610 22.754 16.348 1.00 67.65 C ANISOU 1164 CG GLN A 157 9285 7731 8689 939 -1131 98 C ATOM 1165 CD GLN A 157 -30.246 21.284 16.318 1.00 77.88 C ANISOU 1165 CD GLN A 157 10482 9143 9965 848 -1034 118 C ATOM 1166 OE1 GLN A 157 -29.121 20.906 16.643 1.00 84.57 O ANISOU 1166 OE1 GLN A 157 11334 10002 10797 752 -955 132 O ATOM 1167 NE2 GLN A 157 -31.196 20.446 15.918 1.00 77.18 N ANISOU 1167 NE2 GLN A 157 10306 9141 9878 879 -1044 119 N ATOM 1168 N GLY A 158 -34.039 25.596 18.368 1.00 53.35 N ANISOU 1168 N GLY A 158 7377 5863 7029 1433 -1382 -148 N ATOM 1169 CA GLY A 158 -35.359 25.811 18.930 1.00 49.40 C ANISOU 1169 CA GLY A 158 6769 5428 6575 1579 -1433 -239 C ATOM 1170 C GLY A 158 -35.828 24.710 19.854 1.00 56.56 C ANISOU 1170 C GLY A 158 7488 6509 7495 1575 -1342 -297 C ATOM 1171 O GLY A 158 -37.037 24.490 19.978 1.00 69.13 O ANISOU 1171 O GLY A 158 8967 8189 9109 1668 -1375 -359 O ATOM 1172 N CYS A 159 -34.905 24.006 20.507 1.00 54.41 N ANISOU 1172 N CYS A 159 7180 6289 7205 1466 -1229 -281 N ATOM 1173 CA CYS A 159 -35.289 22.986 21.472 1.00 53.74 C ANISOU 1173 CA CYS A 159 6932 6361 7126 1454 -1142 -334 C ATOM 1174 C CYS A 159 -35.915 23.643 22.698 1.00 52.60 C ANISOU 1174 C CYS A 159 6713 6250 7023 1559 -1153 -440 C ATOM 1175 O CYS A 159 -35.650 24.806 23.009 1.00 61.22 O ANISOU 1175 O CYS A 159 7887 7237 8136 1612 -1199 -465 O ATOM 1176 CB CYS A 159 -34.079 22.144 21.888 1.00 42.98 C ANISOU 1176 CB CYS A 159 5565 5032 5734 1317 -1030 -290 C ATOM 1177 SG CYS A 159 -33.156 21.378 20.529 1.00 57.94 S ANISOU 1177 SG CYS A 159 7546 6889 7579 1184 -1006 -174 S ATOM 1178 N GLY A 160 -36.765 22.887 23.391 1.00 52.93 N ANISOU 1178 N GLY A 160 6599 6439 7072 1585 -1109 -506 N ATOM 1179 CA GLY A 160 -37.443 23.391 24.565 1.00 49.80 C ANISOU 1179 CA GLY A 160 6113 6097 6711 1679 -1110 -616 C ATOM 1180 C GLY A 160 -36.600 23.262 25.820 1.00 61.00 C ANISOU 1180 C GLY A 160 7511 7543 8124 1614 -1016 -637 C ATOM 1181 O GLY A 160 -35.464 22.791 25.803 1.00 63.48 O ANISOU 1181 O GLY A 160 7879 7833 8409 1500 -953 -568 O ATOM 1182 N GLU A 161 -37.182 23.694 26.937 1.00 79.05 N ANISOU 1182 N GLU A 161 9713 9885 10437 1690 -1010 -740 N ATOM 1183 CA GLU A 161 -36.509 23.571 28.222 1.00 86.08 C ANISOU 1183 CA GLU A 161 10572 10815 11321 1635 -923 -771 C ATOM 1184 C GLU A 161 -36.387 22.102 28.604 1.00 70.86 C ANISOU 1184 C GLU A 161 8550 9020 9353 1529 -822 -748 C ATOM 1185 O GLU A 161 -37.329 21.320 28.443 1.00 71.59 O ANISOU 1185 O GLU A 161 8541 9223 9436 1537 -813 -772 O ATOM 1186 CB GLU A 161 -37.266 24.338 29.307 1.00 97.93 C ANISOU 1186 CB GLU A 161 11997 12356 12857 1742 -941 -894 C ATOM 1187 CG GLU A 161 -37.380 25.827 29.047 1.00112.22 C ANISOU 1187 CG GLU A 161 13904 14026 14707 1855 -1044 -925 C ATOM 1188 CD GLU A 161 -36.037 26.483 28.787 1.00119.26 C ANISOU 1188 CD GLU A 161 14959 14765 15590 1794 -1050 -850 C ATOM 1189 OE1 GLU A 161 -35.299 26.746 29.761 1.00124.51 O ANISOU 1189 OE1 GLU A 161 15636 15420 16254 1755 -995 -872 O ATOM 1190 OE2 GLU A 161 -35.716 26.726 27.605 1.00114.21 O ANISOU 1190 OE2 GLU A 161 14435 14019 14942 1779 -1108 -769 O ATOM 1191 N GLY A 162 -35.215 21.725 29.110 1.00 65.58 N ANISOU 1191 N GLY A 162 7918 8338 8660 1428 -749 -704 N ATOM 1192 CA GLY A 162 -34.934 20.341 29.416 1.00 61.61 C ANISOU 1192 CA GLY A 162 7353 7939 8118 1323 -660 -671 C ATOM 1193 C GLY A 162 -34.605 19.486 28.215 1.00 62.24 C ANISOU 1193 C GLY A 162 7474 8003 8171 1250 -658 -575 C ATOM 1194 O GLY A 162 -34.416 18.272 28.374 1.00 66.20 O ANISOU 1194 O GLY A 162 7927 8586 8640 1166 -590 -546 O ATOM 1195 N GLN A 163 -34.524 20.074 27.023 1.00 58.42 N ANISOU 1195 N GLN A 163 7083 7415 7699 1278 -731 -527 N ATOM 1196 CA GLN A 163 -34.238 19.347 25.797 1.00 53.63 C ANISOU 1196 CA GLN A 163 6521 6790 7067 1211 -734 -439 C ATOM 1197 C GLN A 163 -32.876 19.752 25.246 1.00 49.12 C ANISOU 1197 C GLN A 163 6084 6096 6484 1144 -736 -365 C ATOM 1198 O GLN A 163 -32.387 20.857 25.497 1.00 53.42 O ANISOU 1198 O GLN A 163 6705 6545 7045 1173 -766 -379 O ATOM 1199 CB GLN A 163 -35.320 19.596 24.739 1.00 53.30 C ANISOU 1199 CB GLN A 163 6476 6738 7038 1287 -819 -441 C ATOM 1200 CG GLN A 163 -36.603 18.835 24.977 1.00 47.55 C ANISOU 1200 CG GLN A 163 5608 6152 6308 1321 -807 -498 C ATOM 1201 CD GLN A 163 -37.458 18.763 23.736 1.00 49.61 C ANISOU 1201 CD GLN A 163 5869 6411 6570 1364 -879 -478 C ATOM 1202 OE1 GLN A 163 -37.454 19.676 22.911 1.00 53.48 O ANISOU 1202 OE1 GLN A 163 6453 6792 7075 1420 -965 -454 O ATOM 1203 NE2 GLN A 163 -38.188 17.667 23.586 1.00 53.58 N ANISOU 1203 NE2 GLN A 163 6272 7034 7051 1334 -846 -486 N ATOM 1204 N VAL A 164 -32.264 18.836 24.491 1.00 46.17 N ANISOU 1204 N VAL A 164 5736 5728 6079 1049 -701 -290 N ATOM 1205 CA VAL A 164 -30.977 19.066 23.849 1.00 46.29 C ANISOU 1205 CA VAL A 164 5868 5644 6078 971 -696 -221 C ATOM 1206 C VAL A 164 -31.036 18.518 22.429 1.00 38.18 C ANISOU 1206 C VAL A 164 4879 4601 5027 928 -720 -152 C ATOM 1207 O VAL A 164 -31.892 17.699 22.089 1.00 36.47 O ANISOU 1207 O VAL A 164 4588 4465 4804 938 -719 -152 O ATOM 1208 CB VAL A 164 -29.805 18.416 24.624 1.00 45.44 C ANISOU 1208 CB VAL A 164 5746 5568 5949 880 -608 -210 C ATOM 1209 CG1 VAL A 164 -29.637 19.076 25.978 1.00 49.71 C ANISOU 1209 CG1 VAL A 164 6266 6113 6510 917 -589 -275 C ATOM 1210 CG2 VAL A 164 -30.029 16.921 24.788 1.00 44.36 C ANISOU 1210 CG2 VAL A 164 5518 5547 5791 829 -547 -198 C ATOM 1211 N ALA A 165 -30.122 19.001 21.591 1.00 38.27 N ANISOU 1211 N ALA A 165 5008 4509 5022 874 -740 -95 N ATOM 1212 CA ALA A 165 -29.932 18.415 20.271 1.00 41.24 C ANISOU 1212 CA ALA A 165 5429 4871 5370 810 -748 -26 C ATOM 1213 C ALA A 165 -29.327 17.028 20.439 1.00 34.90 C ANISOU 1213 C ALA A 165 4564 4152 4543 718 -660 -3 C ATOM 1214 O ALA A 165 -28.223 16.884 20.973 1.00 42.48 O ANISOU 1214 O ALA A 165 5539 5106 5495 655 -605 0 O ATOM 1215 CB ALA A 165 -29.033 19.302 19.415 1.00 44.15 C ANISOU 1215 CB ALA A 165 5943 5112 5721 763 -784 23 C ATOM 1216 N CYS A 166 -30.054 16.007 19.998 1.00 36.86 N ANISOU 1216 N CYS A 166 4745 4480 4781 712 -651 10 N ATOM 1217 CA CYS A 166 -29.696 14.623 20.295 1.00 40.30 C ANISOU 1217 CA CYS A 166 5112 5002 5197 640 -573 21 C ATOM 1218 C CYS A 166 -28.585 14.164 19.360 1.00 46.43 C ANISOU 1218 C CYS A 166 5957 5740 5946 541 -548 83 C ATOM 1219 O CYS A 166 -28.828 13.834 18.196 1.00 41.03 O ANISOU 1219 O CYS A 166 5298 5047 5243 515 -571 125 O ATOM 1220 CB CYS A 166 -30.913 13.717 20.174 1.00 39.77 C ANISOU 1220 CB CYS A 166 4951 5034 5127 665 -573 8 C ATOM 1221 SG CYS A 166 -30.531 12.001 20.548 1.00 44.76 S ANISOU 1221 SG CYS A 166 5513 5762 5730 577 -483 23 S ATOM 1222 N LEU A 167 -27.360 14.123 19.883 1.00 45.45 N ANISOU 1222 N LEU A 167 5856 5597 5815 484 -498 84 N ATOM 1223 CA LEU A 167 -26.198 13.631 19.159 1.00 41.30 C ANISOU 1223 CA LEU A 167 5381 5049 5264 387 -464 127 C ATOM 1224 C LEU A 167 -25.419 12.692 20.067 1.00 38.78 C ANISOU 1224 C LEU A 167 5005 4791 4940 343 -391 111 C ATOM 1225 O LEU A 167 -25.359 12.894 21.283 1.00 39.16 O ANISOU 1225 O LEU A 167 5016 4861 5003 375 -372 70 O ATOM 1226 CB LEU A 167 -25.304 14.786 18.687 1.00 42.62 C ANISOU 1226 CB LEU A 167 5657 5112 5423 356 -489 143 C ATOM 1227 CG LEU A 167 -25.951 15.738 17.679 1.00 43.18 C ANISOU 1227 CG LEU A 167 5810 5106 5492 391 -569 168 C ATOM 1228 CD1 LEU A 167 -25.166 17.035 17.586 1.00 45.53 C ANISOU 1228 CD1 LEU A 167 6218 5297 5784 371 -596 171 C ATOM 1229 CD2 LEU A 167 -26.057 15.077 16.311 1.00 44.03 C ANISOU 1229 CD2 LEU A 167 5940 5220 5570 337 -578 220 C ATOM 1230 N PHE A 168 -24.822 11.658 19.467 1.00 34.81 N ANISOU 1230 N PHE A 168 4498 4313 4414 272 -355 142 N ATOM 1231 CA PHE A 168 -24.168 10.622 20.263 1.00 34.39 C ANISOU 1231 CA PHE A 168 4392 4319 4356 237 -295 128 C ATOM 1232 C PHE A 168 -23.073 11.210 21.146 1.00 34.32 C ANISOU 1232 C PHE A 168 4403 4282 4353 225 -272 100 C ATOM 1233 O PHE A 168 -23.037 10.962 22.356 1.00 31.88 O ANISOU 1233 O PHE A 168 4045 4016 4053 248 -246 67 O ATOM 1234 CB PHE A 168 -23.592 9.539 19.349 1.00 38.15 C ANISOU 1234 CB PHE A 168 4873 4813 4809 165 -267 162 C ATOM 1235 CG PHE A 168 -23.043 8.351 20.092 1.00 33.33 C ANISOU 1235 CG PHE A 168 4212 4261 4193 138 -215 149 C ATOM 1236 CD1 PHE A 168 -21.759 8.373 20.611 1.00 29.08 C ANISOU 1236 CD1 PHE A 168 3685 3712 3654 106 -185 131 C ATOM 1237 CD2 PHE A 168 -23.813 7.213 20.270 1.00 33.93 C ANISOU 1237 CD2 PHE A 168 4231 4401 4261 145 -201 153 C ATOM 1238 CE1 PHE A 168 -21.254 7.284 21.297 1.00 30.75 C ANISOU 1238 CE1 PHE A 168 3853 3970 3858 89 -148 119 C ATOM 1239 CE2 PHE A 168 -23.312 6.120 20.953 1.00 35.10 C ANISOU 1239 CE2 PHE A 168 4345 4592 4399 121 -160 145 C ATOM 1240 CZ PHE A 168 -22.030 6.156 21.467 1.00 32.31 C ANISOU 1240 CZ PHE A 168 4006 4223 4048 98 -137 128 C ATOM 1241 N GLU A 169 -22.169 11.994 20.556 1.00 32.12 N ANISOU 1241 N GLU A 169 4199 3937 4069 183 -281 111 N ATOM 1242 CA GLU A 169 -21.017 12.502 21.291 1.00 36.36 C ANISOU 1242 CA GLU A 169 4755 4453 4608 158 -256 82 C ATOM 1243 C GLU A 169 -21.354 13.673 22.207 1.00 37.57 C ANISOU 1243 C GLU A 169 4921 4572 4782 219 -281 48 C ATOM 1244 O GLU A 169 -20.494 14.082 22.995 1.00 40.94 O ANISOU 1244 O GLU A 169 5354 4989 5211 205 -258 19 O ATOM 1245 CB GLU A 169 -19.911 12.914 20.315 1.00 33.85 C ANISOU 1245 CB GLU A 169 4511 4081 4269 79 -252 100 C ATOM 1246 CG GLU A 169 -19.269 11.732 19.588 1.00 39.80 C ANISOU 1246 CG GLU A 169 5245 4875 5003 12 -216 118 C ATOM 1247 CD GLU A 169 -18.007 12.107 18.825 1.00 41.69 C ANISOU 1247 CD GLU A 169 5542 5078 5219 -75 -199 120 C ATOM 1248 OE1 GLU A 169 -17.279 13.017 19.277 1.00 43.53 O ANISOU 1248 OE1 GLU A 169 5812 5276 5453 -92 -195 94 O ATOM 1249 OE2 GLU A 169 -17.745 11.487 17.774 1.00 36.00 O ANISOU 1249 OE2 GLU A 169 4832 4369 4478 -130 -188 142 O ATOM 1250 N ASP A 170 -22.570 14.219 22.132 1.00 37.09 N ANISOU 1250 N ASP A 170 4861 4496 4737 288 -327 46 N ATOM 1251 CA ASP A 170 -22.961 15.278 23.054 1.00 39.58 C ANISOU 1251 CA ASP A 170 5179 4784 5074 355 -351 5 C ATOM 1252 C ASP A 170 -23.489 14.719 24.372 1.00 38.22 C ANISOU 1252 C ASP A 170 4914 4693 4913 400 -322 -36 C ATOM 1253 O ASP A 170 -23.326 15.358 25.417 1.00 43.53 O ANISOU 1253 O ASP A 170 5580 5361 5599 430 -316 -78 O ATOM 1254 CB ASP A 170 -24.017 16.185 22.409 1.00 39.93 C ANISOU 1254 CB ASP A 170 5266 4773 5131 418 -420 11 C ATOM 1255 CG ASP A 170 -23.423 17.167 21.398 1.00 48.60 C ANISOU 1255 CG ASP A 170 6483 5767 6217 379 -457 42 C ATOM 1256 OD1 ASP A 170 -22.199 17.117 21.144 1.00 48.47 O ANISOU 1256 OD1 ASP A 170 6508 5730 6180 294 -423 56 O ATOM 1257 OD2 ASP A 170 -24.187 17.997 20.859 1.00 42.53 O ANISOU 1257 OD2 ASP A 170 5766 4938 5456 431 -523 50 O ATOM 1258 N VAL A 171 -24.109 13.543 24.354 1.00 33.63 N ANISOU 1258 N VAL A 171 4266 4188 4324 400 -303 -26 N ATOM 1259 CA VAL A 171 -24.707 12.965 25.550 1.00 33.20 C ANISOU 1259 CA VAL A 171 4128 4214 4271 433 -276 -63 C ATOM 1260 C VAL A 171 -23.838 11.863 26.146 1.00 32.93 C ANISOU 1260 C VAL A 171 4065 4229 4217 377 -221 -58 C ATOM 1261 O VAL A 171 -23.726 11.758 27.368 1.00 31.46 O ANISOU 1261 O VAL A 171 3842 4081 4029 389 -196 -92 O ATOM 1262 CB VAL A 171 -26.131 12.451 25.241 1.00 35.41 C ANISOU 1262 CB VAL A 171 4353 4549 4551 472 -294 -63 C ATOM 1263 CG1 VAL A 171 -27.014 13.594 24.749 1.00 38.98 C ANISOU 1263 CG1 VAL A 171 4831 4954 5026 542 -357 -77 C ATOM 1264 CG2 VAL A 171 -26.097 11.329 24.218 1.00 34.66 C ANISOU 1264 CG2 VAL A 171 4258 4477 4436 418 -282 -14 C ATOM 1265 N VAL A 172 -23.222 11.031 25.315 1.00 31.29 N ANISOU 1265 N VAL A 172 3874 4021 3993 318 -206 -18 N ATOM 1266 CA VAL A 172 -22.384 9.947 25.821 1.00 36.18 C ANISOU 1266 CA VAL A 172 4470 4681 4595 273 -163 -15 C ATOM 1267 C VAL A 172 -20.980 10.483 26.084 1.00 31.54 C ANISOU 1267 C VAL A 172 3920 4054 4009 242 -150 -29 C ATOM 1268 O VAL A 172 -20.388 11.110 25.190 1.00 39.08 O ANISOU 1268 O VAL A 172 4931 4953 4966 212 -163 -15 O ATOM 1269 CB VAL A 172 -22.350 8.789 24.824 1.00 34.02 C ANISOU 1269 CB VAL A 172 4195 4427 4306 229 -153 25 C ATOM 1270 CG1 VAL A 172 -21.608 7.593 25.412 1.00 29.57 C ANISOU 1270 CG1 VAL A 172 3606 3905 3724 195 -117 24 C ATOM 1271 CG2 VAL A 172 -23.759 8.384 24.422 1.00 35.27 C ANISOU 1271 CG2 VAL A 172 4319 4620 4460 256 -169 37 C ATOM 1272 N PRO A 173 -20.406 10.272 27.268 1.00 34.67 N ANISOU 1272 N PRO A 173 4292 4482 4401 242 -125 -58 N ATOM 1273 CA PRO A 173 -19.044 10.756 27.521 1.00 34.51 C ANISOU 1273 CA PRO A 173 4300 4432 4381 210 -113 -77 C ATOM 1274 C PRO A 173 -17.985 9.868 26.885 1.00 31.40 C ANISOU 1274 C PRO A 173 3911 4046 3973 153 -94 -60 C ATOM 1275 O PRO A 173 -18.120 8.645 26.820 1.00 35.61 O ANISOU 1275 O PRO A 173 4415 4621 4495 145 -82 -43 O ATOM 1276 CB PRO A 173 -18.923 10.720 29.052 1.00 29.74 C ANISOU 1276 CB PRO A 173 3659 3867 3773 235 -97 -114 C ATOM 1277 CG PRO A 173 -20.294 10.410 29.576 1.00 31.02 C ANISOU 1277 CG PRO A 173 3779 4074 3935 279 -101 -119 C ATOM 1278 CD PRO A 173 -21.005 9.684 28.477 1.00 32.97 C ANISOU 1278 CD PRO A 173 4021 4329 4176 270 -109 -79 C ATOM 1279 N MET A 174 -16.901 10.507 26.432 1.00 30.24 N ANISOU 1279 N MET A 174 3804 3861 3826 112 -90 -69 N ATOM 1280 CA MET A 174 -15.845 9.773 25.740 1.00 30.73 C ANISOU 1280 CA MET A 174 3866 3933 3876 56 -72 -64 C ATOM 1281 C MET A 174 -14.986 8.949 26.688 1.00 29.61 C ANISOU 1281 C MET A 174 3683 3839 3728 55 -51 -92 C ATOM 1282 O MET A 174 -14.389 7.956 26.260 1.00 31.22 O ANISOU 1282 O MET A 174 3871 4067 3923 29 -40 -88 O ATOM 1283 CB MET A 174 -14.949 10.731 24.958 1.00 28.96 C ANISOU 1283 CB MET A 174 3696 3660 3648 2 -71 -72 C ATOM 1284 CG MET A 174 -15.426 11.006 23.552 1.00 40.37 C ANISOU 1284 CG MET A 174 5188 5064 5087 -25 -89 -34 C ATOM 1285 SD MET A 174 -15.489 9.521 22.527 1.00 46.54 S ANISOU 1285 SD MET A 174 5943 5884 5856 -54 -76 -4 S ATOM 1286 CE MET A 174 -16.135 10.209 21.005 1.00 48.35 C ANISOU 1286 CE MET A 174 6240 6056 6076 -83 -105 39 C ATOM 1287 N ASN A 175 -14.879 9.345 27.959 1.00 29.43 N ANISOU 1287 N ASN A 175 3644 3829 3708 85 -50 -122 N ATOM 1288 CA ASN A 175 -14.127 8.521 28.901 1.00 32.71 C ANISOU 1288 CA ASN A 175 4025 4291 4114 89 -38 -146 C ATOM 1289 C ASN A 175 -14.870 7.226 29.210 1.00 25.50 C ANISOU 1289 C ASN A 175 3084 3416 3189 113 -39 -121 C ATOM 1290 O ASN A 175 -14.235 6.201 29.473 1.00 29.24 O ANISOU 1290 O ASN A 175 3541 3918 3651 107 -36 -126 O ATOM 1291 CB ASN A 175 -13.819 9.300 30.186 1.00 33.93 C ANISOU 1291 CB ASN A 175 4173 4450 4269 110 -36 -185 C ATOM 1292 CG ASN A 175 -15.065 9.803 30.895 1.00 34.82 C ANISOU 1292 CG ASN A 175 4280 4562 4386 156 -45 -183 C ATOM 1293 OD1 ASN A 175 -16.179 9.353 30.626 1.00 41.54 O ANISOU 1293 OD1 ASN A 175 5122 5425 5237 176 -51 -155 O ATOM 1294 ND2 ASN A 175 -14.875 10.739 31.819 1.00 27.61 N ANISOU 1294 ND2 ASN A 175 3370 3642 3478 172 -44 -218 N ATOM 1295 N TYR A 176 -16.205 7.245 29.163 1.00 23.76 N ANISOU 1295 N TYR A 176 2861 3198 2970 138 -46 -97 N ATOM 1296 CA TYR A 176 -16.954 5.997 29.248 1.00 27.03 C ANISOU 1296 CA TYR A 176 3254 3647 3367 145 -44 -71 C ATOM 1297 C TYR A 176 -16.739 5.149 28.002 1.00 26.97 C ANISOU 1297 C TYR A 176 3257 3633 3358 113 -43 -43 C ATOM 1298 O TYR A 176 -16.613 3.921 28.090 1.00 26.16 O ANISOU 1298 O TYR A 176 3145 3554 3241 106 -40 -32 O ATOM 1299 CB TYR A 176 -18.447 6.276 29.441 1.00 29.30 C ANISOU 1299 CB TYR A 176 3528 3948 3655 174 -49 -62 C ATOM 1300 CG TYR A 176 -19.317 5.078 29.111 1.00 26.64 C ANISOU 1300 CG TYR A 176 3178 3644 3302 167 -46 -31 C ATOM 1301 CD1 TYR A 176 -19.642 4.142 30.083 1.00 24.94 C ANISOU 1301 CD1 TYR A 176 2945 3472 3060 168 -37 -31 C ATOM 1302 CD2 TYR A 176 -19.798 4.875 27.822 1.00 27.38 C ANISOU 1302 CD2 TYR A 176 3280 3722 3400 152 -53 0 C ATOM 1303 CE1 TYR A 176 -20.425 3.042 29.784 1.00 28.00 C ANISOU 1303 CE1 TYR A 176 3325 3886 3427 151 -32 -4 C ATOM 1304 CE2 TYR A 176 -20.580 3.777 27.513 1.00 29.15 C ANISOU 1304 CE2 TYR A 176 3492 3977 3607 140 -49 25 C ATOM 1305 CZ TYR A 176 -20.891 2.864 28.498 1.00 32.62 C ANISOU 1305 CZ TYR A 176 3915 4458 4021 138 -37 23 C ATOM 1306 OH TYR A 176 -21.669 1.768 28.197 1.00 32.45 O ANISOU 1306 OH TYR A 176 3887 4465 3977 117 -31 48 O ATOM 1307 N MET A 177 -16.702 5.787 26.830 1.00 27.15 N ANISOU 1307 N MET A 177 3303 3621 3393 92 -48 -32 N ATOM 1308 CA MET A 177 -16.596 5.038 25.583 1.00 28.25 C ANISOU 1308 CA MET A 177 3451 3755 3528 58 -45 -6 C ATOM 1309 C MET A 177 -15.228 4.383 25.437 1.00 24.35 C ANISOU 1309 C MET A 177 2953 3270 3030 30 -34 -27 C ATOM 1310 O MET A 177 -15.124 3.262 24.927 1.00 23.67 O ANISOU 1310 O MET A 177 2860 3198 2936 16 -31 -15 O ATOM 1311 CB MET A 177 -16.876 5.962 24.399 1.00 27.10 C ANISOU 1311 CB MET A 177 3339 3568 3390 38 -56 11 C ATOM 1312 CG MET A 177 -18.333 6.392 24.283 1.00 32.90 C ANISOU 1312 CG MET A 177 4074 4296 4128 72 -75 33 C ATOM 1313 SD MET A 177 -19.466 5.008 24.031 1.00 27.70 S ANISOU 1313 SD MET A 177 3386 3683 3457 78 -72 64 S ATOM 1314 CE MET A 177 -18.835 4.307 22.512 1.00 28.51 C ANISOU 1314 CE MET A 177 3510 3771 3551 22 -66 88 C ATOM 1315 N VAL A 178 -14.168 5.061 25.874 1.00 24.28 N ANISOU 1315 N VAL A 178 2944 3255 3026 22 -30 -65 N ATOM 1316 CA VAL A 178 -12.810 4.558 25.692 1.00 28.72 C ANISOU 1316 CA VAL A 178 3494 3832 3587 -3 -21 -97 C ATOM 1317 C VAL A 178 -12.431 3.620 26.832 1.00 26.31 C ANISOU 1317 C VAL A 178 3163 3560 3275 31 -28 -115 C ATOM 1318 O VAL A 178 -12.032 2.474 26.599 1.00 29.16 O ANISOU 1318 O VAL A 178 3513 3936 3630 31 -31 -117 O ATOM 1319 CB VAL A 178 -11.806 5.720 25.583 1.00 27.73 C ANISOU 1319 CB VAL A 178 3379 3691 3466 -36 -12 -134 C ATOM 1320 CG1 VAL A 178 -10.381 5.197 25.495 1.00 28.45 C ANISOU 1320 CG1 VAL A 178 3444 3812 3555 -59 -2 -180 C ATOM 1321 CG2 VAL A 178 -12.134 6.580 24.381 1.00 24.07 C ANISOU 1321 CG2 VAL A 178 2956 3188 3002 -77 -10 -112 C ATOM 1322 N TYR A 179 -12.546 4.100 28.071 1.00 27.88 N ANISOU 1322 N TYR A 179 3355 3766 3471 60 -33 -129 N ATOM 1323 CA TYR A 179 -12.081 3.324 29.218 1.00 28.28 C ANISOU 1323 CA TYR A 179 3389 3845 3510 89 -44 -147 C ATOM 1324 C TYR A 179 -13.057 2.212 29.585 1.00 27.32 C ANISOU 1324 C TYR A 179 3273 3736 3370 109 -52 -110 C ATOM 1325 O TYR A 179 -12.652 1.059 29.772 1.00 28.72 O ANISOU 1325 O TYR A 179 3452 3925 3537 118 -65 -110 O ATOM 1326 CB TYR A 179 -11.861 4.245 30.420 1.00 26.63 C ANISOU 1326 CB TYR A 179 3175 3644 3300 107 -45 -176 C ATOM 1327 CG TYR A 179 -10.655 5.158 30.309 1.00 32.39 C ANISOU 1327 CG TYR A 179 3897 4369 4040 84 -37 -222 C ATOM 1328 CD1 TYR A 179 -9.462 4.711 29.752 1.00 33.74 C ANISOU 1328 CD1 TYR A 179 4051 4554 4213 63 -37 -253 C ATOM 1329 CD2 TYR A 179 -10.709 6.468 30.767 1.00 39.60 C ANISOU 1329 CD2 TYR A 179 4820 5267 4959 81 -31 -240 C ATOM 1330 CE1 TYR A 179 -8.360 5.541 29.654 1.00 35.39 C ANISOU 1330 CE1 TYR A 179 4251 4769 4428 32 -26 -302 C ATOM 1331 CE2 TYR A 179 -9.611 7.307 30.672 1.00 39.96 C ANISOU 1331 CE2 TYR A 179 4864 5310 5010 51 -22 -284 C ATOM 1332 CZ TYR A 179 -8.441 6.838 30.115 1.00 40.02 C ANISOU 1332 CZ TYR A 179 4852 5338 5017 23 -18 -315 C ATOM 1333 OH TYR A 179 -7.347 7.666 30.020 1.00 40.49 O ANISOU 1333 OH TYR A 179 4905 5402 5076 -17 -5 -364 O ATOM 1334 N PHE A 180 -14.344 2.536 29.702 1.00 29.85 N ANISOU 1334 N PHE A 180 3600 4055 3688 116 -47 -82 N ATOM 1335 CA PHE A 180 -15.306 1.560 30.202 1.00 29.57 C ANISOU 1335 CA PHE A 180 3568 4040 3628 125 -51 -54 C ATOM 1336 C PHE A 180 -15.781 0.632 29.091 1.00 26.85 C ANISOU 1336 C PHE A 180 3233 3689 3281 105 -49 -20 C ATOM 1337 O PHE A 180 -15.692 -0.594 29.217 1.00 31.41 O ANISOU 1337 O PHE A 180 3822 4272 3840 103 -58 -8 O ATOM 1338 CB PHE A 180 -16.494 2.280 30.850 1.00 32.68 C ANISOU 1338 CB PHE A 180 3953 4447 4017 139 -43 -49 C ATOM 1339 CG PHE A 180 -17.403 1.375 31.646 1.00 30.29 C ANISOU 1339 CG PHE A 180 3652 4176 3681 140 -42 -31 C ATOM 1340 CD1 PHE A 180 -18.419 0.667 31.025 1.00 33.25 C ANISOU 1340 CD1 PHE A 180 4029 4561 4045 123 -37 1 C ATOM 1341 CD2 PHE A 180 -17.248 1.247 33.018 1.00 35.49 C ANISOU 1341 CD2 PHE A 180 4312 4857 4315 151 -45 -48 C ATOM 1342 CE1 PHE A 180 -19.257 -0.164 31.756 1.00 37.51 C ANISOU 1342 CE1 PHE A 180 4573 5133 4548 112 -32 15 C ATOM 1343 CE2 PHE A 180 -18.085 0.420 33.754 1.00 32.51 C ANISOU 1343 CE2 PHE A 180 3943 4510 3899 140 -42 -31 C ATOM 1344 CZ PHE A 180 -19.088 -0.287 33.121 1.00 28.60 C ANISOU 1344 CZ PHE A 180 3450 4025 3391 118 -34 -1 C ATOM 1345 N ASN A 181 -16.274 1.195 27.989 1.00 26.60 N ANISOU 1345 N ASN A 181 3201 3642 3265 89 -42 -5 N ATOM 1346 CA ASN A 181 -16.858 0.360 26.946 1.00 31.75 C ANISOU 1346 CA ASN A 181 3860 4291 3911 68 -40 27 C ATOM 1347 C ASN A 181 -15.782 -0.351 26.128 1.00 32.98 C ANISOU 1347 C ASN A 181 4023 4435 4073 48 -41 18 C ATOM 1348 O ASN A 181 -15.818 -1.578 25.981 1.00 32.85 O ANISOU 1348 O ASN A 181 4015 4423 4043 43 -46 31 O ATOM 1349 CB ASN A 181 -17.759 1.204 26.042 1.00 29.48 C ANISOU 1349 CB ASN A 181 3573 3992 3636 60 -37 45 C ATOM 1350 CG ASN A 181 -18.674 0.358 25.177 1.00 31.08 C ANISOU 1350 CG ASN A 181 3778 4204 3828 41 -36 80 C ATOM 1351 OD1 ASN A 181 -19.780 0.001 25.585 1.00 36.54 O ANISOU 1351 OD1 ASN A 181 4459 4922 4504 47 -34 94 O ATOM 1352 ND2 ASN A 181 -18.215 0.031 23.975 1.00 35.82 N ANISOU 1352 ND2 ASN A 181 4389 4787 4433 12 -34 89 N ATOM 1353 N PHE A 182 -14.809 0.394 25.600 1.00 24.92 N ANISOU 1353 N PHE A 182 2998 3400 3069 34 -37 -8 N ATOM 1354 CA PHE A 182 -13.854 -0.196 24.664 1.00 31.25 C ANISOU 1354 CA PHE A 182 3798 4198 3876 10 -34 -25 C ATOM 1355 C PHE A 182 -12.799 -1.036 25.382 1.00 30.02 C ANISOU 1355 C PHE A 182 3633 4057 3718 33 -47 -59 C ATOM 1356 O PHE A 182 -12.665 -2.235 25.122 1.00 28.37 O ANISOU 1356 O PHE A 182 3429 3849 3502 36 -55 -55 O ATOM 1357 CB PHE A 182 -13.191 0.904 23.827 1.00 29.41 C ANISOU 1357 CB PHE A 182 3567 3951 3656 -24 -22 -46 C ATOM 1358 CG PHE A 182 -12.207 0.387 22.815 1.00 29.73 C ANISOU 1358 CG PHE A 182 3600 3997 3698 -58 -13 -71 C ATOM 1359 CD1 PHE A 182 -12.495 -0.738 22.058 1.00 33.84 C ANISOU 1359 CD1 PHE A 182 4124 4521 4214 -67 -13 -53 C ATOM 1360 CD2 PHE A 182 -10.999 1.032 22.611 1.00 32.81 C ANISOU 1360 CD2 PHE A 182 3978 4393 4094 -84 -3 -118 C ATOM 1361 CE1 PHE A 182 -11.595 -1.212 21.122 1.00 31.06 C ANISOU 1361 CE1 PHE A 182 3760 4177 3863 -98 -4 -83 C ATOM 1362 CE2 PHE A 182 -10.095 0.563 21.674 1.00 34.84 C ANISOU 1362 CE2 PHE A 182 4221 4665 4351 -119 9 -151 C ATOM 1363 CZ PHE A 182 -10.395 -0.562 20.929 1.00 34.01 C ANISOU 1363 CZ PHE A 182 4116 4563 4242 -123 8 -135 C ATOM 1364 N PHE A 183 -12.037 -0.421 26.288 1.00 29.60 N ANISOU 1364 N PHE A 183 3566 4011 3668 51 -51 -94 N ATOM 1365 CA PHE A 183 -10.942 -1.136 26.939 1.00 32.33 C ANISOU 1365 CA PHE A 183 3900 4372 4013 77 -70 -133 C ATOM 1366 C PHE A 183 -11.457 -2.293 27.788 1.00 30.60 C ANISOU 1366 C PHE A 183 3702 4152 3773 108 -93 -107 C ATOM 1367 O PHE A 183 -10.982 -3.427 27.665 1.00 30.30 O ANISOU 1367 O PHE A 183 3671 4110 3730 123 -112 -116 O ATOM 1368 CB PHE A 183 -10.126 -0.174 27.805 1.00 33.08 C ANISOU 1368 CB PHE A 183 3976 4480 4113 88 -72 -175 C ATOM 1369 CG PHE A 183 -9.232 0.763 27.025 1.00 33.14 C ANISOU 1369 CG PHE A 183 3965 4491 4135 50 -52 -214 C ATOM 1370 CD1 PHE A 183 -9.125 0.683 25.643 1.00 40.87 C ANISOU 1370 CD1 PHE A 183 4945 5464 5120 9 -36 -212 C ATOM 1371 CD2 PHE A 183 -8.486 1.719 27.689 1.00 31.33 C ANISOU 1371 CD2 PHE A 183 3721 4274 3910 49 -49 -255 C ATOM 1372 CE1 PHE A 183 -8.296 1.548 24.945 1.00 33.11 C ANISOU 1372 CE1 PHE A 183 3951 4486 4142 -37 -15 -250 C ATOM 1373 CE2 PHE A 183 -7.656 2.581 26.997 1.00 39.06 C ANISOU 1373 CE2 PHE A 183 4688 5258 4896 4 -29 -293 C ATOM 1374 CZ PHE A 183 -7.563 2.495 25.625 1.00 33.01 C ANISOU 1374 CZ PHE A 183 3925 4484 4131 -42 -11 -290 C ATOM 1375 N ALA A 184 -12.427 -2.022 28.661 1.00 29.24 N ANISOU 1375 N ALA A 184 3543 3983 3584 117 -92 -78 N ATOM 1376 CA ALA A 184 -12.826 -3.007 29.661 1.00 26.29 C ANISOU 1376 CA ALA A 184 3196 3612 3181 137 -112 -59 C ATOM 1377 C ALA A 184 -13.840 -4.003 29.111 1.00 25.38 C ANISOU 1377 C ALA A 184 3106 3487 3049 118 -109 -14 C ATOM 1378 O ALA A 184 -13.677 -5.217 29.276 1.00 27.03 O ANISOU 1378 O ALA A 184 3345 3685 3241 127 -131 -6 O ATOM 1379 CB ALA A 184 -13.392 -2.296 30.893 1.00 29.85 C ANISOU 1379 CB ALA A 184 3647 4079 3616 147 -108 -55 C ATOM 1380 N CYS A 185 -14.897 -3.517 28.462 1.00 31.93 N ANISOU 1380 N CYS A 185 3929 4320 3882 93 -85 12 N ATOM 1381 CA CYS A 185 -16.024 -4.364 28.092 1.00 32.25 C ANISOU 1381 CA CYS A 185 3989 4361 3902 70 -80 52 C ATOM 1382 C CYS A 185 -15.953 -4.910 26.671 1.00 27.40 C ANISOU 1382 C CYS A 185 3378 3733 3301 48 -75 62 C ATOM 1383 O CYS A 185 -16.745 -5.792 26.328 1.00 33.47 O ANISOU 1383 O CYS A 185 4166 4500 4051 27 -72 92 O ATOM 1384 CB CYS A 185 -17.333 -3.590 28.268 1.00 24.39 C ANISOU 1384 CB CYS A 185 2978 3387 2900 59 -60 71 C ATOM 1385 SG CYS A 185 -17.644 -3.113 29.986 1.00 32.75 S ANISOU 1385 SG CYS A 185 4036 4472 3936 78 -62 59 S ATOM 1386 N VAL A 186 -15.037 -4.422 25.840 1.00 27.68 N ANISOU 1386 N VAL A 186 3394 3760 3364 45 -71 35 N ATOM 1387 CA VAL A 186 -14.906 -4.918 24.476 1.00 29.99 C ANISOU 1387 CA VAL A 186 3688 4042 3666 19 -64 39 C ATOM 1388 C VAL A 186 -13.531 -5.546 24.300 1.00 32.09 C ANISOU 1388 C VAL A 186 3950 4301 3943 34 -78 -3 C ATOM 1389 O VAL A 186 -13.413 -6.727 23.952 1.00 28.70 O ANISOU 1389 O VAL A 186 3538 3860 3506 35 -90 -2 O ATOM 1390 CB VAL A 186 -15.126 -3.792 23.448 1.00 32.67 C ANISOU 1390 CB VAL A 186 4011 4381 4022 -9 -44 42 C ATOM 1391 CG1 VAL A 186 -14.711 -4.247 22.055 1.00 28.61 C ANISOU 1391 CG1 VAL A 186 3496 3860 3514 -40 -36 36 C ATOM 1392 CG2 VAL A 186 -16.580 -3.343 23.447 1.00 36.99 C ANISOU 1392 CG2 VAL A 186 4560 4935 4559 -16 -37 81 C ATOM 1393 N LEU A 187 -12.482 -4.766 24.562 1.00 27.96 N ANISOU 1393 N LEU A 187 3401 3787 3437 46 -79 -47 N ATOM 1394 CA LEU A 187 -11.136 -5.187 24.188 1.00 34.25 C ANISOU 1394 CA LEU A 187 4178 4588 4247 56 -88 -99 C ATOM 1395 C LEU A 187 -10.650 -6.339 25.061 1.00 30.92 C ANISOU 1395 C LEU A 187 3773 4158 3816 103 -126 -114 C ATOM 1396 O LEU A 187 -10.089 -7.316 24.552 1.00 32.31 O ANISOU 1396 O LEU A 187 3952 4327 3998 115 -141 -138 O ATOM 1397 CB LEU A 187 -10.181 -3.995 24.267 1.00 29.97 C ANISOU 1397 CB LEU A 187 3602 4064 3721 49 -77 -145 C ATOM 1398 CG LEU A 187 -8.811 -4.184 23.620 1.00 42.81 C ANISOU 1398 CG LEU A 187 5195 5709 5362 43 -76 -211 C ATOM 1399 CD1 LEU A 187 -8.939 -4.547 22.145 1.00 50.41 C ANISOU 1399 CD1 LEU A 187 6157 6669 6327 0 -55 -207 C ATOM 1400 CD2 LEU A 187 -7.984 -2.924 23.788 1.00 41.64 C ANISOU 1400 CD2 LEU A 187 5017 5582 5222 25 -61 -254 C ATOM 1401 N VAL A 188 -10.847 -6.246 26.379 1.00 33.93 N ANISOU 1401 N VAL A 188 4170 4540 4182 131 -144 -103 N ATOM 1402 CA VAL A 188 -10.452 -7.348 27.260 1.00 34.75 C ANISOU 1402 CA VAL A 188 4304 4629 4269 174 -186 -110 C ATOM 1403 C VAL A 188 -11.172 -8.640 26.892 1.00 35.09 C ANISOU 1403 C VAL A 188 4395 4643 4294 166 -197 -71 C ATOM 1404 O VAL A 188 -10.499 -9.667 26.713 1.00 37.75 O ANISOU 1404 O VAL A 188 4748 4962 4634 194 -228 -95 O ATOM 1405 CB VAL A 188 -10.662 -6.951 28.734 1.00 35.63 C ANISOU 1405 CB VAL A 188 4431 4748 4360 195 -200 -98 C ATOM 1406 CG1 VAL A 188 -10.706 -8.191 29.619 1.00 29.71 C ANISOU 1406 CG1 VAL A 188 3736 3973 3579 225 -244 -81 C ATOM 1407 CG2 VAL A 188 -9.551 -6.019 29.198 1.00 26.17 C ANISOU 1407 CG2 VAL A 188 3190 3574 3180 216 -204 -152 C ATOM 1408 N PRO A 189 -12.505 -8.672 26.773 1.00 38.86 N ANISOU 1408 N PRO A 189 4896 5118 4751 129 -175 -17 N ATOM 1409 CA PRO A 189 -13.164 -9.907 26.305 1.00 35.87 C ANISOU 1409 CA PRO A 189 4561 4714 4353 111 -181 15 C ATOM 1410 C PRO A 189 -12.615 -10.443 24.992 1.00 30.94 C ANISOU 1410 C PRO A 189 3925 4080 3752 106 -179 -10 C ATOM 1411 O PRO A 189 -12.445 -11.660 24.855 1.00 34.42 O ANISOU 1411 O PRO A 189 4404 4490 4183 119 -205 -11 O ATOM 1412 CB PRO A 189 -14.633 -9.480 26.170 1.00 36.50 C ANISOU 1412 CB PRO A 189 4644 4810 4416 66 -148 64 C ATOM 1413 CG PRO A 189 -14.798 -8.394 27.171 1.00 32.95 C ANISOU 1413 CG PRO A 189 4174 4384 3963 75 -140 62 C ATOM 1414 CD PRO A 189 -13.479 -7.664 27.230 1.00 30.93 C ANISOU 1414 CD PRO A 189 3880 4134 3737 107 -148 12 C ATOM 1415 N LEU A 190 -12.339 -9.575 24.016 1.00 32.14 N ANISOU 1415 N LEU A 190 4028 4253 3930 83 -149 -31 N ATOM 1416 CA LEU A 190 -11.819 -10.055 22.739 1.00 33.04 C ANISOU 1416 CA LEU A 190 4128 4364 4062 70 -141 -59 C ATOM 1417 C LEU A 190 -10.446 -10.690 22.909 1.00 38.90 C ANISOU 1417 C LEU A 190 4859 5101 4820 119 -175 -122 C ATOM 1418 O LEU A 190 -10.161 -11.738 22.317 1.00 35.15 O ANISOU 1418 O LEU A 190 4399 4607 4349 128 -190 -140 O ATOM 1419 CB LEU A 190 -11.763 -8.909 21.732 1.00 29.63 C ANISOU 1419 CB LEU A 190 3653 3958 3647 29 -103 -69 C ATOM 1420 CG LEU A 190 -13.117 -8.453 21.178 1.00 37.46 C ANISOU 1420 CG LEU A 190 4654 4951 4626 -17 -76 -13 C ATOM 1421 CD1 LEU A 190 -12.970 -7.154 20.397 1.00 38.42 C ANISOU 1421 CD1 LEU A 190 4745 5090 4762 -51 -49 -22 C ATOM 1422 CD2 LEU A 190 -13.740 -9.529 20.303 1.00 33.90 C ANISOU 1422 CD2 LEU A 190 4229 4487 4163 -43 -73 11 C ATOM 1423 N LEU A 191 -9.581 -10.075 23.717 1.00 34.43 N ANISOU 1423 N LEU A 191 4266 4552 4264 152 -190 -160 N ATOM 1424 CA LEU A 191 -8.281 -10.677 23.986 1.00 33.31 C ANISOU 1424 CA LEU A 191 4109 4411 4137 208 -229 -226 C ATOM 1425 C LEU A 191 -8.439 -12.033 24.663 1.00 38.63 C ANISOU 1425 C LEU A 191 4847 5040 4792 252 -280 -207 C ATOM 1426 O LEU A 191 -7.704 -12.979 24.356 1.00 37.47 O ANISOU 1426 O LEU A 191 4705 4877 4656 291 -313 -250 O ATOM 1427 CB LEU A 191 -7.441 -9.731 24.843 1.00 35.06 C ANISOU 1427 CB LEU A 191 4290 4662 4367 233 -236 -266 C ATOM 1428 CG LEU A 191 -7.044 -8.420 24.157 1.00 31.23 C ANISOU 1428 CG LEU A 191 3748 4219 3901 187 -191 -297 C ATOM 1429 CD1 LEU A 191 -6.439 -7.449 25.157 1.00 33.43 C ANISOU 1429 CD1 LEU A 191 3998 4522 4181 205 -196 -325 C ATOM 1430 CD2 LEU A 191 -6.073 -8.692 23.019 1.00 28.95 C ANISOU 1430 CD2 LEU A 191 3415 3954 3633 177 -180 -364 C ATOM 1431 N LEU A 192 -9.405 -12.153 25.577 1.00 33.13 N ANISOU 1431 N LEU A 192 4203 4322 4062 244 -288 -145 N ATOM 1432 CA LEU A 192 -9.677 -13.446 26.198 1.00 33.16 C ANISOU 1432 CA LEU A 192 4285 4278 4038 271 -334 -118 C ATOM 1433 C LEU A 192 -10.072 -14.483 25.151 1.00 34.00 C ANISOU 1433 C LEU A 192 4422 4354 4143 250 -331 -106 C ATOM 1434 O LEU A 192 -9.581 -15.617 25.169 1.00 35.47 O ANISOU 1434 O LEU A 192 4649 4499 4327 291 -377 -127 O ATOM 1435 CB LEU A 192 -10.773 -13.300 27.257 1.00 36.26 C ANISOU 1435 CB LEU A 192 4726 4664 4389 245 -331 -53 C ATOM 1436 CG LEU A 192 -10.378 -12.593 28.556 1.00 39.85 C