HEADER MEMBRANE PROTEIN 28-JUL-17 5OM4 TITLE STRUCTURE OF THE A2A-STAR2-BRIL562-COMPOUND 4E COMPLEX AT 1.86A TITLE 2 OBTAINED FROM IN MESO SOAKING EXPERIMENTS (24 HOUR SOAK). COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE COMPND 3 RECEPTOR A2A; COMPND 4 CHAIN: A; COMPND 5 SYNONYM: CYTOCHROME B-562; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606, 562; SOURCE 5 GENE: ADORA2A, ADORA2, CYBC; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS KEYWDS G-PROTEIN COUPLED RECEPTOR, ADENOSINE 2A RECEPTOR, 7 TM INTEGRAL KEYWDS 2 MEMBRANE PROTEIN, THERMOSTABILIZING MUTATIONS, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR P.RUCKTOOA,R.K.Y.CHENG,E.SEGALA,T.GENG,J.C.ERREY,G.A.BROWN,R.COOKE, AUTHOR 2 F.H.MARSHALL,A.S.DORE REVDAT 1 17-JAN-18 5OM4 0 JRNL AUTH P.RUCKTOOA,R.K.Y.CHENG,E.SEGALA,T.GENG,J.C.ERREY,G.A.BROWN, JRNL AUTH 2 R.M.COOKE,F.H.MARSHALL,A.S.DORE JRNL TITL TOWARDS HIGH THROUGHPUT GPCR CRYSTALLOGRAPHY: IN MESO JRNL TITL 2 SOAKING OF ADENOSINE A2A RECEPTOR CRYSTALS. JRNL REF SCI REP V. 8 41 2018 JRNL REFN ESSN 2045-2322 JRNL PMID 29311713 JRNL DOI 10.1038/S41598-017-18570-W REMARK 2 REMARK 2 RESOLUTION. 2.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.12RC2_2821: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 32.92 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.080 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 63810 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.184 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.205 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 3185 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 32.9268 - 5.6785 0.99 2675 115 0.1790 0.1856 REMARK 3 2 5.6785 - 4.5109 1.00 2706 126 0.1655 0.1853 REMARK 3 3 4.5109 - 3.9417 1.00 2659 134 0.1459 0.1598 REMARK 3 4 3.9417 - 3.5818 1.00 2658 130 0.1446 0.1622 REMARK 3 5 3.5818 - 3.3253 1.00 2691 139 0.1553 0.1629 REMARK 3 6 3.3253 - 3.1294 0.99 2721 115 0.1651 0.1872 REMARK 3 7 3.1294 - 2.9728 0.99 2627 124 0.1695 0.1814 REMARK 3 8 2.9728 - 2.8435 1.00 2632 164 0.1660 0.2185 REMARK 3 9 2.8435 - 2.7341 0.98 2619 170 0.1667 0.2044 REMARK 3 10 2.7341 - 2.6398 0.99 2618 141 0.1717 0.1895 REMARK 3 11 2.6398 - 2.5573 0.97 2619 124 0.1790 0.2019 REMARK 3 12 2.5573 - 2.4842 0.99 2617 122 0.1947 0.2257 REMARK 3 13 2.4842 - 2.4188 0.96 2551 190 0.1995 0.2596 REMARK 3 14 2.4188 - 2.3598 0.99 2652 130 0.1994 0.2260 REMARK 3 15 2.3598 - 2.3062 0.98 2612 145 0.2111 0.2531 REMARK 3 16 2.3062 - 2.2571 0.95 2590 98 0.2345 0.2454 REMARK 3 17 2.2571 - 2.2120 0.99 2634 146 0.2392 0.2394 REMARK 3 18 2.2120 - 2.1702 0.97 2577 150 0.2518 0.2432 REMARK 3 19 2.1702 - 2.1315 0.98 2676 131 0.2570 0.2235 REMARK 3 20 2.1315 - 2.0954 1.00 2601 150 0.2717 0.3022 REMARK 3 21 2.0954 - 2.0616 0.98 2637 146 0.2798 0.3082 REMARK 3 22 2.0616 - 2.0299 0.97 2570 148 0.3046 0.3193 REMARK 3 23 2.0299 - 2.0000 1.00 2683 147 0.3201 0.3716 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) : 20.050 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 3741 REMARK 3 ANGLE : 0.929 4974 REMARK 3 CHIRALITY : 0.039 543 REMARK 3 PLANARITY : 0.003 593 REMARK 3 DIHEDRAL : 11.507 1916 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN A AND (RESSEQ -1:208 OR RESSEQ 219:305 OR REMARK 3 RESSEQ 1201)) REMARK 3 ORIGIN FOR THE GROUP (A): -22.8179 -5.9816 17.6668 REMARK 3 T TENSOR REMARK 3 T11: 0.1526 T22: 0.2271 REMARK 3 T33: 0.1210 T12: -0.0020 REMARK 3 T13: 0.0094 T23: 0.0087 REMARK 3 L TENSOR REMARK 3 L11: 0.9658 L22: 1.5815 REMARK 3 L33: 1.2675 L12: 0.1684 REMARK 3 L13: 0.2874 L23: 0.0498 REMARK 3 S TENSOR REMARK 3 S11: 0.0027 S12: -0.0149 S13: -0.0841 REMARK 3 S21: -0.0730 S22: 0.0038 S23: -0.0038 REMARK 3 S31: 0.1335 S32: -0.0836 S33: -0.0001 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN A AND (RESSEQ 1001:1106)) REMARK 3 ORIGIN FOR THE GROUP (A): 0.8667 -54.6646 20.1003 REMARK 3 T TENSOR REMARK 3 T11: 0.4121 T22: 0.3254 REMARK 3 T33: 0.7840 T12: 0.0766 REMARK 3 T13: -0.0001 T23: -0.0678 REMARK 3 L TENSOR REMARK 3 L11: 1.2811 L22: 6.3110 REMARK 3 L33: 4.4319 L12: -1.9157 REMARK 3 L13: 1.2706 L23: -2.3303 REMARK 3 S TENSOR REMARK 3 S11: 0.0016 S12: -0.3263 S13: 0.5259 REMARK 3 S21: -0.3628 S22: -0.0076 S23: -0.2663 REMARK 3 S31: 0.0587 S32: 0.0556 S33: -0.0180 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 5OM4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JUL-17. REMARK 100 THE DEPOSITION ID IS D_1200006028. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-NOV-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.3-5.4 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : DIAMOND REMARK 200 BEAMLINE : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.96857 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 33687 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000 REMARK 200 RESOLUTION RANGE LOW (A) : 32.920 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 200 DATA REDUNDANCY : 6.300 REMARK 200 R MERGE (I) : 0.13700 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05 REMARK 200 COMPLETENESS FOR SHELL (%) : 98.8 REMARK 200 DATA REDUNDANCY IN SHELL : 6.50 REMARK 200 R MERGE FOR SHELL (I) : 1.50800 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.300 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 5MZJ REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 42.21 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL GROWTH: 0.L M TRI-SODIUM REMARK 280 CITRATE PH 5.3-5.4, 0.05 M SODIUM THIOCYANATE, 29-32% PEG400, 2% REMARK 280 (V/V) 2,5-HEXANEDIOL AND 0.5 MM THEOPHYLLINE COMPOUND 4E WAS REMARK 280 ADDED TO THE MOTHER LIQUOR TO A CONCENTRATION OF 0.005 MM FOR REMARK 280 THE SOAKING EXPERIMENTS., LIPIDIC CUBIC PHASE, TEMPERATURE REMARK 280 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 70.01600 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 70.01600 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 19.73250 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.55450 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.73250 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.55450 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.01600 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.73250 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.55450 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.01600 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.73250 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.55450 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 10560 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21050 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ALA A -9 REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ALA A 1043 REMARK 465 THR A 1044 REMARK 465 PRO A 1045 REMARK 465 PRO A 1046 REMARK 465 LYS A 1047 REMARK 465 LEU A 1048 REMARK 465 GLU A 1049 REMARK 465 ASP A 1050 REMARK 465 LYS A 1051 REMARK 465 SER A 1052 REMARK 465 PRO A 1053 REMARK 465 ASP A 1054 REMARK 465 SER A 1055 REMARK 465 PRO A 1056 REMARK 465 GLU A 1057 REMARK 465 MET A 1058 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O HOH A 1412 O HOH A 1437 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 LEU A 58 -52.87 -121.13 REMARK 500 TYR A1101 -56.77 -132.67 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 OLA A 1209 REMARK 610 OLA A 1211 REMARK 610 OLA A 1212 REMARK 610 OLA A 1213 REMARK 610 OLA A 1214 REMARK 610 OLA A 1215 REMARK 610 OLA A 1216 REMARK 610 OLA A 1218 REMARK 610 OLA A 1219 REMARK 610 OLA A 1220 REMARK 610 OLA A 1221 REMARK 610 OLC A 1223 REMARK 610 OLC A 1224 REMARK 610 OLC A 1225 REMARK 610 OLC A 1228 REMARK 610 OLC A 1229 REMARK 610 OLC A 1230 REMARK 610 OLC A 1232 REMARK 610 OLC A 1233 REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 NA A1202 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 131.1 REMARK 620 3 HOH A1373 O 76.7 120.3 REMARK 620 4 HOH A1359 O 101.4 122.3 89.8 REMARK 620 5 HOH A1382 O 90.2 68.7 166.9 92.7 REMARK 620 N 1 2 3 4 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue T4E A 1201 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1202 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1203 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1204 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1205 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1206 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1210 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1211 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1220 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1221 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1222 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1223 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1224 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1225 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1226 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1227 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1228 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1229 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1231 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1232 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1233 DBREF 5OM4 A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5OM4 A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5OM4 A 219 317 UNP P29274 AA2AR_HUMAN 219 317 SEQADV 5OM4 ALA A -9 UNP P29274 EXPRESSION TAG SEQADV 5OM4 ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5OM4 TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5OM4 LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5OM4 ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5OM4 ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5OM4 ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5OM4 ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5OM4 GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5OM4 ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5OM4 PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5OM4 LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 5OM4 ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 5OM4 ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 5OM4 ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 5OM4 ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 5OM4 ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 5OM4 TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5OM4 ILE A 1102 UNP P0ABE7 HIS 124 ENGINEERED MUTATION SEQADV 5OM4 LEU A 1106 UNP P0ABE7 ARG 128 ENGINEERED MUTATION SEQADV 5OM4 ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 5OM4 ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 5OM4 ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 5OM4 ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 5OM4 HIS A 328 UNP P29274 EXPRESSION TAG SEQRES 1 A 434 ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE SEQRES 2 A 434 MET GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE SEQRES 3 A 434 ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP SEQRES 4 A 434 ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN SEQRES 5 A 434 TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL SEQRES 6 A 434 GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR SEQRES 7 A 434 GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA SEQRES 8 A 434 CYS PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER SEQRES 9 A 434 LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA SEQRES 10 A 434 ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG SEQRES 11 A 434 ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE SEQRES 12 A 434 ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS SEQRES 13 A 434 GLY GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS SEQRES 14 A 434 GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL SEQRES 15 A 434 PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS SEQRES 16 A 434 VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU SEQRES 17 A 434 ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU SEQRES 18 A 434 GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL SEQRES 19 A 434 ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA SEQRES 20 A 434 LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS SEQRES 21 A 434 ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER SEQRES 22 A 434 PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU SEQRES 23 A 434 VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU SEQRES 24 A 434 GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU SEQRES 25 A 434 LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU SEQRES 26 A 434 ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA SEQRES 27 A 434 LYS SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS SEQRES 28 A 434 TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE SEQRES 29 A 434 CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR SEQRES 30 A 434 LEU ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN SEQRES 31 A 434 PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN SEQRES 32 A 434 THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN SEQRES 33 A 434 GLN GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS SEQRES 34 A 434 HIS HIS HIS HIS HIS HET T4E A1201 21 HET NA A1202 1 HET CLR A1203 28 HET CLR A1204 28 HET CLR A1205 28 HET CLR A1206 28 HET OLA A1207 20 HET OLA A1208 20 HET OLA A1209 9 HET OLA A1210 20 HET OLA A1211 18 HET OLA A1212 14 HET OLA A1213 13 HET OLA A1214 12 HET OLA A1215 12 HET OLA A1216 10 HET OLA A1217 20 HET OLA A1218 9 HET OLA A1219 19 HET OLA A1220 12 HET OLA A1221 9 HET OLA A1222 20 HET OLC A1223 19 HET OLC A1224 16 HET OLC A1225 22 HET OLC A1226 25 HET OLC A1227 25 HET OLC A1228 24 HET OLC A1229 17 HET OLC A1230 14 HET OLC A1231 25 HET OLC A1232 17 HET OLC A1233 17 HETNAM T4E 4-(3-AMINO-5-PHENYL-1,2,4-TRIAZIN-6-YL)-2-CHLOROPHENOL HETNAM NA SODIUM ION HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 T4E C15 H11 CL N4 O FORMUL 3 NA NA 1+ FORMUL 4 CLR 4(C27 H46 O) FORMUL 8 OLA 16(C18 H34 O2) FORMUL 24 OLC 11(C21 H40 O4) FORMUL 35 HOH *156(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 THR A 68 1 11 HELIX 5 AA5 CYS A 74 ILE A 108 1 35 HELIX 6 AA6 ARG A 111 VAL A 116 1 6 HELIX 7 AA7 THR A 117 LEU A 137 1 21 HELIX 8 AA8 THR A 138 GLY A 142 5 5 HELIX 9 AA9 LYS A 150 GLN A 157 1 8 HELIX 10 AB1 LEU A 167 VAL A 172 1 6 HELIX 11 AB2 PRO A 173 PHE A 180 1 8 HELIX 12 AB3 VAL A 186 LYS A 1019 1 42 HELIX 13 AB4 ASN A 1022 LYS A 1042 1 21 HELIX 14 AB5 ASP A 1060 GLU A 1081 1 22 HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11 HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9 HELIX 17 AB8 TYR A 1101 CYS A 259 1 47 HELIX 18 AB9 PRO A 266 ILE A 292 1 27 HELIX 19 AC1 ILE A 292 VAL A 307 1 16 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.04 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.04 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.04 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.04 LINK OD1 ASP A 52 NA NA A1202 1555 1555 2.46 LINK OG SER A 91 NA NA A1202 1555 1555 2.52 LINK NA NA A1202 O HOH A1373 1555 1555 2.35 LINK NA NA A1202 O HOH A1359 1555 1555 2.60 LINK NA NA A1202 O HOH A1382 1555 1555 2.54 SITE 1 AC1 13 VAL A 84 LEU A 85 PHE A 168 GLU A 169 SITE 2 AC1 13 MET A 177 TRP A 246 LEU A 249 HIS A 250 SITE 3 AC1 13 ASN A 253 HIS A 278 HOH A1318 HOH A1381 SITE 4 AC1 13 HOH A1413 SITE 1 AC2 5 ASP A 52 SER A 91 HOH A1359 HOH A1373 SITE 2 AC2 5 HOH A1382 SITE 1 AC3 7 HIS A 75 GLY A 76 LEU A 137 CLR A1204 SITE 2 AC3 7 OLC A1232 OLC A1233 HOH A1313 SITE 1 AC4 9 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 2 AC4 9 CLR A1203 CLR A1206 OLC A1223 OLC A1227 SITE 3 AC4 9 HOH A1354 SITE 1 AC5 5 PRO A 248 CYS A 262 SER A 263 OLA A1221 SITE 2 AC5 5 HOH A1338 SITE 1 AC6 7 CYS A 254 PHE A 255 CYS A 259 CLR A1204 SITE 2 AC6 7 OLC A1225 OLC A1227 HOH A1370 SITE 1 AC7 4 THR A 65 OLA A1217 OLC A1227 HOH A1324 SITE 1 AC8 1 THR A 11 SITE 1 AC9 3 PHE A 44 ALA A 97 VAL A 116 SITE 1 AD1 7 GLY A 123 ILE A 127 LEU A 131 ALA A 184 SITE 2 AD1 7 VAL A 188 OLC A1224 OLC A1226 SITE 1 AD2 4 GLY A 5 TYR A 271 VAL A 275 OLA A1213 SITE 1 AD3 3 LEU A 198 ARG A 199 ALA A 202 SITE 1 AD4 4 VAL A 12 THR A 279 PHE A 286 OLA A1211 SITE 1 AD5 3 SER A 7 LEU A 19 PHE A 286 SITE 1 AD6 3 TRP A 268 LEU A 272 OLA A1222 SITE 1 AD7 1 ILE A 287 SITE 1 AD8 3 OLA A1207 OLC A1225 OLC A1231 SITE 1 AD9 2 LEU A 190 ALA A 236 SITE 1 AE1 5 TRP A 29 TRP A 32 PHE A 201 LYS A 233 SITE 2 AE1 5 OLC A1229 SITE 1 AE2 3 ALA A 236 GLY A 240 LEU A 244 SITE 1 AE3 2 LEU A 244 CLR A1205 SITE 1 AE4 1 OLA A1215 SITE 1 AE5 8 GLN A 163 PHE A 258 CLR A1204 OLC A1233 SITE 2 AE5 8 HOH A1303 HOH A1336 HOH A1354 HOH A1406 SITE 1 AE6 9 HIS A 75 MET A 140 LEU A 141 GLY A 142 SITE 2 AE6 9 ASN A 144 ASN A 175 TYR A 179 OLA A1210 SITE 3 AE6 9 OLC A1232 SITE 1 AE7 7 ASP A 261 CYS A 262 CLR A1206 OLA A1217 SITE 2 AE7 7 OLC A1227 HOH A1338 HOH A1405 SITE 1 AE8 4 TYR A 103 ARG A 120 ILE A 127 OLA A1210 SITE 1 AE9 11 VAL A 57 LEU A 58 THR A 65 PHE A 70 SITE 2 AE9 11 CYS A 71 CLR A1204 CLR A1206 OLA A1207 SITE 3 AE9 11 OLC A1225 HOH A1354 HOH A1404 SITE 1 AF1 4 TYR A 43 LEU A 58 ILE A 125 TRP A 129 SITE 1 AF2 6 CYS A 28 VAL A 31 TYR A 43 ALA A 50 SITE 2 AF2 6 ARG A 205 OLA A1219 SITE 1 AF3 7 PRO A 2 SER A 6 ILE A 10 SER A 67 SITE 2 AF3 7 THR A 68 GLN A 157 OLA A1217 SITE 1 AF4 4 HIS A 75 MET A 140 CLR A1203 OLC A1224 SITE 1 AF5 5 TYR A 179 CLR A1203 OLC A1223 HOH A1345 SITE 2 AF5 5 HOH A1368 CRYST1 39.465 179.109 140.032 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 0.025339 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005583 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007141 0.00000 ATOM 1 N GLY A -1 -20.749 24.584 1.475 1.00 70.84 N ANISOU 1 N GLY A -1 10665 8103 8150 -346 -721 1260 N ATOM 2 CA GLY A -1 -21.496 23.657 2.306 1.00 69.47 C ANISOU 2 CA GLY A -1 10339 8026 8031 -234 -730 1145 C ATOM 3 C GLY A -1 -22.727 23.088 1.625 1.00 69.87 C ANISOU 3 C GLY A -1 10403 8124 8019 -148 -819 1149 C ATOM 4 O GLY A -1 -23.796 23.701 1.644 1.00 71.90 O ANISOU 4 O GLY A -1 10692 8306 8322 -46 -955 1158 O ATOM 5 N ALA A 0 -22.566 21.909 1.025 1.00 66.91 N ANISOU 5 N ALA A 0 10002 7873 7546 -187 -745 1139 N ATOM 6 CA ALA A 0 -23.656 21.254 0.317 1.00 65.27 C ANISOU 6 CA ALA A 0 9808 7720 7270 -123 -827 1141 C ATOM 7 C ALA A 0 -24.819 20.968 1.268 1.00 62.81 C ANISOU 7 C ALA A 0 9363 7435 7068 12 -906 1049 C ATOM 8 O ALA A 0 -24.615 20.800 2.474 1.00 62.55 O ANISOU 8 O ALA A 0 9207 7426 7134 41 -851 966 O ATOM 9 CB ALA A 0 -23.167 19.953 -0.315 1.00 64.06 C ANISOU 9 CB ALA A 0 9639 7696 7004 -192 -717 1124 C ATOM 10 N PRO A 1 -26.048 20.913 0.751 1.00 60.83 N ANISOU 10 N PRO A 1 9130 7181 6801 92 -1036 1064 N ATOM 11 CA PRO A 1 -27.216 20.656 1.611 1.00 57.30 C ANISOU 11 CA PRO A 1 8544 6765 6463 219 -1107 979 C ATOM 12 C PRO A 1 -27.034 19.387 2.421 1.00 54.51 C ANISOU 12 C PRO A 1 8039 6540 6133 214 -996 879 C ATOM 13 O PRO A 1 -26.663 18.336 1.874 1.00 53.97 O ANISOU 13 O PRO A 1 7972 6562 5974 148 -927 876 O ATOM 14 CB PRO A 1 -28.371 20.515 0.608 1.00 56.58 C ANISOU 14 CB PRO A 1 8501 6680 6316 271 -1248 1023 C ATOM 15 CG PRO A 1 -27.935 21.307 -0.571 1.00 58.04 C ANISOU 15 CG PRO A 1 8880 6775 6395 202 -1293 1144 C ATOM 16 CD PRO A 1 -26.439 21.158 -0.650 1.00 59.42 C ANISOU 16 CD PRO A 1 9103 6968 6504 70 -1131 1163 C ATOM 17 N PRO A 2 -27.273 19.447 3.733 1.00 52.16 N ANISOU 17 N PRO A 2 7617 6249 5953 281 -977 797 N ATOM 18 CA PRO A 2 -27.016 18.269 4.577 1.00 48.29 C ANISOU 18 CA PRO A 2 6993 5873 5483 269 -870 710 C ATOM 19 C PRO A 2 -27.872 17.070 4.219 1.00 41.76 C ANISOU 19 C PRO A 2 6099 5149 4621 292 -894 680 C ATOM 20 O PRO A 2 -27.453 15.932 4.456 1.00 40.33 O ANISOU 20 O PRO A 2 5855 5058 4412 247 -800 636 O ATOM 21 CB PRO A 2 -27.321 18.781 5.993 1.00 49.73 C ANISOU 21 CB PRO A 2 7079 6027 5791 349 -871 636 C ATOM 22 CG PRO A 2 -27.213 20.278 5.896 1.00 50.36 C ANISOU 22 CG PRO A 2 7261 5966 5909 370 -941 686 C ATOM 23 CD PRO A 2 -27.705 20.612 4.522 1.00 51.21 C ANISOU 23 CD PRO A 2 7485 6028 5946 368 -1044 778 C ATOM 24 N ILE A 3 -29.054 17.287 3.637 1.00 42.42 N ANISOU 24 N ILE A 3 6196 5215 4707 358 -1024 704 N ATOM 25 CA ILE A 3 -29.946 16.177 3.329 1.00 42.37 C ANISOU 25 CA ILE A 3 6118 5304 4678 376 -1061 673 C ATOM 26 C ILE A 3 -29.394 15.295 2.211 1.00 41.64 C ANISOU 26 C ILE A 3 6112 5261 4446 279 -1021 707 C ATOM 27 O ILE A 3 -29.801 14.134 2.090 1.00 40.73 O ANISOU 27 O ILE A 3 5938 5232 4306 268 -1013 666 O ATOM 28 CB ILE A 3 -31.348 16.709 2.971 1.00 41.33 C ANISOU 28 CB ILE A 3 5971 5139 4595 473 -1224 693 C ATOM 29 CG1 ILE A 3 -32.389 15.589 3.044 1.00 44.04 C ANISOU 29 CG1 ILE A 3 6188 5585 4959 501 -1258 639 C ATOM 30 CG2 ILE A 3 -31.342 17.325 1.589 1.00 43.68 C ANISOU 30 CG2 ILE A 3 6434 5366 4795 445 -1325 794 C ATOM 31 CD1 ILE A 3 -33.760 16.000 2.554 1.00 46.92 C ANISOU 31 CD1 ILE A 3 6527 5931 5370 588 -1427 661 C ATOM 32 N MET A 4 -28.471 15.803 1.392 1.00 37.54 N ANISOU 32 N MET A 4 5738 4690 3836 206 -992 779 N ATOM 33 CA MET A 4 -27.912 14.986 0.318 1.00 34.09 C ANISOU 33 CA MET A 4 5391 4303 3258 117 -939 805 C ATOM 34 C MET A 4 -27.010 13.890 0.875 1.00 34.50 C ANISOU 34 C MET A 4 5366 4435 3307 64 -785 739 C ATOM 35 O MET A 4 -27.251 12.696 0.654 1.00 31.40 O ANISOU 35 O MET A 4 4938 4119 2873 50 -766 695 O ATOM 36 CB MET A 4 -27.154 15.870 -0.672 1.00 32.94 C ANISOU 36 CB MET A 4 5418 4084 3014 49 -935 903 C ATOM 37 CG MET A 4 -28.024 16.908 -1.343 1.00 33.20 C ANISOU 37 CG MET A 4 5550 4029 3036 98 -1100 980 C ATOM 38 SD MET A 4 -27.157 17.798 -2.644 1.00 41.05 S ANISOU 38 SD MET A 4 6770 4942 3884 -1 -1093 1108 S ATOM 39 CE MET A 4 -26.740 16.448 -3.748 1.00 44.50 C ANISOU 39 CE MET A 4 7254 5492 4161 -89 -997 1086 C ATOM 40 N GLY A 5 -25.957 14.277 1.600 1.00 31.19 N ANISOU 40 N GLY A 5 4923 3993 2936 35 -682 731 N ATOM 41 CA GLY A 5 -25.122 13.281 2.246 1.00 26.90 C ANISOU 41 CA GLY A 5 4293 3520 2408 -1 -549 667 C ATOM 42 C GLY A 5 -25.889 12.452 3.256 1.00 32.88 C ANISOU 42 C GLY A 5 4908 4337 3249 61 -562 586 C ATOM 43 O GLY A 5 -25.598 11.267 3.449 1.00 32.53 O ANISOU 43 O GLY A 5 4809 4362 3190 37 -488 537 O ATOM 44 N SER A 6 -26.886 13.057 3.904 1.00 31.81 N ANISOU 44 N SER A 6 4712 4172 3202 141 -651 572 N ATOM 45 CA SER A 6 -27.722 12.316 4.838 1.00 33.48 C ANISOU 45 CA SER A 6 4787 4445 3489 196 -661 501 C ATOM 46 C SER A 6 -28.542 11.249 4.122 1.00 28.56 C ANISOU 46 C SER A 6 4154 3883 2814 189 -710 489 C ATOM 47 O SER A 6 -28.726 10.147 4.648 1.00 27.91 O ANISOU 47 O SER A 6 3984 3868 2753 184 -667 433 O ATOM 48 CB SER A 6 -28.632 13.281 5.597 1.00 40.45 C ANISOU 48 CB SER A 6 5610 5283 4475 288 -740 487 C ATOM 49 OG SER A 6 -29.497 12.586 6.474 1.00 49.62 O ANISOU 49 OG SER A 6 6637 6511 5706 337 -741 421 O ATOM 50 N ASER A 7 -29.042 11.557 2.920 0.67 28.38 N ANISOU 50 N ASER A 7 4228 3834 2720 185 -808 543 N ATOM 51 N BSER A 7 -29.042 11.556 2.922 0.33 28.55 N ANISOU 51 N BSER A 7 4249 3856 2742 185 -808 543 N ATOM 52 CA ASER A 7 -29.849 10.588 2.182 0.67 28.95 C ANISOU 52 CA ASER A 7 4301 3961 2739 173 -873 531 C ATOM 53 CA BSER A 7 -29.849 10.584 2.189 0.33 28.87 C ANISOU 53 CA BSER A 7 4289 3950 2729 174 -873 530 C ATOM 54 C ASER A 7 -29.031 9.365 1.788 0.67 27.69 C ANISOU 54 C ASER A 7 4177 3852 2492 96 -771 504 C ATOM 55 C BSER A 7 -29.029 9.362 1.794 0.33 27.69 C ANISOU 55 C BSER A 7 4177 3852 2492 96 -771 503 C ATOM 56 O ASER A 7 -29.556 8.246 1.763 0.67 27.38 O ANISOU 56 O ASER A 7 4088 3868 2447 86 -783 459 O ATOM 57 O BSER A 7 -29.549 8.241 1.773 0.33 27.34 O ANISOU 57 O BSER A 7 4083 3864 2443 86 -781 458 O ATOM 58 CB ASER A 7 -30.455 11.240 0.940 0.67 30.64 C ANISOU 58 CB ASER A 7 4629 4131 2882 181 -1007 600 C ATOM 59 CB BSER A 7 -30.459 11.234 0.949 0.33 30.73 C ANISOU 59 CB BSER A 7 4640 4143 2895 182 -1007 599 C ATOM 60 OG ASER A 7 -31.279 12.338 1.286 0.67 32.49 O ANISOU 60 OG ASER A 7 4824 4311 3207 266 -1113 622 O ATOM 61 OG BSER A 7 -29.443 11.643 0.051 0.33 31.68 O ANISOU 61 OG BSER A 7 4914 4223 2901 117 -962 659 O ATOM 62 N VAL A 8 -27.749 9.557 1.470 1.00 26.76 N ANISOU 62 N VAL A 8 4144 3714 2310 42 -670 528 N ATOM 63 CA VAL A 8 -26.896 8.426 1.114 1.00 25.62 C ANISOU 63 CA VAL A 8 4029 3615 2092 -20 -562 496 C ATOM 64 C VAL A 8 -26.654 7.548 2.332 1.00 27.55 C ANISOU 64 C VAL A 8 4141 3902 2423 -8 -481 427 C ATOM 65 O VAL A 8 -26.792 6.320 2.274 1.00 24.71 O ANISOU 65 O VAL A 8 3757 3587 2044 -26 -459 380 O ATOM 66 CB VAL A 8 -25.570 8.918 0.506 1.00 23.73 C ANISOU 66 CB VAL A 8 3894 3347 1773 -80 -465 541 C ATOM 67 CG1 VAL A 8 -24.576 7.766 0.404 1.00 21.90 C ANISOU 67 CG1 VAL A 8 3659 3165 1496 -127 -332 493 C ATOM 68 CG2 VAL A 8 -25.809 9.540 -0.861 1.00 25.21 C ANISOU 68 CG2 VAL A 8 4238 3501 1841 -107 -539 613 C ATOM 69 N TYR A 9 -26.289 8.171 3.455 1.00 28.00 N ANISOU 69 N TYR A 9 4123 3940 2575 20 -442 420 N ATOM 70 CA TYR A 9 -26.066 7.427 4.686 1.00 22.72 C ANISOU 70 CA TYR A 9 3339 3309 1985 33 -374 361 C ATOM 71 C TYR A 9 -27.322 6.673 5.116 1.00 21.01 C ANISOU 71 C TYR A 9 3035 3134 1813 66 -437 321 C ATOM 72 O TYR A 9 -27.251 5.492 5.476 1.00 22.73 O ANISOU 72 O TYR A 9 3205 3393 2038 47 -391 278 O ATOM 73 CB TYR A 9 -25.599 8.384 5.784 1.00 26.52 C ANISOU 73 CB TYR A 9 3768 3758 2550 60 -344 363 C ATOM 74 CG TYR A 9 -25.673 7.800 7.174 1.00 27.20 C ANISOU 74 CG TYR A 9 3737 3881 2718 86 -304 307 C ATOM 75 CD1 TYR A 9 -24.785 6.809 7.579 1.00 25.60 C ANISOU 75 CD1 TYR A 9 3504 3711 2513 54 -213 276 C ATOM 76 CD2 TYR A 9 -26.623 8.242 8.086 1.00 24.63 C ANISOU 76 CD2 TYR A 9 3334 3556 2470 145 -356 286 C ATOM 77 CE1 TYR A 9 -24.847 6.264 8.846 1.00 22.44 C ANISOU 77 CE1 TYR A 9 3009 3341 2177 74 -183 234 C ATOM 78 CE2 TYR A 9 -26.692 7.703 9.359 1.00 23.97 C ANISOU 78 CE2 TYR A 9 3153 3509 2444 162 -313 239 C ATOM 79 CZ TYR A 9 -25.803 6.714 9.732 1.00 25.20 C ANISOU 79 CZ TYR A 9 3292 3695 2589 123 -231 217 C ATOM 80 OH TYR A 9 -25.864 6.173 10.993 1.00 24.10 O ANISOU 80 OH TYR A 9 3070 3588 2498 137 -195 178 O ATOM 81 N ILE A 10 -28.481 7.335 5.074 1.00 20.87 N ANISOU 81 N ILE A 10 2994 3104 1833 113 -545 337 N ATOM 82 CA ILE A 10 -29.725 6.704 5.511 1.00 21.88 C ANISOU 82 CA ILE A 10 3020 3277 2017 142 -603 301 C ATOM 83 C ILE A 10 -30.098 5.546 4.590 1.00 21.05 C ANISOU 83 C ILE A 10 2952 3204 1842 95 -637 289 C ATOM 84 O ILE A 10 -30.550 