ANISOU 1436 CG LEU A 192 5171 5137 4834 274 -348 -63 C ATOM 1437 CD1 LEU A 192 -11.613 -12.273 29.377 1.00 51.41 C ANISOU 1437 CD1 LEU A 192 6668 6607 6258 232 -327 -4 C ATOM 1438 CD2 LEU A 192 -9.413 -13.441 29.371 1.00 47.77 C ANISOU 1438 CD2 LEU A 192 6214 6108 5828 341 -418 -93 C ATOM 1439 N MET A 193 -10.962 -14.109 24.225 1.00 33.05 N ANISOU 1439 N MET A 193 4285 4250 4023 188 -280 -74 N ATOM 1440 CA MET A 193 -11.347 -15.020 23.149 1.00 35.09 C ANISOU 1440 CA MET A 193 4567 4486 4280 162 -271 -65 C ATOM 1441 C MET A 193 -10.123 -15.513 22.391 1.00 38.05 C ANISOU 1441 C MET A 193 4912 4858 4688 200 -291 -137 C ATOM 1442 O MET A 193 -9.993 -16.707 22.096 1.00 39.81 O ANISOU 1442 O MET A 193 5178 5040 4908 220 -320 -148 O ATOM 1443 CB MET A 193 -12.306 -14.328 22.180 1.00 40.00 C ANISOU 1443 CB MET A 193 5159 5138 4902 93 -214 -31 C ATOM 1444 CG MET A 193 -13.703 -14.099 22.710 1.00 43.85 C ANISOU 1444 CG MET A 193 5676 5630 5356 52 -195 36 C ATOM 1445 SD MET A 193 -14.737 -13.317 21.455 1.00 44.04 S ANISOU 1445 SD MET A 193 5659 5689 5384 -15 -140 65 S ATOM 1446 CE MET A 193 -15.688 -12.174 22.458 1.00 38.02 C ANISOU 1446 CE MET A 193 4883 4956 4604 -27 -122 103 C ATOM 1447 N LEU A 194 -9.223 -14.592 22.048 1.00 36.55 N ANISOU 1447 N LEU A 194 4647 4712 4528 208 -272 -192 N ATOM 1448 CA LEU A 194 -7.996 -14.966 21.356 1.00 36.67 C ANISOU 1448 CA LEU A 194 4619 4739 4574 242 -286 -275 C ATOM 1449 C LEU A 194 -7.251 -16.052 22.123 1.00 34.15 C ANISOU 1449 C LEU A 194 4338 4381 4256 323 -357 -310 C ATOM 1450 O LEU A 194 -6.808 -17.050 21.544 1.00 35.67 O ANISOU 1450 O LEU A 194 4542 4550 4461 353 -382 -351 O ATOM 1451 CB LEU A 194 -7.117 -13.728 21.172 1.00 39.51 C ANISOU 1451 CB LEU A 194 4897 5158 4957 234 -258 -330 C ATOM 1452 CG LEU A 194 -5.830 -13.907 20.372 1.00 37.83 C ANISOU 1452 CG LEU A 194 4622 4979 4774 253 -260 -426 C ATOM 1453 CD1 LEU A 194 -6.144 -14.274 18.930 1.00 42.67 C ANISOU 1453 CD1 LEU A 194 5229 5595 5390 201 -223 -430 C ATOM 1454 CD2 LEU A 194 -4.997 -12.641 20.442 1.00 38.69 C ANISOU 1454 CD2 LEU A 194 4658 5146 4897 238 -234 -477 C ATOM 1455 N GLY A 195 -7.115 -15.876 23.438 1.00 38.42 N ANISOU 1455 N GLY A 195 4903 4912 4783 363 -393 -296 N ATOM 1456 CA GLY A 195 -6.414 -16.866 24.238 1.00 38.28 C ANISOU 1456 CA GLY A 195 4930 4853 4763 444 -469 -326 C ATOM 1457 C GLY A 195 -7.117 -18.209 24.259 1.00 36.39 C ANISOU 1457 C GLY A 195 4790 4540 4496 446 -503 -279 C ATOM 1458 O GLY A 195 -6.469 -19.258 24.269 1.00 46.87 O ANISOU 1458 O GLY A 195 6152 5825 5832 510 -562 -320 O ATOM 1459 N VAL A 196 -8.450 -18.198 24.271 1.00 36.75 N ANISOU 1459 N VAL A 196 4885 4570 4508 378 -468 -197 N ATOM 1460 CA VAL A 196 -9.201 -19.450 24.280 1.00 34.63 C ANISOU 1460 CA VAL A 196 4716 4236 4207 364 -493 -150 C ATOM 1461 C VAL A 196 -9.014 -20.189 22.961 1.00 38.29 C ANISOU 1461 C VAL A 196 5171 4685 4694 360 -485 -186 C ATOM 1462 O VAL A 196 -8.780 -21.404 22.940 1.00 37.07 O ANISOU 1462 O VAL A 196 5083 4468 4533 399 -536 -200 O ATOM 1463 CB VAL A 196 -10.689 -19.179 24.570 1.00 40.07 C ANISOU 1463 CB VAL A 196 5444 4927 4852 283 -450 -64 C ATOM 1464 CG1 VAL A 196 -11.520 -20.437 24.345 1.00 36.77 C ANISOU 1464 CG1 VAL A 196 5122 4450 4400 249 -463 -19 C ATOM 1465 CG2 VAL A 196 -10.868 -18.666 25.990 1.00 35.08 C ANISOU 1465 CG2 VAL A 196 4835 4302 4191 290 -466 -32 C ATOM 1466 N TYR A 197 -9.112 -19.470 21.840 1.00 37.43 N ANISOU 1466 N TYR A 197 4984 4629 4608 312 -422 -203 N ATOM 1467 CA TYR A 197 -8.927 -20.116 20.544 1.00 34.64 C ANISOU 1467 CA TYR A 197 4618 4270 4275 301 -409 -241 C ATOM 1468 C TYR A 197 -7.494 -20.601 20.372 1.00 36.76 C ANISOU 1468 C TYR A 197 4852 4535 4580 384 -456 -339 C ATOM 1469 O TYR A 197 -7.257 -21.652 19.766 1.00 35.52 O ANISOU 1469 O TYR A 197 4724 4340 4432 408 -481 -372 O ATOM 1470 CB TYR A 197 -9.322 -19.163 19.415 1.00 36.06 C ANISOU 1470 CB TYR A 197 4726 4510 4466 228 -334 -237 C ATOM 1471 CG TYR A 197 -10.819 -19.102 19.194 1.00 36.88 C ANISOU 1471 CG TYR A 197 4869 4609 4537 150 -295 -152 C ATOM 1472 CD1 TYR A 197 -11.511 -20.202 18.702 1.00 34.32 C ANISOU 1472 CD1 TYR A 197 4608 4241 4191 122 -299 -124 C ATOM 1473 CD2 TYR A 197 -11.542 -17.951 19.483 1.00 37.41 C ANISOU 1473 CD2 TYR A 197 4908 4715 4591 105 -256 -104 C ATOM 1474 CE1 TYR A 197 -12.878 -20.160 18.504 1.00 38.71 C ANISOU 1474 CE1 TYR A 197 5193 4801 4715 49 -263 -53 C ATOM 1475 CE2 TYR A 197 -12.913 -17.898 19.286 1.00 40.03 C ANISOU 1475 CE2 TYR A 197 5268 5050 4894 40 -224 -36 C ATOM 1476 CZ TYR A 197 -13.576 -19.008 18.798 1.00 45.51 C ANISOU 1476 CZ TYR A 197 6018 5707 5566 10 -227 -11 C ATOM 1477 OH TYR A 197 -14.939 -18.969 18.599 1.00 42.44 O ANISOU 1477 OH TYR A 197 5650 5329 5146 -57 -194 50 O ATOM 1478 N LEU A 198 -6.523 -19.857 20.904 1.00 38.47 N ANISOU 1478 N LEU A 198 5006 4794 4819 430 -469 -391 N ATOM 1479 CA LEU A 198 -5.146 -20.338 20.890 1.00 38.56 C ANISOU 1479 CA LEU A 198 4980 4807 4863 517 -521 -491 C ATOM 1480 C LEU A 198 -5.026 -21.659 21.637 1.00 39.35 C ANISOU 1480 C LEU A 198 5179 4823 4950 593 -608 -486 C ATOM 1481 O LEU A 198 -4.347 -22.583 21.176 1.00 44.83 O ANISOU 1481 O LEU A 198 5877 5489 5666 652 -650 -552 O ATOM 1482 CB LEU A 198 -4.215 -19.289 21.499 1.00 40.51 C ANISOU 1482 CB LEU A 198 5147 5116 5128 548 -523 -541 C ATOM 1483 CG LEU A 198 -3.873 -18.097 20.602 1.00 53.79 C ANISOU 1483 CG LEU A 198 6724 6882 6830 488 -450 -582 C ATOM 1484 CD1 LEU A 198 -3.217 -16.992 21.416 1.00 47.93 C ANISOU 1484 CD1 LEU A 198 5925 6192 6095 504 -449 -609 C ATOM 1485 CD2 LEU A 198 -2.969 -18.524 19.452 1.00 50.67 C ANISOU 1485 CD2 LEU A 198 6266 6519 6468 503 -443 -682 C ATOM 1486 N ARG A 199 -5.689 -21.771 22.790 1.00 40.66 N ANISOU 1486 N ARG A 199 5428 4944 5076 591 -637 -408 N ATOM 1487 CA ARG A 199 -5.654 -23.012 23.553 1.00 40.40 C ANISOU 1487 CA ARG A 199 5509 4822 5020 652 -722 -392 C ATOM 1488 C ARG A 199 -6.458 -24.123 22.889 1.00 37.25 C ANISOU 1488 C ARG A 199 5196 4357 4601 616 -721 -354 C ATOM 1489 O ARG A 199 -6.180 -25.302 23.136 1.00 39.27 O ANISOU 1489 O ARG A 199 5538 4533 4850 676 -795 -368 O ATOM 1490 CB ARG A 199 -6.164 -22.756 24.972 1.00 37.09 C ANISOU 1490 CB ARG A 199 5156 4380 4555 645 -747 -320 C ATOM 1491 CG ARG A 199 -5.251 -21.842 25.774 1.00 41.61 C ANISOU 1491 CG ARG A 199 5659 5006 5146 696 -766 -363 C ATOM 1492 CD ARG A 199 -5.926 -21.295 27.023 1.00 59.39 C ANISOU 1492 CD ARG A 199 7957 7257 7352 663 -763 -288 C ATOM 1493 NE ARG A 199 -6.015 -22.284 28.090 1.00 72.63 N ANISOU 1493 NE ARG A 199 9759 8852 8986 704 -846 -251 N ATOM 1494 CZ ARG A 199 -6.493 -22.035 29.301 1.00 74.65 C ANISOU 1494 CZ ARG A 199 10073 9098 9194 684 -860 -191 C ATOM 1495 N ILE A 200 -7.441 -23.777 22.055 1.00 38.39 N ANISOU 1495 N ILE A 200 5322 4529 4736 520 -643 -308 N ATOM 1496 CA ILE A 200 -8.186 -24.791 21.311 1.00 39.01 C ANISOU 1496 CA ILE A 200 5470 4554 4796 478 -635 -279 C ATOM 1497 C ILE A 200 -7.312 -25.397 20.221 1.00 44.78 C ANISOU 1497 C ILE A 200 6161 5283 5572 525 -649 -370 C ATOM 1498 O ILE A 200 -7.218 -26.623 20.085 1.00 44.73 O ANISOU 1498 O ILE A 200 6234 5201 5561 563 -701 -385 O ATOM 1499 CB ILE A 200 -9.470 -24.184 20.716 1.00 45.02 C ANISOU 1499 CB ILE A 200 6214 5357 5535 365 -550 -210 C ATOM 1500 CG1 ILE A 200 -10.501 -23.914 21.812 1.00 44.85 C ANISOU 1500 CG1 ILE A 200 6254 5324 5462 317 -544 -120 C ATOM 1501 CG2 ILE A 200 -10.056 -25.106 19.652 1.00 47.18 C ANISOU 1501 CG2 ILE A 200 6529 5596 5801 320 -532 -201 C ATOM 1502 CD1 ILE A 200 -11.668 -23.049 21.360 1.00 39.07 C ANISOU 1502 CD1 ILE A 200 5479 4650 4714 219 -463 -65 C ATOM 1503 N PHE A 201 -6.674 -24.546 19.416 1.00 50.27 N ANISOU 1503 N PHE A 201 6734 6061 6306 519 -601 -435 N ATOM 1504 CA PHE A 201 -5.835 -25.042 18.331 1.00 49.36 C ANISOU 1504 CA PHE A 201 6566 5959 6231 554 -604 -531 C ATOM 1505 C PHE A 201 -4.599 -25.753 18.861 1.00 47.49 C ANISOU 1505 C PHE A 201 6337 5687 6021 678 -694 -617 C ATOM 1506 O PHE A 201 -4.137 -26.723 18.252 1.00 52.61 O ANISOU 1506 O PHE A 201 6999 6299 6690 726 -728 -681 O ATOM 1507 CB PHE A 201 -5.441 -23.886 17.414 1.00 47.44 C ANISOU 1507 CB PHE A 201 6193 5817 6014 506 -529 -579 C ATOM 1508 CG PHE A 201 -6.606 -23.250 16.714 1.00 40.92 C ANISOU 1508 CG PHE A 201 5360 5023 5165 392 -448 -505 C ATOM 1509 CD1 PHE A 201 -7.490 -24.020 15.977 1.00 45.73 C ANISOU 1509 CD1 PHE A 201 6027 5593 5755 340 -430 -465 C ATOM 1510 CD2 PHE A 201 -6.829 -21.887 16.806 1.00 49.37 C ANISOU 1510 CD2 PHE A 201 6369 6158 6231 340 -395 -475 C ATOM 1511 CE1 PHE A 201 -8.567 -23.442 15.335 1.00 48.20 C ANISOU 1511 CE1 PHE A 201 6331 5938 6046 241 -362 -399 C ATOM 1512 CE2 PHE A 201 -7.906 -21.303 16.165 1.00 45.95 C ANISOU 1512 CE2 PHE A 201 5931 5750 5777 244 -330 -409 C ATOM 1513 CZ PHE A 201 -8.775 -22.083 15.430 1.00 39.63 C ANISOU 1513 CZ PHE A 201 5184 4917 4958 197 -315 -372 C ATOM 1514 N ALA A 202 -4.054 -25.294 19.988 1.00 49.59 N ANISOU 1514 N ALA A 202 6593 5963 6287 734 -736 -623 N ATOM 1515 CA ALA A 202 -2.938 -26.004 20.601 1.00 49.76 C ANISOU 1515 CA ALA A 202 6630 5946 6330 859 -833 -700 C ATOM 1516 C ALA A 202 -3.370 -27.378 21.097 1.00 50.04 C ANISOU 1516 C ALA A 202 6817 5859 6336 899 -912 -655 C ATOM 1517 O ALA A 202 -2.626 -28.356 20.960 1.00 57.80 O ANISOU 1517 O ALA A 202 7827 6792 7343 992 -985 -727 O ATOM 1518 CB ALA A 202 -2.355 -25.178 21.747 1.00 46.82 C ANISOU 1518 CB ALA A 202 6219 5612 5957 902 -861 -708 C ATOM 1519 N ALA A 203 -4.572 -27.472 21.671 1.00 43.99 N ANISOU 1519 N ALA A 203 6153 5044 5516 828 -899 -539 N ATOM 1520 CA ALA A 203 -5.047 -28.752 22.186 1.00 48.27 C ANISOU 1520 CA ALA A 203 6853 5468 6020 849 -971 -488 C ATOM 1521 C ALA A 203 -5.362 -29.731 21.062 1.00 49.97 C ANISOU 1521 C ALA A 203 7108 5636 6242 828 -960 -505 C ATOM 1522 O ALA A 203 -5.183 -30.942 21.231 1.00 58.49 O ANISOU 1522 O ALA A 203 8294 6615 7313 889 -1040 -517 O ATOM 1523 CB ALA A 203 -6.282 -28.540 23.061 1.00 46.84 C ANISOU 1523 CB ALA A 203 6763 5261 5774 763 -948 -365 C ATOM 1524 N ALA A 204 -5.836 -29.236 19.918 1.00 53.52 N ANISOU 1524 N ALA A 204 7479 6152 6705 743 -867 -505 N ATOM 1525 CA ALA A 204 -6.090 -30.120 18.787 1.00 52.78 C ANISOU 1525 CA ALA A 204 7412 6022 6618 720 -853 -528 C ATOM 1526 C ALA A 204 -4.786 -30.627 18.189 1.00 58.82 C ANISOU 1526 C ALA A 204 8119 6790 7440 825 -899 -659 C ATOM 1527 O ALA A 204 -4.680 -31.799 17.811 1.00 56.94 O ANISOU 1527 O ALA A 204 7954 6474 7207 866 -947 -691 O ATOM 1528 CB ALA A 204 -6.913 -29.393 17.726 1.00 42.74 C ANISOU 1528 CB ALA A 204 6069 4827 5343 601 -743 -496 C ATOM 1529 N ARG A 205 -3.782 -29.754 18.097 1.00 59.32 N ANISOU 1529 N ARG A 205 8049 6945 7545 867 -885 -740 N ATOM 1530 CA ARG A 205 -2.495 -30.156 17.544 1.00 61.07 C ANISOU 1530 CA ARG A 205 8196 7188 7820 966 -925 -878 C ATOM 1531 C ARG A 205 -1.827 -31.206 18.423 1.00 65.08 C ANISOU 1531 C ARG A 205 8796 7599 8334 1099 -1052 -915 C ATOM 1532 O ARG A 205 -1.293 -32.201 17.919 1.00 68.48 O ANISOU 1532 O ARG A 205 9246 7980 8791 1173 -1104 -995 O ATOM 1533 CB ARG A 205 -1.602 -28.925 17.387 1.00 66.26 C ANISOU 1533 CB ARG A 205 8694 7970 8512 971 -881 -953 C ATOM 1534 CG ARG A 205 -0.250 -29.184 16.742 1.00 83.67 C ANISOU 1534 CG ARG A 205 10796 10225 10771 1059 -907 -1109 C ATOM 1535 CD ARG A 205 0.660 -27.980 16.916 1.00 78.06 C ANISOU 1535 CD ARG A 205 9944 9630 10084 1068 -877 -1177 C ATOM 1536 NE ARG A 205 0.889 -27.686 18.326 1.00 83.10 N ANISOU 1536 NE ARG A 205 10616 10247 10710 1127 -940 -1143 N ATOM 1537 CZ ARG A 205 1.394 -26.551 18.787 1.00 90.00 C ANISOU 1537 CZ ARG A 205 11398 11206 11590 1119 -915 -1163 C ATOM 1538 NH1 ARG A 205 1.736 -25.565 17.974 1.00 88.40 N ANISOU 1538 NH1 ARG A 205 11069 11115 11404 1051 -828 -1216 N ATOM 1539 NH2 ARG A 205 1.557 -26.399 20.099 1.00 99.29 N ANISOU 1539 NH2 ARG A 205 12618 12356 12753 1176 -978 -1129 N ATOM 1540 N ARG A 206 -1.856 -31.007 19.743 1.00 57.85 N ANISOU 1540 N ARG A 206 7939 6650 7391 1132 -1106 -858 N ATOM 1541 CA ARG A 206 -1.241 -31.974 20.647 1.00 55.51 C ANISOU 1541 CA ARG A 206 7742 6255 7094 1259 -1235 -885 C ATOM 1542 C ARG A 206 -1.951 -33.320 20.580 1.00 60.41 C ANISOU 1542 C ARG A 206 8529 6741 7681 1254 -1284 -832 C ATOM 1543 O ARG A 206 -1.311 -34.373 20.678 1.00 69.48 O ANISOU 1543 O ARG A 206 9745 7807 8848 1365 -1384 -894 O ATOM 1544 CB ARG A 206 -1.252 -31.438 22.080 1.00 46.99 C ANISOU 1544 CB ARG A 206 6701 5171 5982 1276 -1275 -823 C ATOM 1545 CG ARG A 206 -0.335 -30.246 22.304 1.00 69.57 C ANISOU 1545 CG ARG A 206 9407 8150 8877 1307 -1252 -892 C ATOM 1546 N GLN A 207 -3.273 -33.309 20.412 1.00 54.47 N ANISOU 1546 N GLN A 207 7849 5967 6881 1126 -1217 -720 N ATOM 1547 CA GLN A 207 -4.025 -34.558 20.408 1.00 54.74 C ANISOU 1547 CA GLN A 207 8050 5874 6874 1104 -1258 -662 C ATOM 1548 C GLN A 207 -3.836 -35.324 19.104 1.00 55.58 C ANISOU 1548 C GLN A 207 8139 5962 7016 1117 -1247 -738 C ATOM 1549 O GLN A 207 -3.765 -36.557 19.115 1.00 56.03 O ANISOU 1549 O GLN A 207 8319 5904 7067 1173 -1326 -752 O ATOM 1550 CB GLN A 207 -5.504 -34.271 20.667 1.00 50.94 C ANISOU 1550 CB GLN A 207 7640 5387 6327 958 -1187 -526 C ATOM 1551 CG GLN A 207 -5.798 -33.927 22.119 1.00 47.36 C ANISOU 1551 CG GLN A 207 7260 4911 5823 951 -1223 -443 C ATOM 1552 CD GLN A 207 -7.215 -33.444 22.339 1.00 49.11 C ANISOU 1552 CD GLN A 207 7518 5157 5986 805 -1140 -325 C ATOM 1553 OE1 GLN A 207 -8.159 -33.953 21.735 1.00 57.72 O ANISOU 1553 OE1 GLN A 207 8667 6217 7047 716 -1097 -279 O ATOM 1554 NE2 GLN A 207 -7.371 -32.451 23.205 1.00 49.17 N ANISOU 1554 NE2 GLN A 207 7485 5224 5974 779 -1116 -281 N ATOM 1555 N LEU A 208 -3.748 -34.617 17.975 1.00 56.36 N ANISOU 1555 N LEU A 208 8092 6171 7150 1064 -1151 -788 N ATOM 1556 CA LEU A 208 -3.443 -35.286 16.714 1.00 59.42 C ANISOU 1556 CA LEU A 208 8447 6556 7574 1080 -1138 -875 C ATOM 1557 C LEU A 208 -2.043 -35.883 16.740 1.00 66.80 C ANISOU 1557 C LEU A 208 9349 7468 8564 1239 -1234 -1012 C ATOM 1558 O LEU A 208 -1.833 -37.017 16.292 1.00 58.66 O ANISOU 1558 O LEU A 208 8386 6354 7547 1297 -1289 -1066 O ATOM 1559 CB LEU A 208 -3.578 -34.303 15.552 1.00 57.45 C ANISOU 1559 CB LEU A 208 8045 6437 7345 986 -1016 -902 C ATOM 1560 CG LEU A 208 -5.001 -33.888 15.181 1.00 78.33 C ANISOU 1560 CG LEU A 208 10717 9103 9943 832 -921 -785 C ATOM 1561 CD1 LEU A 208 -5.005 -32.530 14.491 1.00 71.55 C ANISOU 1561 CD1 LEU A 208 9704 8381 9100 755 -817 -797 C ATOM 1562 CD2 LEU A 208 -5.644 -34.943 14.291 1.00 75.25 C ANISOU 1562 CD2 LEU A 208 10408 8646 9539 786 -911 -777 C ATOM 1563 N ALA A1001 -1.071 -35.132 17.263 1.00 67.60 N ANISOU 1563 N ALA A1001 8357 4669 12659 1183 719 -519 N ATOM 1564 CA ALA A1001 0.297 -35.634 17.332 1.00 67.34 C ANISOU 1564 CA ALA A1001 8299 4671 12617 1084 753 -562 C ATOM 1565 C ALA A1001 0.387 -36.863 18.227 1.00 67.15 C ANISOU 1565 C ALA A1001 8160 4831 12522 1058 684 -603 C ATOM 1566 O ALA A1001 1.072 -37.836 17.891 1.00 64.87 O ANISOU 1566 O ALA A1001 7864 4606 12178 1012 666 -573 O ATOM 1567 CB ALA A1001 1.232 -34.534 17.833 1.00 60.76 C ANISOU 1567 CB ALA A1001 7463 3747 11877 1019 847 -672 C ATOM 1568 N ASP A1002 -0.297 -36.837 19.373 1.00 69.21 N ANISOU 1568 N ASP A1002 8333 5178 12784 1089 645 -672 N ATOM 1569 CA ASP A1002 -0.283 -37.992 20.265 1.00 74.94 C ANISOU 1569 CA ASP A1002 8951 6080 13442 1069 579 -710 C ATOM 1570 C ASP A1002 -0.843 -39.225 19.571 1.00 73.98 C ANISOU 1570 C ASP A1002 8842 6039 13227 1105 495 -593 C ATOM 1571 O ASP A1002 -0.303 -40.327 19.717 1.00 79.20 O ANISOU 1571 O ASP A1002 9457 6809 13825 1060 460 -593 O ATOM 1572 CB ASP A1002 -1.075 -37.687 21.535 1.00 70.70 C ANISOU 1572 CB ASP A1002 8329 5612 12921 1110 553 -791 C ATOM 1573 CG ASP A1002 -0.353 -36.723 22.454 1.00 92.67 C ANISOU 1573 CG ASP A1002 11080 8351 15780 1059 624 -927 C ATOM 1574 OD1 ASP A1002 0.796 -36.346 22.138 1.00 99.27 O ANISOU 1574 OD1 ASP A1002 11950 9110 16658 985 690 -960 O ATOM 1575 OD2 ASP A1002 -0.936 -36.342 23.492 1.00 98.80 O ANISOU 1575 OD2 ASP A1002 11796 9168 16574 1093 613 -1001 O ATOM 1576 N LEU A1003 -1.926 -39.063 18.810 1.00 66.00 N ANISOU 1576 N LEU A1003 7894 4976 12206 1186 461 -493 N ATOM 1577 CA LEU A1003 -2.459 -40.187 18.049 1.00 62.47 C ANISOU 1577 CA LEU A1003 7471 4591 11674 1219 380 -377 C ATOM 1578 C LEU A1003 -1.412 -40.742 17.091 1.00 71.08 C ANISOU 1578 C LEU A1003 8627 5651 12730 1162 402 -326 C ATOM 1579 O LEU A1003 -1.255 -41.962 16.966 1.00 67.26 O ANISOU 1579 O LEU A1003 8119 5270 12166 1144 344 -286 O ATOM 1580 CB LEU A1003 -3.711 -39.753 17.285 1.00 64.20 C ANISOU 1580 CB LEU A1003 7759 4735 11899 1312 348 -278 C ATOM 1581 CG LEU A1003 -4.938 -39.414 18.134 1.00 74.01 C ANISOU 1581 CG LEU A1003 8934 6026 13161 1383 309 -304 C ATOM 1582 CD1 LEU A1003 -6.058 -38.875 17.258 1.00 68.85 C ANISOU 1582 CD1 LEU A1003 8359 5279 12522 1473 287 -203 C ATOM 1583 CD2 LEU A1003 -5.410 -40.631 18.916 1.00 82.40 C ANISOU 1583 CD2 LEU A1003 9891 7266 14151 1388 222 -308 C ATOM 1584 N GLU A1004 -0.684 -39.862 16.404 1.00 84.15 N ANISOU 1584 N GLU A1004 10366 7164 14443 1134 488 -325 N ATOM 1585 CA GLU A1004 0.342 -40.309 15.473 1.00 87.64 C ANISOU 1585 CA GLU A1004 10874 7569 14857 1082 520 -276 C ATOM 1586 C GLU A1004 1.568 -40.857 16.195 1.00 87.72 C ANISOU 1586 C GLU A1004 10804 7666 14857 992 545 -364 C ATOM 1587 O GLU A1004 2.347 -41.600 15.590 1.00 88.15 O ANISOU 1587 O GLU A1004 10887 7739 14865 952 549 -322 O ATOM 1588 CB GLU A1004 0.722 -39.150 14.555 1.00 84.98 C ANISOU 1588 CB GLU A1004 10649 7051 14590 1081 610 -248 C ATOM 1589 CG GLU A1004 1.764 -39.485 13.503 1.00103.19 C ANISOU 1589 CG GLU A1004 13033 9302 16873 1034 655 -190 C ATOM 1590 CD GLU A1004 1.274 -40.489 12.469 1.00103.52 C ANISOU 1590 CD GLU A1004 13141 9370 16821 1080 583 -61 C ATOM 1591 OE1 GLU A1004 1.291 -41.703 12.754 1.00 95.51 O ANISOU 1591 OE1 GLU A1004 12070 8491 15730 1067 515 -52 O ATOM 1592 OE2 GLU A1004 0.873 -40.058 11.367 1.00110.98 O ANISOU 1592 OE2 GLU A1004 14199 10201 17769 1129 595 31 O ATOM 1593 N ASP A1005 1.755 -40.512 17.472 1.00 76.81 N ANISOU 1593 N ASP A1005 9326 6340 13518 962 561 -485 N ATOM 1594 CA ASP A1005 2.832 -41.110 18.254 1.00 72.93 C ANISOU 1594 CA ASP A1005 8750 5949 13012 881 571 -571 C ATOM 1595 C ASP A1005 2.482 -42.534 18.667 1.00 72.67 C ANISOU 1595 C ASP A1005 8647 6084 12882 891 477 -549 C ATOM 1596 O ASP A1005 3.301 -43.449 18.525 1.00 79.89 O ANISOU 1596 O ASP A1005 9546 7065 13745 842 468 -540 O ATOM 1597 CB ASP A1005 3.134 -40.256 19.489 1.00 66.13 C ANISOU 1597 CB ASP A1005 7813 5089 12226 846 615 -709 C ATOM 1598 CG ASP A1005 3.861 -38.972 19.145 1.00 87.65 C ANISOU 1598 CG ASP A1005 10599 7657 15048 808 717 -747 C ATOM 1599 OD1 ASP A1005 4.526 -38.934 18.089 1.00 82.05 O ANISOU 1599 OD1 ASP A1005 9969 6862 14344 781 763 -684 O ATOM 1600 OD2 ASP A1005 3.772 -38.006 19.932 1.00 85.27 O ANISOU 1600 OD2 ASP A1005 10267 7314 14816 804 751 -839 O ATOM 1601 N ASN A1006 1.267 -42.739 19.182 1.00 65.61 N ANISOU 1601 N ASN A1006 7709 5258 11961 956 407 -538 N ATOM 1602 CA ASN A1006 0.855 -44.079 19.586 1.00 78.49 C ANISOU 1602 CA ASN A1006 9274 7048 13502 968 315 -513 C ATOM 1603 C ASN A1006 0.871 -45.039 18.402 1.00 68.05 C ANISOU 1603 C ASN A1006 8024 5728 12103 978 273 -391 C ATOM 1604 O ASN A1006 1.321 -46.184 18.525 1.00 61.83 O ANISOU 1604 O ASN A1006 7200 5046 11245 945 232 -384 O ATOM 1605 CB ASN A1006 -0.535 -44.027 20.218 1.00 77.99 C ANISOU 1605 CB ASN A1006 9160 7041 13431 1042 253 -509 C ATOM 1606 CG ASN A1006 -0.511 -43.482 21.632 1.00 75.11 C ANISOU 1606 CG ASN A1006 8700 6725 13114 1028 276 -638 C ATOM 1607 OD1 ASN A1006 0.351 -42.678 21.985 1.00 82.80 O ANISOU 1607 OD1 ASN A1006 9671 7638 14153 978 351 -727 O ATOM 1608 ND2 ASN A1006 -1.455 -43.927 22.454 1.00 75.84 N ANISOU 1608 ND2 ASN A1006 8716 6929 13172 1073 211 -649 N ATOM 1609 N TRP A1007 0.388 -44.584 17.243 1.00 69.60 N ANISOU 1609 N TRP A1007 8328 5806 12311 1025 280 -295 N ATOM 1610 CA TRP A1007 0.372 -45.431 16.055 1.00 62.29 C ANISOU 1610 CA TRP A1007 7485 4871 11312 1040 240 -176 C ATOM 1611 C TRP A1007 1.785 -45.804 15.624 1.00 68.45 C ANISOU 1611 C TRP A1007 8294 5639 12077 968 294 -185 C ATOM 1612 O TRP A1007 2.043 -46.950 15.239 1.00 71.85 O ANISOU 1612 O TRP A1007 8735 6139 12425 956 248 -131 O ATOM 1613 CB TRP A1007 -0.374 -44.714 14.929 1.00 59.73 C ANISOU 1613 CB TRP A1007 7274 4411 11011 1105 246 -80 C ATOM 1614 CG TRP A1007 -0.317 -45.397 13.593 1.00 72.09 C ANISOU 1614 CG TRP A1007 8944 5939 12509 1121 217 41 C ATOM 1615 CD1 TRP A1007 0.502 -45.080 12.548 1.00 65.88 C ANISOU 1615 CD1 TRP A1007 8260 5039 11733 1099 285 84 C ATOM 1616 CD2 TRP A1007 -1.118 -46.502 13.153 1.00 75.99 C ANISOU 1616 CD2 TRP A1007 9453 6507 12913 1165 113 135 C ATOM 1617 NE1 TRP A1007 0.264 -45.919 11.487 1.00 74.33 N ANISOU 1617 NE1 TRP A1007 9413 6108 12723 1128 229 198 N ATOM 1618 CE2 TRP A1007 -0.726 -46.802 11.833 1.00 72.19 C ANISOU 1618 CE2 TRP A1007 9091 5950 12390 1167 121 230 C ATOM 1619 CE3 TRP A1007 -2.127 -47.267 13.746 1.00 73.47 C ANISOU 1619 CE3 TRP A1007 9061 6310 12546 1200 13 149 C ATOM 1620 CZ2 TRP A1007 -1.306 -47.834 11.097 1.00 72.03 C ANISOU 1620 CZ2 TRP A1007 9120 5970 12279 1204 30 335 C ATOM 1621 CZ3 TRP A1007 -2.701 -48.292 13.014 1.00 69.44 C ANISOU 1621 CZ3 TRP A1007 8595 5838 11950 1234 -77 255 C ATOM 1622 CH2 TRP A1007 -2.290 -48.565 11.704 1.00 75.00 C ANISOU 1622 CH2 TRP A1007 9420 6464 12612 1235 -70 345 C ATOM 1623 N GLU A1008 2.716 -44.850 15.688 1.00 74.85 N ANISOU 1623 N GLU A1008 9116 6358 12965 918 393 -251 N ATOM 1624 CA GLU A1008 4.100 -45.145 15.329 1.00 76.41 C ANISOU 1624 CA GLU A1008 9331 6543 13157 847 451 -263 C ATOM 1625 C GLU A1008 4.745 -46.090 16.335 1.00 71.99 C ANISOU 1625 C GLU A1008 8661 6137 12556 792 423 -339 C ATOM 1626 O GLU A1008 5.541 -46.957 15.957 1.00 76.55 O ANISOU 1626 O GLU A1008 9249 6758 13079 756 422 -311 O ATOM 1627 CB GLU A1008 4.901 -43.848 15.227 1.00 85.53 C ANISOU 1627 CB GLU A1008 10517 7566 14414 805 563 -319 C ATOM 1628 CG GLU A1008 4.657 -43.072 13.948 1.00 93.21 C ANISOU 1628 CG GLU A1008 11622 8377 15417 844 607 -228 C ATOM 1629 CD GLU A1008 5.096 -41.627 14.054 1.00107.66 C ANISOU 1629 CD GLU A1008 13472 10076 17358 816 706 -292 C ATOM 1630 OE1 GLU A1008 5.876 -41.308 14.976 1.00107.86 O ANISOU 1630 OE1 GLU A1008 13417 10129 17434 751 750 -403 O ATOM 1631 OE2 GLU A1008 4.653 -40.807 13.222 1.00116.06 O ANISOU 1631 OE2 GLU A1008 14635 11007 18457 860 738 -231 O ATOM 1632 N THR A1009 4.414 -45.940 17.620 1.00 73.24 N ANISOU 1632 N THR A1009 8716 6376 12737 789 400 -434 N ATOM 1633 CA THR A1009 5.010 -46.799 18.639 1.00 72.34 C ANISOU 1633 CA THR A1009 8495 6407 12584 739 373 -512 C ATOM 1634 C THR A1009 4.619 -48.255 18.429 1.00 62.12 C ANISOU 1634 C THR A1009 7194 5230 11180 763 281 -437 C ATOM 1635 O THR A1009 5.447 -49.159 18.592 1.00 66.59 O ANISOU 1635 O THR A1009 7725 5880 11696 717 272 -453 O ATOM 1636 CB THR A1009 4.590 -46.329 20.033 1.00 64.45 C ANISOU 1636 CB THR A1009 7394 5468 11626 742 362 -622 C ATOM 1637 OG1 THR A1009 5.094 -45.008 20.265 1.00 80.07 O ANISOU 1637 OG1 THR A1009 9380 7338 13706 711 449 -699 O ATOM 1638 CG2 THR A1009 5.126 -47.268 21.103 1.00 69.35 C ANISOU 1638 CG2 THR A1009 7906 6244 12199 697 327 -698 C ATOM 1639 N LEU A1010 3.360 -48.503 18.068 1.00 56.37 N ANISOU 1639 N LEU A1010 6497 4507 10414 834 211 -355 N ATOM 1640 CA LEU A1010 2.918 -49.870 17.816 1.00 68.61 C ANISOU 1640 CA LEU A1010 8048 6160 11861 857 119 -279 C ATOM 1641 C LEU A1010 3.702 -50.492 16.667 1.00 62.89 C ANISOU 1641 C LEU A1010 7411 5399 11086 836 133 -201 C ATOM 1642 O LEU A1010 4.182 -51.627 16.769 1.00 67.69 O ANISOU 1642 O LEU A1010 7992 6105 11620 809 97 -193 O ATOM 1643 CB LEU A1010 1.419 -49.881 17.513 1.00 63.72 C ANISOU 1643 CB LEU A1010 7456 5533 11222 937 45 -199 C ATOM 1644 CG LEU A1010 0.758 -51.254 17.400 1.00 73.50 C ANISOU 1644 CG LEU A1010 8682 6884 12359 965 -62 -125 C ATOM 1645 CD1 LEU A1010 0.314 -51.751 18.769 1.00 87.84 C ANISOU 1645 CD1 LEU A1010 10372 8845 14157 963 -114 -195 C ATOM 1646 CD2 LEU A1010 -0.411 -51.202 16.432 1.00 70.11 C ANISOU 1646 CD2 LEU A1010 8336 6391 11912 1037 -117 -8 C ATOM 1647 N ASN A1011 3.851 -49.755 15.564 1.00 63.50 N ANISOU 1647 N ASN A1011 7595 5331 11199 849 189 -142 N ATOM 1648 CA ASN A1011 4.515 -50.307 14.388 1.00 66.78 C ANISOU 1648 CA ASN A1011 8107 5704 11564 838 205 -58 C ATOM 1649 C ASN A1011 6.011 -50.472 14.620 1.00 67.48 C ANISOU 1649 C ASN A1011 8163 5814 11665 761 275 -123 C ATOM 1650 O ASN A1011 6.605 -51.467 14.188 1.00 63.39 O ANISOU 1650 O ASN A1011 7667 5344 11074 743 259 -81 O ATOM 1651 CB ASN A1011 4.256 -49.412 13.178 1.00 64.20 C ANISOU 1651 CB ASN A1011 7905 5214 11275 876 250 20 C ATOM 1652 CG ASN A1011 2.780 -49.271 12.867 1.00 78.02 C ANISOU 1652 CG ASN A1011 9692 6941 13012 956 177 91 C ATOM 1653 OD1 ASN A1011 1.965 -50.086 13.300 1.00 75.93 O ANISOU 1653 OD1 ASN A1011 9377 6783 12690 984 83 109 O ATOM 1654 ND2 ASN A1011 2.427 -48.238 12.112 1.00 78.95 N ANISOU 1654 ND2 ASN A1011 9897 6918 13183 992 219 134 N ATOM 1655 N ASP A1012 6.640 -49.508 15.296 1.00 60.42 N ANISOU 1655 N ASP A1012 7214 4883 10860 715 352 -224 N ATOM 1656 CA ASP A1012 8.069 -49.618 15.562 1.00 56.03 C ANISOU 1656 CA ASP A1012 6617 4349 10323 639 419 -289 C ATOM 1657 C ASP A1012 8.365 -50.777 16.504 1.00 62.49 C ANISOU 1657 C ASP A1012 7334 5334 11076 611 360 -340 C ATOM 1658 O ASP A1012 9.304 -51.548 16.273 1.00 67.30 O ANISOU 1658 O ASP A1012 7941 5988 11640 573 373 -330 O ATOM 1659 CB ASP A1012 8.597 -48.307 16.140 1.00 59.01 C ANISOU 1659 CB ASP A1012 6956 4651 10815 595 506 -389 C ATOM 1660 CG ASP A1012 8.513 -47.164 15.152 1.00 74.36 C ANISOU 1660 CG ASP A1012 9005 6422 12825 614 576 -339 C ATOM 1661 OD1 ASP A1012 8.429 -47.439 13.936 1.00 75.31 O ANISOU 1661 OD1 ASP A1012 9232 6480 12903 645 577 -230 O ATOM 1662 OD2 ASP A1012 8.536 -45.994 15.589 1.00 78.27 O ANISOU 1662 OD2 ASP A1012 9482 6843 13412 599 631 -408 O ATOM 1663 N ASN A1013 7.574 -50.922 17.569 1.00 61.00 N ANISOU 1663 N ASN A1013 7059 5238 10880 630 298 -394 N ATOM 1664 CA ASN A1013 7.808 -52.010 18.511 1.00 64.45 C ANISOU 1664 CA ASN A1013 7399 5834 11254 606 241 -444 C ATOM 1665 C ASN A1013 7.483 -53.365 17.896 1.00 61.42 C ANISOU 1665 C ASN A1013 7058 5520 10759 636 163 -345 C ATOM 1666 O ASN A1013 8.070 -54.378 18.292 1.00 60.47 O ANISOU 1666 O ASN A1013 6888 5510 10579 606 136 -365 O ATOM 1667 CB ASN A1013 6.994 -51.786 19.781 1.00 62.32 C ANISOU 1667 CB ASN A1013 7033 5641 11004 624 198 -522 C ATOM 1668 CG ASN A1013 7.538 -50.651 20.618 1.00 70.04 C ANISOU 1668 CG ASN A1013 7953 6580 12081 581 270 -641 C ATOM 1669 OD1 ASN A1013 8.380 -49.880 20.159 1.00 81.04 O ANISOU 1669 OD1 ASN A1013 9385 7869 13538 543 354 -658 O ATOM 1670 ND2 ASN A1013 7.065 -50.542 21.851 1.00 78.09 N ANISOU 1670 ND2 ASN A1013 8880 7681 13112 588 239 -725 N ATOM 1671 N LEU A1014 6.553 -53.409 16.941 1.00 59.24 N ANISOU 1671 N LEU A1014 6874 5182 10454 696 124 -238 N ATOM 1672 CA LEU A1014 6.347 -54.634 16.176 1.00 61.59 C ANISOU 1672 CA LEU A1014 7231 5523 10648 721 56 -137 C ATOM 1673 C LEU A1014 7.611 -55.009 15.415 1.00 69.81 C ANISOU 1673 C LEU A1014 8328 6533 11664 682 112 -110 C ATOM 1674 O LEU A1014 8.031 -56.173 15.412 1.00 70.11 O ANISOU 1674 O LEU A1014 8356 6662 11622 668 74 -91 O ATOM 1675 CB LEU A1014 5.172 -54.462 15.214 1.00 62.93 C ANISOU 1675 CB LEU A1014 7497 5613 10801 791 9 -28 C ATOM 1676 CG LEU A1014 3.776 -54.701 15.790 1.00 68.75 C ANISOU 1676 CG LEU A1014 8185 6419 11517 841 -83 -16 C ATOM 1677 CD1 LEU A1014 2.722 -54.067 14.900 1.00 76.88 C ANISOU 1677 CD1 LEU A1014 9303 7339 12567 905 -102 71 C ATOM 1678 CD2 LEU A1014 3.507 -56.189 15.947 1.00 69.20 C ANISOU 1678 CD2 LEU A1014 8217 6606 11469 846 -180 25 C ATOM 1679 N LYS A1015 8.235 -54.026 14.761 1.00 72.89 N ANISOU 1679 N LYS A1015 8778 6793 12122 665 206 -108 N ATOM 1680 CA LYS A1015 9.481 -54.282 14.046 1.00 71.02 C ANISOU 1680 CA LYS A1015 8591 6521 11872 627 272 -84 C ATOM 1681 C LYS A1015 10.587 -54.706 15.004 1.00 64.84 C ANISOU 1681 C LYS A1015 7701 5842 11092 561 298 -181 C ATOM 1682 O LYS A1015 11.404 -55.575 14.676 1.00 70.90 O ANISOU 1682 O LYS A1015 8482 6654 11801 540 303 -156 O ATOM 1683 CB LYS A1015 9.889 -53.036 13.262 1.00 71.16 C ANISOU 1683 CB LYS A1015 8685 6378 11973 619 373 -69 C ATOM 1684 CG LYS A1015 9.032 -52.788 12.032 1.00 77.56 C ANISOU 1684 CG LYS A1015 9626 7079 12763 685 355 47 C ATOM 1685 CD LYS A1015 8.959 -51.313 11.668 1.00 86.65 C ANISOU 1685 CD LYS A1015 10826 8082 14017 689 435 39 C ATOM 1686 CE LYS A1015 10.339 -50.696 11.526 1.00 89.55 C ANISOU 1686 CE LYS A1015 11192 8382 14451 624 552 -6 C ATOM 1687 NZ LYS A1015 10.302 -49.457 10.699 1.00 94.44 N ANISOU 1687 NZ LYS A1015 11903 8834 15144 638 631 30 N ATOM 1688 N VAL A1016 10.632 -54.102 16.193 1.00 66.62 N ANISOU 1688 N VAL A1016 7821 6106 11385 530 312 -293 N ATOM 1689 CA VAL A1016 11.614 -54.510 17.194 1.00 69.72 C ANISOU 1689 CA VAL A1016 8105 6604 11779 469 327 -391 C ATOM 1690 C VAL A1016 11.422 -55.976 17.557 1.00 66.77 C ANISOU 1690 C VAL A1016 7695 6377 11297 482 236 -371 C ATOM 1691 O VAL A1016 12.392 -56.733 17.683 1.00 71.35 O ANISOU 1691 O VAL A1016 8244 7027 11838 445 246 -388 O ATOM 1692 CB VAL A1016 11.516 -53.602 18.436 1.00 62.76 C ANISOU 1692 CB VAL A1016 7124 5739 10983 442 346 -512 C ATOM 1693 CG1 VAL A1016 12.323 -54.180 19.588 1.00 57.82 C ANISOU 1693 CG1 VAL A1016 6381 5244 10343 390 336 -612 C ATOM 1694 CG2 VAL A1016 11.993 -52.198 18.104 1.00 72.13 C ANISOU 1694 CG2 VAL A1016 8344 6782 12280 415 446 -542 C ATOM 1695 N ILE A1017 10.168 -56.400 17.727 1.00 67.93 N ANISOU 1695 N ILE A1017 7844 6571 11396 535 147 -331 N ATOM 1696 CA ILE A1017 9.891 -57.790 18.079 1.00 72.50 C ANISOU 1696 CA ILE A1017 8390 7285 11872 548 57 -309 C ATOM 1697 C ILE A1017 10.316 -58.722 16.951 1.00 72.95 C ANISOU 1697 C ILE A1017 8541 7331 11847 559 46 -209 C ATOM 1698 O ILE A1017 10.861 -59.806 17.194 1.00 73.64 O ANISOU 1698 O ILE A1017 8599 7519 11863 541 16 -214 O ATOM 1699 CB ILE A1017 8.399 -57.961 18.424 1.00 61.45 C ANISOU 1699 CB ILE A1017 6976 5927 10446 603 -33 -280 C ATOM 1700 CG1 ILE A1017 8.087 -57.300 19.770 1.00 61.01 C ANISOU 1700 CG1 ILE A1017 6809 5919 10453 591 -30 -391 C ATOM 1701 CG2 ILE A1017 8.020 -59.436 18.451 1.00 56.18 C ANISOU 1701 CG2 ILE A1017 6306 5375 9666 623 -129 -225 C ATOM 1702 CD1 ILE A1017 6.620 -56.964 19.961 1.00 65.55 C ANISOU 1702 CD1 ILE A1017 7382 6487 11039 648 -86 -364 C ATOM 1703 N GLU A1018 10.077 -58.317 15.701 1.00 70.71 N ANISOU 1703 N GLU A1018 8376 6923 11568 591 71 -118 N ATOM 1704 CA GLU A1018 10.441 -59.159 14.565 1.00 65.02 C ANISOU 1704 CA GLU A1018 7757 6182 10767 607 62 -20 C ATOM 1705 C GLU A1018 11.933 -59.466 14.566 1.00 77.88 C ANISOU 1705 C GLU A1018 9364 7835 12393 554 132 -56 C ATOM 1706 O GLU A1018 12.342 -60.622 14.403 1.00 85.18 O ANISOU 1706 O GLU A1018 10300 8834 13230 553 98 -24 O ATOM 1707 CB GLU A1018 10.039 -58.475 13.257 1.00 72.95 C ANISOU 1707 CB GLU A1018 8892 7036 11791 647 92 73 C ATOM 1708 CG GLU A1018 8.546 -58.470 12.986 1.00 80.62 C ANISOU 1708 CG GLU A1018 9907 7987 12738 710 7 140 C ATOM 1709 CD GLU A1018 8.151 -57.460 11.922 1.00 90.78 C ANISOU 1709 CD GLU A1018 11302 9117 14072 745 50 206 C ATOM 1710 OE1 GLU A1018 8.913 -57.288 10.947 1.00 93.93 O ANISOU 1710 OE1 GLU A1018 11790 9428 14471 739 117 252 O ATOM 1711 OE2 GLU A1018 7.082 -56.830 12.067 1.00 89.83 O ANISOU 1711 OE2 GLU A1018 11179 8963 13991 782 18 211 O ATOM 1712 N LYS A1019 12.763 -58.442 14.748 1.00 79.52 N ANISOU 1712 N LYS A1019 9540 7979 12697 509 230 -123 N ATOM 1713 CA LYS A1019 14.209 -58.584 14.680 1.00 77.12 C ANISOU 1713 CA LYS A1019 9214 7684 12404 457 306 -155 C ATOM 1714 C LYS A1019 14.844 -58.828 16.045 1.00 78.14 C ANISOU 1714 C LYS A1019 9202 7936 12552 404 303 -272 C ATOM 1715 O LYS A1019 16.070 -58.744 16.168 1.00 78.62 O ANISOU 1715 O LYS A1019 9224 8004 12645 353 372 -319 O ATOM 1716 CB LYS A1019 14.827 -57.337 14.038 1.00 84.03 C ANISOU 1716 CB LYS A1019 10136 8415 13377 433 419 -155 C ATOM 1717 CG LYS A1019 14.094 -56.837 12.794 1.00 82.93 C ANISOU 1717 CG LYS A1019 10132 8142 13237 486 427 -51 C ATOM 1718 CD LYS A1019 13.816 -57.957 11.796 1.00 96.88 C ANISOU 1718 CD LYS A1019 12003 9920 14887 535 371 64 C ATOM 1719 CE LYS A1019 13.313 -57.401 10.469 1.00102.57 C ANISOU 1719 CE LYS A1019 12865 10496 15611 583 394 167 C ATOM 1720 NZ LYS A1019 12.505 -58.393 9.700 1.00102.30 N ANISOU 1720 NZ LYS A1019 12927 10479 15466 645 302 274 N ATOM 1721 N ALA A1020 14.045 -59.131 17.065 1.00 80.28 N ANISOU 1721 N ALA A1020 9396 8303 12802 416 224 -320 N ATOM 1722 CA ALA A1020 14.588 -59.377 18.391 1.00 88.51 C ANISOU 1722 CA ALA A1020 10309 9465 13856 371 216 -432 C ATOM 1723 C ALA A1020 15.381 -60.680 18.416 1.00 90.61 C ANISOU 1723 C ALA A1020 10557 9835 14034 357 192 -419 C ATOM 1724 O ALA A1020 15.150 -61.592 17.618 1.00 83.28 O ANISOU 1724 O ALA A1020 9710 8916 13018 394 150 -324 O ATOM 1725 CB ALA A1020 13.465 -59.429 19.426 1.00 77.55 C ANISOU 1725 CB ALA A1020 8852 8154 12460 395 136 -477 C ATOM 1726 N ASP A1021 16.330 -60.758 19.353 1.00 95.00 N ANISOU 1726 N ASP A1021 11009 10471 14616 304 218 -517 N ATOM 1727 CA ASP A1021 17.195 -61.920 19.485 1.00102.24 C ANISOU 1727 CA ASP A1021 11897 11490 15458 287 203 -518 C ATOM 1728 C ASP A1021 16.916 -62.750 20.728 1.00 99.41 C ANISOU 1728 C ASP A1021 11440 11285 15045 286 123 -581 C ATOM 1729 O ASP A1021 17.250 -63.939 20.740 1.00 91.70 O ANISOU 1729 O ASP A1021 10461 10399 13980 292 82 -555 O ATOM 1730 CB ASP A1021 18.667 -61.480 19.499 1.00107.55 C ANISOU 1730 CB ASP A1021 12528 12139 16196 227 300 -573 C ATOM 1731 CG ASP A1021 19.001 -60.531 18.362 1.00112.62 C ANISOU 1731 CG ASP A1021 13258 12627 16906 222 390 -520 C ATOM 1732 OD1 ASP A1021 18.719 -60.877 17.194 1.00113.28 O ANISOU 1732 OD1 ASP A1021 13456 12649 16936 264 388 -410 O ATOM 1733 OD2 ASP A1021 19.533 -59.435 18.636 1.00117.31 O ANISOU 1733 OD2 ASP A1021 13809 13158 17605 177 463 -588 O ATOM 1734 N ASN A1022 16.311 -62.166 21.762 1.00 97.31 N ANISOU 1734 N ASN A1022 11097 11047 14827 280 99 -661 N ATOM 1735 CA ASN A1022 16.025 -62.878 22.999 1.00 88.87 C ANISOU 1735 CA ASN A1022 9934 10122 13711 280 27 -725 C ATOM 1736 C ASN A1022 14.609 -62.560 23.454 1.00 80.04 C ANISOU 1736 C ASN A1022 8807 9007 12597 319 -31 -725 C ATOM 1737 O ASN A1022 13.977 -61.612 22.980 1.00 82.19 O ANISOU 1737 O ASN A1022 9129 9171 12929 339 -7 -699 O ATOM 1738 CB ASN A1022 17.025 -62.513 24.106 1.00 79.08 C ANISOU 1738 CB ASN A1022 8579 8940 12527 221 67 -852 C ATOM 1739 CG ASN A1022 17.280 -61.026 24.189 1.00 83.81 C ANISOU 1739 CG ASN A1022 9162 9432 13249 188 145 -915 C ATOM 1740 OD1 ASN A1022 16.586 -60.302 24.903 1.00 90.37 O ANISOU 1740 OD1 ASN A1022 9954 10255 14128 194 132 -973 O ATOM 1741 ND2 ASN A1022 18.282 -60.560 23.455 1.00 95.96 N ANISOU 1741 ND2 ASN A1022 10734 10887 14839 153 228 -902 N ATOM 1742 N ALA A1023 14.114 -63.376 24.388 1.00 72.89 N ANISOU 1742 N ALA A1023 7837 8229 11630 333 -108 -753 N ATOM 1743 CA ALA A1023 12.772 -63.167 24.920 1.00 63.14 C ANISOU 1743 CA ALA A1023 6582 7013 10396 372 -166 -755 C ATOM 1744 C ALA A1023 12.666 -61.856 25.686 1.00 67.02 C ANISOU 1744 C ALA A1023 7013 7462 10990 354 -120 -853 C ATOM 1745 O ALA A1023 11.612 -61.211 25.665 1.00 74.30 O ANISOU 1745 O ALA A1023 7953 8332 11945 389 -134 -836 O ATOM 1746 CB ALA A1023 12.377 -64.332 25.826 1.00 62.43 C ANISOU 1746 CB ALA A1023 6429 7074 10218 385 -251 -770 C ATOM 1747 N ALA A1024 13.737 -61.449 26.372 1.00 63.97 N ANISOU 1747 N ALA A1024 6555 7096 10654 300 -68 -955 N ATOM 1748 CA ALA A1024 13.685 -60.220 27.155 1.00 65.30 C ANISOU 1748 CA ALA A1024 6668 7226 10919 280 -28 -1055 C ATOM 1749 C ALA A1024 13.442 -59.008 26.265 1.00 68.59 C ANISOU 1749 C ALA A1024 7160 7483 11418 288 34 -1019 C ATOM 1750 O ALA A1024 12.707 -58.087 26.643 1.00 73.31 O ANISOU 1750 O ALA A1024 7747 8033 12074 306 41 -1054 O ATOM 1751 CB ALA A1024 14.979 -60.052 27.950 1.00 61.31 C ANISOU 1751 CB ALA A1024 6078 6767 10450 217 15 -1166 C ATOM 1752 N GLN A1025 14.052 -58.987 25.078 1.00 71.49 N ANISOU 1752 N GLN A1025 7607 7764 11792 277 82 -948 N ATOM 1753 CA GLN A1025 13.796 -57.901 24.139 1.00 70.82 C ANISOU 1753 CA GLN A1025 7605 7525 11779 289 139 -902 C ATOM 1754 C GLN A1025 12.334 -57.881 23.711 1.00 72.60 C ANISOU 1754 C GLN A1025 7892 7717 11978 357 85 -820 C ATOM 1755 O GLN A1025 11.718 -56.813 23.625 1.00 71.41 O ANISOU 1755 O GLN A1025 7764 7474 11896 376 110 -827 O ATOM 1756 CB GLN A1025 14.709 -58.035 22.922 1.00 61.43 C ANISOU 1756 CB GLN A1025 6494 6261 10587 270 197 -831 C ATOM 1757 CG GLN A1025 16.110 -57.494 23.142 1.00 73.88 C ANISOU 1757 CG GLN A1025 8022 7813 12234 201 280 -910 C ATOM 1758 CD GLN A1025 17.062 -57.865 22.022 1.00 86.16 C ANISOU 1758 CD GLN A1025 9644 9322 13771 184 331 -837 C ATOM 1759 OE1 GLN A1025 16.641 -58.302 20.951 1.00 86.49 O ANISOU 1759 OE1 GLN A1025 9785 9319 13758 227 316 -726 O ATOM 1760 NE2 GLN A1025 18.356 -57.696 22.268 1.00 86.56 N ANISOU 1760 NE2 GLN A1025 9641 9382 13867 123 393 -900 N ATOM 1761 N VAL A1026 11.763 -59.056 23.439 1.00 74.95 N ANISOU 1761 N VAL A1026 8215 8087 12176 394 8 -742 N ATOM 1762 CA VAL A1026 10.347 -59.129 23.095 1.00 73.29 C ANISOU 1762 CA VAL A1026 8053 7857 11937 457 -54 -665 C ATOM 1763 C VAL A1026 9.494 -58.647 24.261 1.00 76.38 C ANISOU 1763 C VAL A1026 8363 8296 12362 474 -83 -739 C ATOM 1764 O VAL A1026 8.515 -57.915 24.075 1.00 82.53 O ANISOU 1764 O VAL A1026 9172 9006 13181 514 -88 -713 O ATOM 1765 CB VAL A1026 9.978 -60.564 22.677 1.00 68.71 C ANISOU 1765 CB VAL A1026 7508 7356 11242 486 -136 -575 C ATOM 1766 CG1 VAL A1026 8.477 -60.698 22.484 1.00 68.27 C ANISOU 1766 CG1 VAL A1026 7485 7298 11158 548 -210 -503 C ATOM 1767 CG2 VAL A1026 10.724 -60.950 21.406 1.00 67.75 C ANISOU 1767 CG2 VAL A1026 7483 7171 11087 480 -104 -493 C ATOM 1768 N LYS A1027 9.857 -59.045 25.483 1.00 76.52 N ANISOU 1768 N LYS A1027 8279 8433 12363 447 -102 -831 N ATOM 1769 CA LYS A1027 9.100 -58.623 26.658 1.00 80.89 C ANISOU 1769 CA LYS A1027 8754 9038 12943 464 -127 -906 C ATOM 1770 C LYS A1027 9.080 -57.104 26.783 1.00 82.44 C ANISOU 1770 C LYS A1027 8951 9122 13248 457 -57 -967 C ATOM 1771 O LYS A1027 8.028 -56.509 27.048 1.00 81.66 O ANISOU 1771 O LYS A1027 8850 8997 13180 499 -73 -967 O ATOM 1772 CB LYS A1027 9.699 -59.260 27.913 1.00 81.63 C ANISOU 1772 CB LYS A1027 8743 9270 13001 430 -148 -1002 C ATOM 1773 CG LYS A1027 8.981 -58.920 29.214 1.00 84.85 C ANISOU 1773 CG LYS A1027 9067 9745 13426 448 -174 -1084 C ATOM 1774 CD LYS A1027 9.898 -59.146 30.409 1.00 85.19 C ANISOU 1774 CD LYS A1027 9014 9889 13464 401 -167 -1202 C ATOM 1775 CE LYS A1027 9.307 -58.587 31.693 1.00 92.47 C ANISOU 1775 CE LYS A1027 9861 10859 14416 417 -177 -1296 C ATOM 1776 NZ LYS A1027 8.306 -59.499 32.310 1.00 86.63 N ANISOU 1776 NZ LYS A1027 9082 10236 13598 461 -256 -1269 N ATOM 1777 N ASP A1028 10.233 -56.459 26.593 1.00 87.12 N ANISOU 1777 N ASP A1028 9551 9648 13905 403 20 -1017 N ATOM 1778 CA ASP A1028 10.298 -55.008 26.741 1.00 96.26 C ANISOU 1778 CA ASP A1028 10710 10696 15169 390 88 -1080 C ATOM 1779 C ASP A1028 9.420 -54.308 25.712 1.00 88.78 C ANISOU 1779 C ASP A1028 9858 9619 14255 438 102 -991 C ATOM 1780 O ASP A1028 8.708 -53.352 26.041 1.00 88.66 O ANISOU 1780 O ASP A1028 9839 9549 14299 465 115 -1022 O ATOM 1781 CB ASP A1028 11.747 -54.534 26.621 1.00 96.31 C ANISOU 1781 CB ASP A1028 10708 10652 15234 319 168 -1138 C ATOM 1782 CG ASP A1028 11.863 -53.023 26.551 1.00113.42 C ANISOU 1782 CG ASP A1028 12896 12685 17514 302 243 -1188 C ATOM 1783 OD1 ASP A1028 11.729 -52.363 27.605 1.00111.67 O ANISOU 1783 OD1 ASP A1028 12610 12480 17340 293 249 -1290 O ATOM 1784 OD2 ASP A1028 12.083 -52.493 25.441 1.00110.37 O ANISOU 1784 OD2 ASP A1028 12594 12175 17168 300 296 -1124 O ATOM 1785 N ALA A1029 9.458 -54.766 24.459 1.00 77.33 N ANISOU 1785 N ALA A1029 8498 8118 12766 453 100 -880 N ATOM 1786 CA ALA A1029 8.641 -54.142 23.424 1.00 78.90 C ANISOU 1786 CA ALA A1029 8794 8193 12991 501 110 -790 C ATOM 1787 C ALA A1029 7.156 -54.350 23.692 1.00 74.46 C ANISOU 1787 C ALA A1029 8223 7673 12395 568 33 -750 C ATOM 1788 O ALA A1029 6.349 -53.433 23.498 1.00 72.76 O ANISOU 1788 O ALA A1029 8040 7371 12233 607 46 -734 O ATOM 1789 CB ALA A1029 9.020 -54.697 22.051 1.00 61.22 C ANISOU 1789 CB ALA A1029 6654 5901 10707 505 117 -679 C ATOM 1790 N LEU A1030 6.774 -55.549 24.138 1.00 67.75 N ANISOU 1790 N LEU A1030 7329 6955 11459 583 -47 -730 N ATOM 1791 CA LEU A1030 5.368 -55.823 24.413 1.00 67.43 C ANISOU 1791 CA LEU A1030 7274 6963 11386 644 -121 -688 C ATOM 1792 C LEU A1030 4.876 -55.042 25.625 1.00 64.89 C ANISOU 1792 C LEU A1030 6870 6667 11120 655 -112 -786 C ATOM 1793 O LEU A1030 3.726 -54.588 25.653 1.00 62.75 O ANISOU 1793 O LEU A1030 6606 6368 10869 709 -135 -757 O ATOM 1794 CB LEU A1030 5.160 -57.322 24.622 1.00 68.89 C ANISOU 1794 CB LEU A1030 7429 7282 11464 651 -206 -646 C ATOM 1795 CG LEU A1030 5.328 -58.201 23.381 1.00 57.74 C ANISOU 1795 CG LEU A1030 6107 5847 9982 657 -235 -532 C ATOM 1796 CD1 LEU A1030 5.422 -59.665 23.780 1.00 59.92 C ANISOU 1796 CD1 LEU A1030 6343 6264 10159 649 -306 -517 C ATOM 1797 CD2 LEU A1030 4.178 -57.985 22.408 1.00 56.11 C ANISOU 1797 CD2 LEU A1030 5985 5559 9774 717 -270 -423 C ATOM 1798 N THR A1031 5.728 -54.882 26.641 1.00 69.74 N ANISOU 1798 N THR A1031 7405 7335 11756 606 -79 -902 N ATOM 1799 CA THR A1031 5.338 -54.103 27.811 1.00 75.05 C ANISOU 1799 CA THR A1031 8005 8028 12481 615 -65 -1002 C ATOM 1800 C THR A1031 5.040 -52.657 27.431 1.00 75.84 C ANISOU 1800 C THR A1031 8156 7982 12677 633 -4 -1011 C ATOM 1801 O THR A1031 4.085 -52.056 27.939 1.00 70.31 O ANISOU 1801 O THR A1031 7434 7273 12007 679 -13 -1032 O ATOM 1802 CB THR A1031 6.436 -54.166 28.874 1.00 75.28 C ANISOU 1802 CB THR A1031 7953 8132 12520 554 -39 -1125 C ATOM 1803 OG1 THR A1031 6.596 -55.519 29.319 1.00 73.08 O ANISOU 1803 OG1 THR A1031 7623 7995 12148 545 -101 -1118 O ATOM 1804 CG2 THR A1031 6.085 -53.284 30.061 1.00 68.27 C ANISOU 1804 CG2 THR A1031 6999 7254 11686 564 -21 -1234 C ATOM 1805 N LYS A1032 5.847 -52.081 26.536 1.00 66.26 N ANISOU 1805 N LYS A1032 7011 6652 11512 600 62 -994 N ATOM 1806 CA LYS A1032 5.554 -50.743 26.036 1.00 67.22 C ANISOU 1806 CA LYS A1032 7194 6626 11721 619 120 -989 C ATOM 1807 C LYS A1032 4.267 -50.730 25.221 1.00 71.53 C ANISOU 1807 C LYS A1032 7807 7122 12249 693 79 -876 C ATOM 1808 O LYS A1032 3.446 -49.816 25.358 1.00 81.29 O ANISOU 1808 O LYS A1032 9054 8296 13539 737 91 -884 O ATOM 1809 CB LYS A1032 6.717 -50.233 25.187 1.00 75.70 C ANISOU 1809 CB LYS A1032 8330 7589 12845 566 198 -985 C ATOM 1810 CG LYS A1032 8.001 -49.965 25.954 1.00 71.63 C ANISOU 1810 CG LYS A1032 7749 7095 12370 489 250 -1103 C ATOM 1811 CD LYS A1032 9.212 -50.166 25.053 1.00 90.92 C ANISOU 1811 CD LYS A1032 10240 9489 14818 436 300 -1069 C ATOM 1812 CE LYS A1032 10.450 -49.465 25.586 1.00 90.73 C ANISOU 1812 CE LYS A1032 10169 9434 14869 360 372 -1180 C ATOM 1813 NZ LYS A1032 10.419 -48.003 25.311 1.00101.16 N ANISOU 1813 NZ LYS A1032 11538 10603 16294 356 444 -1205 N ATOM 1814 N MET A1033 4.075 -51.739 24.367 1.00 69.06 N ANISOU 1814 N MET A1033 7541 6836 11861 710 28 -769 N ATOM 1815 CA MET A1033 2.907 -51.756 23.491 1.00 70.04 C ANISOU 1815 CA MET A1033 7737 6909 11968 777 -15 -655 C ATOM 1816 C MET A1033 1.612 -51.839 24.290 1.00 66.19 C ANISOU 1816 C MET A1033 7187 6496 11467 834 -76 -660 C ATOM 1817 O MET A1033 0.619 -51.188 23.944 1.00 63.22 O ANISOU 1817 O MET A1033 6846 6050 11124 891 -82 -614 O ATOM 1818 CB MET A1033 3.004 -52.926 22.513 1.00 66.61 C ANISOU 1818 CB MET A1033 7361 6501 11447 780 -65 -547 C ATOM 1819 CG MET A1033 3.985 -52.698 21.374 1.00 70.53 C ANISOU 1819 CG MET A1033 7950 6890 11959 747 -2 -506 C ATOM 1820 SD MET A1033 4.336 -54.197 20.430 1.00 79.40 S ANISOU 1820 SD MET A1033 9131 8065 12972 741 -57 -400 S ATOM 1821 CE MET A1033 2.882 -54.306 19.389 1.00 66.85 C ANISOU 1821 CE MET A1033 7631 6418 11349 822 -126 -264 C ATOM 1822 N ARG A1034 1.599 -52.639 25.357 1.00 61.13 N ANISOU 1822 N ARG A1034 6452 5997 10776 821 -121 -713 N ATOM 1823 CA ARG A1034 0.384 -52.785 26.151 1.00 64.97 C ANISOU 1823 CA ARG A1034 6875 6564 11248 875 -177 -716 C ATOM 1824 C ARG A1034 -0.035 -51.452 26.760 1.00 65.78 C ANISOU 1824 C ARG A1034 6954 6601 11436 901 -127 -789 C ATOM 1825 O ARG A1034 -1.211 -51.074 26.710 1.00 70.47 O ANISOU 1825 O ARG A1034 7555 7174 12048 965 -151 -746 O ATOM 1826 CB ARG A1034 0.594 -53.837 27.241 1.00 64.74 C ANISOU 1826 CB ARG A1034 6749 6696 11152 851 -223 -770 C ATOM 1827 CG ARG A1034 -0.682 -54.236 27.961 1.00 69.98 C ANISOU 1827 CG ARG A1034 7349 7455 11784 906 -290 -752 C ATOM 1828 CD ARG A1034 -0.444 -55.385 28.925 1.00 65.11 C ANISOU 1828 CD ARG A1034 6648 6997 11094 881 -337 -793 C ATOM 1829 NE ARG A1034 -1.691 -55.883 29.494 1.00 79.08 N ANISOU 1829 NE ARG A1034 8361 8858 12826 933 -404 -759 N ATOM 1830 CZ ARG A1034 -2.301 -55.359 30.549 1.00 84.16 C ANISOU 1830 CZ ARG A1034 8935 9541 13500 965 -395 -825 C ATOM 1831 NH1 ARG A1034 -1.805 -54.310 31.186 1.00 88.23 N ANISOU 1831 NH1 ARG A1034 9430 10011 14081 950 -326 -933 N ATOM 1832 NH2 ARG A1034 -3.439 -55.900 30.974 1.00 77.69 N ANISOU 1832 NH2 ARG A1034 8067 8808 12645 1012 -457 -781 N ATOM 1833 N ALA A1035 0.920 -50.720 27.338 1.00 66.97 N ANISOU 1833 N ALA A1035 7081 6721 11643 852 -57 -899 N ATOM 1834 CA ALA A1035 0.595 -49.432 27.942 1.00 71.82 C ANISOU 1834 CA ALA A1035 7679 7270 12338 874 -8 -976 C ATOM 1835 C ALA A1035 0.058 -48.455 26.905 1.00 69.81 C ANISOU 1835 C ALA A1035 7518 6864 12143 916 25 -907 C ATOM 1836 O ALA A1035 -0.885 -47.703 27.180 1.00 72.83 O ANISOU 1836 O ALA A1035 7896 7210 12566 973 29 -913 O ATOM 1837 CB ALA A1035 1.828 -48.852 28.634 1.00 69.45 C ANISOU 1837 CB ALA A1035 7346 6954 12088 806 59 -1102 C ATOM 1838 N ALA A1036 0.645 -48.449 25.706 1.00 67.19 N ANISOU 1838 N ALA A1036 7273 6442 11816 892 51 -841 N ATOM 1839 CA ALA A1036 0.179 -47.541 24.663 1.00 72.23 C ANISOU 1839 CA ALA A1036 8007 6931 12505 931 83 -771 C ATOM 1840 C ALA A1036 -1.247 -47.871 24.240 1.00 75.81 C ANISOU 1840 C ALA A1036 8480 7402 12924 1011 12 -667 C ATOM 1841 O ALA A1036 -2.065 -46.968 24.028 1.00 79.49 O ANISOU 1841 O ALA A1036 8978 7783 13441 1067 27 -645 O ATOM 1842 CB ALA A1036 1.119 -47.599 23.459 1.00 63.53 C ANISOU 1842 CB ALA A1036 6994 5740 11404 889 123 -715 C ATOM 1843 N ALA A1037 -1.564 -49.162 24.109 1.00 76.01 N ANISOU 1843 N ALA A1037 8484 7532 12862 1019 -67 -600 N ATOM 1844 CA ALA A1037 -2.906 -49.556 23.691 1.00 68.63 C ANISOU 1844 CA ALA A1037 7563 6618 11893 1089 -142 -497 C ATOM 1845 C ALA A1037 -3.945 -49.195 24.745 1.00 70.82 C ANISOU 1845 C ALA A1037 7760 6954 12194 1141 -162 -541 C ATOM 1846 O ALA A1037 -5.036 -48.721 24.411 1.00 78.74 O ANISOU 1846 O ALA A1037 8787 7908 13222 1208 -181 -482 O ATOM 1847 CB ALA A1037 -2.943 -51.055 23.397 1.00 69.85 C ANISOU 1847 CB ALA A1037 7711 6878 11950 1078 -222 -425 C ATOM 1848 N LEU A1038 -3.628 -49.417 26.022 1.00 75.92 N ANISOU 1848 N LEU A1038 8311 7705 12831 1114 -157 -643 N ATOM 1849 CA LEU A1038 -4.569 -49.074 27.083 1.00 79.76 C ANISOU 1849 CA LEU A1038 8719 8249 13336 1164 -170 -690 C ATOM 1850 C LEU A1038 -4.769 -47.568 27.192 1.00 86.49 C ANISOU 1850 C LEU A1038 9599 8981 14281 1194 -100 -741 C ATOM 1851 O LEU A1038 -5.869 -47.113 27.527 1.00 87.65 O ANISOU 1851 O LEU A1038 9722 9130 14453 1261 -113 -729 O ATOM 1852 CB LEU A1038 -4.083 -49.647 28.413 1.00 76.77 C ANISOU 1852 CB LEU A1038 8240 8005 12923 1125 -177 -791 C ATOM 1853 CG LEU A1038 -4.141 -51.172 28.504 1.00 78.16 C ANISOU 1853 CG LEU A1038 8375 8318 13004 1109 -256 -740 C ATOM 1854 CD1 LEU A1038 -3.267 -51.680 29.637 1.00 83.35 C ANISOU 1854 CD1 LEU A1038 8953 9085 13630 1054 -248 -847 C ATOM 1855 CD2 LEU A1038 -5.577 -51.641 28.686 1.00 83.12 C ANISOU 1855 CD2 LEU A1038 8962 9017 13601 1178 -328 -668 C ATOM 1856 N ASP A1039 -3.725 -46.780 26.920 1.00 86.74 N ANISOU 1856 N ASP A1039 9680 8909 14366 1145 -24 -796 N ATOM 1857 CA ASP A1039 -3.890 -45.331 26.871 1.00 86.49 C ANISOU 1857 CA ASP A1039 9691 8748 14425 1172 44 -835 C ATOM 1858 C ASP A1039 -4.750 -44.919 25.684 1.00 83.91 C ANISOU 1858 C ASP A1039 9451 8315 14118 1234 32 -719 C ATOM 1859 O ASP A1039 -5.585 -44.014 25.798 1.00 96.08 O ANISOU 1859 O ASP A1039 11001 9795 15709 1296 50 -720 O ATOM 1860 CB ASP A1039 -2.524 -44.649 26.807 1.00 92.75 C ANISOU 1860 CB ASP A1039 10518 9454 15270 1098 125 -916 C ATOM 1861 CG ASP A1039 -1.908 -44.445 28.177 1.00100.41 C ANISOU 1861 CG ASP A1039 11404 10490 16256 1057 153 -1057 C ATOM 1862 OD1 ASP A1039 -2.498 -43.702 28.990 1.00 97.12 O ANISOU 1862 OD1 ASP A1039 10954 10069 15879 1098 170 -1120 O ATOM 1863 OD2 ASP A1039 -0.840 -45.035 28.445 1.00 99.87 O ANISOU 1863 OD2 ASP A1039 11306 10480 16161 986 158 -1105 O ATOM 1864 N ALA A1040 -4.559 -45.569 24.534 1.00 83.62 N ANISOU 1864 N ALA A1040 9480 8253 14039 1221 3 -619 N ATOM 1865 CA ALA A1040 -5.401 -45.284 23.378 1.00 89.93 C ANISOU 1865 CA ALA A1040 10364 8959 14847 1282 -18 -503 C ATOM 1866 C ALA A1040 -6.855 -45.642 23.663 1.00 88.89 C ANISOU 1866 C ALA A1040 10183 8903 14690 1359 -93 -445 C ATOM 1867 O ALA A1040 -7.774 -44.936 23.231 1.00 84.09 O ANISOU 1867 O ALA A1040 9612 8217 14120 1427 -94 -393 O ATOM 1868 CB ALA A1040 -4.890 -46.046 22.155 1.00 77.37 C ANISOU 1868 CB ALA A1040 8851 7341 13205 1252 -42 -409 C ATOM 1869 N GLN A1041 -7.080 -46.739 24.393 1.00 89.99 N ANISOU 1869 N GLN A1041 10235 9193 14764 1350 -156 -452 N ATOM 1870 CA GLN A1041 -8.440 -47.135 24.746 1.00 90.20 C ANISOU 1870 CA GLN A1041 10203 9303 14767 1419 -226 -400 C ATOM 1871 C GLN A1041 -9.111 -46.090 25.628 1.00101.42 C ANISOU 1871 C GLN A1041 11576 10706 16252 1472 -188 -467 C ATOM 1872 O GLN A1041 -10.329 -45.897 25.542 1.00106.60 O ANISOU 1872 O GLN A1041 12220 11363 16920 1547 -223 -407 O ATOM 1873 CB GLN A1041 -8.419 -48.493 25.449 1.00 89.33 C ANISOU 1873 CB GLN A1041 10006 9357 14577 1390 -292 -406 C ATOM 1874 CG GLN A1041 -9.688 -49.307 25.277 1.00100.10 C ANISOU 1874 CG GLN A1041 11339 10800 15895 1445 -385 -303 C ATOM 1875 CD GLN A1041 -9.572 -50.677 25.907 1.00 95.37 C ANISOU 1875 CD GLN A1041 10663 10357 15215 1410 -447 -307 C ATOM 1876 OE1 GLN A1041 -8.824 -50.868 26.865 1.00 94.68 O ANISOU 1876 OE1 GLN A1041 10518 10341 15117 1364 -418 -405 O ATOM 1877 NE2 GLN A1041 -10.303 -51.643 25.366 1.00102.91 N ANISOU 1877 NE2 GLN A1041 11622 11365 16115 1431 -534 -199 N ATOM 1878 N LYS A1042 -8.335 -45.400 26.472 1.00 97.28 N ANISOU 1878 N LYS A1042 11026 10167 15770 1436 -116 -591 N ATOM 1879 CA LYS A1042 -8.896 -44.355 27.322 1.00 93.45 C ANISOU 1879 CA LYS A1042 10504 9657 15345 1486 -74 -663 C ATOM 1880 C LYS A1042 -9.495 -43.238 26.480 1.00102.58 C ANISOU 1880 C LYS A1042 11744 10666 16566 1546 -43 -609 C ATOM 1881 O LYS A1042 -10.617 -42.785 26.735 1.00104.02 O ANISOU 1881 O LYS A1042 11902 10847 16774 1624 -55 -587 O ATOM 1882 CB LYS A1042 -7.819 -43.802 28.257 1.00 87.53 C ANISOU 1882 CB LYS A1042 9728 8902 14629 1428 -3 -806 C ATOM 1883 N ALA A1043 -8.762 -42.787 25.465 1.00 99.15 N ANISOU 1883 N ALA A1043 11407 10105 16159 1512 -1 -585 N ATOM 1884 CA ALA A1043 -9.250 -41.752 24.559 1.00 90.07 C ANISOU 1884 CA ALA A1043 10348 8807 15068 1565 30 -528 C ATOM 1885 C ALA A1043 -10.582 -42.157 23.937 1.00 97.73 C ANISOU 1885 C ALA A1043 11324 9798 16010 1644 -47 -402 C ATOM 1886 O ALA A1043 -10.727 -42.167 22.711 1.00101.00 O ANISOU 1886 O ALA A1043 11825 10131 16419 1659 -65 -303 O ATOM 1887 CB ALA A1043 -8.230 -41.475 23.470 1.00 84.86 C ANISOU 1887 CB ALA A1043 9792 8026 14424 1512 75 -504 C ATOM 1888 N GLU A1057 -20.494 -49.414 15.863 1.00113.88 N ANISOU 1888 N GLU A1057 13521 12101 17648 2068 -1065 901 N ATOM 1889 CA GLU A1057 -19.130 -49.164 15.408 1.00120.46 C ANISOU 1889 CA GLU A1057 14453 12847 18468 2012 -990 853 C ATOM 1890 C GLU A1057 -18.210 -48.873 16.596 1.00128.27 C ANISOU 1890 C GLU A1057 15377 13880 19479 1962 -895 717 C ATOM 1891 O GLU A1057 -17.059 -49.313 16.625 1.00134.73 O ANISOU 1891 O GLU A1057 16223 14708 20259 1891 -863 669 O ATOM 1892 CB GLU A1057 -19.102 -47.996 14.417 1.00103.90 C ANISOU 1892 CB GLU A1057 12473 10583 16419 2057 -941 884 C ATOM 1893 CG GLU A1057 -17.770 -47.816 13.697 1.00107.06 C ANISOU 1893 CG GLU A1057 12992 10884 16802 2002 -875 860 C ATOM 1894 CD GLU A1057 -17.653 -46.467 13.007 1.00117.09 C ANISOU 1894 CD GLU A1057 14362 11992 18135 2044 -800 864 C ATOM 1895 OE1 GLU A1057 -18.576 -45.637 13.153 1.00115.66 O ANISOU 1895 OE1 GLU A1057 14157 11777 18013 2116 -796 876 O ATOM 1896 OE2 GLU A1057 -16.633 -46.236 12.323 1.00116.20 O ANISOU 1896 OE2 GLU A1057 14352 11785 18012 2006 -743 855 O ATOM 1897 N MET A1058 -18.723 -48.116 17.570 1.00113.38 N ANISOU 1897 N MET A1058 13406 12017 17654 2003 -851 655 N ATOM 1898 CA MET A1058 -17.953 -47.844 18.780 1.00107.39 C ANISOU 1898 CA MET A1058 12580 11308 16917 1961 -769 524 C ATOM 1899 C MET A1058 -17.699 -49.124 19.566 1.00122.09 C ANISOU 1899 C MET A1058 14353 13324 18713 1904 -815 497 C ATOM 1900 O MET A1058 -16.593 -49.339 20.078 1.00122.82 O ANISOU 1900 O MET A1058 14435 13445 18785 1837 -765 412 O ATOM 1901 CB MET A1058 -18.686 -46.820 19.649 1.00 95.01 C ANISOU 1901 CB MET A1058 10942 9737 15422 2025 -721 471 C ATOM 1902 N LYS A1059 -18.717 -49.983 19.680 1.00127.67 N ANISOU 1902 N LYS A1059 14993 14130 19385 1930 -911 571 N ATOM 1903 CA LYS A1059 -18.517 -51.290 20.297 1.00122.73 C ANISOU 1903 CA LYS A1059 14294 13647 18692 1877 -964 561 C ATOM 1904 C LYS A1059 -17.537 -52.124 19.482 1.00124.47 C ANISOU 1904 C LYS A1059 14600 13848 18843 1810 -988 589 C ATOM 1905 O LYS A1059 -16.676 -52.813 20.044 1.00124.47 O ANISOU 1905 O LYS A1059 14570 13924 18799 1745 -974 528 O ATOM 1906 CB LYS A1059 -19.857 -52.013 20.433 1.00111.21 C ANISOU 1906 CB LYS A1059 12757 12285 17215 1919 -1065 647 C ATOM 1907 N ASP A1060 -17.649 -52.065 18.151 1.00137.16 N ANISOU 1907 N ASP A1060 16319 15355 20440 1827 -1023 681 N ATOM 1908 CA ASP A1060 -16.710 -52.763 17.280 1.00144.35 C ANISOU 1908 CA ASP A1060 17326 16233 21286 1771 -1039 711 C ATOM 1909 C ASP A1060 -15.298 -52.217 17.420 1.00142.99 C ANISOU 1909 C ASP A1060 17197 16001 21130 1718 -931 614 C ATOM 1910 O ASP A1060 -14.336 -52.928 17.109 1.00147.27 O ANISOU 1910 O ASP A1060 17785 16555 21616 1658 -930 609 O ATOM 1911 CB ASP A1060 -17.167 -52.665 15.817 1.00140.34 C ANISOU 1911 CB ASP A1060 16935 15619 20769 1810 -1092 828 C ATOM 1912 CG ASP A1060 -16.298 -53.485 14.872 1.00142.95 C ANISOU 1912 CG ASP A1060 17369 15921 21025 1758 -1118 871 C ATOM 1913 OD1 ASP A1060 -15.217 -52.997 14.475 1.00142.81 O ANISOU 1913 OD1 ASP A1060 17431 15815 21014 1727 -1037 830 O ATOM 1914 OD2 ASP A1060 -16.691 -54.623 14.536 1.00148.41 O ANISOU 1914 OD2 ASP A1060 18061 16678 21649 1748 -1218 945 O ATOM 1915 N PHE A1061 -15.148 -50.976 17.886 1.00133.09 N ANISOU 1915 N PHE A1061 15932 14683 19953 1738 -839 537 N ATOM 1916 CA PHE A1061 -13.816 -50.435 18.125 1.00132.32 C ANISOU 1916 CA PHE A1061 15864 14533 19877 1684 -737 438 C ATOM 1917 C PHE A1061 -13.243 -50.911 19.456 1.00128.72 C ANISOU 1917 C PHE A1061 15301 14202 19404 1632 -713 333 C ATOM 1918 O PHE A1061 -12.053 -51.234 19.542 1.00130.81 O ANISOU 1918 O PHE A1061 15584 14476 19643 1565 -674 279 O ATOM 1919 CB PHE A1061 -13.855 -48.907 18.098 1.00129.17 C ANISOU 1919 CB PHE A1061 15500 14012 19568 1723 -649 396 C ATOM 1920 CG PHE A1061 -13.816 -48.310 16.713 1.00120.27 C ANISOU 1920 CG PHE A1061 14506 12734 18457 1750 -636 472 C ATOM 1921 CD1 PHE A1061 -13.011 -48.846 15.716 1.00112.58 C ANISOU 1921 CD1 PHE A1061 13629 11713 17431 1707 -644 519 C ATOM 1922 CD2 PHE A1061 -14.585 -47.200 16.413 1.00112.51 C ANISOU 1922 CD2 PHE A1061 13554 11654 17541 1821 -614 498 C ATOM 1923 CE1 PHE A1061 -12.982 -48.286 14.450 1.00104.72 C ANISOU 1923 CE1 PHE A1061 12761 10578 16449 1735 -629 590 C ATOM 1924 CE2 PHE A1061 -14.561 -46.637 15.152 1.00105.09 C ANISOU 1924 CE2 PHE A1061 12740 10575 16615 1848 -602 568 C ATOM 1925 CZ PHE A1061 -13.759 -47.180 14.169 1.00102.52 C ANISOU 1925 CZ PHE A1061 12512 10205 16236 1804 -609 615 C ATOM 1926 N ARG A1062 -14.066 -50.943 20.507 1.00120.25 N ANISOU 1926 N ARG A1062 14117 13224 18347 1664 -734 303 N ATOM 1927 CA ARG A1062 -13.584 -51.397 21.807 1.00117.64 C ANISOU 1927 CA ARG A1062 13685 13014 17997 1620 -714 205 C ATOM 1928 C ARG A1062 -13.349 -52.903 21.813 1.00106.34 C ANISOU 1928 C ARG A1062 12230 11697 16477 1572 -789 241 C ATOM 1929 O ARG A1062 -12.514 -53.397 22.580 1.00 98.19 O ANISOU 1929 O ARG A1062 11150 10743 15414 1516 -766 163 O ATOM 1930 CB ARG A1062 -14.582 -51.002 22.895 1.00127.54 C ANISOU 1930 CB ARG A1062 14832 14336 19291 1674 -714 169 C ATOM 1931 CG ARG A1062 -14.033 -51.095 24.312 1.00131.62 C ANISOU 1931 CG ARG A1062 15253 14951 19804 1638 -669 47 C ATOM 1932 CD ARG A1062 -13.496 -49.756 24.797 1.00133.13 C ANISOU 1932 CD ARG A1062 15454 15058 20069 1640 -564 -60 C ATOM 1933 NE ARG A1062 -13.128 -49.800 26.207 1.00138.75 N ANISOU 1933 NE ARG A1062 16071 15866 20779 1616 -528 -176 N ATOM 1934 CZ ARG A1062 -13.984 -49.674 27.212 1.00136.43 C ANISOU 1934 CZ ARG A1062 15686 15652 20501 1664 -534 -204 C ATOM 1935 NH1 ARG A1062 -15.278 -49.494 27.001 1.00132.93 N ANISOU 1935 NH1 ARG A1062 15223 15206 20078 1738 -575 -126 N ATOM 1936 NH2 ARG A1062 -13.532 -49.734 28.461 1.00134.15 N ANISOU 1936 NH2 ARG A1062 15320 15446 20204 1637 -500 -313 N ATOM 1937 N HIS A1063 -14.079 -53.645 20.971 1.00100.77 N ANISOU 1937 N HIS A1063 11558 11000 15728 1595 -882 359 N ATOM 1938 CA HIS A1063 -13.766 -55.055 20.757 1.00 92.10 C ANISOU 1938 CA HIS A1063 10464 9986 14542 1547 -953 402 C ATOM 1939 C HIS A1063 -12.418 -55.218 20.066 1.00 83.59 C ANISOU 1939 C HIS A1063 9481 8845 13433 1489 -912 386 C ATOM 1940 O HIS A1063 -11.748 -56.239 20.251 1.00 78.69 O ANISOU 1940 O HIS A1063 8849 8302 12747 1436 -935 373 O ATOM 1941 CB HIS A1063 -14.871 -55.733 19.935 1.00 89.60 C ANISOU 1941 CB HIS A1063 10174 9680 14191 1586 -1063 534 C ATOM 1942 CG HIS A1063 -14.622 -57.188 19.656 1.00 84.00 C ANISOU 1942 CG HIS A1063 9476 9049 13389 1540 -1143 586 C ATOM 1943 ND1 HIS A1063 -14.473 -58.125 20.657 1.00 84.53 N ANISOU 1943 ND1 HIS A1063 9451 9255 13411 1503 -1168 543 N ATOM 1944 CD2 HIS A1063 -14.507 -57.867 18.488 1.00 84.17 C ANISOU 1944 CD2 HIS A1063 9596 9029 13354 1529 -1204 676 C ATOM 1945 CE1 HIS A1063 -14.270 -59.315 20.118 1.00 74.85 C ANISOU 1945 CE1 HIS A1063 8265 8068 12107 1469 -1240 605 C ATOM 1946 NE2 HIS A1063 -14.286 -59.187 18.804 1.00 72.57 N ANISOU 1946 NE2 HIS A1063 8093 7672 11809 1484 -1264 686 N ATOM 1947 N GLY A1064 -12.006 -54.227 19.273 1.00 78.59 N ANISOU 1947 N GLY A1064 8941 8072 12846 1500 -849 388 N ATOM 1948 CA GLY A1064 -10.693 -54.289 18.652 1.00 68.68 C ANISOU 1948 CA GLY A1064 7773 6754 11570 1445 -798 369 C ATOM 1949 C GLY A1064 -9.569 -54.093 19.651 1.00 67.59 C ANISOU 1949 C GLY A1064 7577 6656 11448 1388 -717 242 C ATOM 1950 O GLY A1064 -8.511 -54.720 19.539 1.00 67.34 O ANISOU 1950 O GLY A1064 7568 6648 11370 1330 -703 219 O ATOM 1951 N PHE A1065 -9.777 -53.221 20.638 1.00 62.01 N ANISOU 1951 N PHE A1065 6796 5958 10807 1405 -664 156 N ATOM 1952 CA PHE A1065 -8.778 -53.041 21.684 1.00 70.60 C ANISOU 1952 CA PHE A1065 7822 7093 11910 1352 -595 30 C ATOM 1953 C PHE A1065 -8.784 -54.196 22.676 1.00 73.68 C ANISOU 1953 C PHE A1065 8113 7645 12237 1324 -647 -1 C ATOM 1954 O PHE A1065 -7.748 -54.490 23.282 1.00 71.68 O ANISOU 1954 O PHE A1065 7827 7443 11965 1266 -610 -83 O ATOM 1955 CB PHE A1065 -9.007 -51.716 22.413 1.00 67.45 C ANISOU 1955 CB PHE A1065 7384 6645 11598 1381 -523 -53 C ATOM 1956 CG PHE A1065 -8.483 -50.520 21.670 1.00 75.55 C ANISOU 1956 CG PHE A1065 8504 7512 12690 1382 -442 -64 C ATOM 1957 CD1 PHE A1065 -7.135 -50.205 21.708 1.00 67.92 C ANISOU 1957 CD1 PHE A1065 7563 6501 11741 1318 -365 -140 C ATOM 1958 CD2 PHE A1065 -9.335 -49.712 20.936 1.00 73.99 C ANISOU 1958 CD2 PHE A1065 8365 7210 12538 1446 -443 3 C ATOM 1959 CE1 PHE A1065 -6.646 -49.108 21.026 1.00 70.50 C ANISOU 1959 CE1 PHE A1065 7976 6681 12131 1316 -289 -148 C ATOM 1960 CE2 PHE A1065 -8.852 -48.613 20.251 1.00 66.41 C ANISOU 1960 CE2 PHE A1065 7495 6102 11638 1447 -367 -6 C ATOM 1961 CZ PHE A1065 -7.506 -48.311 20.297 1.00 74.76 C ANISOU 1961 CZ PHE A1065 8578 7114 12712 1381 -289 -81 C ATOM 1962 N ASP A1066 -9.932 -54.854 22.860 1.00 79.93 N ANISOU 1962 N ASP A1066 8854 8518 12997 1363 -731 63 N ATOM 1963 CA ASP A1066 -9.958 -56.077 23.654 1.00 74.71 C ANISOU 1963 CA ASP A1066 8111 8008 12267 1336 -788 51 C ATOM 1964 C ASP A1066 -9.103 -57.158 23.008 1.00 63.65 C ANISOU 1964 C ASP A1066 6768 6628 10790 1282 -820 88 C ATOM 1965 O ASP A1066 -8.366 -57.875 23.695 1.00 70.85 O ANISOU 1965 O ASP A1066 7631 7631 11657 1233 -817 30 O ATOM 1966 CB ASP A1066 -11.397 -56.567 23.823 1.00 85.12 C ANISOU 1966 CB ASP A1066 9374 9398 13569 1388 -874 128 C ATOM 1967 CG ASP A1066 -12.228 -55.652 24.699 1.00 91.77 C ANISOU 1967 CG ASP A1066 10138 10250 14478 1442 -842 81 C ATOM 1968 OD1 ASP A1066 -11.702 -54.610 25.141 1.00100.15 O ANISOU 1968 OD1 ASP A1066 11198 11256 15599 1438 -755 -11 O ATOM 1969 OD2 ASP A1066 -13.407 -55.979 24.947 1.00 90.75 O ANISOU 1969 OD2 ASP A1066 9952 10185 14344 1486 -904 137 O ATOM 1970 N