4.492 5.051 1.00 21.59 O ANISOU 84 O ILE A 10 2946 3316 1943 80 -626 247 O ATOM 85 CB ILE A 10 -30.857 7.749 5.590 1.00 22.37 C ANISOU 85 CB ILE A 10 3041 3318 2142 211 -713 320 C ATOM 86 CG1 ILE A 10 -30.624 8.725 6.747 1.00 23.65 C ANISOU 86 CG1 ILE A 10 3149 3451 2387 265 -674 309 C ATOM 87 CG2 ILE A 10 -32.217 7.074 5.719 1.00 22.35 C ANISOU 87 CG2 ILE A 10 2936 3369 2189 230 -786 290 C ATOM 88 CD1 ILE A 10 -31.597 9.900 6.766 1.00 23.76 C ANISOU 88 CD1 ILE A 10 3137 3425 2463 345 -777 326 C ATOM 89 N THR A 11 -29.930 5.725 3.275 1.00 21.92 N ANISOU 89 N THR A 11 3186 3290 1850 65 -681 326 N ATOM 90 CA THR A 11 -30.284 4.666 2.332 1.00 23.45 C ANISOU 90 CA THR A 11 3435 3510 1965 19 -721 309 C ATOM 91 C THR A 11 -29.412 3.431 2.533 1.00 23.80 C ANISOU 91 C THR A 11 3485 3575 1982 -27 -606 262 C ATOM 92 O THR A 11 -29.909 2.297 2.514 1.00 26.27 O ANISOU 92 O THR A 11 3770 3916 2297 -52 -624 221 O ATOM 93 CB THR A 11 -30.161 5.177 0.897 1.00 21.39 C ANISOU 93 CB THR A 11 3326 3218 1583 -5 -781 359 C ATOM 94 OG1 THR A 11 -31.049 6.287 0.707 1.00 24.74 O ANISOU 94 OG1 THR A 11 3745 3615 2040 45 -906 406 O ATOM 95 CG2 THR A 11 -30.524 4.075 -0.097 1.00 22.01 C ANISOU 95 CG2 THR A 11 3475 3322 1568 -55 -828 333 C ATOM 96 N VAL A 12 -28.108 3.634 2.721 1.00 20.35 N ANISOU 96 N VAL A 12 3082 3122 1527 -38 -491 267 N ATOM 97 CA VAL A 12 -27.205 2.519 2.984 1.00 20.04 C ANISOU 97 CA VAL A 12 3038 3098 1477 -67 -382 222 C ATOM 98 C VAL A 12 -27.577 1.826 4.290 1.00 22.45 C ANISOU 98 C VAL A 12 3217 3428 1886 -50 -365 183 C ATOM 99 O VAL A 12 -27.595 0.591 4.369 1.00 21.99 O ANISOU 99 O VAL A 12 3148 3383 1824 -75 -341 142 O ATOM 100 CB VAL A 12 -25.744 3.012 2.990 1.00 19.74 C ANISOU 100 CB VAL A 12 3040 3041 1418 -78 -269 239 C ATOM 101 CG1 VAL A 12 -24.799 1.905 3.466 1.00 19.66 C ANISOU 101 CG1 VAL A 12 2998 3046 1426 -91 -159 191 C ATOM 102 CG2 VAL A 12 -25.340 3.505 1.597 1.00 19.35 C ANISOU 102 CG2 VAL A 12 3131 2975 1248 -111 -268 278 C ATOM 103 N GLU A 13 -27.879 2.605 5.336 1.00 19.44 N ANISOU 103 N GLU A 13 2745 3048 1592 -9 -375 194 N ATOM 104 CA GLU A 13 -28.274 2.011 6.611 1.00 17.17 C ANISOU 104 CA GLU A 13 2344 2788 1391 4 -354 162 C ATOM 105 C GLU A 13 -29.518 1.146 6.457 1.00 19.52 C ANISOU 105 C GLU A 13 2600 3115 1702 -13 -427 141 C ATOM 106 O GLU A 13 -29.576 0.031 6.988 1.00 20.73 O ANISOU 106 O GLU A 13 2712 3284 1878 -39 -394 110 O ATOM 107 CB GLU A 13 -28.518 3.100 7.657 1.00 21.84 C ANISOU 107 CB GLU A 13 2859 3378 2061 55 -359 173 C ATOM 108 CG GLU A 13 -27.256 3.779 8.165 1.00 25.57 C ANISOU 108 CG GLU A 13 3349 3824 2542 63 -281 184 C ATOM 109 CD GLU A 13 -26.615 3.041 9.328 1.00 29.76 C ANISOU 109 CD GLU A 13 3820 4374 3115 57 -202 153 C ATOM 110 OE1 GLU A 13 -26.494 3.647 10.415 1.00 32.21 O ANISOU 110 OE1 GLU A 13 4076 4683 3479 86 -183 148 O ATOM 111 OE2 GLU A 13 -26.236 1.860 9.161 1.00 29.22 O ANISOU 111 OE2 GLU A 13 3765 4316 3022 25 -164 134 O ATOM 112 N LEU A 14 -30.528 1.640 5.736 1.00 18.40 N ANISOU 112 N LEU A 14 2466 2975 1548 -3 -534 160 N ATOM 113 CA LEU A 14 -31.738 0.844 5.545 1.00 20.95 C ANISOU 113 CA LEU A 14 2740 3329 1891 -27 -614 141 C ATOM 114 C LEU A 14 -31.449 -0.420 4.748 1.00 20.98 C ANISOU 114 C LEU A 14 2827 3325 1820 -89 -607 114 C ATOM 115 O LEU A 14 -32.011 -1.482 5.038 1.00 21.70 O ANISOU 115 O LEU A 14 2869 3433 1942 -126 -620 84 O ATOM 116 CB LEU A 14 -32.816 1.681 4.857 1.00 27.81 C ANISOU 116 CB LEU A 14 3602 4201 2765 1 -743 169 C ATOM 117 CG LEU A 14 -33.347 2.846 5.698 1.00 30.66 C ANISOU 117 CG LEU A 14 3864 4567 3218 73 -762 185 C ATOM 118 CD1 LEU A 14 -34.360 3.660 4.912 1.00 33.67 C ANISOU 118 CD1 LEU A 14 4246 4941 3605 110 -900 215 C ATOM 119 CD2 LEU A 14 -33.955 2.327 7.004 1.00 31.65 C ANISOU 119 CD2 LEU A 14 3845 4739 3440 79 -720 151 C ATOM 120 N ALA A 15 -30.575 -0.330 3.740 1.00 20.11 N ANISOU 120 N ALA A 15 2846 3186 1609 -104 -582 121 N ATOM 121 CA ALA A 15 -30.179 -1.527 3.006 1.00 19.24 C ANISOU 121 CA ALA A 15 2824 3062 1423 -154 -559 84 C ATOM 122 C ALA A 15 -29.521 -2.545 3.931 1.00 21.99 C ANISOU 122 C ALA A 15 3129 3407 1820 -164 -459 48 C ATOM 123 O ALA A 15 -29.809 -3.745 3.855 1.00 20.59 O ANISOU 123 O ALA A 15 2961 3224 1641 -203 -470 10 O ATOM 124 CB ALA A 15 -29.236 -1.152 1.863 1.00 19.66 C ANISOU 124 CB ALA A 15 3020 3093 1359 -162 -523 97 C ATOM 125 N ILE A 16 -28.636 -2.085 4.814 1.00 17.69 N ANISOU 125 N ILE A 16 2542 2860 1319 -131 -368 59 N ATOM 126 CA ILE A 16 -27.988 -2.995 5.754 1.00 18.45 C ANISOU 126 CA ILE A 16 2596 2950 1463 -135 -285 32 C ATOM 127 C ILE A 16 -29.011 -3.595 6.710 1.00 20.91 C ANISOU 127 C ILE A 16 2807 3283 1854 -149 -322 24 C ATOM 128 O ILE A 16 -28.942 -4.787 7.044 1.00 19.37 O ANISOU 128 O ILE A 16 2611 3074 1676 -179 -298 -2 O ATOM 129 CB ILE A 16 -26.869 -2.264 6.514 1.00 16.36 C ANISOU 129 CB ILE A 16 2302 2682 1231 -98 -198 50 C ATOM 130 CG1 ILE A 16 -25.761 -1.834 5.555 1.00 22.98 C ANISOU 130 CG1 ILE A 16 3235 3502 1995 -97 -143 58 C ATOM 131 CG2 ILE A 16 -26.296 -3.152 7.617 1.00 16.60 C ANISOU 131 CG2 ILE A 16 2280 2707 1318 -95 -131 30 C ATOM 132 CD1 ILE A 16 -24.806 -0.846 6.180 1.00 22.41 C ANISOU 132 CD1 ILE A 16 3130 3428 1958 -70 -81 84 C ATOM 133 N ALA A 17 -29.970 -2.782 7.168 1.00 18.84 N ANISOU 133 N ALA A 17 2463 3053 1644 -129 -377 47 N ATOM 134 CA ALA A 17 -30.971 -3.276 8.109 1.00 20.34 C ANISOU 134 CA ALA A 17 2544 3273 1909 -145 -398 41 C ATOM 135 C ALA A 17 -31.779 -4.421 7.508 1.00 20.31 C ANISOU 135 C ALA A 17 2556 3267 1894 -207 -462 19 C ATOM 136 O ALA A 17 -32.006 -5.441 8.171 1.00 22.53 O ANISOU 136 O ALA A 17 2799 3548 2214 -247 -440 5 O ATOM 137 CB ALA A 17 -31.892 -2.139 8.547 1.00 19.31 C ANISOU 137 CB ALA A 17 2322 3181 1836 -104 -444 62 C ATOM 138 N AVAL A 18 -32.241 -4.253 6.264 1.00 19.61 N ANISOU 138 N AVAL A 18 2529 3174 1749 -222 -549 17 N ATOM 139 CA AVAL A 18 -32.981 -5.311 5.579 1.00 21.95 C ANISOU 139 CA AVAL A 18 2853 3461 2025 -287 -624 -9 C ATOM 140 C AVAL A 18 -32.147 -6.582 5.502 1.00 22.35 C ANISOU 140 C AVAL A 18 2987 3464 2041 -323 -560 -45 C ATOM 141 O AVAL A 18 -32.638 -7.687 5.767 1.00 22.62 O ANISOU 141 O AVAL A 18 3001 3486 2109 -378 -579 -65 O ATOM 142 CB AVAL A 18 -33.402 -4.838 4.173 1.00 23.55 C ANISOU 142 CB AVAL A 18 3137 3661 2152 -291 -729 -4 C ATOM 143 CG1AVAL A 18 -33.995 -5.995 3.376 1.00 22.92 C ANISOU 143 CG1AVAL A 18 3112 3564 2034 -365 -809 -40 C ATOM 144 CG2AVAL A 18 -34.392 -3.680 4.268 1.00 23.82 C ANISOU 144 CG2AVAL A 18 3077 3735 2237 -252 -813 32 C ATOM 145 N LEU A 19 -30.873 -6.446 5.136 1.00 23.57 N ANISOU 145 N LEU A 19 3233 3588 2133 -292 -484 -53 N ATOM 146 CA LEU A 19 -30.023 -7.618 4.951 1.00 24.32 C ANISOU 146 CA LEU A 19 3412 3633 2197 -311 -424 -94 C ATOM 147 C LEU A 19 -29.709 -8.289 6.281 1.00 23.62 C ANISOU 147 C LEU A 19 3253 3533 2189 -310 -357 -92 C ATOM 148 O LEU A 19 -29.621 -9.520 6.353 1.00 24.32 O ANISOU 148 O LEU A 19 3378 3577 2286 -345 -349 -122 O ATOM 149 CB LEU A 19 -28.729 -7.223 4.238 1.00 23.27 C ANISOU 149 CB LEU A 19 3376 3481 1984 -273 -349 -103 C ATOM 150 CG LEU A 19 -28.861 -6.748 2.792 1.00 23.82 C ANISOU 150 CG LEU A 19 3553 3552 1945 -283 -402 -107 C ATOM 151 CD1 LEU A 19 -27.510 -6.254 2.268 1.00 25.93 C ANISOU 151 CD1 LEU A 19 3899 3811 2143 -249 -302 -107 C ATOM 152 CD2 LEU A 19 -29.420 -7.854 1.903 1.00 25.80 C ANISOU 152 CD2 LEU A 19 3891 3774 2138 -338 -470 -157 C ATOM 153 N ALA A 20 -29.534 -7.492 7.339 1.00 22.80 N ANISOU 153 N ALA A 20 3060 3463 2142 -271 -314 -57 N ATOM 154 CA ALA A 20 -29.252 -8.048 8.659 1.00 24.31 C ANISOU 154 CA ALA A 20 3192 3647 2399 -270 -257 -48 C ATOM 155 C ALA A 20 -30.455 -8.804 9.206 1.00 25.71 C ANISOU 155 C ALA A 20 3304 3836 2628 -330 -305 -43 C ATOM 156 O ALA A 20 -30.300 -9.841 9.861 1.00 23.11 O ANISOU 156 O ALA A 20 2978 3474 2329 -360 -277 -46 O ATOM 157 CB ALA A 20 -28.846 -6.933 9.623 1.00 19.03 C ANISOU 157 CB ALA A 20 2451 3014 1765 -218 -209 -16 C ATOM 158 N ILE A 21 -31.660 -8.289 8.961 1.00 21.28 N ANISOU 158 N ILE A 21 2682 3321 2084 -350 -379 -32 N ATOM 159 CA ILE A 21 -32.864 -8.966 9.426 1.00 23.69 C ANISOU 159 CA ILE A 21 2909 3646 2446 -416 -423 -27 C ATOM 160 C ILE A 21 -33.069 -10.269 8.664 1.00 25.95 C ANISOU 160 C ILE A 21 3276 3877 2708 -487 -472 -59 C ATOM 161 O ILE A 21 -33.266 -11.331 9.264 1.00 27.93 O ANISOU 161 O ILE A 21 3516 4098 2996 -543 -459 -58 O ATOM 162 CB ILE A 21 -34.078 -8.029 9.305 1.00 24.31 C ANISOU 162 CB ILE A 21 2886 3791 2559 -410 -492 -11 C ATOM 163 CG1 ILE A 21 -33.947 -6.883 10.314 1.00 22.22 C ANISOU 163 CG1 ILE A 21 2538 3573 2332 -343 -435 14 C ATOM 164 CG2 ILE A 21 -35.376 -8.791 9.528 1.00 26.47 C ANISOU 164 CG2 ILE A 21 3076 4090 2892 -490 -548 -10 C ATOM 165 CD1 ILE A 21 -34.891 -5.731 10.051 1.00 26.51 C ANISOU 165 CD1 ILE A 21 3000 4168 2904 -305 -499 24 C ATOM 166 N LEU A 22 -32.981 -10.215 7.332 1.00 22.30 N ANISOU 166 N LEU A 22 2905 3391 2175 -488 -529 -88 N ATOM 167 CA LEU A 22 -33.273 -11.388 6.513 1.00 22.68 C ANISOU 167 CA LEU A 22 3039 3385 2192 -557 -589 -129 C ATOM 168 C LEU A 22 -32.282 -12.517 6.775 1.00 25.64 C ANISOU 168 C LEU A 22 3500 3682 2560 -560 -518 -155 C ATOM 169 O LEU A 22 -32.676 -13.675 6.957 1.00 23.94 O ANISOU 169 O LEU A 22 3301 3419 2375 -628 -544 -169 O ATOM 170 CB LEU A 22 -33.267 -11.010 5.032 1.00 26.88 C ANISOU 170 CB LEU A 22 3671 3912 2631 -549 -657 -156 C ATOM 171 CG LEU A 22 -34.457 -10.208 4.497 1.00 31.11 C ANISOU 171 CG LEU A 22 4144 4505 3171 -563 -771 -137 C ATOM 172 CD1 LEU A 22 -34.267 -9.932 3.010 1.00 30.40 C ANISOU 172 CD1 LEU A 22 4186 4398 2967 -556 -834 -162 C ATOM 173 CD2 LEU A 22 -35.772 -10.932 4.748 1.00 35.14 C ANISOU 173 CD2 LEU A 22 4567 5030 3755 -649 -856 -138 C ATOM 174 N GLY A 23 -30.987 -12.205 6.779 1.00 23.01 N ANISOU 174 N GLY A 23 3221 3331 2193 -488 -433 -161 N ATOM 175 CA GLY A 23 -29.996 -13.250 6.964 1.00 22.97 C ANISOU 175 CA GLY A 23 3292 3248 2186 -476 -371 -190 C ATOM 176 C GLY A 23 -30.074 -13.891 8.335 1.00 24.84 C ANISOU 176 C GLY A 23 3465 3469 2505 -498 -340 -157 C ATOM 177 O GLY A 23 -29.949 -15.110 8.471 1.00 25.22 O ANISOU 177 O GLY A 23 3569 3442 2572 -533 -342 -176 O ATOM 178 N ASN A 24 -30.298 -13.087 9.370 1.00 23.77 N ANISOU 178 N ASN A 24 3220 3398 2415 -480 -312 -106 N ATOM 179 CA ASN A 24 -30.254 -13.648 10.711 1.00 22.58 C ANISOU 179 CA ASN A 24 3022 3235 2324 -497 -273 -71 C ATOM 180 C ASN A 24 -31.568 -14.309 11.105 1.00 23.11 C ANISOU 180 C ASN A 24 3035 3309 2436 -594 -325 -51 C ATOM 181 O ASN A 24 -31.560 -15.256 11.899 1.00 23.88 O ANISOU 181 O ASN A 24 3142 3361 2569 -636 -307 -30 O ATOM 182 CB ASN A 24 -29.835 -12.566 11.699 1.00 20.93 C ANISOU 182 CB ASN A 24 2733 3088 2133 -437 -215 -32 C ATOM 183 CG ASN A 24 -28.362 -12.254 11.588 1.00 23.25 C ANISOU 183 CG ASN A 24 3078 3356 2401 -357 -155 -45 C ATOM 184 OD1 ASN A 24 -27.517 -13.039 12.035 1.00 22.03 O ANISOU 184 OD1 ASN A 24 2964 3144 2262 -340 -119 -47 O ATOM 185 ND2 ASN A 24 -28.038 -11.134 10.948 1.00 17.64 N ANISOU 185 ND2 ASN A 24 2365 2683 1654 -310 -147 -53 N ATOM 186 N VAL A 25 -32.694 -13.853 10.554 1.00 20.54 N ANISOU 186 N VAL A 25 2653 3038 2113 -633 -392 -55 N ATOM 187 CA VAL A 25 -33.934 -14.608 10.708 1.00 24.54 C ANISOU 187 CA VAL A 25 3111 3547 2668 -738 -450 -44 C ATOM 188 C VAL A 25 -33.779 -15.997 10.096 1.00 25.29 C ANISOU 188 C VAL A 25 3324 3537 2749 -798 -489 -81 C ATOM 189 O VAL A 25 -34.269 -16.992 10.642 1.00 29.01 O ANISOU 189 O VAL A 25 3789 3968 3266 -882 -500 -63 O ATOM 190 CB VAL A 25 -35.114 -13.827 10.097 1.00 23.96 C ANISOU 190 CB VAL A 25 2949 3549 2604 -759 -528 -47 C ATOM 191 CG1 VAL A 25 -36.290 -14.744 9.823 1.00 25.89 C ANISOU 191 CG1 VAL A 25 3166 3780 2889 -875 -610 -53 C ATOM 192 CG2 VAL A 25 -35.540 -12.706 11.036 1.00 25.40 C ANISOU 192 CG2 VAL A 25 2994 3828 2829 -717 -485 -8 C ATOM 193 N LEU A 26 -33.058 -16.089 8.975 1.00 24.59 N ANISOU 193 N LEU A 26 3352 3397 2594 -756 -505 -134 N ATOM 194 CA LEU A 26 -32.783 -17.384 8.361 1.00 25.15 C ANISOU 194 CA LEU A 26 3551 3359 2645 -797 -534 -182 C ATOM 195 C LEU A 26 -31.959 -18.276 9.286 1.00 25.61 C ANISOU 195 C LEU A 26 3652 3339 2740 -783 -469 -166 C ATOM 196 O LEU A 26 -32.206 -19.485 9.375 1.00 26.15 O ANISOU 196 O LEU A 26 3779 3320 2837 -853 -500 -175 O ATOM 197 CB LEU A 26 -32.061 -17.175 7.029 1.00 27.65 C ANISOU 197 CB LEU A 26 3984 3648 2872 -740 -542 -246 C ATOM 198 CG LEU A 26 -31.771 -18.402 6.165 1.00 36.33 C ANISOU 198 CG LEU A 26 5233 4637 3934 -769 -574 -316 C ATOM 199 CD1 LEU A 26 -33.061 -19.001 5.611 1.00 37.23 C ANISOU 199 CD1 LEU A 26 5357 4733 4055 -885 -692 -335 C ATOM 200 CD2 LEU A 26 -30.814 -18.033 5.038 1.00 38.47 C ANISOU 200 CD2 LEU A 26 5612 4897 4109 -690 -540 -374 C ATOM 201 N VAL A 27 -30.970 -17.697 9.974 1.00 23.58 N ANISOU 201 N VAL A 27 3371 3105 2484 -694 -386 -140 N ATOM 202 CA VAL A 27 -30.184 -18.454 10.947 1.00 24.96 C ANISOU 202 CA VAL A 27 3577 3212 2697 -673 -334 -115 C ATOM 203 C VAL A 27 -31.086 -19.014 12.040 1.00 25.62 C ANISOU 203 C VAL A 27 3600 3296 2838 -766 -348 -55 C ATOM 204 O VAL A 27 -31.011 -20.200 12.386 1.00 26.96 O ANISOU 204 O VAL A 27 3837 3369 3036 -812 -359 -46 O ATOM 205 CB VAL A 27 -29.070 -17.573 11.545 1.00 24.18 C ANISOU 205 CB VAL A 27 3440 3156 2592 -568 -255 -93 C ATOM 206 CG1 VAL A 27 -28.398 -18.288 12.710 1.00 23.06 C ANISOU 206 CG1 VAL A 27 3314 2955 2492 -551 -218 -54 C ATOM 207 CG2 VAL A 27 -28.049 -17.193 10.486 1.00 24.21 C ANISOU 207 CG2 VAL A 27 3509 3146 2542 -484 -227 -150 C ATOM 208 N CYS A 28 -31.946 -18.162 12.610 1.00 25.50 N ANISOU 208 N CYS A 28 3461 3389 2841 -793 -343 -12 N ATOM 209 CA CYS A 28 -32.823 -18.606 13.691 1.00 27.60 C ANISOU 209 CA CYS A 28 3659 3673 3156 -884 -338 48 C ATOM 210 C CYS A 28 -33.815 -19.653 13.203 1.00 31.16 C ANISOU 210 C CYS A 28 4136 4069 3635 -1007 -412 36 C ATOM 211 O CYS A 28 -34.118 -20.611 13.924 1.00 35.44 O ANISOU 211 O CYS A 28 4695 4556 4214 -1089 -409 76 O ATOM 212 CB CYS A 28 -33.563 -17.414 14.300 1.00 26.63 C ANISOU 212 CB CYS A 28 3391 3682 3045 -879 -310 82 C ATOM 213 SG CYS A 28 -32.502 -16.190 15.107 1.00 27.43 S ANISOU 213 SG CYS A 28 3459 3845 3120 -754 -227 102 S ATOM 214 N ATRP A 29 -34.342 -19.484 11.988 0.49 30.96 N ANISOU 214 N ATRP A 29 4119 4054 3591 -1027 -483 -16 N ATOM 215 N BTRP A 29 -34.321 -19.491 11.979 0.51 30.95 N ANISOU 215 N BTRP A 29 4121 4052 3589 -1026 -483 -17 N ATOM 216 CA ATRP A 29 -35.263 -20.478 11.448 0.49 32.47 C ANISOU 216 CA ATRP A 29 4341 4188 3809 -1149 -567 -35 C ATOM 217 CA BTRP A 29 -35.262 -20.459 11.425 0.51 32.45 C ANISOU 217 CA BTRP A 29 4338 4187 3805 -1148 -568 -36 C ATOM 218 C ATRP A 29 -34.563 -21.812 11.217 0.49 31.82 C ANISOU 218 C ATRP A 29 4416 3953 3721 -1165 -581 -65 C ATOM 219 C BTRP A 29 -34.588 -21.797 11.141 0.51 31.84 C ANISOU 219 C BTRP A 29 4420 3957 3722 -1165 -585 -69 C ATOM 220 O ATRP A 29 -35.148 -22.874 11.457 0.49 31.94 O ANISOU 220 O ATRP A 29 4459 3897 3780 -1276 -620 -48 O ATOM 221 O BTRP A 29 -35.222 -22.849 11.274 0.51 32.56 O ANISOU 221 O BTRP A 29 4540 3978 3855 -1279 -631 -57 O ATOM 222 CB ATRP A 29 -35.896 -19.971 10.150 0.49 36.02 C ANISOU 222 CB ATRP A 29 4778 4681 4228 -1159 -654 -88 C ATOM 223 CB BTRP A 29 -35.899 -19.883 10.157 0.51 35.94 C ANISOU 223 CB BTRP A 29 4761 4678 4217 -1154 -652 -87 C ATOM 224 CG ATRP A 29 -37.181 -19.211 10.352 0.49 40.89 C ANISOU 224 CG ATRP A 29 5229 5418 4889 -1210 -687 -56 C ATOM 225 CG BTRP A 29 -37.127 -20.606 9.674 0.51 41.87 C ANISOU 225 CG BTRP A 29 5493 5409 5005 -1290 -753 -100 C ATOM 226 CD1ATRP A 29 -37.366 -17.866 10.232 0.49 40.97 C ANISOU 226 CD1ATRP A 29 5144 5537 4887 -1137 -679 -50 C ATOM 227 CD1BTRP A 29 -37.302 -21.192 8.456 0.51 45.39 C ANISOU 227 CD1BTRP A 29 6043 5786 5417 -1333 -849 -165 C ATOM 228 CD2ATRP A 29 -38.458 -19.759 10.710 0.49 45.09 C ANISOU 228 CD2ATRP A 29 5666 5971 5493 -1344 -732 -26 C ATOM 229 CD2BTRP A 29 -38.351 -20.809 10.395 0.51 46.01 C ANISOU 229 CD2BTRP A 29 5884 5987 5609 -1405 -770 -48 C ATOM 230 NE1ATRP A 29 -38.677 -17.540 10.489 0.49 41.95 N ANISOU 230 NE1ATRP A 29 5115 5749 5074 -1204 -717 -23 N ATOM 231 NE1BTRP A 29 -38.554 -21.748 8.370 0.51 47.70 N ANISOU 231 NE1BTRP A 29 6275 6082 5768 -1471 -936 -157 N ATOM 232 CE2ATRP A 29 -39.367 -18.685 10.788 0.49 46.00 C ANISOU 232 CE2ATRP A 29 5620 6218 5642 -1335 -746 -7 C ATOM 233 CE2BTRP A 29 -39.218 -21.529 9.549 0.51 49.01 C ANISOU 233 CE2BTRP A 29 6288 6325 6008 -1519 -885 -83 C ATOM 234 CE3ATRP A 29 -38.919 -21.053 10.972 0.49 47.90 C ANISOU 234 CE3ATRP A 29 6057 6246 5895 -1472 -761 -12 C ATOM 235 CE3BTRP A 29 -38.797 -20.453 11.673 0.51 46.84 C ANISOU 235 CE3BTRP A 29 5854 6175 5768 -1426 -695 23 C ATOM 236 CZ2ATRP A 29 -40.710 -18.864 11.116 0.49 48.41 C ANISOU 236 CZ2ATRP A 29 5783 6584 6026 -1447 -783 22 C ATOM 237 CZ2BTRP A 29 -40.504 -21.902 9.938 0.51 50.80 C ANISOU 237 CZ2BTRP A 29 6394 6591 6317 -1656 -927 -46 C ATOM 238 CZ3ATRP A 29 -40.254 -21.229 11.298 0.49 49.37 C ANISOU 238 CZ3ATRP A 29 6110 6493 6158 -1596 -797 22 C ATOM 239 CZ3BTRP A 29 -40.074 -20.825 12.058 0.51 48.97 C ANISOU 239 CZ3BTRP A 29 6007 6488 6113 -1558 -724 58 C ATOM 240 CH2ATRP A 29 -41.133 -20.140 11.367 0.49 49.46 C ANISOU 240 CH2ATRP A 29 5946 6645 6203 -1581 -805 37 C ATOM 241 CH2BTRP A 29 -40.913 -21.542 11.193 0.51 50.50 C ANISOU 241 CH2BTRP A 29 6213 6639 6335 -1673 -840 26 C ATOM 242 N ALA A 30 -33.306 -21.780 10.764 1.00 31.17 N ANISOU 242 N ALA A 30 4435 3816 3591 -1055 -547 -110 N ATOM 243 CA ALA A 30 -32.584 -23.027 10.523 1.00 34.13 C ANISOU 243 CA ALA A 30 4960 4042 3967 -1050 -556 -147 C ATOM 244 C ALA A 30 -32.367 -23.806 11.816 1.00 34.10 C ANISOU 244 C ALA A 30 4964 3973 4018 -1079 -521 -78 C ATOM 245 O ALA A 30 -32.522 -25.032 11.838 1.00 35.51 O ANISOU 245 O ALA A 30 5235 4029 4229 -1151 -562 -82 O ATOM 246 CB ALA A 30 -31.244 -22.741 9.843 1.00 24.68 C ANISOU 246 CB ALA A 30 3846 2815 2714 -915 -510 -208 C ATOM 247 N VAL A 31 -32.005 -23.119 12.901 1.00 32.32 N ANISOU 247 N VAL A 31 4656 3821 3801 -1027 -450 -15 N ATOM 248 CA VAL A 31 -31.798 -23.815 14.168 1.00 30.87 C ANISOU 248 CA VAL A 31 4490 3583 3657 -1056 -421 59 C ATOM 249 C VAL A 31 -33.124 -24.347 14.704 1.00 31.29 C ANISOU 249 C VAL A 31 4492 3646 3752 -1212 -451 115 C ATOM 250 O VAL A 31 -33.190 -25.455 15.246 1.00 29.51 O ANISOU 250 O VAL A 31 4338 3315 3559 -1285 -466 155 O ATOM 251 CB VAL A 31 -31.097 -22.890 15.182 1.00 31.67 C ANISOU 251 CB VAL A 31 4520 3768 3745 -965 -344 108 C ATOM 252 CG1 VAL A 31 -30.953 -23.588 16.530 1.00 30.99 C ANISOU 252 CG1 VAL A 31 4457 3631 3685 -1002 -322 192 C ATOM 253 CG2 VAL A 31 -29.727 -22.465 14.658 1.00 22.84 C ANISOU 253 CG2 VAL A 31 3449 2632 2597 -820 -314 55 C ATOM 254 N TRP A 32 -34.201 -23.576 14.542 1.00 31.70 N ANISOU 254 N TRP A 32 4418 3820 3808 -1268 -462 119 N ATOM 255 CA TRP A 32 -35.517 -24.024 14.987 1.00 35.87 C ANISOU 255 CA TRP A 32 4873 4373 4384 -1421 -485 169 C ATOM 256 C TRP A 32 -35.952 -25.296 14.263 1.00 39.39 C ANISOU 256 C TRP A 32 5420 4689 4858 -1530 -572 136 C ATOM 257 O TRP A 32 -36.541 -26.194 14.874 1.00 38.64 O ANISOU 257 O TRP A 32 5335 4538 4808 -1656 -583 191 O ATOM 258 CB TRP A 32 -36.544 -22.912 14.768 1.00 39.06 C ANISOU 258 CB TRP A 32 5114 4932 4794 -1441 -489 164 C ATOM 259 CG TRP A 32 -37.952 -23.286 15.152 1.00 47.06 C ANISOU 259 CG TRP A 32 6023 5989 5867 -1597 -509 208 C ATOM 260 CD1 TRP A 32 -38.856 -23.987 14.398 1.00 48.62 C ANISOU 260 CD1 TRP A 32 6224 6145 6104 -1719 -600 182 C ATOM 261 CD2 TRP A 32 -38.621 -22.957 16.375 1.00 54.49 C ANISOU 261 CD2 TRP A 32 6837 7032 6836 -1651 -433 284 C ATOM 262 NE1 TRP A 32 -40.038 -24.124 15.085 1.00 52.02 N ANISOU 262 NE1 TRP A 32 6525 6646 6595 -1849 -584 241 N ATOM 263 CE2 TRP A 32 -39.921 -23.500 16.299 1.00 56.79 C ANISOU 263 CE2 TRP A 32 7047 7340 7190 -1808 -475 303 C ATOM 264 CE3 TRP A 32 -38.246 -22.262 17.531 1.00 57.75 C ANISOU 264 CE3 TRP A 32 7197 7522 7222 -1585 -332 333 C ATOM 265 CZ2 TRP A 32 -40.846 -23.367 17.333 1.00 61.55 C ANISOU 265 CZ2 TRP A 32 7513 8043 7832 -1899 -407 371 C ATOM 266 CZ3 TRP A 32 -39.167 -22.130 18.555 1.00 60.80 C ANISOU 266 CZ3 TRP A 32 7461 8003 7636 -1672 -267 397 C ATOM 267 CH2 TRP A 32 -40.451 -22.680 18.449 1.00 62.64 C ANISOU 267 CH2 TRP A 32 7609 8257 7934 -1826 -298 416 C ATOM 268 N LEU A 33 -35.666 -25.397 12.961 1.00 41.37 N ANISOU 268 N LEU A 33 5753 4886 5079 -1490 -635 47 N ATOM 269 CA LEU A 33 -36.196 -26.510 12.181 1.00 43.99 C ANISOU 269 CA LEU A 33 6178 5102 5433 -1599 -729 3 C ATOM 270 C LEU A 33 -35.305 -27.747 12.252 1.00 42.62 C ANISOU 270 C LEU A 33 6182 4746 5267 -1581 -736 -11 C ATOM 271 O LEU A 33 -35.812 -28.872 12.315 1.00 44.89 O ANISOU 271 O LEU A 33 6537 4921 5598 -1704 -791 1 O ATOM 272 CB LEU A 33 -36.390 -26.086 10.725 1.00 47.03 C ANISOU 272 CB LEU A 33 6584 5513 5772 -1573 -802 -90 C ATOM 273 CG LEU A 33 -37.498 -25.072 10.421 1.00 51.39 C ANISOU 273 CG LEU A 33 6975 6219 6331 -1614 -838 -83 C ATOM 274 CD1 LEU A 33 -37.578 -24.839 8.924 1.00 53.23 C ANISOU 274 CD1 LEU A 33 7270 6448 6506 -1591 -925 -174 C ATOM 275 CD2 LEU A 33 -38.841 -25.538 10.967 1.00 52.81 C ANISOU 275 CD2 LEU A 33 7048 6426 6590 -1783 -875 -27 C ATOM 276 N ASN A 34 -33.986 -27.570 12.234 1.00 38.21 N ANISOU 276 N ASN A 34 5696 4150 4673 -1431 -684 -38 N ATOM 277 CA ASN A 34 -33.063 -28.692 12.115 1.00 40.11 C ANISOU 277 CA ASN A 34 6104 4214 4924 -1387 -696 -71 C ATOM 278 C ASN A 34 -32.578 -29.117 13.497 1.00 38.52 C ANISOU 278 C ASN A 34 5913 3963 4760 -1377 -646 24 C ATOM 279 O ASN A 34 -31.869 -28.363 14.170 1.00 32.03 O ANISOU 279 O ASN A 34 5031 3218 3920 -1274 -576 61 O ATOM 280 CB ASN A 34 -31.886 -28.314 11.218 1.00 41.18 C ANISOU 280 CB ASN A 34 6308 4334 5004 -1227 -667 -162 C ATOM 281 CG ASN A 34 -31.082 -29.518 10.774 1.00 44.59 C ANISOU 281 CG ASN A 34 6916 4579 5448 -1183 -692 -226 C ATOM 282 OD1 ASN A 34 -31.165 -30.595 11.371 1.00 46.97 O ANISOU 282 OD1 ASN A 34 7292 4751 5805 -1245 -721 -186 O ATOM 283 ND2 ASN A 34 -30.288 -29.340 9.728 1.00 44.19 N ANISOU 283 ND2 ASN A 34 6935 4509 5345 -1072 -676 -326 N ATOM 284 N SER A 35 -32.946 -30.336 13.909 1.00 36.60 N ANISOU 284 N SER A 35 5755 3586 4565 -1486 -691 64 N ATOM 285 CA SER A 35 -32.501 -30.836 15.207 1.00 39.28 C ANISOU 285 CA SER A 35 6127 3864 4934 -1485 -656 162 C ATOM 286 C SER A 35 -30.999 -31.093 15.224 1.00 41.19 C ANISOU 286 C SER A 35 6472 4007 5172 -1318 -635 131 C ATOM 287 O SER A 35 -30.373 -31.043 16.291 1.00 44.68 O ANISOU 287 O SER A 35 6909 4448 5620 -1263 -596 206 O ATOM 288 CB SER A 35 -33.270 -32.107 15.581 1.00 44.49 C ANISOU 288 CB SER A 35 6866 4391 5646 -1651 -714 216 C ATOM 289 OG SER A 35 -33.006 -33.162 14.672 1.00 48.26 O ANISOU 289 OG SER A 35 7502 4688 6146 -1653 -788 135 O ATOM 290 N ASN A 36 -30.399 -31.358 14.061 1.00 37.21 N ANISOU 290 N ASN A 36 6059 3423 4656 -1233 -661 18 N ATOM 291 CA ASN A 36 -28.946 -31.479 13.988 1.00 40.04 C ANISOU 291 CA ASN A 36 6488 3709 5017 -1061 -629 -23 C ATOM 292 C ASN A 36 -28.234 -30.155 14.243 1.00 39.22 C ANISOU 292 C ASN A 36 6264 3763 4875 -936 -551 -15 C ATOM 293 O ASN A 36 -27.017 -30.154 14.457 1.00 38.71 O ANISOU 293 O ASN A 36 6225 3660 4823 -799 -518 -25 O ATOM 294 CB ASN A 36 -28.525 -32.035 12.626 1.00 43.87 C ANISOU 294 CB ASN A 36 7094 4083 5490 -1003 -661 -156 C ATOM 295 CG ASN A 36 -29.183 -33.363 12.307 1.00 47.52 C ANISOU 295 CG ASN A 36 7691 4373 5991 -1124 -747 -177 C ATOM 296 OD1 ASN A 36 -29.450 -34.167 13.199 1.00 49.34 O ANISOU 296 OD1 ASN A 36 7967 4506 6274 -1205 -779 -92 O ATOM 297 ND2 ASN A 36 -29.456 -33.596 11.029 1.00 46.29 N ANISOU 297 ND2 ASN A 36 7608 4177 5804 -1143 -789 -290 N ATOM 298 N LEU A 37 -28.952 -29.038 14.226 1.00 37.33 N ANISOU 298 N LEU A 37 5893 3695 4598 -980 -524 3 N ATOM 299 CA LEU A 37 -28.380 -27.747 14.572 1.00 36.07 C ANISOU 299 CA LEU A 37 5619 3680 4405 -879 -455 20 C ATOM 300 C LEU A 37 -28.704 -27.330 15.997 1.00 34.66 C ANISOU 300 C LEU A 37 5351 3584 4233 -924 -424 133 C ATOM 301 O LEU A 37 -28.245 -26.274 16.433 1.00 31.02 O ANISOU 301 O LEU A 37 4801 3238 3747 -846 -371 153 O ATOM 302 CB LEU A 37 -28.867 -26.669 13.596 1.00 34.47 C ANISOU 302 CB LEU A 37 5336 3609 4151 -878 -445 -39 C ATOM 303 CG LEU A 37 -28.297 -26.734 12.177 1.00 35.42 C ANISOU 303 CG LEU A 37 5536 3684 4236 -802 -452 -155 C ATOM 304 CD1 LEU A 37 -28.988 -25.723 11.278 1.00 35.46 C ANISOU 304 CD1 LEU A 37 5471 3815 4186 -828 -461 -194 C ATOM 305 CD2 LEU A 37 -26.789 -26.502 12.188 1.00 32.97 C ANISOU 305 CD2 LEU A 37 5246 3357 3926 -642 -390 -184 C ATOM 306 N GLN A 38 -29.469 -28.136 16.734 1.00 35.48 N ANISOU 306 N GLN A 38 5484 3631 4366 -1049 -453 207 N ATOM 307 CA GLN A 38 -29.919 -27.771 18.078 1.00 35.45 C ANISOU 307 CA GLN A 38 5401 3714 4354 -1110 -415 315 C ATOM 308 C GLN A 38 -28.921 -28.314 19.096 1.00 38.35 C ANISOU 308 C GLN A 38 5845 3991 4734 -1045 -411 380 C ATOM 309 O GLN A 38 -29.069 -29.412 19.630 1.00 41.03 O ANISOU 309 O GLN A 38 6280 4207 5103 -1118 -448 439 O ATOM 310 CB GLN A 38 -31.330 -28.286 18.329 1.00 35.34 C ANISOU 310 CB GLN A 38 5365 3703 4361 -1291 -438 366 C ATOM 311 CG GLN A 38 -32.377 -27.616 17.457 1.00 37.74 C ANISOU 311 CG GLN A 38 5565 4118 4657 -1353 -449 312 C ATOM 312 CD GLN A 38 -33.749 -28.239 17.607 1.00 45.16 C ANISOU 312 CD GLN A 38 6477 5050 5632 -1538 -481 355 C ATOM 313 OE1 GLN A 38 -33.926 -29.214 18.338 1.00 47.37 O ANISOU 313 OE1 GLN A 38 6827 5234 5939 -1630 -491 426 O ATOM 314 NE2 GLN A 38 -34.728 -27.679 16.914 1.00 48.48 N ANISOU 314 NE2 GLN A 38 6793 5570 6056 -1597 -500 315 N ATOM 315 N ASN A 39 -27.887 -27.522 19.357 1.00 40.13 N ANISOU 315 N ASN A 39 6030 4277 4939 -909 -374 371 N ATOM 316 CA ASN A 39 -26.883 -27.820 20.363 1.00 39.15 C ANISOU 316 CA ASN A 39 5956 4095 4824 -833 -377 433 C ATOM 317 C ASN A 39 -26.546 -26.524 21.086 1.00 37.34 C ANISOU 317 C ASN A 39 5615 4020 4550 -772 -322 462 C ATOM 318 O ASN A 39 -26.971 -25.437 20.682 1.00 34.78 O ANISOU 318 O ASN A 39 5186 3830 4197 -771 -282 423 O ATOM 319 CB ASN A 39 -25.631 -28.439 19.735 1.00 41.14 C ANISOU 319 CB ASN A 39 6299 4214 5120 -701 -408 368 C ATOM 320 CG ASN A 39 -25.133 -27.647 18.543 1.00 41.86 C ANISOU 320 CG ASN A 39 6336 4370 5199 -602 -375 258 C ATOM 321 OD1 ASN A 39 -24.604 -26.550 18.696 1.00 39.97 O ANISOU 321 OD1 ASN A 39 6004 4247 4934 -523 -330 252 O ATOM 322 ND2 ASN A 39 -25.307 -28.198 17.344 1.00 42.48 N ANISOU 322 ND2 ASN A 39 6480 4371 5290 -610 -398 171 N ATOM 323 N VAL A 40 -25.759 -26.645 22.156 1.00 35.65 N ANISOU 323 N VAL A 40 5432 3780 4332 -718 -329 530 N ATOM 324 CA VAL A 40 -25.451 -25.486 22.992 1.00 32.47 C ANISOU 324 CA VAL A 40 4940 3514 3883 -672 -286 563 C ATOM 325 C VAL A 40 -24.696 -24.429 22.198 1.00 33.39 C ANISOU 325 C VAL A 40 4978 3708 4001 -551 -258 476 C ATOM 326 O VAL A 40 -24.961 -23.226 22.331 1.00 32.29 O ANISOU 326 O VAL A 40 4738 3707 3822 -547 -212 467 O ATOM 327 CB VAL A 40 -24.663 -25.923 24.239 1.00 33.54 C ANISOU 327 CB VAL A 40 5142 3591 4012 -634 -318 650 C ATOM 328 CG1 VAL A 40 -24.159 -24.707 24.989 1.00 37.23 C ANISOU 328 CG1 VAL A 40 5526 4190 4432 -570 -285 666 C ATOM 329 CG2 VAL A 40 -25.534 -26.781 25.130 1.00 33.54 C ANISOU 329 CG2 VAL A 40 5213 3539 3990 -772 -332 750 C ATOM 330 N THR A 41 -23.736 -24.856 21.372 1.00 32.91 N ANISOU 330 N THR A 41 4963 3555 3986 -452 -280 411 N ATOM 331 CA THR A 41 -22.989 -23.906 20.555 1.00 30.48 C ANISOU 331 CA THR A 41 4584 3317 3679 -347 -244 331 C ATOM 332 C THR A 41 -23.927 -23.034 19.733 1.00 31.36 C ANISOU 332 C THR A 41 4625 3538 3754 -401 -208 282 C ATOM 333 O THR A 41 -23.765 -21.808 19.676 1.00 28.72 O ANISOU 333 O THR A 41 4201 3320 3392 -361 -169 265 O ATOM 334 CB THR A 41 -22.022 -24.650 19.634 1.00 33.18 C ANISOU 334 CB THR A 41 4993 3541 4074 -251 -261 259 C ATOM 335 OG1 THR A 41 -21.293 -25.624 20.388 1.00 36.55 O ANISOU 335 OG1 THR A 41 5495 3845 4547 -205 -310 308 O ATOM 336 CG2 THR A 41 -21.046 -23.680 18.993 1.00 30.40 C ANISOU 336 CG2 THR A 41 4565 3263 3724 -137 -216 191 C ATOM 337 N ASN A 42 -24.929 -23.645 19.108 1.00 29.28 N ANISOU 337 N ASN A 42 4400 3234 3492 -495 -229 263 N ATOM 338 CA ASN A 42 -25.825 -22.897 18.243 1.00 24.76 C ANISOU 338 CA ASN A 42 3764 2755 2890 -543 -212 216 C ATOM 339 C ASN A 42 -26.885 -22.115 19.009 1.00 24.14 C ANISOU 339 C ASN A 42 3590 2801 2782 -625 -188 272 C ATOM 340 O ASN A 42 -27.536 -21.249 18.416 1.00 24.72 O ANISOU 340 O ASN A 42 3588 2970 2835 -642 -174 238 O ATOM 341 CB ASN A 42 -26.470 -23.845 17.231 1.00 25.65 C ANISOU 341 CB ASN A 42 3952 2776 3017 -611 -255 167 C ATOM 342 CG ASN A 42 -25.495 -24.277 16.148 1.00 29.41 C ANISOU 342 CG ASN A 42 4506 3162 3506 -516 -260 79 C ATOM 343 OD1 ASN A 42 -24.437 -23.673 15.983 1.00 30.33 O ANISOU 343 OD1 ASN A 42 4594 3311 3619 -402 -222 49 O ATOM 344 ND2 ASN A 42 -25.849 -25.312 15.400 1.00 29.42 N ANISOU 344 ND2 ASN A 42 4605 3052 3523 -563 -303 34 N ATOM 345 N TYR A 43 -27.072 -22.378 20.303 1.00 24.80 N ANISOU 345 N TYR A 43 3676 2888 2861 -671 -182 356 N ATOM 346 CA TYR A 43 -27.927 -21.494 21.092 1.00 27.48 C ANISOU 346 CA TYR A 43 3917 3358 3165 -727 -140 399 C ATOM 347 C TYR A 43 -27.278 -20.125 21.260 1.00 25.34 C ANISOU 347 C TYR A 43 3571 3190 2867 -627 -103 378 C ATOM 348 O TYR A 43 -27.963 -19.096 21.230 1.00 23.38 O ANISOU 348 O TYR A 43 3231 3056 2597 -642 -71 366 O ATOM 349 CB TYR A 43 -28.239 -22.130 22.447 1.00 27.99 C ANISOU 349 CB TYR A 43 4018 3401 3217 -803 -134 495 C ATOM 350 CG TYR A 43 -28.936 -23.465 22.322 1.00 33.38 C ANISOU 350 CG TYR A 43 4777 3977 3930 -917 -172 524 C ATOM 351 CD1 TYR A 43 -29.739 -23.749 21.221 1.00 35.08 C ANISOU 351 CD1 TYR A 43 4980 4174 4174 -981 -197 471 C ATOM 352 CD2 TYR A 43 -28.776 -24.450 23.287 1.00 36.55 C ANISOU 352 CD2 TYR A 43 5269 4288 4331 -965 -190 607 C ATOM 353 CE1 TYR A 43 -30.365 -24.971 21.088 1.00 37.75 C ANISOU 353 CE1 TYR A 43 5391 4407 4544 -1093 -238 495 C ATOM 354 CE2 TYR A 43 -29.402 -25.677 23.165 1.00 40.87 C ANISOU 354 CE2 TYR A 43 5894 4726 4911 -1077 -227 638 C ATOM 355 CZ TYR A 43 -30.195 -25.931 22.064 1.00 43.07 C ANISOU 355 CZ TYR A 43 6154 4987 5222 -1143 -250 579 C ATOM 356 OH TYR A 43 -30.822 -27.149 21.937 1.00 50.70 O ANISOU 356 OH TYR A 43 7200 5839 6225 -1263 -294 606 O ATOM 357 N PHE A 44 -25.952 -20.091 21.422 1.00 20.62 N ANISOU 357 N PHE A 44 3009 2550 2276 -525 -109 371 N ATOM 358 CA PHE A 44 -25.250 -18.812 21.430 1.00 21.14 C ANISOU 358 CA PHE A 44 3006 2702 2324 -435 -81 344 C ATOM 359 C PHE A 44 -25.227 -18.181 20.043 1.00 21.70 C ANISOU 359 C PHE A 44 3044 2802 2400 -397 -71 265 C ATOM 360 O PHE A 44 -25.289 -16.951 19.923 1.00 22.88 O ANISOU 360 O PHE A 44 3119 3046 2528 -368 -44 246 O ATOM 361 CB PHE A 44 -23.832 -19.001 21.972 1.00 21.44 C ANISOU 361 CB PHE A 44 3081 2686 2378 -344 -97 360 C ATOM 362 CG PHE A 44 -23.792 -19.446 23.411 1.00 25.31 C ANISOU 362 CG PHE A 44 3609 3160 2849 -375 -114 444 C ATOM 363 CD1 PHE A 44 -24.154 -18.574 24.427 1.00 32.07 C ANISOU 363 CD1 PHE A 44 4414 4118 3651 -399 -84 482 C ATOM 364 CD2 PHE A 44 -23.402 -20.731 23.747 1.00 25.95 C ANISOU 364 CD2 PHE A 44 3785 3117 2957 -380 -160 485 C ATOM 365 CE1 PHE A 44 -24.129 -18.980 25.750 1.00 31.82 C ANISOU 365 CE1 PHE A 44 4431 4075 3584 -432 -97 560 C ATOM 366 CE2 PHE A 44 -23.369 -21.139 25.067 1.00 29.20 C ANISOU 366 CE2 PHE A 44 4245 3511 3339 -412 -180 571 C ATOM 367 CZ PHE A 44 -23.736 -20.263 26.068 1.00 29.30 C ANISOU 367 CZ PHE A 44 4210 3634 3287 -442 -148 609 C ATOM 368 N VAL A 45 -25.139 -19.003 18.992 1.00 20.44 N ANISOU 368 N VAL A 45 2947 2556 2263 -398 -96 219 N ATOM 369 CA VAL A 45 -25.269 -18.504 17.624 1.00 20.95 C ANISOU 369 CA VAL A 45 2998 2647 2315 -378 -91 148 C ATOM 370 C VAL A 45 -26.607 -17.797 17.435 1.00 21.70 C ANISOU 370 C VAL A 45 3022 2836 2387 -452 -92 150 C ATOM 371 O VAL A 45 -26.682 -16.736 16.801 1.00 19.75 O ANISOU 371 O VAL A 45 2725 2661 2118 -420 -79 118 O ATOM 372 CB VAL A 45 -25.093 -19.661 16.618 1.00 24.09 C ANISOU 372 CB VAL A 45 3492 2930 2731 -381 -120 97 C ATOM 373 CG1 VAL A 45 -25.477 -19.220 15.211 1.00 23.87 C ANISOU 373 CG1 VAL A 45 3464 2932 2672 -386 -123 28 C ATOM 374 CG2 VAL A 45 -23.658 -20.171 16.638 1.00 19.93 C ANISOU 374 CG2 VAL A 45 3017 2320 2234 -281 -110 78 C ATOM 375 N VAL A 46 -27.685 -18.376 17.974 1.00 22.30 N ANISOU 375 N VAL A 46 3091 2910 2472 -551 -109 192 N ATOM 376 CA VAL A 46 -29.000 -17.751 17.861 1.00 23.87 C ANISOU 376 CA VAL A 46 3205 3202 2664 -619 -110 196 C ATOM 377 C VAL A 46 -29.051 -16.460 18.667 1.00 24.68 C ANISOU 377 C VAL A 46 3215 3416 2746 -581 -65 219 C ATOM 378 O VAL A 46 -29.601 -15.449 18.209 1.00 22.43 O ANISOU 378 O VAL A 46 2857 3211 2453 -570 -62 194 O ATOM 379 CB VAL A 46 -30.100 -18.734 18.301 1.00 28.16 C ANISOU 379 CB VAL A 46 3753 3718 3230 -743 -130 237 C ATOM 380 CG1 VAL A 46 -31.443 -18.013 18.441 1.00 27.32 C ANISOU 380 CG1 VAL A 46 3528 3724 3126 -807 -120 249 C ATOM 381 CG2 VAL A 46 -30.208 -19.870 17.306 1.00 27.95 C ANISOU 381 CG2 VAL A 46 3815 3580 3222 -787 -186 199 C ATOM 382 N SER A 47 -28.486 -16.470 19.877 1.00 20.18 N ANISOU 382 N SER A 47 2653 2848 2167 -560 -36 266 N ATOM 383 CA SER A 47 -28.419 -15.244 20.667 1.00 20.57 C ANISOU 383 CA SER A 47 2631 2993 2191 -518 5 279 C ATOM 384 C SER A 47 -27.669 -14.155 19.910 1.00 20.49 C ANISOU 384 C SER A 47 2599 3010 2174 -426 8 229 C ATOM 385 O SER A 47 -28.080 -12.988 19.903 1.00 19.21 O ANISOU 385 O SER A 47 2367 2931 2002 -405 25 216 O ATOM 386 CB SER A 47 -27.753 -15.523 22.016 1.00 22.27 C ANISOU 386 CB SER A 47 2882 3191 2387 -505 22 333 C ATOM 387 OG SER A 47 -27.705 -14.347 22.811 1.00 22.35 O ANISOU 387 OG SER A 47 2834 3293 2367 -468 59 339 O ATOM 388 N LEU A 48 -26.570 -14.526 19.253 1.00 20.06 N ANISOU 388 N LEU A 48 2606 2886 2130 -370 -6 202 N ATOM 389 CA LEU A 48 -25.839 -13.578 18.422 1.00 19.23 C ANISOU 389 CA LEU A 48 2487 2803 2018 -296 4 158 C ATOM 390 C LEU A 48 -26.689 -13.110 17.244 1.00 21.26 C ANISOU 390 C LEU A 48 2721 3093 2264 -319 -13 120 C ATOM 391 O LEU A 48 -26.670 -11.926 16.891 1.00 23.12 O ANISOU 391 O LEU A 48 2914 3387 2485 -281 -4 104 O ATOM 392 CB LEU A 48 -24.540 -14.225 17.945 1.00 17.58 C ANISOU 392 CB LEU A 48 2342 2511 1825 -238 2 134 C ATOM 393 CG LEU A 48 -23.549 -13.453 17.084 1.00 23.03 C ANISOU 393 CG LEU A 48 3026 3212 2510 -164 25 91 C ATOM 394 CD1 LEU A 48 -23.082 -12.197 17.801 1.00 19.69 C ANISOU 394 CD1 LEU A 48 2540 2858 2082 -124 46 109 C ATOM 395 CD2 LEU A 48 -22.358 -14.350 16.757 1.00 22.09 C ANISOU 395 CD2 LEU A 48 2964 3010 2420 -111 31 68 C ATOM 396 N ALA A 49 -27.451 -14.023 16.627 1.00 20.41 N ANISOU 396 N ALA A 49 2647 2946 2163 -382 -47 108 N ATOM 397 CA ALA A 49 -28.305 -13.631 15.507 1.00 19.40 C ANISOU 397 CA ALA A 49 2501 2849 2021 -409 -81 75 C ATOM 398 C ALA A 49 -29.445 -12.726 15.960 1.00 19.71 C ANISOU 398 C ALA A 49 2439 2983 2068 -436 -82 96 C ATOM 399 O ALA A 49 -29.859 -11.831 15.215 1.00 19.96 O ANISOU 399 O ALA A 49 2436 3061 2088 -417 -103 74 O ATOM 400 CB ALA A 49 -28.857 -14.871 14.807 1.00 20.03 C ANISOU 400 CB ALA A 49 2643 2860 2109 -478 -127 54 C ATOM 401 N ALA A 50 -29.965 -12.949 17.167 1.00 18.28 N ANISOU 401 N ALA A 50 2212 2829 1904 -478 -59 138 N ATOM 402 CA ALA A 50 -31.007 -12.083 17.708 1.00 20.69 C ANISOU 402 CA ALA A 50 2413 3230 2220 -494 -44 152 C ATOM 403 C ALA A 50 -30.488 -10.669 17.925 1.00 20.39 C ANISOU 403 C ALA A 50 2339 3243 2164 -408 -17 142 C ATOM 404 O ALA A 50 -31.202 -9.693 17.668 1.00 20.42 O ANISOU 404 O ALA A 50 2273 3308 2176 -390 -26 128 O ATOM 405 CB ALA A 50 -31.542 -12.657 19.021 1.00 20.45 C ANISOU 405 CB ALA A 50 2352 3219 2199 -556 -7 200 C ATOM 406 N ALA A 51 -29.254 -10.538 18.420 1.00 19.37 N ANISOU 406 N ALA A 51 2256 3085 2018 -354 12 148 N ATOM 407 CA ALA A 51 -28.651 -9.218 18.553 1.00 20.61 C ANISOU 407 CA ALA A 51 2389 3278 2162 -280 31 136 C ATOM 408 C ALA A 51 -28.528 -8.539 17.198 1.00 19.53 C ANISOU 408 C ALA A 51 2264 3138 2020 -246 1 103 C ATOM 409 O ALA A 51 -28.733 -7.326 17.079 1.00 21.74 O ANISOU 409 O ALA A 51 2501 3460 2297 -208 0 94 O ATOM 410 CB ALA A 51 -27.282 -9.331 19.223 1.00 19.84 C ANISOU 410 CB ALA A 51 2339 3145 2056 -238 54 148 C ATOM 411 N ASP A 52 -28.192 -9.308 16.160 1.00 17.51 N ANISOU 411 N ASP A 52 2072 2825 1755 -259 -22 84 N ATOM 412 CA ASP A 52 -28.041 -8.721 14.835 1.00 15.84 C ANISOU 412 CA ASP A 52 1889 2609 1520 -233 -47 55 C ATOM 413 C ASP A 52 -29.392 -8.377 14.215 1.00 15.50 C ANISOU 413 C ASP A 52 1803 2607 1481 -266 -99 49 C ATOM 414 O ASP A 52 -29.497 -7.393 13.475 1.00 18.69 O ANISOU 414 O ASP A 52 2202 3032 1866 -233 -123 40 O ATOM 415 CB ASP A 52 -27.236 -9.668 13.944 1.00 17.77 C ANISOU 415 CB ASP A 52 2223 2783 1745 -233 -48 29 C ATOM 416 CG ASP A 52 -25.757 -9.694 14.315 1.00 24.49 C ANISOU 416 CG ASP A 52 3102 3603 2601 -179 1 29 C ATOM 417 OD1 ASP A 52 -25.240 -8.646 14.775 1.00 24.29 O ANISOU 417 OD1 ASP A 52 3040 3613 2578 -138 26 42 O ATOM 418 OD2 ASP A 52 -25.111 -10.757 14.156 1.00 27.20 O ANISOU 418 OD2 ASP A 52 3502 3884 2950 -177 11 16 O ATOM 419 N ILE A 53 -30.433 -9.160 14.513 1.00 19.86 N ANISOU 419 N ILE A 53 2319 3169 2059 -331 -122 58 N ATOM 420 CA ILE A 53 -31.784 -8.789 14.099 1.00 22.70 C ANISOU 420 CA ILE A 53 2609 3579 2438 -361 -175 55 C ATOM 421 C ILE A 53 -32.184 -7.461 14.730 1.00 21.18 C ANISOU 421 C ILE A 53 2327 3454 2265 -311 -156 65 C ATOM 422 O ILE A 53 -32.728 -6.577 14.059 1.00 21.17 O ANISOU 422 O ILE A 53 2295 3482 2268 -283 -202 56 O ATOM 423 CB ILE A 53 -32.782 -9.910 14.454 1.00 21.96 C ANISOU 423 CB ILE A 53 2479 3486 2378 -451 -193 66 C ATOM 424 CG1 ILE A 53 -32.558 -11.133 13.566 1.00 22.53 C ANISOU 424 CG1 ILE A 53 2647 3480 2432 -501 -233 46 C ATOM 425 CG2 ILE A 53 -34.219 -9.424 14.309 1.00 24.92 C ANISOU 425 CG2 ILE A 53 2745 3931 2794 -478 -238 67 C ATOM 426 CD1 ILE A 53 -33.324 -12.367 14.027 1.00 25.39 C ANISOU 426 CD1 ILE A 53 2995 3821 2831 -599 -246 62 C ATOM 427 N LEU A 54 -31.911 -7.294 16.028 1.00 18.02 N ANISOU 427 N LEU A 54 1895 3076 1875 -295 -93 82 N ATOM 428 CA LEU A 54 -32.224 -6.039 16.705 1.00 20.80 C ANISOU 428 CA LEU A 54 2175 3487 2243 -242 -69 82 C ATOM 429 C LEU A 54 -31.362 -4.877 16.217 1.00 20.96 C ANISOU 429 C LEU A 54 2235 3488 2240 -168 -75 70 C ATOM 430 O LEU A 54 -31.751 -3.719 16.396 1.00 19.29 O ANISOU 430 O LEU A 54 1974 3311 2044 -119 -79 63 O ATOM 431 CB LEU A 54 -32.067 -6.201 18.218 1.00 21.47 C ANISOU 431 CB LEU A 54 2236 3596 2327 -248 0 99 C ATOM 432 CG LEU A 54 -33.046 -7.177 18.882 1.00 26.31 C ANISOU 432 CG LEU A 54 2797 4240 2961 -327 20 119 C ATOM 433 CD1 LEU A 54 -32.731 -7.353 20.370 1.00 25.77 C ANISOU 433 CD1 LEU A 54 2732 4190 2870 -335 91 142 C ATOM 434 CD2 LEU A 54 -34.481 -6.706 18.688 1.00 25.45 C ANISOU 434 CD2 LEU A 54 2574 4199 2897 -338 1 108 C ATOM 435 N VAL A 55 -30.197 -5.145 15.622 1.00 17.54 N ANISOU 435 N VAL A 55 1891 3000 1775 -158 -73 67 N ATOM 436 CA VAL A 55 -29.452 -4.060 14.987 1.00 15.52 C ANISOU 436 CA VAL A 55 1672 2728 1498 -104 -79 61 C ATOM 437 C VAL A 55 -30.263 -3.479 13.837 1.00 16.81 C ANISOU 437 C VAL A 55 1829 2900 1656 -98 -145 56 C ATOM 438 O VAL A 55 -30.354 -2.256 13.675 1.00 20.34 O ANISOU 438 O VAL A 55 2263 3358 2108 -51 -163 58 O ATOM 439 CB VAL A 55 -28.065 -4.543 14.515 1.00 18.86 C ANISOU 439 CB VAL A 55 2179 3097 1890 -100 -54 57 C ATOM 440 CG1 VAL A 55 -27.436 -3.513 13.569 1.00 16.57 C ANISOU 440 CG1 VAL A 55 1931 2792 1572 -63 -62 55 C ATOM 441 CG2 VAL A 55 -27.149 -4.778 15.705 1.00 16.87 C ANISOU 441 CG2 VAL A 55 1924 2836 1649 -87 -2 67 C ATOM 442 N GLY A 56 -30.885 -4.347 13.034 1.00 17.70 N ANISOU 442 N GLY A 56 1958 3006 1761 -147 -192 49 N ATOM 443 CA GLY A 56 -31.680 -3.874 11.916 1.00 18.34 C ANISOU 443 CA GLY A 56 2040 3096 1832 -145 -270 47 C ATOM 444 C GLY A 56 -33.010 -3.278 12.318 1.00 22.68 C ANISOU 444 C GLY A 56 2477 3701 2438 -132 -309 50 C ATOM 445 O GLY A 56 -33.465 -2.310 11.705 1.00 26.35 O ANISOU 445 O GLY A 56 2929 4175 2907 -93 -367 55 O ATOM 446 N VAL A 57 -33.653 -3.841 13.341 1.00 22.14 N ANISOU 446 N VAL A 57 2326 3670 2415 -164 -276 51 N ATOM 447 CA VAL A 57 -34.981 -3.387 13.738 1.00 22.17 C ANISOU 447 CA VAL A 57 2206 3736 2480 -155 -300 49 C ATOM 448 C VAL A 57 -34.906 -2.110 14.575 1.00 21.17 C ANISOU 448 C VAL A 57 2032 3635 2376 -75 -258 45 C ATOM 449 O VAL A 57 -35.752 -1.219 14.439 1.00 21.22 O ANISOU 449 O VAL A 57 1966 3672 2426 -28 -299 38 O ATOM 450 CB VAL A 57 -35.712 -4.520 14.487 1.00 25.80 C ANISOU 450 CB VAL A 57 2597 4231 2976 -231 -271 53 C ATOM 451 CG1 VAL A 57 -37.027 -4.024 15.080 1.00 28.73 C ANISOU 451 CG1 VAL A 57 2820 4678 3417 -218 -270 48 C ATOM 452 CG2 VAL A 57 -35.959 -5.700 13.552 1.00 25.39 C ANISOU 452 CG2 VAL A 57 2591 4146 2912 -311 -332 51 C ATOM 453 N LEU A 58 -33.904 -1.993 15.446 1.00 17.95 N ANISOU 453 N LEU A 58 1666 3211 1944 -57 -183 45 N ATOM 454 CA LEU A 58 -33.837 -0.893 16.403 1.00 21.14 C ANISOU 454 CA LEU A 58 2031 3635 2365 9 -139 34 C ATOM 455 C LEU A 58 -32.579 -0.045 16.273 1.00 18.98 C ANISOU 455 C LEU A 58 1844 3310 2057 56 -129 35 C ATOM 456 O LEU A 58 -32.684 1.182 16.159 1.00 20.19 O ANISOU 456 O LEU A 58 1991 3456 2227 118 -152 27 O ATOM 457 CB LEU A 58 -33.956 -1.436 17.841 1.00 21.74 C ANISOU 457 CB LEU A 58 2063 3753 2446 -18 -57 31 C ATOM 458 CG LEU A 58 -35.289 -2.088 18.236 1.00 26.05 C ANISOU 458 CG LEU A 58 2501 4364 3035 -66 -44 31 C ATOM 459 CD1 LEU A 58 -35.225 -2.671 19.643 1.00 24.13 C ANISOU 459 CD1 LEU A 58 2241 4153 2773 -102 45 39 C ATOM 460 CD2 LEU A 58 -36.452 -1.100 18.122 1.00 26.09 C ANISOU 460 CD2 LEU A 58 2395 4417 3099 -9 -72 9 C ATOM 461 N ALA A 59 -31.385 -0.651 16.294 1.00 17.38 N ANISOU 461 N ALA A 59 1720 3069 1813 28 -98 45 N ATOM 462 CA ALA A 59 -30.164 0.155 16.354 1.00 17.23 C ANISOU 462 CA ALA A 59 1764 3010 1772 65 -79 46 C ATOM 463 C ALA A 59 -29.990 1.020 15.107 1.00 18.65 C ANISOU 463 C ALA A 59 1992 3154 1939 92 -133 55 C ATOM 464 O ALA A 59 -29.512 2.157 15.192 1.00 17.04 O ANISOU 464 O ALA A 59 1810 2925 1738 134 -133 55 O ATOM 465 CB ALA A 59 -28.941 -0.740 16.552 1.00 17.61 C ANISOU 465 CB ALA A 59 1872 3029 1791 32 -40 55 C ATOM 466 N ILE A 60 -30.358 0.505 13.940 1.00 17.60 N ANISOU 466 N ILE A 60 1886 3014 1788 63 -181 63 N ATOM 467 CA ILE A 60 -30.162 1.280 12.715 1.00 18.15 C ANISOU 467 CA ILE A 60 2019 3049 1830 81 -233 78 C ATOM 468 C ILE A 60 -31.202 2.397 12.635 1.00 19.14 C ANISOU 468 C ILE A 60 2093 3186 1994 133 -293 80 C ATOM 469 O ILE A 60 -30.827 3.545 12.362 1.00 17.08 O ANISOU 469 O ILE A 60 1873 2888 1729 173 -311 93 O ATOM 470 CB ILE A 60 -30.157 0.373 11.473 1.00 20.18 C ANISOU 470 CB ILE A 60 2337 3291 2037 33 -267 83 C ATOM 471 CG1 ILE A 60 -28.810 -0.371 11.413 1.00 19.39 C ANISOU 471 CG1 ILE A 60 2305 3163 1898 5 -201 79 C ATOM 472 CG2 ILE A 60 -30.413 1.196 10.199 1.00 17.93 C ANISOU 472 CG2 ILE A 60 2109 2985 1719 49 -341 103 C ATOM 473 CD1 ILE A 60 -28.676 -1.387 10.292 1.00 18.48 C ANISOU 473 CD1 ILE A 60 2261 3028 1730 -38 -217 70 C ATOM 474 N PRO A 61 -32.495 2.150 12.882 1.00 19.05 N ANISOU 474 N PRO A 61 1990 3220 2029 137 -326 68 N ATOM 475 CA PRO A 61 -33.412 3.293 13.026 1.00 19.99 C ANISOU 475 CA PRO A 61 2044 3350 2201 205 -372 63 C ATOM 476 C PRO A 61 -32.960 4.301 14.075 1.00 21.17 C ANISOU 476 C PRO A 61 2185 3485 2374 262 -319 46 C ATOM 477 O PRO A 61 -33.125 5.508 13.861 1.00 19.70 O ANISOU 477 O PRO A 61 2010 3266 2211 324 -361 49 O ATOM 478 CB PRO A 61 -34.740 2.622 13.402 1.00 21.14 C ANISOU 478 CB PRO A 61 2070 3562 2402 189 -386 46 C ATOM 479 CG PRO A 61 -34.679 1.316 12.679 1.00 22.23 C ANISOU 479 CG PRO A 61 2246 3701 2500 107 -406 57 C ATOM 480 CD PRO A 61 -33.237 0.875 12.862 1.00 20.65 C ANISOU 480 CD PRO A 61 2144 3462 2242 79 -335 61 C ATOM 481 N PHE A 62 -32.367 3.847 15.188 1.00 17.49 N ANISOU 481 N PHE A 62 1711 3036 1899 241 -236 30 N ATOM 482 CA PHE A 62 -31.856 4.778 16.193 1.00 16.21 C ANISOU 482 CA PHE A 62 1555 2856 1747 288 -191 10 C ATOM 483 C PHE A 62 -30.653 5.554 15.668 1.00 21.24 C ANISOU 483 C PHE A 62 2292 3423 2354 294 -203 29 C ATOM 484 O PHE A 62 -30.508 6.749 15.952 1.00 21.68 O ANISOU 484 O PHE A 62 2365 3443 2431 345 -214 19 O ATOM 485 CB PHE A 62 -31.471 4.035 17.477 1.00 16.62 C ANISOU 485 CB PHE A 62 1587 2944 1784 257 -110 -7 C ATOM 486 CG PHE A 62 -32.642 3.479 18.251 1.00 20.83 C ANISOU 486 CG PHE A 62 2020 3549 2347 251 -78 -26 C ATOM 487 CD1 PHE A 62 -33.947 3.737 17.862 1.00 23.79 C ANISOU 487 CD1 PHE A 62 2310 3957 2773 281 -120 -35 C ATOM 488 CD2 PHE A 62 -32.427 2.704 19.387 1.00 17.67 C ANISOU 488 CD2 PHE A 62 1607 3184 1924 214 -7 -32 C ATOM 489 CE1 PHE A 62 -35.017 3.222 18.583 1.00 23.81 C ANISOU 489 CE1 PHE A 62 2206 4033 2809 269 -80 -53 C ATOM 490 CE2 PHE A 62 -33.488 2.186 20.105 1.00 19.74 C ANISOU 490 CE2 PHE A 62 1779 3514 2207 197 33 -45 C ATOM 491 CZ PHE A 62 -34.786 2.448 19.706 1.00 24.59 C ANISOU 491 CZ PHE A 62 2299 4167 2878 223 3 -56 C ATOM 492 N ALA A 63 -29.768 4.883 14.922 1.00 21.22 N ANISOU 492 N ALA A 63 2357 3401 2306 240 -197 55 N ATOM 493 CA ALA A 63 -28.611 5.561 14.346 1.00 15.40 C ANISOU 493 CA ALA A 63 1706 2606 1540 234 -198 78 C ATOM 494 C ALA A 63 -29.038 6.606 13.323 1.00 17.58 C ANISOU 494 C ALA A 63 2022 2841 1818 266 -271 102 C ATOM 495 O ALA A 63 -28.463 7.696 13.263 1.00 19.26 O ANISOU 495 O ALA A 63 2284 2999 2034 286 -279 115 O ATOM 496 CB ALA A 63 -27.668 4.543 13.707 1.00 16.18 C ANISOU 496 CB ALA A 63 1856 2699 1590 175 -167 95 C ATOM 497 N ILE A 64 -30.042 6.286 12.503 1.00 20.11 N ANISOU 497 N ILE A 64 2324 3180 2135 268 -332 112 N ATOM 498 CA ILE A 64 -30.569 7.260 11.550 1.00 19.95 C ANISOU 498 CA ILE A 64 2342 3120 2117 304 -418 140 C ATOM 499 C ILE A 64 -31.147 8.461 12.288 1.00 26.01 C ANISOU 499 C ILE A 64 3064 3867 2953 384 -442 121 C ATOM 500 O ILE A 64 -30.919 9.617 11.906 1.00 24.78 O ANISOU 500 O ILE A 64 2969 3644 2800 417 -483 144 O ATOM 501 CB ILE A 64 -31.619 6.594 10.643 1.00 18.92 C ANISOU 501 CB ILE A 64 2189 3022 1976 291 -492 150 C ATOM 502 CG1 ILE A 64 -30.962 5.568 9.717 1.00 20.49 C ANISOU 502 CG1 ILE A 64 2465 3224 2096 217 -476 166 C ATOM 503 CG2 ILE A 64 -32.395 7.642 9.849 1.00 20.29 C ANISOU 503 CG2 ILE A 64 2382 3161 2167 344 -599 178 C ATOM 504 CD1 ILE A 64 -31.972 4.652 9.036 1.00 18.48 C ANISOU 504 CD1 ILE A 64 2183 3007 1831 189 -541 162 C ATOM 505 N THR A 65 -31.894 8.202 13.366 1.00 22.34 N ANISOU 505 N THR A 65 2495 3454 2539 414 -411 78 N ATOM 506 CA THR A 65 -32.505 9.277 14.142 1.00 22.21 C ANISOU 506 CA THR A 65 2429 3424 2587 498 -421 45 C ATOM 507 C THR A 65 -31.450 10.196 14.751 1.00 19.31 C ANISOU 507 C THR A 65 2129 2993 2213 511 -384 36 C ATOM 508 O THR A 65 -31.565 11.425 14.674 1.00 23.45 O ANISOU 508 O THR A 65 2686 3453 2770 571 -429 35 O ATOM 509 CB THR A 65 -33.394 8.683 15.236 1.00 24.27 C ANISOU 509 CB THR A 65 2568 3765 2890 515 -370 -2 C ATOM 510 OG1 THR A 65 -34.309 7.743 14.658 1.00 26.23 O ANISOU 510 OG1 THR A 65 2749 4070 3147 485 -405 9 O ATOM 511 CG2 THR A 65 -34.188 9.769 15.929 1.00 24.34 C ANISOU 511 CG2 THR A 65 2515 3766 2968 613 -378 -45 C ATOM 512 N ILE A 66 -30.413 9.625 15.368 1.00 19.95 N ANISOU 512 N ILE A 66 2233 3088 2258 456 -310 28 N ATOM 513 CA ILE A 66 -29.412 10.449 16.039 1.00 26.19 C ANISOU 513 CA ILE A 66 3079 3826 3048 461 -281 15 C ATOM 514 C ILE A 66 -28.490 11.162 15.066 1.00 29.90 C ANISOU 514 C ILE A 66 3650 4217 3494 432 -315 63 C ATOM 515 O ILE A 66 -27.776 12.086 15.472 1.00 36.90 O ANISOU 515 O ILE A 66 4584 5043 4392 438 -311 57 O ATOM 516 CB ILE A 66 -28.555 9.629 17.027 1.00 28.91 C ANISOU 516 CB ILE A 66 3412 4209 3364 411 -203 -5 C ATOM 517 CG1 ILE A 66 -27.741 8.566 16.290 1.00 34.51 C ANISOU 517 CG1 ILE A 66 4153 4932 4027 336 -183 34 C ATOM 518 CG2 ILE A 66 -29.431 9.010 18.109 1.00 30.07 C ANISOU 518 CG2 ILE A 66 3471 4430 3523 432 -161 -48 C ATOM 519 CD1 ILE A 66 -26.977 7.632 17.220 1.00 37.61 C ANISOU 519 CD1 ILE A 66 4529 5362 4400 295 -120 19 C ATOM 520 N SER A 67 -28.479 10.759 13.792 1.00 26.04 N ANISOU 520 N SER A 67 3200 3727 2969 396 -347 111 N ATOM 521 CA SER A 67 -27.711 11.499 12.796 1.00 25.72 C ANISOU 521 CA SER A 67 3260 3614 2897 367 -376 163 C ATOM 522 C SER A 67 -28.356 12.837 12.459 1.00 26.94 C ANISOU 522 C SER A 67 3452 3696 3089 431 -458 179 C ATOM 523 O SER A 67 -27.685 13.712 11.901 1.00 28.59 O ANISOU 523 O SER A 67 3752 3828 3284 410 -480 221 O ATOM 524 CB SER A 67 -27.544 10.664 11.521 1.00 21.43 C ANISOU 524 CB SER A 67 2760 3094 2289 311 -382 206 C ATOM 525 OG SER A 67 -28.759 10.602 10.789 1.00 22.47 O ANISOU 525 OG SER A 67 2878 3238 2421 344 -462 219 O ATOM 526 N THR A 68 -29.641 13.014 12.777 1.00 27.57 N ANISOU 526 N THR A 68 3460 3795 3220 509 -503 148 N ATOM 527 CA THR A 68 -30.329 14.259 12.460 1.00 27.88 C ANISOU 527 CA THR A 68 3526 3759 3306 586 -590 160 C ATOM 528 C THR A 68 -30.081 15.355 13.489 1.00 27.21 C ANISOU 528 C THR A 68 3454 3611 3274 637 -575 118 C ATOM 529 O THR A 68 -30.320 16.529 13.188 1.00 25.72 O ANISOU 529 O THR A 68 3321 3331 3121 691 -645 134 O ATOM 530 CB THR A 68 -31.839 14.028 12.350 1.00 30.85 C ANISOU 530 CB THR A 68 3807 4184 3730 657 -649 141 C ATOM 531 OG1 THR A 68 -32.374 13.714 13.644 1.00 29.18 O ANISOU 531 OG1 THR A 68 3484 4036 3567 698 -587 68 O ATOM 532 CG2 THR A 68 -32.135 12.882 11.394 1.00 29.94 C ANISOU 532 CG2 THR A 68 3679 4132 3563 600 -671 174 C ATOM 533 N GLY A 69 -29.623 15.007 14.689 1.00 23.41 N ANISOU 533 N GLY A 69 2930 3168 2795 622 -494 63 N ATOM 534 CA GLY A 69 -29.485 16.004 15.733 1.00 26.47 C ANISOU 534 CA GLY A 69 3331 3499 3226 674 -484 10 C ATOM 535 C GLY A 69 -30.800 16.591 16.195 1.00 26.33 C ANISOU 535 C GLY A 69 3249 3478 3277 790 -517 -42 C ATOM 536 O GLY A 69 -30.826 17.721 16.689 1.00 27.81 O ANISOU 536 O GLY A 69 3475 3584 3508 852 -539 -78 O ATOM 537 N PHE A 70 -31.898 15.849 16.045 1.00 25.21 N ANISOU 537 N PHE A 70 3006 3420 3152 822 -522 -51 N ATOM 538 CA PHE A 70 -33.219 16.362 16.385 1.00 26.00 C ANISOU 538 CA PHE A 70 3021 3527 3329 936 -553 -100 C ATOM 539 C PHE A 70 -33.309 16.696 17.872 1.00 25.96 C ANISOU 539 C PHE A 70 2979 3538 3349 988 -477 -190 C ATOM 540 O PHE A 70 -32.592 16.133 18.704 1.00 26.48 O ANISOU 540 O PHE A 70 3050 3646 3363 927 -396 -214 O ATOM 541 CB PHE A 70 -34.290 15.334 16.013 1.00 26.84 C ANISOU 541 CB PHE A 70 3010 3738 3448 938 -561 -92 C ATOM 542 CG PHE A 70 -34.423 14.213 17.005 1.00 27.00 C ANISOU 542 CG PHE A 70 2940 3872 3449 898 -457 -137 C ATOM 543 CD1 PHE A 70 -33.406 13.290 17.171 1.00 30.22 C ANISOU 543 CD1 PHE A 70 3388 4311 3782 794 -396 -116 C ATOM 544 CD2 PHE A 70 -35.571 14.080 17.768 1.00 31.67 C ANISOU 544 CD2 PHE A 70 3403 4535 4096 965 -420 -196 C ATOM 545 CE1 PHE A 70 -33.523 12.266 18.091 1.00 31.82 C ANISOU 545 CE1 PHE A 70 3520 4608 3963 757 -309 -148 C ATOM 546 CE2 PHE A 70 -35.697 13.056 18.683 1.00 31.03 C ANISOU 546 CE2 PHE A 70 3247 4555 3987 919 -322 -228 C ATOM 547 CZ PHE A 70 -34.674 12.146 18.843 1.00 31.31 C ANISOU 547 CZ PHE A 70 3338 4613 3945 814 -271 -201 C ATOM 548 N CYS A 71 -34.207 17.624 18.202 1.00 26.77 N ANISOU 548 N CYS A 71 3044 3602 3525 1107 -506 -241 N ATOM 549 CA CYS A 71 -34.391 18.035 19.589 1.00 29.85 C ANISOU 549 CA CYS A 71 3405 4002 3934 1169 -432 -337 C ATOM 550 C CYS A 71 -35.034 16.911 20.388 1.00 30.28 C ANISOU 550 C CYS A 71 3332 4200 3972 1155 -336 -378 C ATOM 551 O CYS A 71 -36.039 16.332 19.965 1.00 29.61 O ANISOU 551 O CYS A 71 3137 4190 3924 1174 -348 -365 O ATOM 552 CB CYS A 71 -35.263 19.288 19.663 1.00 34.92 C ANISOU 552 CB CYS A 71 4034 4565 4667 1311 -486 -387 C ATOM 553 SG CYS A 71 -34.529 20.781 18.946 1.00 39.95 S ANISOU 553 SG CYS A 71 4839 5011 5329 1335 -598 -346 S ATOM 554 N ALA A 72 -34.468 16.611 21.556 1.00 25.23 N ANISOU 554 N ALA A 72 2711 3600 3277 1117 -244 -426 N ATOM 555 CA ALA A 72 -34.996 15.524 22.365 1.00 26.62 C ANISOU 555 CA ALA A 72 2783 3906 3424 1090 -147 -456 C ATOM 556 C ALA A 72 -34.644 15.757 23.824 1.00 28.66 C ANISOU 556 C ALA A 72 3075 4180 3637 1102 -59 -535 C ATOM 557 O ALA A 72 -33.625 16.378 24.138 1.00 29.44 O ANISOU 557 O ALA A 72 3288 4197 3701 1083 -75 -547 O ATOM 558 CB ALA A 72 -34.447 14.169 21.900 1.00 27.33 C ANISOU 558 CB ALA A 72 2871 4058 3454 966 -135 -384 C ATOM 559 N ALA A 73 -35.495 15.242 24.711 1.00 26.42 N ANISOU 559 N ALA A 73 2690 4001 3346 1126 34 -587 N ATOM 560 CA ALA A 73 -35.124 15.147 26.116 1.00 27.09 C ANISOU 560 CA ALA A 73 2812 4124 3356 1111 128 -651 C ATOM 561 C ALA A 73 -33.817 14.377 26.228 1.00 24.85 C ANISOU 561 C ALA A 73 2615 3840 2986 987 127 -596 C ATOM 562 O ALA A 73 -33.651 13.327 25.599 1.00 22.87 O ANISOU 562 O ALA A 73 2336 3633 2722 907 116 -523 O ATOM 563 CB ALA A 73 -36.228 14.458 26.914 1.00 28.56 C ANISOU 563 CB ALA A 73 2873 4441 3537 1128 237 -693 C ATOM 564 N CYS A 74 -32.877 14.913 27.013 1.00 24.99 N ANISOU 564 N CYS A 74 2740 3804 2950 975 132 -634 