ILE A1067 -9.188 -57.288 21.683 1.00 57.45 N ANISOU 1970 N ILE A1067 6088 5755 9986 1293 -851 186 N ATOM 1971 CA ILE A1067 -8.363 -58.260 20.975 1.00 57.48 C ANISOU 1971 CA ILE A1067 6158 5765 9916 1248 -877 226 C ATOM 1972 C ILE A1067 -6.894 -57.866 21.051 1.00 60.59 C ANISOU 1972 C ILE A1067 6579 6117 10327 1193 -784 140 C ATOM 1973 O ILE A1067 -6.017 -58.719 21.234 1.00 57.86 O ANISOU 1973 O ILE A1067 6224 5835 9923 1143 -787 114 O ATOM 1974 CB ILE A1067 -8.835 -58.392 19.514 1.00 59.61 C ANISOU 1974 CB ILE A1067 6543 5942 10164 1279 -928 350 C ATOM 1975 CG1 ILE A1067 -10.270 -58.920 19.456 1.00 62.65 C ANISOU 1975 CG1 ILE A1067 6895 6381 10528 1327 -1031 438 C ATOM 1976 CG2 ILE A1067 -7.897 -59.310 18.734 1.00 53.94 C ANISOU 1976 CG2 ILE A1067 5906 5219 9371 1235 -944 387 C ATOM 1977 CD1 ILE A1067 -10.967 -58.657 18.134 1.00 59.00 C ANISOU 1977 CD1 ILE A1067 6535 5811 10071 1373 -1075 551 C ATOM 1978 N LEU A1068 -6.601 -56.571 20.919 1.00 64.18 N ANISOU 1978 N LEU A1068 7063 6462 10860 1202 -699 94 N ATOM 1979 CA LEU A1068 -5.212 -56.127 20.872 1.00 58.02 C ANISOU 1979 CA LEU A1068 6314 5628 10104 1148 -610 21 C ATOM 1980 C LEU A1068 -4.511 -56.367 22.203 1.00 54.26 C ANISOU 1980 C LEU A1068 5734 5259 9623 1102 -580 -96 C ATOM 1981 O LEU A1068 -3.411 -56.930 22.243 1.00 58.35 O ANISOU 1981 O LEU A1068 6256 5810 10104 1047 -560 -130 O ATOM 1982 CB LEU A1068 -5.150 -54.648 20.494 1.00 62.30 C ANISOU 1982 CB LEU A1068 6906 6028 10736 1169 -528 -2 C ATOM 1983 CG LEU A1068 -3.788 -54.164 19.994 1.00 56.00 C ANISOU 1983 CG LEU A1068 6175 5140 9964 1119 -440 -41 C ATOM 1984 CD1 LEU A1068 -3.536 -54.660 18.577 1.00 57.62 C ANISOU 1984 CD1 LEU A1068 6497 5276 10119 1119 -463 65 C ATOM 1985 CD2 LEU A1068 -3.694 -52.651 20.063 1.00 63.57 C ANISOU 1985 CD2 LEU A1068 7150 5982 11022 1131 -353 -97 C ATOM 1986 N VAL A1069 -5.127 -55.938 23.305 1.00 58.59 N ANISOU 1986 N VAL A1069 6191 5863 10210 1125 -575 -160 N ATOM 1987 CA VAL A1069 -4.521 -56.142 24.618 1.00 58.17 C ANISOU 1987 CA VAL A1069 6040 5913 10151 1085 -550 -273 C ATOM 1988 C VAL A1069 -4.386 -57.632 24.908 1.00 56.93 C ANISOU 1988 C VAL A1069 5843 5888 9898 1059 -621 -249 C ATOM 1989 O VAL A1069 -3.326 -58.108 25.329 1.00 53.73 O ANISOU 1989 O VAL A1069 5414 5538 9463 1005 -599 -311 O ATOM 1990 CB VAL A1069 -5.341 -55.425 25.706 1.00 66.28 C ANISOU 1990 CB VAL A1069 6981 6973 11229 1125 -537 -335 C ATOM 1991 CG1 VAL A1069 -4.813 -55.773 27.091 1.00 59.96 C ANISOU 1991 CG1 VAL A1069 6079 6292 10409 1089 -524 -446 C ATOM 1992 CG2 VAL A1069 -5.311 -53.919 25.484 1.00 69.86 C ANISOU 1992 CG2 VAL A1069 7475 7292 11776 1146 -459 -372 C ATOM 1993 N GLY A1070 -5.460 -58.391 24.678 1.00 54.98 N ANISOU 1993 N GLY A1070 5590 5693 9605 1096 -709 -158 N ATOM 1994 CA GLY A1070 -5.393 -59.825 24.898 1.00 48.07 C ANISOU 1994 CA GLY A1070 4686 4938 8640 1072 -780 -128 C ATOM 1995 C GLY A1070 -4.297 -60.485 24.085 1.00 53.66 C ANISOU 1995 C GLY A1070 5471 5623 9296 1026 -776 -101 C ATOM 1996 O GLY A1070 -3.567 -61.342 24.587 1.00 55.61 O ANISOU 1996 O GLY A1070 5682 5960 9488 983 -786 -140 O ATOM 1997 N GLN A1071 -4.162 -60.091 22.817 1.00 52.94 N ANISOU 1997 N GLN A1071 5487 5408 9219 1036 -760 -34 N ATOM 1998 CA GLN A1071 -3.113 -60.660 21.980 1.00 50.56 C ANISOU 1998 CA GLN A1071 5266 5075 8869 997 -749 -5 C ATOM 1999 C GLN A1071 -1.726 -60.305 22.498 1.00 52.74 C ANISOU 1999 C GLN A1071 5516 5352 9172 942 -662 -112 C ATOM 2000 O GLN A1071 -0.799 -61.114 22.391 1.00 57.50 O ANISOU 2000 O GLN A1071 6131 5997 9718 901 -663 -119 O ATOM 2001 CB GLN A1071 -3.278 -60.186 20.537 1.00 53.54 C ANISOU 2001 CB GLN A1071 5767 5313 9263 1024 -742 86 C ATOM 2002 CG GLN A1071 -4.371 -60.917 19.775 1.00 58.49 C ANISOU 2002 CG GLN A1071 6443 5945 9836 1066 -843 209 C ATOM 2003 CD GLN A1071 -4.505 -60.438 18.344 1.00 55.86 C ANISOU 2003 CD GLN A1071 6237 5473 9516 1094 -837 297 C ATOM 2004 OE1 GLN A1071 -4.373 -59.247 18.061 1.00 63.82 O ANISOU 2004 OE1 GLN A1071 7278 6373 10597 1108 -765 275 O ATOM 2005 NE2 GLN A1071 -4.766 -61.367 17.432 1.00 55.19 N ANISOU 2005 NE2 GLN A1071 6228 5386 9356 1105 -912 398 N ATOM 2006 N ILE A1072 -1.560 -59.102 23.054 1.00 57.59 N ANISOU 2006 N ILE A1072 6094 5918 9871 940 -588 -197 N ATOM 2007 CA ILE A1072 -0.273 -58.726 23.632 1.00 55.97 C ANISOU 2007 CA ILE A1072 5853 5715 9696 885 -509 -306 C ATOM 2008 C ILE A1072 0.017 -59.563 24.871 1.00 56.08 C ANISOU 2008 C ILE A1072 5765 5881 9663 856 -537 -378 C ATOM 2009 O ILE A1072 1.164 -59.952 25.120 1.00 52.76 O ANISOU 2009 O ILE A1072 5328 5499 9220 805 -508 -432 O ATOM 2010 CB ILE A1072 -0.252 -57.220 23.946 1.00 54.39 C ANISOU 2010 CB ILE A1072 5642 5425 9600 892 -429 -379 C ATOM 2011 CG1 ILE A1072 -0.193 -56.415 22.646 1.00 58.17 C ANISOU 2011 CG1 ILE A1072 6233 5746 10122 908 -386 -314 C ATOM 2012 CG2 ILE A1072 0.928 -56.881 24.849 1.00 58.72 C ANISOU 2012 CG2 ILE A1072 6128 6003 10180 835 -361 -505 C ATOM 2013 CD1 ILE A1072 -0.493 -54.943 22.819 1.00 52.41 C ANISOU 2013 CD1 ILE A1072 5505 4917 9492 930 -322 -361 C ATOM 2014 N ASP A1073 -1.015 -59.851 25.667 1.00 55.46 N ANISOU 2014 N ASP A1073 5614 5890 9569 890 -593 -380 N ATOM 2015 CA ASP A1073 -0.827 -60.687 26.847 1.00 55.46 C ANISOU 2015 CA ASP A1073 5519 6035 9518 867 -623 -442 C ATOM 2016 C ASP A1073 -0.442 -62.109 26.456 1.00 60.85 C ANISOU 2016 C ASP A1073 6227 6789 10105 844 -682 -383 C ATOM 2017 O ASP A1073 0.342 -62.762 27.156 1.00 56.74 O ANISOU 2017 O ASP A1073 5656 6361 9543 805 -680 -443 O ATOM 2018 CB ASP A1073 -2.100 -60.692 27.695 1.00 59.18 C ANISOU 2018 CB ASP A1073 5914 6579 9993 913 -669 -443 C ATOM 2019 CG ASP A1073 -2.458 -59.315 28.222 1.00 64.71 C ANISOU 2019 CG ASP A1073 6583 7218 10784 939 -610 -511 C ATOM 2020 OD1 ASP A1073 -1.540 -58.489 28.418 1.00 66.98 O ANISOU 2020 OD1 ASP A1073 6874 7450 11125 907 -533 -596 O ATOM 2021 OD2 ASP A1073 -3.661 -59.060 28.445 1.00 65.30 O ANISOU 2021 OD2 ASP A1073 6631 7303 10877 992 -640 -479 O ATOM 2022 N ASP A1074 -0.987 -62.609 25.345 1.00 59.19 N ANISOU 2022 N ASP A1074 6098 6537 9856 868 -736 -265 N ATOM 2023 CA ASP A1074 -0.615 -63.939 24.875 1.00 54.15 C ANISOU 2023 CA ASP A1074 5497 5954 9124 848 -791 -205 C ATOM 2024 C ASP A1074 0.875 -64.004 24.563 1.00 59.47 C ANISOU 2024 C ASP A1074 6207 6600 9790 799 -730 -246 C ATOM 2025 O ASP A1074 1.578 -64.917 25.013 1.00 56.67 O ANISOU 2025 O ASP A1074 5819 6337 9375 765 -745 -276 O ATOM 2026 CB ASP A1074 -1.439 -64.309 23.640 1.00 51.88 C ANISOU 2026 CB ASP A1074 5303 5606 8804 885 -855 -73 C ATOM 2027 CG ASP A1074 -2.920 -64.426 23.940 1.00 57.08 C ANISOU 2027 CG ASP A1074 5919 6305 9463 931 -927 -23 C ATOM 2028 OD1 ASP A1074 -3.306 -64.263 25.117 1.00 66.58 O ANISOU 2028 OD1 ASP A1074 7021 7588 10688 937 -925 -90 O ATOM 2029 OD2 ASP A1074 -3.700 -64.678 22.997 1.00 52.77 O ANISOU 2029 OD2 ASP A1074 5441 5712 8896 963 -986 83 O ATOM 2030 N ALA A1075 1.375 -63.034 23.794 1.00 54.88 N ANISOU 2030 N ALA A1075 5692 5891 9269 794 -659 -245 N ATOM 2031 CA ALA A1075 2.791 -63.025 23.452 1.00 59.70 C ANISOU 2031 CA ALA A1075 6335 6468 9879 747 -595 -280 C ATOM 2032 C ALA A1075 3.657 -62.705 24.663 1.00 60.11 C ANISOU 2032 C ALA A1075 6290 6583 9965 704 -540 -411 C ATOM 2033 O ALA A1075 4.785 -63.202 24.766 1.00 57.88 O ANISOU 2033 O ALA A1075 5998 6340 9653 661 -516 -447 O ATOM 2034 CB ALA A1075 3.050 -62.017 22.333 1.00 64.27 C ANISOU 2034 CB ALA A1075 7010 6892 10519 753 -530 -244 C ATOM 2035 N LEU A1076 3.148 -61.889 25.588 1.00 57.49 N ANISOU 2035 N LEU A1076 5886 6263 9695 716 -522 -483 N ATOM 2036 CA LEU A1076 3.929 -61.517 26.763 1.00 60.40 C ANISOU 2036 CA LEU A1076 6165 6686 10098 677 -474 -612 C ATOM 2037 C LEU A1076 4.125 -62.708 27.694 1.00 62.54 C ANISOU 2037 C LEU A1076 6360 7110 10290 660 -527 -645 C ATOM 2038 O LEU A1076 5.188 -62.856 28.307 1.00 59.85 O ANISOU 2038 O LEU A1076 5973 6822 9947 615 -494 -728 O ATOM 2039 CB LEU A1076 3.240 -60.363 27.491 1.00 62.51 C ANISOU 2039 CB LEU A1076 6383 6923 10444 701 -446 -675 C ATOM 2040 CG LEU A1076 3.998 -59.695 28.639 1.00 66.01 C ANISOU 2040 CG LEU A1076 6745 7394 10939 664 -388 -813 C ATOM 2041 CD1 LEU A1076 5.325 -59.124 28.169 1.00 60.87 C ANISOU 2041 CD1 LEU A1076 6130 6660 10337 612 -309 -854 C ATOM 2042 CD2 LEU A1076 3.135 -58.606 29.254 1.00 72.90 C ANISOU 2042 CD2 LEU A1076 7583 8233 11882 700 -369 -860 C ATOM 2043 N LYS A1077 3.111 -63.568 27.811 1.00 64.46 N ANISOU 2043 N LYS A1077 6592 7428 10471 694 -609 -581 N ATOM 2044 CA LYS A1077 3.250 -64.765 28.633 1.00 65.72 C ANISOU 2044 CA LYS A1077 6689 7732 10550 680 -663 -602 C ATOM 2045 C LYS A1077 4.289 -65.713 28.048 1.00 73.06 C ANISOU 2045 C LYS A1077 7664 8681 11415 646 -668 -572 C ATOM 2046 O LYS A1077 5.082 -66.308 28.788 1.00 75.52 O ANISOU 2046 O LYS A1077 7920 9085 11688 614 -667 -636 O ATOM 2047 CB LYS A1077 1.896 -65.462 28.766 1.00 59.50 C ANISOU 2047 CB LYS A1077 5886 7008 9714 724 -750 -528 C ATOM 2048 CG LYS A1077 1.910 -66.716 29.634 1.00 71.85 C ANISOU 2048 CG LYS A1077 7386 8721 11194 713 -809 -543 C ATOM 2049 CD LYS A1077 1.598 -67.966 28.822 1.00 87.64 C ANISOU 2049 CD LYS A1077 9447 10745 13106 722 -885 -430 C ATOM 2050 CE LYS A1077 1.175 -69.124 29.716 1.00 87.60 C ANISOU 2050 CE LYS A1077 9375 10882 13025 724 -955 -430 C ATOM 2051 NZ LYS A1077 0.857 -70.350 28.930 1.00 95.34 N ANISOU 2051 NZ LYS A1077 10420 11884 13921 730 -1034 -320 N ATOM 2052 N LEU A1078 4.299 -65.869 26.722 1.00 65.24 N ANISOU 2052 N LEU A1078 6776 7603 10407 656 -674 -475 N ATOM 2053 CA LEU A1078 5.306 -66.711 26.085 1.00 64.01 C ANISOU 2053 CA LEU A1078 6673 7456 10191 628 -672 -443 C ATOM 2054 C LEU A1078 6.702 -66.136 26.278 1.00 60.03 C ANISOU 2054 C LEU A1078 6149 6926 9735 581 -584 -532 C ATOM 2055 O LEU A1078 7.670 -66.883 26.460 1.00 61.06 O ANISOU 2055 O LEU A1078 6263 7121 9818 549 -580 -557 O ATOM 2056 CB LEU A1078 4.994 -66.862 24.597 1.00 64.83 C ANISOU 2056 CB LEU A1078 6899 7460 10272 653 -691 -322 C ATOM 2057 CG LEU A1078 3.724 -67.642 24.259 1.00 57.75 C ANISOU 2057 CG LEU A1078 6034 6592 9315 695 -789 -223 C ATOM 2058 CD1 LEU A1078 3.317 -67.390 22.820 1.00 56.01 C ANISOU 2058 CD1 LEU A1078 5933 6249 9098 724 -796 -116 C ATOM 2059 CD2 LEU A1078 3.933 -69.127 24.503 1.00 51.52 C ANISOU 2059 CD2 LEU A1078 5235 5918 8424 683 -855 -199 C ATOM 2060 N ALA A1079 6.826 -64.808 26.238 1.00 64.05 N ANISOU 2060 N ALA A1079 6656 7339 10340 575 -514 -579 N ATOM 2061 CA ALA A1079 8.133 -64.183 26.408 1.00 62.31 C ANISOU 2061 CA ALA A1079 6415 7086 10175 526 -430 -663 C ATOM 2062 C ALA A1079 8.686 -64.428 27.807 1.00 65.84 C ANISOU 2062 C ALA A1079 6749 7652 10614 494 -430 -777 C ATOM 2063 O ALA A1079 9.880 -64.708 27.967 1.00 67.54 O ANISOU 2063 O ALA A1079 6941 7899 10820 452 -397 -824 O ATOM 2064 CB ALA A1079 8.035 -62.685 26.122 1.00 63.44 C ANISOU 2064 CB ALA A1079 6581 7100 10424 528 -359 -689 C ATOM 2065 N ASN A1080 7.836 -64.330 28.832 1.00 69.19 N ANISOU 2065 N ASN A1080 7103 8144 11042 516 -466 -821 N ATOM 2066 CA ASN A1080 8.303 -64.556 30.196 1.00 73.12 C ANISOU 2066 CA ASN A1080 7497 8756 11528 490 -469 -930 C ATOM 2067 C ASN A1080 8.676 -66.014 30.429 1.00 65.99 C ANISOU 2067 C ASN A1080 6575 7974 10523 481 -525 -909 C ATOM 2068 O ASN A1080 9.555 -66.304 31.247 1.00 73.02 O ANISOU 2068 O ASN A1080 7400 8944 11399 447 -513 -992 O ATOM 2069 CB ASN A1080 7.238 -64.110 31.197 1.00 74.18 C ANISOU 2069 CB ASN A1080 7566 8930 11686 522 -493 -974 C ATOM 2070 CG ASN A1080 7.052 -62.604 31.216 1.00 78.91 C ANISOU 2070 CG ASN A1080 8169 9421 12391 526 -430 -1023 C ATOM 2071 OD1 ASN A1080 7.905 -61.857 30.734 1.00 78.96 O ANISOU 2071 OD1 ASN A1080 8207 9336 12458 493 -363 -1050 O ATOM 2072 ND2 ASN A1080 5.938 -62.149 31.778 1.00 78.93 N ANISOU 2072 ND2 ASN A1080 8140 9433 12416 567 -450 -1034 N ATOM 2073 N GLU A1081 8.024 -66.942 29.728 1.00 69.25 N ANISOU 2073 N GLU A1081 7047 8401 10865 511 -588 -800 N ATOM 2074 CA GLU A1081 8.417 -68.343 29.807 1.00 63.97 C ANISOU 2074 CA GLU A1081 6375 7833 10096 502 -639 -771 C ATOM 2075 C GLU A1081 9.738 -68.607 29.098 1.00 68.02 C ANISOU 2075 C GLU A1081 6934 8315 10597 468 -595 -764 C ATOM 2076 O GLU A1081 10.414 -69.590 29.420 1.00 74.77 O ANISOU 2076 O GLU A1081 7765 9261 11384 451 -617 -778 O ATOM 2077 CB GLU A1081 7.325 -69.231 29.207 1.00 62.37 C ANISOU 2077 CB GLU A1081 6229 7646 9823 542 -721 -654 C ATOM 2078 CG GLU A1081 6.028 -69.246 29.997 1.00 67.63 C ANISOU 2078 CG GLU A1081 6840 8371 10486 576 -774 -655 C ATOM 2079 CD GLU A1081 4.940 -70.052 29.313 1.00 79.77 C ANISOU 2079 CD GLU A1081 8434 9911 11963 612 -855 -534 C ATOM 2080 OE1 GLU A1081 5.052 -70.288 28.091 1.00 73.70 O ANISOU 2080 OE1 GLU A1081 7762 9068 11173 617 -862 -448 O ATOM 2081 OE2 GLU A1081 3.974 -70.451 29.997 1.00 81.31 O ANISOU 2081 OE2 GLU A1081 8578 10183 12131 635 -911 -524 O ATOM 2082 N GLY A1082 10.119 -67.756 28.146 1.00 71.86 N ANISOU 2082 N GLY A1082 7484 8674 11145 460 -532 -740 N ATOM 2083 CA GLY A1082 11.350 -67.910 27.396 1.00 71.28 C ANISOU 2083 CA GLY A1082 7457 8560 11068 430 -482 -727 C ATOM 2084 C GLY A1082 11.163 -68.352 25.960 1.00 76.65 C ANISOU 2084 C GLY A1082 8257 9163 11704 455 -496 -603 C ATOM 2085 O GLY A1082 12.148 -68.389 25.211 1.00 84.23 O ANISOU 2085 O GLY A1082 9266 10073 12664 435 -446 -583 O ATOM 2086 N LYS A1083 9.941 -68.688 25.550 1.00 60.70 N ANISOU 2086 N LYS A1083 6286 7132 9646 498 -563 -518 N ATOM 2087 CA LYS A1083 9.661 -69.133 24.184 1.00 60.55 C ANISOU 2087 CA LYS A1083 6386 7039 9580 525 -587 -397 C ATOM 2088 C LYS A1083 9.678 -67.912 23.271 1.00 64.31 C ANISOU 2088 C LYS A1083 6930 7367 10140 530 -519 -372 C ATOM 2089 O LYS A1083 8.708 -67.155 23.209 1.00 63.93 O ANISOU 2089 O LYS A1083 6888 7261 10140 556 -527 -357 O ATOM 2090 CB LYS A1083 8.318 -69.853 24.122 1.00 69.60 C ANISOU 2090 CB LYS A1083 7554 8226 10665 566 -685 -319 C ATOM 2091 CG LYS A1083 8.196 -71.047 25.058 1.00 62.79 C ANISOU 2091 CG LYS A1083 6626 7509 9722 563 -755 -340 C ATOM 2092 CD LYS A1083 6.738 -71.333 25.391 1.00 70.08 C ANISOU 2092 CD LYS A1083 7531 8474 10624 597 -837 -297 C ATOM 2093 CE LYS A1083 6.582 -72.530 26.316 1.00 69.36 C ANISOU 2093 CE LYS A1083 7376 8525 10452 594 -905 -313 C ATOM 2094 NZ LYS A1083 6.663 -73.834 25.595 1.00102.35 N ANISOU 2094 NZ LYS A1083 11631 12728 14529 601 -966 -224 N ATOM 2095 N VAL A1084 10.784 -67.717 22.554 1.00 66.16 N ANISOU 2095 N VAL A1084 7212 7537 10388 507 -449 -366 N ATOM 2096 CA VAL A1084 10.946 -66.515 21.741 1.00 62.49 C ANISOU 2096 CA VAL A1084 6806 6930 10007 506 -373 -351 C ATOM 2097 C VAL A1084 10.125 -66.612 20.462 1.00 58.11 C ANISOU 2097 C VAL A1084 6373 6284 9421 552 -407 -228 C ATOM 2098 O VAL A1084 9.220 -65.806 20.221 1.00 59.92 O ANISOU 2098 O VAL A1084 6628 6439 9701 579 -411 -204 O ATOM 2099 CB VAL A1084 12.434 -66.275 21.429 1.00 67.69 C ANISOU 2099 CB VAL A1084 7471 7554 10696 463 -284 -386 C ATOM 2100 CG1 VAL A1084 12.605 -64.991 20.634 1.00 58.24 C ANISOU 2100 CG1 VAL A1084 6332 6208 9589 459 -201 -372 C ATOM 2101 CG2 VAL A1084 13.248 -66.225 22.711 1.00 76.99 C ANISOU 2101 CG2 VAL A1084 8525 8826 11901 417 -259 -508 C ATOM 2102 N LYS A1085 10.433 -67.604 19.622 1.00 67.16 N ANISOU 2102 N LYS A1085 7601 7435 10482 564 -434 -148 N ATOM 2103 CA LYS A1085 9.798 -67.690 18.310 1.00 64.25 C ANISOU 2103 CA LYS A1085 7361 6971 10082 606 -461 -30 C ATOM 2104 C LYS A1085 8.280 -67.755 18.429 1.00 53.78 C ANISOU 2104 C LYS A1085 6037 5656 8743 646 -549 14 C ATOM 2105 O LYS A1085 7.562 -67.163 17.615 1.00 58.26 O ANISOU 2105 O LYS A1085 6678 6120 9336 679 -553 79 O ATOM 2106 CB LYS A1085 10.335 -68.902 17.549 1.00 56.64 C ANISOU 2106 CB LYS A1085 6476 6029 9014 614 -488 42 C ATOM 2107 CG LYS A1085 11.810 -68.789 17.193 1.00 61.41 C ANISOU 2107 CG LYS A1085 7097 6605 9633 581 -395 16 C ATOM 2108 CD LYS A1085 12.018 -68.495 15.714 1.00 58.00 C ANISOU 2108 CD LYS A1085 6801 6041 9197 605 -351 108 C ATOM 2109 CE LYS A1085 13.449 -68.051 15.436 1.00 69.87 C ANISOU 2109 CE LYS A1085 8305 7500 10743 569 -240 72 C ATOM 2110 NZ LYS A1085 13.930 -68.471 14.087 1.00 70.94 N ANISOU 2110 NZ LYS A1085 8571 7561 10821 593 -214 168 N ATOM 2111 N GLU A1086 7.769 -68.463 19.438 1.00 58.46 N ANISOU 2111 N GLU A1086 6546 6370 9296 646 -619 -17 N ATOM 2112 CA GLU A1086 6.324 -68.488 19.643 1.00 64.33 C ANISOU 2112 CA GLU A1086 7277 7130 10036 682 -698 21 C ATOM 2113 C GLU A1086 5.800 -67.101 19.993 1.00 60.66 C ANISOU 2113 C GLU A1086 6769 6601 9676 690 -654 -26 C ATOM 2114 O GLU A1086 4.708 -66.715 19.560 1.00 58.88 O ANISOU 2114 O GLU A1086 6582 6319 9470 729 -690 33 O ATOM 2115 CB GLU A1086 5.957 -69.493 20.734 1.00 55.96 C ANISOU 2115 CB GLU A1086 6129 6218 8918 676 -773 -9 C ATOM 2116 CG GLU A1086 6.104 -70.936 20.301 1.00 75.38 C ANISOU 2116 CG GLU A1086 8644 8734 11264 680 -840 59 C ATOM 2117 CD GLU A1086 5.543 -71.910 21.314 1.00 83.54 C ANISOU 2117 CD GLU A1086 9597 9903 12240 679 -921 42 C ATOM 2118 OE1 GLU A1086 4.733 -71.483 22.166 1.00 77.76 O ANISOU 2118 OE1 GLU A1086 8783 9211 11551 687 -940 3 O ATOM 2119 OE2 GLU A1086 5.911 -73.102 21.257 1.00 78.91 O ANISOU 2119 OE2 GLU A1086 9033 9385 11565 672 -965 70 O ATOM 2120 N ALA A1087 6.563 -66.337 20.777 1.00 58.08 N ANISOU 2120 N ALA A1087 6365 6283 9420 654 -578 -133 N ATOM 2121 CA ALA A1087 6.171 -64.963 21.072 1.00 60.96 C ANISOU 2121 CA ALA A1087 6699 6577 9888 660 -527 -182 C ATOM 2122 C ALA A1087 6.188 -64.111 19.809 1.00 55.94 C ANISOU 2122 C ALA A1087 6171 5787 9297 678 -477 -119 C ATOM 2123 O ALA A1087 5.242 -63.363 19.540 1.00 50.41 O ANISOU 2123 O ALA A1087 5495 5016 8642 713 -485 -88 O ATOM 2124 CB ALA A1087 7.094 -64.371 22.139 1.00 57.27 C ANISOU 2124 CB ALA A1087 6132 6146 9480 613 -457 -310 C ATOM 2125 N GLN A1088 7.257 -64.216 19.015 1.00 57.64 N ANISOU 2125 N GLN A1088 6452 5948 9499 656 -422 -97 N ATOM 2126 CA GLN A1088 7.314 -63.484 17.754 1.00 57.18 C ANISOU 2126 CA GLN A1088 6507 5745 9476 674 -373 -30 C ATOM 2127 C GLN A1088 6.168 -63.887 16.835 1.00 57.91 C ANISOU 2127 C GLN A1088 6692 5797 9515 729 -452 87 C ATOM 2128 O GLN A1088 5.566 -63.037 16.169 1.00 62.43 O ANISOU 2128 O GLN A1088 7325 6260 10134 760 -437 132 O ATOM 2129 CB GLN A1088 8.661 -63.722 17.070 1.00 52.29 C ANISOU 2129 CB GLN A1088 5941 5089 8836 643 -306 -20 C ATOM 2130 CG GLN A1088 9.845 -63.098 17.795 1.00 62.55 C ANISOU 2130 CG GLN A1088 7159 6400 10207 587 -216 -130 C ATOM 2131 CD GLN A1088 11.180 -63.469 17.172 1.00 66.15 C ANISOU 2131 CD GLN A1088 7658 6838 10638 557 -155 -116 C ATOM 2132 OE1 GLN A1088 11.464 -64.643 16.935 1.00 59.00 O ANISOU 2132 OE1 GLN A1088 6778 5997 9640 562 -197 -74 O ATOM 2133 NE2 GLN A1088 12.007 -62.464 16.902 1.00 58.49 N ANISOU 2133 NE2 GLN A1088 6696 5777 9751 527 -54 -151 N ATOM 2134 N ALA A1089 5.849 -65.182 16.788 1.00 49.76 N ANISOU 2134 N ALA A1089 5672 4850 8385 741 -539 140 N ATOM 2135 CA ALA A1089 4.723 -65.629 15.975 1.00 52.43 C ANISOU 2135 CA ALA A1089 6092 5157 8670 791 -626 249 C ATOM 2136 C ALA A1089 3.415 -65.047 16.490 1.00 56.94 C ANISOU 2136 C ALA A1089 6610 5732 9291 821 -669 244 C ATOM 2137 O ALA A1089 2.554 -64.639 15.702 1.00 65.08 O ANISOU 2137 O ALA A1089 7713 6678 10336 863 -697 319 O ATOM 2138 CB ALA A1089 4.660 -67.157 15.960 1.00 49.38 C ANISOU 2138 CB ALA A1089 5720 4870 8172 792 -713 296 C ATOM 2139 N ALA A1090 3.247 -65.000 17.812 1.00 59.49 N ANISOU 2139 N ALA A1090 6808 6153 9641 804 -676 157 N ATOM 2140 CA ALA A1090 2.029 -64.435 18.379 1.00 56.38 C ANISOU 2140 CA ALA A1090 6357 5769 9296 835 -711 148 C ATOM 2141 C ALA A1090 1.966 -62.927 18.177 1.00 61.73 C ANISOU 2141 C ALA A1090 7049 6328 10076 846 -633 119 C ATOM 2142 O ALA A1090 0.871 -62.360 18.092 1.00 58.90 O ANISOU 2142 O ALA A1090 6694 5930 9756 888 -661 151 O ATOM 2143 CB ALA A1090 1.939 -64.773 19.866 1.00 52.93 C ANISOU 2143 CB ALA A1090 5786 5467 8856 814 -731 59 C ATOM 2144 N ALA A1091 3.123 -62.266 18.096 1.00 61.12 N ANISOU 2144 N ALA A1091 6982 6194 10048 810 -535 61 N ATOM 2145 CA ALA A1091 3.139 -60.818 17.925 1.00 66.68 C ANISOU 2145 CA ALA A1091 7701 6782 10852 816 -456 29 C ATOM 2146 C ALA A1091 2.722 -60.411 16.518 1.00 71.29 C ANISOU 2146 C ALA A1091 8414 7233 11440 856 -454 134 C ATOM 2147 O ALA A1091 2.168 -59.322 16.329 1.00 76.52 O ANISOU 2147 O ALA A1091 9096 7805 12174 884 -425 136 O ATOM 2148 CB ALA A1091 4.530 -60.268 18.240 1.00 61.09 C ANISOU 2148 CB ALA A1091 6965 6052 10195 760 -354 -61 C ATOM 2149 N GLU A1092 2.979 -61.263 15.522 1.00 64.86 N ANISOU 2149 N GLU A1092 7694 6403 10548 863 -485 220 N ATOM 2150 CA GLU A1092 2.605 -60.924 14.153 1.00 73.28 C ANISOU 2150 CA GLU A1092 8890 7343 11610 903 -487 321 C ATOM 2151 C GLU A1092 1.093 -60.942 13.962 1.00 73.40 C ANISOU 2151 C GLU A1092 8921 7353 11617 960 -577 391 C ATOM 2152 O GLU A1092 0.576 -60.254 13.074 1.00 74.49 O ANISOU 2152 O GLU A1092 9142 7377 11783 999 -570 454 O ATOM 2153 CB GLU A1092 3.280 -61.884 13.173 1.00 76.57 C ANISOU 2153 CB GLU A1092 9405 7749 11938 897 -499 393 C ATOM 2154 CG GLU A1092 4.762 -61.604 12.960 1.00 83.53 C ANISOU 2154 CG GLU A1092 10306 8590 12842 852 -393 350 C ATOM 2155 CD GLU A1092 5.011 -60.361 12.123 1.00 86.20 C ANISOU 2155 CD GLU A1092 10724 8775 13254 862 -305 368 C ATOM 2156 OE1 GLU A1092 4.368 -60.217 11.062 1.00 82.53 O ANISOU 2156 OE1 GLU A1092 10367 8220 12770 909 -332 463 O ATOM 2157 OE2 GLU A1092 5.846 -59.525 12.529 1.00 86.90 O ANISOU 2157 OE2 GLU A1092 10768 8831 13419 823 -209 289 O ATOM 2158 N GLN A1093 0.369 -61.711 14.780 1.00 61.67 N ANISOU 2158 N GLN A1093 7352 5987 10092 965 -661 382 N ATOM 2159 CA GLN A1093 -1.086 -61.719 14.688 1.00 67.19 C ANISOU 2159 CA GLN A1093 8050 6690 10790 1016 -747 445 C ATOM 2160 C GLN A1093 -1.684 -60.357 15.009 1.00 72.02 C ANISOU 2160 C GLN A1093 8626 7235 11503 1043 -702 408 C ATOM 2161 O GLN A1093 -2.821 -60.080 14.611 1.00 69.73 O ANISOU 2161 O GLN A1093 8364 6906 11226 1094 -754 473 O ATOM 2162 CB GLN A1093 -1.665 -62.778 15.628 1.00 61.53 C ANISOU 2162 CB GLN A1093 7238 6121 10020 1011 -835 433 C ATOM 2163 CG GLN A1093 -1.208 -64.195 15.315 1.00 67.40 C ANISOU 2163 CG GLN A1093 8020 6932 10658 990 -891 477 C ATOM 2164 CD GLN A1093 -1.644 -64.659 13.938 1.00 76.44 C ANISOU 2164 CD GLN A1093 9296 8003 11743 1024 -953 600 C ATOM 2165 OE1 GLN A1093 -2.731 -64.318 13.470 1.00 83.99 O ANISOU 2165 OE1 GLN A1093 10285 8909 12718 1069 -1003 665 O ATOM 2166 NE2 GLN A1093 -0.792 -65.436 13.279 1.00 68.98 N ANISOU 2166 NE2 GLN A1093 8430 7053 10727 1005 -951 633 N ATOM 2167 N LEU A1094 -0.944 -59.501 15.717 1.00 66.16 N ANISOU 2167 N LEU A1094 7826 6481 10833 1010 -608 304 N ATOM 2168 CA LEU A1094 -1.438 -58.161 16.006 1.00 64.70 C ANISOU 2168 CA LEU A1094 7615 6224 10744 1035 -559 265 C ATOM 2169 C LEU A1094 -1.685 -57.368 14.731 1.00 68.64 C ANISOU 2169 C LEU A1094 8236 6571 11274 1073 -533 342 C ATOM 2170 O LEU A1094 -2.542 -56.477 14.712 1.00 74.84 O ANISOU 2170 O LEU A1094 9020 7296 12118 1116 -531 353 O ATOM 2171 CB LEU A1094 -0.442 -57.426 16.900 1.00 66.38 C ANISOU 2171 CB LEU A1094 7757 6441 11023 987 -462 141 C ATOM 2172 CG LEU A1094 -0.256 -58.006 18.302 1.00 58.14 C ANISOU 2172 CG LEU A1094 6584 5543 9961 954 -481 50 C ATOM 2173 CD1 LEU A1094 1.018 -57.470 18.927 1.00 64.13 C ANISOU 2173 CD1 LEU A1094 7298 6299 10770 896 -386 -61 C ATOM 2174 CD2 LEU A1094 -1.458 -57.679 19.177 1.00 62.98 C ANISOU 2174 CD2 LEU A1094 7115 6208 10607 993 -522 27 C ATOM 2175 N LYS A1095 -0.952 -57.675 13.659 1.00 69.06 N ANISOU 2175 N LYS A1095 8395 6560 11286 1062 -512 399 N ATOM 2176 CA LYS A1095 -1.086 -56.904 12.427 1.00 77.18 C ANISOU 2176 CA LYS A1095 9546 7439 12341 1097 -479 471 C ATOM 2177 C LYS A1095 -2.489 -57.029 11.846 1.00 72.04 C ANISOU 2177 C LYS A1095 8940 6765 11667 1162 -573 569 C ATOM 2178 O LYS A1095 -3.045 -56.050 11.334 1.00 73.09 O ANISOU 2178 O LYS A1095 9123 6792 11855 1204 -552 601 O ATOM 2179 CB LYS A1095 -0.038 -57.358 11.413 1.00 83.65 C ANISOU 2179 CB LYS A1095 10469 8205 13107 1073 -444 517 C ATOM 2180 CG LYS A1095 1.387 -57.014 11.822 1.00 92.94 C ANISOU 2180 CG LYS A1095 11612 9377 14322 1011 -336 427 C ATOM 2181 CD LYS A1095 2.403 -57.538 10.821 1.00 98.51 C ANISOU 2181 CD LYS A1095 12418 10040 14972 992 -302 478 C ATOM 2182 CE LYS A1095 3.685 -56.720 10.857 1.00 99.41 C ANISOU 2182 CE LYS A1095 12529 10088 15154 943 -176 410 C ATOM 2183 NZ LYS A1095 4.730 -57.273 9.950 1.00109.75 N ANISOU 2183 NZ LYS A1095 13927 11366 16408 924 -137 457 N ATOM 2184 N THR A1096 -3.079 -58.223 11.911 1.00 66.65 N ANISOU 2184 N THR A1096 8239 6179 10904 1172 -679 619 N ATOM 2185 CA THR A1096 -4.451 -58.381 11.444 1.00 65.20 C ANISOU 2185 CA THR A1096 8085 5985 10703 1231 -776 710 C ATOM 2186 C THR A1096 -5.402 -57.517 12.263 1.00 66.96 C ANISOU 2186 C THR A1096 8217 6219 11005 1262 -776 668 C ATOM 2187 O THR A1096 -6.294 -56.863 11.709 1.00 66.56 O ANISOU 2187 O THR A1096 8212 6090 10990 1316 -796 725 O ATOM 2188 CB THR A1096 -4.865 -59.851 11.512 1.00 66.66 C ANISOU 2188 CB THR A1096 8253 6282 10792 1227 -889 761 C ATOM 2189 OG1 THR A1096 -3.927 -60.647 10.776 1.00 69.37 O ANISOU 2189 OG1 THR A1096 8684 6614 11060 1200 -884 795 O ATOM 2190 CG2 THR A1096 -6.255 -60.045 10.924 1.00 59.30 C ANISOU 2190 CG2 THR A1096 7358 5333 9840 1285 -994 862 C ATOM 2191 N THR A1097 -5.224 -57.498 13.585 1.00 65.64 N ANISOU 2191 N THR A1097 7923 6149 10867 1232 -752 569 N ATOM 2192 CA THR A1097 -6.039 -56.629 14.425 1.00 58.83 C ANISOU 2192 CA THR A1097 6975 5297 10082 1262 -740 520 C ATOM 2193 C THR A1097 -5.779 -55.165 14.104 1.00 64.09 C ANISOU 2193 C THR A1097 7688 5827 10836 1277 -642 491 C ATOM 2194 O THR A1097 -6.703 -54.342 14.109 1.00 65.55 O ANISOU 2194 O THR A1097 7866 5962 11077 1328 -647 506 O ATOM 2195 CB THR A1097 -5.751 -56.908 15.900 1.00 54.68 C ANISOU 2195 CB THR A1097 6314 4900 9564 1223 -726 414 C ATOM 2196 OG1 THR A1097 -5.803 -58.319 16.139 1.00 62.08 O ANISOU 2196 OG1 THR A1097 7217 5958 10413 1202 -808 441 O ATOM 2197 CG2 THR A1097 -6.767 -56.203 16.790 1.00 52.40 C ANISOU 2197 CG2 THR A1097 5933 4639 9339 1263 -731 376 C ATOM 2198 N ARG A1098 -4.522 -54.823 13.820 1.00 64.07 N ANISOU 2198 N ARG A1098 7733 5762 10849 1233 -553 449 N ATOM 2199 CA ARG A1098 -4.179 -53.447 13.483 1.00 64.86 C ANISOU 2199 CA ARG A1098 7884 5728 11033 1240 -456 421 C ATOM 2200 C ARG A1098 -4.919 -52.992 12.231 1.00 64.33 C ANISOU 2200 C ARG A1098 7932 5540 10971 1301 -480 528 C ATOM 2201 O ARG A1098 -5.504 -51.903 12.200 1.00 70.51 O ANISOU 2201 O ARG A1098 8723 6243 11824 1342 -450 525 O ATOM 2202 CB ARG A1098 -2.666 -53.336 13.293 1.00 66.09 C ANISOU 2202 CB ARG A1098 8074 5844 11195 1177 -364 372 C ATOM 2203 CG ARG A1098 -2.151 -51.939 13.002 1.00 65.24 C ANISOU 2203 CG ARG A1098 8014 5599 11177 1173 -255 335 C ATOM 2204 CD ARG A1098 -0.698 -51.990 12.559 1.00 70.63 C ANISOU 2204 CD ARG A1098 8747 6237 11853 1114 -174 314 C ATOM 2205 NE ARG A1098 -0.531 -52.807 11.362 1.00 72.83 N ANISOU 2205 NE ARG A1098 9133 6489 12051 1125 -211 418 N ATOM 2206 CZ ARG A1098 0.637 -53.105 10.811 1.00 73.29 C ANISOU 2206 CZ ARG A1098 9246 6518 12082 1084 -157 425 C ATOM 2207 NH1 ARG A1098 1.777 -52.673 11.326 1.00 75.24 N ANISOU 2207 NH1 ARG A1098 9449 6761 12379 1024 -64 335 N ATOM 2208 NH2 ARG A1098 0.662 -53.857 9.714 1.00 66.41 N ANISOU 2208 NH2 ARG A1098 8479 5623 11132 1103 -197 524 N ATOM 2209 N ASN A1099 -4.915 -53.825 11.188 1.00 68.89 N ANISOU 2209 N ASN A1099 8602 6102 11469 1310 -535 625 N ATOM 2210 CA ASN A1099 -5.543 -53.441 9.928 1.00 72.62 C ANISOU 2210 CA ASN A1099 9196 6458 11939 1368 -560 730 C ATOM 2211 C ASN A1099 -7.058 -53.354 10.065 1.00 75.69 C ANISOU 2211 C ASN A1099 9549 6871 12340 1432 -648 778 C ATOM 2212 O ASN A1099 -7.678 -52.402 9.575 1.00 85.75 O ANISOU 2212 O ASN A1099 10872 8044 13666 1483 -634 814 O ATOM 2213 CB ASN A1099 -5.169 -54.441 8.834 1.00 75.66 C ANISOU 2213 CB ASN A1099 9688 6830 12229 1362 -605 818 C ATOM 2214 CG ASN A1099 -3.672 -54.533 8.614 1.00 83.13 C ANISOU 2214 CG ASN A1099 10674 7749 13162 1304 -516 779 C ATOM 2215 OD1 ASN A1099 -2.886 -53.931 9.345 1.00 80.87 O ANISOU 2215 OD1 ASN A1099 10326 7465 12936 1261 -426 682 O ATOM 2216 ND2 ASN A1099 -3.269 -55.299 7.606 1.00 87.16 N ANISOU 2216 ND2 ASN A1099 11289 8235 13593 1303 -541 855 N ATOM 2217 N ALA A1100 -7.671 -54.333 10.730 1.00 65.69 N ANISOU 2217 N ALA A1100 8195 5737 11028 1429 -738 783 N ATOM 2218 CA ALA A1100 -9.126 -54.417 10.752 1.00 62.34 C ANISOU 2218 CA ALA A1100 7740 5342 10606 1489 -833 844 C ATOM 2219 C ALA A1100 -9.748 -53.382 11.683 1.00 67.11 C ANISOU 2219 C ALA A1100 8250 5948 11300 1518 -795 779 C ATOM 2220 O ALA A1100 -10.748 -52.750 11.326 1.00 81.42 O ANISOU 2220 O ALA A1100 10083 7702 13150 1580 -821 830 O ATOM 2221 CB ALA A1100 -9.559 -55.823 11.167 1.00 64.81 C ANISOU 2221 CB ALA A1100 7989 5796 10842 1474 -940 872 C ATOM 2222 N TYR A1101 -9.178 -53.195 12.872 1.00 73.35 N ANISOU 2222 N TYR A1101 8940 6806 12125 1476 -734 667 N ATOM 2223 CA TYR A1101 -9.785 -52.368 13.909 1.00 77.08 C ANISOU 2223 CA TYR A1101 9313 7303 12672 1502 -706 598 C ATOM 2224 C TYR A1101 -9.013 -51.088 14.193 1.00 67.46 C ANISOU 2224 C TYR A1101 8103 5993 11535 1485 -583 508 C ATOM 2225 O TYR A1101 -9.593 -49.998 14.164 1.00 64.92 O ANISOU 2225 O TYR A1101 7792 5593 11283 1533 -551 505 O ATOM 2226 CB TYR A1101 -9.918 -53.182 15.206 1.00 66.35 C ANISOU 2226 CB TYR A1101 7818 6105 11286 1474 -744 537 C ATOM 2227 CG TYR A1101 -10.813 -54.394 15.083 1.00 79.61 C ANISOU 2227 CG TYR A1101 9473 7882 12895 1491 -867 622 C ATOM 2228 CD1 TYR A1101 -12.177 -54.301 15.325 1.00 85.43 C ANISOU 2228 CD1 TYR A1101 10154 8653 13653 1550 -932 666 C ATOM 2229 CD2 TYR A1101 -10.294 -55.632 14.727 1.00 72.64 C ANISOU 2229 CD2 TYR A1101 8621 7055 11925 1450 -917 658 C ATOM 2230 CE1 TYR A1101 -12.999 -55.407 15.215 1.00 82.46 C ANISOU 2230 CE1 TYR A1101 9751 8364 13216 1562 -1046 744 C ATOM 2231 CE2 TYR A1101 -11.108 -56.742 14.615 1.00 67.18 C ANISOU 2231 CE2 TYR A1101 7909 6448 11169 1463 -1032 734 C ATOM 2232 CZ TYR A1101 -12.459 -56.624 14.859 1.00 82.46 C ANISOU 2232 CZ TYR A1101 9786 8415 13129 1517 -1096 777 C ATOM 2233 OH TYR A1101 -13.273 -57.728 14.748 1.00 84.57 O ANISOU 2233 OH TYR A1101 10030 8766 13338 1526 -1211 855 O ATOM 2234 N ILE A1102 -7.713 -51.191 14.470 1.00 65.49 N ANISOU 2234 N ILE A1102 7850 5752 11280 1417 -515 435 N ATOM 2235 CA ILE A1102 -6.972 -50.046 14.992 1.00 64.58 C ANISOU 2235 CA ILE A1102 7718 5572 11245 1392 -403 333 C ATOM 2236 C ILE A1102 -6.852 -48.951 13.938 1.00 70.41 C ANISOU 2236 C ILE A1102 8575 6142 12036 1419 -341 373 C ATOM 2237 O ILE A1102 -7.026 -47.764 14.238 1.00 71.71 O ANISOU 2237 O ILE A1102 8732 6233 12280 1441 -279 325 O ATOM 2238 CB ILE A1102 -5.591 -50.496 15.502 1.00 68.95 C ANISOU 2238 CB ILE A1102 8239 6180 11779 1310 -352 250 C ATOM 2239 CG1 ILE A1102 -5.733 -51.674 16.474 1.00 69.21 C ANISOU 2239 CG1 ILE A1102 8163 6381 11751 1286 -420 220 C ATOM 2240 CG2 ILE A1102 -4.870 -49.339 16.171 1.00 60.61 C ANISOU 2240 CG2 ILE A1102 7152 5069 10809 1279 -244 137 C ATOM 2241 CD1 ILE A1102 -6.710 -51.434 17.611 1.00 62.69 C ANISOU 2241 CD1 ILE A1102 7227 5634 10958 1321 -448 174 C ATOM 2242 N GLN A1103 -6.545 -49.323 12.694 1.00 75.77 N ANISOU 2242 N GLN A1103 9367 6755 12668 1419 -355 461 N ATOM 2243 CA GLN A1103 -6.446 -48.320 11.639 1.00 70.02 C ANISOU 2243 CA GLN A1103 8758 5864 11983 1447 -297 507 C ATOM 2244 C GLN A1103 -7.768 -47.593 11.441 1.00 69.21 C ANISOU 2244 C GLN A1103 8667 5707 11921 1529 -332 557 C ATOM 2245 O GLN A1103 -7.781 -46.425 11.036 1.00 64.68 O ANISOU 2245 O GLN A1103 8156 5006 11414 1556 -266 556 O ATOM 2246 CB GLN A1103 -5.997 -48.972 10.333 1.00 76.73 C ANISOU 2246 CB GLN A1103 9728 6662 12762 1441 -317 602 C ATOM 2247 CG GLN A1103 -5.647 -47.979 9.239 1.00 79.49 C ANISOU 2247 CG GLN A1103 10206 6844 13151 1460 -243 643 C ATOM 2248 CD GLN A1103 -4.977 -48.637 8.051 1.00 88.65 C ANISOU 2248 CD GLN A1103 11483 7959 14240 1444 -246 722 C ATOM 2249 OE1 GLN A1103 -5.179 -49.822 7.786 1.00 93.22 O ANISOU 2249 OE1 GLN A1103 12070 8617 14734 1445 -332 778 O ATOM 2250 NE2 GLN A1103 -4.165 -47.871 7.332 1.00 91.40 N ANISOU 2250 NE2 GLN A1103 11924 8179 14623 1430 -151 726 N ATOM 2251 N LYS A1104 -8.888 -48.263 11.720 1.00 66.08 N ANISOU 2251 N LYS A1104 8213 5406 11490 1569 -435 601 N ATOM 2252 CA LYS A1104 -10.185 -47.606 11.608 1.00 64.25 C ANISOU 2252 CA LYS A1104 7979 5133 11299 1649 -471 647 C ATOM 2253 C LYS A1104 -10.412 -46.646 12.768 1.00 64.15 C ANISOU 2253 C LYS A1104 7873 5132 11370 1660 -413 547 C ATOM 2254 O LYS A1104 -11.002 -45.575 12.586 1.00 63.45 O ANISOU 2254 O LYS A1104 7814 4952 11344 1716 -384 557 O ATOM 2255 CB LYS A1104 -11.298 -48.652 11.546 1.00 63.56 C ANISOU 2255 CB LYS A1104 7853 5147 11151 1685 -600 729 C ATOM 2256 N TYR A1105 -9.949 -47.005 13.969 1.00 71.87 N ANISOU 2256 N TYR A1105 8743 6220 12346 1611 -395 450 N ATOM 2257 CA TYR A1105 -10.071 -46.090 15.099 1.00 71.35 C ANISOU 2257 CA TYR A1105 8593 6163 12355 1619 -336 347 C ATOM 2258 C TYR A1105 -9.214 -44.847 14.891 1.00 69.15 C ANISOU 2258 C TYR A1105 8380 5747 12148 1598 -220 289 C ATOM 2259 O TYR A1105 -9.614 -43.739 15.270 1.00 65.57 O ANISOU 2259 O TYR A1105 7914 5231 11767 1635 -173 247 O ATOM 2260 CB TYR A1105 -9.686 -46.794 16.401 1.00 73.07 C ANISOU 2260 CB TYR A1105 8688 6528 12548 1567 -343 256 C ATOM 2261 CG TYR A1105 -9.467 -45.832 17.549 1.00 80.05 C ANISOU 2261 CG TYR A1105 9501 7410 13506 1559 -265 134 C ATOM 2262 CD1 TYR A1105 -10.540 -45.202 18.167 1.00 83.22 C ANISOU 2262 CD1 TYR A1105 9845 7821 13953 1625 -274 119 C ATOM 2263 CD2 TYR A1105 -8.188 -45.545 18.008 1.00 78.28 C ANISOU 2263 CD2 TYR A1105 9268 7171 13305 1488 -184 33 C ATOM 2264 CE1 TYR A1105 -10.346 -44.316 19.211 1.00 80.52 C ANISOU 2264 CE1 TYR A1105 9446 7474 13675 1621 -204 6 C ATOM 2265 CE2 TYR A1105 -7.984 -44.661 19.052 1.00 77.64 C ANISOU 2265 CE2 TYR A1105 9127 7084 13290 1480 -117 -81 C ATOM 2266 CZ TYR A1105 -9.066 -44.050 19.649 1.00 87.80 C ANISOU 2266 CZ TYR A1105 10365 8379 14618 1547 -127 -94 C ATOM 2267 OH TYR A1105 -8.871 -43.169 20.688 1.00 88.24 O ANISOU 2267 OH TYR A1105 10367 8426 14735 1542 -61 -209 O ATOM 2268 N LEU A1106 -8.029 -45.011 14.298 1.00 70.77 N ANISOU 2268 N LEU A1106 8653 5901 12334 1538 -172 286 N ATOM 2269 CA LEU A1106 -7.188 -43.858 13.996 1.00 75.19 C ANISOU 2269 CA LEU A1106 9281 6324 12963 1514 -63 240 C ATOM 2270 C LEU A1106 -7.885 -42.915 13.027 1.00 67.34 C ANISOU 2270 C LEU A1106 8388 5188 12009 1584 -51 316 C ATOM 2271 O LEU A1106 -7.988 -41.710 13.280 1.00 73.13 O ANISOU 2271 O LEU A1106 9131 5834 12822 1606 16 268 O ATOM 2272 CB LEU A1106 -5.849 -44.313 13.411 1.00 79.60 C ANISOU 2272 CB LEU A1106 9898 6857 13488 1441 -20 241 C ATOM 2273 CG LEU A1106 -4.925 -43.179 12.945 1.00 94.54 C ANISOU 2273 CG LEU A1106 11871 8602 15450 1412 94 208 C ATOM 2274 CD1 LEU A1106 -4.505 -42.318 14.128 1.00 90.84 C ANISOU 2274 CD1 LEU A1106 11322 8134 15059 1378 167 76 C ATOM 2275 CD2 LEU A1106 -3.704 -43.720 12.210 1.00 87.26 C ANISOU 2275 CD2 LEU A1106 11013 7655 14487 1350 129 231 C ATOM 2276 N GLU A 219 -8.361 -43.449 11.902 1.00 77.42 N ANISOU 2276 N GLU A 219 11425 8653 9337 1036 155 -552 N ATOM 2277 CA GLU A 219 -8.851 -42.590 10.834 1.00 73.68 C ANISOU 2277 CA GLU A 219 10996 8190 8808 1005 179 -559 C ATOM 2278 C GLU A 219 -10.134 -41.876 11.235 1.00 74.31 C ANISOU 2278 C GLU A 219 11016 8302 8916 875 105 -514 C ATOM 2279 O GLU A 219 -10.429 -40.790 10.716 1.00 75.72 O ANISOU 2279 O GLU A 219 11163 8528 9078 839 144 -507 O ATOM 2280 CB GLU A 219 -9.047 -43.424 9.569 1.00 83.09 C ANISOU 2280 CB GLU A 219 12390 9275 9905 1052 146 -601 C ATOM 2281 CG GLU A 219 -7.722 -43.815 8.904 1.00 96.29 C ANISOU 2281 CG GLU A 219 14117 10937 11533 1193 245 -651 C ATOM 2282 CD GLU A 219 -7.850 -44.977 7.931 1.00 94.51 C ANISOU 2282 CD GLU A 219 14098 10591 11222 1254 193 -695 C ATOM 2283 OE1 GLU A 219 -8.967 -45.511 7.777 1.00 85.96 O ANISOU 2283 OE1 GLU A 219 13118 9427 10115 1181 75 -686 O ATOM 2284 OE2 GLU A 219 -6.826 -45.356 7.325 1.00 90.78 O ANISOU 2284 OE2 GLU A 219 13683 10106 10703 1376 268 -738 O ATOM 2285 N ARG A 220 -10.900 -42.460 12.160 1.00 64.50 N ANISOU 2285 N ARG A 220 9756 7038 7715 805 -1 -480 N ATOM 2286 CA ARG A 220 -12.112 -41.809 12.641 1.00 62.36 C ANISOU 2286 CA ARG A 220 9415 6808 7470 686 -73 -433 C ATOM 2287 C ARG A 220 -11.790 -40.771 13.707 1.00 60.48 C ANISOU 2287 C ARG A 220 8981 6685 7312 661 -17 -404 C ATOM 2288 O ARG A 220 -12.372 -39.680 13.714 1.00 61.85 O ANISOU 2288 O ARG A 220 9084 6920 7494 598 -11 -381 O ATOM 2289 CB ARG A 220 -13.084 -42.852 13.195 1.00 55.60 C ANISOU 2289 CB ARG A 220 8616 5890 6620 618 -211 -404 C ATOM 2290 N ALA A 221 -10.869 -41.103 14.617 1.00 62.48 N ANISOU 2290 N ALA A 221 9149 6968 7623 712 21 -404 N ATOM 2291 CA ALA A 221 -10.410 -40.138 15.609 1.00 55.20 C ANISOU 2291 CA ALA A 221 8044 6154 6775 699 82 -381 C ATOM 2292 C ALA A 221 -9.781 -38.926 14.940 1.00 58.09 C ANISOU 2292 C ALA A 221 8365 6580 7128 730 195 -398 C ATOM 2293 O ALA A 221 -10.005 -37.789 15.367 1.00 57.03 O ANISOU 2293 O ALA A 221 8114 6524 7031 679 217 -374 O ATOM 2294 CB ALA A 221 -9.413 -40.800 16.566 1.00 60.15 C ANISOU 2294 CB ALA A 221 8601 6794 7457 760 110 -383 C ATOM 2295 N ARG A 222 -8.977 -39.152 13.896 1.00 59.26 N ANISOU 2295 N ARG A 222 8604 6692 7220 816 267 -439 N ATOM 2296 CA ARG A 222 -8.336 -38.045 13.193 1.00 54.24 C ANISOU 2296 CA ARG A 222 7931 6113 6566 846 376 -452 C ATOM 2297 C ARG A 222 -9.366 -37.192 12.463 1.00 62.44 C ANISOU 2297 C ARG A 222 9007 7152 7566 773 347 -441 C ATOM 2298 O ARG A 222 -9.256 -35.960 12.433 1.00 58.44 O ANISOU 2298 O ARG A 222 8412 6716 7077 748 404 -428 O ATOM 2299 CB ARG A 222 -7.297 -38.593 12.216 1.00 65.22 C ANISOU 2299 CB ARG A 222 9417 7465 7897 958 452 -496 C ATOM 2300 CG ARG A 222 -6.256 -37.587 11.755 1.00 73.56 C ANISOU 2300 CG ARG A 222 10403 8598 8949 1007 581 -504 C ATOM 2301 CD ARG A 222 -5.181 -38.269 10.920 1.00 77.21 C ANISOU 2301 CD ARG A 222 10952 9031 9354 1127 654 -545 C ATOM 2302 NE ARG A 222 -4.053 -38.714 11.730 1.00 94.16 N ANISOU 2302 NE ARG A 222 13015 11215 11548 1198 706 -547 N ATOM 2303 CZ ARG A 222 -3.223 -39.695 11.397 1.00 99.23 C ANISOU 2303 CZ ARG A 222 13730 11820 12153 1305 738 -580 C ATOM 2304 NH1 ARG A 222 -3.398 -40.407 10.295 1.00 98.61 N ANISOU 2304 NH1 ARG A 222 13817 11660 11990 1356 719 -616 N ATOM 2305 NH2 ARG A 222 -2.194 -39.972 12.193 1.00 96.07 N ANISOU 2305 NH2 ARG A 222 13236 11466 11800 1365 788 -577 N ATOM 2306 N SER A 223 -10.378 -37.830 11.873 1.00 68.29 N ANISOU 2306 N SER A 223 9881 7814 8253 737 256 -445 N ATOM 2307 CA SER A 223 -11.417 -37.079 11.179 1.00 57.87 C ANISOU 2307 CA SER A 223 8600 6494 6893 667 223 -433 C ATOM 2308 C SER A 223 -12.210 -36.214 12.150 1.00 58.37 C ANISOU 2308 C SER A 223 8533 6628 7016 575 179 -388 C ATOM 2309 O SER A 223 -12.604 -35.091 11.815 1.00 64.15 O ANISOU 2309 O SER A 223 9230 7405 7740 534 200 -377 O ATOM 2310 CB SER A 223 -12.345 -38.039 10.436 1.00 63.68 C ANISOU 2310 CB SER A 223 9503 7130 7562 644 125 -443 C ATOM 2311 OG SER A 223 -13.326 -37.330 9.701 1.00 83.25 O ANISOU 2311 OG SER A 223 12024 9610 9997 580 95 -432 O ATOM 2312 N THR A 224 -12.454 -36.718 13.361 1.00 54.80 N ANISOU 2312 N THR A 224 8010 6189 6621 544 117 -362 N ATOM 2313 CA THR A 224 -13.238 -35.958 14.328 1.00 53.62 C ANISOU 2313 CA THR A 224 7737 6111 6524 462 71 -320 C ATOM 2314 C THR A 224 -12.474 -34.732 14.816 1.00 51.17 C ANISOU 2314 C THR A 224 7283 5894 6267 477 164 -316 C ATOM 2315 O THR A 224 -13.060 -33.656 14.982 1.00 54.65 O ANISOU 2315 O THR A 224 7654 6390 6720 422 157 -295 O ATOM 2316 CB THR A 224 -13.626 -36.854 15.504 1.00 43.38 C ANISOU 2316 CB THR A 224 6400 4810 5274 429 -17 -292 C ATOM 2317 OG1 THR A 224 -14.358 -37.987 15.020 1.00 55.60 O ANISOU 2317 OG1 THR A 224 8089 6267 6771 408 -110 -293 O ATOM 2318 CG2 THR A 224 -14.484 -36.099 16.500 1.00 44.99 C ANISOU 2318 CG2 THR A 224 6477 5093 5525 348 -68 -248 C ATOM 2319 N LEU A 225 -11.168 -34.873 15.051 1.00 54.92 N ANISOU 2319 N LEU A 225 7710 6386 6770 551 249 -336 N ATOM 2320 CA LEU A 225 -10.372 -33.728 15.481 1.00 56.76 C ANISOU 2320 CA LEU A 225 7810 6705 7051 564 338 -331 C ATOM 2321 C LEU A 225 -10.309 -32.666 14.392 1.00 59.93 C ANISOU 2321 C LEU A 225 8242 7119 7409 564 400 -341 C ATOM 2322 O LEU A 225 -10.323 -31.464 14.684 1.00 58.45 O ANISOU 2322 O LEU A 225 7958 6997 7252 530 431 -325 O ATOM 2323 CB LEU A 225 -8.964 -34.181 15.867 1.00 55.97 C ANISOU 2323 CB LEU A 225 7661 6620 6984 645 416 -348 C ATOM 2324 CG LEU A 225 -8.830 -34.861 17.229 1.00 70.10 C ANISOU 2324 CG LEU A 225 9367 8428 8840 643 374 -330 C ATOM 2325 CD1 LEU A 225 -7.467 -35.523 17.372 1.00 66.41 C ANISOU 2325 CD1 LEU A 225 8887 7959 8388 735 446 -352 C ATOM 2326 CD2 LEU A 225 -9.055 -33.858 18.351 1.00 65.12 C ANISOU 2326 CD2 LEU A 225 8580 7885 8277 586 367 -299 C ATOM 2327 N GLN A 226 -10.238 -33.087 13.129 1.00 57.55 N ANISOU 2327 N GLN A 226 8078 6756 7034 601 418 -369 N ATOM 2328 CA GLN A 226 -10.196 -32.122 12.037 1.00 55.20 C ANISOU 2328 CA GLN A 226 7816 6469 6689 601 476 -377 C ATOM 2329 C GLN A 226 -11.519 -31.378 11.911 1.00 52.04 C ANISOU 2329 C GLN A 226 7421 6075 6275 515 407 -353 C ATOM 2330 O GLN A 226 -11.536 -30.182 11.599 1.00 49.82 O ANISOU 2330 O GLN A 226 7098 5837 5993 492 449 -345 O ATOM 2331 CB GLN A 226 -9.844 -32.829 10.729 1.00 53.83 C ANISOU 2331 CB GLN A 226 7791 6228 6436 665 507 -412 C ATOM 2332 CG GLN A 226 -8.378 -33.215 10.630 1.00 63.53 C ANISOU 2332 CG GLN A 226 9004 7469 7666 762 603 -436 C ATOM 2333 CD GLN A 226 -8.121 -34.273 9.575 1.00 90.27 C ANISOU 2333 CD GLN A 226 12545 10778 10975 835 609 -474 C ATOM 2334 OE1 GLN A 226 -8.990 -34.577 8.758 1.00 96.28 O ANISOU 2334 OE1 GLN A 226 13431 11476 11676 811 551 -484 O ATOM 2335 NE2 GLN A 226 -6.923 -34.846 9.594 1.00 86.90 N ANISOU 2335 NE2 GLN A 226 12113 10358 10549 927 678 -495 N ATOM 2336 N LYS A 227 -12.637 -32.065 12.155 1.00 51.96 N ANISOU 2336 N LYS A 227 7462 6026 6255 465 300 -340 N ATOM 2337 CA LYS A 227 -13.933 -31.398 12.103 1.00 50.68 C ANISOU 2337 CA LYS A 227 7299 5879 6080 385 230 -314 C ATOM 2338 C LYS A 227 -14.113 -30.435 13.269 1.00 48.20 C ANISOU 2338 C LYS A 227 6829 5649 5835 342 224 -284 C ATOM 2339 O LYS A 227 -14.828 -29.435 13.139 1.00 56.48 O ANISOU 2339 O LYS A 227 7852 6732 6877 294 207 -267 O ATOM 2340 CB LYS A 227 -15.054 -32.437 12.084 1.00 50.22 C ANISOU 2340 CB LYS A 227 7331 5762 5990 341 114 -303 C ATOM 2341 CG LYS A 227 -15.154 -33.183 10.764 1.00 56.05 C ANISOU 2341 CG LYS A 227 8239 6412 6645 370 105 -332 C ATOM 2342 CD LYS A 227 -15.988 -34.450 10.885 1.00 74.83 C ANISOU 2342 CD LYS A 227 10708 8724 9002 337 -7 -323 C ATOM 2343 CE LYS A 227 -16.148 -35.148 9.536 1.00 84.24 C ANISOU 2343 CE LYS A 227 12077 9825 10108 362 -23 -353 C ATOM 2344 NZ LYS A 227 -14.958 -34.979 8.649 1.00 85.27 N ANISOU 2344 NZ LYS A 227 12251 9943 10207 452 90 -395 N ATOM 2345 N GLU A 228 -13.478 -30.712 14.409 1.00 48.23 N ANISOU 2345 N GLU A 228 6730 5688 5905 361 237 -278 N ATOM 2346 CA GLU A 228 -13.501 -29.751 15.506 1.00 50.19 C ANISOU 2346 CA GLU A 228 6831 6020 6220 329 241 -254 C ATOM 2347 C GLU A 228 -12.622 -28.547 15.191 1.00 46.98 C ANISOU 2347 C GLU A 228 6368 5656 5825 354 342 -264 C ATOM 2348 O GLU A 228 -12.983 -27.408 15.507 1.00 46.84 O ANISOU 2348 O GLU A 228 6277 5690 5829 316 339 -248 O ATOM 2349 CB GLU A 228 -13.049 -30.416 16.806 1.00 51.41 C ANISOU 2349 CB GLU A 228 6894 6201 6440 343 226 -245 C ATOM 2350 CG GLU A 228 -14.043 -31.411 17.382 1.00 53.58 C ANISOU 2350 CG GLU A 228 7193 6452 6715 301 115 -222 C ATOM 2351 CD GLU A 228 -13.696 -31.818 18.802 1.00 58.13 C ANISOU 2351 CD GLU A 228 7655 7070 7362 304 98 -206 C ATOM 2352 OE1 GLU A 228 -13.968 -31.030 19.732 1.00 61.80 O ANISOU 2352 OE1 GLU A 228 7999 7609 7872 271 85 -183 O ATOM 2353 OE2 GLU A 228 -13.138 -32.921 18.989 1.00 61.23 O ANISOU 2353 OE2 GLU A 228 8080 7423 7763 344 97 -216 O ATOM 2354 N VAL A 229 -11.465 -28.779 14.567 1.00 49.45 N ANISOU 2354 N VAL A 229 6716 5950 6123 419 429 -289 N ATOM 2355 CA VAL A 229 -10.595 -27.670 14.186 1.00 49.97 C ANISOU 2355 CA VAL A 229 6734 6058 6196 439 525 -294 C ATOM 2356 C VAL A 229 -11.289 -26.777 13.167 1.00 46.36 C ANISOU 2356 C VAL A 229 6340 5590 5685 404 521 -291 C ATOM 2357 O VAL A 229 -11.243 -25.545 13.266 1.00 45.04 O ANISOU 2357 O VAL A 229 6105 5469 5539 377 549 -278 O ATOM 2358 CB VAL A 229 -9.255 -28.207 13.648 1.00 49.06 C ANISOU 2358 CB VAL A 229 6649 5928 6064 519 616 -318 C ATOM 2359 CG1 VAL A 229 -8.442 -27.082 13.024 1.00 49.28 C ANISOU 2359 CG1 VAL A 229 6646 5997 6083 534 712 -318 C ATOM 2360 CG2 VAL A 229 -8.471 -28.881 14.762 1.00 54.70 C ANISOU 2360 CG2 VAL A 229 7278 6668 6839 554 628 -317 C ATOM 2361 N HIS A 230 -11.943 -27.382 12.173 1.00 47.95 N ANISOU 2361 N HIS A 230 6674 5728 5817 402 484 -303 N ATOM 2362 CA HIS A 230 -12.639 -26.595 11.161 1.00 50.03 C ANISOU 2362 CA HIS A 230 7004 5978 6026 370 477 -300 C ATOM 2363 C HIS A 230 -13.787 -25.803 11.775 1.00 48.01 C ANISOU 2363 C HIS A 230 6690 5758 5793 299 404 -272 C ATOM 2364 O HIS A 230 -14.004 -24.637 11.425 1.00 48.54 O ANISOU 2364 O HIS A 230 6740 5852 5853 274 423 -263 O ATOM 2365 CB HIS A 230 -13.148 -27.512 10.050 1.00 55.10 C ANISOU 2365 CB HIS A 230 7801 6543 6589 382 443 -318 C ATOM 2366 CG HIS A 230 -13.813 -26.786 8.922 1.00 69.71 C ANISOU 2366 CG HIS A 230 9730 8379 8379 353 440 -316 C ATOM 2367 ND1 HIS A 230 -15.130 -26.998 8.574 1.00 69.33 N ANISOU 2367 ND1 HIS A 230 9757 8297 8288 303 349 -307 N ATOM 2368 CD2 HIS A 230 -13.343 -25.849 8.065 1.00 70.79 C ANISOU 2368 CD2 HIS A 230 9878 8531 8488 366 514 -320 C ATOM 2369 CE1 HIS A 230 -15.441 -26.225 7.548 1.00 67.69 C ANISOU 2369 CE1 HIS A 230 9606 8083 8030 289 370 -307 C ATOM 2370 NE2 HIS A 230 -14.375 -25.517 7.221 1.00 67.15 N ANISOU 2370 NE2 HIS A 230 9501 8043 7969 326 469 -315 N ATOM 2371 N ALA A 231 -14.531 -26.417 12.696 1.00 43.25 N ANISOU 2371 N ALA A 231 6056 5160 5217 268 319 -256 N ATOM 2372 CA ALA A 231 -15.621 -25.707 13.357 1.00 47.69 C ANISOU 2372 CA ALA A 231 6555 5767 5800 207 248 -228 C ATOM 2373 C ALA A 231 -15.094 -24.559 14.209 1.00 48.30 C ANISOU 2373 C ALA A 231 6497 5914 5939 205 291 -219 C ATOM 2374 O ALA A 231 -15.697 -23.480 14.250 1.00 45.23 O ANISOU 2374 O ALA A 231 6076 5559 5551 170 273 -205 O ATOM 2375 CB ALA A 231 -16.437 -26.676 14.212 1.00 47.68 C ANISOU 2375 CB ALA A 231 6541 5763 5814 177 151 -210 C ATOM 2376 N ALA A 232 -13.972 -24.774 14.901 1.00 46.20 N ANISOU 2376 N ALA A 232 6156 5671 5728 242 346 -227 N ATOM 2377 CA ALA A 232 -13.394 -23.710 15.712 1.00 43.11 C ANISOU 2377 CA ALA A 232 5639 5343 5396 240 387 -219 C ATOM 2378 C ALA A 232 -12.860 -22.577 14.845 1.00 47.46 C ANISOU 2378 C ALA A 232 6205 5899 5927 246 461 -225 C ATOM 2379 O ALA A 232 -12.863 -21.418 15.274 1.00 47.99 O ANISOU 2379 O ALA A 232 6197 6010 6026 223 469 -213 O ATOM 2380 CB ALA A 232 -12.285 -24.270 16.603 1.00 43.05 C ANISOU 2380 CB ALA A 232 5550 5359 5447 279 429 -224 C ATOM 2381 N LYS A 233 -12.402 -22.888 13.630 1.00 43.53 N ANISOU 2381 N LYS A 233 5807 5357 5377 277 514 -241 N ATOM 2382 CA LYS A 233 -11.985 -21.837 12.706 1.00 46.30 C ANISOU 2382 CA LYS A 233 6180 5711 5700 278 580 -242 C ATOM 2383 C LYS A 233 -13.174 -20.989 12.278 1.00 42.84 C ANISOU 2383 C LYS A 233 5780 5268 5228 228 525 -229 C ATOM 2384 O LYS A 233 -13.098 -19.755 12.267 1.00 42.94 O ANISOU 2384 O LYS A 233 5750 5311 5255 207 547 -219 O ATOM 2385 CB LYS A 233 -11.301 -22.446 11.483 1.00 50.30 C ANISOU 2385 CB LYS A 233 6788 6175 6149 326 644 -262 C ATOM 2386 CG LYS A 233 -9.844 -22.808 11.699 1.00 58.43 C ANISOU 2386 CG LYS A 233 7768 7226 7208 382 729 -271 C ATOM 2387 CD LYS A 233 -9.239 -23.392 10.431 1.00 67.59 C ANISOU 2387 CD LYS A 233 9032 8347 8300 435 790 -291 C ATOM 2388 CE LYS A 233 -7.887 -24.029 10.701 1.00 71.09 C ANISOU 2388 CE LYS A 233 9434 8811 8767 500 864 -302 C ATOM 2389 NZ LYS A 233 -6.953 -23.076 11.351 1.00 66.31 N ANISOU 2389 NZ LYS A 233 8700 8274 8220 494 925 -284 N ATOM 2390 N SER A 234 -14.283 -21.636 11.916 1.00 41.28 N ANISOU 2390 N SER A 234 5665 5034 4985 208 451 -229 N ATOM 2391 CA SER A 234 -15.478 -20.893 11.536 1.00 38.16 C ANISOU 2391 CA SER A 234 5304 4639 4555 162 394 -215 C ATOM 2392 C SER A 234 -15.918 -19.960 12.656 1.00 41.76 C ANISOU 2392 C SER A 234 5648 5154 5064 131 355 -196 C ATOM 2393 O SER A 234 -16.237 -18.790 12.411 1.00 39.97 O ANISOU 2393 O SER A 234 5412 4944 4830 109 356 -187 O ATOM 2394 CB SER A 234 -16.600 -21.863 11.165 1.00 39.03 C ANISOU 2394 CB SER A 234 5506 4708 4614 143 312 -213 C ATOM 2395 OG SER A 234 -16.213 -22.691 10.080 1.00 46.58 O ANISOU 2395 OG SER A 234 6576 5605 5516 175 345 -234 O ATOM 2396 N ALA A 235 -15.929 -20.456 13.896 1.00 39.47 N ANISOU 2396 N ALA A 235 5274 4896 4827 130 319 -190 N ATOM 2397 CA ALA A 235 -16.314 -19.615 15.024 1.00 36.99 C ANISOU 2397 CA ALA A 235 4850 4641 4562 107 281 -175 C ATOM 2398 C ALA A 235 -15.307 -18.494 15.248 1.00 35.15 C ANISOU 2398 C ALA A 235 4545 4438 4372 119 353 -178 C ATOM 2399 O ALA A 235 -15.684 -17.381 15.633 1.00 34.70 O ANISOU 2399 O ALA A 235 4438 4414 4331 98 332 -169 O ATOM 2400 CB ALA A 235 -16.455 -20.466 16.286 1.00 33.95 C ANISOU 2400 CB ALA A 235 4390 4287 4223 107 232 -167 C ATOM 2401 N ALA A 236 -14.020 -18.765 15.013 1.00 39.11 N ANISOU 2401 N ALA A 236 5043 4929 4890 153 436 -191 N ATOM 2402 CA ALA A 236 -13.000 -17.738 15.200 1.00 39.29 C ANISOU 2402 CA ALA A 236 4996 4981 4952 159 504 -189 C ATOM 2403 C ALA A 236 -13.081 -16.664 14.122 1.00 34.51 C ANISOU 2403 C ALA A 236 4450 4358 4306 143 533 -185 C ATOM 2404 O ALA A 236 -12.742 -15.504 14.379 1.00 31.72 O ANISOU 2404 O ALA A 236 4041 4030 3981 128 554 -177 O ATOM 2405 CB ALA A 236 -11.609 -18.374 15.210 1.00 40.64 C ANISOU 2405 CB ALA A 236 5143 5151 5145 201 584 -199 C ATOM 2406 N ILE A 237 -13.517 -17.028 12.915 1.00 36.37 N ANISOU 2406 N ILE A 237 4799 4547 4472 144 533 -190 N ATOM 2407 CA ILE A 237 -13.694 -16.035 11.861 1.00 34.37 C ANISOU 2407 CA ILE A 237 4607 4277 4175 127 555 -184 C ATOM 2408 C ILE A 237 -14.817 -15.070 12.220 1.00 34.03 C ANISOU 2408 C ILE A 237 4544 4251 4134 90 483 -171 C ATOM 2409 O ILE A 237 -14.708 -13.859 11.998 1.00 34.72 O ANISOU 2409 O ILE A 237 4622 4347 4225 73 501 -163 O ATOM 2410 CB ILE A 237 -13.958 -16.733 10.515 1.00 34.62 C ANISOU 2410 CB ILE A 237 4768 4257 4131 140 566 -194 C ATOM 2411 CG1 ILE A 237 -12.686 -17.425 10.019 1.00 29.75 C ANISOU 2411 CG1 ILE A 237 4170 3627 3506 185 652 -207 C ATOM 2412 CG2 ILE A 237 -14.468 -15.729 9.488 1.00 34.94 C ANISOU 2412 CG2 ILE A 237 4874 4281 4122 115 566 -185 C ATOM 2413 CD1 ILE A 237 -12.935 -18.445 8.930 1.00 37.16 C ANISOU 2413 CD1 ILE A 237 5232 4513 4373 209 652 -223 C ATOM 2414 N ILE A 238 -15.916 -15.592 12.772 1.00 33.82 N ANISOU 2414 N ILE A 238 4515 4232 4103 77 400 -168 N ATOM 2415 CA ILE A 238 -17.018 -14.735 13.203 1.00 32.48 C ANISOU 2415 CA ILE A 238 4319 4089 3932 49 328 -155 C ATOM 2416 C ILE A 238 -16.527 -13.724 14.232 1.00 34.05 C ANISOU 2416 C ILE A 238 4410 4332 4196 47 338 -152 C ATOM 2417 O ILE A 238 -16.784 -12.518 14.120 1.00 34.38 O ANISOU 2417 O ILE A 238 4448 4381 4235 33 329 -146 O ATOM 2418 CB ILE A 238 -18.169 -15.587 13.768 1.00 37.74 C ANISOU 2418 CB ILE A 238 4983 4770 4587 37 239 -148 C ATOM 2419 CG1 ILE A 238 -18.696 -16.568 12.714 1.00 40.81 C ANISOU 2419 CG1 ILE A 238 5487 5109 4909 33 222 -151 C ATOM 2420 CG2 ILE A 238 -19.284 -14.691 14.290 1.00 37.20 C ANISOU 2420 CG2 ILE A 238 4877 4742 4517 15 167 -134 C ATOM 2421 CD1 ILE A 238 -19.369 -15.922 11.532 1.00 45.14 C ANISOU 2421 CD1 ILE A 238 6127 5631 5394 16 213 -146 C ATOM 2422 N ALA A 239 -15.820 -14.205 15.258 1.00 37.07 N ANISOU 2422 N ALA A 239 4706 4743 4635 63 354 -157 N ATOM 2423 CA ALA A 239 -15.307 -13.308 16.289 1.00 34.33 C ANISOU 2423 CA ALA A 239 4256 4438 4351 62 361 -155 C ATOM 2424 C ALA A 239 -14.312 -12.312 15.706 1.00 29.72 C ANISOU 2424 C ALA A 239 3678 3841 3775 58 434 -154 C ATOM 2425 O ALA A 239 -14.297 -11.138 16.094 1.00 28.53 O ANISOU 2425 O ALA A 239 3484 3706 3648 44 424 -149 O ATOM 2426 CB ALA A 239 -14.658 -14.118 17.410 1.00 36.53 C ANISOU 2426 CB ALA A 239 4445 4747 4686 80 370 -159 C ATOM 2427 N GLY A 240 -13.474 -12.760 14.772 1.00 30.31 N ANISOU 2427 N GLY A 240 3804 3885 3826 72 507 -157 N ATOM 2428 CA GLY A 240 -12.521 -11.852 14.160 1.00 25.04 C ANISOU 2428 CA GLY A 240 3143 3211 3161 65 577 -149 C ATOM 2429 C GLY A 240 -13.196 -10.783 13.325 1.00 28.55 C ANISOU 2429 C GLY A 240 3654 3632 3563 39 557 -140 C ATOM 2430 O GLY A 240 -12.794 -9.616 13.352 1.00 30.09 O ANISOU 2430 O GLY A 240 3824 3832 3778 21 575 -130 O ATOM 2431 N LEU A 241 -14.235 -11.162 12.576 1.00 30.00 N ANISOU 2431 N LEU A 241 3926 3787 3687 36 517 -142 N ATOM 2432 CA LEU A 241 -14.963 -10.182 11.778 1.00 33.79 C ANISOU 2432 CA LEU A 241 4471 4245 4122 14 493 -133 C ATOM 2433 C LEU A 241 -15.702 -9.180 12.655 1.00 32.01 C ANISOU 2433 C LEU A 241 4193 4045 3924 -1 425 -128 C ATOM 2434 O LEU A 241 -15.929 -8.041 12.235 1.00 27.22 O ANISOU 2434 O LEU A 241 3615 3426 3303 -18 418 -119 O ATOM 2435 CB LEU A 241 -15.934 -10.891 10.838 1.00 29.85 C ANISOU 2435 CB LEU A 241 4074 3714 3552 15 461 -136 C ATOM 2436 CG LEU A 241 -15.262 -11.586 9.648 1.00 37.11 C ANISOU 2436 CG LEU A 241 5074 4600 4428 31 531 -141 C ATOM 2437 CD1 LEU A 241 -16.263 -12.409 8.864 1.00 36.35 C ANISOU 2437 CD1 LEU A 241 5075 4471 4264 31 488 -146 C ATOM 2438 CD2 LEU A 241 -14.588 -10.568 8.735 1.00 34.07 C ANISOU 2438 CD2 LEU A 241 4719 4201 4024 20 593 -128 C ATOM 2439 N PHE A 242 -16.086 -9.578 13.868 1.00 29.80 N ANISOU 2439 N PHE A 242 3838 3802 3682 7 374 -134 N ATOM 2440 CA PHE A 242 -16.667 -8.622 14.804 1.00 29.99 C ANISOU 2440 CA PHE A 242 3803 3858 3734 1 314 -132 C ATOM 2441 C PHE A 242 -15.649 -7.554 15.180 1.00 29.95 C ANISOU 2441 C PHE A 242 3744 3858 3779 -7 354 -130 C ATOM 2442 O PHE A 242 -15.956 -6.356 15.186 1.00 26.12 O ANISOU 2442 O PHE A 242 3265 3368 3292 -18 327 -125 O ATOM 2443 CB PHE A 242 -17.166 -9.353 16.050 1.00 30.66 C ANISOU 2443 CB PHE A 242 3812 3988 3850 14 258 -137 C ATOM 2444 CG PHE A 242 -17.792 -8.454 17.071 1.00 22.13 C ANISOU 2444 CG PHE A 242 2667 2948 2794 16 194 -137 C ATOM 2445 CD1 PHE A 242 -17.019 -7.852 18.048 1.00 30.49 C ANISOU 2445 CD1 PHE A 242 3639 4032 3915 21 208 -143 C ATOM 2446 CD2 PHE A 242 -19.153 -8.213 17.056 1.00 25.78 C ANISOU 2446 CD2 PHE A 242 3155 3426 3215 16 119 -131 C ATOM 2447 CE1 PHE A 242 -17.591 -7.021 18.991 1.00 32.27 C ANISOU 2447 CE1 PHE A 242 3809 4293 4159 28 147 -146 C ATOM 2448 CE2 PHE A 242 -19.735 -7.385 17.996 1.00 30.18 C ANISOU 2448 CE2 PHE A 242 3653 4024 3789 27 60 -133 C ATOM 2449 CZ PHE A 242 -18.953 -6.789 18.967 1.00 32.88 C ANISOU 2449 CZ PHE A 242 3913 4387 4192 34 74 -142 C ATOM 2450 N ALA A 243 -14.423 -7.977 15.493 1.00 32.39 N ANISOU 2450 N ALA A 243 4000 4176 4130 0 416 -132 N ATOM 2451 CA ALA A 243 -13.370 -7.024 15.827 1.00 35.01 C ANISOU 2451 CA ALA A 243 4279 4515 4509 -13 457 -126 C ATOM 2452 C ALA A 243 -13.076 -6.098 14.652 1.00 26.43 C ANISOU 2452 C ALA A 243 3264 3390 3388 -36 495 -111 C ATOM 2453 O ALA A 243 -13.006 -4.874 14.812 1.00 30.05 O ANISOU 2453 O ALA A 243 3712 3843 3863 -56 479 -103 O ATOM 2454 CB ALA A 243 -12.110 -7.778 16.252 1.00 28.71 C ANISOU 2454 CB ALA A 243 3416 3737 3754 -1 521 -127 C ATOM 2455 N LEU A 244 -12.903 -6.667 13.458 1.00 33.03 N ANISOU 2455 N LEU A 244 4176 4199 4174 -33 543 -106 N ATOM 2456 CA LEU A 244 -12.573 -5.858 12.289 1.00 33.95 C ANISOU 2456 CA LEU A 244 4360 4284 4256 -55 584 -89 C ATOM 2457 C LEU A 244 -13.651 -4.816 12.013 1.00 32.31 C ANISOU 2457 C LEU A 244 4203 4054 4018 -72 520 -84 C ATOM 2458 O LEU A 244 -13.345 -3.686 11.611 1.00 28.28 O ANISOU 2458 O LEU A 244 3713 3525 3507 -97 532 -68 O ATOM 2459 CB LEU A 244 -12.384 -6.762 11.071 1.00 37.82 C ANISOU 2459 CB LEU A 244 4929 4753 4690 -42 637 -88 C ATOM 2460 CG LEU A 244 -11.557 -6.189 9.921 1.00 50.03 C ANISOU 2460 CG LEU A 244 6522 6282 6207 -58 710 -68 C ATOM 2461 CD1 LEU A 244 -10.084 -6.153 10.296 1.00 48.19 C ANISOU 2461 CD1 LEU A 244 6211 6078 6021 -59 781 -56 C ATOM 2462 CD2 LEU A 244 -11.772 -7.000 8.652 1.00 56.09 C ANISOU 2462 CD2 LEU A 244 7385 7023 6903 -41 741 -71 C ATOM 2463 N CYS A 245 -14.919 -5.178 12.218 1.00 25.72 N ANISOU 2463 N CYS A 245 3391 3222 3157 -59 450 -96 N ATOM 2464 CA CYS A 245 -16.016 -4.269 11.906 1.00 26.58 C ANISOU 2464 CA CYS A 245 3553 3315 3231 -68 388 -91 C ATOM 2465 C CYS A 245 -16.186 -3.176 12.953 1.00 30.14 C ANISOU 2465 C CYS A 245 3943 3783 3726 -71 337 -94 C ATOM 2466 O CYS A 245 -16.609 -2.064 12.615 1.00 27.92 O ANISOU 2466 O CYS A 245 3703 3480 3426 -83 307 -86 O ATOM 2467 CB CYS A 245 -17.323 -5.051 11.769 1.00 30.06 C ANISOU 2467 CB CYS A 245 4034 3761 3625 -54 329 -99 C ATOM 2468 SG CYS A 245 -17.453 -6.034 10.259 1.00 37.20 S ANISOU 2468 SG CYS A 245 5047 4630 4458 -54 370 -96 S ATOM 2469 N TRP A 246 -15.873 -3.462 14.217 1.00 31.03 N ANISOU 2469 N TRP A 246 3961 3933 3894 -58 323 -105 N ATOM 2470 CA TRP A 246 -16.094 -2.504 15.292 1.00 33.03 C ANISOU 2470 CA TRP A 246 4157 4207 4187 -54 269 -112 C ATOM 2471 C TRP A 246 -14.854 -1.703 15.662 1.00 29.11 C ANISOU 2471 C TRP A 246 3613 3704 3744 -75 309 -105 C ATOM 2472 O TRP A 246 -14.991 -0.619 16.241 1.00 28.45 O ANISOU 2472 O TRP A 246 3510 3618 3683 -78 265 -108 O ATOM 2473 CB TRP A 246 -16.612 -3.223 16.544 1.00 30.52 C ANISOU 2473 CB TRP A 246 3760 3940 3895 -27 219 -127 C ATOM 2474 CG TRP A 246 -18.083 -3.489 16.500 1.00 27.75 C ANISOU 2474 CG TRP A 246 3442 3606 3497 -10 148 -129 C ATOM 2475 CD1 TRP A 246 -18.700 -4.653 16.144 1.00 25.46 C ANISOU 2475 CD1 TRP A 246 3180 3324 3170 -4 139 -128 C ATOM 2476 CD2 TRP A 246 -19.127 -2.563 16.820 1.00 26.18 C ANISOU 2476 CD2 TRP A 246 3250 3418 3277 3 73 -132 C ATOM 2477 NE1 TRP A 246 -20.063 -4.509 16.226 1.00 25.91 N ANISOU 2477 NE1 TRP A 246 3256 3402 3186 7 63 -125 N ATOM 2478 CE2 TRP A 246 -20.351 -3.235 16.638 1.00 25.01 C ANISOU 2478 CE2 TRP A 246 3129 3293 3080 16 24 -129 C ATOM 2479 CE3 TRP A 246 -19.144 -1.231 17.242 1.00 27.87 C ANISOU 2479 CE3 TRP A 246 3453 3626 3508 8 41 -137 C ATOM 2480 CZ2 TRP A 246 -21.579 -2.619 16.860 1.00 25.76 C ANISOU 2480 CZ2 TRP A 246 3234 3412 3141 35 -52 -128 C ATOM 2481 CZ3 TRP A 246 -20.362 -0.624 17.467 1.00 26.93 C ANISOU 2481 CZ3 TRP A 246 3350 3525 3355 32 -36 -140 C ATOM 2482 CH2 TRP A 246 -21.563 -1.315 17.272 1.00 20.91 C ANISOU 2482 CH2 TRP A 246 2609 2794 2544 47 -80 -135 C ATOM 2483 N LEU A 247 -13.659 -2.194 15.342 1.00 29.43 N ANISOU 2483 N LEU A 247 3635 3742 3804 -88 387 -96 N ATOM 2484 CA LEU A 247 -12.447 -1.505 15.775 1.00 33.43 C ANISOU 2484 CA LEU A 247 4086 4253 4364 -111 424 -86 C ATOM 2485 C LEU A 247 -12.309 -0.108 15.186 1.00 31.26 C ANISOU 2485 C LEU A 247 3861 3937 4077 -144 419 -68 C ATOM 2486 O LEU A 247 -11.914 0.807 15.930 1.00 32.57 O ANISOU 2486 O LEU A 247 3984 4103 4287 -159 395 -67 O ATOM 2487 CB LEU A 247 -11.218 -2.357 15.435 1.00 35.12 C ANISOU 2487 CB LEU A 247 4273 4478 4591 -115 513 -76 C ATOM 2488 CG LEU A 247 -10.812 -3.370 16.510 1.00 43.56 C ANISOU 2488 CG LEU A 247 5252 5592 5706 -90 522 -90 C ATOM 2489 CD1 LEU A 247 -9.776 -4.341 15.972 1.00 46.71 C ANISOU 2489 CD1 LEU A 247 5645 6001 6103 -83 609 -82 C ATOM 2490 CD2 LEU A 247 -10.281 -2.660 17.746 1.00 37.42 C ANISOU 2490 CD2 LEU A 247 4384 4839 4994 -101 500 -93 C ATOM 2491 N PRO A 248 -12.595 0.132 13.902 1.00 33.45 N ANISOU 2491 N PRO A 248 4232 4179 4300 -157 436 -53 N ATOM 2492 CA PRO A 248 -12.453 1.502 13.377 1.00 34.01 C ANISOU 2492 CA PRO A 248 4350 4209 4362 -192 427 -33 C ATOM 2493 C PRO A 248 -13.205 2.534 14.198 1.00 24.94 C ANISOU 2493 C PRO A 248 3195 3052 3231 -184 339 -46 C ATOM 2494 O PRO A 248 -12.647 3.583 14.537 1.00 29.78 O ANISOU 2494 O PRO A 248 3792 3646 3876 -211 328 -36 O ATOM 2495 CB PRO A 248 -13.003 1.380 11.948 1.00 30.36 C ANISOU 2495 CB PRO A 248 3991 3716 3829 -195 444 -21 C ATOM 2496 CG PRO A 248 -12.815 -0.048 11.592 1.00 27.49 C ANISOU 2496 CG PRO A 248 3624 3375 3446 -174 496 -28 C ATOM 2497 CD PRO A 248 -13.030 -0.815 12.862 1.00 28.87 C ANISOU 2497 CD PRO A 248 3718 3590 3661 -144 464 -53 C ATOM 2498 N LEU A 249 -14.462 2.256 14.540 1.00 26.76 N ANISOU 2498 N LEU A 249 3436 3295 3436 -148 275 -68 N ATOM 2499 CA LEU A 249 -15.233 3.204 15.336 1.00 34.00 C ANISOU 2499 CA LEU A 249 4346 4210 4362 -130 191 -83 C ATOM 2500 C LEU A 249 -14.591 3.416 16.703 1.00 30.03 C ANISOU 2500 C LEU A 249 3747 3735 3927 -127 176 -96 C ATOM 2501 O LEU A 249 -14.457 4.556 17.163 1.00 24.64 O ANISOU 2501 O LEU A 249 3063 3032 3268 -136 136 -98 O ATOM 2502 CB LEU A 249 -16.672 2.705 15.468 1.00 29.54 C ANISOU 2502 CB LEU A 249 3799 3671 3755 -89 130 -100 C ATOM 2503 CG LEU A 249 -17.759 3.706 15.858 1.00 29.89 C ANISOU 2503 CG LEU A 249 3867 3710 3779 -62 43 -111 C ATOM 2504 CD1 LEU A 249 -17.765 4.924 14.959 1.00 30.03 C ANISOU 2504 CD1 LEU A 249 3972 3668 3771 -86 36 -95 C ATOM 2505 CD2 LEU A 249 -19.108 3.006 15.807 1.00 31.53 C ANISOU 2505 CD2 LEU A 249 4091 3952 3938 -26 -3 -120 C ATOM 2506 N HIS A 250 -14.160 2.335 17.355 1.00 31.95 N ANISOU 2506 N HIS A 250 3914 4023 4202 -114 206 -105 N ATOM 2507 CA HIS A 250 -13.501 2.470 18.651 1.00 29.37 C ANISOU 2507 CA HIS A 250 3494 3727 3940 -112 196 -117 