N ATOM 565 CA CYS A 74 -31.502 14.424 26.960 1.00 28.76 C ANISOU 565 CA CYS A 74 3303 4258 3368 870 105 -580 C ATOM 566 C CYS A 74 -31.411 12.945 27.307 1.00 25.78 C ANISOU 566 C CYS A 74 2882 3984 2928 785 163 -538 C ATOM 567 O CYS A 74 -30.644 12.202 26.683 1.00 24.99 O ANISOU 567 O CYS A 74 2801 3880 2814 705 131 -466 O ATOM 568 CB CYS A 74 -30.606 15.240 27.891 1.00 33.05 C ANISOU 568 CB CYS A 74 3956 4736 3867 872 98 -637 C ATOM 569 SG CYS A 74 -28.840 14.889 27.667 1.00 37.30 S ANISOU 569 SG CYS A 74 4586 5226 4362 753 41 -570 S ATOM 570 N HIS A 75 -32.177 12.496 28.306 1.00 21.43 N ANISOU 570 N HIS A 75 2278 3526 2340 800 253 -582 N ATOM 571 CA HIS A 75 -32.092 11.092 28.693 1.00 25.08 C ANISOU 571 CA HIS A 75 2712 4077 2740 713 306 -537 C ATOM 572 C HIS A 75 -32.774 10.185 27.673 1.00 28.54 C ANISOU 572 C HIS A 75 3055 4561 3229 682 296 -473 C ATOM 573 O HIS A 75 -32.389 9.019 27.527 1.00 26.37 O ANISOU 573 O HIS A 75 2780 4319 2920 597 301 -413 O ATOM 574 CB HIS A 75 -32.676 10.902 30.089 1.00 29.93 C ANISOU 574 CB HIS A 75 3310 4774 3286 727 410 -597 C ATOM 575 CG HIS A 75 -31.863 11.552 31.165 1.00 35.16 C ANISOU 575 CG HIS A 75 4086 5399 3873 735 415 -654 C ATOM 576 ND1 HIS A 75 -32.053 12.861 31.554 1.00 39.22 N ANISOU 576 ND1 HIS A 75 4639 5858 4403 824 412 -742 N ATOM 577 CD2 HIS A 75 -30.834 11.085 31.912 1.00 35.00 C ANISOU 577 CD2 HIS A 75 4153 5382 3763 664 409 -637 C ATOM 578 CE1 HIS A 75 -31.190 13.166 32.507 1.00 37.74 C ANISOU 578 CE1 HIS A 75 4561 5644 4133 803 407 -780 C ATOM 579 NE2 HIS A 75 -30.436 12.107 32.740 1.00 35.90 N ANISOU 579 NE2 HIS A 75 4356 5448 3835 706 402 -715 N ATOM 580 N GLY A 76 -33.771 10.700 26.952 1.00 29.99 N ANISOU 580 N GLY A 76 3160 4740 3496 751 273 -486 N ATOM 581 CA GLY A 76 -34.313 9.953 25.830 1.00 26.12 C ANISOU 581 CA GLY A 76 2594 4276 3055 718 237 -425 C ATOM 582 C GLY A 76 -33.309 9.820 24.703 1.00 24.29 C ANISOU 582 C GLY A 76 2436 3970 2824 668 150 -359 C ATOM 583 O GLY A 76 -33.140 8.740 24.135 1.00 21.86 O ANISOU 583 O GLY A 76 2116 3689 2502 594 140 -301 O ATOM 584 N CYS A 77 -32.635 10.919 24.361 1.00 23.71 N ANISOU 584 N CYS A 77 2442 3801 2766 705 91 -367 N ATOM 585 CA CYS A 77 -31.527 10.854 23.415 1.00 25.61 C ANISOU 585 CA CYS A 77 2760 3974 2995 650 27 -307 C ATOM 586 C CYS A 77 -30.473 9.858 23.878 1.00 24.05 C ANISOU 586 C CYS A 77 2605 3801 2731 561 59 -278 C ATOM 587 O CYS A 77 -29.951 9.073 23.078 1.00 18.59 O ANISOU 587 O CYS A 77 1927 3106 2030 499 37 -221 O ATOM 588 CB CYS A 77 -30.907 12.243 23.248 1.00 27.13 C ANISOU 588 CB CYS A 77 3038 4062 3210 694 -27 -325 C ATOM 589 SG CYS A 77 -29.511 12.286 22.105 1.00 28.72 S ANISOU 589 SG CYS A 77 3331 4183 3399 620 -91 -251 S ATOM 590 N LEU A 78 -30.163 9.869 25.174 1.00 23.59 N ANISOU 590 N LEU A 78 2573 3767 2625 558 110 -319 N ATOM 591 CA LEU A 78 -29.169 8.951 25.716 1.00 21.36 C ANISOU 591 CA LEU A 78 2332 3504 2281 481 130 -291 C ATOM 592 C LEU A 78 -29.574 7.499 25.497 1.00 21.68 C ANISOU 592 C LEU A 78 2317 3612 2307 425 161 -245 C ATOM 593 O LEU A 78 -28.730 6.659 25.159 1.00 22.28 O ANISOU 593 O LEU A 78 2423 3678 2365 364 145 -197 O ATOM 594 CB LEU A 78 -28.970 9.244 27.202 1.00 23.34 C ANISOU 594 CB LEU A 78 2620 3775 2474 493 174 -346 C ATOM 595 CG LEU A 78 -27.776 8.625 27.920 1.00 24.53 C ANISOU 595 CG LEU A 78 2834 3927 2560 428 172 -325 C ATOM 596 CD1 LEU A 78 -26.463 8.995 27.231 1.00 22.21 C ANISOU 596 CD1 LEU A 78 2593 3554 2291 399 102 -294 C ATOM 597 CD2 LEU A 78 -27.796 9.106 29.357 1.00 26.54 C ANISOU 597 CD2 LEU A 78 3133 4201 2751 451 207 -390 C ATOM 598 N PHE A 79 -30.863 7.180 25.666 1.00 20.44 N ANISOU 598 N PHE A 79 2078 3522 2167 444 204 -260 N ATOM 599 CA PHE A 79 -31.289 5.793 25.500 1.00 16.90 C ANISOU 599 CA PHE A 79 1580 3133 1709 380 230 -217 C ATOM 600 C PHE A 79 -31.092 5.319 24.066 1.00 17.14 C ANISOU 600 C PHE A 79 1609 3128 1773 348 169 -166 C ATOM 601 O PHE A 79 -30.515 4.253 23.834 1.00 17.74 O ANISOU 601 O PHE A 79 1712 3203 1825 283 166 -123 O ATOM 602 CB PHE A 79 -32.745 5.607 25.914 1.00 19.29 C ANISOU 602 CB PHE A 79 1781 3515 2033 399 289 -243 C ATOM 603 CG PHE A 79 -33.242 4.200 25.708 1.00 25.65 C ANISOU 603 CG PHE A 79 2535 4375 2837 322 311 -196 C ATOM 604 CD1 PHE A 79 -32.921 3.198 26.614 1.00 27.37 C ANISOU 604 CD1 PHE A 79 2783 4627 2989 255 364 -172 C ATOM 605 CD2 PHE A 79 -33.998 3.870 24.593 1.00 25.64 C ANISOU 605 CD2 PHE A 79 2465 4382 2896 313 269 -173 C ATOM 606 CE1 PHE A 79 -33.361 1.902 26.424 1.00 28.62 C ANISOU 606 CE1 PHE A 79 2904 4821 3148 179 380 -126 C ATOM 607 CE2 PHE A 79 -34.436 2.571 24.393 1.00 27.57 C ANISOU 607 CE2 PHE A 79 2668 4666 3141 234 282 -132 C ATOM 608 CZ PHE A 79 -34.121 1.587 25.311 1.00 30.85 C ANISOU 608 CZ PHE A 79 3116 5110 3497 166 340 -109 C ATOM 609 N ILE A 80 -31.562 6.094 23.086 1.00 18.37 N ANISOU 609 N ILE A 80 1744 3253 1984 396 117 -170 N ATOM 610 CA ILE A 80 -31.437 5.632 21.708 1.00 19.38 C ANISOU 610 CA ILE A 80 1881 3354 2130 363 59 -123 C ATOM 611 C ILE A 80 -29.990 5.657 21.238 1.00 18.79 C ANISOU 611 C ILE A 80 1899 3214 2025 331 32 -94 C ATOM 612 O ILE A 80 -29.636 4.936 20.297 1.00 21.39 O ANISOU 612 O ILE A 80 2250 3530 2347 287 8 -56 O ATOM 613 CB ILE A 80 -32.317 6.456 20.754 1.00 19.63 C ANISOU 613 CB ILE A 80 1874 3367 2218 421 -1 -128 C ATOM 614 CG1 ILE A 80 -31.855 7.905 20.708 1.00 20.57 C ANISOU 614 CG1 ILE A 80 2050 3414 2352 485 -35 -149 C ATOM 615 CG2 ILE A 80 -33.762 6.395 21.184 1.00 22.83 C ANISOU 615 CG2 ILE A 80 2165 3843 2667 455 25 -158 C ATOM 616 CD1 ILE A 80 -32.653 8.739 19.752 1.00 27.56 C ANISOU 616 CD1 ILE A 80 2911 4267 3293 546 -106 -145 C ATOM 617 N ALA A 81 -29.141 6.469 21.866 1.00 16.52 N ANISOU 617 N ALA A 81 1665 2889 1724 351 38 -115 N ATOM 618 CA ALA A 81 -27.725 6.452 21.527 1.00 18.12 C ANISOU 618 CA ALA A 81 1937 3039 1907 314 20 -88 C ATOM 619 C ALA A 81 -27.015 5.250 22.133 1.00 19.73 C ANISOU 619 C ALA A 81 2152 3272 2074 259 54 -70 C ATOM 620 O ALA A 81 -26.121 4.679 21.500 1.00 20.97 O ANISOU 620 O ALA A 81 2338 3405 2226 221 44 -38 O ATOM 621 CB ALA A 81 -27.054 7.747 21.987 1.00 22.84 C ANISOU 621 CB ALA A 81 2585 3583 2511 346 4 -115 C ATOM 622 N CYS A 82 -27.404 4.843 23.342 1.00 20.06 N ANISOU 622 N CYS A 82 2171 3362 2089 257 96 -90 N ATOM 623 CA CYS A 82 -26.725 3.767 24.047 1.00 19.35 C ANISOU 623 CA CYS A 82 2102 3289 1960 209 119 -69 C ATOM 624 C CYS A 82 -27.225 2.382 23.672 1.00 20.51 C ANISOU 624 C CYS A 82 2221 3467 2105 164 134 -35 C ATOM 625 O CYS A 82 -26.548 1.398 23.979 1.00 19.10 O ANISOU 625 O CYS A 82 2069 3285 1904 125 140 -8 O ATOM 626 CB CYS A 82 -26.870 3.946 25.561 1.00 20.11 C ANISOU 626 CB CYS A 82 2208 3422 2012 219 155 -100 C ATOM 627 SG CYS A 82 -25.916 5.303 26.227 1.00 24.67 S ANISOU 627 SG CYS A 82 2844 3952 2579 252 128 -141 S ATOM 628 N PHE A 83 -28.389 2.268 23.034 1.00 19.16 N ANISOU 628 N PHE A 83 1997 3323 1962 168 133 -36 N ATOM 629 CA PHE A 83 -28.935 0.935 22.820 1.00 18.66 C ANISOU 629 CA PHE A 83 1907 3288 1897 115 146 -8 C ATOM 630 C PHE A 83 -28.012 0.076 21.957 1.00 20.89 C ANISOU 630 C PHE A 83 2237 3523 2176 79 118 24 C ATOM 631 O PHE A 83 -27.930 -1.140 22.165 1.00 22.49 O ANISOU 631 O PHE A 83 2451 3729 2366 33 131 48 O ATOM 632 CB PHE A 83 -30.330 1.016 22.206 1.00 20.49 C ANISOU 632 CB PHE A 83 2065 3554 2167 122 136 -16 C ATOM 633 CG PHE A 83 -31.011 -0.314 22.122 1.00 22.93 C ANISOU 633 CG PHE A 83 2340 3894 2478 58 149 9 C ATOM 634 CD1 PHE A 83 -31.517 -0.922 23.264 1.00 25.43 C ANISOU 634 CD1 PHE A 83 2626 4261 2773 23 208 13 C ATOM 635 CD2 PHE A 83 -31.119 -0.975 20.910 1.00 20.04 C ANISOU 635 CD2 PHE A 83 1981 3503 2129 25 104 28 C ATOM 636 CE1 PHE A 83 -32.134 -2.158 23.191 1.00 26.93 C ANISOU 636 CE1 PHE A 83 2790 4473 2969 -48 218 42 C ATOM 637 CE2 PHE A 83 -31.730 -2.207 20.832 1.00 19.82 C ANISOU 637 CE2 PHE A 83 1929 3493 2107 -42 109 49 C ATOM 638 CZ PHE A 83 -32.236 -2.803 21.970 1.00 22.02 C ANISOU 638 CZ PHE A 83 2174 3818 2374 -81 165 58 C ATOM 639 N VAL A 84 -27.288 0.682 21.010 1.00 18.72 N ANISOU 639 N VAL A 84 1996 3202 1913 100 86 25 N ATOM 640 CA VAL A 84 -26.371 -0.109 20.194 1.00 16.11 C ANISOU 640 CA VAL A 84 1709 2833 1578 72 74 47 C ATOM 641 C VAL A 84 -25.276 -0.726 21.059 1.00 16.50 C ANISOU 641 C VAL A 84 1788 2869 1613 58 92 59 C ATOM 642 O VAL A 84 -24.767 -1.809 20.749 1.00 16.49 O ANISOU 642 O VAL A 84 1810 2846 1611 32 93 76 O ATOM 643 CB VAL A 84 -25.776 0.740 19.054 1.00 16.47 C ANISOU 643 CB VAL A 84 1787 2840 1633 92 48 47 C ATOM 644 CG1 VAL A 84 -24.803 1.790 19.597 1.00 15.51 C ANISOU 644 CG1 VAL A 84 1684 2695 1514 117 51 39 C ATOM 645 CG2 VAL A 84 -25.080 -0.158 18.028 1.00 14.81 C ANISOU 645 CG2 VAL A 84 1615 2600 1413 64 48 62 C ATOM 646 N LEU A 85 -24.910 -0.060 22.160 1.00 13.10 N ANISOU 646 N LEU A 85 1360 2448 1170 77 100 47 N ATOM 647 CA LEU A 85 -23.903 -0.590 23.075 1.00 17.95 C ANISOU 647 CA LEU A 85 2001 3051 1767 66 102 60 C ATOM 648 C LEU A 85 -24.375 -1.874 23.746 1.00 16.29 C ANISOU 648 C LEU A 85 1794 2862 1534 30 119 84 C ATOM 649 O LEU A 85 -23.565 -2.769 24.013 1.00 17.64 O ANISOU 649 O LEU A 85 1994 3007 1702 16 109 109 O ATOM 650 CB LEU A 85 -23.567 0.458 24.137 1.00 18.19 C ANISOU 650 CB LEU A 85 2040 3090 1780 90 98 37 C ATOM 651 CG LEU A 85 -23.022 1.805 23.652 1.00 19.38 C ANISOU 651 CG LEU A 85 2197 3210 1956 118 76 16 C ATOM 652 CD1 LEU A 85 -22.886 2.766 24.832 1.00 18.51 C ANISOU 652 CD1 LEU A 85 2104 3106 1823 138 70 -16 C ATOM 653 CD2 LEU A 85 -21.670 1.607 22.980 1.00 18.96 C ANISOU 653 CD2 LEU A 85 2157 3116 1929 106 59 35 C ATOM 654 N VAL A 86 -25.670 -1.960 24.054 1.00 13.64 N ANISOU 654 N VAL A 86 1427 2571 1187 16 145 79 N ATOM 655 CA VAL A 86 -26.252 -3.196 24.569 1.00 17.63 C ANISOU 655 CA VAL A 86 1932 3093 1672 -33 166 108 C ATOM 656 C VAL A 86 -26.059 -4.325 23.569 1.00 20.97 C ANISOU 656 C VAL A 86 2373 3472 2121 -62 145 130 C ATOM 657 O VAL A 86 -25.603 -5.420 23.919 1.00 20.57 O ANISOU 657 O VAL A 86 2361 3393 2062 -90 140 161 O ATOM 658 CB VAL A 86 -27.745 -2.988 24.882 1.00 19.51 C ANISOU 658 CB VAL A 86 2113 3393 1906 -47 203 96 C ATOM 659 CG1 VAL A 86 -28.377 -4.288 25.360 1.00 17.43 C ANISOU 659 CG1 VAL A 86 1849 3148 1626 -113 229 132 C ATOM 660 CG2 VAL A 86 -27.936 -1.864 25.890 1.00 17.34 C ANISOU 660 CG2 VAL A 86 1828 3159 1602 -8 232 63 C ATOM 661 N LEU A 87 -26.421 -4.073 22.305 1.00 13.70 N ANISOU 661 N LEU A 87 1434 2543 1230 -55 129 114 N ATOM 662 CA LEU A 87 -26.364 -5.118 21.290 1.00 20.61 C ANISOU 662 CA LEU A 87 2333 3377 2120 -84 110 124 C ATOM 663 C LEU A 87 -24.929 -5.541 21.013 1.00 22.56 C ANISOU 663 C LEU A 87 2630 3569 2373 -65 100 129 C ATOM 664 O LEU A 87 -24.653 -6.733 20.820 1.00 20.46 O ANISOU 664 O LEU A 87 2399 3261 2113 -87 94 143 O ATOM 665 CB LEU A 87 -27.043 -4.639 20.007 1.00 18.50 C ANISOU 665 CB LEU A 87 2044 3117 1870 -79 87 103 C ATOM 666 CG LEU A 87 -28.525 -4.269 20.142 1.00 20.61 C ANISOU 666 CG LEU A 87 2243 3439 2148 -92 88 96 C ATOM 667 CD1 LEU A 87 -29.108 -3.863 18.793 1.00 17.19 C ANISOU 667 CD1 LEU A 87 1795 3004 1731 -84 46 81 C ATOM 668 CD2 LEU A 87 -29.320 -5.412 20.761 1.00 14.64 C ANISOU 668 CD2 LEU A 87 1467 2704 1393 -155 107 117 C ATOM 669 N ALA A 88 -24.001 -4.580 20.975 1.00 18.13 N ANISOU 669 N ALA A 88 2070 3002 1816 -23 98 117 N ATOM 670 CA ALA A 88 -22.599 -4.936 20.796 1.00 17.45 C ANISOU 670 CA ALA A 88 2012 2873 1747 -2 94 121 C ATOM 671 C ALA A 88 -22.093 -5.755 21.976 1.00 17.41 C ANISOU 671 C ALA A 88 2024 2853 1736 -8 86 147 C ATOM 672 O ALA A 88 -21.369 -6.740 21.790 1.00 18.85 O ANISOU 672 O ALA A 88 2233 2989 1939 -3 77 158 O ATOM 673 CB ALA A 88 -21.748 -3.679 20.607 1.00 15.10 C ANISOU 673 CB ALA A 88 1701 2577 1460 31 93 106 C ATOM 674 N GLN A 89 -22.466 -5.369 23.198 1.00 15.87 N ANISOU 674 N GLN A 89 1822 2694 1512 -16 88 157 N ATOM 675 CA GLN A 89 -22.015 -6.123 24.364 1.00 18.11 C ANISOU 675 CA GLN A 89 2137 2966 1777 -25 73 190 C ATOM 676 C GLN A 89 -22.581 -7.535 24.357 1.00 21.66 C ANISOU 676 C GLN A 89 2617 3389 2225 -67 75 220 C ATOM 677 O GLN A 89 -21.875 -8.497 24.688 1.00 20.24 O ANISOU 677 O GLN A 89 2475 3160 2054 -65 50 248 O ATOM 678 CB GLN A 89 -22.407 -5.405 25.653 1.00 15.75 C ANISOU 678 CB GLN A 89 1837 2718 1430 -30 81 190 C ATOM 679 CG GLN A 89 -21.527 -5.824 26.816 1.00 19.14 C ANISOU 679 CG GLN A 89 2308 3132 1834 -27 48 220 C ATOM 680 CD GLN A 89 -20.071 -5.508 26.551 1.00 19.40 C ANISOU 680 CD GLN A 89 2331 3129 1909 14 8 211 C ATOM 681 OE1 GLN A 89 -19.747 -4.436 26.041 1.00 23.11 O ANISOU 681 OE1 GLN A 89 2769 3608 2402 36 11 178 O ATOM 682 NE2 GLN A 89 -19.186 -6.443 26.876 1.00 20.78 N ANISOU 682 NE2 GLN A 89 2531 3262 2102 23 -30 243 N ATOM 683 N SER A 90 -23.858 -7.674 23.995 1.00 19.62 N ANISOU 683 N SER A 90 2339 3156 1958 -106 98 216 N ATOM 684 CA SER A 90 -24.462 -8.995 23.899 1.00 17.99 C ANISOU 684 CA SER A 90 2161 2919 1756 -159 96 243 C ATOM 685 C SER A 90 -23.714 -9.862 22.897 1.00 17.81 C ANISOU 685 C SER A 90 2175 2821 1772 -143 72 236 C ATOM 686 O SER A 90 -23.498 -11.053 23.136 1.00 19.01 O ANISOU 686 O SER A 90 2375 2915 1932 -163 55 264 O ATOM 687 CB SER A 90 -25.934 -8.868 23.509 1.00 17.70 C ANISOU 687 CB SER A 90 2079 2928 1719 -204 119 233 C ATOM 688 OG SER A 90 -26.547 -10.143 23.407 1.00 20.42 O ANISOU 688 OG SER A 90 2448 3240 2071 -268 114 260 O ATOM 689 N SER A 91 -23.311 -9.273 21.767 1.00 17.77 N ANISOU 689 N SER A 91 2153 2812 1789 -106 73 197 N ATOM 690 CA SER A 91 -22.553 -10.010 20.762 1.00 18.26 C ANISOU 690 CA SER A 91 2249 2808 1879 -84 64 179 C ATOM 691 C SER A 91 -21.226 -10.499 21.323 1.00 19.11 C ANISOU 691 C SER A 91 2379 2870 2012 -41 49 194 C ATOM 692 O SER A 91 -20.820 -11.640 21.079 1.00 20.96 O ANISOU 692 O SER A 91 2657 3037 2272 -34 35 198 O ATOM 693 CB SER A 91 -22.326 -9.126 19.532 1.00 17.40 C ANISOU 693 CB SER A 91 2122 2716 1775 -55 77 138 C ATOM 694 OG SER A 91 -23.564 -8.695 18.989 1.00 20.64 O ANISOU 694 OG SER A 91 2512 3164 2167 -89 76 127 O ATOM 695 N ILE A 92 -20.535 -9.641 22.077 1.00 19.62 N ANISOU 695 N ILE A 92 2414 2966 2073 -10 44 202 N ATOM 696 CA ILE A 92 -19.264 -10.015 22.692 1.00 18.77 C ANISOU 696 CA ILE A 92 2314 2823 1994 32 16 219 C ATOM 697 C ILE A 92 -19.450 -11.182 23.650 1.00 17.16 C ANISOU 697 C ILE A 92 2162 2577 1779 8 -15 267 C ATOM 698 O ILE A 92 -18.653 -12.129 23.660 1.00 18.17 O ANISOU 698 O ILE A 92 2319 2638 1946 40 -43 280 O ATOM 699 CB ILE A 92 -18.652 -8.793 23.401 1.00 23.01 C ANISOU 699 CB ILE A 92 2811 3408 2524 54 7 218 C ATOM 700 CG1 ILE A 92 -18.116 -7.804 22.364 1.00 21.79 C ANISOU 700 CG1 ILE A 92 2613 3270 2395 81 33 178 C ATOM 701 CG2 ILE A 92 -17.576 -9.224 24.386 1.00 19.55 C ANISOU 701 CG2 ILE A 92 2382 2942 2105 84 -42 248 C ATOM 702 CD1 ILE A 92 -17.741 -6.465 22.943 1.00 28.62 C ANISOU 702 CD1 ILE A 92 3443 4178 3252 89 23 172 C ATOM 703 N PHE A 93 -20.496 -11.131 24.478 1.00 16.64 N ANISOU 703 N PHE A 93 2110 2549 1662 -46 -9 296 N ATOM 704 CA PHE A 93 -20.755 -12.238 25.395 1.00 18.88 C ANISOU 704 CA PHE A 93 2454 2795 1925 -83 -33 351 C ATOM 705 C PHE A 93 -21.031 -13.532 24.633 1.00 20.05 C ANISOU 705 C PHE A 93 2647 2865 2107 -105 -39 354 C ATOM 706 O PHE A 93 -20.536 -14.602 25.009 1.00 21.25 O ANISOU 706 O PHE A 93 2855 2940 2279 -96 -77 390 O ATOM 707 CB PHE A 93 -21.921 -11.891 26.326 1.00 21.11 C ANISOU 707 CB PHE A 93 2737 3144 2141 -146 -5 378 C ATOM 708 CG PHE A 93 -21.562 -10.904 27.415 1.00 25.69 C ANISOU 708 CG PHE A 93 3306 3782 2674 -126 -10 382 C ATOM 709 CD1 PHE A 93 -20.288 -10.889 27.967 1.00 34.79 C ANISOU 709 CD1 PHE A 93 4476 4906 3837 -78 -63 397 C ATOM 710 CD2 PHE A 93 -22.491 -9.984 27.874 1.00 25.23 C ANISOU 710 CD2 PHE A 93 3217 3804 2565 -153 34 367 C ATOM 711 CE1 PHE A 93 -19.956 -9.980 28.961 1.00 36.23 C ANISOU 711 CE1 PHE A 93 4656 5138 3971 -66 -78 396 C ATOM 712 CE2 PHE A 93 -22.166 -9.076 28.862 1.00 25.85 C ANISOU 712 CE2 PHE A 93 3297 3928 2595 -134 28 362 C ATOM 713 CZ PHE A 93 -20.898 -9.073 29.409 1.00 27.04 C ANISOU 713 CZ PHE A 93 3476 4050 2749 -95 -31 377 C ATOM 714 N SER A 94 -21.815 -13.456 23.555 1.00 16.84 N ANISOU 714 N SER A 94 2221 2468 1708 -132 -10 317 N ATOM 715 CA SER A 94 -22.083 -14.659 22.769 1.00 21.05 C ANISOU 715 CA SER A 94 2805 2923 2271 -156 -22 310 C ATOM 716 C SER A 94 -20.812 -15.191 22.115 1.00 20.14 C ANISOU 716 C SER A 94 2714 2730 2208 -81 -39 281 C ATOM 717 O SER A 94 -20.576 -16.404 22.104 1.00 24.52 O ANISOU 717 O SER A 94 3331 3193 2791 -78 -68 295 O ATOM 718 CB SER A 94 -23.149 -14.376 21.712 1.00 23.26 C ANISOU 718 CB SER A 94 3059 3236 2544 -199 1 270 C ATOM 719 OG SER A 94 -24.403 -14.116 22.323 1.00 25.28 O ANISOU 719 OG SER A 94 3284 3554 2767 -271 18 298 O ATOM 720 N LEU A 95 -19.987 -14.301 21.558 1.00 19.66 N ANISOU 720 N LEU A 95 2603 2703 2163 -19 -20 240 N ATOM 721 CA LEU A 95 -18.744 -14.732 20.922 1.00 18.18 C ANISOU 721 CA LEU A 95 2422 2457 2030 57 -21 207 C ATOM 722 C LEU A 95 -17.810 -15.392 21.925 1.00 20.52 C ANISOU 722 C LEU A 95 2737 2699 2362 100 -68 249 C ATOM 723 O LEU A 95 -17.160 -16.395 21.611 1.00 20.58 O ANISOU 723 O LEU A 95 2779 2619 2419 147 -86 238 O ATOM 724 CB LEU A 95 -18.051 -13.540 20.263 1.00 15.94 C ANISOU 724 CB LEU A 95 2071 2231 1753 101 15 165 C ATOM 725 CG LEU A 95 -18.753 -12.975 19.028 1.00 20.17 C ANISOU 725 CG LEU A 95 2602 2803 2258 74 55 121 C ATOM 726 CD1 LEU A 95 -18.097 -11.673 18.567 1.00 19.55 C ANISOU 726 CD1 LEU A 95 2464 2784 2179 106 89 97 C ATOM 727 CD2 LEU A 95 -18.749 -14.002 17.916 1.00 16.09 C ANISOU 727 CD2 LEU A 95 2143 2216 1753 82 65 79 C ATOM 728 N LEU A 96 -17.724 -14.837 23.133 1.00 20.27 N ANISOU 728 N LEU A 96 2685 2714 2303 91 -94 294 N ATOM 729 CA LEU A 96 -16.860 -15.414 24.156 1.00 24.68 C ANISOU 729 CA LEU A 96 3266 3225 2886 130 -154 341 C ATOM 730 C LEU A 96 -17.391 -16.763 24.625 1.00 25.46 C ANISOU 730 C LEU A 96 3456 3239 2978 91 -190 392 C ATOM 731 O LEU A 96 -16.614 -17.698 24.856 1.00 26.64 O ANISOU 731 O LEU A 96 3645 3301 3177 142 -240 413 O ATOM 732 CB LEU A 96 -16.729 -14.440 25.329 1.00 24.46 C ANISOU 732 CB LEU A 96 3208 3271 2813 118 -176 374 C ATOM 733 CG LEU A 96 -15.866 -14.888 26.512 1.00 28.15 C ANISOU 733 CG LEU A 96 3703 3703 3290 152 -253 429 C ATOM 734 CD1 LEU A 96 -14.463 -15.268 26.047 1.00 27.34 C ANISOU 734 CD1 LEU A 96 3561 3545 3284 246 -285 405 C ATOM 735 CD2 LEU A 96 -15.809 -13.796 27.583 1.00 27.59 C ANISOU 735 CD2 LEU A 96 3609 3714 3160 134 -272 448 C ATOM 736 N ALA A 97 -18.713 -16.883 24.763 1.00 23.09 N ANISOU 736 N ALA A 97 3189 2962 2624 1 -167 413 N ATOM 737 CA ALA A 97 -19.312 -18.160 25.133 1.00 25.32 C ANISOU 737 CA ALA A 97 3560 3161 2900 -55 -195 464 C ATOM 738 C ALA A 97 -19.035 -19.224 24.080 1.00 24.21 C ANISOU 738 C ALA A 97 3465 2911 2824 -23 -205 425 C ATOM 739 O ALA A 97 -18.741 -20.374 24.419 1.00 23.61 O ANISOU 739 O ALA A 97 3464 2727 2778 -12 -255 462 O ATOM 740 CB ALA A 97 -20.817 -17.992 25.343 1.00 22.47 C ANISOU 740 CB ALA A 97 3202 2858 2477 -164 -156 485 C ATOM 741 N ILE A 98 -19.131 -18.861 22.798 1.00 25.88 N ANISOU 741 N ILE A 98 3639 3143 3051 -7 -161 350 N ATOM 742 CA ILE A 98 -18.869 -19.824 21.729 1.00 24.11 C ANISOU 742 CA ILE A 98 3465 2818 2878 26 -163 299 C ATOM 743 C ILE A 98 -17.433 -20.325 21.808 1.00 27.34 C ANISOU 743 C ILE A 98 3878 3153 3356 137 -193 289 C ATOM 744 O ILE A 98 -17.176 -21.530 21.699 1.00 29.38 O ANISOU 744 O ILE A 98 4211 3290 3661 164 -229 291 O ATOM 745 CB ILE A 98 -19.182 -19.199 20.356 1.00 21.47 C ANISOU 745 CB ILE A 98 3094 2534 2530 24 -109 220 C ATOM 746 CG1 ILE A 98 -20.687 -18.966 20.209 1.00 22.46 C ANISOU 746 CG1 ILE A 98 3220 2711 2602 -84 -97 229 C ATOM 747 CG2 ILE A 98 -18.675 -20.093 19.230 1.00 21.65 C ANISOU 747 CG2 ILE A 98 3170 2459 2597 76 -103 153 C ATOM 748 CD1 ILE A 98 -21.073 -18.083 19.034 1.00 18.19 C ANISOU 748 CD1 ILE A 98 2635 2240 2035 -90 -56 166 C ATOM 749 N ALA A 99 -16.478 -19.413 22.017 1.00 25.67 N ANISOU 749 N ALA A 99 3584 3008 3162 204 -184 280 N ATOM 750 CA ALA A 99 -15.079 -19.815 22.128 1.00 25.83 C ANISOU 750 CA ALA A 99 3583 2970 3260 313 -215 271 C ATOM 751 C ALA A 99 -14.864 -20.752 23.311 1.00 27.52 C ANISOU 751 C ALA A 99 3864 3099 3493 321 -300 350 C ATOM 752 O ALA A 99 -14.167 -21.768 23.191 1.00 27.59 O ANISOU 752 O ALA A 99 3911 2997 3574 394 -339 344 O ATOM 753 CB ALA A 99 -14.186 -18.578 22.253 1.00 19.95 C ANISOU 753 CB ALA A 99 2728 2323 2529 362 -195 255 C ATOM 754 N ILE A 100 -15.458 -20.429 24.463 1.00 25.45 N ANISOU 754 N ILE A 100 3621 2886 3165 250 -330 424 N ATOM 755 CA ILE A 100 -15.305 -21.276 25.642 1.00 26.16 C ANISOU 755 CA ILE A 100 3788 2899 3253 246 -414 511 C ATOM 756 C ILE A 100 -15.959 -22.632 25.414 1.00 25.91 C ANISOU 756 C ILE A 100 3869 2742 3233 203 -433 531 C ATOM 757 O ILE A 100 -15.398 -23.675 25.770 1.00 28.30 O ANISOU 757 O ILE A 100 4241 2925 3589 252 -503 568 O ATOM 758 CB ILE A 100 -15.874 -20.561 26.881 1.00 27.51 C ANISOU 758 CB ILE A 100 3962 3161 3330 170 -426 580 C ATOM 759 CG1 ILE A 100 -15.012 -19.336 27.219 1.00 27.10 C ANISOU 759 CG1 ILE A 100 3812 3206 3278 224 -431 561 C ATOM 760 CG2 ILE A 100 -15.972 -21.517 28.067 1.00 23.82 C ANISOU 760 CG2 ILE A 100 3601 2614 2835 139 -504 679 C ATOM 761 CD1 ILE A 100 -15.527 -18.513 28.370 1.00 27.31 C ANISOU 761 CD1 ILE A 100 3843 3326 3206 157 -437 610 C ATOM 762 N ASP A 101 -17.145 -22.638 24.805 1.00 23.26 N ANISOU 762 N ASP A 101 3554 2427 2856 111 -379 508 N ATOM 763 CA ASP A 101 -17.826 -23.892 24.502 1.00 26.54 C ANISOU 763 CA ASP A 101 4075 2722 3285 55 -398 520 C ATOM 764 C ASP A 101 -16.964 -24.793 23.623 1.00 27.41 C ANISOU 764 C ASP A 101 4221 2705 3488 157 -418 459 C ATOM 765 O ASP A 101 -16.909 -26.010 23.834 1.00 29.52 O ANISOU 765 O ASP A 101 4591 2832 3794 161 -475 492 O ATOM 766 CB ASP A 101 -19.162 -23.601 23.819 1.00 26.02 C ANISOU 766 CB ASP A 101 4000 2715 3171 -54 -338 488 C ATOM 767 CG ASP A 101 -19.903 -24.864 23.442 1.00 34.16 C ANISOU 767 CG ASP A 101 5136 3624 4221 -125 -361 495 C ATOM 768 OD1 ASP A 101 -20.531 -25.466 24.334 1.00 37.56 O ANISOU 768 OD1 ASP A 101 5634 4014 4623 -213 -392 581 O ATOM 769 OD2 ASP A 101 -19.843 -25.262 22.264 1.00 34.28 O ANISOU 769 OD2 ASP A 101 5171 3580 4274 -97 -348 415 O ATOM 770 N ARG A 102 -16.288 -24.215 22.627 1.00 24.40 N ANISOU 770 N ARG A 102 3761 2368 3142 239 -367 367 N ATOM 771 CA ARG A 102 -15.445 -25.029 21.758 1.00 28.03 C ANISOU 771 CA ARG A 102 4247 2716 3685 344 -370 297 C ATOM 772 C ARG A 102 -14.183 -25.490 22.475 1.00 29.78 C ANISOU 772 C ARG A 102 4462 2867 3986 460 -438 331 C ATOM 773 O ARG A 102 -13.675 -26.579 22.188 1.00 31.26 O ANISOU 773 O ARG A 102 4713 2915 4248 534 -473 308 O ATOM 774 CB ARG A 102 -15.105 -24.257 20.480 1.00 31.93 C ANISOU 774 CB ARG A 102 4661 3287 4182 391 -284 192 C ATOM 775 CG ARG A 102 -16.295 -24.044 19.518 1.00 34.40 C ANISOU 775 CG ARG A 102 5002 3639 4430 294 -232 144 C ATOM 776 CD ARG A 102 -16.841 -25.370 18.961 1.00 39.16 C ANISOU 776 CD ARG A 102 5729 4098 5050 262 -259 116 C ATOM 777 NE ARG A 102 -17.750 -26.032 19.896 1.00 42.46 N ANISOU 777 NE ARG A 102 6225 4460 5448 158 -320 207 N ATOM 778 CZ ARG A 102 -17.978 -27.341 19.934 1.00 43.51 C ANISOU 778 CZ ARG A 102 6477 4440 5616 137 -373 221 C ATOM 779 NH1 ARG A 102 -17.361 -28.152 19.085 1.00 45.28 N ANISOU 779 NH1 ARG A 102 6758 4545 5900 223 -376 141 N ATOM 780 NH2 ARG A 102 -18.821 -27.840 20.830 1.00 40.64 N ANISOU 780 NH2 ARG A 102 6176 4038 5228 28 -421 314 N ATOM 781 N TYR A 103 -13.672 -24.692 23.417 1.00 25.10 N ANISOU 781 N TYR A 103 3795 2362 3380 478 -465 384 N ATOM 782 CA TYR A 103 -12.516 -25.131 24.191 1.00 26.08 C ANISOU 782 CA TYR A 103 3911 2421 3578 582 -549 427 C ATOM 783 C TYR A 103 -12.872 -26.294 25.113 1.00 30.28 C ANISOU 783 C TYR A 103 4578 2823 4106 547 -643 522 C ATOM 784 O TYR A 103 -12.082 -27.232 25.268 1.00 33.43 O ANISOU 784 O TYR A 103 5018 3093 4590 643 -715 534 O ATOM 785 CB TYR A 103 -11.935 -23.970 25.000 1.00 25.45 C ANISOU 785 CB TYR A 103 3726 2467 3476 597 -567 461 C ATOM 786 CG TYR A 103 -10.800 -24.403 25.905 1.00 40.00 C ANISOU 786 CG TYR A 103 5560 4249 5390 694 -674 516 C ATOM 787 CD1 TYR A 103 -9.546 -24.694 25.384 1.00 39.62 C ANISOU 787 CD1 TYR A 103 5437 4153 5464 834 -684 458 C ATOM 788 CD2 TYR A 103 -10.989 -24.549 27.275 1.00 44.49 C ANISOU 788 CD2 TYR A 103 6195 4807 5903 648 -766 624 C ATOM 789 CE1 TYR A 103 -8.510 -25.104 26.202 1.00 44.60 C ANISOU 789 CE1 TYR A 103 6049 4725 6170 930 -794 508 C ATOM 790 CE2 TYR A 103 -9.961 -24.963 28.101 1.00 46.06 C ANISOU 790 CE2 TYR A 103 6392 4945 6163 737 -880 679 C ATOM 791 CZ TYR A 103 -8.722 -25.237 27.559 1.00 47.53 C ANISOU 791 CZ TYR A 103 6493 5083 6482 881 -899 621 C ATOM 792 OH TYR A 103 -7.688 -25.647 28.372 1.00 52.18 O ANISOU 792 OH TYR A 103 7069 5612 7144 977 -1024 675 O ATOM 793 N ILE A 104 -14.044 -26.243 25.750 1.00 31.46 N ANISOU 793 N ILE A 104 4793 3002 4157 410 -645 593 N ATOM 794 CA ILE A 104 -14.457 -27.346 26.617 1.00 33.75 C ANISOU 794 CA ILE A 104 5221 3169 4432 357 -725 693 C ATOM 795 C ILE A 104 -14.600 -28.629 25.809 1.00 33.89 C ANISOU 795 C ILE A 104 5338 3020 4519 375 -738 654 C ATOM 796 O ILE A 104 -14.209 -29.713 26.260 1.00 36.52 O ANISOU 796 O ILE A 104 5769 3202 4906 419 -826 707 O ATOM 797 CB ILE A 104 -15.763 -26.990 27.352 1.00 35.41 C ANISOU 797 CB ILE A 104 5472 3460 4523 195 -699 767 C ATOM 798 CG1 ILE A 104 -15.555 -25.766 28.245 1.00 32.11 C ANISOU 798 CG1 ILE A 104 4972 3192 4034 188 -695 802 C ATOM 799 CG2 ILE A 104 -16.263 -28.182 28.165 1.00 38.48 C ANISOU 799 CG2 ILE A 104 6013 3718 4891 122 -770 874 C ATOM 800 CD1 ILE A 104 -16.821 -25.264 28.894 1.00 31.90 C ANISOU 800 CD1 ILE A 104 4966 3265 3889 42 -647 856 C ATOM 801 N ALA A 105 -15.146 -28.524 24.595 1.00 30.89 N ANISOU 801 N ALA A 105 4941 2659 4138 345 -657 560 N ATOM 802 CA ALA A 105 -15.349 -29.704 23.764 1.00 34.45 C ANISOU 802 CA ALA A 105 5493 2951 4644 354 -667 510 C ATOM 803 C ALA A 105 -14.030 -30.317 23.307 1.00 38.23 C ANISOU 803 C ALA A 105 5967 3318 5239 527 -697 447 C ATOM 804 O ALA A 105 -13.936 -31.541 23.170 1.00 41.77 O ANISOU 804 O ALA A 105 6530 3590 5749 560 -752 446 O ATOM 805 CB ALA A 105 -16.214 -29.347 22.557 1.00 33.08 C ANISOU 805 CB ALA A 105 5300 2837 4431 282 -579 418 C ATOM 806 N ILE A 106 -13.007 -29.499 23.068 1.00 40.18 N ANISOU 806 N ILE A 106 6081 3660 5524 639 -662 394 N ATOM 807 CA ILE A 106 -11.728 -30.033 