C ATOM 2508 C HIS A 250 -12.175 3.210 18.527 1.00 29.37 C ANISOU 2508 C HIS A 250 3479 3701 3977 -158 241 -96 C ATOM 2509 O HIS A 250 -11.831 4.028 19.389 1.00 24.63 O ANISOU 2509 O HIS A 250 2839 3099 3419 -166 207 -102 O ATOM 2510 CB HIS A 250 -13.280 1.093 19.271 1.00 31.67 C ANISOU 2510 CB HIS A 250 3710 4070 4254 -90 224 -127 C ATOM 2511 CG HIS A 250 -14.523 0.475 19.828 1.00 31.15 C ANISOU 2511 CG HIS A 250 3630 4041 4166 -48 163 -146 C ATOM 2512 ND1 HIS A 250 -15.217 1.026 20.884 1.00 26.55 N ANISOU 2512 ND1 HIS A 250 3008 3485 3596 -20 87 -165 N ATOM 2513 CD2 HIS A 250 -15.190 -0.651 19.486 1.00 34.02 C ANISOU 2513 CD2 HIS A 250 4010 4423 4494 -30 165 -147 C ATOM 2514 CE1 HIS A 250 -16.261 0.268 21.164 1.00 32.04 C ANISOU 2514 CE1 HIS A 250 3693 4219 4263 13 47 -174 C ATOM 2515 NE2 HIS A 250 -16.270 -0.755 20.329 1.00 31.17 N ANISOU 2515 NE2 HIS A 250 3616 4101 4124 4 91 -162 N ATOM 2516 N ILE A 251 -11.410 2.928 17.472 1.00 29.08 N ANISOU 2516 N ILE A 251 3475 3648 3925 -189 317 -70 N ATOM 2517 CA ILE A 251 -10.134 3.609 17.284 1.00 25.20 C ANISOU 2517 CA ILE A 251 2969 3141 3467 -238 363 -43 C ATOM 2518 C ILE A 251 -10.343 5.099 17.037 1.00 23.31 C ANISOU 2518 C ILE A 251 2789 2849 3220 -266 313 -32 C ATOM 2519 O ILE A 251 -9.541 5.926 17.482 1.00 27.75 O ANISOU 2519 O ILE A 251 3321 3399 3823 -302 308 -19 O ATOM 2520 CB ILE A 251 -9.346 2.941 16.141 1.00 31.84 C ANISOU 2520 CB ILE A 251 3832 3983 4283 -258 456 -15 C ATOM 2521 CG1 ILE A 251 -8.885 1.543 16.570 1.00 37.84 C ANISOU 2521 CG1 ILE A 251 4522 4793 5062 -230 505 -26 C ATOM 2522 CG2 ILE A 251 -8.159 3.797 15.740 1.00 33.32 C ANISOU 2522 CG2 ILE A 251 4017 4153 4489 -314 498 22 C ATOM 2523 CD1 ILE A 251 -8.362 0.684 15.427 1.00 41.72 C ANISOU 2523 CD1 ILE A 251 5047 5289 5516 -231 589 -9 C ATOM 2524 N ILE A 252 -11.419 5.472 16.338 1.00 25.21 N ANISOU 2524 N ILE A 252 3115 3056 3406 -253 273 -35 N ATOM 2525 CA ILE A 252 -11.705 6.890 16.133 1.00 27.99 C ANISOU 2525 CA ILE A 252 3531 3355 3749 -274 219 -27 C ATOM 2526 C ILE A 252 -11.986 7.576 17.463 1.00 24.35 C ANISOU 2526 C ILE A 252 3027 2898 3327 -252 140 -54 C ATOM 2527 O ILE A 252 -11.566 8.716 17.692 1.00 26.42 O ANISOU 2527 O ILE A 252 3303 3122 3613 -283 109 -45 O ATOM 2528 CB ILE A 252 -12.881 7.065 15.155 1.00 30.33 C ANISOU 2528 CB ILE A 252 3925 3621 3977 -255 190 -27 C ATOM 2529 CG1 ILE A 252 -12.464 6.662 13.741 1.00 27.91 C ANISOU 2529 CG1 ILE A 252 3673 3301 3632 -285 266 5 C ATOM 2530 CG2 ILE A 252 -13.372 8.507 15.179 1.00 33.10 C ANISOU 2530 CG2 ILE A 252 4337 3920 4320 -261 116 -26 C ATOM 2531 CD1 ILE A 252 -13.629 6.463 12.801 1.00 30.90 C ANISOU 2531 CD1 ILE A 252 4137 3663 3942 -261 247 1 C ATOM 2532 N ASN A 253 -12.711 6.904 18.357 1.00 27.44 N ANISOU 2532 N ASN A 253 3368 3334 3723 -200 104 -87 N ATOM 2533 CA ASN A 253 -12.999 7.509 19.652 1.00 30.30 C ANISOU 2533 CA ASN A 253 3686 3708 4118 -172 30 -115 C ATOM 2534 C ASN A 253 -11.729 7.718 20.461 1.00 25.42 C ANISOU 2534 C ASN A 253 2992 3099 3566 -206 52 -109 C ATOM 2535 O ASN A 253 -11.619 8.705 21.196 1.00 30.40 O ANISOU 2535 O ASN A 253 3617 3710 4224 -209 -4 -120 O ATOM 2536 CB ASN A 253 -13.999 6.647 20.420 1.00 30.72 C ANISOU 2536 CB ASN A 253 3693 3819 4159 -111 -7 -145 C ATOM 2537 CG ASN A 253 -15.380 6.680 19.801 1.00 26.81 C ANISOU 2537 CG ASN A 253 3270 3316 3598 -76 -50 -151 C ATOM 2538 OD1 ASN A 253 -15.715 7.603 19.059 1.00 28.34 O ANISOU 2538 OD1 ASN A 253 3549 3460 3761 -87 -74 -141 O ATOM 2539 ND2 ASN A 253 -16.193 5.680 20.108 1.00 25.37 N ANISOU 2539 ND2 ASN A 253 3056 3187 3396 -36 -63 -165 N ATOM 2540 N CYS A 254 -10.754 6.817 20.334 1.00 28.48 N ANISOU 2540 N CYS A 254 3325 3519 3979 -230 132 -93 N ATOM 2541 CA CYS A 254 -9.481 7.022 21.015 1.00 27.77 C ANISOU 2541 CA CYS A 254 3161 3440 3949 -267 158 -82 C ATOM 2542 C CYS A 254 -8.793 8.286 20.519 1.00 26.88 C ANISOU 2542 C CYS A 254 3098 3271 3845 -327 154 -51 C ATOM 2543 O CYS A 254 -8.251 9.060 21.316 1.00 30.80 O ANISOU 2543 O CYS A 254 3562 3756 4384 -350 119 -53 O ATOM 2544 CB CYS A 254 -8.582 5.802 20.820 1.00 31.15 C ANISOU 2544 CB CYS A 254 3529 3914 4394 -277 249 -66 C ATOM 2545 SG CYS A 254 -9.183 4.338 21.694 1.00 31.44 S ANISOU 2545 SG CYS A 254 3492 4018 4437 -213 245 -99 S ATOM 2546 N PHE A 255 -8.813 8.522 19.208 1.00 32.09 N ANISOU 2546 N PHE A 255 3837 3894 4463 -356 187 -22 N ATOM 2547 CA PHE A 255 -8.219 9.742 18.675 1.00 34.29 C ANISOU 2547 CA PHE A 255 4167 4116 4745 -417 179 12 C ATOM 2548 C PHE A 255 -8.949 10.975 19.196 1.00 29.91 C ANISOU 2548 C PHE A 255 3663 3512 4190 -404 77 -10 C ATOM 2549 O PHE A 255 -8.321 11.939 19.649 1.00 34.52 O ANISOU 2549 O PHE A 255 4242 4063 4809 -445 44 1 O ATOM 2550 CB PHE A 255 -8.228 9.701 17.148 1.00 29.18 C ANISOU 2550 CB PHE A 255 3598 3444 4046 -444 231 47 C ATOM 2551 CG PHE A 255 -7.009 9.053 16.557 1.00 34.85 C ANISOU 2551 CG PHE A 255 4273 4195 4772 -483 331 85 C ATOM 2552 CD1 PHE A 255 -5.860 9.793 16.336 1.00 37.22 C ANISOU 2552 CD1 PHE A 255 4564 4482 5098 -553 356 129 C ATOM 2553 CD2 PHE A 255 -7.007 7.705 16.230 1.00 30.77 C ANISOU 2553 CD2 PHE A 255 3729 3726 4237 -450 396 78 C ATOM 2554 CE1 PHE A 255 -4.732 9.207 15.799 1.00 35.05 C ANISOU 2554 CE1 PHE A 255 4244 4246 4826 -586 449 166 C ATOM 2555 CE2 PHE A 255 -5.880 7.111 15.688 1.00 37.78 C ANISOU 2555 CE2 PHE A 255 4579 4649 5128 -478 488 111 C ATOM 2556 CZ PHE A 255 -4.740 7.865 15.473 1.00 37.55 C ANISOU 2556 CZ PHE A 255 4533 4612 5121 -544 517 156 C ATOM 2557 N THR A 256 -10.282 10.957 19.152 1.00 30.40 N ANISOU 2557 N THR A 256 3775 3567 4210 -347 24 -40 N ATOM 2558 CA THR A 256 -11.055 12.074 19.685 1.00 28.82 C ANISOU 2558 CA THR A 256 3621 3324 4003 -320 -75 -65 C ATOM 2559 C THR A 256 -10.718 12.322 21.150 1.00 32.12 C ANISOU 2559 C THR A 256 3965 3764 4476 -306 -121 -93 C ATOM 2560 O THR A 256 -10.551 13.471 21.573 1.00 29.91 O ANISOU 2560 O THR A 256 3714 3436 4214 -323 -182 -96 O ATOM 2561 CB THR A 256 -12.551 11.795 19.518 1.00 30.36 C ANISOU 2561 CB THR A 256 3861 3531 4144 -251 -118 -93 C ATOM 2562 OG1 THR A 256 -12.852 11.601 18.130 1.00 35.94 O ANISOU 2562 OG1 THR A 256 4641 4216 4799 -267 -77 -67 O ATOM 2563 CG2 THR A 256 -13.384 12.944 20.057 1.00 30.02 C ANISOU 2563 CG2 THR A 256 3868 3449 4088 -213 -220 -120 C ATOM 2564 N PHE A 257 -10.587 11.251 21.932 1.00 32.29 N ANISOU 2564 N PHE A 257 3893 3855 4523 -276 -92 -111 N ATOM 2565 CA PHE A 257 -10.405 11.383 23.373 1.00 34.73 C ANISOU 2565 CA PHE A 257 4127 4193 4878 -253 -138 -142 C ATOM 2566 C PHE A 257 -8.962 11.715 23.732 1.00 32.77 C ANISOU 2566 C PHE A 257 3827 3937 4687 -319 -109 -118 C ATOM 2567 O PHE A 257 -8.708 12.625 24.529 1.00 40.54 O ANISOU 2567 O PHE A 257 4807 4894 5701 -329 -169 -130 O ATOM 2568 CB PHE A 257 -10.851 10.089 24.060 1.00 35.35 C ANISOU 2568 CB PHE A 257 4122 4349 4958 -197 -121 -168 C ATOM 2569 CG PHE A 257 -10.741 10.119 25.556 1.00 34.29 C ANISOU 2569 CG PHE A 257 3907 4255 4868 -167 -167 -200 C ATOM 2570 CD1 PHE A 257 -11.557 10.947 26.308 1.00 34.81 C ANISOU 2570 CD1 PHE A 257 3995 4309 4922 -119 -260 -234 C ATOM 2571 CD2 PHE A 257 -9.838 9.299 26.211 1.00 38.07 C ANISOU 2571 CD2 PHE A 257 4285 4786 5394 -182 -117 -196 C ATOM 2572 CE1 PHE A 257 -11.463 10.968 27.686 1.00 31.85 C ANISOU 2572 CE1 PHE A 257 3544 3974 4583 -88 -302 -265 C ATOM 2573 CE2 PHE A 257 -9.741 9.314 27.589 1.00 35.18 C ANISOU 2573 CE2 PHE A 257 3843 4459 5067 -154 -158 -225 C ATOM 2574 CZ PHE A 257 -10.555 10.151 28.327 1.00 34.60 C ANISOU 2574 CZ PHE A 257 3792 4373 4981 -107 -251 -260 C ATOM 2575 N PHE A 258 -8.001 10.998 23.151 1.00 29.82 N ANISOU 2575 N PHE A 258 3416 3587 4327 -364 -18 -82 N ATOM 2576 CA PHE A 258 -6.618 11.139 23.588 1.00 37.76 C ANISOU 2576 CA PHE A 258 4354 4604 5387 -422 16 -58 C ATOM 2577 C PHE A 258 -5.892 12.284 22.895 1.00 39.60 C ANISOU 2577 C PHE A 258 4647 4774 5624 -500 13 -15 C ATOM 2578 O PHE A 258 -4.949 12.841 23.467 1.00 45.32 O ANISOU 2578 O PHE A 258 5332 5492 6394 -549 1 0 O ATOM 2579 CB PHE A 258 -5.855 9.836 23.353 1.00 34.19 C ANISOU 2579 CB PHE A 258 3827 4216 4949 -430 115 -38 C ATOM 2580 CG PHE A 258 -6.272 8.713 24.262 1.00 33.49 C ANISOU 2580 CG PHE A 258 3660 4192 4872 -367 117 -75 C ATOM 2581 CD1 PHE A 258 -6.347 8.896 25.637 1.00 44.72 C ANISOU 2581 CD1 PHE A 258 5021 5638 6333 -341 60 -107 C ATOM 2582 CD2 PHE A 258 -6.590 7.470 23.741 1.00 31.95 C ANISOU 2582 CD2 PHE A 258 3456 4035 4650 -335 174 -75 C ATOM 2583 CE1 PHE A 258 -6.730 7.859 26.471 1.00 39.94 C ANISOU 2583 CE1 PHE A 258 4342 5095 5737 -286 62 -136 C ATOM 2584 CE2 PHE A 258 -6.973 6.431 24.567 1.00 33.03 C ANISOU 2584 CE2 PHE A 258 3524 4229 4798 -282 173 -105 C ATOM 2585 CZ PHE A 258 -7.040 6.624 25.936 1.00 36.42 C ANISOU 2585 CZ PHE A 258 3888 4685 5266 -258 117 -133 C ATOM 2586 N CYS A 259 -6.307 12.658 21.682 1.00 40.62 N ANISOU 2586 N CYS A 259 4870 4858 5706 -515 20 7 N ATOM 2587 CA CYS A 259 -5.656 13.757 20.983 1.00 44.20 C ANISOU 2587 CA CYS A 259 5384 5251 6160 -591 14 52 C ATOM 2588 C CYS A 259 -6.607 14.938 20.826 1.00 44.39 C ANISOU 2588 C CYS A 259 5514 5197 6154 -577 -79 36 C ATOM 2589 O CYS A 259 -7.222 15.101 19.764 1.00 46.93 O ANISOU 2589 O CYS A 259 5919 5487 6426 -573 -74 49 O ATOM 2590 CB CYS A 259 -5.148 13.312 19.609 1.00 39.65 C ANISOU 2590 CB CYS A 259 4829 4684 5553 -633 106 102 C ATOM 2591 SG CYS A 259 -4.127 14.586 18.808 1.00 62.21 S ANISOU 2591 SG CYS A 259 7739 7481 8416 -740 108 170 S ATOM 2592 N PRO A 260 -6.756 15.783 21.851 1.00 51.69 N ANISOU 2592 N PRO A 260 6443 6091 7106 -565 -166 7 N ATOM 2593 CA PRO A 260 -7.548 17.012 21.677 1.00 51.31 C ANISOU 2593 CA PRO A 260 6503 5963 7030 -553 -258 -5 C ATOM 2594 C PRO A 260 -6.905 18.023 20.743 1.00 51.81 C ANISOU 2594 C PRO A 260 6641 5954 7088 -640 -259 49 C ATOM 2595 O PRO A 260 -7.589 18.961 20.313 1.00 61.43 O ANISOU 2595 O PRO A 260 7963 7102 8274 -632 -323 47 O ATOM 2596 CB PRO A 260 -7.660 17.568 23.103 1.00 53.78 C ANISOU 2596 CB PRO A 260 6788 6268 7378 -521 -344 -49 C ATOM 2597 CG PRO A 260 -6.487 16.992 23.832 1.00 55.43 C ANISOU 2597 CG PRO A 260 6885 6532 7644 -559 -295 -38 C ATOM 2598 CD PRO A 260 -6.249 15.636 23.227 1.00 45.76 C ANISOU 2598 CD PRO A 260 5600 5378 6410 -556 -188 -18 C ATOM 2599 N ASP A 261 -5.617 17.873 20.426 1.00 57.51 N ANISOU 2599 N ASP A 261 7315 6696 7840 -721 -192 101 N ATOM 2600 CA ASP A 261 -4.970 18.738 19.448 1.00 57.39 C ANISOU 2600 CA ASP A 261 7365 6625 7817 -809 -184 162 C ATOM 2601 C ASP A 261 -5.249 18.306 18.015 1.00 48.60 C ANISOU 2601 C ASP A 261 6299 5517 6650 -814 -116 194 C ATOM 2602 O ASP A 261 -5.143 19.132 17.102 1.00 55.03 O ANISOU 2602 O ASP A 261 7195 6273 7441 -868 -128 237 O ATOM 2603 CB ASP A 261 -3.459 18.766 19.684 1.00 71.92 C ANISOU 2603 CB ASP A 261 9127 8492 9707 -896 -140 210 C ATOM 2604 CG ASP A 261 -3.091 19.372 21.024 1.00 78.15 C ANISOU 2604 CG ASP A 261 9881 9264 10550 -907 -215 186 C ATOM 2605 OD1 ASP A 261 -3.841 20.249 21.505 1.00 70.69 O ANISOU 2605 OD1 ASP A 261 9007 8255 9599 -874 -315 149 O ATOM 2606 OD2 ASP A 261 -2.052 18.973 21.593 1.00 75.08 O ANISOU 2606 OD2 ASP A 261 9395 8928 10206 -945 -174 203 O ATOM 2607 N CYS A 262 -5.589 17.038 17.797 1.00 53.68 N ANISOU 2607 N CYS A 262 6896 6227 7272 -760 -47 176 N ATOM 2608 CA CYS A 262 -5.953 16.565 16.471 1.00 53.25 C ANISOU 2608 CA CYS A 262 6891 6178 7162 -755 13 199 C ATOM 2609 C CYS A 262 -7.356 17.036 16.108 1.00 51.87 C ANISOU 2609 C CYS A 262 6818 5951 6938 -701 -54 169 C ATOM 2610 O CYS A 262 -8.222 17.203 16.971 1.00 48.92 O ANISOU 2610 O CYS A 262 6450 5569 6567 -637 -127 117 O ATOM 2611 CB CYS A 262 -5.902 15.038 16.400 1.00 48.77 C ANISOU 2611 CB CYS A 262 6248 5695 6588 -712 100 186 C ATOM 2612 SG CYS A 262 -4.321 14.266 16.812 1.00 60.65 S ANISOU 2612 SG CYS A 262 7626 7275 8144 -758 189 217 S ATOM 2613 N SER A 263 -7.577 17.242 14.814 1.00 54.21 N ANISOU 2613 N SER A 263 7193 6219 7187 -724 -28 203 N ATOM 2614 CA SER A 263 -8.903 17.603 14.337 1.00 47.12 C ANISOU 2614 CA SER A 263 6390 5278 6235 -672 -83 180 C ATOM 2615 C SER A 263 -9.824 16.389 14.384 1.00 45.66 C ANISOU 2615 C SER A 263 6177 5151 6020 -591 -56 138 C ATOM 2616 O SER A 263 -9.408 15.261 14.107 1.00 42.30 O ANISOU 2616 O SER A 263 5693 4787 5594 -591 28 147 O ATOM 2617 CB SER A 263 -8.827 18.153 12.913 1.00 45.58 C ANISOU 2617 CB SER A 263 6284 5036 5997 -724 -60 232 C ATOM 2618 OG SER A 263 -8.139 19.390 12.880 1.00 64.21 O ANISOU 2618 OG SER A 263 8683 7333 8381 -799 -102 271 O ATOM 2619 N HIS A 264 -11.083 16.624 14.743 1.00 43.10 N ANISOU 2619 N HIS A 264 5895 4810 5670 -522 -130 95 N ATOM 2620 CA HIS A 264 -12.038 15.529 14.830 1.00 39.85 C ANISOU 2620 CA HIS A 264 5459 4455 5228 -448 -116 59 C ATOM 2621 C HIS A 264 -12.217 14.888 13.460 1.00 39.73 C ANISOU 2621 C HIS A 264 5486 4450 5161 -459 -47 86 C ATOM 2622 O HIS A 264 -12.269 15.577 12.437 1.00 45.22 O ANISOU 2622 O HIS A 264 6265 5094 5823 -493 -48 119 O ATOM 2623 CB HIS A 264 -13.380 16.037 15.361 1.00 34.10 C ANISOU 2623 CB HIS A 264 4775 3708 4473 -374 -212 15 C ATOM 2624 CG HIS A 264 -14.295 14.949 15.831 1.00 36.87 C ANISOU 2624 CG HIS A 264 5077 4127 4805 -300 -212 -25 C ATOM 2625 ND1 HIS A 264 -14.902 14.062 14.969 1.00 43.19 N ANISOU 2625 ND1 HIS A 264 5897 4957 5557 -280 -168 -19 N ATOM 2626 CD2 HIS A 264 -14.710 14.609 17.075 1.00 34.64 C ANISOU 2626 CD2 HIS A 264 4726 3890 4544 -243 -253 -67 C ATOM 2627 CE1 HIS A 264 -15.649 13.220 15.662 1.00 37.46 C ANISOU 2627 CE1 HIS A 264 5118 4291 4825 -219 -184 -54 C ATOM 2628 NE2 HIS A 264 -15.551 13.532 16.941 1.00 39.44 N ANISOU 2628 NE2 HIS A 264 5313 4555 5117 -194 -233 -83 N ATOM 2629 N ALA A 265 -12.293 13.562 13.443 1.00 35.03 N ANISOU 2629 N ALA A 265 4834 3919 4558 -430 12 73 N ATOM 2630 CA ALA A 265 -12.468 12.845 12.189 1.00 42.09 C ANISOU 2630 CA ALA A 265 5766 4825 5400 -434 77 94 C ATOM 2631 C ALA A 265 -13.666 13.413 11.431 1.00 36.99 C ANISOU 2631 C ALA A 265 5224 4137 4695 -409 26 92 C ATOM 2632 O ALA A 265 -14.665 13.801 12.053 1.00 35.79 O ANISOU 2632 O ALA A 265 5089 3975 4533 -357 -53 58 O ATOM 2633 CB ALA A 265 -12.666 11.350 12.450 1.00 39.17 C ANISOU 2633 CB ALA A 265 5331 4524 5027 -391 123 69 C ATOM 2634 N PRO A 266 -13.613 13.475 10.103 1.00 39.77 N ANISOU 2634 N PRO A 266 5644 4466 5001 -440 68 127 N ATOM 2635 CA PRO A 266 -14.691 14.130 9.356 1.00 39.49 C ANISOU 2635 CA PRO A 266 5710 4386 4909 -421 18 129 C ATOM 2636 C PRO A 266 -15.985 13.334 9.418 1.00 36.05 C ANISOU 2636 C PRO A 266 5280 3987 4432 -350 -7 93 C ATOM 2637 O PRO A 266 -16.006 12.132 9.690 1.00 32.35 O ANISOU 2637 O PRO A 266 4750 3574 3967 -326 32 75 O ATOM 2638 CB PRO A 266 -14.144 14.202 7.927 1.00 31.98 C ANISOU 2638 CB PRO A 266 4814 3414 3923 -476 84 179 C ATOM 2639 CG PRO A 266 -13.173 13.079 7.835 1.00 41.13 C ANISOU 2639 CG PRO A 266 5898 4628 5099 -495 178 189 C ATOM 2640 CD PRO A 266 -12.588 12.900 9.213 1.00 40.59 C ANISOU 2640 CD PRO A 266 5733 4590 5099 -489 166 166 C ATOM 2641 N LEU A 267 -17.086 14.039 9.154 1.00 38.17 N ANISOU 2641 N LEU A 267 5623 4220 4658 -319 -75 84 N ATOM 2642 CA LEU A 267 -18.402 13.430 9.293 1.00 35.53 C ANISOU 2642 CA LEU A 267 5294 3923 4282 -251 -112 53 C ATOM 2643 C LEU A 267 -18.551 12.215 8.384 1.00 34.14 C ANISOU 2643 C LEU A 267 5123 3784 4066 -254 -44 62 C ATOM 2644 O LEU A 267 -19.163 11.214 8.773 1.00 37.65 O ANISOU 2644 O LEU A 267 5526 4280 4499 -212 -46 37 O ATOM 2645 CB LEU A 267 -19.484 14.471 9.002 1.00 38.83 C ANISOU 2645 CB LEU A 267 5800 4298 4656 -220 -192 50 C ATOM 2646 CG LEU A 267 -20.939 14.006 9.090 1.00 48.76 C ANISOU 2646 CG LEU A 267 7067 5596 5863 -151 -238 23 C ATOM 2647 CD1 LEU A 267 -21.229 13.371 10.439 1.00 41.28 C ANISOU 2647 CD1 LEU A 267 6026 4712 4947 -102 -266 -15 C ATOM 2648 CD2 LEU A 267 -21.882 15.174 8.834 1.00 38.73 C ANISOU 2648 CD2 LEU A 267 5883 4280 4552 -119 -318 22 C ATOM 2649 N TRP A 268 -17.989 12.274 7.174 1.00 34.74 N ANISOU 2649 N TRP A 268 5250 3832 4116 -302 16 99 N ATOM 2650 CA TRP A 268 -18.146 11.157 6.248 1.00 36.39 C ANISOU 2650 CA TRP A 268 5476 4071 4281 -301 77 106 C ATOM 2651 C TRP A 268 -17.425 9.909 6.744 1.00 33.80 C ANISOU 2651 C TRP A 268 5060 3797 3988 -300 139 94 C ATOM 2652 O TRP A 268 -17.891 8.790 6.499 1.00 30.84 O ANISOU 2652 O TRP A 268 4679 3457 3582 -274 161 80 O ATOM 2653 CB TRP A 268 -17.646 11.544 4.855 1.00 37.74 C ANISOU 2653 CB TRP A 268 5720 4204 4416 -351 128 150 C ATOM 2654 CG TRP A 268 -16.167 11.754 4.763 1.00 32.09 C ANISOU 2654 CG TRP A 268 4969 3482 3742 -410 192 181 C ATOM 2655 CD1 TRP A 268 -15.502 12.940 4.859 1.00 37.13 C ANISOU 2655 CD1 TRP A 268 5621 4077 4411 -455 174 209 C ATOM 2656 CD2 TRP A 268 -15.168 10.750 4.548 1.00 32.28 C ANISOU 2656 CD2 TRP A 268 4939 3548 3778 -428 282 191 C ATOM 2657 NE1 TRP A 268 -14.150 12.738 4.721 1.00 39.19 N ANISOU 2657 NE1 TRP A 268 5833 4354 4702 -506 248 239 N ATOM 2658 CE2 TRP A 268 -13.919 11.402 4.529 1.00 35.31 C ANISOU 2658 CE2 TRP A 268 5299 3917 4199 -486 317 228 C ATOM 2659 CE3 TRP A 268 -15.208 9.363 4.372 1.00 38.74 C ANISOU 2659 CE3 TRP A 268 5729 4414 4578 -401 334 174 C ATOM 2660 CZ2 TRP A 268 -12.721 10.715 4.340 1.00 38.77 C ANISOU 2660 CZ2 TRP A 268 5682 4395 4656 -513 405 248 C ATOM 2661 CZ3 TRP A 268 -14.017 8.683 4.186 1.00 43.02 C ANISOU 2661 CZ3 TRP A 268 6220 4987 5137 -424 420 190 C ATOM 2662 CH2 TRP A 268 -12.791 9.359 4.171 1.00 45.00 C ANISOU 2662 CH2 TRP A 268 6444 5231 5424 -478 456 227 C ATOM 2663 N LEU A 269 -16.297 10.073 7.438 1.00 34.41 N ANISOU 2663 N LEU A 269 5070 3879 4126 -328 165 99 N ATOM 2664 CA LEU A 269 -15.604 8.918 7.998 1.00 33.32 C ANISOU 2664 CA LEU A 269 4844 3793 4023 -322 220 87 C ATOM 2665 C LEU A 269 -16.358 8.347 9.193 1.00 35.25 C ANISOU 2665 C LEU A 269 5029 4078 4287 -268 167 45 C ATOM 2666 O LEU A 269 -16.348 7.128 9.407 1.00 32.88 O ANISOU 2666 O LEU A 269 4682 3822 3989 -247 200 30 O ATOM 2667 CB LEU A 269 -14.178 9.306 8.392 1.00 36.80 C ANISOU 2667 CB LEU A 269 5229 4232 4522 -369 261 108 C ATOM 2668 CG LEU A 269 -13.272 8.175 8.881 1.00 31.23 C ANISOU 2668 CG LEU A 269 4432 3580 3854 -367 327 101 C ATOM 2669 CD1 LEU A 269 -13.162 7.091 7.829 1.00 39.97 C ANISOU 2669 CD1 LEU A 269 5566 4708 4914 -361 401 110 C ATOM 2670 CD2 LEU A 269 -11.897 8.705 9.238 1.00 33.87 C ANISOU 2670 CD2 LEU A 269 4714 3914 4243 -417 362 128 C ATOM 2671 N MET A 270 -17.015 9.204 9.977 1.00 29.29 N ANISOU 2671 N MET A 270 4275 3310 3545 -243 85 27 N ATOM 2672 CA MET A 270 -17.861 8.715 11.061 1.00 29.88 C ANISOU 2672 CA MET A 270 4296 3430 3629 -188 30 -10 C ATOM 2673 C MET A 270 -18.984 7.841 10.515 1.00 32.98 C ANISOU 2673 C MET A 270 4721 3849 3962 -155 22 -17 C ATOM 2674 O MET A 270 -19.193 6.714 10.979 1.00 32.41 O ANISOU 2674 O MET A 270 4594 3825 3894 -132 32 -34 O ATOM 2675 CB MET A 270 -18.437 9.893 11.852 1.00 34.44 C ANISOU 2675 CB MET A 270 4882 3986 4218 -162 -59 -26 C ATOM 2676 CG MET A 270 -17.399 10.803 12.510 1.00 33.54 C ANISOU 2676 CG MET A 270 4738 3843 4164 -194 -65 -21 C ATOM 2677 SD MET A 270 -16.310 9.959 13.677 1.00 36.65 S ANISOU 2677 SD MET A 270 5006 4288 4630 -202 -21 -34 S ATOM 2678 CE MET A 270 -17.497 9.117 14.725 1.00 33.80 C ANISOU 2678 CE MET A 270 4588 3996 4260 -128 -75 -76 C ATOM 2679 N TYR A 271 -19.722 8.350 9.523 1.00 33.75 N ANISOU 2679 N TYR A 271 4909 3912 4001 -155 0 -4 N ATOM 2680 CA TYR A 271 -20.796 7.565 8.922 1.00 34.05 C ANISOU 2680 CA TYR A 271 4984 3974 3979 -130 -10 -8 C ATOM 2681 C TYR A 271 -20.267 6.245 8.378 1.00 36.67 C ANISOU 2681 C TYR A 271 5303 4327 4304 -147 66 -2 C ATOM 2682 O TYR A 271 -20.905 5.197 8.535 1.00 32.15 O ANISOU 2682 O TYR A 271 4711 3795 3712 -122 57 -16 O ATOM 2683 CB TYR A 271 -21.475 8.362 7.803 1.00 37.05 C ANISOU 2683 CB TYR A 271 5468 4311 4300 -135 -34 12 C ATOM 2684 CG TYR A 271 -22.358 9.508 8.261 1.00 43.26 C ANISOU 2684 CG TYR A 271 6281 5081 5075 -101 -122 2 C ATOM 2685 CD1 TYR A 271 -22.974 9.494 9.507 1.00 39.31 C ANISOU 2685 CD1 TYR A 271 5718 4623 4593 -52 -185 -27 C ATOM 2686 CD2 TYR A 271 -22.583 10.605 7.435 1.00 42.33 C ANISOU 2686 CD2 TYR A 271 6252 4909 4925 -114 -143 22 C ATOM 2687 CE1 TYR A 271 -23.783 10.539 9.920 1.00 45.42 C ANISOU 2687 CE1 TYR A 271 6519 5387 5353 -12 -265 -37 C ATOM 2688 CE2 TYR A 271 -23.391 11.653 7.838 1.00 36.09 C ANISOU 2688 CE2 TYR A 271 5490 4101 4120 -76 -225 12 C ATOM 2689 CZ TYR A 271 -23.988 11.616 9.081 1.00 54.99 C ANISOU 2689 CZ TYR A 271 7822 6539 6532 -23 -286 -19 C ATOM 2690 OH TYR A 271 -24.793 12.661 9.487 1.00 53.97 O ANISOU 2690 OH TYR A 271 7724 6397 6386 23 -368 -32 O ATOM 2691 N LEU A 272 -19.100 6.277 7.734 1.00 35.27 N ANISOU 2691 N LEU A 272 5137 4126 4140 -189 140 20 N ATOM 2692 CA LEU A 272 -18.536 5.054 7.175 1.00 39.15 C ANISOU 2692 CA LEU A 272 5620 4635 4620 -199 215 24 C ATOM 2693 C LEU A 272 -18.189 4.059 8.275 1.00 29.67 C ANISOU 2693 C LEU A 272 4325 3483 3468 -179 226 1 C ATOM 2694 O LEU A 272 -18.436 2.856 8.136 1.00 29.39 O ANISOU 2694 O LEU A 272 4283 3473 3412 -163 245 -9 O ATOM 2695 CB LEU A 272 -17.304 5.392 6.336 1.00 37.49 C ANISOU 2695 CB LEU A 272 5432 4398 4414 -245 292 54 C ATOM 2696 CG LEU A 272 -16.578 4.222 5.676 1.00 40.80 C ANISOU 2696 CG LEU A 272 5847 4836 4818 -251 377 60 C ATOM 2697 CD1 LEU A 272 -17.526 3.407 4.815 1.00 47.65 C ANISOU 2697 CD1 LEU A 272 6782 5705 5617 -230 372 52 C ATOM 2698 CD2 LEU A 272 -15.405 4.739 4.849 1.00 43.71 C ANISOU 2698 CD2 LEU A 272 6237 5186 5187 -294 447 95 C ATOM 2699 N ALA A 273 -17.616 4.545 9.379 1.00 32.48 N ANISOU 2699 N ALA A 273 4608 3848 3886 -181 211 -7 N ATOM 2700 CA ALA A 273 -17.286 3.664 10.495 1.00 29.22 C ANISOU 2700 CA ALA A 273 4100 3482 3520 -162 218 -27 C ATOM 2701 C ALA A 273 -18.541 3.129 11.172 1.00 27.58 C ANISOU 2701 C ALA A 273 3872 3311 3296 -119 149 -51 C ATOM 2702 O ALA A 273 -18.571 1.975 11.615 1.00 28.79 O ANISOU 2702 O ALA A 273 3977 3502 3460 -103 161 -63 O ATOM 2703 CB ALA A 273 -16.415 4.408 11.505 1.00 27.90 C ANISOU 2703 CB ALA A 273 3864 3315 3421 -176 213 -29 C ATOM 2704 N ILE A 274 -19.579 3.960 11.282 1.00 27.87 N ANISOU 2704 N ILE A 274 3942 3339 3306 -99 76 -55 N ATOM 2705 CA ILE A 274 -20.850 3.492 11.825 1.00 27.58 C ANISOU 2705 CA ILE A 274 3888 3346 3245 -59 10 -71 C ATOM 2706 C ILE A 274 -21.465 2.447 10.905 1.00 30.37 C ANISOU 2706 C ILE A 274 4291 3706 3541 -59 26 -64 C ATOM 2707 O ILE A 274 -21.967 1.413 11.360 1.00 27.07 O ANISOU 2707 O ILE A 274 3835 3331 3118 -41 8 -74 O ATOM 2708 CB ILE A 274 -21.804 4.682 12.040 1.00 28.66 C ANISOU 2708 CB ILE A 274 4057 3475 3360 -33 -69 -75 C ATOM 2709 CG1 ILE A 274 -21.289 5.596 13.151 1.00 28.66 C ANISOU 2709 CG1 ILE A 274 4000 3472 3416 -25 -98 -89 C ATOM 2710 CG2 ILE A 274 -23.212 4.190 12.367 1.00 32.11 C ANISOU 2710 CG2 ILE A 274 4484 3962 3754 8 -135 -84 C ATOM 2711 CD1 ILE A 274 -21.872 6.996 13.097 1.00 31.86 C ANISOU 2711 CD1 ILE A 274 4460 3844 3801 -8 -161 -89 C ATOM 2712 N VAL A 275 -21.444 2.703 9.596 1.00 30.40 N ANISOU 2712 N VAL A 275 4384 3668 3500 -82 56 -46 N ATOM 2713 CA VAL A 275 -22.000 1.753 8.639 1.00 32.66 C ANISOU 2713 CA VAL A 275 4727 3954 3727 -84 71 -40 C ATOM 2714 C VAL A 275 -21.239 0.435 8.694 1.00 29.85 C ANISOU 2714 C VAL A 275 4335 3613 3392 -91 130 -46 C ATOM 2715 O VAL A 275 -21.832 -0.646 8.597 1.00 26.80 O ANISOU 2715 O VAL A 275 3956 3249 2977 -81 118 -52 O ATOM 2716 CB VAL A 275 -21.986 2.368 7.226 1.00 36.16 C ANISOU 2716 CB VAL A 275 5270 4347 4120 -108 97 -20 C ATOM 2717 CG1 VAL A 275 -22.040 1.291 6.159 1.00 37.48 C ANISOU 2717 CG1 VAL A 275 5495 4508 4239 -118 141 -14 C ATOM 2718 CG2 VAL A 275 -23.147 3.344 7.067 1.00 34.70 C ANISOU 2718 CG2 VAL A 275 5135 4155 3897 -92 24 -15 C ATOM 2719 N LEU A 276 -19.917 0.501 8.855 1.00 32.93 N ANISOU 2719 N LEU A 276 4688 3994 3830 -108 194 -44 N ATOM 2720 CA LEU A 276 -19.127 -0.724 8.920 1.00 30.51 C ANISOU 2720 CA LEU A 276 4347 3703 3543 -108 253 -50 C ATOM 2721 C LEU A 276 -19.468 -1.533 10.164 1.00 27.16 C ANISOU 2721 C LEU A 276 3841 3326 3153 -83 214 -69 C ATOM 2722 O LEU A 276 -19.547 -2.765 10.108 1.00 26.28 O ANISOU 2722 O LEU A 276 3727 3228 3029 -75 227 -76 O ATOM 2723 CB LEU A 276 -17.639 -0.385 8.891 1.00 34.45 C ANISOU 2723 CB LEU A 276 4814 4189 4085 -130 327 -41 C ATOM 2724 CG LEU A 276 -16.664 -1.559 9.019 1.00 34.73 C ANISOU 2724 CG LEU A 276 4806 4244 4145 -124 394 -46 C ATOM 2725 CD1 LEU A 276 -16.904 -2.605 7.934 1.00 32.06 C ANISOU 2725 CD1 LEU A 276 4541 3894 3747 -117 425 -47 C ATOM 2726 CD2 LEU A 276 -15.239 -1.039 8.955 1.00 38.56 C ANISOU 2726 CD2 LEU A 276 5259 4724 4669 -148 463 -30 C ATOM 2727 N ALA A 277 -19.672 -0.860 11.297 1.00 28.24 N ANISOU 2727 N ALA A 277 3913 3486 3330 -71 164 -77 N ATOM 2728 CA ALA A 277 -20.063 -1.569 12.510 1.00 25.98 C ANISOU 2728 CA ALA A 277 3547 3252 3074 -47 123 -92 C ATOM 2729 C ALA A 277 -21.393 -2.286 12.318 1.00 27.60 C ANISOU 2729 C ALA A 277 3783 3480 3225 -33 67 -92 C ATOM 2730 O ALA A 277 -21.552 -3.438 12.739 1.00 31.37 O ANISOU 2730 O ALA A 277 4225 3987 3708 -25 61 -97 O ATOM 2731 CB ALA A 277 -20.137 -0.591 13.682 1.00 25.69 C ANISOU 2731 CB ALA A 277 3444 3237 3080 -32 74 -101 C ATOM 2732 N HIS A 278 -22.359 -1.624 11.675 1.00 28.86 N ANISOU 2732 N HIS A 278 4008 3625 3332 -31 25 -83 N ATOM 2733 CA HIS A 278 -23.663 -2.242 11.449 1.00 31.88 C ANISOU 2733 CA HIS A 278 4421 4034 3660 -22 -31 -78 C ATOM 2734 C HIS A 278 -23.585 -3.378 10.435 1.00 29.81 C ANISOU 2734 C HIS A 278 4222 3748 3358 -39 8 -72 C ATOM 2735 O HIS A 278 -24.361 -4.337 10.522 1.00 30.19 O ANISOU 2735 O HIS A 278 4270 3822 3379 -37 -30 -70 O ATOM 2736 CB HIS A 278 -24.667 -1.188 10.981 1.00 33.11 C ANISOU 2736 CB HIS A 278 4632 4181 3766 -13 -84 -69 C ATOM 2737 CG HIS A 278 -25.051 -0.201 12.041 1.00 34.80 C ANISOU 2737 CG HIS A 278 4790 4427 4006 16 -142 -77 C ATOM 2738 ND1 HIS A 278 -25.425 1.094 11.753 1.00 35.97 N ANISOU 2738 ND1 HIS A 278 4981 4552 4133 26 -172 -74 N ATOM 2739 CD2 HIS A 278 -25.132 -0.324 13.388 1.00 37.33 C ANISOU 2739 CD2 HIS A 278 5016 4800 4367 40 -177 -89 C ATOM 2740 CE1 HIS A 278 -25.712 1.728 12.876 1.00 34.34 C ANISOU 2740 CE1 HIS A 278 4713 4382 3954 58 -224 -85 C ATOM 2741 NE2 HIS A 278 -25.544 0.889 13.883 1.00 35.37 N ANISOU 2741 NE2 HIS A 278 4757 4560 4121 67 -227 -95 N ATOM 2742 N THR A 279 -22.665 -3.291 9.471 1.00 30.98 N ANISOU 2742 N THR A 279 4423 3847 3500 -58 80 -69 N ATOM 2743 CA THR A 279 -22.519 -4.347 8.474 1.00 32.56 C ANISOU 2743 CA THR A 279 4688 4022 3660 -68 121 -68 C ATOM 2744 C THR A 279 -22.174 -5.691 9.103 1.00 31.00 C ANISOU 2744 C THR A 279 4441 3847 3491 -61 132 -79 C ATOM 2745 O THR A 279 -22.448 -6.734 8.499 1.00 30.27 O ANISOU 2745 O THR A 279 4400 3742 3359 -64 135 -79 O ATOM 2746 CB THR A 279 -21.442 -3.957 7.452 1.00 35.08 C ANISOU 2746 CB THR A 279 5060 4296 3973 -84 202 -62 C ATOM 2747 OG1 THR A 279 -21.860 -2.790 6.734 1.00 39.92 O ANISOU 2747 OG1 THR A 279 5733 4884 4551 -95 187 -48 O ATOM 2748 CG2 THR A 279 -21.199 -5.077 6.461 1.00 37.62 C ANISOU 2748 CG2 THR A 279 5447 4594 4253 -87 248 -64 C ATOM 2749 N ASN A 280 -21.582 -5.692 10.300 1.00 29.01 N ANISOU 2749 N ASN A 280 4092 3624 3304 -50 136 -87 N ATOM 2750 CA ASN A 280 -21.267 -6.952 10.962 1.00 34.28 C ANISOU 2750 CA ASN A 280 4710 4315 4001 -42 144 -96 C ATOM 2751 C ASN A 280 -22.519 -7.781 11.218 1.00 33.19 C ANISOU 2751 C ASN A 280 4576 4204 3829 -40 69 -91 C ATOM 2752 O ASN A 280 -22.443 -9.011 11.296 1.00 35.16 O ANISOU 2752 O ASN A 280 4826 4454 4078 -40 73 -95 O ATOM 2753 CB ASN A 280 -20.533 -6.689 12.276 1.00 30.61 C ANISOU 2753 CB ASN A 280 4136 3882 3611 -31 152 -104 C ATOM 2754 CG ASN A 280 -20.077 -7.966 12.948 1.00 31.17 C ANISOU 2754 CG ASN A 280 4154 3973 3716 -21 166 -112 C ATOM 2755 OD1 ASN A 280 -19.195 -8.659 12.447 1.00 39.68 O ANISOU 2755 OD1 ASN A 280 5254 5025 4795 -20 230 -117 O ATOM 2756 ND2 ASN A 280 -20.675 -8.285 14.088 1.00 33.84 N ANISOU 2756 ND2 ASN A 280 4420 4361 4078 -12 106 -113 N ATOM 2757 N SER A 281 -23.674 -7.134 11.354 1.00 35.31 N ANISOU 2757 N SER A 281 4849 4498 4070 -39 0 -82 N ATOM 2758 CA SER A 281 -24.920 -7.862 11.557 1.00 35.34 C ANISOU 2758 CA SER A 281 4855 4537 4036 -42 -74 -71 C ATOM 2759 C SER A 281 -25.410 -8.559 10.294 1.00 33.50 C ANISOU 2759 C SER A 281 4727 4267 3735 -61 -75 -63 C ATOM 2760 O SER A 281 -26.459 -9.211 10.338 1.00 35.99 O ANISOU 2760 O SER A 281 5054 4608 4014 -71 -138 -50 O ATOM 2761 CB SER A 281 -25.993 -6.905 12.077 1.00 38.99 C ANISOU 2761 CB SER A 281 5286 5045 4483 -30 -146 -61 C ATOM 2762 OG SER A 281 -25.614 -6.354 13.327 1.00 42.90 O ANISOU 2762 OG SER A 281 5684 5578 5038 -9 -154 -70 O ATOM 2763 N VAL A 282 -24.684 -8.441 9.183 1.00 35.94 N ANISOU 2763 N VAL A 282 5110 4519 4025 -67 -8 -69 N ATOM 2764 CA VAL A 282 -25.057 -9.095 7.934 1.00 36.70 C ANISOU 2764 CA VAL A 282 5312 4576 4054 -82 -3 -65 C ATOM 2765 C VAL A 282 -24.181 -10.304 7.616 1.00 37.20 C ANISOU 2765 C VAL A 282 5403 4608 4125 -80 50 -79 C ATOM 2766 O VAL A 282 -24.626 -11.192 6.870 1.00 39.83 O ANISOU 2766 O VAL A 282 5812 4915 4406 -90 35 -78 O ATOM 2767 CB VAL A 282 -25.001 -8.091 6.762 1.00 36.58 C ANISOU 2767 CB VAL A 282 5375 4523 3999 -88 28 -60 C ATOM 2768 CG1 VAL A 282 -25.381 -8.768 5.454 1.00 36.96 C ANISOU 2768 CG1 VAL A 282 5534 4532 3975 -102 33 -58 C ATOM 2769 CG2 VAL A 282 -25.895 -6.886 7.029 1.00 35.10 C ANISOU 2769 CG2 VAL A 282 5171 4364 3801 -85 -28 -48 C ATOM 2770 N VAL A 283 -22.969 -10.378 8.159 1.00 36.00 N ANISOU 2770 N VAL A 283 5192 4455 4031 -65 110 -91 N ATOM 2771 CA VAL A 283 -21.974 -11.302 7.626 1.00 38.66 C ANISOU 2771 CA VAL A 283 5566 4755 4366 -54 177 -105 C ATOM 2772 C VAL A 283 -22.077 -12.710 8.211 1.00 37.90 C ANISOU 2772 C VAL A 283 5451 4666 4282 -49 149 -112 C ATOM 2773 O VAL A 283 -21.733 -13.682 7.529 1.00 47.16 O ANISOU 2773 O VAL A 283 6691 5802 5427 -42 177 -122 O ATOM 2774 CB VAL A 283 -20.560 -10.730 7.833 1.00 37.22 C ANISOU 2774 CB VAL A 283 5334 4572 4237 -40 260 -112 C ATOM 2775 CG1 VAL A 283 -20.409 -9.422 7.073 1.00 43.10 C ANISOU 2775 CG1 VAL A 283 6114 5300 4961 -51 289 -103 C ATOM 2776 CG2 VAL A 283 -20.260 -10.532 9.317 1.00 39.57 C ANISOU 2776 CG2 VAL A 283 5512 4915 4609 -33 243 -114 C ATOM 2777 N ASN A 284 -22.534 -12.859 9.454 1.00 35.89 N ANISOU 2777 N ASN A 284 5110 4459 4068 -52 93 -105 N ATOM 2778 CA ASN A 284 -22.551 -14.193 10.056 1.00 46.50 C ANISOU 2778 CA ASN A 284 6432 5809 5428 -49 67 -108 C ATOM 2779 C ASN A 284 -23.370 -15.188 9.242 1.00 43.90 C ANISOU 2779 C ASN A 284 6200 5447 5033 -66 23 -103 C ATOM 2780 O ASN A 284 -22.876 -16.303 8.995 1.00 42.88 O ANISOU 2780 O ASN A 284 6111 5282 4898 -57 45 -115 O ATOM 2781 CB ASN A 284 -23.050 -14.102 11.503 1.00 43.24 C ANISOU 2781 CB ASN A 284 5908 