22.606 1.00 40.86 C ANISOU 807 CA ILE A 106 6140 3655 5731 809 -679 327 C ATOM 808 C ILE A 106 -10.849 -30.495 23.770 1.00 41.07 C ANISOU 808 C ILE A 106 6176 3606 5823 896 -797 418 C ATOM 809 O ILE A 106 -10.063 -31.437 23.616 1.00 39.76 O ANISOU 809 O ILE A 106 6046 3296 5765 1021 -849 393 O ATOM 810 CB ILE A 106 -10.996 -28.995 21.730 1.00 40.92 C ANISOU 810 CB ILE A 106 5994 3797 5758 887 -580 225 C ATOM 811 CG1 ILE A 106 -9.875 -29.653 20.922 1.00 46.10 C ANISOU 811 CG1 ILE A 106 6626 4356 6534 1053 -561 127 C ATOM 812 CG2 ILE A 106 -10.412 -27.874 22.572 1.00 37.54 C ANISOU 812 CG2 ILE A 106 5438 3510 5316 901 -596 279 C ATOM 813 CD1 ILE A 106 -10.365 -30.511 19.787 1.00 50.17 C ANISOU 813 CD1 ILE A 106 7251 4760 7053 1048 -516 35 C ATOM 814 N ALA A 107 -10.977 -29.872 24.941 1.00 40.32 N ANISOU 814 N ALA A 107 6057 3601 5663 834 -845 521 N ATOM 815 CA ALA A 107 -10.091 -30.168 26.059 1.00 44.09 C ANISOU 815 CA ALA A 107 6536 4026 6191 915 -966 608 C ATOM 816 C ALA A 107 -10.629 -31.280 26.949 1.00 48.47 C ANISOU 816 C ALA A 107 7264 4430 6722 854 -1071 723 C ATOM 817 O ALA A 107 -9.858 -32.129 27.409 1.00 52.59 O ANISOU 817 O ALA A 107 7837 4816 7330 957 -1179 766 O ATOM 818 CB ALA A 107 -9.851 -28.905 26.889 1.00 44.52 C ANISOU 818 CB ALA A 107 6483 4251 6181 886 -974 656 C ATOM 819 N ILE A 108 -11.933 -31.294 27.205 1.00 48.90 N ANISOU 819 N ILE A 108 7408 4506 6666 687 -1041 777 N ATOM 820 CA ILE A 108 -12.539 -32.315 28.057 1.00 50.90 C ANISOU 820 CA ILE A 108 7830 4624 6884 603 -1128 896 C ATOM 821 C ILE A 108 -13.791 -32.873 27.388 1.00 47.06 C ANISOU 821 C ILE A 108 7440 4079 6363 472 -1068 872 C ATOM 822 O ILE A 108 -14.902 -32.704 27.912 1.00 45.90 O ANISOU 822 O ILE A 108 7341 3987 6110 311 -1044 945 O ATOM 823 CB ILE A 108 -12.854 -31.750 29.451 1.00 54.68 C ANISOU 823 CB ILE A 108 8326 5202 7250 510 -1170 1023 C ATOM 824 CG1 ILE A 108 -13.478 -30.360 29.337 1.00 53.35 C ANISOU 824 CG1 ILE A 108 8043 5247 6982 420 -1060 985 C ATOM 825 CG2 ILE A 108 -11.591 -31.686 30.293 1.00 58.60 C ANISOU 825 CG2 ILE A 108 8787 5683 7794 638 -1285 1074 C ATOM 826 CD1 ILE A 108 -13.893 -29.773 30.665 1.00 56.73 C ANISOU 826 CD1 ILE A 108 8494 5776 7284 323 -1085 1095 C ATOM 827 N PRO A 109 -13.666 -33.557 26.247 1.00 46.91 N ANISOU 827 N PRO A 109 7450 3946 6426 533 -1044 771 N ATOM 828 CA PRO A 109 -14.870 -34.048 25.557 1.00 49.23 C ANISOU 828 CA PRO A 109 7832 4187 6685 401 -995 740 C ATOM 829 C PRO A 109 -15.622 -35.129 26.321 1.00 55.67 C ANISOU 829 C PRO A 109 8819 4855 7477 283 -1072 859 C ATOM 830 O PRO A 109 -16.820 -35.313 26.074 1.00 54.65 O ANISOU 830 O PRO A 109 8745 4727 7293 127 -1032 868 O ATOM 831 CB PRO A 109 -14.316 -34.587 24.231 1.00 49.04 C ANISOU 831 CB PRO A 109 7811 4060 6761 522 -967 599 C ATOM 832 CG PRO A 109 -12.914 -34.977 24.551 1.00 49.19 C ANISOU 832 CG PRO A 109 7811 3990 6889 708 -1042 601 C ATOM 833 CD PRO A 109 -12.428 -33.972 25.563 1.00 47.22 C ANISOU 833 CD PRO A 109 7451 3894 6598 724 -1063 678 C ATOM 834 N LEU A 110 -14.966 -35.846 27.238 1.00 60.57 N ANISOU 834 N LEU A 110 9526 5348 8139 348 -1186 956 N ATOM 835 CA LEU A 110 -15.652 -36.912 27.962 1.00 67.91 C ANISOU 835 CA LEU A 110 10634 6124 9045 231 -1262 1078 C ATOM 836 C LEU A 110 -16.689 -36.362 28.934 1.00 71.78 C ANISOU 836 C LEU A 110 11131 6746 9395 45 -1229 1194 C ATOM 837 O LEU A 110 -17.670 -37.048 29.242 1.00 73.31 O ANISOU 837 O LEU A 110 11447 6860 9547 -109 -1239 1273 O ATOM 838 CB LEU A 110 -14.641 -37.783 28.707 1.00 68.52 C ANISOU 838 CB LEU A 110 10806 6029 9199 356 -1401 1158 C ATOM 839 CG LEU A 110 -13.650 -38.560 27.839 1.00 68.24 C ANISOU 839 CG LEU A 110 10772 5845 9313 540 -1432 1046 C ATOM 840 CD1 LEU A 110 -12.714 -39.388 28.705 1.00 68.28 C ANISOU 840 CD1 LEU A 110 10799 5770 9375 643 -1529 1111 C ATOM 841 CD2 LEU A 110 -14.384 -39.439 26.839 1.00 68.17 C ANISOU 841 CD2 LEU A 110 10864 5700 9337 475 -1397 970 C ATOM 842 N ARG A 111 -16.496 -35.137 29.426 1.00 72.23 N ANISOU 842 N ARG A 111 11062 7003 9381 55 -1187 1203 N ATOM 843 CA ARG A 111 -17.439 -34.520 30.353 1.00 73.21 C ANISOU 843 CA ARG A 111 11183 7265 9368 -106 -1143 1299 C ATOM 844 C ARG A 111 -18.081 -33.266 29.772 1.00 66.15 C ANISOU 844 C ARG A 111 10138 6581 8417 -163 -1015 1211 C ATOM 845 O ARG A 111 -18.594 -32.433 30.525 1.00 63.11 O ANISOU 845 O ARG A 111 9706 6348 7925 -249 -969 1265 O ATOM 846 CB ARG A 111 -16.752 -34.203 31.682 1.00 79.35 C ANISOU 846 CB ARG A 111 11973 8085 10090 -62 -1220 1407 C ATOM 847 CG ARG A 111 -15.349 -33.653 31.542 1.00 85.06 C ANISOU 847 CG ARG A 111 12584 8847 10887 131 -1263 1342 C ATOM 848 CD ARG A 111 -14.673 -33.550 32.899 1.00 92.80 C ANISOU 848 CD ARG A 111 13605 9837 11819 169 -1370 1460 C ATOM 849 NE ARG A 111 -13.253 -33.238 32.779 1.00 98.41 N ANISOU 849 NE ARG A 111 14214 10551 12626 358 -1436 1406 N ATOM 850 CZ ARG A 111 -12.426 -33.110 33.811 1.00102.15 C ANISOU 850 CZ ARG A 111 14693 11037 13084 424 -1543 1483 C ATOM 851 NH1 ARG A 111 -12.877 -33.266 35.050 1.00103.51 N ANISOU 851 NH1 ARG A 111 14946 11251 13134 313 -1561 1589 N ATOM 852 NH2 ARG A 111 -11.147 -32.826 33.605 1.00103.14 N ANISOU 852 NH2 ARG A 111 14704 11170 13314 594 -1599 1424 N ATOM 853 N TYR A 112 -18.074 -33.119 28.445 1.00 61.86 N ANISOU 853 N TYR A 112 9524 6043 7936 -115 -957 1078 N ATOM 854 CA TYR A 112 -18.677 -31.939 27.834 1.00 55.69 C ANISOU 854 CA TYR A 112 8606 5450 7103 -164 -847 997 C ATOM 855 C TYR A 112 -20.199 -31.995 27.913 1.00 56.69 C ANISOU 855 C TYR A 112 8761 5621 7156 -357 -791 1037 C ATOM 856 O TYR A 112 -20.848 -31.000 28.255 1.00 54.29 O ANISOU 856 O TYR A 112 8370 5488 6769 -434 -720 1050 O ATOM 857 CB TYR A 112 -18.210 -31.802 26.383 1.00 51.18 C ANISOU 857 CB TYR A 112 7967 4868 6611 -59 -806 849 C ATOM 858 CG TYR A 112 -18.939 -30.731 25.601 1.00 46.53 C ANISOU 858 CG TYR A 112 7263 4446 5972 -119 -702 768 C ATOM 859 CD1 TYR A 112 -18.516 -29.409 25.632 1.00 44.20 C ANISOU 859 CD1 TYR A 112 6830 4318 5645 -62 -651 732 C ATOM 860 CD2 TYR A 112 -20.046 -31.045 24.824 1.00 47.75 C ANISOU 860 CD2 TYR A 112 7446 4581 6114 -233 -664 728 C ATOM 861 CE1 TYR A 112 -19.183 -28.428 24.915 1.00 41.22 C ANISOU 861 CE1 TYR A 112 6355 4082 5223 -113 -565 664 C ATOM 862 CE2 TYR A 112 -20.720 -30.075 24.111 1.00 46.74 C ANISOU 862 CE2 TYR A 112 7215 4601 5943 -282 -583 659 C ATOM 863 CZ TYR A 112 -20.284 -28.769 24.158 1.00 43.47 C ANISOU 863 CZ TYR A 112 6672 4347 5497 -219 -534 629 C ATOM 864 OH TYR A 112 -20.957 -27.806 23.443 1.00 42.44 O ANISOU 864 OH TYR A 112 6447 4352 5326 -264 -461 565 O ATOM 865 N ASN A 113 -20.788 -33.156 27.606 1.00 59.37 N ANISOU 865 N ASN A 113 9221 5807 7532 -439 -822 1056 N ATOM 866 CA ASN A 113 -22.244 -33.270 27.622 1.00 61.66 C ANISOU 866 CA ASN A 113 9526 6135 7767 -631 -771 1091 C ATOM 867 C ASN A 113 -22.814 -33.105 29.025 1.00 61.19 C ANISOU 867 C ASN A 113 9494 6147 7609 -750 -760 1230 C ATOM 868 O ASN A 113 -23.912 -32.558 29.186 1.00 62.36 O ANISOU 868 O ASN A 113 9578 6427 7690 -882 -681 1246 O ATOM 869 CB ASN A 113 -22.676 -34.610 27.030 1.00 65.32 C ANISOU 869 CB ASN A 113 10120 6401 8296 -697 -819 1084 C ATOM 870 CG ASN A 113 -22.434 -34.688 25.541 1.00 69.53 C ANISOU 870 CG ASN A 113 10626 6892 8903 -616 -807 933 C ATOM 871 OD1 ASN A 113 -22.423 -33.669 24.849 1.00 69.91 O ANISOU 871 OD1 ASN A 113 10544 7086 8933 -572 -739 840 O ATOM 872 ND2 ASN A 113 -22.238 -35.900 25.035 1.00 73.67 N ANISOU 872 ND2 ASN A 113 11279 7208 9504 -596 -872 907 N ATOM 873 N GLY A 114 -22.090 -33.563 30.047 1.00 59.13 N ANISOU 873 N GLY A 114 9328 5805 7335 -703 -837 1330 N ATOM 874 CA GLY A 114 -22.552 -33.369 31.408 1.00 60.86 C ANISOU 874 CA GLY A 114 9585 6097 7442 -809 -825 1462 C ATOM 875 C GLY A 114 -22.350 -31.961 31.928 1.00 59.58 C ANISOU 875 C GLY A 114 9297 6144 7198 -767 -767 1446 C ATOM 876 O GLY A 114 -23.118 -31.499 32.779 1.00 60.89 O ANISOU 876 O GLY A 114 9450 6427 7256 -882 -706 1514 O ATOM 877 N LEU A 115 -21.324 -31.262 31.436 1.00 55.71 N ANISOU 877 N LEU A 115 8712 5701 6756 -605 -780 1353 N ATOM 878 CA LEU A 115 -21.036 -29.925 31.942 1.00 54.74 C ANISOU 878 CA LEU A 115 8477 5760 6561 -561 -738 1336 C ATOM 879 C LEU A 115 -21.820 -28.863 31.178 1.00 50.29 C ANISOU 879 C LEU A 115 7770 5357 5979 -603 -625 1239 C ATOM 880 O LEU A 115 -22.411 -27.961 31.782 1.00 49.12 O ANISOU 880 O LEU A 115 7562 5361 5739 -668 -557 1258 O ATOM 881 CB LEU A 115 -19.534 -29.653 31.864 1.00 60.54 C ANISOU 881 CB LEU A 115 9173 6470 7358 -377 -811 1294 C ATOM 882 CG LEU A 115 -19.066 -28.191 31.920 1.00 64.48 C ANISOU 882 CG LEU A 115 9530 7146 7824 -306 -768 1231 C ATOM 883 CD1 LEU A 115 -19.428 -27.541 33.245 1.00 66.07 C ANISOU 883 CD1 LEU A 115 9746 7465 7892 -382 -753 1315 C ATOM 884 CD2 LEU A 115 -17.571 -28.092 31.666 1.00 66.63 C ANISOU 884 CD2 LEU A 115 9755 7374 8186 -131 -843 1183 C ATOM 885 N VAL A 116 -21.851 -28.964 29.854 1.00 46.83 N ANISOU 885 N VAL A 116 7284 4884 5625 -565 -605 1134 N ATOM 886 CA VAL A 116 -22.433 -27.945 28.990 1.00 45.99 C ANISOU 886 CA VAL A 116 7045 4917 5512 -580 -517 1036 C ATOM 887 C VAL A 116 -23.765 -28.488 28.485 1.00 49.97 C ANISOU 887 C VAL A 116 7569 5397 6019 -726 -478 1035 C ATOM 888 O VAL A 116 -23.808 -29.290 27.545 1.00 54.16 O ANISOU 888 O VAL A 116 8147 5808 6622 -724 -506 987 O ATOM 889 CB VAL A 116 -21.491 -27.584 27.837 1.00 44.63 C ANISOU 889 CB VAL A 116 6803 4735 5419 -436 -522 918 C ATOM 890 CG1 VAL A 116 -21.946 -26.313 27.169 1.00 40.42 C ANISOU 890 CG1 VAL A 116 6135 4363 4860 -441 -438 835 C ATOM 891 CG2 VAL A 116 -20.067 -27.438 28.348 1.00 47.01 C ANISOU 891 CG2 VAL A 116 7103 5012 5747 -294 -584 931 C ATOM 892 N THR A 117 -24.859 -28.051 29.105 1.00 46.72 N ANISOU 892 N THR A 117 7119 5101 5531 -854 -412 1085 N ATOM 893 CA THR A 117 -26.205 -28.483 28.759 1.00 43.67 C ANISOU 893 CA THR A 117 6730 4714 5148 -1008 -372 1094 C ATOM 894 C THR A 117 -27.012 -27.311 28.215 1.00 41.84 C ANISOU 894 C THR A 117 6346 4654 4896 -1034 -288 1020 C ATOM 895 O THR A 117 -26.641 -26.143 28.358 1.00 41.61 O ANISOU 895 O THR A 117 6227 4751 4833 -953 -252 982 O ATOM 896 CB THR A 117 -26.922 -29.090 29.973 1.00 45.40 C ANISOU 896 CB THR A 117 7031 4918 5302 -1152 -360 1226 C ATOM 897 OG1 THR A 117 -27.002 -28.111 31.018 1.00 46.00 O ANISOU 897 OG1 THR A 117 7052 5148 5280 -1155 -301 1267 O ATOM 898 CG2 THR A 117 -26.176 -30.319 30.489 1.00 43.13 C ANISOU 898 CG2 THR A 117 6911 4442 5037 -1131 -456 1310 C ATOM 899 N GLY A 118 -28.144 -27.642 27.592 1.00 40.73 N ANISOU 899 N GLY A 118 6179 4515 4783 -1151 -265 1001 N ATOM 900 CA GLY A 118 -28.992 -26.608 27.024 1.00 38.08 C ANISOU 900 CA GLY A 118 5698 4332 4438 -1178 -198 933 C ATOM 901 C GLY A 118 -29.621 -25.715 28.076 1.00 38.21 C ANISOU 901 C GLY A 118 5633 4510 4376 -1230 -117 982 C ATOM 902 O GLY A 118 -29.729 -24.501 27.886 1.00 38.66 O ANISOU 902 O GLY A 118 5574 4702 4413 -1174 -69 923 O ATOM 903 N THR A 119 -30.048 -26.303 29.196 1.00 40.25 N ANISOU 903 N THR A 119 5957 4753 4585 -1337 -97 1089 N ATOM 904 CA THR A 119 -30.679 -25.525 30.260 1.00 41.99 C ANISOU 904 CA THR A 119 6111 5126 4719 -1392 -7 1135 C ATOM 905 C THR A 119 -29.706 -24.516 30.857 1.00 39.05 C ANISOU 905 C THR A 119 5724 4827 4285 -1259 -2 1118 C ATOM 906 O THR A 119 -30.052 -23.347 31.062 1.00 42.16 O ANISOU 906 O THR A 119 6012 5370 4639 -1236 67 1078 O ATOM 907 CB THR A 119 -31.212 -26.461 31.347 1.00 45.06 C ANISOU 907 CB THR A 119 6596 5469 5056 -1535 13 1261 C ATOM 908 OG1 THR A 119 -32.197 -27.336 30.785 1.00 50.69 O ANISOU 908 OG1 THR A 119 7308 6121 5831 -1674 11 1275 O ATOM 909 CG2 THR A 119 -31.836 -25.665 32.480 1.00 46.30 C ANISOU 909 CG2 THR A 119 6692 5790 5110 -1589 119 1304 C ATOM 910 N ARG A 120 -28.481 -24.955 31.154 1.00 38.22 N ANISOU 910 N ARG A 120 5726 4615 4179 -1171 -80 1147 N ATOM 911 CA ARG A 120 -27.470 -24.028 31.652 1.00 37.72 C ANISOU 911 CA ARG A 120 5647 4613 4070 -1045 -92 1127 C ATOM 912 C ARG A 120 -27.102 -22.988 30.602 1.00 39.75 C ANISOU 912 C ARG A 120 5789 4934 4379 -934 -85 1008 C ATOM 913 O ARG A 120 -26.776 -21.848 30.951 1.00 39.11 O ANISOU 913 O ARG A 120 5645 4959 4254 -868 -57 976 O ATOM 914 CB ARG A 120 -26.223 -24.794 32.098 1.00 35.95 C ANISOU 914 CB ARG A 120 5552 4254 3854 -971 -192 1182 C ATOM 915 CG ARG A 120 -26.470 -25.785 33.228 1.00 39.27 C ANISOU 915 CG ARG A 120 6108 4603 4211 -1074 -212 1312 C ATOM 916 CD ARG A 120 -25.221 -26.596 33.541 1.00 40.89 C ANISOU 916 CD ARG A 120 6439 4657 4442 -987 -329 1363 C ATOM 917 NE ARG A 120 -25.468 -27.596 34.577 1.00 48.48 N ANISOU 917 NE ARG A 120 7545 5534 5341 -1089 -358 1497 N ATOM 918 CZ ARG A 120 -24.610 -28.554 34.913 1.00 51.34 C ANISOU 918 CZ ARG A 120 8041 5738 5727 -1043 -468 1566 C ATOM 919 NH1 ARG A 120 -24.922 -29.420 35.868 1.00 56.10 N ANISOU 919 NH1 ARG A 120 8783 6268 6265 -1148 -491 1697 N ATOM 920 NH2 ARG A 120 -23.440 -28.649 34.294 1.00 48.31 N ANISOU 920 NH2 ARG A 120 7651 5270 5436 -891 -553 1507 N ATOM 921 N ALA A 121 -27.148 -23.355 29.319 1.00 40.03 N ANISOU 921 N ALA A 121 5805 4904 4501 -918 -111 944 N ATOM 922 CA ALA A 121 -26.869 -22.383 28.267 1.00 37.66 C ANISOU 922 CA ALA A 121 5405 4665 4240 -825 -99 838 C ATOM 923 C ALA A 121 -27.936 -21.298 28.224 1.00 34.71 C ANISOU 923 C ALA A 121 4908 4445 3835 -871 -19 804 C ATOM 924 O ALA A 121 -27.614 -20.110 28.104 1.00 30.92 O ANISOU 924 O ALA A 121 4353 4056 3341 -791 4 749 O ATOM 925 CB ALA A 121 -26.763 -23.082 26.913 1.00 35.34 C ANISOU 925 CB ALA A 121 5132 4265 4029 -809 -141 777 C ATOM 926 N ALA A 122 -29.212 -21.684 28.320 1.00 33.63 N ANISOU 926 N ALA A 122 4748 4336 3694 -999 22 835 N ATOM 927 CA ALA A 122 -30.283 -20.693 28.292 1.00 32.32 C ANISOU 927 CA ALA A 122 4453 4316 3510 -1038 97 801 C ATOM 928 C ALA A 122 -30.154 -19.710 29.452 1.00 35.01 C ANISOU 928 C ALA A 122 4766 4768 3768 -1005 154 820 C ATOM 929 O ALA A 122 -30.420 -18.513 29.293 1.00 35.30 O ANISOU 929 O ALA A 122 4701 4915 3796 -957 197 762 O ATOM 930 CB ALA A 122 -31.645 -21.387 28.320 1.00 32.90 C ANISOU 930 CB ALA A 122 4501 4399 3601 -1190 131 841 C ATOM 931 N GLY A 123 -29.736 -20.197 30.623 1.00 35.92 N ANISOU 931 N GLY A 123 4979 4852 3818 -1028 149 901 N ATOM 932 CA GLY A 123 -29.551 -19.308 31.759 1.00 33.66 C ANISOU 932 CA GLY A 123 4685 4664 3439 -997 196 916 C ATOM 933 C GLY A 123 -28.369 -18.375 31.578 1.00 31.46 C ANISOU 933 C GLY A 123 4393 4395 3163 -856 153 857 C ATOM 934 O GLY A 123 -28.439 -17.195 31.931 1.00 34.60 O ANISOU 934 O GLY A 123 4729 4900 3519 -813 198 815 O ATOM 935 N ILE A 124 -27.267 -18.890 31.029 1.00 27.36 N ANISOU 935 N ILE A 124 3931 3764 2698 -784 68 849 N ATOM 936 CA ILE A 124 -26.121 -18.038 30.721 1.00 27.63 C ANISOU 936 CA ILE A 124 3938 3807 2752 -657 29 790 C ATOM 937 C ILE A 124 -26.513 -16.962 29.716 1.00 26.97 C ANISOU 937 C ILE A 124 3737 3801 2708 -618 68 699 C ATOM 938 O ILE A 124 -26.138 -15.790 29.859 1.00 25.66 O ANISOU 938 O ILE A 124 3521 3707 2521 -552 82 655 O ATOM 939 CB ILE A 124 -24.946 -18.895 30.216 1.00 27.73 C ANISOU 939 CB ILE A 124 4020 3686 2831 -589 -59 795 C ATOM 940 CG1 ILE A 124 -24.413 -19.776 31.350 1.00 33.26 C ANISOU 940 CG1 ILE A 124 4839 4312 3487 -606 -113 889 C ATOM 941 CG2 ILE A 124 -23.835 -18.021 29.661 1.00 26.66 C ANISOU 941 CG2 ILE A 124 3831 3565 2734 -467 -87 725 C ATOM 942 CD1 ILE A 124 -23.317 -20.720 30.918 1.00 35.31 C ANISOU 942 CD1 ILE A 124 5165 4430 3821 -535 -203 898 C ATOM 943 N ILE A 125 -27.285 -17.338 28.693 1.00 23.60 N ANISOU 943 N ILE A 125 3273 3357 2338 -664 79 671 N ATOM 944 CA ILE A 125 -27.727 -16.366 27.696 1.00 24.48 C ANISOU 944 CA ILE A 125 3281 3536 2484 -632 105 592 C ATOM 945 C ILE A 125 -28.558 -15.268 28.352 1.00 24.08 C ANISOU 945 C ILE A 125 3150 3615 2384 -648 176 580 C ATOM 946 O ILE A 125 -28.364 -14.078 28.083 1.00 20.56 O ANISOU 946 O ILE A 125 2643 3230 1939 -578 188 524 O ATOM 947 CB ILE A 125 -28.498 -17.075 26.567 1.00 25.57 C ANISOU 947 CB ILE A 125 3403 3629 2681 -691 92 571 C ATOM 948 CG1 ILE A 125 -27.535 -17.928 25.733 1.00 27.52 C ANISOU 948 CG1 ILE A 125 3726 3750 2979 -644 27 555 C ATOM 949 CG2 ILE A 125 -29.246 -16.057 25.698 1.00 21.65 C ANISOU 949 CG2 ILE A 125 2798 3220 2209 -678 118 505 C ATOM 950 CD1 ILE A 125 -28.214 -18.787 24.681 1.00 29.14 C ANISOU 950 CD1 ILE A 125 3945 3892 3234 -708 3 534 C ATOM 951 N ALA A 126 -29.477 -15.649 29.244 1.00 27.50 N ANISOU 951 N ALA A 126 3587 4091 2772 -742 228 633 N ATOM 952 CA ALA A 126 -30.300 -14.658 29.933 1.00 26.17 C ANISOU 952 CA ALA A 126 3341 4048 2555 -754 308 617 C ATOM 953 C ALA A 126 -29.447 -13.724 30.785 1.00 25.64 C ANISOU 953 C ALA A 126 3301 4018 2421 -674 310 604 C ATOM 954 O ALA A 126 -29.653 -12.504 30.781 1.00 25.00 O ANISOU 954 O ALA A 126 3149 4017 2332 -621 345 546 O ATOM 955 CB ALA A 126 -31.354 -15.361 30.792 1.00 23.01 C ANISOU 955 CB ALA A 126 2946 3683 2112 -876 373 683 C ATOM 956 N ILE A 127 -28.483 -14.278 31.523 1.00 25.14 N ANISOU 956 N ILE A 127 3344 3893 2314 -664 265 656 N ATOM 957 CA ILE A 127 -27.610 -13.456 32.356 1.00 26.05 C ANISOU 957 CA ILE A 127 3493 4039 2366 -594 250 645 C ATOM 958 C ILE A 127 -26.803 -12.492 31.499 1.00 25.14 C ANISOU 958 C ILE A 127 3327 3917 2308 -491 210 571 C ATOM 959 O ILE A 127 -26.653 -11.311 31.838 1.00 25.17 O ANISOU 959 O ILE A 127 3298 3985 2280 -441 228 526 O ATOM 960 CB ILE A 127 -26.696 -14.354 33.212 1.00 30.41 C ANISOU 960 CB ILE A 127 4169 4514 2871 -603 188 722 C ATOM 961 CG1 ILE A 127 -27.528 -15.135 34.232 1.00 31.64 C ANISOU 961 CG1 ILE A 127 4387 4689 2947 -713 239 803 C ATOM 962 CG2 ILE A 127 -25.617 -13.526 33.901 1.00 28.62 C ANISOU 962 CG2 ILE A 127 3973 4305 2594 -524 145 704 C ATOM 963 CD1 ILE A 127 -26.728 -16.132 35.041 1.00 34.88 C ANISOU 963 CD1 ILE A 127 4932 5012 3310 -729 169 892 C ATOM 964 N CYS A 128 -26.272 -12.978 30.372 1.00 21.80 N ANISOU 964 N CYS A 128 2901 3415 1967 -461 157 556 N ATOM 965 CA CYS A 128 -25.465 -12.126 29.508 1.00 23.29 C ANISOU 965 CA CYS A 128 3046 3596 2207 -373 125 493 C ATOM 966 C CYS A 128 -26.287 -10.992 28.901 1.00 21.61 C ANISOU 966 C CYS A 128 2740 3461 2011 -359 174 430 C ATOM 967 O CYS A 128 -25.772 -9.882 28.732 1.00 19.24 O ANISOU 967 O CYS A 128 2408 3186 1716 -294 166 384 O ATOM 968 CB CYS A 128 -24.809 -12.965 28.414 1.00 26.22 C ANISOU 968 CB CYS A 128 3439 3871 2654 -349 74 488 C ATOM 969 SG CYS A 128 -23.512 -14.068 29.019 1.00 30.63 S ANISOU 969 SG CYS A 128 4096 4326 3216 -322 -1 547 S ATOM 970 N TRP A 129 -27.558 -11.241 28.574 1.00 21.94 N ANISOU 970 N TRP A 129 2734 3537 2066 -421 217 430 N ATOM 971 CA TRP A 129 -28.409 -10.153 28.098 1.00 22.43 C ANISOU 971 CA TRP A 129 2702 3675 2146 -403 256 375 C ATOM 972 C TRP A 129 -28.657 -9.119 29.192 1.00 20.83 C ANISOU 972 C TRP A 129 2480 3554 1881 -381 307 358 C ATOM 973 O TRP A 129 -28.658 -7.915 28.921 1.00 20.05 O ANISOU 973 O TRP A 129 2332 3491 1794 -320 313 303 O ATOM 974 CB TRP A 129 -29.732 -10.702 27.565 1.00 22.67 C ANISOU 974 CB TRP A 129 2676 3727 2212 -476 283 381 C ATOM 975 CG TRP A 129 -29.645 -11.082 26.125 1.00 23.44 C ANISOU 975 CG TRP A 129 2765 3765 2375 -470 232 357 C ATOM 976 CD1 TRP A 129 -29.524 -12.340 25.621 1.00 23.78 C ANISOU 976 CD1 TRP A 129 2862 3727 2446 -518 195 384 C ATOM 977 CD2 TRP A 129 -29.646 -10.193 24.998 1.00 22.60 C ANISOU 977 CD2 TRP A 129 2609 3671 2309 -413 209 301 C ATOM 978 NE1 TRP A 129 -29.461 -12.297 24.248 1.00 25.43 N ANISOU 978 NE1 TRP A 129 3057 3903 2703 -494 155 342 N ATOM 979 CE2 TRP A 129 -29.535 -10.992 23.839 1.00 23.77 C ANISOU 979 CE2 TRP A 129 2784 3750 2497 -432 163 295 C ATOM 980 CE3 TRP A 129 -29.743 -8.802 24.856 1.00 18.01 C ANISOU 980 CE3 TRP A 129 1970 3145 1728 -349 222 256 C ATOM 981 CZ2 TRP A 129 -29.506 -10.449 22.558 1.00 25.06 C ANISOU 981 CZ2 TRP A 129 2923 3907 2691 -392 132 249 C ATOM 982 CZ3 TRP A 129 -29.711 -8.260 23.586 1.00 20.67 C ANISOU 982 CZ3 TRP A 129 2281 3468 2103 -310 186 218 C ATOM 983 CH2 TRP A 129 -29.597 -9.084 22.449 1.00 25.95 C ANISOU 983 CH2 TRP A 129 2982 4077 2802 -334 143 216 C ATOM 984 N VAL A 130 -28.865 -9.561 30.432 1.00 22.30 N ANISOU 984 N VAL A 130 2712 3765 1995 -430 343 403 N ATOM 985 CA VAL A 130 -29.050 -8.599 31.516 1.00 22.98 C ANISOU 985 CA VAL A 130 2795 3928 2007 -408 395 379 C ATOM 986 C VAL A 130 -27.788 -7.761 31.692 1.00 22.99 C ANISOU 986 C VAL A 130 2838 3904 1994 -327 340 348 C ATOM 987 O VAL A 130 -27.850 -6.528 31.769 1.00 21.50 O ANISOU 987 O VAL A 130 2613 3757 1799 -273 358 289 O ATOM 988 CB VAL A 130 -29.459 -9.314 32.817 1.00 26.38 C ANISOU 988 CB VAL A 130 3285 4391 2348 -484 446 440 C ATOM 989 CG1 VAL A 130 -29.488 -8.329 33.985 1.00 28.94 C ANISOU 989 CG1 VAL A 130 3628 4789 2577 -454 497 408 C ATOM 990 CG2 VAL A 130 -30.828 -9.957 32.654 1.00 24.91 C ANISOU 990 CG2 VAL A 130 3035 4246 2183 -571 514 464 C ATOM 991 N LEU A 131 -26.620 -8.416 31.726 1.00 21.04 N ANISOU 991 N LEU A 131 2663 3582 1750 -317 268 386 N ATOM 992 CA LEU A 131 -25.363 -7.684 31.863 1.00 22.14 C ANISOU 992 CA LEU A 131 2829 3696 1888 -249 209 360 C ATOM 993 C LEU A 131 -25.100 -6.775 30.669 1.00 21.63 C ANISOU 993 C LEU A 131 2697 3620 1901 -190 192 300 C ATOM 994 O LEU A 131 -24.420 -5.752 30.807 1.00 19.58 O ANISOU 994 O LEU A 131 2436 3365 1639 -140 168 262 O ATOM 995 CB LEU A 131 -24.200 -8.657 32.038 1.00 23.47 C ANISOU 995 CB LEU A 131 3069 3786 2064 -246 133 413 C ATOM 996 CG LEU A 131 -24.251 -9.544 33.281 1.00 29.87 C ANISOU 996 CG LEU A 131 3969 4593 2789 -300 128 484 C ATOM 997 CD1 LEU A 131 -23.118 -10.560 33.236 1.00 31.34 C ANISOU 997 CD1 LEU A 131 4216 4685 3007 -284 40 536 C ATOM 998 CD2 LEU A 131 -24.181 -8.701 34.545 1.00 30.44 C ANISOU 998 CD2 LEU A 131 4080 4727 2758 -293 142 470 C ATOM 999 N SER A 132 -25.604 -7.142 29.490 1.00 18.93 N ANISOU 999 N SER A 132 2309 3260 1626 -201 200 294 N ATOM 1000 CA SER A 132 -25.439 -6.290 28.319 1.00 17.70 C ANISOU 1000 CA SER A 132 2100 3095 1531 -153 186 244 C ATOM 1001 C SER A 132 -26.228 -4.994 28.463 1.00 19.37 C ANISOU 1001 C SER A 132 2259 3371 1731 -127 226 194 C ATOM 1002 O SER A 132 -25.738 -3.921 28.095 1.00 17.77 O ANISOU 1002 O SER A 132 2042 3161 1550 -75 206 155 O ATOM 1003 CB SER A 132 -25.859 -7.047 27.063 1.00 16.65 C ANISOU 1003 CB SER A 132 1943 2928 1456 -176 179 249 C ATOM 1004 OG SER A 132 -24.992 -8.144 26.847 1.00 22.78 O ANISOU 1004 OG SER A 132 2771 3632 2251 -183 139 283 O ATOM 1005 N PHE A 133 -27.449 -5.074 29.006 1.00 18.38 N ANISOU 1005 N PHE A 133 2102 3306 1576 -162 286 195 N ATOM 1006 CA PHE A 133 -28.209 -3.860 29.285 1.00 21.19 C ANISOU 1006 CA PHE A 133 2407 3724 1922 -126 330 143 C ATOM 1007 C PHE A 133 -27.535 -3.021 30.363 1.00 22.68 C ANISOU 1007 C PHE A 133 2646 3923 2047 -90 328 117 C ATOM 1008 O PHE A 133 -27.452 -1.795 30.236 1.00 21.67 O ANISOU 1008 O PHE A 133 2502 3800 1934 -34 323 64 O ATOM 1009 CB PHE A 133 -29.641 -4.208 29.693 1.00 20.75 C ANISOU 1009 CB PHE A 133 2295 3738 1851 -173 404 149 C ATOM 1010 CG PHE A 133 -30.576 -4.396 28.529 1.00 22.87 C ANISOU 1010 CG PHE A 133 2480 4013 2196 -187 401 143 C ATOM 1011 CD1 PHE A 133 -31.288 -3.321 28.012 1.00 22.68 C ANISOU 1011 CD1 PHE A 133 2379 4023 2216 -134 410 91 C ATOM 1012 CD2 PHE A 133 -30.751 -5.649 27.956 1.00 23.40 C ANISOU 1012 CD2 PHE A 133 2552 4048 2290 -252 381 188 C ATOM 1013 CE1 PHE A 133 -32.155 -3.493 26.941 1.00 25.28 C ANISOU 1013 CE1 PHE A 133 2632 4360 2614 -147 393 88 C ATOM 1014 CE2 PHE A 133 -31.614 -5.830 26.885 1.00 22.00 C ANISOU 1014 CE2 PHE A 133 2304 3877 2179 -271 367 179 C ATOM 1015 CZ PHE A 133 -32.316 -4.749 26.375 1.00 24.19 C ANISOU 1015 CZ PHE A 133 2499 4194 2497 -219 370 131 C ATOM 1016 N ALA A 134 -27.030 -3.664 31.421 1.00 21.33 N ANISOU 1016 N ALA A 134 2548 3750 1806 -123 324 156 N ATOM 1017 CA ALA A 134 -26.366 -2.921 32.489 1.00 21.14 C ANISOU 1017 CA ALA A 134 2583 3736 1712 -95 311 131 C ATOM 1018 C ALA A 134 -25.119 -2.206 31.973 1.00 21.48 C ANISOU 1018 C ALA A 134 2639 3721 1801 -46 234 107 C ATOM 1019 O ALA A 134 -24.880 -1.041 32.311 1.00 22.33 O ANISOU 1019 O ALA A 134 2755 3835 1893 -6 226 55 O ATOM 1020 CB ALA A 134 -26.011 -3.861 33.642 1.00 20.75 C ANISOU 1020 CB ALA A 134 2619 3689 1575 -144 304 188 C ATOM 1021 N ILE A 135 -24.324 -2.880 31.140 1.00 20.41 N ANISOU 1021 N ILE A 135 2501 3527 1725 -49 181 142 N ATOM 1022 CA ILE A 135 -23.106 -2.268 30.614 1.00 22.11 C ANISOU 1022 CA ILE A 135 2716 3694 1990 -11 118 124 C ATOM 1023 C ILE A 135 -23.445 -1.189 29.590 1.00 19.13 C ANISOU 1023 C ILE A 135 2285 3314 1671 25 131 76 C ATOM 1024 O ILE A 135 -22.920 -0.070 29.644 1.00 18.69 O ANISOU 1024 O ILE A 135 2233 3244 1623 56 106 38 O ATOM 1025 CB ILE A 135 -22.180 -3.344 30.014 1.00 23.96 C ANISOU 1025 CB ILE A 135 2958 3871 2273 -20 71 170 C ATOM 1026 CG1 ILE A 135 -21.553 -4.197 31.119 1.00 22.36 C ANISOU 1026 CG1 ILE A 135 2821 3657 2018 -40 32 217 C ATOM 1027 CG2 ILE A 135 -21.093 -2.702 29.161 1.00 24.05 C ANISOU 1027 CG2 ILE A 135 2944 3843 2353 16 29 148 C ATOM 1028 CD1 ILE A 135 -20.727 -5.368 30.596 1.00 26.14 C ANISOU 1028 CD1 ILE A 135 3307 4073 2550 -40 -13 262 C ATOM 1029 N GLY A 136 -24.330 -1.508 28.642 1.00 18.21 N ANISOU 1029 N GLY A 136 2120 3204 1594 16 161 80 N ATOM 1030 CA GLY A 136 -24.616 -0.576 27.563 1.00 14.36 C ANISOU 1030 CA GLY A 136 1590 2707 1160 50 159 46 C ATOM 1031 C GLY A 136 -25.412 0.640 27.992 1.00 19.10 C ANISOU 1031 C GLY A 136 2171 3341 1746 85 188 -5 C ATOM 1032 O GLY A 136 -25.305 1.703 27.374 1.00 17.24 O ANISOU 1032 O GLY A 136 1923 3080 1547 123 168 -35 O ATOM 1033 N LEU A 137 -26.223 0.511 29.041 1.00 15.36 N ANISOU 1033 N LEU A 137 1697 2923 1217 75 238 -15 N ATOM 1034 CA LEU A 137 -27.010 1.632 29.537 1.00 18.73 C ANISOU 1034 CA LEU A 137 2103 3384 1629 118 275 -73 C ATOM 1035 C LEU A 137 -26.405 2.257 30.786 1.00 18.03 C ANISOU 1035 C LEU A 137 2082 3298 1471 132 271 -105 C ATOM 1036 O LEU A 137 -27.076 3.040 31.467 1.00 21.41 O ANISOU 1036 O LEU A 137 2508 3760 1866 165 315 -159 O ATOM 1037 CB LEU A 137 -28.449 1.192 29.806 1.00 17.82 C ANISOU 1037 CB LEU A 137 1929 3339 1503 101 349 -75 C ATOM 1038 CG LEU A 137 -29.178 0.571 28.609 1.00 18.93 C ANISOU 1038 CG LEU A 137 2000 3481 1711 81 344 -47 C ATOM 1039 CD1 LEU A 137 -30.631 0.285 28.958 1.00 18.81 C ANISOU 1039 CD1 LEU A 137 1909 3542 1695 63 417 -55 C ATOM 1040 CD2 LEU A 137 -29.078 1.465 27.382 1.00 19.18 C ANISOU 1040 CD2 LEU A 137 2007 3469 1812 130 294 -69 C ATOM 1041 N THR A 138 -25.161 1.913 31.110 1.00 18.46 N ANISOU 1041 N THR A 138 2194 3317 1504 109 217 -77 N ATOM 1042 CA THR A 138 -24.473 2.565 32.222 1.00 17.52 C ANISOU 1042 CA THR A 138 2143 3192 1321 120 191 -110 C ATOM 1043 C THR A 138 -24.512 4.089 32.148 1.00 16.72 C ANISOU 1043 C THR A 138 2045 3066 1242 172 181 -180 C ATOM 1044 O THR A 138 -24.700 4.719 33.203 1.00 21.56 O ANISOU 1044 O THR A 138 2705 3701 1787 190 200 -232 O ATOM 1045 CB THR A 138 -23.026 2.044 32.309 1.00 20.80 C ANISOU 1045 CB THR A 138 2599 3564 1740 93 113 -67 C ATOM 1046 OG1 THR A 138 -23.020 0.764 32.954 1.00 22.31 O ANISOU 1046 OG1 THR A 138 2821 3778 1876 51 120 -12 O ATOM 1047 CG2 THR A 138 -22.134 2.999 33.100 1.00 16.65 C ANISOU 1047 CG2 THR A 138 2131 3015 1180 106 58 -108 C ATOM 1048 N PRO A 139 -24.366 4.740 30.983 1.00 18.51 N ANISOU 1048 N PRO A 139 2235 3246 1554 197 152 -188 N ATOM 1049 CA PRO A 139 -24.539 6.203 30.954 1.00 16.52 C ANISOU 1049 CA PRO A 139 1994 2961 1323 248 143 -253 C ATOM 1050 C PRO A 139 -25.876 6.676 31.502 1.00 19.74 C ANISOU 1050 C PRO A 139 2382 3416 1702 294 214 -309 C ATOM 1051 O PRO A 139 -25.938 7.774 32.070 1.00 17.90 O ANISOU 1051 O PRO A 139 2187 3163 1450 336 213 -377 O ATOM 1052 CB PRO A 139 -24.385 6.542 29.466 1.00 18.34 C ANISOU 1052 CB PRO A 139 2184 3140 1644 259 111 -231 C ATOM 1053 CG PRO A 139 -23.458 5.482 28.960 1.00 17.16 C ANISOU 1053 CG PRO A 139 2029 2981 1512 209 82 -167 C ATOM 1054 CD PRO A 139 -23.867 4.234 29.688 1.00 16.57 C ANISOU 1054 CD PRO A 139 1952 2963 1379 179 120 -138 C ATOM 1055 N AMET A 140 -26.943 5.884 31.362 0.48 19.12 N ANISOU 1055 N AMET A 140 2243 3400 1624 286 276 -288 N ATOM 1056 N BMET A 140 -26.944 5.882 31.353 0.52 19.07 N ANISOU 1056 N BMET A 140 2236 3393 1618 286 276 -287 N ATOM 1057 CA AMET A 140 -28.245 6.279 31.892 0.48 20.57 C ANISOU 1057 CA AMET A 140 2387 3640 1788 329 355 -342 C ATOM 1058 CA BMET A 140 -28.248 6.254 31.896 0.52 20.57 C ANISOU 1058 CA BMET A 140 2386 3641 1787 328 356 -341 C ATOM 1059 C AMET A 140 -28.296 6.260 33.414 0.48 22.88 C ANISOU 1059 C AMET A 140 2741 3981 1970 321 407 -378 C ATOM 1060 C BMET A 140 -28.235 6.355 33.414 0.52 22.90 C ANISOU 1060 C BMET A 140 2748 3978 1973 324 402 -382 C ATOM 1061 O AMET A 140 -29.267 6.765 33.987 0.48 23.82 O ANISOU 1061 O AMET A 140 2838 4147 2065 365 481 -439 O ATOM 1062 O BMET A 140 -29.098 7.030 33.987 0.52 24.05 O ANISOU 1062 O BMET A 140 2881 4160 2097 375 466 -451 O ATOM 1063 CB AMET A 140 -29.347 5.375 31.330 0.48 21.43 C ANISOU 1063 CB AMET A 140 2403 3807 1934 308 405 -304 C ATOM 1064 CB BMET A 140 -29.317 5.242 31.472 0.52 21.12 C ANISOU 1064 CB BMET A 140 2369 3774 1882 300 411 -300 C ATOM 1065 CG AMET A 140 -29.415 5.360 29.804 0.48 22.16 C ANISOU 1065 CG AMET A 140 2441 3857 2122 315 353 -271 C ATOM 1066 CG BMET A 140 -29.405 5.003 29.970 0.52 22.44 C ANISOU 1066 CG BMET A 140 2479 3907 2142 296 363 -258 C ATOM 1067 SD AMET A 140 -30.898 4.552 29.174 0.48 23.82 S ANISOU 1067 SD AMET A 140 2534 4134 2382 300 400 -246 S ATOM 1068 SD BMET A 140 -30.209 6.352 29.088 0.52 25.20 S ANISOU 1068 SD BMET A 140 2770 4226 2580 385 344 -310 S ATOM 1069 CE AMET A 140 -32.180 5.645 29.786 0.48 24.48 C ANISOU 1069 CE AMET A 140 2554 4268 2480 384 469 -330 C ATOM 1070 CE BMET A 140 -31.857 6.299 29.795 0.52 24.61 C ANISOU 1070 CE BMET A 140 2601 4249 2500 417 446 -355 C ATOM 1071 N LEU A 141 -27.295 5.688 34.080 1.00 23.99 N ANISOU 1071 N LEU A 141 2958 4115 2042 269 370 -344 N ATOM 1072 CA LEU A 141 -27.218 5.730 35.533 1.00 26.06 C ANISOU 1072 CA LEU A 141 3301 4416 2183 258 403 -377 C ATOM 1073 C LEU A 141 -26.511 6.977 36.043 1.00 29.19 C ANISOU 1073 C LEU A 141 3778 4760 2555 296 351 -450 C ATOM 1074 O LEU A 141 -26.398 7.152 37.261 1.00 28.45 O ANISOU 1074 O LEU A 141 3765 4693 2351 291 368 -489 O ATOM 1075 CB LEU A 141 -26.515 4.481 36.068 1.00 27.34 C ANISOU 1075 CB LEU A 141 3516 4594 2277 183 376 -301 C ATOM 1076 CG LEU A 141 -27.059 3.141 35.564 1.00 29.81 C ANISOU 1076 CG LEU A 141 3769 4942 2617 134 414 -222 C ATOM 1077 CD1 LEU A 141 -26.320 1.989 36.221 1.00 30.24 C ANISOU 1077 CD1 LEU A 141 3893 4996 2599 68 379 -150 C ATOM 1078 CD2 LEU A 141 -28.554 3.026 35.802 1.00 28.77 C ANISOU 1078 CD2 LEU A 141 3572 4889 2468 139 530 -244 C ATOM 1079 N GLY A 142 -26.035 7.844 35.150 1.00 19.80 N ANISOU 1079 N GLY A 142 2573 3493 1458 328 285 -467 N ATOM 1080 CA GLY A 142 -25.480 9.112 35.576 1.00 22.95 C ANISOU 1080 CA GLY A 142 3044 3831 1844 361 235 -540 C ATOM 1081 C GLY A 142 -24.164 9.472 34.922 1.00 23.02 C ANISOU 1081 C GLY A 142 3072 3754 1918 334 127 -512 C ATOM 1082 O GLY A 142 -23.717 10.619 35.015 1.00 22.13 O ANISOU 1082 O GLY A 142 3009 3575 1823 357 77 -568 O ATOM 1083 N TRP A 143 -23.519 8.506 34.271 1.00 21.66 N ANISOU 1083 N TRP A 143 2863 3581 1785 284 92 -428 N ATOM 1084 CA TRP A 143 -22.268 8.773 33.563 1.00 18.83 C ANISOU 1084 CA TRP A 143 2506 3153 1497 256 3 -397 C ATOM 1085 C TRP A 143 -22.598 9.269 32.156 1.00 18.62 C ANISOU 1085 C TRP A 143 2419 3083 1574 283 7 -386 C ATOM 1086 O TRP A 143 -22.448 8.570 31.152 1.00 18.33 O ANISOU 1086 O TRP A 143 2328 3047 1591 262 5 -323 O ATOM 1087 CB TRP A 143 -21.391 7.529 33.534 1.00 19.14 C ANISOU 1087 CB TRP A 143 2533 3209 1531 200 -32 -320 C ATOM 1088 CG TRP A 143 -19.959 7.781 33.147 1.00 22.14 C ANISOU 1088 CG TRP A 143 2914 3530 1969 168 -121 -297 C ATOM 1089 CD1 TRP A 143 -19.392 8.976 32.783 1.00 19.22 C ANISOU 1089 CD1 TRP A 143 2556 3093 1654 171 -170 -332 C ATOM 1090 CD2 TRP A 143 -18.908 6.809 33.101 1.00 18.86 C ANISOU 1090 CD2 TRP A 143 2481 3116 1569 127 -171 -235 C ATOM 1091 NE1 TRP A 143 -18.053 8.797 32.504 1.00 18.08 N ANISOU 1091 NE1 TRP A 143 2393 2917 1559 127 -240 -293 N ATOM 1092 CE2 TRP A 143 -17.733 7.478 32.697 1.00 20.94 C ANISOU 1092 CE2 TRP A 143 2734 3323 1901 106 -242 -236 C ATOM 1093 CE3 TRP A 143 -18.851 5.435 33.354 1.00 17.98 C ANISOU 1093 CE3 TRP A 143 2361 3045 1426 107 -163 -177 C ATOM 1094 CZ2 TRP A 143 -16.514 6.819 32.545 1.00 24.42 C ANISOU 1094 CZ2 TRP A 143 3141 3754 2382 72 -300 -187 C ATOM 1095 CZ3 TRP A 143 -17.644 4.781 33.206 1.00 20.69 C ANISOU 1095 CZ3 TRP A 143 2683 3369 1809 80 -227 -128 C ATOM 1096 CH2 TRP A 143 -16.489 5.473 32.799 1.00 22.54 C ANISOU 1096 CH2 TRP A 143 2894 3555 2117 66 -293 -135 C ATOM 1097 N ASN A 144 -23.075 10.509 32.103 1.00 19.79 N ANISOU 1097 N ASN A 144 2587 3189 1746 334 9 -449 N ATOM 1098 CA ASN A 144 -23.513 11.103 30.851 1.00 20.42 C ANISOU 1098 CA ASN A 144 2622 3222 1913 368 6 -440 C ATOM 1099 C ASN A 144 -23.198 12.594 30.877 1.00 21.83 C ANISOU 1099 C ASN A 144 2859 3310 2124 396 -43 -497 C ATOM 1100 O ASN A 144 -22.740 13.139 31.887 1.00 22.93 O ANISOU 1100 O ASN A 144 3068 3428 2215 392 -69 -552 O ATOM 1101 CB ASN A 144 -25.005 10.834 30.604 1.00 19.88 C ANISOU 1101 CB ASN A 144 2492 3209 1853 419 80 -450 C ATOM 1102 CG ASN A 144 -25.889 11.382 31.704 1.00 19.48 C ANISOU 1102 CG ASN A 144 2463 3190 1748 476 134 -534 C ATOM 1103 OD1 ASN A 144 -25.943 12.585 31.922 1.00 26.66 O ANISOU 1103 OD1 ASN A 144 3417 4040 2672 525 115 -600 O ATOM 1104 ND2 ASN A 144 -26.595 10.499 32.396 1.00 21.72 N ANISOU 1104 ND2 ASN A 144 2719 3565 1969 468 208 -532 N ATOM 1105 N ASN A 145 -23.451 13.261 29.752 1.00 20.28 N ANISOU 1105 N ASN A 145 2642 3055 2007 422 -61 -483 N ATOM 1106 CA ASN A 145 -23.234 14.696 29.630 1.00 21.26 C ANISOU 1106 CA ASN A 145 2826 3079 2173 449 -111 -528 C ATOM 1107 C ASN A 145 -24.532 15.483 29.692 1.00 25.50 C ANISOU 1107 C ASN A 145 3360 3600 2729 546 -78 -592 C ATOM 1108 O ASN A 145 -24.557 16.658 29.312 1.00 28.56 O ANISOU 1108 O ASN A 145 3790 3892 3170 582 -121 -619 O ATOM 1109 CB ASN A 145 -22.496 15.016 28.332 1.00 25.30 C ANISOU 1109 CB ASN A 145 3333 3521 2759 408 -162 -463 C ATOM 1110 CG ASN A 145 -21.099 14.443 28.304 1.00 29.69 C ANISOU 1110 CG ASN A 145 3887 4082 3312 319 -195 -412 C ATOM 1111 OD1 ASN A 145 -20.429 14.362 29.332 1.00 32.95 O ANISOU 1111 OD1 ASN A 145 4333 4506 3682 289 -218 -441 O ATOM 1112 ND2 ASN A 145 -20.648 14.042 27.123 1.00 30.83 N ANISOU 1112 ND2 ASN A 145 3992 4221 3501 279 -198 -339 N ATOM 1113 N CYS A 146 -25.612 14.859 30.160 1.00 25.21 N ANISOU 1113 N CYS A 146 3271 3653 2655 588 -4 -615 N ATOM 1114 CA CYS A 146 -26.879 15.567 30.252 1.00 26.23 C ANISOU 1114 CA CYS A 146 3377 3777 2811 688 34 -680 C ATOM 1115 C CYS A 146 -26.839 16.681 31.286 1.00 29.67 C ANISOU 1115 C CYS A 146 3899 4157 3216 738 29 -783 C ATOM 1116 O CYS A 146 -27.631 17.622 31.190 1.00 31.25 O ANISOU 1116 O CYS A 146 4101 4308 3463 829 34 -842 O ATOM 1117 CB CYS A 146 -28.004 14.575 30.549 1.00 30.48 C ANISOU 1117 CB CYS A 146 3828 4436 3319 709 124 -679 C ATOM 1118 SG CYS A 146 -28.380 13.515 29.102 1.00 32.78 S ANISOU 1118 SG CYS A 146 4016 4768 3669 674 119 -574 S ATOM 1119 N GLY A 147 -25.920 16.613 32.251 1.00 31.49 N ANISOU 1119 N GLY A 147 4205 4387 3371 683 11 -807 N ATOM 1120 CA GLY A 147 -25.755 17.698 33.202 1.00 33.28 C ANISOU 1120 CA GLY A 147 4532 4550 3563 720 -8 -909 C ATOM 1121 C GLY A 147 -25.105 18.938 32.622 1.00 34.29 C ANISOU 1121 C GLY A 147 4727 4535 3767 719 -101 -919 C ATOM 1122 O GLY A 147 -25.224 20.017 33.210 1.00 40.94 O ANISOU 1122 O GLY A 147 5650 5301 4605 772 -119 -1012 O ATOM 1123 N GLN A 148 -24.428 18.816 31.482 1.00 33.40 N ANISOU 1123 N GLN A 148 4588 4381 3723 659 -157 -826 N ATOM 1124 CA GLN A 148 -23.752 19.938 30.830 1.00 36.46 C ANISOU 1124 CA GLN A 148 5038 4631 4183 640 -242 -817 C ATOM 1125 C GLN A 148 -24.202 20.021 29.375 1.00 32.95 C ANISOU 1125 C GLN A 148 4538 4155 3824 662 -252 -742 C ATOM 1126 O GLN A 148 -23.417 19.774 28.452 1.00 34.04 O ANISOU 1126 O GLN A 148 4662 4274 3996 586 -289 -654 O ATOM 1127 CB GLN A 148 -22.232 19.789 30.917 1.00 46.34 C ANISOU 1127 CB GLN A 148 6324 5857 5425 524 -307 -774 C ATOM 1128 CG GLN A 148 -21.691 19.532 32.319 1.00 57.57 C ANISOU 1128 CG GLN A 148 7798 7323 6755 490 -313 -832 C ATOM 1129 CD GLN A 148 -21.698 18.059 32.693 1.00 65.36 C ANISOU 1129 CD GLN A 148 8719 8443 7672 458 -260 -787 C ATOM 1130 OE1 GLN A 148 -21.521 17.186 31.839 1.00 65.22 O ANISOU 1130 OE1 GLN A 148 8624 8471 7687 422 -247 -698 O ATOM 1131 NE2 GLN A 148 -21.903 17.777 33.975 1.00 69.58 N ANISOU 1131 NE2 GLN A 148 9295 9038 8105 472 -231 -850 N ATOM 1132 N PRO A 149 -25.464 20.367 29.133 1.00 33.75 N ANISOU 1132 N PRO A 149 4608 4255 3961 766 -222 -775 N ATOM 1133 CA PRO A 149 -25.956 20.400 27.753 1.00 31.97 C ANISOU 1133 CA PRO A 149 4333 4005 3809 789 -243 -701 C ATOM 1134 C PRO A 149 -25.305 21.515 26.947 1.00 35.53 C ANISOU 1134 C PRO A 149 4865 4310 4324 764 -330 -667 C ATOM 1135 O PRO A 149 -24.901 22.552 27.480 1.00 34.10 O ANISOU 1135 O PRO A 149 4776 4026 4155 771 -373 -726 O ATOM 1136 CB PRO A 149 -27.460 20.639 27.920 1.00 29.33 C ANISOU 1136 CB PRO A 149 3946 3698 3501 917 -199 -762 C ATOM 1137 CG PRO A 149 -27.584 21.358 29.216 1.00 31.49 C ANISOU 1137 CG PRO A 149 4284 3941 3738 972 -177 -880 C ATOM 1138 CD PRO A 149 -26.483 20.824 30.097 1.00 31.49 C ANISOU 1138 CD PRO A 149 4331 3982 3651 873 -171 -885 C ATOM 1139 N LYS A 150 -25.200 21.282 25.638 1.00 35.38 N ANISOU 1139 N LYS A 150 4818 4280 4343 729 -355 -569 N ATOM 1140 CA LYS A 150 -24.732 22.305 24.705 1.00 37.09 C ANISOU 1140 CA LYS A 150 5111 4362 4620 705 -431 -520 C ATOM 1141 C LYS A 150 -25.898 23.240 24.418 1.00 37.00 C ANISOU 1141 C LYS A 150 5118 4273 4668 829 -462 -555 C ATOM 1142 O LYS A 150 -26.657 23.057 23.464 1.00 34.15 O ANISOU 1142 O LYS A 150 4711 3927 4338 872 -473 -503 O ATOM 1143 CB LYS A 150 -24.188 21.674 23.432 1.00 34.71 C ANISOU 1143 CB LYS A 150 4782 4087 4321 620 -438 -404 C ATOM 1144 CG LYS A 150 -22.915 20.883 23.647 1.00 38.02 C ANISOU 1144 CG LYS A 150 5184 4564 4700 503 -415 -370 C ATOM 1145 CD LYS A 150 -22.333 20.418 22.337 1.00 41.66 C ANISOU 1145 CD LYS A 150 5627 5034 5166 425 -416 -264 C ATOM 1146 CE LYS A 150 -21.052 19.635 22.567 1.00 46.62 C ANISOU 1146 CE LYS A 150 6226 5720 5767 320 -390 -236 C ATOM 1147 NZ LYS A 150 -20.035 20.466 23.262 1.00 50.94 N ANISOU 1147 NZ LYS A 150 6833 6189 6332 263 -432 -269 N ATOM 1148 N GLU A 151 -26.034 24.266 25.259 1.00 40.70 N ANISOU 1148 N GLU A 151 5658 4651 5154 891 -483 -649 N ATOM 1149 CA GLU A 151 -27.199 25.141 25.183 1.00 46.32 C ANISOU 1149 CA GLU A 151 6380 5291 5928 1030 -506 -703 C ATOM 1150 C GLU A 151 -27.196 25.973 23.907 1.00 44.07 C ANISOU 1150 C GLU A 151 6155 4876 5714 1036 -596 -622 C ATOM 1151 O GLU A 151 -28.260 26.265 23.350 1.00 45.32 O ANISOU 1151 O GLU A 151 6281 5011 5926 1141 -621 -616 O ATOM 1152 CB GLU A 151 -27.251 26.041 26.416 1.00 54.69 C ANISOU 1152 CB GLU A 151 7516 6278 6984 1094 -505 -831 C ATOM 1153 CG GLU A 151 -28.623 26.136 27.059 1.00 65.48 C ANISOU 1153 CG GLU A 151 8823 7692 8365 1245 -448 -932 C ATOM 1154 CD GLU A 151 -29.126 24.798 27.566 1.00 69.41 C ANISOU 1154 CD GLU A 151 9197 8379 8797 1240 -345 -941 C ATOM 1155 OE1 GLU A 151 -29.772 24.065 26.786 1.00 71.22 O ANISOU 1155 OE1 GLU A 151 9323 8690 9049 1252 -328 -873 O ATOM 1156 OE2 GLU A 151 -28.869 24.475 28.744 1.00 71.55 O ANISOU 1156 OE2 GLU A 151 9482 8712 8990 1219 -285 -1012 O ATOM 1157 N GLY A 152 -26.015 26.363 23.426 1.00 41.54 N ANISOU 1157 N GLY A 152 5920 4469 5395 921 -646 -556 N ATOM 1158 CA GLY A 152 -25.955 27.126 22.189 1.00 43.40 C ANISOU 1158 CA GLY A 152 6225 4581 5685 910 -726 -467 C ATOM 1159 C GLY A 152 -26.443 26.332 20.994 1.00 42.40 C ANISOU 1159 C GLY A 152 6025 4536 5550 906 -721 -368 C ATOM 1160 O GLY A 152 -27.173 26.851 20.144 1.00 42.59 O ANISOU 1160 O GLY A 152 6070 4492 5621 976 -782 -327 O ATOM 1161 N LYS A 153 -26.044 25.061 20.913 1.00 38.83 N ANISOU 1161 N LYS A 153 5491 4226 5037 826 -656 -331 N ATOM 1162 CA LYS A 153 -26.541 24.194 19.852 1.00 36.35 C ANISOU 1162 CA LYS A 153 5108 3999 4706 822 -647 -251 C ATOM 1163 C LYS A 153 -28.038 23.952 20.000 1.00 33.81 C ANISOU 1163 C LYS A 153 4696 3739 4413 955 -639 -300 C ATOM 1164 O LYS A 153 -28.773 23.935 19.006 1.00 31.27 O ANISOU 1164 O LYS A 153 4354 3412 4115 999 -686 -243 O ATOM 1165 CB LYS A 153 -25.774 22.872 19.864 1.00 35.74 C ANISOU 1165 CB LYS A 153 4967 4051 4561 714 -577 -216 C ATOM 1166 CG LYS A 153 -26.077 21.959 18.703 1.00 35.57 C ANISOU 1166 CG LYS A 153 4894 4108 4513 688 -569 -133 C ATOM 1167 CD LYS A 153 -25.269 20.669 18.798 1.00 37.88 C ANISOU 1167 CD LYS A 153 5131 4517 4746 589 -498 -109 C ATOM 1168 CE LYS A 153 -23.778 20.942 18.727 1.00 39.30 C ANISOU 1168 CE LYS A 153 5373 4646 4915 475 -494 -73 C ATOM 1169 NZ LYS A 153 -22.987 19.681 18.663 1.00 40.08 N ANISOU 1169 NZ LYS A 153 5412 4852 4966 389 -431 -44 N ATOM 1170 N ALA A 154 -28.507 23.773 21.236 1.00 33.61 N ANISOU 1170 N ALA A 154 4615 3773 4383 1019 -581 -404 N ATOM 1171 CA ALA A 154 -29.928 23.529 21.463 1.00 35.34 C ANISOU 1171 CA ALA A 154 4731 4062 4634 1142 -558 -456 C ATOM 1172 C ALA A 154 -30.766 24.751 21.101 1.00 35.56 C ANISOU 1172 C ALA A 154 4796 3966 4750 1269 -638 -476 C ATOM 1173 O ALA A 154 -31.825 24.620 20.476 1.00 36.34 O ANISOU 1173 O ALA A 154 4820 4094 4893 1348 -669 -454 O ATOM 1174 CB ALA A 154 -30.161 23.123 22.918 1.00 33.36 C ANISOU 1174 CB ALA A 154 4425 3902 4350 1173 -466 -563 C ATOM 1175 N HIS A 155 -30.311 25.948 21.480 1.00 36.95 N ANISOU 1175 N HIS A 155 5088 3997 4956 1290 -681 -517 N ATOM 1176 CA HIS A 155 -31.052 27.157 21.129 1.00 39.47 C ANISOU 1176 CA HIS A 155 5456 4177 5364 1416 -766 -535 C ATOM 1177 C HIS A 155 -31.051 27.391 19.624 1.00 38.71 C ANISOU 1177 C HIS A 155 5407 4011 5292 1389 -864 -407 C ATOM 1178 O HIS A 155 -32.079 27.767 19.050 1.00 43.31 O ANISOU 1178 O HIS A 155 5959 4557 5941 1501 -929 -394 O ATOM 1179 CB HIS A 155 -30.475 28.366 21.865 1.00 43.61 C ANISOU 1179 CB HIS A 155 6111 4548 5912 1431 -795 -607 C ATOM 1180 CG HIS A 155 -30.762 28.370 23.334 1.00 51.93 C ANISOU 1180 CG HIS A 155 7134 5651 6948 1498 -713 -749 C ATOM 1181 ND1 HIS A 155 -32.042 28.307 23.840 1.00 56.47 N ANISOU 1181 ND1 HIS A 155 7605 6289 7561 1645 -667 -836 N ATOM 1182 CD2 HIS A 155 -29.937 28.437 24.406 1.00 54.41 C ANISOU 1182 CD2 HIS A 155 7506 5961 7205 1436 -670 -820 C ATOM 1183 CE1 HIS A 155 -31.993 28.326 25.160 1.00 57.48 C ANISOU 1183 CE1 HIS A 155 7739 6454 7648 1669 -587 -955 C ATOM 1184 NE2 HIS A 155 -30.727 28.403 25.529 1.00 55.47 N ANISOU 1184 NE2 HIS A 155 7586 6157 7331 1544 -594 -947 N ATOM 1185 N SER A 156 -29.913 27.163 18.962 1.00 37.20 N ANISOU 1185 N SER A 156 5287 3803 5046 1242 -875 -312 N ATOM 1186 CA SER A 156 -29.840 27.389 17.522 1.00 41.22 C ANISOU 1186 CA SER A 156 5858 4247 5558 1204 -959 -187 C ATOM 1187 C SER A 156 -30.771 26.472 16.739 1.00 43.25 C ANISOU 1187 C SER A 156 6007 4622 5805 1239 -967 -140 C ATOM 1188 O SER A 156 -31.129 26.796 15.602 1.00 45.87 O ANISOU 1188 O SER A 156 6382 4894 6152 1257 -1057 -54 O ATOM 1189 CB SER A 156 -28.403 27.211 17.027 1.00 41.70 C ANISOU 1189 CB SER A 156 6001 4290 5553 1031 -944 -101 C ATOM 1190 OG SER A 156 -27.965 25.876 17.203 1.00 45.34 O ANISOU 1190 OG SER A 156 6371 4912 5944 945 -852 -96 O ATOM 1191 N GLN A 157 -31.170 25.337 17.309 1.00 45.23 N ANISOU 1191 N GLN A 157 6123 5034 6026 1243 -880 -189 N ATOM 1192 CA GLN A 157 -32.092 24.426 16.648 1.00 46.70 C ANISOU 1192 CA GLN A 157 6199 5335 6209 1270 -888 -154 C ATOM 1193 C GLN A 157 -33.512 24.541 17.185 1.00 45.77 C ANISOU 1193 C GLN A 157 5962 5257 6170 1424 -890 -237 C ATOM 1194 O GLN A 157 -34.366 23.722 16.832 1.00 47.40 O ANISOU 1194 O GLN A 157 6051 5575 6384 1448 -888 -224 O ATOM 1195 CB GLN A 157 -31.598 22.986 16.778 1.00 48.73 C ANISOU 1195 CB GLN A 157 6385 5744 6384 1158 -795 -140 C ATOM 1196 CG GLN A 157 -30.203 22.771 16.233 1.00 55.56 C ANISOU 1196 CG GLN A 157 7346 6587 7179 1011 -781 -63 C ATOM 1197 CD GLN A 157 -29.812 21.315 16.237 1.00 61.47 C ANISOU 1197 CD GLN A 157 8021 7478 7856 918 -700 -47 C ATOM 1198 OE1 GLN A 157 -30.638 20.445 16.512 1.00 63.36 O ANISOU 1198 OE1 GLN A 157 8147 7829 8097 955 -664 -80 O ATOM 1199 NE2 GLN A 157 -28.549 21.035 15.931 1.00 64.39 N ANISOU 1199 NE2 GLN A 157 8454 7843 8170 797 -669 4 N ATOM 1200 N GLY A 158 -33.780 25.533 18.029 1.00 43.37 N ANISOU 1200 N GLY A 158 5683 4868 5929 1527 -892 -326 N ATOM 1201 CA GLY A 158 -35.118 25.730 18.550 1.00 46.42 C ANISOU 1201 CA GLY A 158 5952 5289 6399 1685 -885 -413 C ATOM 1202 C GLY A 158 -35.586 24.661 19.511 1.00 45.65 C ANISOU 1202 C GLY A 158 5706 5364 6273 1684 -759 -488 C ATOM 1203 O GLY A 158 -36.794 24.445 19.642 1.00 49.27 O ANISOU 1203 O GLY A 158 6028 5899 6795 1787 -747 -531 O ATOM 1204 N CYS A 159 -34.665 23.983 20.188 1.00 39.40 N ANISOU 1204 N CYS A 159 4937 4641 5394 1570 -667 -502 N ATOM 1205 CA CYS A 159 -35.066 22.960 21.141 1.00 39.51 C ANISOU 1205 CA CYS A 159 4827 4813 5372 1561 -548 -566 C ATOM 1206 C CYS A 159 -35.751 23.592 22.348 1.00 41.51 C ANISOU 1206 C CYS A 159 5041 5062 5669 1688 -487 -696 C ATOM 1207 O CYS A 159 -35.506 24.750 22.698 1.00 41.27 O ANISOU 1207 O CYS A 159 5111 4899 5669 1752 -520 -749 O ATOM 1208 CB CYS A 159 -33.860 22.134 21.587 1.00 36.99 C ANISOU 1208 CB CYS A 159 4554 4552 4948 1414 -478 -545 C ATOM 1209 SG CYS A 159 -33.028 21.269 20.231 1.00 37.14 S ANISOU 1209 SG CYS A 159 4610 4592 4910 1268 -524 -406 S ATOM 1210 N GLY A 160 -36.636 22.821 22.973 1.00 41.77 N ANISOU 1210 N GLY A 160 4929 5239 5703 1724 -394 -750 N ATOM 1211 CA GLY A 160 -37.336 23.279 24.150 1.00 42.90 C ANISOU 1211 CA GLY A 160 5021 5404 5876 1840 -311 -878 C ATOM 1212 C GLY A 160 -36.490 23.140 25.397 1.00 46.37 C ANISOU 1212 C GLY A 160 5539 5866 6215 1775 -217 -944 C ATOM 1213 O GLY A 160 -35.346 22.689 25.368 1.00 46.99 O ANISOU 1213 O GLY A 160 5701 5942 6210 1643 -220 -889 O ATOM 1214 N GLU A 161 -37.074 23.541 26.521 1.00 49.33 N ANISOU 1214 N GLU A 161 5883 6264 6595 1874 -130 -1067 N ATOM 1215 CA GLU A 161 -36.363 23.455 27.787 1.00 53.92 C ANISOU 1215 CA GLU A 161 6546 6870 7072 1822 -44 -1140 C ATOM 1216 C GLU A 161 -36.141 21.997 28.169 1.00 51.03 C ANISOU 1216 C GLU A 161 6116 6666 6609 1698 46 -1097 C ATOM 1217 O GLU A 161 -37.011 21.144 27.969 1.00 50.84 O ANISOU 1217 O GLU A 161 5947 6765 6605 1701 95 -1071 O ATOM 1218 CB GLU A 161 -37.134 24.192 28.882 1.00 65.23 C ANISOU 1218 CB GLU A 161 7962 8299 8524 1964 37 -1288 C ATOM 1219 CG GLU A 161 -37.313 25.684 28.607 1.00 76.26 C ANISOU 1219 CG GLU A 161 9439 9517 10019 2096 -52 -1343 C ATOM 1220 CD GLU A 161 -35.991 26.425 28.466 1.00 84.11 C ANISOU 1220 CD GLU A 161 10626 10350 10981 2021 -148 -1317 C ATOM 1221 OE1 GLU A 161 -35.018 26.058 29.160 1.00 86.21 O ANISOU 1221 OE1 GLU A 161 10975 10642 11138 1908 -111 -1325 O ATOM 1222 OE2 GLU A 161 -35.924 27.375 27.657 1.00 87.78 O ANISOU 1222 OE2 GLU A 161 11161 10661 11532 2072 -264 -1286 O ATOM 1223 N GLY A 162 -34.956 21.710 28.705 1.00 46.57 N ANISOU 1223 N GLY A 162 5658 6094 5941 1586 57 -1086 N ATOM 1224 CA GLY A 162 -34.572 20.352 29.019 1.00 42.29 C ANISOU 1224 CA GLY A 162 5080 5682 5308 1463 121 -1033 C ATOM 1225 C GLY A 162 -34.210 19.501 27.823 1.00 41.63 C ANISOU 1225 C GLY A 162 4961 5619 5236 1365 61 -904 C ATOM 1226 O GLY A 162 -33.849 18.330 28.003 1.00 46.31 O ANISOU 1226 O GLY A 162 5528 6308 5760 1263 106 -855 O ATOM 1227 N GLN A 163 -34.303 20.040 26.612 1.00 37.66 N ANISOU 1227 N GLN A 163 4466 5029 4816 1394 -40 -848 N ATOM 1228 CA GLN A 163 -33.959 19.310 25.403 1.00 35.54 C ANISOU 1228 CA GLN A 163 4179 4774 4553 1306 -99 -730 C ATOM 1229 C GLN A 163 -32.553 19.667 24.937 1.00 33.96 C ANISOU 1229 C GLN A 163 4113 4468 4322 1218 -171 -673 C ATOM 1230 O GLN A 163 -32.000 20.717 25.275 1.00 38.29 O ANISOU 1230 O GLN A 163 4765 4905 4877 1241 -205 -715 O ATOM 1231 CB GLN A 163 -34.960 19.596 24.280 1.00 31.06 C ANISOU 1231 CB GLN A 163 3535 4183 4081 1384 -170 -693 C ATOM 1232 CG GLN A 163 -36.340 19.013 24.500 1.00 35.11 C ANISOU 1232 CG GLN A 163 3885 4819 4637 1447 -108 -727 C ATOM 1233 CD GLN A 163 -37.226 19.164 23.278 1.00 40.39 C ANISOU 1233 CD GLN A 163 4475 5471 5399 1506 -199 -675 C ATOM 1234 OE1 GLN A 163 -36.991 20.023 22.428 1.00 42.98 O ANISOU 1234 OE1 GLN A 163 4883 5677 5771 1539 -307 -637 O ATOM 1235 NE2 GLN A 163 -38.246 18.324 23.179 1.00 43.19 N ANISOU 1235 NE2 GLN A 163 4678 5946 5785 1512 -163 -669 N ATOM 1236 N VAL A 164 -31.979 18.762 24.148 1.00 26.86 N ANISOU 1236 N VAL A 164 3208 3607 3393 1114 -189 -579 N ATOM 1237 CA VAL A 164 -30.689 18.967 23.504 1.00 26.85 C ANISOU 1237 CA VAL A 164 3309 3523 3370 1023 -249 -511 C ATOM 1238 C VAL A 164 -30.819 18.528 22.054 1.00 26.14 C ANISOU 1238 C VAL A 164 3194 3436 3300 988 -303 -414 C ATOM 1239 O VAL A 164 -31.736 17.792 21.686 1.00 28.68 O ANISOU 1239 O VAL A 164 3418 3842 3636 1008 -289 -397 O ATOM 1240 CB VAL A 164 -29.557 18.175 24.192 1.00 28.25 C ANISOU 1240 CB VAL A 164 3516 3751 3467 914 -200 -503 C ATOM 1241 CG1 VAL A 164 -29.383 18.622 25.631 1.00 27.04 C ANISOU 1241 CG1 VAL A 164 3404 3593 3278 942 -157 -599 C ATOM 1242 CG2 VAL A 164 -29.853 16.680 24.128 1.00 26.84 C ANISOU 1242 CG2 VAL A 164 3246 3704 3249 863 -143 -465 C ATOM 1243 N ALA A 165 -29.892 18.995 21.225 1.00 25.58 N ANISOU 1243 N ALA A 165 3217 3274 3229 930 -364 -349 N ATOM 1244 CA ALA A 165 -29.722 18.400 19.906 1.00 29.59 C ANISOU 1244 CA ALA A 165 3722 3797 3723 868 -400 -254 C ATOM 1245 C ALA A 165 -29.170 16.992 20.088 1.00 27.69 C ANISOU 1245 C ALA A 165 3438 3665 3420 774 -333 -231 C ATOM 1246 O ALA A 165 -28.114 16.811 20.702 1.00 26.15 O ANISOU 1246 O ALA A 165 3280 3470 3186 709 -299 -240 O ATOM 1247 CB ALA A 165 -28.789 19.249 19.048 1.00 30.62 C ANISOU 1247 CB ALA A 165 3968 3807 3858 819 -465 -191 C ATOM 1248 N CYS A 166 -29.888 15.992 19.582 1.00 23.42 N ANISOU 1248 N CYS A 166 2818 3210 2872 769 -321 -203 N ATOM 1249 CA CYS A 166 -29.559 14.604 19.899 1.00 23.49 C ANISOU 1249 CA CYS A 166 2779 3319 2828 695 -256 -193 C ATOM 1250 C CYS A 166 -28.436 14.119 18.994 1.00 28.10 C ANISOU 1250 C CYS A 166 3419 3885 3372 600 -267 -121 C ATOM 1251 O CYS A 166 -28.653 13.792 17.824 1.00 29.02 O ANISOU 1251 O CYS A 166 3538 4004 3484 580 -302 -67 O ATOM 1252 CB CYS A 166 -30.779 13.703 19.774 1.00 26.16 C ANISOU 1252 CB CYS A 166 3010 3752 3178 718 -238 -196 C ATOM 1253 SG CYS A 166 -30.392 12.024 20.284 1.00 30.17 S ANISOU 1253 SG CYS A 166 3474 4365 3625 628 -160 -185 S ATOM 1254 N LEU A 167 -27.235 14.047 19.559 1.00 23.00 N ANISOU 1254 N LEU A 167 2815 3227 2698 541 -236 -125 N ATOM 1255 CA LEU A 167 -26.040 13.578 18.880 1.00 25.86 C ANISOU 1255 CA LEU A 167 3217 3579 3028 453 -230 -69 C ATOM 1256 C LEU A 167 -25.274 12.687 19.842 1.00 23.73 C ANISOU 1256 C LEU A 167 2923 3367 2727 405 -174 -88 C ATOM 1257 O LEU A 167 -25.181 12.998 21.032 1.00 21.84 O ANISOU 1257 O LEU A 167 2685 3130 2486 424 -159 -141 O ATOM 1258 CB LEU A 167 -25.163 14.753 18.429 1.00 25.75 C ANISOU 1258 CB LEU A 167 3290 3462 3032 429 -270 -42 C ATOM 1259 CG LEU A 167 -25.790 15.705 17.412 1.00 28.20 C ANISOU 1259 CG LEU A 167 3648 3698 3370 471 -337 -9 C ATOM 1260 CD1 LEU A 167 -24.920 16.943 17.251 1.00 31.01 C ANISOU 1260 CD1 LEU A 167 4096 3942 3746 443 -372 11 C ATOM 1261 CD2 LEU A 167 -25.974 14.993 16.083 1.00 23.42 C ANISOU 1261 CD2 LEU A 167 3042 3124 2733 438 -348 56 C ATOM 1262 N PHE A 168 -24.717 11.590 19.315 1.00 20.80 N ANISOU 1262 N PHE A 168 2537 3038 2327 344 -148 -48 N ATOM 1263 CA PHE A 168 -24.084 10.584 20.167 1.00 19.83 C ANISOU 1263 CA PHE A 168 2387 2971 2178 306 -104 -59 C ATOM 1264 C PHE A 168 -23.011 11.202 21.059 1.00 17.60 C ANISOU 1264 C PHE A 168 2138 2651 1899 284 -109 -82 C ATOM 1265 O PHE A 168 -23.035 11.029 22.283 1.00 19.33 O ANISOU 1265 O PHE A 168 2345 2900 2100 296 -93 -124 O ATOM 1266 CB PHE A 168 -23.493 9.463 19.305 1.00 19.86 C ANISOU 1266 CB PHE A 168 2381 3002 2161 250 -83 -12 C ATOM 1267 CG PHE A 168 -22.954 8.299 20.099 1.00 19.27 C ANISOU 1267 CG PHE A 168 2277 2979 2066 220 -46 -18 C ATOM 1268 CD1 PHE A 168 -21.679 8.343 20.648 1.00 20.43 C ANISOU 1268 CD1 PHE A 168 2437 3111 2216 186 -42 -18 C ATOM 1269 CD2 PHE A 168 -23.720 7.160 20.286 1.00 19.85 C ANISOU 1269 CD2 PHE A 168 2309 3112 2120 223 -22 -20 C ATOM 1270 CE1 PHE A 168 -21.179 7.278 21.369 1.00 18.23 C ANISOU 1270 CE1 PHE A 168 2134 2873 1921 165 -21 -19 C ATOM 1271 CE2 PHE A 168 -23.228 6.084 21.011 1.00 18.51 C ANISOU 1271 CE2 PHE A 168 2123 2977 1931 195 5 -18 C ATOM 1272 CZ PHE A 168 -21.951 6.142 21.551 1.00 17.93 C ANISOU 1272 CZ PHE A 168 2066 2886 1859 171 3 -17 