5459 5062 -52 7 -97 C ATOM 2782 CG ASN A 284 -22.131 -13.274 12.382 1.00 48.55 C ANISOU 2782 CG ASN A 284 6484 6159 5802 -34 50 -105 C ATOM 2783 OD1 ASN A 284 -21.126 -12.732 11.915 1.00 35.81 O ANISOU 2783 OD1 ASN A 284 4883 4519 4203 -23 124 -116 O ATOM 2784 ND2 ASN A 284 -22.476 -13.162 13.658 1.00 45.88 N ANISOU 2784 ND2 ASN A 284 6048 5878 5506 -31 2 -98 N ATOM 2785 N PRO A 285 -24.593 -14.875 8.799 1.00 41.48 N ANISOU 2785 N PRO A 285 5938 5148 4673 -90 -40 -86 N ATOM 2786 CA PRO A 285 -25.322 -15.828 7.941 1.00 43.69 C ANISOU 2786 CA PRO A 285 6318 5393 4888 -111 -81 -81 C ATOM 2787 C PRO A 285 -24.510 -16.356 6.766 1.00 50.30 C ANISOU 2787 C PRO A 285 7257 6163 5692 -96 -14 -102 C ATOM 2788 O PRO A 285 -24.621 -17.543 6.431 1.00 46.79 O ANISOU 2788 O PRO A 285 6875 5682 5219 -100 -34 -108 O ATOM 2789 CB PRO A 285 -26.528 -15.005 7.471 1.00 37.00 C ANISOU 2789 CB PRO A 285 5502 4567 3990 -133 -135 -60 C ATOM 2790 CG PRO A 285 -26.777 -14.052 8.588 1.00 41.69 C ANISOU 2790 CG PRO A 285 5985 5225 4629 -126 -160 -49 C ATOM 2791 CD PRO A 285 -25.427 -13.717 9.169 1.00 36.75 C ANISOU 2791 CD PRO A 285 5294 4597 4073 -99 -85 -69 C ATOM 2792 N PHE A 286 -23.698 -15.509 6.125 1.00 54.16 N ANISOU 2792 N PHE A 286 7764 6633 6181 -77 64 -114 N ATOM 2793 CA PHE A 286 -22.900 -15.967 4.990 1.00 50.14 C ANISOU 2793 CA PHE A 286 7347 6070 5636 -58 132 -133 C ATOM 2794 C PHE A 286 -21.774 -16.892 5.431 1.00 50.97 C ANISOU 2794 C PHE A 286 7424 6162 5781 -26 181 -153 C ATOM 2795 O PHE A 286 -21.428 -17.832 4.706 1.00 48.29 O ANISOU 2795 O PHE A 286 7167 5777 5405 -8 204 -170 O ATOM 2796 CB PHE A 286 -22.331 -14.769 4.227 1.00 49.41 C ANISOU 2796 CB PHE A 286 7273 5970 5532 -49 200 -134 C ATOM 2797 CG PHE A 286 -23.362 -14.010 3.445 1.00 55.19 C ANISOU 2797 CG PHE A 286 8064 6698 6207 -75 161 -118 C ATOM 2798 CD1 PHE A 286 -24.106 -13.008 4.044 1.00 48.45 C ANISOU 2798 CD1 PHE A 286 7152 5886 5372 -92 112 -99 C ATOM 2799 CD2 PHE A 286 -23.596 -14.306 2.111 1.00 54.52 C ANISOU 2799 CD2 PHE A 286 8096 6570 6049 -78 170 -122 C ATOM 2800 CE1 PHE A 286 -25.062 -12.312 3.328 1.00 56.32 C ANISOU 2800 CE1 PHE A 286 8204 6881 6315 -111 75 -84 C ATOM 2801 CE2 PHE A 286 -24.549 -13.614 1.390 1.00 61.27 C ANISOU 2801 CE2 PHE A 286 9006 7423 6851 -101 133 -106 C ATOM 2802 CZ PHE A 286 -25.283 -12.614 1.999 1.00 60.77 C ANISOU 2802 CZ PHE A 286 8881 7401 6807 -117 85 -86 C ATOM 2803 N ILE A 287 -21.196 -16.650 6.607 1.00 52.72 N ANISOU 2803 N ILE A 287 7534 6423 6076 -16 197 -152 N ATOM 2804 CA ILE A 287 -20.123 -17.511 7.089 1.00 48.49 C ANISOU 2804 CA ILE A 287 6964 5880 5581 16 243 -169 C ATOM 2805 C ILE A 287 -20.657 -18.906 7.393 1.00 56.59 C ANISOU 2805 C ILE A 287 8020 6887 6594 11 180 -171 C ATOM 2806 O ILE A 287 -20.035 -19.915 7.037 1.00 54.90 O ANISOU 2806 O ILE A 287 7858 6633 6367 38 210 -189 O ATOM 2807 CB ILE A 287 -19.449 -16.876 8.316 1.00 44.52 C ANISOU 2807 CB ILE A 287 6331 5428 5159 24 268 -165 C ATOM 2808 CG1 ILE A 287 -18.850 -15.511 7.953 1.00 42.85 C ANISOU 2808 CG1 ILE A 287 6099 5227 4957 26 330 -161 C ATOM 2809 CG2 ILE A 287 -18.384 -17.805 8.879 1.00 50.51 C ANISOU 2809 CG2 ILE A 287 7049 6183 5959 57 312 -180 C ATOM 2810 CD1 ILE A 287 -17.792 -15.556 6.869 1.00 47.24 C ANISOU 2810 CD1 ILE A 287 6716 5750 5484 51 421 -173 C ATOM 2811 N TYR A 288 -21.819 -18.989 8.048 1.00 56.37 N ANISOU 2811 N TYR A 288 7961 6888 6569 -24 89 -150 N ATOM 2812 CA TYR A 288 -22.426 -20.293 8.300 1.00 53.30 C ANISOU 2812 CA TYR A 288 7605 6482 6165 -39 19 -145 C ATOM 2813 C TYR A 288 -22.688 -21.035 6.995 1.00 45.83 C ANISOU 2813 C TYR A 288 6800 5469 5143 -41 12 -156 C ATOM 2814 O TYR A 288 -22.419 -22.237 6.888 1.00 52.88 O ANISOU 2814 O TYR A 288 7746 6319 6025 -28 4 -169 O ATOM 2815 CB TYR A 288 -23.729 -20.129 9.085 1.00 48.87 C ANISOU 2815 CB TYR A 288 6989 5972 5607 -81 -78 -113 C ATOM 2816 CG TYR A 288 -23.573 -19.402 10.401 1.00 42.52 C ANISOU 2816 CG TYR A 288 6047 5236 4872 -77 -79 -103 C ATOM 2817 CD1 TYR A 288 -22.504 -19.668 11.246 1.00 52.56 C ANISOU 2817 CD1 TYR A 288 7243 6519 6210 -49 -32 -116 C ATOM 2818 CD2 TYR A 288 -24.494 -18.442 10.794 1.00 47.36 C ANISOU 2818 CD2 TYR A 288 6608 5904 5483 -98 -128 -81 C ATOM 2819 CE1 TYR A 288 -22.361 -18.998 12.452 1.00 47.47 C ANISOU 2819 CE1 TYR A 288 6474 5936 5625 -45 -36 -108 C ATOM 2820 CE2 TYR A 288 -24.358 -17.766 11.994 1.00 42.78 C ANISOU 2820 CE2 TYR A 288 5907 5385 4962 -90 -132 -75 C ATOM 2821 CZ TYR A 288 -23.292 -18.046 12.817 1.00 40.31 C ANISOU 2821 CZ TYR A 288 5521 5080 4713 -65 -86 -89 C ATOM 2822 OH TYR A 288 -23.164 -17.372 14.010 1.00 45.97 O ANISOU 2822 OH TYR A 288 6120 5858 5487 -57 -92 -83 O ATOM 2823 N ALA A 289 -23.206 -20.331 5.986 1.00 50.95 N ANISOU 2823 N ALA A 289 7516 6106 5737 -56 13 -152 N ATOM 2824 CA ALA A 289 -23.548 -20.979 4.724 1.00 53.17 C ANISOU 2824 CA ALA A 289 7934 6328 5941 -60 0 -162 C ATOM 2825 C ALA A 289 -22.311 -21.553 4.042 1.00 58.33 C ANISOU 2825 C ALA A 289 8649 6931 6582 -9 84 -195 C ATOM 2826 O ALA A 289 -22.327 -22.692 3.561 1.00 57.47 O ANISOU 2826 O ALA A 289 8631 6768 6435 0 64 -211 O ATOM 2827 CB ALA A 289 -24.254 -19.984 3.802 1.00 46.38 C ANISOU 2827 CB ALA A 289 7123 5470 5027 -82 -7 -151 C ATOM 2828 N TYR A 290 -21.227 -20.777 3.988 1.00 58.92 N ANISOU 2828 N TYR A 290 8677 7022 6686 24 176 -206 N ATOM 2829 CA TYR A 290 -20.048 -21.213 3.249 1.00 62.73 C ANISOU 2829 CA TYR A 290 9216 7469 7150 76 262 -234 C ATOM 2830 C TYR A 290 -19.224 -22.245 4.010 1.00 59.88 C ANISOU 2830 C TYR A 290 8818 7101 6834 113 279 -250 C ATOM 2831 O TYR A 290 -18.517 -23.042 3.384 1.00 61.32 O ANISOU 2831 O TYR A 290 9073 7241 6985 157 322 -276 O ATOM 2832 CB TYR A 290 -19.161 -20.012 2.904 1.00 58.72 C ANISOU 2832 CB TYR A 290 8666 6988 6656 95 354 -233 C ATOM 2833 CG TYR A 290 -19.660 -19.177 1.745 1.00 65.97 C ANISOU 2833 CG TYR A 290 9658 7896 7513 76 361 -226 C ATOM 2834 CD1 TYR A 290 -19.733 -19.706 0.461 1.00 82.32 C ANISOU 2834 CD1 TYR A 290 11856 9917 9506 92 373 -241 C ATOM 2835 CD2 TYR A 290 -20.040 -17.855 1.929 1.00 71.14 C ANISOU 2835 CD2 TYR A 290 10257 8587 8186 46 355 -203 C ATOM 2836 CE1 TYR A 290 -20.184 -18.944 -0.603 1.00 79.16 C ANISOU 2836 CE1 TYR A 290 11521 9508 9047 74 380 -233 C ATOM 2837 CE2 TYR A 290 -20.492 -17.085 0.872 1.00 80.76 C ANISOU 2837 CE2 TYR A 290 11542 9794 9348 29 360 -194 C ATOM 2838 CZ TYR A 290 -20.562 -17.634 -0.391 1.00 87.72 C ANISOU 2838 CZ TYR A 290 12546 10630 10153 42 373 -208 C ATOM 2839 OH TYR A 290 -21.011 -16.870 -1.446 1.00 89.71 O ANISOU 2839 OH TYR A 290 12865 10873 10349 25 379 -198 O ATOM 2840 N ARG A 291 -19.299 -22.257 5.342 1.00 58.28 N ANISOU 2840 N ARG A 291 8506 6939 6699 98 247 -236 N ATOM 2841 CA ARG A 291 -18.384 -23.051 6.150 1.00 59.71 C ANISOU 2841 CA ARG A 291 8633 7121 6931 135 274 -249 C ATOM 2842 C ARG A 291 -19.042 -24.190 6.917 1.00 53.13 C ANISOU 2842 C ARG A 291 7801 6275 6113 115 186 -242 C ATOM 2843 O ARG A 291 -18.323 -25.040 7.452 1.00 50.91 O ANISOU 2843 O ARG A 291 7498 5982 5863 148 203 -255 O ATOM 2844 CB ARG A 291 -17.648 -22.145 7.148 1.00 54.37 C ANISOU 2844 CB ARG A 291 7818 6508 6332 141 323 -239 C ATOM 2845 CG ARG A 291 -16.854 -21.026 6.497 1.00 46.29 C ANISOU 2845 CG ARG A 291 6784 5501 5303 158 413 -242 C ATOM 2846 CD ARG A 291 -15.850 -20.433 7.465 1.00 50.34 C ANISOU 2846 CD ARG A 291 7170 6066 5892 174 468 -237 C ATOM 2847 NE ARG A 291 -14.879 -21.430 7.898 1.00 62.12 N ANISOU 2847 NE ARG A 291 8639 7551 7412 220 506 -254 N ATOM 2848 CZ ARG A 291 -13.790 -21.761 7.218 1.00 61.83 C ANISOU 2848 CZ ARG A 291 8640 7500 7354 271 588 -272 C ATOM 2849 NH1 ARG A 291 -13.489 -21.180 6.068 1.00 50.36 N ANISOU 2849 NH1 ARG A 291 7246 6037 5851 280 645 -274 N ATOM 2850 NH2 ARG A 291 -12.984 -22.702 7.704 1.00 57.42 N ANISOU 2850 NH2 ARG A 291 8058 6938 6822 315 614 -286 N ATOM 2851 N ILE A 292 -20.369 -24.238 6.994 1.00 45.88 N ANISOU 2851 N ILE A 292 6904 5359 5170 61 91 -219 N ATOM 2852 CA ILE A 292 -21.071 -25.258 7.766 1.00 44.73 C ANISOU 2852 CA ILE A 292 6750 5208 5037 32 0 -204 C ATOM 2853 C ILE A 292 -22.117 -25.888 6.856 1.00 48.85 C ANISOU 2853 C ILE A 292 7400 5678 5483 -3 -74 -199 C ATOM 2854 O ILE A 292 -23.106 -25.237 6.496 1.00 49.25 O ANISOU 2854 O ILE A 292 7465 5749 5500 -45 -117 -179 O ATOM 2855 CB ILE A 292 -21.718 -24.685 9.034 1.00 51.04 C ANISOU 2855 CB ILE A 292 7422 6081 5891 -7 -53 -171 C ATOM 2856 CG1 ILE A 292 -20.686 -23.889 9.838 1.00 48.43 C ANISOU 2856 CG1 ILE A 292 6970 5800 5631 24 23 -178 C ATOM 2857 CG2 ILE A 292 -22.293 -25.807 9.891 1.00 46.74 C ANISOU 2857 CG2 ILE A 292 6860 5535 5363 -35 -140 -152 C ATOM 2858 CD1 ILE A 292 -21.254 -23.181 11.048 1.00 41.21 C ANISOU 2858 CD1 ILE A 292 5930 4961 4766 -6 -22 -150 C ATOM 2859 N ARG A 293 -21.909 -27.158 6.498 1.00 47.37 N ANISOU 2859 N ARG A 293 7307 5425 5268 16 -92 -217 N ATOM 2860 CA ARG A 293 -22.780 -27.808 5.524 1.00 53.15 C ANISOU 2860 CA ARG A 293 8174 6098 5923 -13 -158 -217 C ATOM 2861 C ARG A 293 -24.202 -27.982 6.047 1.00 53.00 C ANISOU 2861 C ARG A 293 8135 6105 5897 -88 -275 -175 C ATOM 2862 O ARG A 293 -25.157 -27.910 5.266 1.00 55.05 O ANISOU 2862 O ARG A 293 8473 6348 6095 -128 -328 -163 O ATOM 2863 CB ARG A 293 -22.196 -29.164 5.127 1.00 47.17 C ANISOU 2863 CB ARG A 293 7521 5261 5141 27 -157 -248 C ATOM 2864 N GLU A 294 -24.370 -28.216 7.350 1.00 57.79 N ANISOU 2864 N GLU A 294 8636 6757 6564 -109 -318 -150 N ATOM 2865 CA GLU A 294 -25.712 -28.432 7.883 1.00 49.62 C ANISOU 2865 CA GLU A 294 7576 5757 5520 -180 -431 -105 C ATOM 2866 C GLU A 294 -26.549 -27.161 7.801 1.00 52.07 C ANISOU 2866 C GLU A 294 7833 6133 5816 -212 -443 -80 C ATOM 2867 O GLU A 294 -27.758 -27.225 7.546 1.00 48.53 O ANISOU 2867 O GLU A 294 7419 5697 5323 -267 -526 -49 O ATOM 2868 CB GLU A 294 -25.632 -28.929 9.325 1.00 53.91 C ANISOU 2868 CB GLU A 294 8011 6342 6132 -191 -467 -83 C ATOM 2869 CG GLU A 294 -26.924 -29.544 9.835 1.00 57.86 C ANISOU 2869 CG GLU A 294 8503 6865 6617 -263 -591 -35 C ATOM 2870 CD GLU A 294 -27.252 -30.861 9.157 1.00 70.11 C ANISOU 2870 CD GLU A 294 10195 8329 8115 -287 -657 -37 C ATOM 2871 OE1 GLU A 294 -26.376 -31.402 8.449 1.00 75.88 O ANISOU 2871 OE1 GLU A 294 11021 8980 8829 -237 -604 -80 O ATOM 2872 OE2 GLU A 294 -28.385 -31.356 9.332 1.00 69.42 O ANISOU 2872 OE2 GLU A 294 10123 8253 8002 -355 -762 5 O ATOM 2873 N PHE A 295 -25.930 -25.998 8.025 1.00 52.42 N ANISOU 2873 N PHE A 295 7795 6223 5898 -179 -364 -91 N ATOM 2874 CA PHE A 295 -26.640 -24.735 7.835 1.00 55.57 C ANISOU 2874 CA PHE A 295 8157 6675 6280 -200 -370 -73 C ATOM 2875 C PHE A 295 -26.922 -24.483 6.359 1.00 51.76 C ANISOU 2875 C PHE A 295 7799 6145 5722 -203 -356 -86 C ATOM 2876 O PHE A 295 -28.010 -24.019 5.998 1.00 49.42 O ANISOU 2876 O PHE A 295 7522 5872 5383 -243 -411 -60 O ATOM 2877 CB PHE A 295 -25.831 -23.573 8.420 1.00 50.02 C ANISOU 2877 CB PHE A 295 7345 6022 5636 -163 -290 -83 C ATOM 2878 CG PHE A 295 -26.123 -23.289 9.868 1.00 46.78 C ANISOU 2878 CG PHE A 295 6797 5692 5287 -177 -328 -57 C ATOM 2879 CD1 PHE A 295 -27.311 -22.682 10.244 1.00 45.19 C ANISOU 2879 CD1 PHE A 295 6544 5554 5071 -215 -397 -23 C ATOM 2880 CD2 PHE A 295 -25.201 -23.609 10.852 1.00 51.94 C ANISOU 2880 CD2 PHE A 295 7368 6359 6009 -148 -293 -68 C ATOM 2881 CE1 PHE A 295 -27.580 -22.413 11.576 1.00 43.08 C ANISOU 2881 CE1 PHE A 295 6149 5365 4855 -222 -432 0 C ATOM 2882 CE2 PHE A 295 -25.463 -23.341 12.186 1.00 46.05 C ANISOU 2882 CE2 PHE A 295 6494 5687 5315 -159 -327 -45 C ATOM 2883 CZ PHE A 295 -26.654 -22.742 12.548 1.00 42.28 C ANISOU 2883 CZ PHE A 295 5968 5274 4821 -195 -396 -11 C ATOM 2884 N ARG A 296 -25.950 -24.783 5.495 1.00 46.98 N ANISOU 2884 N ARG A 296 7278 5475 5097 -159 -283 -124 N ATOM 2885 CA ARG A 296 -26.113 -24.529 4.067 1.00 50.95 C ANISOU 2885 CA ARG A 296 7898 5933 5527 -156 -261 -138 C ATOM 2886 C ARG A 296 -27.289 -25.317 3.500 1.00 57.11 C ANISOU 2886 C ARG A 296 8779 6679 6241 -206 -360 -120 C ATOM 2887 O ARG A 296 -28.127 -24.771 2.772 1.00 55.76 O ANISOU 2887 O ARG A 296 8654 6516 6018 -236 -389 -106 O ATOM 2888 CB ARG A 296 -24.817 -24.879 3.333 1.00 52.32 C ANISOU 2888 CB ARG A 296 8140 6049 5691 -94 -168 -181 C ATOM 2889 CG ARG A 296 -24.875 -24.679 1.833 1.00 58.61 C ANISOU 2889 CG ARG A 296 9061 6800 6410 -84 -139 -199 C ATOM 2890 CD ARG A 296 -23.488 -24.736 1.197 1.00 65.58 C ANISOU 2890 CD ARG A 296 9982 7648 7287 -15 -31 -238 C ATOM 2891 NE ARG A 296 -22.776 -25.973 1.505 1.00 56.81 N ANISOU 2891 NE ARG A 296 8898 6495 6192 23 -24 -261 N ATOM 2892 CZ ARG A 296 -21.714 -26.068 2.297 1.00 53.68 C ANISOU 2892 CZ ARG A 296 8418 6119 5859 65 34 -273 C ATOM 2893 NH1 ARG A 296 -21.191 -25.008 2.892 1.00 62.33 N ANISOU 2893 NH1 ARG A 296 9396 7277 7011 73 93 -263 N ATOM 2894 NH2 ARG A 296 -21.155 -27.260 2.490 1.00 60.02 N ANISOU 2894 NH2 ARG A 296 9259 6878 6667 100 33 -294 N ATOM 2895 N GLN A 297 -27.369 -26.609 3.829 1.00 52.45 N ANISOU 2895 N GLN A 297 8227 6051 5653 -218 -416 -120 N ATOM 2896 CA GLN A 297 -28.446 -27.438 3.301 1.00 53.22 C ANISOU 2896 CA GLN A 297 8425 6110 5687 -272 -515 -101 C ATOM 2897 C GLN A 297 -29.800 -27.032 3.866 1.00 48.80 C ANISOU 2897 C GLN A 297 7797 5622 5124 -339 -606 -49 C ATOM 2898 O GLN A 297 -30.817 -27.149 3.175 1.00 46.22 O ANISOU 2898 O GLN A 297 7544 5284 4733 -385 -673 -28 O ATOM 2899 CB GLN A 297 -28.163 -28.909 3.601 1.00 58.63 C ANISOU 2899 CB GLN A 297 9164 6735 6380 -269 -557 -111 C ATOM 2900 CG GLN A 297 -26.969 -29.466 2.838 1.00 64.55 C ANISOU 2900 CG GLN A 297 10010 7406 7112 -200 -480 -164 C ATOM 2901 CD GLN A 297 -26.596 -30.866 3.278 1.00 65.13 C ANISOU 2901 CD GLN A 297 10124 7421 7201 -189 -517 -175 C ATOM 2902 OE1 GLN A 297 -26.879 -31.270 4.406 1.00 68.00 O ANISOU 2902 OE1 GLN A 297 10407 7815 7613 -220 -573 -146 O ATOM 2903 NE2 GLN A 297 -25.960 -31.618 2.387 1.00 65.57 N ANISOU 2903 NE2 GLN A 297 10308 7393 7214 -141 -488 -217 N ATOM 2904 N THR A 298 -29.838 -26.557 5.112 1.00 57.01 N ANISOU 2904 N THR A 298 8695 6738 6227 -343 -611 -25 N ATOM 2905 CA THR A 298 -31.103 -26.108 5.680 1.00 50.26 C ANISOU 2905 CA THR A 298 7766 5964 5367 -398 -692 25 C ATOM 2906 C THR A 298 -31.554 -24.794 5.058 1.00 51.93 C ANISOU 2906 C THR A 298 7972 6212 5546 -396 -667 30 C ATOM 2907 O THR A 298 -32.759 -24.547 4.941 1.00 48.74 O ANISOU 2907 O THR A 298 7568 5852 5101 -444 -741 67 O ATOM 2908 CB THR A 298 -30.977 -25.960 7.193 1.00 45.79 C ANISOU 2908 CB THR A 298 7051 5472 4876 -396 -701 46 C ATOM 2909 OG1 THR A 298 -30.429 -27.162 7.747 1.00 45.60 O ANISOU 2909 OG1 THR A 298 7033 5408 4884 -391 -716 39 O ATOM 2910 CG2 THR A 298 -32.339 -25.686 7.818 1.00 43.74 C ANISOU 2910 CG2 THR A 298 6717 5300 4603 -452 -796 101 C ATOM 2911 N PHE A 299 -30.609 -23.939 4.661 1.00 56.34 N ANISOU 2911 N PHE A 299 8527 6758 6121 -344 -566 -5 N ATOM 2912 CA PHE A 299 -30.980 -22.709 3.971 1.00 58.60 C ANISOU 2912 CA PHE A 299 8823 7069 6374 -341 -541 -2 C ATOM 2913 C PHE A 299 -31.603 -23.013 2.615 1.00 60.32 C ANISOU 2913 C PHE A 299 9179 7234 6507 -367 -572 -2 C ATOM 2914 O PHE A 299 -32.610 -22.402 2.238 1.00 61.79 O ANISOU 2914 O PHE A 299 9374 7455 6649 -398 -616 24 O ATOM 2915 CB PHE A 299 -29.758 -21.803 3.806 1.00 54.89 C ANISOU 2915 CB PHE A 299 8325 6590 5940 -284 -427 -36 C ATOM 2916 CG PHE A 299 -29.200 -21.275 5.106 1.00 53.44 C ANISOU 2916 CG PHE A 299 8002 6464 5839 -260 -396 -34 C ATOM 2917 CD1 PHE A 299 -29.961 -21.271 6.266 1.00 55.48 C ANISOU 2917 CD1 PHE A 299 8160 6793 6127 -288 -467 0 C ATOM 2918 CD2 PHE A 299 -27.910 -20.775 5.160 1.00 50.59 C ANISOU 2918 CD2 PHE A 299 7609 6091 5522 -211 -297 -64 C ATOM 2919 CE1 PHE A 299 -29.443 -20.784 7.452 1.00 47.15 C ANISOU 2919 CE1 PHE A 299 6980 5792 5145 -264 -440 -1 C ATOM 2920 CE2 PHE A 299 -27.388 -20.283 6.342 1.00 49.24 C ANISOU 2920 CE2 PHE A 299 7313 5971 5425 -192 -271 -63 C ATOM 2921 CZ PHE A 299 -28.155 -20.289 7.490 1.00 47.15 C ANISOU 2921 CZ PHE A 299 6952 5772 5189 -217 -343 -33 C ATOM 2922 N ARG A 300 -31.023 -23.957 1.868 1.00 61.34 N ANISOU 2922 N ARG A 300 9419 7281 6608 -351 -551 -33 N ATOM 2923 CA ARG A 300 -31.593 -24.317 0.574 1.00 69.63 C ANISOU 2923 CA ARG A 300 10606 8276 7573 -374 -584 -37 C ATOM 2924 C ARG A 300 -33.034 -24.790 0.723 1.00 63.64 C ANISOU 2924 C ARG A 300 9860 7544 6776 -446 -706 10 C ATOM 2925 O ARG A 300 -33.918 -24.367 -0.029 1.00 63.35 O ANISOU 2925 O ARG A 300 9872 7519 6679 -477 -742 28 O ATOM 2926 CB ARG A 300 -30.746 -25.397 -0.101 1.00 66.75 C ANISOU 2926 CB ARG A 300 10356 7819 7186 -342 -551 -78 C ATOM 2927 CG ARG A 300 -29.360 -24.936 -0.527 1.00 72.01 C ANISOU 2927 CG ARG A 300 11029 8459 7871 -270 -428 -122 C ATOM 2928 CD ARG A 300 -28.753 -25.885 -1.552 1.00 84.91 C ANISOU 2928 CD ARG A 300 12804 10005 9454 -237 -402 -162 C ATOM 2929 NE ARG A 300 -27.341 -25.612 -1.805 1.00 78.56 N ANISOU 2929 NE ARG A 300 11993 9184 8671 -164 -285 -201 N ATOM 2930 CZ ARG A 300 -26.330 -26.291 -1.276 1.00 80.70 C ANISOU 2930 CZ ARG A 300 12242 9434 8985 -119 -244 -225 C ATOM 2931 NH1 ARG A 300 -26.531 -27.291 -0.431 1.00 71.48 N ANISOU 2931 NH1 ARG A 300 11058 8254 7848 -138 -309 -217 N ATOM 2932 NH2 ARG A 300 -25.085 -25.961 -1.607 1.00 82.78 N ANISOU 2932 NH2 ARG A 300 12500 9691 9260 -54 -135 -256 N ATOM 2933 N LYS A 301 -33.293 -25.661 1.701 1.00 55.86 N ANISOU 2933 N LYS A 301 8828 6575 5823 -476 -772 32 N ATOM 2934 CA LYS A 301 -34.630 -26.227 1.847 1.00 56.45 C ANISOU 2934 CA LYS A 301 8915 6675 5859 -550 -892 81 C ATOM 2935 C LYS A 301 -35.642 -25.173 2.281 1.00 57.61 C ANISOU 2935 C LYS A 301 8962 6924 6003 -577 -929 126 C ATOM 2936 O LYS A 301 -36.793 -25.191 1.829 1.00 63.78 O ANISOU 2936 O LYS A 301 9780 7728 6724 -629 -1005 162 O ATOM 2937 CB LYS A 301 -34.588 -27.392 2.835 1.00 57.96 C ANISOU 2937 CB LYS A 301 9073 6860 6089 -575 -951 98 C ATOM 2938 CG LYS A 301 -33.930 -28.626 2.241 1.00 74.46 C ANISOU 2938 CG LYS A 301 11292 8841 8160 -561 -948 61 C ATOM 2939 CD LYS A 301 -33.501 -29.634 3.290 1.00 76.75 C ANISOU 2939 CD LYS A 301 11539 9118 8505 -562 -975 66 C ATOM 2940 CE LYS A 301 -32.575 -30.676 2.673 1.00 83.91 C ANISOU 2940 CE LYS A 301 12571 9912 9397 -523 -946 17 C ATOM 2941 NZ LYS A 301 -32.342 -31.848 3.561 1.00 81.00 N ANISOU 2941 NZ LYS A 301 12190 9518 9070 -535 -995 26 N ATOM 2942 N ILE A 302 -35.238 -24.244 3.149 1.00 62.44 N ANISOU 2942 N ILE A 302 9449 7601 6675 -541 -877 125 N ATOM 2943 CA ILE A 302 -36.143 -23.170 3.550 1.00 65.80 C ANISOU 2943 CA ILE A 302 9783 8123 7096 -554 -907 162 C ATOM 2944 C ILE A 302 -36.475 -22.284 2.357 1.00 64.24 C ANISOU 2944 C ILE A 302 9657 7912 6839 -548 -882 154 C ATOM 2945 O ILE A 302 -37.634 -21.912 2.141 1.00 65.99 O ANISOU 2945 O ILE A 302 9875 8186 7013 -584 -946 192 O ATOM 2946 CB ILE A 302 -35.528 -22.349 4.699 1.00 54.58 C ANISOU 2946 CB ILE A 302 8223 6762 5752 -510 -853 154 C ATOM 2947 CG1 ILE A 302 -35.404 -23.203 5.960 1.00 55.58 C ANISOU 2947 CG1 ILE A 302 8268 6918 5933 -523 -892 171 C ATOM 2948 CG2 ILE A 302 -36.371 -21.111 4.978 1.00 52.67 C ANISOU 2948 CG2 ILE A 302 7901 6611 5499 -510 -874 184 C ATOM 2949 CD1 ILE A 302 -34.450 -22.634 6.987 1.00 51.01 C ANISOU 2949 CD1 ILE A 302 7575 6371 5435 -472 -823 150 C ATOM 2950 N ILE A 303 -35.461 -21.929 1.567 1.00 61.90 N ANISOU 2950 N ILE A 303 9424 7552 6544 -501 -788 107 N ATOM 2951 CA ILE A 303 -35.671 -21.010 0.455 1.00 69.74 C ANISOU 2951 CA ILE A 303 10479 8533 7484 -490 -756 100 C ATOM 2952 C ILE A 303 -36.492 -21.674 -0.644 1.00 76.61 C ANISOU 2952 C ILE A 303 11476 9362 8271 -536 -819 112 C ATOM 2953 O ILE A 303 -37.367 -21.043 -1.250 1.00 78.32 O ANISOU 2953 O ILE A 303 11717 9607 8434 -557 -850 135 O ATOM 2954 CB ILE A 303 -34.312 -20.507 -0.066 1.00 67.64 C ANISOU 2954 CB ILE A 303 10243 8215 7243 -431 -638 51 C ATOM 2955 CG1 ILE A 303 -33.649 -19.610 0.983 1.00 62.58 C ANISOU 2955 CG1 ILE A 303 9473 7626 6680 -392 -583 46 C ATOM 2956 CG2 ILE A 303 -34.483 -19.763 -1.381 1.00 65.50 C ANISOU 2956 CG2 ILE A 303 10059 7918 6909 -425 -607 43 C ATOM 2957 CD1 ILE A 303 -32.138 -19.567 0.885 1.00 65.47 C ANISOU 2957 CD1 ILE A 303 9843 7943 7089 -340 -477 2 C ATOM 2958 N ARG A 304 -36.236 -22.955 -0.915 1.00 76.18 N ANISOU 2958 N ARG A 304 11506 9239 8201 -552 -843 97 N ATOM 2959 CA ARG A 304 -36.948 -23.637 -1.992 1.00 82.24 C ANISOU 2959 CA ARG A 304 12404 9956 8887 -595 -904 105 C ATOM 2960 C ARG A 304 -38.432 -23.769 -1.675 1.00 84.76 C ANISOU 2960 C ARG A 304 12690 10342 9171 -665 -1020 165 C ATOM 2961 O ARG A 304 -39.287 -23.431 -2.502 1.00101.23 O ANISOU 2961 O ARG A 304 14819 12438 11206 -691 -1049 184 O ATOM 2962 CB ARG A 304 -36.324 -25.010 -2.247 1.00 76.78 C ANISOU 2962 CB ARG A 304 11810 9174 8190 -592 -909 74 C ATOM 2963 CG ARG A 304 -34.936 -24.949 -2.871 1.00 87.76 C ANISOU 2963 CG ARG A 304 13260 10495 9591 -522 -797 15 C ATOM 2964 CD ARG A 304 -34.348 -26.338 -3.074 1.00 96.59 C ANISOU 2964 CD ARG A 304 14473 11525 10701 -512 -808 -16 C ATOM 2965 NE ARG A 304 -32.979 -26.283 -3.575 1.00111.36 N ANISOU 2965 NE ARG A 304 16387 13342 12583 -437 -697 -71 N ATOM 2966 CZ ARG A 304 -32.202 -27.343 -3.753 1.00118.22 C ANISOU 2966 CZ ARG A 304 17333 14136 13450 -404 -680 -107 C ATOM 2967 NH1 ARG A 304 -32.627 -28.567 -3.486 1.00119.25 N ANISOU 2967 NH1 ARG A 304 17514 14226 13569 -442 -769 -97 N ATOM 2968 NH2 ARG A 304 -30.964 -27.169 -4.208 1.00112.46 N ANISOU 2968 NH2 ARG A 304 16629 13373 12727 -332 -574 -153 N ATOM 2969 N SER A 305 -38.761 -24.259 -0.478 1.00 82.53 N ANISOU 2969 N SER A 305 12315 10111 8930 -693 -1078 198 N ATOM 2970 CA SER A 305 -40.164 -24.421 -0.113 1.00 86.01 C ANISOU 2970 CA SER A 305 12669 10622 9389 -746 -1156 255 C ATOM 2971 C SER A 305 -40.882 -23.078 -0.064 1.00 98.08 C ANISOU 2971 C SER A 305 14097 12239 10930 -728 -1135 277 C ATOM 2972 O SER A 305 -42.040 -22.970 -0.483 1.00112.71 O ANISOU 2972 O SER A 305 15916 14125 12783 -753 -1163 307 O ATOM 2973 CB SER A 305 -40.277 -25.141 1.232 1.00 87.58 C ANISOU 2973 CB SER A 305 12767 10864 9647 -769 -1204 285 C ATOM 2974 OG SER A 305 -39.564 -24.453 2.245 1.00 86.09 O ANISOU 2974 OG SER A 305 12496 10728 9486 -731 -1171 276 O ATOM 2975 N HIS A 306 -40.213 -22.043 0.438 1.00 99.11 N ANISOU 2975 N HIS A 306 14183 12407 11069 -683 -1086 262 N ATOM 2976 CA HIS A 306 -40.818 -20.719 0.555 1.00 99.77 C ANISOU 2976 CA HIS A 306 14174 12569 11163 -658 -1067 279 C ATOM 2977 C HIS A 306 -40.095 -19.717 -0.338 1.00 94.49 C ANISOU 2977 C HIS A 306 13594 11859 10447 -619 -999 243 C ATOM 2978 O HIS A 306 -40.181 -18.508 -0.127 1.00 96.45 O ANISOU 2978 O HIS A 306 13782 12160 10703 -587 -973 247 O ATOM 2979 CB HIS A 306 -40.790 -20.242 2.010 1.00 95.76 C ANISOU 2979 CB HIS A 306 13521 12151 10711 -637 -1073 297 C ATOM 2980 CG HIS A 306 -40.882 -21.351 3.011 1.00 97.47 C ANISOU 2980 CG HIS A 306 13675 12386 10973 -666 -1120 318 C ATOM 2981 ND1 HIS A 306 -41.974 -22.188 3.098 1.00102.09 N ANISOU 2981 ND1 HIS A 306 14218 12994 11579 -709 -1172 354 N ATOM 2982 CD2 HIS A 306 -40.017 -21.762 3.968 1.00 95.49 C ANISOU 2982 CD2 HIS A 306 13398 12133 10750 -660 -1121 308 C ATOM 2983 CE1 HIS A 306 -41.777 -23.067 4.065 1.00104.73 C ANISOU 2983 CE1 HIS A 306 14503 13338 11953 -728 -1202 368 C ATOM 2984 NE2 HIS A 306 -40.597 -22.829 4.609 1.00103.18 N ANISOU 2984 NE2 HIS A 306 14313 13127 11763 -698 -1174 340 N TER 2985 HIS A 306 HETATM 2986 C02 TKO A3001 -19.327 7.614 18.208 1.00 25.38 C HETATM 2987 C04 TKO A3001 -20.097 5.352 18.453 1.00 31.86 C HETATM 2988 C05 TKO A3001 -19.795 3.948 18.994 1.00 31.77 C HETATM 2989 C06 TKO A3001 -20.603 2.914 19.428 1.00 34.70 C HETATM 2990 C07 TKO A3001 -19.768 1.817 19.829 1.00 43.71 C HETATM 2991 C08 TKO A3001 -18.494 2.244 19.617 1.00 39.02 C HETATM 2992 C10 TKO A3001 -21.319 5.715 17.730 1.00 32.18 C HETATM 2993 C11 TKO A3001 -22.385 4.825 17.440 1.00 31.99 C HETATM 2994 C12 TKO A3001 -23.497 5.255 16.759 1.00 44.02 C HETATM 2995 C14 TKO A3001 -23.639 6.584 16.313 1.00 35.02 C HETATM 2996 C15 TKO A3001 -22.620 7.479 16.578 1.00 39.30 C HETATM 2997 C16 TKO A3001 -21.437 7.072 17.291 1.00 33.02 C HETATM 2998 N01 TKO A3001 -18.268 8.531 18.481 1.00 38.96 N HETATM 2999 N03 TKO A3001 -19.150 6.266 18.677 1.00 29.50 N HETATM 3000 N17 TKO A3001 -20.429 8.017 17.536 1.00 32.16 N HETATM 3001 O09 TKO A3001 -18.467 3.526 19.113 1.00 34.39 O HETATM 3002 BR13 TKO A3001 -24.950 4.000 16.371 1.00 69.52 BR HETATM 3003 C1 CLR A3002 -8.302 10.842 13.189 1.00 44.68 C HETATM 3004 C2 CLR A3002 -8.311 12.365 13.169 1.00 46.15 C HETATM 3005 C3 CLR A3002 -6.906 12.910 12.953 1.00 50.00 C HETATM 3006 C4 CLR A3002 -6.374 12.418 11.616 1.00 53.35 C HETATM 3007 C5 CLR A3002 -6.456 10.914 11.541 1.00 49.43 C HETATM 3008 C6 CLR A3002 -5.358 10.249 11.139 1.00 43.10 C HETATM 3009 C7 CLR A3002 -5.307 8.750 10.964 1.00 47.87 C HETATM 3010 C8 CLR A3002 -6.695 8.129 10.992 1.00 47.68 C HETATM 3011 C9 CLR A3002 -7.535 8.735 12.112 1.00 41.87 C HETATM 3012 C10 CLR A3002 -7.760 10.235 11.896 1.00 51.63 C HETATM 3013 C11 CLR A3002 -8.848 7.972 12.325 1.00 40.56 C HETATM 3014 C12 CLR A3002 -8.676 6.452 12.442 1.00 44.63 C HETATM 3015 C13 CLR A3002 -7.905 5.890 11.261 1.00 40.92 C HETATM 3016 C14 CLR A3002 -6.578 6.635 11.233 1.00 51.39 C HETATM 3017 C15 CLR A3002 -5.710 5.852 10.257 1.00 50.68 C HETATM 3018 C16 CLR A3002 -6.167 4.407 10.451 1.00 45.87 C HETATM 3019 C17 CLR A3002 -7.419 4.440 11.349 1.00 48.13 C HETATM 3020 C18 CLR A3002 -8.700 6.084 9.968 1.00 46.07 C HETATM 3021 C19 CLR A3002 -8.747 10.516 10.765 1.00 59.77 C HETATM 3022 C20 CLR A3002 -8.397 3.318 10.975 1.00 50.57 C HETATM 3023 C21 CLR A3002 -9.564 3.209 11.953 1.00 42.56 C HETATM 3024 C22 CLR A3002 -7.619 2.004 10.857 1.00 49.95 C HETATM 3025 C23 CLR A3002 -8.372 0.754 11.306 1.00 43.26 C HETATM 3026 C24 CLR A3002 -7.491 -0.473 11.086 1.00 45.63 C HETATM 3027 C25 CLR A3002 -8.199 -1.803 11.339 1.00 53.59 C HETATM 3028 C26 CLR A3002 -9.251 -1.706 12.439 1.00 50.12 C HETATM 3029 C27 CLR A3002 -8.809 -2.345 10.052 1.00 62.58 C HETATM 3030 O1 CLR A3002 -6.925 14.342 12.948 1.00 52.95 O HETATM 3031 C1 CLR A3003 -3.015 8.370 21.285 1.00 37.61 C HETATM 3032 C2 CLR A3003 -2.853 9.882 21.201 1.00 41.05 C HETATM 3033 C3 CLR A3003 -1.907 10.280 20.080 1.00 40.19 C HETATM 3034 C4 CLR A3003 -2.426 9.745 18.752 1.00 52.40 C HETATM 3035 C5 CLR A3003 -2.687 8.260 18.858 1.00 46.25 C HETATM 3036 C6 CLR A3003 -2.133 7.460 17.930 1.00 43.94 C HETATM 3037 C7 CLR A3003 -2.334 5.963 17.895 1.00 39.71 C HETATM 3038 C8 CLR A3003 -3.513 5.547 18.759 1.00 40.48 C HETATM 3039 C9 CLR A3003 -3.490 6.237 20.118 1.00 41.27 C HETATM 3040 C10 CLR A3003 -3.554 7.763 19.992 1.00 43.10 C HETATM 3041 C11 CLR A3003 -4.581 5.682 21.050 1.00 42.24 C HETATM 3042 C12 CLR A3003 -4.613 4.152 21.156 1.00 43.15 C HETATM 3043 C13 CLR A3003 -4.648 3.501 19.785 1.00 47.09 C HETATM 3044 C14 CLR A3003 -3.456 4.052 19.015 1.00 41.77 C HETATM 3045 C15 CLR A3003 -3.321 3.155 17.794 1.00 42.51 C HETATM 3046 C16 CLR A3003 -3.789 1.790 18.300 1.00 48.47 C HETATM 3047 C17 CLR A3003 -4.368 1.994 19.710 1.00 52.73 C HETATM 3048 C18 CLR A3003 -5.982 3.824 19.105 1.00 41.69 C HETATM 3049 C19 CLR A3003 -4.982 8.255 19.742 1.00 36.57 C HETATM 3050 C20 CLR A3003 -5.533 1.046 20.015 1.00 49.56 C HETATM 3051 C21 CLR A3003 -5.908 1.131 21.494 1.00 41.06 C HETATM 3052 C22 CLR A3003 -5.202 -0.401 19.636 1.00 50.68 C HETATM 3053 C23 CLR A3003 -6.376 -1.351 19.866 1.00 59.32 C HETATM 3054 C24 CLR A3003 -5.893 -2.721 20.330 1.00 55.87 C HETATM 3055 C25 CLR A3003 -5.333 -3.575 19.199 1.00 54.75 C HETATM 3056 C26 CLR A3003 -4.794 -4.888 19.757 1.00 56.28 C HETATM 3057 C27 CLR A3003 -6.373 -3.852 18.120 1.00 55.86 C HETATM 3058 O1 CLR A3003 -1.816 11.707 20.034 1.00 41.54 O HETATM 3059 C1 CLR A3004 -38.330 10.563 21.833 1.00 45.31 C HETATM 3060 C2 CLR A3004 -37.955 12.021 22.066 1.00 45.16 C HETATM 3061 C3 CLR A3004 -38.262 12.413 23.502 1.00 47.08 C HETATM 3062 C4 CLR A3004 -37.411 11.564 24.435 1.00 41.49 C HETATM 3063 C5 CLR A3004 -37.604 10.091 24.153 1.00 42.62 C HETATM 3064 C6 CLR A3004 -37.783 9.279 25.209 1.00 41.47 C HETATM 3065 C7 CLR A3004 -37.939 7.779 25.110 1.00 49.73 C HETATM 3066 C8 CLR A3004 -37.743 7.248 23.698 1.00 51.16 C HETATM 3067 C9 CLR A3004 -38.231 8.215 22.624 1.00 45.06 C HETATM 3068 C10 CLR A3004 -37.563 9.591 22.727 1.00 46.10 C HETATM 3069 C11 CLR A3004 -38.080 7.581 21.235 1.00 45.58 C HETATM 3070 C12 CLR A3004 -38.769 6.218 21.100 1.00 45.46 C HETATM 3071 C13 CLR A3004 -38.325 5.261 22.192 1.00 45.46 C HETATM 3072 C14 CLR A3004 -38.539 5.966 23.524 1.00 45.47 C HETATM 3073 C15 CLR A3004 -38.344 4.875 24.569 1.00 47.31 C HETATM 3074 C16 CLR A3004 -38.901 3.628 23.873 1.00 51.29 C HETATM 3075 C17 CLR A3004 -39.174 4.006 22.405 1.00 50.64 C HETATM 3076 C18 CLR A3004 -36.861 4.858 21.988 1.00 51.88 C HETATM 3077 C19 CLR A3004 -36.099 9.551 22.302 1.00 46.17 C HETATM 3078 C20 CLR A3004 -38.955 2.827 21.456 1.00 50.26 C HETATM 3079 C21 CLR A3004 -39.057 3.246 19.993 1.00 43.47 C HETATM 3080 C22 CLR A3004 -39.986 1.730 21.733 1.00 50.98 C HETATM 3081 C23 CLR A3004 -39.560 0.363 21.209 1.00 54.69 C HETATM 3082 C24 CLR A3004 -40.714 -0.628 21.329 1.00 61.31 C HETATM 3083 C25 CLR A3004 -40.255 -2.063 21.096 1.00 67.16 C HETATM 3084 C26 CLR A3004 -41.095 -3.047 21.898 1.00 65.90 C HETATM 3085 C27 CLR A3004 -40.314 -2.405 19.613 1.00 59.75 C HETATM 3086 O1 CLR A3004 -37.971 13.801 23.700 1.00 55.25 O HETATM 3087 C10 OLC A3005 -38.102 3.456 15.006 1.00 45.92 C HETATM 3088 C9 OLC A3005 -37.769 4.706 15.345 1.00 50.17 C HETATM 3089 C11 OLC A3005 -38.669 2.470 15.966 1.00 50.33 C HETATM 3090 C8 OLC A3005 -37.925 5.259 16.723 1.00 47.45 C HETATM 3091 C24 OLC A3005 -39.732 17.373 18.710 1.00 83.59 C HETATM 3092 C16 OLC A3005 -41.006 -3.354 15.563 1.00 52.97 C HETATM 3093 C12 OLC A3005 -39.082 1.213 15.199 1.00 52.91 C HETATM 3094 C7 OLC A3005 -36.810 6.268 17.001 1.00 55.26 C HETATM 3095 C15 OLC A3005 -40.523 -2.144 16.358 1.00 57.76 C HETATM 3096 C13 OLC A3005 -39.852 0.267 16.126 1.00 61.56 C HETATM 3097 C6 OLC A3005 -37.361 7.502 17.728 1.00 46.91 C HETATM 3098 C14 OLC A3005 -40.180 -1.022 15.383 1.00 62.76 C HETATM 3099 C5 OLC A3005 -37.836 8.543 16.725 1.00 44.01 C HETATM 3100 C4 OLC A3005 -37.999 9.920 17.393 1.00 48.66 C HETATM 3101 C3 OLC A3005 -38.864 10.763 16.469 1.00 56.30 C HETATM 3102 C2 OLC A3005 -38.426 12.228 16.370 1.00 58.25 C HETATM 3103 C21 OLC A3005 -40.257 15.054 17.922 1.00 62.35 C HETATM 3104 C1 OLC A3005 -39.182 12.990 17.404 1.00 62.60 C HETATM 3105 C22 OLC A3005 -39.323 15.880 18.841 1.00 64.83 C HETATM 3106 O19 OLC A3005 -39.608 12.571 18.472 1.00 59.61 O HETATM 3107 O25 OLC A3005 -39.050 18.025 19.744 1.00 79.78 O HETATM 3108 O23 OLC A3005 -39.414 15.448 20.151 1.00 76.62 O HETATM 3109 O20 OLC A3005 -39.382 14.309 17.079 1.00 68.80 O HETATM 3110 C9 OLC A3006 -35.064 -11.104 18.359 1.00 45.74 C HETATM 3111 C8 OLC A3006 -35.885 -12.261 17.921 1.00 43.66 C HETATM 3112 C24 OLC A3006 -33.794 -24.606 20.231 1.00 75.95 C HETATM 3113 C7 OLC A3006 -35.599 -13.472 18.796 1.00 51.81 C HETATM 3114 C6 OLC A3006 -35.200 -14.639 17.904 1.00 49.84 C HETATM 3115 C5 OLC A3006 -35.039 -15.898 18.735 1.00 50.30 C HETATM 3116 C4 OLC A3006 -35.796 -17.045 18.085 1.00 57.18 C HETATM 3117 C3 OLC A3006 -35.231 -18.352 18.600 1.00 57.23 C HETATM 3118 C2 OLC A3006 -35.781 -19.523 17.795 1.00 63.09 C HETATM 3119 C21 OLC A3006 -33.987 -22.547 18.847 1.00 60.94 C HETATM 3120 C1 OLC A3006 -34.746 -20.594 17.839 1.00 69.14 C HETATM 3121 C22 OLC A3006 -34.799 -23.678 19.504 1.00 77.50 C HETATM 3122 O19 OLC A3006 -33.872 -20.803 17.010 1.00 67.43 O HETATM 3123 O25 OLC A3006 -34.599 -25.496 20.944 1.00 80.49 O HETATM 3124 O23 OLC A3006 -35.748 -23.171 20.375 1.00 89.79 O HETATM 3125 O20 OLC A3006 -34.826 -21.411 18.924 1.00 74.93 O HETATM 3126 C10 OLC A3007 -3.101 2.207 24.031 1.00 59.88 C HETATM 3127 C9 OLC A3007 -2.882 3.500 24.279 1.00 59.66 C HETATM 3128 C11 OLC A3007 -3.966 1.332 24.865 1.00 65.14 C HETATM 3129 C8 OLC A3007 -3.472 4.250 25.418 1.00 49.18 C HETATM 3130 C24 OLC A3007 -3.299 17.022 25.663 1.00 81.16 C HETATM 3131 C12 OLC A3007 -3.787 -0.109 24.365 1.00 67.20 C HETATM 3132 C7 OLC A3007 -3.429 5.754 25.076 1.00 39.16 C HETATM 3133 C13 OLC A3007 -4.878 -1.006 24.912 1.00 61.15 C HETATM 3134 C6 OLC A3007 -3.343 6.595 26.329 1.00 49.00 C HETATM 3135 C14 OLC A3007 -4.472 -2.460 24.699 1.00 72.46 C HETATM 3136 C5 OLC A3007 -2.165 7.539 26.227 1.00 40.14 C HETATM 3137 C4 OLC A3007 -2.483 8.714 25.308 1.00 34.37 C HETATM 3138 C3 OLC A3007 -2.219 10.005 26.063 1.00 38.06 C HETATM 3139 C2 OLC A3007 -2.363 11.220 25.151 1.00 49.39 C HETATM 3140 C21 OLC A3007 -2.949 14.550 25.740 1.00 64.51 C HETATM 3141 C1 OLC A3007 -2.021 12.406 25.987 1.00 56.73 C HETATM 3142 C22 OLC A3007 -2.624 15.832 24.936 1.00 68.94 C HETATM 3143 O19 OLC A3007 -1.771 12.408 27.184 1.00 64.37 O HETATM 3144 O25 OLC A3007 -3.081 18.115 24.821 1.00 70.68 O HETATM 3145 O23 OLC A3007 -1.258 16.021 24.820 1.00 68.30 O HETATM 3146 O20 OLC A3007 -1.990 13.592 25.308 1.00 59.91 O HETATM 3147 C10 OLC A3008 -33.558 -10.350 23.251 1.00 55.52 C HETATM 3148 C9 OLC A3008 -33.692 -11.566 22.710 1.00 55.31 C HETATM 3149 C11 OLC A3008 -33.548 -10.126 24.721 1.00 54.54 C HETATM 3150 C8 OLC A3008 -33.851 -12.808 23.523 1.00 51.34 C HETATM 3151 C24 OLC A3008 -32.980 -24.543 24.393 1.00 74.15 C HETATM 3152 C12 OLC A3008 -33.443 -8.642 25.024 1.00 51.89 C HETATM 3153 C7 OLC A3008 -32.788 -13.821 23.135 1.00 48.23 C HETATM 3154 C13 OLC A3008 -34.671 -7.943 24.481 1.00 52.36 C HETATM 3155 C6 OLC A3008 -33.422 -14.923 22.303 1.00 57.77 C HETATM 3156 C5 OLC A3008 -32.393 -15.996 22.016 1.00 51.02 C HETATM 3157 C4 OLC A3008 -32.565 -17.159 22.976 1.00 49.98 C HETATM 3158 C3 OLC A3008 -31.463 -18.155 22.708 1.00 55.77 C HETATM 3159 C2 OLC A3008 -31.643 -19.400 23.556 1.00 65.73 C HETATM 3160 C21 OLC A3008 -33.388 -22.132 23.906 1.00 71.52 C HETATM 3161 C1 OLC A3008 -32.538 -20.293 22.769 1.00 76.26 C HETATM 3162 C22 OLC A3008 -32.635 -23.098 24.838 1.00 72.28 C HETATM 3163 O19 OLC A3008 -33.356 -19.958 21.924 1.00 81.23 O HETATM 3164 O25 OLC A3008 -32.323 -25.361 25.317 1.00 76.27 O HETATM 3165 O23 OLC A3008 -31.271 -22.863 24.792 1.00 75.79 O HETATM 3166 O20 OLC A3008 -32.390 -21.616 23.051 1.00 74.64 O HETATM 3167 C1 OLA A3009 -21.414 12.480 3.144 1.00 77.47 C HETATM 3168 O1 OLA A3009 -21.184 13.027 2.040 1.00 76.15 O HETATM 3169 O2 OLA A3009 -21.300 13.159 4.191 1.00 65.30 O HETATM 3170 C2 OLA A3009 -21.828 11.007 3.209 1.00 58.96 C HETATM 3171 C3 OLA A3009 -20.749 10.112 2.601 1.00 60.87 C HETATM 3172 C4 OLA A3009 -21.110 8.632 2.718 1.00 56.17 C HETATM 3173 C5 OLA A3009 -21.026 8.154 4.166 1.00 64.44 C HETATM 3174 C6 OLA A3009 -20.695 6.665 4.245 1.00 50.82 C HETATM 3175 C7 OLA A3009 -21.937 5.803 4.027 1.00 46.86 C HETATM 3176 C8 OLA A3009 -21.560 4.459 3.427 1.00 52.46 C HETATM 3177 C9 OLA A3009 -21.448 4.569 1.925 1.00 58.92 C HETATM 3178 C10 OLA A3009 -20.758 3.694 1.189 1.00 49.02 C HETATM 3179 C11 OLA A3009 -20.030 2.520 1.794 1.00 58.87 C HETATM 3180 C12 OLA A3009 -20.975 1.471 2.354 1.00 60.40 C HETATM 3181 C13 OLA A3009 -20.400 0.062 2.187 1.00 68.02 C HETATM 3182 C14 OLA A3009 -20.588 -0.786 3.446 1.00 68.08 C HETATM 3183 C15 OLA A3009 -19.425 -0.603 4.419 1.00 59.40 C HETATM 3184 C16 OLA A3009 -18.225 -1.457 4.014 1.00 61.88 C HETATM 3185 C1 OLA A3010 -36.639 14.590 13.082 1.00 75.32 C HETATM 3186 O1 OLA A3010 -35.881 15.583 12.982 1.00 73.30 O HETATM 3187 O2 OLA A3010 -37.646 14.677 13.820 1.00 73.23 O HETATM 3188 C2 OLA A3010 -36.350 13.292 12.318 1.00 62.92 C HETATM 3189 C3 OLA A3010 -35.966 12.164 13.275 1.00 60.59 C HETATM 3190 C4 OLA A3010 -35.814 10.827 12.548 1.00 49.39 C HETATM 3191 C5 OLA A3010 -37.171 10.192 12.256 1.00 51.77 C HETATM 3192 C6 OLA A3010 -37.162 8.687 12.530 1.00 45.43 C HETATM 3193 C7 OLA A3010 -36.355 7.935 11.475 1.00 43.26 C HETATM 3194 C8 OLA A3010 -36.651 6.443 11.500 1.00 46.66 C HETATM 3195 C9 OLA A3010 -36.240 5.805 10.195 1.00 55.29 C HETATM 3196 C10 OLA A3010 -36.718 4.623 9.802 1.00 52.66 C HETATM 3197 C11 OLA A3010 -37.703 3.847 10.640 1.00 61.83 C HETATM 3198 C12 OLA A3010 -37.924 2.459 10.061 1.00 59.05 C HETATM 3199 C13 OLA A3010 -39.006 1.696 10.828 1.00 64.82 C HETATM 3200 C14 OLA A3010 -38.543 0.289 11.217 1.00 69.60 C HETATM 3201 C15 OLA A3010 -39.718 -0.542 11.735 1.00 67.67 C HETATM 3202 C16 OLA A3010 -39.291 -1.954 12.142 1.00 53.24 C HETATM 3203 C17 OLA A3010 -39.375 -2.933 10.972 1.00 58.45 C HETATM 3204 C18 OLA A3010 -39.673 -4.336 11.466 1.00 73.48 C HETATM 3205 C1 OLA A3011 -33.821 13.939 8.146 1.00 88.35 C HETATM 3206 O1 OLA A3011 -32.707 14.468 7.923 1.00 81.20 O HETATM 3207 O2 OLA A3011 -34.806 14.677 8.380 1.00 87.85 O HETATM 3208 C2 OLA A3011 -33.980 12.417 8.135 1.00 77.60 C HETATM 3209 C3 OLA A3011 -35.401 12.014 8.527 1.00 73.54 C HETATM 3210 C4 OLA A3011 -35.555 10.494 8.568 1.00 69.27 C HETATM 3211 C5 OLA A3011 -35.893 9.934 7.188 1.00 63.28 C HETATM 3212 C6 OLA A3011 -35.805 8.410 7.179 1.00 61.18 C HETATM 3213 C7 OLA A3011 -36.130 7.851 5.795 1.00 64.00 C HETATM 3214 C8 OLA A3011 -37.132 6.715 5.888 1.00 64.32 C HETATM 3215 C9 OLA A3011 -37.548 6.242 4.518 1.00 61.52 C HETATM 3216 C1 OLA A3012 -20.530 -22.574 28.275 1.00 59.57 C HETATM 3217 O1 OLA A3012 -20.846 -22.350 27.085 1.00 60.40 O HETATM 3218 O2 OLA A3012 -20.782 -23.698 28.767 1.00 72.52 O HETATM 3219 C2 OLA A3012 -19.847 -21.496 29.119 1.00 53.03 C HETATM 3220 C3 OLA A3012 -20.360 -20.107 28.751 1.00 50.45 C HETATM 3221 C4 OLA A3012 -19.487 -19.015 29.371 1.00 43.05 C HETATM 3222 C5 OLA A3012 -20.223 -17.676 29.388 1.00 54.49 C HETATM 3223 C6 OLA A3012 -19.296 -16.525 29.006 1.00 48.58 C HETATM 3224 C7 OLA A3012 -19.858 -15.191 29.493 1.00 42.30 C HETATM 3225 C1 OLA A3013 -33.671 -16.881 27.026 1.00 70.42 C HETATM 3226 O1 OLA A3013 -32.703 -17.558 26.608 1.00 66.79 O HETATM 3227 O2 OLA A3013 -34.479 -17.412 27.820 1.00 74.64 O HETATM 3228 C2 OLA A3013 -33.867 -15.431 26.574 1.00 57.44 C HETATM 3229 C3 OLA A3013 -33.048 -14.468 27.431 1.00 55.32 C HETATM 3230 C4 OLA A3013 -33.471 -13.016 27.196 1.00 54.64 C HETATM 3231 C5 OLA A3013 -33.548 -12.245 28.514 1.00 59.20 C HETATM 3232 C6 OLA A3013 -33.821 -10.756 28.288 1.00 56.31 C HETATM 3233 C7 OLA A3013 -34.231 -10.066 29.589 1.00 49.82 C HETATM 3234 C8 OLA A3013 -34.175 -8.552 29.464 1.00 56.44 C HETATM 3235 C9 OLA A3013 -32.805 -8.050 29.843 1.00 54.27 C HETATM 3236 C10 OLA A3013 -32.609 -6.928 30.544 1.00 57.49 C HETATM 3237 C11 OLA A3013 -33.734 -6.045 31.030 1.00 54.92 C HETATM 3238 C12 OLA A3013 -33.186 -4.812 31.738 1.00 61.53 C HETATM 3239 C13 OLA A3013 -32.391 -5.175 32.997 1.00 59.69 C HETATM 3240 C14 OLA A3013 -32.002 -3.929 33.798 1.00 55.66 C HETATM 3241 C15 OLA A3013 -30.570 -3.480 33.504 1.00 53.65 C HETATM 3242 C16 OLA A3013 -30.316 -2.059 34.007 1.00 60.29 C HETATM 3243 C17 OLA A3013 -30.757 -1.025 32.972 1.00 56.44 C HETATM 3244 C18 OLA A3013 -31.044 0.319 33.614 1.00 49.11 C HETATM 3245 C1 OLA A3014 -27.442 -21.213 39.708 1.00 81.12 C HETATM 3246 O1 OLA A3014 -26.490 -22.031 39.719 1.00 72.71 O HETATM 3247 O2 OLA A3014 -28.598 -21.630 39.947 1.00 70.11 O HETATM 3248 C2 OLA A3014 -27.203 -19.731 39.405 1.00 78.45 C HETATM 3249 C3 OLA A3014 -27.927 -18.842 40.417 1.00 80.00 C HETATM 3250 C4 OLA A3014 -28.027 -17.394 39.929 1.00 72.43 C HETATM 3251 C5 OLA A3014 -26.667 -16.697 39.936 1.00 61.64 C HETATM 3252 C6 OLA A3014 -26.253 -16.285 38.524 1.00 71.65 C HETATM 3253 C7 OLA A3014 -24.897 -15.576 38.522 1.00 65.74 C HETATM 3254 C8 OLA A3014 -25.030 -14.062 38.569 1.00 58.90 C HETATM 3255 C9 OLA A3014 -23.662 -13.433 38.676 1.00 64.30 C HETATM 3256 C10 OLA A3014 -23.488 -12.124 38.876 1.00 66.44 C HETATM 3257 C11 OLA A3014 -24.644 -11.164 39.014 1.00 59.24 C HETATM 3258 C12 OLA A3014 -24.179 -9.866 39.659 1.00 66.30 C HETATM 3259 C13 OLA A3014 -23.706 -8.841 38.627 1.00 73.06 C HETATM 3260 C14 OLA A3014 -22.985 -7.667 39.296 1.00 52.01 C HETATM 3261 C15 OLA A3014 -23.325 -6.333 38.627 1.00 59.31 C HETATM 3262 C16 OLA A3014 -22.540 -6.111 37.334 1.00 58.01 C HETATM 3263 C17 OLA A3014 -23.121 -4.928 36.558 1.00 58.62 C HETATM 3264 C18 OLA A3014 -22.032 -4.119 35.878 1.00 50.47 C HETATM 3265 C7 OLA A3015 -21.149 -11.707 1.159 1.00 63.50 C HETATM 3266 C8 OLA A3015 -21.009 -10.322 1.769 1.00 68.69 C HETATM 3267 C9 OLA A3015 -21.691 -10.249 3.113 1.00 60.54 C HETATM 3268 C10 OLA A3015 -21.740 -9.100 3.783 1.00 53.85 C HETATM 3269 C11 OLA A3015 -21.115 -7.853 3.211 1.00 51.25 C HETATM 3270 C12 OLA A3015 -22.128 -7.053 2.415 1.00 57.27 C HETATM 3271 C13 OLA A3015 -22.631 -5.848 3.207 1.00 49.92 C HETATM 3272 C14 OLA A3015 -22.962 -4.697 2.260 1.00 38.27 C HETATM 3273 C15 OLA A3015 -24.252 -4.001 2.688 1.00 47.39 C HETATM 3274 C16 OLA A3015 -24.484 -2.719 1.892 1.00 49.87 C HETATM 3275 C17 OLA A3015 -23.313 -1.751 2.045 1.00 60.51 C HETATM 3276 C1 OLA A3016 -15.448 12.576 0.737 1.00 58.73 C HETATM 3277 O1 OLA A3016 -14.333 13.128 0.583 1.00 68.05 O HETATM 3278 O2 OLA A3016 -16.455 13.302 0.899 1.00 58.50 O HETATM 3279 C2 OLA A3016 -15.565 11.046 0.727 1.00 61.22 C HETATM 3280 C3 OLA A3016 -16.978 10.572 1.075 1.00 64.41 C HETATM 3281 C4 OLA A3016 -17.285 9.216 0.434 1.00 63.88 C HETATM 3282 C5 OLA A3016 -16.617 8.064 1.187 1.00 58.73 C HETATM 3283 C6 OLA A3016 -17.552 7.476 2.243 1.00 61.50 C HETATM 3284 C1 OLA A3017 -44.092 -24.235 13.300 1.00 72.19 C HETATM 3285 O1 OLA A3017 -44.608 -24.913 12.382 1.00 71.10 O HETATM 3286 O2 OLA A3017 -43.285 -24.788 14.082 1.00 71.71 O HETATM 3287 C2 OLA A3017 -44.453 -22.757 13.453 1.00 60.88 C HETATM 3288 C3 OLA A3017 -43.457 -22.003 14.331 1.00 73.26 C HETATM 3289 C4 OLA A3017 -43.694 -20.497 14.224 1.00 68.73 C HETATM 3290 C5 OLA A3017 -42.835 -19.730 15.225 1.00 74.14 C HETATM 3291 C7 OLA A3018 -39.175 -19.905 15.612 1.00 75.60 C HETATM 3292 C8 OLA A3018 -38.887 -18.445 15.321 1.00 70.16 C HETATM 3293 C9 OLA A3018 -37.766 -18.305 14.323 1.00 70.07 C HETATM 3294 C10 OLA A3018 -37.458 -17.109 13.825 1.00 67.45 C HETATM 3295 C11 OLA A3018 -38.230 -15.890 14.257 1.00 51.72 C HETATM 3296 C12 OLA A3018 -37.475 -14.617 13.919 1.00 52.96 C HETATM 3297 C13 OLA A3018 -37.837 -13.515 14.912 1.00 58.56 C HETATM 3298 C14 OLA A3018 -37.468 -12.131 14.380 1.00 56.66 C HETATM 3299 C15 OLA A3018 -38.649 -11.482 13.663 1.00 58.62 C HETATM 3300 C16 OLA A3018 -38.628 -9.966 13.853 1.00 56.95 C HETATM 3301 C17 OLA A3018 -38.965 -9.240 12.553 1.00 51.04 C HETATM 3302 C1 OLA A3019 -7.201 12.386 28.606 1.00 69.04 C HETATM 3303 O1 OLA A3019 -6.596 12.814 27.597 1.00 71.49 O HETATM 3304 O2 OLA A3019 -8.262 12.946 28.959 1.00 72.58 O HETATM 3305 C2 OLA A3019 -6.648 11.202 29.400 1.00 68.93 C HETATM 3306 C3 OLA A3019 -5.128 11.134 29.275 1.00 63.76 C HETATM 3307 C4 OLA A3019 -4.535 10.204 30.336 1.00 55.67 C HETATM 3308 C5 OLA A3019 -3.604 9.145 29.742 1.00 55.69 C HETATM 3309 C6 OLA A3019 -4.104 7.721 29.998 1.00 51.05 C HETATM 3310 C7 OLA A3019 -3.027 6.837 30.634 1.00 56.52 C HETATM 3311 C8 OLA A3019 -3.226 5.333 30.461 1.00 63.10 C HETATM 3312 C9 OLA A3019 -4.578 4.906 29.945 1.00 59.82 C HETATM 3313 C10 OLA A3019 -4.910 3.618 29.866 1.00 59.27 C HETATM 3314 C11 OLA A3019 -3.986 2.495 30.276 1.00 59.54 C HETATM 3315 C12 OLA A3019 -3.983 1.423 29.201 1.00 55.98 C HETATM 3316 C13 OLA A3019 -4.589 0.115 29.710 1.00 73.20 C HETATM 3317 C14 OLA A3019 -5.181 -0.695 28.559 1.00 73.15 C HETATM 3318 C15 OLA A3019 -6.130 -1.765 29.090 1.00 63.14 C HETATM 3319 C16 OLA A3019 -6.911 -2.394 27.941 1.00 52.48 C HETATM 3320 C17 OLA A3019 -6.105 -3.508 27.283 1.00 52.52 C HETATM 3321 C18 OLA A3019 -6.463 -4.851 27.886 1.00 65.40 C HETATM 3322 C1 OLA A3020 -31.926 7.990 36.524 1.00 62.89 C HETATM 3323 O1 OLA A3020 -31.042 8.876 36.491 1.00 67.15 O HETATM 3324 O2 OLA A3020 -33.129 8.336 36.551 1.00 60.93 O HETATM 3325 C2 OLA A3020 -31.542 6.509 36.529 1.00 46.80 C HETATM 3326 C3 OLA A3020 -32.620 5.663 37.203 1.00 48.10 C HETATM 3327 C4 OLA A3020 -32.469 4.188 36.838 1.00 49.62 C HETATM 3328 C5 OLA A3020 -32.088 3.341 38.051 1.00 42.38 C HETATM 3329 C6 OLA A3020 -31.958 1.871 37.652 1.00 45.53 C HETATM 3330 C7 OLA A3020 -31.319 1.033 38.757 1.00 45.32 C HETATM 3331 C8 OLA A3020 -30.439 -0.055 38.165 1.00 49.71 C HETATM 3332 C9 OLA A3020 -30.445 -1.288 39.032 1.00 41.17 C HETATM 3333 C1 OLA A3021 -8.285 15.462 7.892 1.00 85.81 C HETATM 3334 O1 OLA A3021 -8.193 16.106 6.822 1.00 78.79 O HETATM 3335 O2 OLA A3021 -7.635 15.843 8.892 1.00 88.08 O HETATM 3336 C2 OLA A3021 -9.173 14.222 7.979 1.00 66.04 C HETATM 3337 C3 OLA A3021 -8.378 12.985 7.576 1.00 57.35 C HETATM 3338 C4 OLA A3021 -9.298 11.838 7.170 1.00 62.05 C HETATM 3339 C5 OLA A3021 -8.479 10.614 6.768 1.00 57.55 C HETATM 3340 C6 OLA A3021 -9.342 9.626 5.990 1.00 53.68 C HETATM 3341 C7 OLA A3021 -8.858 8.188 6.175 1.00 48.70 C HETATM 3342 C8 OLA A3021 -9.733 7.251 5.366 1.00 66.02 C HETATM 3343 C9 OLA A3021 -9.362 5.808 5.584 1.00 64.76 C HETATM 3344 C10 OLA A3021 -10.032 4.849 4.945 1.00 77.16 C HETATM 3345 C11 OLA A3021 -11.161 5.195 4.003 1.00 64.41 C HETATM 3346 C12 OLA A3021 -11.897 3.948 3.547 1.00 78.62 C HETATM 3347 C13 OLA A3021 -11.062 3.142 2.553 1.00 87.24 C HETATM 3348 C14 OLA A3021 -10.709 1.760 3.107 1.00 87.50 C HETATM 3349 C15 OLA A3021 -9.579 1.122 2.299 1.00 85.22 C HETATM 3350 C16 OLA A3021 -9.337 -0.326 2.724 1.00 81.92 C HETATM 3351 C17 OLA A3021 -10.194 -1.289 1.905 1.00 90.37 C HETATM 3352 C18 OLA A3021 -10.444 -2.579 2.666 1.00 85.94 C HETATM 3353 C1 OLA A3022 -2.521 14.335 13.345 1.00 66.54 C HETATM 3354 O1 OLA A3022 -3.395 15.137 12.943 1.00 67.35 O HETATM 3355 O2 OLA A3022 -1.577 14.771 14.043 1.00 71.56 O HETATM 3356 C2 OLA A3022 -2.605 12.851 12.982 1.00 53.16 C HETATM 3357 C3 OLA A3022 -2.049 11.959 14.092 1.00 57.83 C HETATM 3358 C4 OLA A3022 -1.276 10.777 13.509 1.00 52.55 C HETATM 3359 C5 OLA A3022 -2.163 9.551 13.297 1.00 55.01 C HETATM 3360 C6 OLA A3022 -1.568 8.626 12.237 1.00 59.39 C HETATM 3361 C7 OLA A3022 -1.051 7.327 12.851 1.00 63.66 C HETATM 3362 C8 OLA A3022 -2.190 6.403 13.243 1.00 60.04 C HETATM 3363 C9 OLA A3022 -2.223 5.184 12.354 1.00 53.47 C HETATM 3364 C10 OLA A3022 -2.921 4.100 12.694 1.00 54.41 C HETATM 3365 C11 OLA A3022 -3.703 4.055 13.980 1.00 48.10 C HETATM 3366 C12 OLA A3022 -4.642 2.862 14.008 1.00 68.01 C HETATM 3367 C13 OLA A3022 -3.892 1.535 14.114 1.00 57.81 C HETATM 3368 C14 OLA A3022 -4.849 0.416 14.524 1.00 58.03 C HETATM 3369 C15 OLA A3022 -4.121 -0.916 14.697 1.00 70.58 C HETATM 3370 C1 OLA A3023 -34.500 11.402 3.388 1.00 79.14 C HETATM 3371 O1 OLA A3023 -35.671 11.699 3.058 1.00 79.93 O HETATM 3372 O2 OLA A3023 -33.778 12.276 3.919 1.00 82.97 O HETATM 3373 C2 OLA A3023 -33.957 9.992 3.145 1.00 64.07 C HETATM 3374 C3 OLA A3023 -34.439 9.449 1.803 1.00 60.32 C HETATM 3375 C4 OLA A3023 -34.087 7.973 1.663 1.00 51.95 C HETATM 3376 C5 OLA A3023 -35.153 7.246 0.850 1.00 58.76 C HETATM 3377 C6 OLA A3023 -35.230 5.786 1.270 1.00 50.95 C HETATM 3378 C7 OLA A3023 -34.068 5.002 0.661 1.00 53.89 C HETATM 3379 C8 OLA A3023 -34.543 3.683 0.071 1.00 56.17 C HETATM 3380 C9 OLA A3023 -34.470 2.584 1.121 1.00 57.26 C HETATM 3381 C10 OLA A3023 -33.635 1.547 1.053 1.00 52.99 C HETATM 3382 C11 OLA A3023 -32.700 1.421 -0.106 1.00 51.09 C HETATM 3383 C1 OLA A3024 -37.076 -19.151 22.475 1.00 85.95 C HETATM 3384 O1 OLA A3024 -38.020 -19.820 21.994 1.00 78.13 O HETATM 3385 O2 OLA A3024 -36.260 -19.722 23.233 1.00 84.93 O HETATM 3386 C2 OLA A3024 -36.922 -17.663 22.141 1.00 81.38 C HETATM 3387 C3 OLA A3024 -36.977 -16.812 23.408 1.00 83.06 C HETATM 3388 C4 OLA A3024 -37.917 -15.616 23.248 1.00 75.98 C HETATM 3389 C5 OLA A3024 -37.356 -14.579 22.276 1.00 80.67 C HETATM 3390 C6 OLA A3024 -37.663 -13.155 22.744 1.00 78.51 C HETATM 3391 C7 OLA A3024 -37.263 -12.135 21.677 1.00 80.71 C HETATM 3392 C8 OLA A3024 -37.598 -10.707 22.077 1.00 72.84 C HETATM 3393 C9 OLA A3024 -37.598 -9.831 20.849 1.00 72.49 C HETATM 3394 C10 OLA A3024 -38.116 -8.601 20.839 1.00 70.81 C HETATM 3395 C11 OLA A3024 -38.749 -7.970 22.055 1.00 68.17 C HETATM 3396 C12 OLA A3024 -38.370 -6.503 22.135 1.00 64.99 C HETATM 3397 C13 OLA A3024 -36.992 -6.339 22.770 1.00 57.01 C HETATM 3398 C14 OLA A3024 -36.434 -4.940 22.521 1.00 64.59 C HETATM 3399 C15 OLA A3024 -36.006 -4.286 23.832 1.00 62.32 C HETATM 3400 C16 OLA A3024 -35.493 -2.868 23.595 1.00 61.52 C HETATM 3401 C17 OLA A3024 -36.633 -1.853 23.629 1.00 58.97 C HETATM 3402 C18 OLA A3024 -36.252 -0.592 22.874 1.00 67.54 C HETATM 3403 C4 OLA A3025 -5.950 -17.980 15.763 1.00 61.40 C HETATM 3404 C5 OLA A3025 -6.827 -17.239 16.770 1.00 63.27 C HETATM 3405 C6 OLA A3025 -8.275 -17.158 16.293 1.00 63.17 C HETATM 3406 C7 OLA A3025 -8.575 -15.817 15.625 1.00 62.88 C HETATM 3407 C8 OLA A3025 -9.048 -14.781 16.632 1.00 60.41 C HETATM 3408 C9 OLA A3025 -10.460 -15.062 17.076 1.00 48.64 C HETATM 3409 C10 OLA A3025 -11.048 -14.346 18.035 1.00 46.33 C HETATM 3410 C11 OLA A3025 -10.343 -13.211 18.738 1.00 49.40 C HETATM 3411 C12 OLA A3025 -10.625 -11.886 18.050 1.00 45.90 C HETATM 3412 C13 OLA A3025 -9.329 -11.161 17.699 1.00 44.17 C HETATM 3413 C14 OLA A3025 -8.734 -10.496 18.936 1.00 45.22 C HETATM 3414 C15 OLA A3025 -9.237 -9.061 19.061 1.00 50.10 C HETATM 3415 C16 OLA A3025 -8.413 -8.109 18.198 1.00 54.44 C HETATM 3416 C17 OLA A3025 -8.091 -6.844 18.989 1.00 40.62 C HETATM 3417 O HOH A3101 -22.079 -6.702 15.309 1.00 34.45 O HETATM 3418 O HOH A3102 -41.929 -26.814 14.503 1.00 67.31 O HETATM 3419 O HOH A3103 -21.038 -11.702 15.045 1.00 44.73 O HETATM 3420 O HOH A3104 -23.233 -9.433 15.915 1.00 38.92 O HETATM 3421 O HOH A3105 -13.450 17.519 11.402 1.00 40.18 O HETATM 3422 O HOH A3106 -16.318 -17.005 19.337 1.00 37.71 O HETATM 3423 O HOH A3107 -25.601 -13.413 13.597 1.00 36.08 O HETATM 3424 O HOH A3108 -19.342 -35.624 26.931 1.00 59.95 O HETATM 3425 O HOH A3109 -24.423 16.800 2.023 1.00 71.23 O HETATM 3426 O HOH A3110 -16.805 15.055 20.752 1.00 58.48 O HETATM 3427 O HOH A3111 -17.181 -25.409 9.753 1.00 59.63 O HETATM 3428 O HOH A3112 -14.749 -26.934 17.359 1.00 43.77 O HETATM 3429 O HOH A3113 -25.139 -15.780 14.633 1.00 46.67 O HETATM 3430 O HOH A3114 -15.209 3.451 21.879 1.00 35.45 O HETATM 3431 O HOH A3115 -16.508 0.549 12.881 1.00 29.00 O HETATM 3432 O HOH A3116 -23.642 -4.895 14.319 1.00 26.55 O HETATM 3433 O HOH A3117 -23.038 -28.106 21.559 1.00 58.56 O HETATM 3434 O HOH A3118 -24.873 13.318 12.071 1.00 48.70 O HETATM 3435 O HOH A3119 -18.241 12.891 23.789 1.00 49.41 O HETATM 3436 O HOH A3120 -11.311 12.123 15.987 1.00 29.58 O HETATM 3437 O HOH A3121 -27.344 2.005 16.209 1.00 42.13 O HETATM 3438 O HOH A3122 -15.125 10.106 18.220 1.00 34.02 O HETATM 3439 O HOH A3123 -19.090 -11.365 13.070 1.00 36.50 O HETATM 3440 O HOH A3124 -28.376 2.723 19.191 1.00 38.72 O HETATM 3441 O HOH A3125 -12.812 -33.757 21.558 1.00 54.58 O HETATM 3442 O HOH A3126 -26.090 -12.088 21.691 1.00 31.22 O HETATM 3443 O HOH A3127 -26.474 18.565 22.265 1.00 39.60 O HETATM 3444 O HOH A3128 -20.579 10.533 16.449 1.00 37.52 O HETATM 3445 O HOH A3129 -25.804 7.608 13.624 1.00 31.91 O HETATM 3446 O HOH A3130 -27.821 20.781 22.498 1.00 42.69 O HETATM 3447 O HOH A3131 -16.778 16.855 9.100 1.00 52.17 O HETATM 3448 O HOH A3132 -25.997 18.893 24.904 1.00 43.84 O HETATM 3449 O HOH A3133 -24.111 -11.371 11.610 1.00 33.42 O HETATM 3450 O HOH A3134 -19.627 -1.635 22.075 1.00 27.33 O HETATM 3451 O HOH A3135 -22.412 12.209 17.649 1.00 27.72 O HETATM 3452 O HOH A3136 -3.505 16.211 21.629 1.00 54.81 O HETATM 3453 O HOH A3137 -5.012 17.608 12.997 1.00 62.10 O HETATM 3454 O HOH A3138 -18.460 -2.752 20.191 1.00 36.23 O HETATM 3455 O HOH A3139 -18.796 9.920 22.984 1.00 44.33 O HETATM 3456 O HOH A3140 -17.570 14.317 28.785 1.00 46.01 O HETATM 3457 O HOH A3141 -20.627 -2.487 24.180 1.00 34.04 O HETATM 3458 O HOH A3142 -24.865 11.382 16.393 1.00 37.54 O HETATM 3459 O HOH A3143 -17.108 15.606 12.877 1.00 45.90 O HETATM 3460 O HOH A3144 -12.201 15.229 4.681 1.00 56.41 O HETATM 3461 O HOH A3145 -14.953 12.460 28.614 1.00 39.12 O HETATM 3462 O HOH A3146 -4.183 -25.734 25.614 1.00 40.48 O HETATM 3463 O HOH A3147 -9.038 13.668 16.889 1.00 39.99 O HETATM 3464 O HOH A3148 -17.469 13.684 26.299 1.00 36.59 O HETATM 3465 O HOH A3149 -18.984 -28.306 7.391 1.00 51.96 O HETATM 3466 O HOH A3150 -24.338 10.075 14.248 1.00 45.58 O HETATM 3467 O HOH A3151 -21.721 11.739 13.709 1.00 51.15 O CONECT 529 1177 CONECT 545 1086 CONECT 565 1221 CONECT 1086 545 CONECT 1177 529 CONECT 1221 565 CONECT 2591 2612 CONECT 2612 2591 CONECT 2986 2998 2999 3000 CONECT 2987 2988 2992 2999 CONECT 2988 2987 2989 3001 CONECT 2989 2988 2990 CONECT 2990 2989 2991 CONECT 2991 2990 3001 CONECT 2992 2987 2993 2997 CONECT 2993 2992 2994 CONECT 2994 2993 2995 3002 CONECT 2995 2994 2996 CONECT 2996 2995 2997 CONECT 2997 2992 2996 3000 CONECT 2998 2986 CONECT 2999 2986 2987 CONECT 3000 2986 2997 CONECT 3001 2988 2991 CONECT 3002 2994 CONECT 3003 3004 3012 CONECT 3004 3003 3005 CONECT 3005 3004 3006 3030 CONECT 3006 3005 3007 CONECT 3007 3006 3008 3012 CONECT 3008 3007 3009 CONECT 3009 3008 3010 CONECT 3010 3009 3011 3016 CONECT 3011 3010 3012 3013 CONECT 3012 3003 3007 3011 3021 CONECT 3013 3011 3014 CONECT 3014 3013 3015 CONECT 3015 3014 3016 3019 3020 CONECT 3016 3010 3015 3017 CONECT 3017 3016 3018 CONECT 3018 3017 3019 CONECT 3019 3015 3018 3022 CONECT 3020 3015 CONECT 3021 3012 CONECT 3022 3019 3023 3024 CONECT 3023 3022 CONECT 3024 3022 3025 CONECT 3025 3024 3026 CONECT 3026 3025 3027 CONECT 3027 3026 3028 3029 CONECT 3028 3027 CONECT 3029 3027 CONECT 3030 3005 CONECT 3031 3032 3040 CONECT 3032 3031 3033 CONECT 3033 3032 3034 3058 CONECT 3034 3033 3035 CONECT 3035 3034 3036 3040 CONECT 3036 3035 3037 CONECT 3037 3036 3038 CONECT 3038 3037 3039 3044 CONECT 3039 3038 3040 3041 CONECT 3040 3031 3035 3039 3049 CONECT 3041 3039 3042 CONECT 3042 3041 3043 CONECT 3043 3042 3044 3047 3048 CONECT 3044 3038 3043 3045 CONECT 3045 3044 3046 CONECT 3046 3045 3047 CONECT 3047 3043 3046 3050 CONECT 3048 3043 CONECT 3049 3040 CONECT 3050 3047 3051 3052 CONECT 3051 3050 CONECT 3052 3050 3053 CONECT 3053 3052 3054 CONECT 3054 3053 3055 CONECT 3055 3054 3056 3057 CONECT 3056 3055 CONECT 3057 3055 CONECT 3058 3033 CONECT 3059 3060 3068 CONECT 3060 3059 3061 CONECT 3061 3060 3062 3086 CONECT 3062 3061 3063 CONECT 3063 3062 3064 3068 CONECT 3064 3063 3065 CONECT 3065 3064 3066 CONECT 3066 3065 3067 3072 CONECT 3067 3066 3068 3069 CONECT 3068 3059 3063 3067 3077 CONECT 3069 3067 3070 CONECT 3070 3069 3071 CONECT 3071 3070 3072 3075 3076 CONECT 3072 3066 3071 3073 CONECT 3073 3072 3074 CONECT 3074 3073 3075 CONECT 3075 3071 3074 3078 CONECT 3076 3071 CONECT 3077 3068 CONECT 3078 3075 3079 3080 CONECT 3079 3078 CONECT 3080 3078 3081 CONECT 3081 3080 3082 CONECT 3082 3081 3083 CONECT 3083 3082 3084 3085 CONECT 3084 3083 CONECT 3085 3083 CONECT 3086 3061 CONECT 3087 3088 3089 CONECT 3088 3087 3090 CONECT 3089 3087 3093 CONECT 3090 3088 3094 CONECT 3091 3105 3107 CONECT 3092 3095 CONECT 3093 3089 3096 CONECT 3094 3090 3097 CONECT 3095 3092 3098 CONECT 3096 3093 3098 CONECT 3097 3094 3099 CONECT 3098 3095 3096 CONECT 3099 3097 3100 CONECT 3100 3099 3101 CONECT 3101 3100 3102 CONECT 3102 3101 3104 CONECT 3103 3105 3109 CONECT 3104 3102 3106 3109 CONECT 3105 3091 3103 3108 CONECT 3106 3104 CONECT 3107 3091 CONECT 3108 3105 CONECT 3109 3103 3104 CONECT 3110 3111 CONECT 3111 3110 3113 CONECT 3112 3121 3123 CONECT 3113 3111 3114 CONECT 3114 3113 3115 CONECT 3115 3114 3116 CONECT 3116 3115 3117 CONECT 3117 3116 3118 CONECT 3118 3117 3120 CONECT 3119 3121 3125 CONECT 3120 3118 3122 3125 CONECT 3121 3112 3119 3124 CONECT 3122 3120 CONECT 3123 3112 CONECT 3124 3121 CONECT 3125 3119 3120 CONECT 3126 3127 3128 CONECT 3127 3126 3129 CONECT 3128 3126 3131 CONECT 3129 3127 3132 CONECT 3130 3142 3144 CONECT 3131 3128 3133 CONECT 3132 3129 3134 CONECT 3133 3131 3135 CONECT 3134 3132 3136 CONECT 3135 3133 CONECT 3136 3134 3137 CONECT 3137 3136 3138 CONECT 3138 3137 3139 CONECT 3139 3138 3141 CONECT 3140 3142 3146 CONECT 3141 3139 3143 3146 CONECT 3142 3130 3140 3145 CONECT 3143 3141 CONECT 3144 3130 CONECT 3145 3142 CONECT 3146 3140 3141 CONECT 3147 3148 3149 CONECT 3148 3147 3150 CONECT 3149 3147 3152 CONECT 3150 3148 3153 CONECT 3151 3162 3164 CONECT 3152 3149 3154 CONECT 3153 3150 3155 CONECT 3154 3152 CONECT 3155 3153 3156 CONECT 3156 3155 3157 CONECT 3157 3156 3158 CONECT 3158 3157 3159 CONECT 3159 3158 3161 CONECT 3160 3162 3166 CONECT 3161 3159 3163 3166 CONECT 3162 3151 3160 3165 CONECT 3163 3161 CONECT 3164 3151 CONECT 3165 3162 CONECT 3166 3160 3161 CONECT 3167 3168 3169 3170 CONECT 3168 3167 CONECT 3169 3167 CONECT 3170 3167 3171 CONECT 3171 3170 3172 CONECT 3172 3171 3173 CONECT 3173 3172 3174 CONECT 3174 3173 3175 CONECT 3175 3174 3176 CONECT 3176 3175 3177 CONECT 3177 3176 3178 CONECT 3178 3177 3179 CONECT 3179 3178 3180 CONECT 3180 3179 3181 CONECT 3181 3180 3182 CONECT 3182 3181 3183 CONECT 3183 3182 3184 CONECT 3184 3183 CONECT 3185 3186 3187 3188 CONECT 3186 3185 CONECT 3187 3185 CONECT 3188 3185 3189 CONECT 3189 3188 3190 CONECT 3190 3189 3191 CONECT 3191 3190 3192 CONECT 3192 3191 3193 CONECT 3193 3192 3194 CONECT 3194 3193 3195 CONECT 3195 3194 3196 CONECT 3196 3195 3197 CONECT 3197 3196 3198 CONECT 3198 3197 3199 CONECT 3199 3198 3200 CONECT 3200 3199 3201 CONECT 3201 3200 3202 CONECT 3202 3201 3203 CONECT 3203 3202 3204 CONECT 3204 3203 CONECT 3205 3206 3207 3208 CONECT 3206 3205 CONECT 3207 3205 CONECT 3208 3205 3209 CONECT 3209 3208 3210 CONECT 3210 3209 3211 CONECT 3211 3210 3212 CONECT 3212 3211 3213 CONECT 3213 3212 3214 CONECT 3214 3213 3215 CONECT 3215 3214 CONECT 3216 3217 3218 3219 CONECT 3217 3216 CONECT 3218 3216 CONECT 3219 3216 3220 CONECT 3220 3219 3221 CONECT 3221 3220 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 CONECT 3224 3223 CONECT 3225 3226 3227 3228 CONECT 3226 3225 CONECT 3227 3225 CONECT 3228 3225 3229 CONECT 3229 3228 3230 CONECT 3230 3229 3231 CONECT 3231 3230 3232 CONECT 3232 3231 3233 CONECT 3233 3232 3234 CONECT 3234 3233 3235 CONECT 3235 3234 3236 CONECT 3236 3235 3237 CONECT 3237 3236 3238 CONECT 3238 3237 3239 CONECT 3239 3238 3240 CONECT 3240 3239 3241 CONECT 3241 3240 3242 CONECT 3242 3241 3243 CONECT 3243 3242 3244 CONECT 3244 3243 CONECT 3245 3246 3247 3248 CONECT 3246 3245 CONECT 3247 3245 CONECT 3248 3245 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 3252 CONECT 3252 3251 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3255 CONECT 3255 3254 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 CONECT 3263 3262 3264 CONECT 3264 3263 CONECT 3265 3266 CONECT 3266 3265 3267 CONECT 3267 3266 3268 CONECT 3268 3267 3269 CONECT 3269 3268 3270 CONECT 3270 3269 3271 CONECT 3271 3270 3272 CONECT 3272 3271 3273 CONECT 3273 3272 3274 CONECT 3274 3273 3275 CONECT 3275 3274 CONECT 3276 3277 3278 3279 CONECT 3277 3276 CONECT 3278 3276 CONECT 3279 3276 3280 CONECT 3280 3279 3281 CONECT 3281 3280 3282 CONECT 3282 3281 3283 CONECT 3283 3282 CONECT 3284 3285 3286 3287 CONECT 3285 3284 CONECT 3286 3284 CONECT 3287 3284 3288 CONECT 3288 3287 3289 CONECT 3289 3288 3290 CONECT 3290 3289 CONECT 3291 3292 CONECT 3292 3291 3293 CONECT 3293 3292 3294 CONECT 3294 3293 3295 CONECT 3295 3294 3296 CONECT 3296 3295 3297 CONECT 3297 3296 3298 CONECT 3298 3297 3299 CONECT 3299 3298 3300 CONECT 3300 3299 3301 CONECT 3301 3300 CONECT 3302 3303 3304 3305 CONECT 3303 3302 CONECT 3304 3302 CONECT 3305 3302 3306 CONECT 3306 3305 3307 CONECT 3307 3306 3308 CONECT 3308 3307 3309 CONECT 3309 3308 3310 CONECT 3310 3309 3311 CONECT 3311 3310 3312 CONECT 3312 3311 3313 CONECT 3313 3312 3314 CONECT 3314 3313 3315 CONECT 3315 3314 3316 CONECT 3316 3315 3317 CONECT 3317 3316 3318 CONECT 3318 3317 3319 CONECT 3319 3318 3320 CONECT 3320 3319 3321 CONECT 3321 3320 CONECT 3322 3323 3324 3325 CONECT 3323 3322 CONECT 3324 3322 CONECT 3325 3322 3326 CONECT 3326 3325 3327 CONECT 3327 3326 3328 CONECT 3328 3327 3329 CONECT 3329 3328 3330 CONECT 3330 3329 3331 CONECT 3331 3330 3332 CONECT 3332 3331 CONECT 3333 3334 3335 3336 CONECT 3334 3333 CONECT 3335 3333 CONECT 3336 3333 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3338 3340 CONECT 3340 3339 3341 CONECT 3341 3340 3342 CONECT 3342 3341 3343 CONECT 3343 3342 3344 CONECT 3344 3343 3345 CONECT 3345 3344 3346 CONECT 3346 3345 3347 CONECT 3347 3346 3348 CONECT 3348 3347 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 CONECT 3353 3354 3355 3356 CONECT 3354 3353 CONECT 3355 3353 CONECT 3356 3353 3357 CONECT 3357 3356 3358 CONECT 3358 3357 3359 CONECT 3359 3358 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 CONECT 3363 3362 3364 CONECT 3364 3363 3365 CONECT 3365 3364 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3368 CONECT 3368 3367 3369 CONECT 3369 3368 CONECT 3370 3371 3372 3373 CONECT 3371 3370 CONECT 3372 3370 CONECT 3373 3370 3374 CONECT 3374 3373 3375 CONECT 3375 3374 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 CONECT 3383 3384 3385 3386 CONECT 3384 3383 CONECT 3385 3383 CONECT 3386 3383 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 3391 CONECT 3391 3390 3392 CONECT 3392 3391 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 CONECT 3403 3404 CONECT 3404 3403 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 3412 CONECT 3412 3411 3413 CONECT 3413 3412 3414 CONECT 3414 3413 3415 CONECT 3415 3414 3416 CONECT 3416 3415 MASTER 377 0 25 19 2 0 0 6 3466 1 439 35 END