C ATOM 1273 N GLU A 169 -22.067 11.937 20.468 1.00 16.50 N ANISOU 1273 N GLU A 169 2043 2446 1779 247 -133 -55 N ATOM 1274 CA GLU A 169 -20.935 12.448 21.237 1.00 19.00 C ANISOU 1274 CA GLU A 169 2384 2729 2107 211 -145 -72 C ATOM 1275 C GLU A 169 -21.302 13.612 22.145 1.00 19.32 C ANISOU 1275 C GLU A 169 2463 2718 2159 255 -177 -130 C ATOM 1276 O GLU A 169 -20.490 13.981 23.000 1.00 21.33 O ANISOU 1276 O GLU A 169 2739 2950 2414 227 -195 -158 O ATOM 1277 CB GLU A 169 -19.796 12.863 20.300 1.00 23.34 C ANISOU 1277 CB GLU A 169 2960 3228 2681 147 -154 -22 C ATOM 1278 CG GLU A 169 -19.190 11.692 19.546 1.00 22.78 C ANISOU 1278 CG GLU A 169 2852 3209 2597 103 -112 22 C ATOM 1279 CD GLU A 169 -17.937 12.054 18.760 1.00 26.43 C ANISOU 1279 CD GLU A 169 3326 3634 3082 34 -102 66 C ATOM 1280 OE1 GLU A 169 -17.290 13.077 19.075 1.00 25.88 O ANISOU 1280 OE1 GLU A 169 3284 3505 3044 4 -131 61 O ATOM 1281 OE2 GLU A 169 -17.601 11.305 17.821 1.00 26.68 O ANISOU 1281 OE2 GLU A 169 3341 3695 3099 8 -62 102 O ATOM 1282 N ASP A 170 -22.489 14.198 21.991 1.00 19.83 N ANISOU 1282 N ASP A 170 2537 2762 2235 324 -190 -153 N ATOM 1283 CA ASP A 170 -22.907 15.249 22.909 1.00 21.99 C ANISOU 1283 CA ASP A 170 2848 2988 2520 379 -212 -220 C ATOM 1284 C ASP A 170 -23.505 14.707 24.201 1.00 23.53 C ANISOU 1284 C ASP A 170 3009 3257 2675 417 -172 -282 C ATOM 1285 O ASP A 170 -23.524 15.430 25.205 1.00 25.22 O ANISOU 1285 O ASP A 170 3263 3441 2879 447 -181 -347 O ATOM 1286 CB ASP A 170 -23.919 16.184 22.238 1.00 23.54 C ANISOU 1286 CB ASP A 170 3065 3123 2756 450 -245 -224 C ATOM 1287 CG ASP A 170 -23.288 17.064 21.168 1.00 34.78 C ANISOU 1287 CG ASP A 170 4554 4449 4214 412 -294 -168 C ATOM 1288 OD1 ASP A 170 -22.057 16.977 20.969 1.00 37.96 O ANISOU 1288 OD1 ASP A 170 4976 4835 4612 327 -293 -132 O ATOM 1289 OD2 ASP A 170 -24.029 17.841 20.525 1.00 35.65 O ANISOU 1289 OD2 ASP A 170 4693 4497 4355 466 -334 -158 O ATOM 1290 N VAL A 171 -24.005 13.472 24.213 1.00 21.62 N ANISOU 1290 N VAL A 171 2704 3107 2404 415 -126 -264 N ATOM 1291 CA VAL A 171 -24.620 12.931 25.414 1.00 21.74 C ANISOU 1291 CA VAL A 171 2692 3196 2374 442 -79 -314 C ATOM 1292 C VAL A 171 -23.820 11.786 26.032 1.00 21.59 C ANISOU 1292 C VAL A 171 2662 3235 2306 379 -58 -292 C ATOM 1293 O VAL A 171 -23.831 11.635 27.260 1.00 20.82 O ANISOU 1293 O VAL A 171 2580 3172 2157 383 -38 -334 O ATOM 1294 CB VAL A 171 -26.084 12.505 25.157 1.00 23.60 C ANISOU 1294 CB VAL A 171 2858 3491 2619 497 -42 -319 C ATOM 1295 CG1 VAL A 171 -26.925 13.721 24.783 1.00 27.32 C ANISOU 1295 CG1 VAL A 171 3335 3902 3141 578 -71 -353 C ATOM 1296 CG2 VAL A 171 -26.179 11.433 24.077 1.00 16.29 C ANISOU 1296 CG2 VAL A 171 1886 2605 1701 456 -38 -250 C ATOM 1297 N VAL A 172 -23.120 10.983 25.236 1.00 15.65 N ANISOU 1297 N VAL A 172 1890 2492 1564 324 -63 -229 N ATOM 1298 CA VAL A 172 -22.349 9.852 25.750 1.00 15.23 C ANISOU 1298 CA VAL A 172 1826 2486 1477 274 -51 -204 C ATOM 1299 C VAL A 172 -20.933 10.332 26.025 1.00 18.04 C ANISOU 1299 C VAL A 172 2217 2793 1844 230 -95 -203 C ATOM 1300 O VAL A 172 -20.257 10.806 25.098 1.00 16.77 O ANISOU 1300 O VAL A 172 2063 2582 1729 203 -119 -173 O ATOM 1301 CB VAL A 172 -22.346 8.678 24.760 1.00 21.16 C ANISOU 1301 CB VAL A 172 2533 3268 2237 245 -31 -146 C ATOM 1302 CG1 VAL A 172 -21.635 7.470 25.374 1.00 20.36 C ANISOU 1302 CG1 VAL A 172 2422 3207 2106 205 -21 -123 C ATOM 1303 CG2 VAL A 172 -23.772 8.318 24.358 1.00 19.82 C ANISOU 1303 CG2 VAL A 172 2324 3139 2068 280 -1 -147 C ATOM 1304 N PRO A 173 -20.433 10.230 27.264 1.00 19.42 N ANISOU 1304 N PRO A 173 2417 2984 1978 217 -110 -231 N ATOM 1305 CA PRO A 173 -19.085 10.733 27.558 1.00 18.90 C ANISOU 1305 CA PRO A 173 2377 2872 1931 172 -166 -233 C ATOM 1306 C PRO A 173 -18.024 9.902 26.858 1.00 17.27 C ANISOU 1306 C PRO A 173 2125 2676 1762 122 -172 -172 C ATOM 1307 O PRO A 173 -18.105 8.674 26.804 1.00 15.23 O ANISOU 1307 O PRO A 173 1832 2468 1486 119 -145 -140 O ATOM 1308 CB PRO A 173 -18.969 10.602 29.083 1.00 20.52 C ANISOU 1308 CB PRO A 173 2621 3108 2070 173 -183 -276 C ATOM 1309 CG PRO A 173 -20.356 10.344 29.571 1.00 20.05 C ANISOU 1309 CG PRO A 173 2564 3099 1956 224 -125 -307 C ATOM 1310 CD PRO A 173 -21.076 9.654 28.456 1.00 18.83 C ANISOU 1310 CD PRO A 173 2350 2971 1833 236 -80 -262 C ATOM 1311 N MET A 174 -17.020 10.588 26.320 1.00 17.78 N ANISOU 1311 N MET A 174 2188 2687 1880 82 -205 -156 N ATOM 1312 CA MET A 174 -15.979 9.883 25.589 1.00 16.64 C ANISOU 1312 CA MET A 174 1991 2553 1778 39 -199 -104 C ATOM 1313 C MET A 174 -15.081 9.079 26.526 1.00 17.05 C ANISOU 1313 C MET A 174 2019 2640 1821 18 -232 -100 C ATOM 1314 O MET A 174 -14.516 8.065 26.107 1.00 19.90 O ANISOU 1314 O MET A 174 2328 3029 2205 7 -215 -62 O ATOM 1315 CB MET A 174 -15.160 10.870 24.755 1.00 19.65 C ANISOU 1315 CB MET A 174 2372 2873 2220 -6 -215 -86 C ATOM 1316 CG MET A 174 -14.340 10.201 23.665 1.00 24.19 C ANISOU 1316 CG MET A 174 2889 3465 2838 -41 -179 -32 C ATOM 1317 SD MET A 174 -15.359 9.268 22.498 1.00 27.72 S ANISOU 1317 SD MET A 174 3329 3948 3257 -4 -112 -2 S ATOM 1318 CE MET A 174 -16.043 10.591 21.506 1.00 25.98 C ANISOU 1318 CE MET A 174 3164 3664 3042 -1 -112 6 C ATOM 1319 N ASN A 175 -14.940 9.491 27.796 1.00 16.79 N ANISOU 1319 N ASN A 175 2025 2603 1752 17 -282 -141 N ATOM 1320 CA ASN A 175 -14.152 8.660 28.704 1.00 16.85 C ANISOU 1320 CA ASN A 175 2016 2644 1742 1 -326 -131 C ATOM 1321 C ASN A 175 -14.864 7.345 29.003 1.00 19.53 C ANISOU 1321 C ASN A 175 2354 3041 2027 32 -287 -110 C ATOM 1322 O ASN A 175 -14.209 6.303 29.104 1.00 21.15 O ANISOU 1322 O ASN A 175 2522 3268 2244 24 -302 -74 O ATOM 1323 CB ASN A 175 -13.776 9.410 30.001 1.00 20.64 C ANISOU 1323 CB ASN A 175 2551 3106 2185 -15 -400 -180 C ATOM 1324 CG ASN A 175 -14.965 10.071 30.715 1.00 19.39 C ANISOU 1324 CG ASN A 175 2472 2944 1950 24 -381 -240 C ATOM 1325 OD1 ASN A 175 -16.124 9.800 30.428 1.00 20.98 O ANISOU 1325 OD1 ASN A 175 2677 3171 2123 66 -314 -242 O ATOM 1326 ND2 ASN A 175 -14.655 10.947 31.670 1.00 18.96 N ANISOU 1326 ND2 ASN A 175 2479 2859 1866 10 -443 -294 N ATOM 1327 N TYR A 176 -16.196 7.358 29.102 1.00 15.56 N ANISOU 1327 N TYR A 176 1883 2558 1471 68 -237 -131 N ATOM 1328 CA TYR A 176 -16.937 6.100 29.120 1.00 17.29 C ANISOU 1328 CA TYR A 176 2090 2826 1652 85 -190 -102 C ATOM 1329 C TYR A 176 -16.625 5.270 27.879 1.00 18.57 C ANISOU 1329 C TYR A 176 2196 2986 1872 78 -162 -54 C ATOM 1330 O TYR A 176 -16.337 4.069 27.970 1.00 17.24 O ANISOU 1330 O TYR A 176 2010 2838 1701 74 -161 -19 O ATOM 1331 CB TYR A 176 -18.445 6.364 29.211 1.00 15.17 C ANISOU 1331 CB TYR A 176 1843 2581 1338 119 -133 -132 C ATOM 1332 CG TYR A 176 -19.257 5.121 28.910 1.00 16.29 C ANISOU 1332 CG TYR A 176 1959 2766 1462 125 -81 -97 C ATOM 1333 CD1 TYR A 176 -19.536 4.194 29.909 1.00 18.61 C ANISOU 1333 CD1 TYR A 176 2276 3103 1690 116 -71 -84 C ATOM 1334 CD2 TYR A 176 -19.710 4.856 27.620 1.00 14.61 C ANISOU 1334 CD2 TYR A 176 1707 2549 1296 130 -47 -74 C ATOM 1335 CE1 TYR A 176 -20.262 3.051 29.639 1.00 15.79 C ANISOU 1335 CE1 TYR A 176 1899 2778 1323 110 -27 -48 C ATOM 1336 CE2 TYR A 176 -20.425 3.711 27.336 1.00 14.70 C ANISOU 1336 CE2 TYR A 176 1698 2594 1295 127 -8 -45 C ATOM 1337 CZ TYR A 176 -20.697 2.813 28.349 1.00 19.77 C ANISOU 1337 CZ TYR A 176 2359 3273 1880 114 2 -32 C ATOM 1338 OH TYR A 176 -21.411 1.670 28.069 1.00 19.87 O ANISOU 1338 OH TYR A 176 2355 3312 1885 101 38 0 O ATOM 1339 N MET A 177 -16.687 5.899 26.701 1.00 17.87 N ANISOU 1339 N MET A 177 2089 2868 1832 77 -139 -52 N ATOM 1340 CA MET A 177 -16.566 5.154 25.453 1.00 18.01 C ANISOU 1340 CA MET A 177 2068 2888 1888 73 -102 -14 C ATOM 1341 C MET A 177 -15.189 4.521 25.292 1.00 17.35 C ANISOU 1341 C MET A 177 1941 2799 1852 52 -120 14 C ATOM 1342 O MET A 177 -15.079 3.424 24.729 1.00 17.29 O ANISOU 1342 O MET A 177 1908 2803 1857 58 -93 40 O ATOM 1343 CB MET A 177 -16.873 6.066 24.266 1.00 16.74 C ANISOU 1343 CB MET A 177 1909 2695 1755 72 -80 -14 C ATOM 1344 CG MET A 177 -18.370 6.349 24.073 1.00 16.16 C ANISOU 1344 CG MET A 177 1859 2632 1650 105 -55 -32 C ATOM 1345 SD MET A 177 -19.348 4.835 23.878 1.00 18.07 S ANISOU 1345 SD MET A 177 2081 2925 1861 117 -15 -12 S ATOM 1346 CE MET A 177 -18.664 4.181 22.353 1.00 17.68 C ANISOU 1346 CE MET A 177 2010 2858 1848 96 7 26 C ATOM 1347 N VAL A 178 -14.135 5.185 25.761 1.00 16.79 N ANISOU 1347 N VAL A 178 1857 2708 1812 28 -169 5 N ATOM 1348 CA VAL A 178 -12.778 4.693 25.541 1.00 18.15 C ANISOU 1348 CA VAL A 178 1968 2879 2048 11 -187 29 C ATOM 1349 C VAL A 178 -12.360 3.744 26.660 1.00 17.19 C ANISOU 1349 C VAL A 178 1842 2778 1909 24 -239 38 C ATOM 1350 O VAL A 178 -11.937 2.613 26.399 1.00 15.15 O ANISOU 1350 O VAL A 178 1548 2530 1680 40 -229 65 O ATOM 1351 CB VAL A 178 -11.786 5.862 25.404 1.00 20.28 C ANISOU 1351 CB VAL A 178 2211 3118 2374 -31 -219 20 C ATOM 1352 CG1 VAL A 178 -10.354 5.355 25.459 1.00 20.11 C ANISOU 1352 CG1 VAL A 178 2110 3105 2424 -48 -248 40 C ATOM 1353 CG2 VAL A 178 -12.040 6.615 24.094 1.00 15.11 C ANISOU 1353 CG2 VAL A 178 1562 2438 1741 -48 -163 28 C ATOM 1354 N TYR A 179 -12.467 4.193 27.914 1.00 16.80 N ANISOU 1354 N TYR A 179 1839 2733 1812 18 -297 16 N ATOM 1355 CA TYR A 179 -11.940 3.412 29.032 1.00 19.71 C ANISOU 1355 CA TYR A 179 2213 3117 2158 24 -362 31 C ATOM 1356 C TYR A 179 -12.871 2.266 29.411 1.00 20.50 C ANISOU 1356 C TYR A 179 2356 3241 2190 49 -334 52 C ATOM 1357 O TYR A 179 -12.429 1.124 29.576 1.00 20.92 O ANISOU 1357 O TYR A 179 2394 3297 2258 63 -356 87 O ATOM 1358 CB TYR A 179 -11.721 4.311 30.249 1.00 21.38 C ANISOU 1358 CB TYR A 179 2473 3325 2326 3 -438 -3 C ATOM 1359 CG TYR A 179 -10.568 5.284 30.135 1.00 23.73 C ANISOU 1359 CG TYR A 179 2725 3593 2696 -35 -494 -18 C ATOM 1360 CD1 TYR A 179 -9.340 4.888 29.615 1.00 22.18 C ANISOU 1360 CD1 TYR A 179 2436 3395 2597 -46 -515 11 C ATOM 1361 CD2 TYR A 179 -10.704 6.598 30.570 1.00 24.58 C ANISOU 1361 CD2 TYR A 179 2883 3676 2781 -60 -525 -64 C ATOM 1362 CE1 TYR A 179 -8.280 5.780 29.523 1.00 21.04 C ANISOU 1362 CE1 TYR A 179 2238 3229 2527 -92 -564 0 C ATOM 1363 CE2 TYR A 179 -9.656 7.494 30.485 1.00 24.67 C ANISOU 1363 CE2 TYR A 179 2856 3654 2863 -107 -581 -76 C ATOM 1364 CZ TYR A 179 -8.444 7.079 29.961 1.00 26.82 C ANISOU 1364 CZ TYR A 179 3025 3931 3233 -128 -600 -41 C ATOM 1365 OH TYR A 179 -7.400 7.970 29.869 1.00 27.90 O ANISOU 1365 OH TYR A 179 3112 4040 3447 -185 -652 -50 O ATOM 1366 N PHE A 180 -14.156 2.565 29.590 1.00 18.84 N ANISOU 1366 N PHE A 180 2199 3047 1911 54 -288 31 N ATOM 1367 CA PHE A 180 -15.101 1.582 30.101 1.00 19.74 C ANISOU 1367 CA PHE A 180 2356 3189 1956 64 -259 51 C ATOM 1368 C PHE A 180 -15.617 0.688 28.977 1.00 19.94 C ANISOU 1368 C PHE A 180 2350 3212 2013 74 -196 77 C ATOM 1369 O PHE A 180 -15.508 -0.541 29.051 1.00 21.09 O ANISOU 1369 O PHE A 180 2498 3354 2160 78 -201 114 O ATOM 1370 CB PHE A 180 -16.247 2.313 30.810 1.00 17.81 C ANISOU 1370 CB PHE A 180 2168 2970 1628 66 -230 11 C ATOM 1371 CG PHE A 180 -17.175 1.420 31.598 1.00 18.94 C ANISOU 1371 CG PHE A 180 2357 3151 1688 63 -199 31 C ATOM 1372 CD1 PHE A 180 -18.244 0.787 30.980 1.00 16.46 C ANISOU 1372 CD1 PHE A 180 2027 2855 1374 65 -128 47 C ATOM 1373 CD2 PHE A 180 -17.013 1.260 32.969 1.00 21.23 C ANISOU 1373 CD2 PHE A 180 2712 3461 1895 51 -241 34 C ATOM 1374 CE1 PHE A 180 -19.115 -0.013 31.706 1.00 20.59 C ANISOU 1374 CE1 PHE A 180 2588 3413 1824 50 -94 68 C ATOM 1375 CE2 PHE A 180 -17.882 0.464 33.700 1.00 17.51 C ANISOU 1375 CE2 PHE A 180 2289 3026 1339 39 -203 57 C ATOM 1376 CZ PHE A 180 -18.933 -0.172 33.067 1.00 18.75 C ANISOU 1376 CZ PHE A 180 2420 3200 1505 36 -126 76 C ATOM 1377 N ASN A 181 -16.159 1.283 27.917 1.00 17.43 N ANISOU 1377 N ASN A 181 2011 2889 1723 78 -146 58 N ATOM 1378 CA ASN A 181 -16.736 0.465 26.858 1.00 18.94 C ANISOU 1378 CA ASN A 181 2185 3079 1933 83 -94 77 C ATOM 1379 C ASN A 181 -15.649 -0.207 26.024 1.00 22.78 C ANISOU 1379 C ASN A 181 2629 3538 2487 88 -98 99 C ATOM 1380 O ASN A 181 -15.640 -1.433 25.873 1.00 25.01 O ANISOU 1380 O ASN A 181 2912 3813 2776 96 -90 124 O ATOM 1381 CB ASN A 181 -17.664 1.299 25.975 1.00 20.00 C ANISOU 1381 CB ASN A 181 2315 3216 2070 87 -50 54 C ATOM 1382 CG ASN A 181 -18.469 0.434 25.023 1.00 23.68 C ANISOU 1382 CG ASN A 181 2773 3686 2539 87 -7 70 C ATOM 1383 OD1 ASN A 181 -18.102 0.264 23.859 1.00 24.08 O ANISOU 1383 OD1 ASN A 181 2804 3717 2628 87 9 77 O ATOM 1384 ND2 ASN A 181 -19.543 -0.164 25.532 1.00 18.99 N ANISOU 1384 ND2 ASN A 181 2194 3119 1900 81 13 75 N ATOM 1385 N PHE A 182 -14.722 0.573 25.470 1.00 18.19 N ANISOU 1385 N PHE A 182 2010 2941 1960 84 -105 88 N ATOM 1386 CA PHE A 182 -13.730 -0.018 24.579 1.00 15.65 C ANISOU 1386 CA PHE A 182 1638 2603 1705 92 -90 102 C ATOM 1387 C PHE A 182 -12.714 -0.869 25.339 1.00 17.38 C ANISOU 1387 C PHE A 182 1832 2814 1956 107 -142 122 C ATOM 1388 O PHE A 182 -12.656 -2.085 25.135 1.00 20.03 O ANISOU 1388 O PHE A 182 2168 3138 2306 130 -133 141 O ATOM 1389 CB PHE A 182 -13.006 1.061 23.766 1.00 18.53 C ANISOU 1389 CB PHE A 182 1964 2957 2119 73 -73 91 C ATOM 1390 CG PHE A 182 -12.020 0.511 22.765 1.00 21.87 C ANISOU 1390 CG PHE A 182 2331 3372 2607 80 -36 100 C ATOM 1391 CD1 PHE A 182 -12.230 -0.720 22.153 1.00 20.78 C ANISOU 1391 CD1 PHE A 182 2198 3229 2469 106 2 107 C ATOM 1392 CD2 PHE A 182 -10.874 1.221 22.450 1.00 23.33 C ANISOU 1392 CD2 PHE A 182 2457 3554 2855 59 -35 99 C ATOM 1393 CE1 PHE A 182 -11.317 -1.218 21.236 1.00 18.64 C ANISOU 1393 CE1 PHE A 182 1878 2951 2254 121 45 105 C ATOM 1394 CE2 PHE A 182 -9.964 0.731 21.539 1.00 22.92 C ANISOU 1394 CE2 PHE A 182 2345 3503 2862 67 13 103 C ATOM 1395 CZ PHE A 182 -10.182 -0.490 20.934 1.00 21.39 C ANISOU 1395 CZ PHE A 182 2160 3305 2663 103 56 103 C ATOM 1396 N PHE A 183 -11.890 -0.250 26.189 1.00 16.70 N ANISOU 1396 N PHE A 183 1726 2731 1887 97 -206 118 N ATOM 1397 CA PHE A 183 -10.812 -1.002 26.832 1.00 19.68 C ANISOU 1397 CA PHE A 183 2068 3101 2307 116 -270 140 C ATOM 1398 C PHE A 183 -11.361 -2.158 27.663 1.00 23.21 C ANISOU 1398 C PHE A 183 2575 3545 2699 135 -299 168 C ATOM 1399 O PHE A 183 -10.970 -3.316 27.470 1.00 22.71 O ANISOU 1399 O PHE A 183 2496 3459 2674 166 -305 192 O ATOM 1400 CB PHE A 183 -9.946 -0.076 27.693 1.00 18.92 C ANISOU 1400 CB PHE A 183 1949 3009 2229 94 -349 129 C ATOM 1401 CG PHE A 183 -9.080 0.874 26.897 1.00 22.10 C ANISOU 1401 CG PHE A 183 2277 3409 2711 69 -331 113 C ATOM 1402 CD1 PHE A 183 -9.035 0.802 25.512 1.00 22.30 C ANISOU 1402 CD1 PHE A 183 2264 3430 2779 72 -244 112 C ATOM 1403 CD2 PHE A 183 -8.309 1.836 27.533 1.00 23.94 C ANISOU 1403 CD2 PHE A 183 2485 3640 2970 35 -401 99 C ATOM 1404 CE1 PHE A 183 -8.244 1.672 24.777 1.00 23.18 C ANISOU 1404 CE1 PHE A 183 2312 3541 2956 39 -218 104 C ATOM 1405 CE2 PHE A 183 -7.514 2.707 26.801 1.00 25.46 C ANISOU 1405 CE2 PHE A 183 2607 3826 3239 -1 -382 90 C ATOM 1406 CZ PHE A 183 -7.486 2.622 25.420 1.00 22.25 C ANISOU 1406 CZ PHE A 183 2162 3419 2872 0 -285 95 C ATOM 1407 N ALA A 184 -12.296 -1.871 28.572 1.00 20.36 N ANISOU 1407 N ALA A 184 2287 3203 2248 115 -311 166 N ATOM 1408 CA ALA A 184 -12.701 -2.878 29.549 1.00 22.07 C ANISOU 1408 CA ALA A 184 2565 3418 2402 120 -344 200 C ATOM 1409 C ALA A 184 -13.702 -3.875 28.969 1.00 19.68 C ANISOU 1409 C ALA A 184 2292 3107 2081 122 -279 218 C ATOM 1410 O ALA A 184 -13.575 -5.086 29.182 1.00 17.83 O ANISOU 1410 O ALA A 184 2080 2845 1852 135 -301 256 O ATOM 1411 CB ALA A 184 -13.283 -2.200 30.791 1.00 20.99 C ANISOU 1411 CB ALA A 184 2497 3311 2166 94 -372 189 C ATOM 1412 N CYS A 185 -14.711 -3.388 28.244 1.00 18.93 N ANISOU 1412 N CYS A 185 2199 3029 1966 107 -207 193 N ATOM 1413 CA CYS A 185 -15.842 -4.224 27.864 1.00 21.96 C ANISOU 1413 CA CYS A 185 2612 3410 2319 95 -155 207 C ATOM 1414 C CYS A 185 -15.752 -4.796 26.456 1.00 20.67 C ANISOU 1414 C CYS A 185 2418 3219 2218 110 -114 201 C ATOM 1415 O CYS A 185 -16.481 -5.746 26.147 1.00 21.99 O ANISOU 1415 O CYS A 185 2612 3370 2371 99 -88 216 O ATOM 1416 CB CYS A 185 -17.146 -3.434 28.004 1.00 23.25 C ANISOU 1416 CB CYS A 185 2796 3615 2422 72 -109 182 C ATOM 1417 SG CYS A 185 -17.530 -3.037 29.720 1.00 26.84 S ANISOU 1417 SG CYS A 185 3309 4108 2780 54 -136 184 S ATOM 1418 N VAL A 186 -14.886 -4.262 25.605 1.00 16.87 N ANISOU 1418 N VAL A 186 1884 2728 1797 127 -104 179 N ATOM 1419 CA VAL A 186 -14.700 -4.771 24.250 1.00 20.65 C ANISOU 1419 CA VAL A 186 2340 3183 2323 143 -58 168 C ATOM 1420 C VAL A 186 -13.308 -5.369 24.070 1.00 20.25 C ANISOU 1420 C VAL A 186 2244 3102 2348 180 -79 173 C ATOM 1421 O VAL A 186 -13.166 -6.544 23.726 1.00 20.30 O ANISOU 1421 O VAL A 186 2262 3071 2380 205 -73 181 O ATOM 1422 CB VAL A 186 -14.974 -3.670 23.204 1.00 20.50 C ANISOU 1422 CB VAL A 186 2301 3182 2305 129 -11 139 C ATOM 1423 CG1 VAL A 186 -14.635 -4.174 21.800 1.00 19.90 C ANISOU 1423 CG1 VAL A 186 2210 3084 2266 143 39 126 C ATOM 1424 CG2 VAL A 186 -16.427 -3.217 23.281 1.00 17.52 C ANISOU 1424 CG2 VAL A 186 1960 2830 1868 105 7 133 C ATOM 1425 N LEU A 187 -12.268 -4.579 24.331 1.00 19.19 N ANISOU 1425 N LEU A 187 2055 2980 2255 186 -107 167 N ATOM 1426 CA LEU A 187 -10.906 -5.019 24.050 1.00 20.17 C ANISOU 1426 CA LEU A 187 2111 3085 2466 224 -119 166 C ATOM 1427 C LEU A 187 -10.513 -6.209 24.918 1.00 22.02 C ANISOU 1427 C LEU A 187 2360 3287 2720 260 -186 197 C ATOM 1428 O LEU A 187 -9.976 -7.204 24.416 1.00 22.79 O ANISOU 1428 O LEU A 187 2436 3348 2875 305 -174 196 O ATOM 1429 CB LEU A 187 -9.940 -3.853 24.256 1.00 24.04 C ANISOU 1429 CB LEU A 187 2533 3600 3000 209 -144 156 C ATOM 1430 CG LEU A 187 -8.580 -3.956 23.580 1.00 32.22 C ANISOU 1430 CG LEU A 187 3470 4633 4137 236 -124 145 C ATOM 1431 CD1 LEU A 187 -8.760 -4.225 22.089 1.00 34.40 C ANISOU 1431 CD1 LEU A 187 3744 4904 4422 244 -21 123 C ATOM 1432 CD2 LEU A 187 -7.811 -2.665 23.801 1.00 34.62 C ANISOU 1432 CD2 LEU A 187 3713 4964 4479 199 -149 138 C ATOM 1433 N VAL A 188 -10.773 -6.132 26.224 1.00 19.97 N ANISOU 1433 N VAL A 188 2144 3035 2408 244 -256 224 N ATOM 1434 CA VAL A 188 -10.392 -7.228 27.121 1.00 21.21 C ANISOU 1434 CA VAL A 188 2329 3156 2573 274 -332 265 C ATOM 1435 C VAL A 188 -11.090 -8.531 26.759 1.00 23.48 C ANISOU 1435 C VAL A 188 2678 3398 2847 286 -303 282 C ATOM 1436 O VAL A 188 -10.411 -9.568 26.663 1.00 23.60 O ANISOU 1436 O VAL A 188 2682 3361 2925 337 -332 296 O ATOM 1437 CB VAL A 188 -10.609 -6.817 28.585 1.00 22.69 C ANISOU 1437 CB VAL A 188 2570 3367 2685 244 -408 291 C ATOM 1438 CG1 VAL A 188 -10.569 -8.046 29.497 1.00 21.88 C ANISOU 1438 CG1 VAL A 188 2530 3223 2559 263 -479 345 C ATOM 1439 CG2 VAL A 188 -9.559 -5.804 29.019 1.00 21.77 C ANISOU 1439 CG2 VAL A 188 2388 3277 2606 243 -468 276 C ATOM 1440 N PRO A 189 -12.416 -8.577 26.551 1.00 22.61 N ANISOU 1440 N PRO A 189 2630 3298 2665 243 -251 281 N ATOM 1441 CA PRO A 189 -13.030 -9.846 26.125 1.00 26.92 C ANISOU 1441 CA PRO A 189 3229 3791 3207 246 -228 295 C ATOM 1442 C PRO A 189 -12.517 -10.354 24.785 1.00 25.33 C ANISOU 1442 C PRO A 189 2991 3553 3081 289 -179 258 C ATOM 1443 O PRO A 189 -12.387 -11.571 24.600 1.00 25.80 O ANISOU 1443 O PRO A 189 3083 3546 3173 320 -191 268 O ATOM 1444 CB PRO A 189 -14.528 -9.512 26.068 1.00 26.17 C ANISOU 1444 CB PRO A 189 3181 3731 3030 184 -178 291 C ATOM 1445 CG PRO A 189 -14.700 -8.363 26.975 1.00 23.17 C ANISOU 1445 CG PRO A 189 2797 3411 2596 158 -196 292 C ATOM 1446 CD PRO A 189 -13.439 -7.559 26.864 1.00 21.25 C ANISOU 1446 CD PRO A 189 2483 3179 2412 191 -223 270 C ATOM 1447 N LEU A 190 -12.230 -9.458 23.837 1.00 20.56 N ANISOU 1447 N LEU A 190 2327 2984 2500 290 -123 215 N ATOM 1448 CA LEU A 190 -11.670 -9.894 22.560 1.00 21.28 C ANISOU 1448 CA LEU A 190 2387 3049 2651 331 -66 176 C ATOM 1449 C LEU A 190 -10.294 -10.519 22.743 1.00 21.57 C ANISOU 1449 C LEU A 190 2366 3049 2781 402 -102 178 C ATOM 1450 O LEU A 190 -9.973 -11.526 22.104 1.00 21.39 O ANISOU 1450 O LEU A 190 2349 2971 2805 451 -79 158 O ATOM 1451 CB LEU A 190 -11.595 -8.720 21.586 1.00 21.68 C ANISOU 1451 CB LEU A 190 2391 3149 2696 310 1 140 C ATOM 1452 CG LEU A 190 -12.943 -8.266 21.021 1.00 23.45 C ANISOU 1452 CG LEU A 190 2669 3397 2844 257 42 129 C ATOM 1453 CD1 LEU A 190 -12.762 -7.014 20.172 1.00 23.66 C ANISOU 1453 CD1 LEU A 190 2657 3467 2866 238 94 104 C ATOM 1454 CD2 LEU A 190 -13.597 -9.384 20.214 1.00 21.37 C ANISOU 1454 CD2 LEU A 190 2465 3088 2565 259 72 114 C ATOM 1455 N LEU A 191 -9.464 -9.933 23.608 1.00 18.59 N ANISOU 1455 N LEU A 191 1929 2699 2436 411 -162 197 N ATOM 1456 CA LEU A 191 -8.165 -10.531 23.891 1.00 23.64 C ANISOU 1456 CA LEU A 191 2502 3306 3174 482 -213 203 C ATOM 1457 C LEU A 191 -8.318 -11.863 24.615 1.00 23.59 C ANISOU 1457 C LEU A 191 2568 3227 3170 517 -285 243 C ATOM 1458 O LEU A 191 -7.561 -12.801 24.348 1.00 26.33 O ANISOU 1458 O LEU A 191 2887 3517 3600 591 -298 235 O ATOM 1459 CB LEU A 191 -7.304 -9.561 24.703 1.00 24.29 C ANISOU 1459 CB LEU A 191 2507 3436 3288 474 -277 217 C ATOM 1460 CG LEU A 191 -6.924 -8.258 23.985 1.00 29.21 C ANISOU 1460 CG LEU A 191 3050 4119 3929 440 -213 181 C ATOM 1461 CD1 LEU A 191 -6.123 -7.333 24.894 1.00 29.76 C ANISOU 1461 CD1 LEU A 191 3052 4226 4029 420 -292 195 C ATOM 1462 CD2 LEU A 191 -6.143 -8.558 22.707 1.00 29.57 C ANISOU 1462 CD2 LEU A 191 3018 4160 4059 486 -125 139 C ATOM 1463 N LEU A 192 -9.295 -11.966 25.521 1.00 21.92 N ANISOU 1463 N LEU A 192 2449 3013 2867 465 -328 288 N ATOM 1464 CA LEU A 192 -9.600 -13.251 26.144 1.00 25.11 C ANISOU 1464 CA LEU A 192 2940 3342 3260 480 -387 335 C ATOM 1465 C LEU A 192 -10.004 -14.287 25.104 1.00 23.16 C ANISOU 1465 C LEU A 192 2737 3027 3035 501 -328 307 C ATOM 1466 O LEU A 192 -9.579 -15.444 25.177 1.00 28.00 O ANISOU 1466 O LEU A 192 3378 3555 3705 559 -370 322 O ATOM 1467 CB LEU A 192 -10.705 -13.084 27.187 1.00 26.76 C ANISOU 1467 CB LEU A 192 3241 3573 3353 404 -417 384 C ATOM 1468 CG LEU A 192 -10.321 -12.345 28.468 1.00 34.82 C ANISOU 1468 CG LEU A 192 4254 4640 4334 387 -497 418 C ATOM 1469 CD1 LEU A 192 -11.535 -12.229 29.386 1.00 38.41 C ANISOU 1469 CD1 LEU A 192 4809 5122 4665 311 -500 457 C ATOM 1470 CD2 LEU A 192 -9.182 -13.058 29.175 1.00 35.47 C ANISOU 1470 CD2 LEU A 192 4323 4670 4483 453 -608 457 C ATOM 1471 N MET A 193 -10.835 -13.893 24.134 1.00 23.14 N ANISOU 1471 N MET A 193 2747 3055 2989 456 -239 266 N ATOM 1472 CA MET A 193 -11.221 -14.809 23.062 1.00 26.90 C ANISOU 1472 CA MET A 193 3270 3470 3481 470 -186 230 C ATOM 1473 C MET A 193 -10.013 -15.264 22.264 1.00 24.48 C ANISOU 1473 C MET A 193 2900 3125 3276 563 -160 182 C ATOM 1474 O MET A 193 -9.904 -16.442 21.906 1.00 26.05 O ANISOU 1474 O MET A 193 3146 3235 3516 610 -164 168 O ATOM 1475 CB MET A 193 -12.215 -14.146 22.114 1.00 28.76 C ANISOU 1475 CB MET A 193 3519 3756 3652 408 -104 192 C ATOM 1476 CG MET A 193 -13.567 -13.855 22.684 1.00 34.47 C ANISOU 1476 CG MET A 193 4300 4512 4285 322 -113 228 C ATOM 1477 SD MET A 193 -14.548 -13.053 21.403 1.00 36.06 S ANISOU 1477 SD MET A 193 4497 4769 4434 270 -30 177 S ATOM 1478 CE MET A 193 -15.544 -11.962 22.425 1.00 33.77 C ANISOU 1478 CE MET A 193 4205 4560 4066 199 -46 215 C ATOM 1479 N LEU A 194 -9.123 -14.329 21.929 1.00 24.18 N ANISOU 1479 N LEU A 194 2756 3151 3281 587 -126 153 N ATOM 1480 CA LEU A 194 -7.891 -14.702 21.247 1.00 26.79 C ANISOU 1480 CA LEU A 194 3005 3457 3715 678 -92 107 C ATOM 1481 C LEU A 194 -7.125 -15.744 22.047 1.00 25.62 C ANISOU 1481 C LEU A 194 2852 3232 3650 758 -185 138 C ATOM 1482 O LEU A 194 -6.619 -16.722 21.486 1.00 27.41 O ANISOU 1482 O LEU A 194 3078 3387 3950 839 -166 102 O ATOM 1483 CB LEU A 194 -7.029 -13.462 21.006 1.00 24.76 C ANISOU 1483 CB LEU A 194 2625 3289 3496 675 -53 86 C ATOM 1484 CG LEU A 194 -5.655 -13.708 20.379 1.00 29.30 C ANISOU 1484 CG LEU A 194 3087 3859 4188 764 -9 41 C ATOM 1485 CD1 LEU A 194 -5.806 -14.362 19.011 1.00 30.26 C ANISOU 1485 CD1 LEU A 194 3247 3945 4307 797 97 -26 C ATOM 1486 CD2 LEU A 194 -4.885 -12.405 20.270 1.00 27.95 C ANISOU 1486 CD2 LEU A 194 2793 3778 4048 738 23 33 C ATOM 1487 N GLY A 195 -7.046 -15.560 23.367 1.00 25.24 N ANISOU 1487 N GLY A 195 2808 3193 3589 741 -289 204 N ATOM 1488 CA GLY A 195 -6.343 -16.525 24.193 1.00 23.43 C ANISOU 1488 CA GLY A 195 2583 2886 3431 816 -394 245 C ATOM 1489 C GLY A 195 -7.029 -17.877 24.216 1.00 25.32 C ANISOU 1489 C GLY A 195 2953 3015 3653 826 -419 266 C ATOM 1490 O GLY A 195 -6.367 -18.918 24.216 1.00 30.00 O ANISOU 1490 O GLY A 195 3549 3515 4334 917 -463 264 O ATOM 1491 N VAL A 196 -8.364 -17.881 24.224 1.00 24.50 N ANISOU 1491 N VAL A 196 2954 2913 3441 732 -392 284 N ATOM 1492 CA VAL A 196 -9.109 -19.136 24.204 1.00 24.39 C ANISOU 1492 CA VAL A 196 3067 2793 3408 721 -412 305 C ATOM 1493 C VAL A 196 -8.876 -19.877 22.892 1.00 24.21 C ANISOU 1493 C VAL A 196 3048 2703 3448 784 -341 226 C ATOM 1494 O VAL A 196 -8.625 -21.088 22.881 1.00 24.42 O ANISOU 1494 O VAL A 196 3133 2612 3534 847 -382 229 O ATOM 1495 CB VAL A 196 -10.607 -18.874 24.450 1.00 24.22 C ANISOU 1495 CB VAL A 196 3133 2805 3263 597 -389 337 C ATOM 1496 CG1 VAL A 196 -11.407 -20.151 24.257 1.00 22.44 C ANISOU 1496 CG1 VAL A 196 3031 2471 3025 571 -398 352 C ATOM 1497 CG2 VAL A 196 -10.822 -18.323 25.856 1.00 22.55 C ANISOU 1497 CG2 VAL A 196 2937 2647 2984 544 -460 414 C ATOM 1498 N TYR A 197 -8.952 -19.164 21.765 1.00 23.02 N ANISOU 1498 N TYR A 197 2845 2620 3281 769 -235 155 N ATOM 1499 CA TYR A 197 -8.730 -19.820 20.481 1.00 23.93 C ANISOU 1499 CA TYR A 197 2974 2679 3439 827 -159 73 C ATOM 1500 C TYR A 197 -7.297 -20.318 20.341 1.00 28.91 C ANISOU 1500 C TYR A 197 3520 3264 4199 961 -167 38 C ATOM 1501 O TYR A 197 -7.072 -21.385 19.760 1.00 28.83 O ANISOU 1501 O TYR A 197 3557 3154 4243 1033 -152 -9 O ATOM 1502 CB TYR A 197 -9.101 -18.882 19.331 1.00 22.39 C ANISOU 1502 CB TYR A 197 2747 2574 3184 778 -47 12 C ATOM 1503 CG TYR A 197 -10.593 -18.837 19.106 1.00 28.34 C ANISOU 1503 CG TYR A 197 3602 3334 3831 669 -35 23 C ATOM 1504 CD1 TYR A 197 -11.272 -19.961 18.656 1.00 26.59 C ANISOU 1504 CD1 TYR A 197 3494 3015 3596 657 -40 2 C ATOM 1505 CD2 TYR A 197 -11.325 -17.683 19.360 1.00 30.00 C ANISOU 1505 CD2 TYR A 197 3793 3644 3962 580 -24 52 C ATOM 1506 CE1 TYR A 197 -12.637 -19.941 18.464 1.00 28.46 C ANISOU 1506 CE1 TYR A 197 3809 3260 3746 553 -37 13 C ATOM 1507 CE2 TYR A 197 -12.697 -17.650 19.167 1.00 27.08 C ANISOU 1507 CE2 TYR A 197 3499 3285 3507 487 -16 61 C ATOM 1508 CZ TYR A 197 -13.346 -18.787 18.722 1.00 28.58 C ANISOU 1508 CZ TYR A 197 3788 3382 3688 471 -24 44 C ATOM 1509 OH TYR A 197 -14.707 -18.778 18.531 1.00 31.38 O ANISOU 1509 OH TYR A 197 4206 3749 3968 374 -23 54 O ATOM 1510 N LEU A 198 -6.319 -19.578 20.873 1.00 25.60 N ANISOU 1510 N LEU A 198 2974 2914 3836 997 -193 57 N ATOM 1511 CA LEU A 198 -4.948 -20.082 20.859 1.00 29.65 C ANISOU 1511 CA LEU A 198 3390 3387 4487 1128 -214 31 C ATOM 1512 C LEU A 198 -4.842 -21.391 21.630 1.00 30.68 C ANISOU 1512 C LEU A 198 3602 3383 4673 1193 -329 77 C ATOM 1513 O LEU A 198 -4.130 -22.311 21.210 1.00 33.40 O ANISOU 1513 O LEU A 198 3931 3639 5120 1309 -325 32 O ATOM 1514 CB LEU A 198 -3.992 -19.034 21.430 1.00 31.12 C ANISOU 1514 CB LEU A 198 3426 3674 4726 1138 -243 54 C ATOM 1515 CG LEU A 198 -3.739 -17.822 20.525 1.00 34.73 C ANISOU 1515 CG LEU A 198 3782 4248 5166 1099 -121 0 C ATOM 1516 CD1 LEU A 198 -2.841 -16.793 21.208 1.00 34.80 C ANISOU 1516 CD1 LEU A 198 3649 4346 5228 1093 -167 30 C ATOM 1517 CD2 LEU A 198 -3.134 -18.268 19.194 1.00 34.38 C ANISOU 1517 CD2 LEU A 198 3691 4186 5187 1180 0 -94 C ATOM 1518 N ARG A 199 -5.561 -21.502 22.751 1.00 31.00 N ANISOU 1518 N ARG A 199 3735 3402 4643 1121 -429 168 N ATOM 1519 CA ARG A 199 -5.553 -22.747 23.513 1.00 31.86 C ANISOU 1519 CA ARG A 199 3942 3376 4789 1168 -544 227 C ATOM 1520 C ARG A 199 -6.277 -23.866 22.775 1.00 30.28 C ANISOU 1520 C ARG A 199 3874 3056 4575 1166 -506 190 C ATOM 1521 O ARG A 199 -5.876 -25.031 22.879 1.00 34.27 O ANISOU 1521 O ARG A 199 4433 3427 5163 1256 -567 194 O ATOM 1522 CB ARG A 199 -6.180 -22.530 24.889 1.00 35.19 C ANISOU 1522 CB ARG A 199 4437 3814 5119 1077 -647 336 C ATOM 1523 CG ARG A 199 -5.364 -21.645 25.816 1.00 42.36 C ANISOU 1523 CG ARG A 199 5238 4810 6046 1090 -721 379 C ATOM 1524 CD ARG A 199 -6.046 -21.507 27.167 1.00 51.52 C ANISOU 1524 CD ARG A 199 6496 5981 7098 1000 -818 482 C ATOM 1525 NE ARG A 199 -5.197 -20.830 28.143 1.00 60.55 N ANISOU 1525 NE ARG A 199 7557 7188 8261 1021 -914 524 N ATOM 1526 CZ ARG A 199 -4.381 -21.458 28.984 1.00 70.01 C ANISOU 1526 CZ ARG A 199 8757 8318 9527 1100 -1052 581 C ATOM 1527 NH1 ARG A 199 -4.305 -22.783 28.971 1.00 74.06 N ANISOU 1527 NH1 ARG A 199 9352 8690 10097 1169 -1105 605 N ATOM 1528 NH2 ARG A 199 -3.643 -20.762 29.839 1.00 71.84 N ANISOU 1528 NH2 ARG A 199 8911 8616 9769 1109 -1145 615 N ATOM 1529 N ILE A 200 -7.342 -23.540 22.036 1.00 27.18 N ANISOU 1529 N ILE A 200 3539 2704 4086 1067 -416 155 N ATOM 1530 CA ILE A 200 -8.063 -24.559 21.274 1.00 31.81 C ANISOU 1530 CA ILE A 200 4250 3180 4655 1054 -385 113 C ATOM 1531 C ILE A 200 -7.165 -25.159 20.200 1.00 31.28 C ANISOU 1531 C ILE A 200 4146 3048 4690 1184 -323 9 C ATOM 1532 O ILE A 200 -7.053 -26.384 20.073 1.00 33.05 O ANISOU 1532 O ILE A 200 4458 3126 4974 1251 -361 -9 O ATOM 1533 CB ILE A 200 -9.343 -23.968 20.654 1.00 28.65 C ANISOU 1533 CB ILE A 200 3899 2853 4134 922 -307 92 C ATOM 1534 CG1 ILE A 200 -10.360 -23.603 21.734 1.00 27.01 C ANISOU 1534 CG1 ILE A 200 3744 2688 3831 797 -365 191 C ATOM 1535 CG2 ILE A 200 -9.951 -24.949 19.664 1.00 26.80 C ANISOU 1535 CG2 ILE A 200 3779 2512 3890 914 -269 28 C ATOM 1536 CD1 ILE A 200 -11.619 -22.945 21.177 1.00 24.21 C ANISOU 1536 CD1 ILE A 200 3416 2414 3368 675 -294 172 C ATOM 1537 N PHE A 201 -6.517 -24.306 19.404 1.00 30.30 N ANISOU 1537 N PHE A 201 3897 3030 4585 1220 -221 -63 N ATOM 1538 CA PHE A 201 -5.670 -24.806 18.324 1.00 32.01 C ANISOU 1538 CA PHE A 201 4072 3202 4887 1342 -138 -170 C ATOM 1539 C PHE A 201 -4.425 -25.503 18.861 1.00 32.89 C ANISOU 1539 C PHE A 201 4113 3234 5149 1492 -210 -164 C ATOM 1540 O PHE A 201 -3.979 -26.501 18.284 1.00 32.97 O ANISOU 1540 O PHE A 201 4156 3133 5240 1602 -189 -234 O ATOM 1541 CB PHE A 201 -5.298 -23.658 17.383 1.00 31.60 C ANISOU 1541 CB PHE A 201 3903 3293 4809 1329 -5 -238 C ATOM 1542 CG PHE A 201 -6.482 -23.050 16.686 1.00 30.03 C ANISOU 1542 CG PHE A 201 3780 3159 4470 1199 64 -255 C ATOM 1543 CD1 PHE A 201 -7.413 -23.854 16.049 1.00 33.19 C ANISOU 1543 CD1 PHE A 201 4328 3472 4812 1161 76 -293 C ATOM 1544 CD2 PHE A 201 -6.676 -21.680 16.685 1.00 32.77 C ANISOU 1544 CD2 PHE A 201 4052 3649 4750 1115 105 -231 C ATOM 1545 CE1 PHE A 201 -8.511 -23.302 15.415 1.00 32.69 C ANISOU 1545 CE1 PHE A 201 4327 3468 4625 1043 125 -306 C ATOM 1546 CE2 PHE A 201 -7.773 -21.120 16.053 1.00 32.85 C ANISOU 1546 CE2 PHE A 201 4129 3713 4639 1005 156 -243 C ATOM 1547 CZ PHE A 201 -8.695 -21.933 15.422 1.00 33.51 C ANISOU 1547 CZ PHE A 201 4351 3716 4666 969 164 -279 C ATOM 1548 N ALA A 202 -3.858 -25.006 19.963 1.00 31.07 N ANISOU 1548 N ALA A 202 3790 3057 4960 1502 -301 -84 N ATOM 1549 CA ALA A 202 -2.725 -25.691 20.576 1.00 33.18 C ANISOU 1549 CA ALA A 202 3992 3244 5373 1644 -395 -65 C ATOM 1550 C ALA A 202 -3.140 -27.049 21.131 1.00 34.89 C ANISOU 1550 C ALA A 202 4369 3282 5607 1672 -509 -15 C ATOM 1551 O ALA A 202 -2.379 -28.017 21.045 1.00 36.02 O ANISOU 1551 O ALA A 202 4507 3305 5875 1813 -548 -46 O ATOM 1552 CB ALA A 202 -2.117 -24.827 21.679 1.00 32.65 C ANISOU 1552 CB ALA A 202 3804 3274 5330 1632 -485 16 C ATOM 1553 N ALA A 203 -4.346 -27.141 21.702 1.00 36.04 N ANISOU 1553 N ALA A 203 4658 3403 5633 1539 -562 63 N ATOM 1554 CA ALA A 203 -4.812 -28.421 22.230 1.00 38.00 C ANISOU 1554 CA ALA A 203 5070 3477 5890 1545 -666 120 C ATOM 1555 C ALA A 203 -5.098 -29.410 21.106 1.00 38.14 C ANISOU 1555 C ALA A 203 5189 3370 5933 1587 -599 24 C ATOM 1556 O ALA A 203 -4.843 -30.610 21.248 1.00 40.44 O ANISOU 1556 O ALA A 203 5567 3491 6306 1675 -673 27 O ATOM 1557 CB ALA A 203 -6.057 -28.211 23.092 1.00 37.50 C ANISOU 1557 CB ALA A 203 5124 3436 5688 1378 -721 227 C ATOM 1558 N ALA A 204 -5.629 -28.925 19.982 1.00 38.40 N ANISOU 1558 N ALA A 204 5220 3477 5892 1525 -465 -64 N ATOM 1559 CA ALA A 204 -5.904 -29.805 18.853 1.00 36.97 C ANISOU 1559 CA ALA A 204 5141 3184 5721 1560 -399 -167 C ATOM 1560 C ALA A 204 -4.616 -30.302 18.215 1.00 39.77 C ANISOU 1560 C ALA A 204 5412 3482 6215 1748 -354 -268 C ATOM 1561 O ALA A 204 -4.508 -31.480 17.854 1.00 38.11 O ANISOU 1561 O ALA A 204 5303 3107 6071 1833 -373 -321 O ATOM 1562 CB ALA A 204 -6.765 -29.078 17.824 1.00 35.61 C ANISOU 1562 CB ALA A 204 4986 3120 5427 1445 -276 -231 C ATOM 1563 N ARG A 205 -3.629 -29.418 18.061 1.00 41.26 N ANISOU 1563 N ARG A 205 5416 3805 6458 1814 -290 -300 N ATOM 1564 CA ARG A 205 -2.360 -29.828 17.473 1.00 45.59 C ANISOU 1564 CA ARG A 205 5858 4317 7148 1995 -234 -397 C ATOM 1565 C ARG A 205 -1.643 -30.835 18.364 1.00 44.80 C ANISOU 1565 C ARG A 205 5764 4068 7190 2129 -378 -347 C ATOM 1566 O ARG A 205 -1.002 -31.770 17.869 1.00 46.69 O ANISOU 1566 O ARG A 205 6012 4185 7543 2280 -362 -430 O ATOM 1567 CB ARG A 205 -1.483 -28.602 17.225 1.00 51.99 C ANISOU 1567 CB ARG A 205 6456 5311 7986 2017 -141 -425 C ATOM 1568 CG ARG A 205 -0.076 -28.929 16.750 1.00 63.55 C ANISOU 1568 CG ARG A 205 7773 6761 9613 2204 -82 -516 C ATOM 1569 CD ARG A 205 0.825 -27.717 16.872 1.00 71.44 C ANISOU 1569 CD ARG A 205 8549 7937 10657 2209 -32 -506 C ATOM 1570 NE ARG A 205 0.718 -27.105 18.194 1.00 78.32 N ANISOU 1570 NE ARG A 205 9383 8863 11511 2131 -172 -373 N ATOM 1571 CZ ARG A 205 1.384 -26.019 18.571 1.00 83.86 C ANISOU 1571 CZ ARG A 205 9910 9708 12244 2111 -170 -340 C ATOM 1572 NH1 ARG A 205 2.212 -25.422 17.724 1.00 87.42 N ANISOU 1572 NH1 ARG A 205 10198 10265 12751 2157 -31 -424 N ATOM 1573 NH2 ARG A 205 1.224 -25.530 19.793 1.00 84.37 N ANISOU 1573 NH2 ARG A 205 9966 9809 12280 2039 -306 -225 N ATOM 1574 N ARG A 206 -1.746 -30.663 19.683 1.00 42.94 N ANISOU 1574 N ARG A 206 5530 3837 6946 2080 -521 -212 N ATOM 1575 CA ARG A 206 -1.099 -31.596 20.598 1.00 45.19 C ANISOU 1575 CA ARG A 206 5835 3980 7357 2200 -677 -148 C ATOM 1576 C ARG A 206 -1.808 -32.946 20.602 1.00 45.26 C ANISOU 1576 C ARG A 206 6062 3776 7358 2199 -744 -136 C ATOM 1577 O ARG A 206 -1.154 -33.995 20.642 1.00 46.92 O ANISOU 1577 O ARG A 206 6294 3859 7673 2316 -785 -150 O ATOM 1578 CB ARG A 206 -1.041 -30.989 22.002 1.00 49.87 C ANISOU 1578 CB ARG A 206 6384 4643 7921 2135 -813 -5 C ATOM 1579 CG ARG A 206 -1.424 -31.932 23.126 1.00 59.20 C ANISOU 1579 CG ARG A 206 7726 5668 9099 2122 -988 117 C ATOM 1580 CD ARG A 206 -0.518 -31.771 24.333 1.00 67.59 C ANISOU 1580 CD ARG A 206 8691 6774 10216 2165 -1117 218 C ATOM 1581 NE ARG A 206 0.789 -32.391 24.123 1.00 76.79 N ANISOU 1581 NE ARG A 206 9745 7915 11519 2313 -1102 171 N ATOM 1582 CZ ARG A 206 1.663 -32.644 25.094 1.00 81.42 C ANISOU 1582 CZ ARG A 206 10272 8503 12160 2366 -1215 251 C ATOM 1583 NH1 ARG A 206 1.370 -32.334 26.351 1.00 81.86 N ANISOU 1583 NH1 ARG A 206 10379 8587 12138 2277 -1348 378 N ATOM 1584 NH2 ARG A 206 2.829 -33.211 24.810 1.00 83.32 N ANISOU 1584 NH2 ARG A 206 10409 8720 12530 2507 -1194 201 N ATOM 1585 N GLN A 207 -3.141 -32.945 20.535 1.00 42.36 N ANISOU 1585 N GLN A 207 5849 3401 6845 2030 -730 -103 N ATOM 1586 CA GLN A 207 -3.872 -34.209 20.516 1.00 43.80 C ANISOU 1586 CA GLN A 207 6242 3381 7019 2008 -792 -91 C ATOM 1587 C GLN A 207 -3.617 -34.981 19.226 1.00 43.54 C ANISOU 1587 C GLN A 207 6253 3240 7051 2118 -698 -245 C ATOM 1588 O GLN A 207 -3.510 -36.213 19.245 1.00 47.73 O ANISOU 1588 O GLN A 207 6898 3586 7651 2184 -756 -252 O ATOM 1589 CB GLN A 207 -5.364 -33.953 20.707 1.00 41.52 C ANISOU 1589 CB GLN A 207 6083 3127 6564 1792 -789 -24 C ATOM 1590 CG GLN A 207 -5.733 -33.526 22.113 1.00 43.59 C ANISOU 1590 CG GLN A 207 6357 3446 6761 1688 -900 136 C ATOM 1591 CD GLN A 207 -7.213 -33.230 22.258 1.00 47.10 C ANISOU 1591 CD GLN A 207 6908 3939 7048 1478 -878 193 C ATOM 1592 OE1 GLN A 207 -8.044 -33.779 21.531 1.00 50.95 O ANISOU 1592 OE1 GLN A 207 7514 4349 7495 1411 -834 142 O ATOM 1593 NE2 GLN A 207 -7.552 -32.354 23.198 1.00 42.10 N ANISOU 1593 NE2 GLN A 207 6232 3437 6327 1375 -910 294 N ATOM 1594 N LEU A 208 -3.513 -34.279 18.101 1.00 44.17 N ANISOU 1594 N LEU A 208 6243 3447 7091 2116 -537 -362 N ATOM 1595 CA LEU A 208 -3.243 -34.917 16.816 1.00 47.01 C ANISOU 1595 CA LEU A 208 6643 3724 7494 2219 -429 -521 C ATOM 1596 C LEU A 208 -1.844 -35.523 16.772 1.00 47.75 C ANISOU 1596 C LEU A 208 6623 3773 7745 2402 -414 -563 C ATOM 1597 O LEU A 208 -1.664 -36.652 16.317 1.00 48.97 O ANISOU 1597 O LEU A 208 6867 3789 7951 2466 -395 -621 O ATOM 1598 CB LEU A 208 -3.414 -33.911 15.678 1.00 50.14 C ANISOU 1598 CB LEU A 208 6962 4297 7790 2157 -254 -620 C ATOM 1599 CG LEU A 208 -4.856 -33.562 15.297 1.00 54.13 C ANISOU 1599 CG LEU A 208 7595 4850 8123 1956 -223 -606 C ATOM 1600 CD1 LEU A 208 -4.914 -32.252 14.518 1.00 55.52 C ANISOU 1600 CD1 LEU A 208 7657 5237 8201 1888 -80 -656 C ATOM 1601 CD2 LEU A 208 -5.477 -34.690 14.486 1.00 56.49 C ANISOU 1601 CD2 LEU A 208 8089 4976 8400 1952 -214 -695 C ATOM 1602 N ALA A1001 -0.874 -34.861 17.429 1.00 67.13 N ANISOU 1602 N ALA A1001 9148 3855 12505 754 -939 -1354 N ATOM 1603 CA ALA A1001 0.492 -35.329 17.638 1.00 63.80 C ANISOU 1603 CA ALA A1001 8503 3396 12342 478 -967 -1285 C ATOM 1604 C ALA A1001 0.502 -36.588 18.496 1.00 61.59 C ANISOU 1604 C ALA A1001 7989 3370 12040 540 -959 -1383 C ATOM 1605 O ALA A1001 1.213 -37.546 18.195 1.00 60.59 O ANISOU 1605 O ALA A1001 7619 3337 12066 405 -837 -1260 O ATOM 1606 CB ALA A1001 1.338 -34.240 18.276 1.00 67.26 C ANISOU 1606 CB ALA A1001 9063 3562 12931 297 -1221 -1349 C ATOM 1607 N ASP A1002 -0.301 -36.582 19.563 1.00 61.57 N ANISOU 1607 N ASP A1002 8083 3473 11836 772 -1062 -1592 N ATOM 1608 CA ASP A1002 -0.384 -37.751 20.433 1.00 64.97 C ANISOU 1608 CA ASP A1002 8330 4145 12212 859 -1045 -1688 C ATOM 1609 C ASP A1002 -0.969 -38.952 19.699 1.00 60.88 C ANISOU 1609 C ASP A1002 7621 3871 11640 923 -813 -1556 C ATOM 1610 O ASP A1002 -0.554 -40.092 19.937 1.00 57.23 O ANISOU 1610 O ASP A1002 6953 3562 11232 866 -751 -1533 O ATOM 1611 CB ASP A1002 -1.210 -37.421 21.677 1.00 70.09 C ANISOU 1611 CB ASP A1002 9165 4849 12617 1144 -1154 -1910 C ATOM 1612 CG ASP A1002 -0.514 -36.431 22.594 1.00 81.52 C ANISOU 1612 CG ASP A1002 10853 6050 14070 1081 -1437 -2063 C ATOM 1613 OD1 ASP A1002 0.666 -36.108 22.337 1.00 86.35 O ANISOU 1613 OD1 ASP A1002 11409 6470 14931 774 -1575 -1988 O ATOM 1614 OD2 ASP A1002 -1.145 -35.971 23.570 1.00 86.32 O ANISOU 1614 OD2 ASP A1002 11712 6654 14432 1343 -1522 -2238 O ATOM 1615 N LEU A1003 -1.934 -38.718 18.805 1.00 57.72 N ANISOU 1615 N LEU A1003 7310 3494 11129 1042 -713 -1463 N ATOM 1616 CA LEU A1003 -2.491 -39.813 18.016 1.00 57.36 C ANISOU 1616 CA LEU A1003 7132 3634 11028 1077 -560 -1322 C ATOM 1617 C LEU A1003 -1.426 -40.447 17.131 1.00 57.46 C ANISOU 1617 C LEU A1003 7061 3602 11170 859 -440 -1146 C ATOM 1618 O LEU A1003 -1.310 -41.676 17.061 1.00 53.46 O ANISOU 1618 O LEU A1003 6412 3253 10649 842 -351 -1085 O ATOM 1619 CB LEU A1003 -3.655 -39.309 17.165 1.00 61.45 C ANISOU 1619 CB LEU A1003 7789 4130 11429 1229 -541 -1249 C ATOM 1620 CG LEU A1003 -5.008 -39.137 17.853 1.00 63.89 C ANISOU 1620 CG LEU A1003 8082 4573 11620 1516 -580 -1347 C ATOM 1621 CD1 LEU A1003 -6.023 -38.559 16.883 1.00 62.57 C ANISOU 1621 CD1 LEU A1003 8032 4345 11398 1646 -589 -1249 C ATOM 1622 CD2 LEU A1003 -5.487 -40.472 18.398 1.00 64.01 C ANISOU 1622 CD2 LEU A1003 7845 4855 11621 1587 -525 -1339 C ATOM 1623 N GLU A1004 -0.641 -39.618 16.443 1.00 63.23 N ANISOU 1623 N GLU A1004 7892 4108 12026 709 -419 -1045 N ATOM 1624 CA GLU A1004 0.398 -40.139 15.563 1.00 68.97 C ANISOU 1624 CA GLU A1004 8539 4776 12888 547 -246 -839 C ATOM 1625 C GLU A1004 1.553 -40.742 16.352 1.00 68.78 C ANISOU 1625 C GLU A1004 8263 4780 13089 407 -255 -856 C ATOM 1626 O GLU A1004 2.214 -41.667 15.867 1.00 64.88 O ANISOU 1626 O GLU A1004 7645 4346 12660 356 -76 -698 O ATOM 1627 CB GLU A1004 0.900 -39.038 14.629 1.00 75.16 C ANISOU 1627 CB GLU A1004 9482 5303 13771 438 -192 -692 C ATOM 1628 CG GLU A1004 -0.154 -38.518 13.658 1.00 80.11 C ANISOU 1628 CG GLU A1004 10388 5881 14169 583 -174 -647 C ATOM 1629 CD GLU A1004 -0.647 -39.587 12.691 1.00 83.06 C ANISOU 1629 CD GLU A1004 10829 6381 14349 685 -40 -521 C ATOM 1630 OE1 GLU A1004 0.119 -40.530 12.390 1.00 82.64 O ANISOU 1630 OE1 GLU A1004 10676 6378 14344 624 118 -397 O ATOM 1631 OE2 GLU A1004 -1.806 -39.484 12.233 1.00 83.92 O ANISOU 1631 OE2 GLU A1004 11105 6520 14259 837 -111 -539 O ATOM 1632 N ASP A1005 1.810 -40.241 17.564 1.00 70.53 N ANISOU 1632 N ASP A1005 8439 4957 13404 365 -473 -1039 N ATOM 1633 CA ASP A1005 2.862 -40.821 18.394 1.00 70.28 C ANISOU 1633 CA ASP A1005 8175 5002 13527 231 -540 -1058 C ATOM 1634 C ASP A1005 2.517 -42.245 18.806 1.00 67.35 C ANISOU 1634 C ASP A1005 7687 4967 12936 350 -453 -1089 C ATOM 1635 O ASP A1005 3.358 -43.146 18.717 1.00 67.99 O ANISOU 1635 O ASP A1005 7580 5180 13075 268 -345 -964 O ATOM 1636 CB ASP A1005 3.106 -39.947 19.623 1.00 74.33 C ANISOU 1636 CB ASP A1005 8755 5365 14122 183 -859 -1270 C ATOM 1637 CG ASP A1005 3.975 -38.749 19.316 1.00 82.15 C ANISOU 1637 CG ASP A1005 9776 6047 15389 -50 -984 -1172 C ATOM 1638 OD1 ASP A1005 4.456 -38.653 18.167 1.00 84.28 O ANISOU 1638 OD1 ASP A1005 9969 6232 15821 -172 -775 -919 O ATOM 1639 OD2 ASP A1005 4.177 -37.907 20.218 1.00 86.48 O ANISOU 1639 OD2 ASP A1005 10452 6455 15951 -103 -1286 -1324 O ATOM 1640 N ASN A1006 1.283 -42.469 19.267 1.00 63.04 N ANISOU 1640 N ASN A1006 7242 4563 12149 551 -490 -1233 N ATOM 1641 CA ASN A1006 0.873 -43.826 19.613 1.00 63.05 C ANISOU 1641 CA ASN A1006 7140 4862 11953 641 -410 -1230 C ATOM 1642 C ASN A1006 0.862 -44.730 18.389 1.00 56.43 C ANISOU 1642 C ASN A1006 6296 4084 11062 624 -212 -1021 C ATOM 1643 O ASN A1006 1.163 -45.923 18.494 1.00 52.34 O ANISOU 1643 O ASN A1006 5683 3747 10458 615 -137 -960 O ATOM 1644 CB ASN A1006 -0.501 -43.813 20.281 1.00 68.48 C ANISOU 1644 CB ASN A1006 7903 5683 12435 856 -461 -1366 C ATOM 1645 CG ASN A1006 -0.462 -43.228 21.680 1.00 74.19 C ANISOU 1645 CG ASN A1006 8687 6387 13113 943 -630 -1582 C ATOM 1646 OD1 ASN A1006 0.565 -43.277 22.357 1.00 78.98 O ANISOU 1646 OD1 ASN A1006 9246 6962 13801 829 -748 -1644 O ATOM 1647 ND2 ASN A1006 -1.585 -42.679 22.124 1.00 73.09 N ANISOU 1647 ND2 ASN A1006 8673 6262 12836 1170 -653 -1689 N ATOM 1648 N TRP A1007 0.524 -44.180 17.221 1.00 56.80 N ANISOU 1648 N TRP A1007 6495 3955 11131 638 -139 -913 N ATOM 1649 CA TRP A1007 0.563 -44.965 15.994 1.00 54.23 C ANISOU 1649 CA TRP A1007 6261 3627 10716 650 29 -717 C ATOM 1650 C TRP A1007 1.995 -45.316 15.608 1.00 55.36 C ANISOU 1650 C TRP A1007 6308 3737 10988 542 202 -552 C ATOM 1651 O TRP A1007 2.271 -46.445 15.192 1.00 54.99 O ANISOU 1651 O TRP A1007 6279 3798 10818 586 335 -436 O ATOM 1652 CB TRP A1007 -0.132 -44.199 14.869 1.00 52.73 C ANISOU 1652 CB TRP A1007 6307 3233 10497 713 41 -646 C ATOM 1653 CG TRP A1007 -0.090 -44.893 13.549 1.00 54.12 C ANISOU 1653 CG TRP A1007 6678 3371 10516 749 184 -448 C ATOM 1654 CD1 TRP A1007 0.652 -44.539 12.460 1.00 56.73 C ANISOU 1654 CD1 TRP A1007 7163 3533 10859 724 365 -265 C ATOM 1655 CD2 TRP A1007 -0.818 -46.070 13.173 1.00 50.76 C ANISOU 1655 CD2 TRP A1007 6360 3047 9878 834 147 -405 C ATOM 1656 NE1 TRP A1007 0.428 -45.418 11.429 1.00 56.95 N ANISOU 1656 NE1 TRP A1007 7438 3558 10640 823 447 -131 N ATOM 1657 CE2 TRP A1007 -0.471 -46.366 11.842 1.00 51.39 C ANISOU 1657 CE2 TRP A1007 6720 3004 9802 875 286 -219 C ATOM 1658 CE3 TRP A1007 -1.734 -46.896 13.832 1.00 49.28 C ANISOU 1658 CE3 TRP A1007 6078 3051 9597 871 1 -487 C ATOM 1659 CZ2 TRP A1007 -1.004 -47.455 11.158 1.00 53.07 C ANISOU 1659 CZ2 TRP A1007 7167 3225 9772 957 234 -143 C ATOM 1660 CZ3 TRP A1007 -2.264 -47.973 13.152 1.00 50.20 C ANISOU 1660 CZ3 TRP A1007 6366 3182 9525 910 -53 -386 C ATOM 1661 CH2 TRP A1007 -1.897 -48.245 11.829 1.00 51.32 C ANISOU 1661 CH2 TRP A1007 6832 3134 9532 958 41 -231 C ATOM 1662 N GLU A1008 2.921 -44.364 15.745 1.00 60.06 N ANISOU 1662 N GLU A1008 6801 4176 11842 409 197 -521 N ATOM 1663 CA GLU A1008 4.319 -44.648 15.436 1.00 64.00 C ANISOU 1663 CA GLU A1008 7122 4665 12529 305 376 -318 C ATOM 1664 C GLU A1008 4.922 -45.615 16.444 1.00 62.44 C ANISOU 1664 C GLU A1008 6687 4700 12337 285 320 -374 C ATOM 1665 O GLU A1008 5.699 -46.502 16.072 1.00 63.89 O ANISOU 1665 O GLU A1008 6773 4982 12521 315 515 -201 O ATOM 1666 CB GLU A1008 5.125 -43.351 15.395 1.00 69.92 C ANISOU 1666 CB GLU A1008 7775 5178 13614 122 338 -241 C ATOM 1667 CG GLU A1008 4.800 -42.450 14.223 1.00 77.41 C ANISOU 1667 CG GLU A1008 8963 5872 14577 136 457 -114 C ATOM 1668 CD GLU A1008 5.482 -41.103 14.333 1.00 88.16 C ANISOU 1668 CD GLU A1008 10247 6971 16278 -74 361 -56 C ATOM 1669 OE1 GLU A1008 6.306 -40.932 15.257 1.00 92.03 O ANISOU 1669 OE1 GLU A1008 10478 7474 17015 -246 193 -90 O ATOM 1670 OE2 GLU A1008 5.191 -40.214 13.503 1.00 92.74 O ANISOU 1670 OE2 GLU A1008 11045 7312 16881 -76 422 28 O ATOM 1671 N THR A1009 4.577 -45.462 17.725 1.00 60.42 N ANISOU 1671 N THR A1009 6369 4525 12062 268 65 -609 N ATOM 1672 CA THR A1009 5.102 -46.359 18.748 1.00 61.72 C ANISOU 1672 CA THR A1009 6350 4896 12204 264 -17 -676 C ATOM 1673 C THR A1009 4.596 -47.783 18.547 1.00 59.26 C ANISOU 1673 C THR A1009 6116 4796 11606 407 111 -645 C ATOM 1674 O THR A1009 5.322 -48.752 18.803 1.00 59.12 O ANISOU 1674 O THR A1009 5968 4920 11573 421 171 -579 O ATOM 1675 CB THR A1009 4.726 -45.840 20.137 1.00 64.76 C ANISOU 1675 CB THR A1009 6750 5291 12565 260 -312 -939 C ATOM 1676 OG1 THR A1009 5.264 -44.523 20.313 1.00 71.16 O ANISOU 1676 OG1 THR A1009 7544 5854 13641 112 -485 -969 O ATOM 1677 CG2 THR A1009 5.278 -46.752 21.224 1.00 65.83 C ANISOU 1677 CG2 THR A1009 6738 5622 12654 268 -417 -1012 C ATOM 1678 N LEU A1010 3.355 -47.930 18.082 1.00 56.52 N ANISOU 1678 N LEU A1010 5979 4453 11042 510 127 -679 N ATOM 1679 CA LEU A1010 2.820 -49.260 17.818 1.00 53.15 C ANISOU 1679 CA LEU A1010 5657 4176 10363 609 195 -630 C ATOM 1680 C LEU A1010 3.581 -49.948 16.690 1.00 52.75 C ANISOU 1680 C LEU A1010 5693 4075 10276 652 421 -409 C ATOM 1681 O LEU A1010 3.901 -51.139 16.785 1.00 53.31 O ANISOU 1681 O LEU A1010 5773 4271 10210 714 480 -356 O ATOM 1682 CB LEU A1010 1.331 -49.164 17.488 1.00 55.20 C ANISOU 1682 CB LEU A1010 6091 4420 10461 679 118 -676 C ATOM 1683 CG LEU A1010 0.569 -50.477 17.315 1.00 59.26 C ANISOU 1683 CG LEU A1010 6714 5060 10741 737 100 -625 C ATOM 1684 CD1 LEU A1010 0.547 -51.252 18.619 1.00 59.40 C ANISOU 1684 CD1 LEU A1010 6582 5301 10687 736 28 -724 C ATOM 1685 CD2 LEU A1010 -0.847 -50.208 16.824 1.00 60.35 C ANISOU 1685 CD2 LEU A1010 6975 5148 10806 779 -6 -620 C ATOM 1686 N ASN A1011 3.892 -49.216 15.618 1.00 53.07 N ANISOU 1686 N ASN A1011 5829 3920 10417 647 566 -267 N ATOM 1687 CA ASN A1011 4.592 -49.818 14.489 1.00 55.31 C ANISOU 1687 CA ASN A1011 6250 4139 10625 749 834 -34 C ATOM 1688 C ASN A1011 6.083 -49.978 14.750 1.00 58.45 C ANISOU 1688 C ASN A1011 6358 4605 11244 720 999 107 C ATOM 1689 O ASN A1011 6.683 -50.963 14.302 1.00 49.68 O ANISOU 1689 O ASN A1011 5307 3555 10015 860 1202 261 O ATOM 1690 CB ASN A1011 4.366 -48.986 13.228 1.00 57.54 C ANISOU 1690 CB ASN A1011 6772 4182 10909 784 960 94 C ATOM 1691 CG ASN A1011 2.941 -49.073 12.728 1.00 60.93 C ANISOU 1691 CG ASN A1011 7518 4539 11095 854 800 10 C ATOM 1692 OD1 ASN A1011 2.296 -50.118 12.842 1.00 58.89 O ANISOU 1692 OD1 ASN A1011 7382 4379 10614 913 690 -39 O ATOM 1693 ND2 ASN A1011 2.436 -47.973 12.175 1.00 64.05 N ANISOU 1693 ND2 ASN A1011 8038 4747 11550 837 763 10 N ATOM 1694 N ASP A1012 6.694 -49.033 15.467 1.00 50.61 N ANISOU 1694 N ASP A1012 5063 3590 10575 551 895 68 N ATOM 1695 CA ASP A1012 8.115 -49.139 15.780 1.00 54.67 C ANISOU 1695 CA ASP A1012 5231 4171 11369 491 994 225 C ATOM 1696 C ASP A1012 8.397 -50.357 16.649 1.00 51.67 C ANISOU 1696 C ASP A1012 4739 4020 10872 565 918 149 C ATOM 1697 O ASP A1012 9.326 -51.126 16.374 1.00 52.84 O ANISOU 1697 O ASP A1012 4770 4258 11050 674 1128 342 O ATOM 1698 CB ASP A1012 8.596 -47.864 16.470 1.00 58.45 C ANISOU 1698 CB ASP A1012 5444 4540 12224 256 784 174 C ATOM 1699 CG ASP A1012 8.682 -46.693 15.521 1.00 65.57 C ANISOU 1699 CG ASP A1012 6409 5196 13307 170 914 333 C ATOM 1700 OD1 ASP A1012 8.910 -46.932 14.317 1.00 68.53 O ANISOU 1700 OD1 ASP A1012 6912 5516 13611 295 1254 577 O ATOM 1701 OD2 ASP A1012 8.520 -45.539 15.974 1.00 68.29 O ANISOU 1701 OD2 ASP A1012 6722 5382 13841 -3 677 216 O ATOM 1702 N ASN A1013 7.607 -50.549 17.705 1.00 50.81 N ANISOU 1702 N ASN A1013 4675 4008 10621 534 640 -114 N ATOM 1703 CA ASN A1013 7.831 -51.690 18.584 1.00 53.09 C ANISOU 1703 CA ASN A1013 4891 4501 10781 602 557 -188 C ATOM 1704 C ASN A1013 7.500 -53.014 17.909 1.00 50.91 C ANISOU 1704 C ASN A1013 4875 4290 10176 790 732 -102 C ATOM 1705 O ASN A1013 8.055 -54.046 18.300 1.00 51.01 O ANISOU 1705 O ASN A1013 4831 4440 10110 883 760 -67 O ATOM 1706 CB ASN A1013 7.025 -51.524 19.869 1.00 53.31 C ANISOU 1706 CB ASN A1013 4941 4601 10713 545 254 -466 C ATOM 1707 CG ASN A1013 7.652 -50.524 20.818 1.00 57.69 C ANISOU 1707 CG ASN A1013 5272 5096 11553 394 16 -568 C ATOM 1708 OD1 ASN A1013 8.874 -50.454 20.938 1.00 64.30 O ANISOU 1708 OD1 ASN A1013 5841 5929 12661 320 7 -443 O ATOM 1709 ND2 ASN A1013 6.819 -49.744 21.498 1.00 55.63 N ANISOU 1709 ND2 ASN A1013 5128 4772 11236 360 -194 -783 N ATOM 1710 N LEU A1014 6.621 -53.008 16.905 1.00 49.57 N ANISOU 1710 N LEU A1014 5023 4003 9809 855 817 -66 N ATOM 1711 CA LEU A1014 6.404 -54.214 16.113 1.00 50.52 C ANISOU 1711 CA LEU A1014 5462 4116 9619 1033 951 38 C ATOM 1712 C LEU A1014 7.669 -54.615 15.365 1.00 53.35 C ANISOU 1712 C LEU A1014 5795 4455 10022 1196 1268 288 C ATOM 1713 O LEU A1014 8.012 -55.801 15.304 1.00 54.43 O ANISOU 1713 O LEU A1014 6061 4662 9959 1366 1355 353 O ATOM 1714 CB LEU A1014 5.249 -54.004 15.137 1.00 53.62 C ANISOU 1714 CB LEU A1014 6214 4342 9818 1058 922 37 C ATOM 1715 CG LEU A1014 3.852 -54.271 15.691 1.00 56.60 C ANISOU 1715 CG LEU A1014 6690 4774 10042 984 647 -137 C ATOM 1716 CD1 LEU A1014 2.797 -53.927 14.652 1.00 58.33 C ANISOU 1716 CD1 LEU A1014 7211 4812 10139 1000 588 -107 C ATOM 1717 CD2 LEU A1014 3.731 -55.726 16.122 1.00 56.35 C ANISOU 1717 CD2 LEU A1014 6769 4860 9781 1042 578 -149 C ATOM 1718 N LYS A1015 8.375 -53.639 14.787 1.00 55.42 N ANISOU 1718 N LYS A1015 5895 4617 10546 1164 1461 453 N ATOM 1719 CA LYS A1015 9.639 -53.939 14.123 1.00 59.57 C ANISOU 1719 CA LYS A1015 6318 5149 11166 1336 1818 744 C ATOM 1720 C LYS A1015 10.703 -54.376 15.121 1.00 61.06 C ANISOU 1720 C LYS A1015 6083 5539 11580 1320 1783 775 C ATOM 1721 O LYS A1015 11.574 -55.186 14.782 1.00 55.86 O ANISOU 1721 O LYS A1015 5393 4954 10879 1544 2042 979 O ATOM 1722 CB LYS A1015 10.125 -52.723 13.333 1.00 62.06 C ANISOU 1722 CB LYS A1015 6511 5311 11757 1271 2037 949 C ATOM 1723 CG LYS A1015 9.179 -52.266 12.238 1.00 65.96 C ANISOU 1723 CG LYS A1015 7452 5586 12022 1323 2092 949 C ATOM 1724 CD LYS A1015 9.686 -50.993 11.575 1.00 74.53 C ANISOU 1724 CD LYS A1015 8404 6512 13402 1234 2297 1155 C ATOM 1725 CE LYS A1015 8.728 -50.508 10.497 1.00 78.45 C ANISOU 1725 CE LYS A1015 9376 6775 13655 1300 2326 1147 C ATOM 1726 NZ LYS A1015 8.566 -51.509 9.405 1.00 81.91 N ANISOU 1726 NZ LYS A1015 10329 7132 13660 1625 2550 1269 N ATOM 1727 N VAL A1016 10.653 -53.848 16.347 1.00 53.43 N ANISOU 1727 N VAL A1016 4816 4648 10836 1087 1457 580 N ATOM 1728 CA VAL A1016 11.611 -54.240 17.378 1.00 62.26 C ANISOU 1728 CA VAL A1016 5557 5937 12160 1061 1342 585 C ATOM 1729 C VAL A1016 11.464 -55.722 17.708 1.00 59.72 C ANISOU 1729 C VAL A1016 5441 5755 11497 1263 1330 519 C ATOM 1730 O VAL A1016 12.458 -56.434 17.895 1.00 54.83 O ANISOU 1730 O VAL A1016 4628 5258 10948 1407 1439 661 O ATOM 1731 CB VAL A1016 11.432 -53.358 18.629 1.00 54.27 C ANISOU 1731 CB VAL A1016 4318 4927 11376 793 941 351 C ATOM 1732 CG1 VAL A1016 12.259 -53.889 19.788 1.00 61.47 C ANISOU 1732 CG1 VAL A1016 4932 6000 12423 781 739 310 C ATOM 1733 CG2 VAL A1016 11.806 -51.917 18.322 1.00 64.67 C ANISOU 1733 CG2 VAL A1016 5419 6077 13077 586 932 453 C ATOM 1734 N ILE A1017 10.223 -56.209 17.773 1.00 54.62 N ANISOU 1734 N ILE A1017 5178 5084 10492 1275 1192 324 N ATOM 1735 CA ILE A1017 9.981 -57.610 18.106 1.00 53.23 C ANISOU 1735 CA ILE A1017 5234 5004 9987 1428 1143 263 C ATOM 1736 C ILE A1017 10.453 -58.522 16.979 1.00 54.38 C ANISOU 1736 C ILE A1017 5654 5093 9915 1721 1464 487 C ATOM 1737 O ILE A1017 10.992 -59.607 17.227 1.00 57.52 O ANISOU 1737 O ILE A1017 6096 5583 10175 1907 1515 539 O ATOM 1738 CB ILE A1017 8.489 -57.825 18.427 1.00 48.31 C ANISOU 1738 CB ILE A1017 4910 4353 9091 1330 909 46 C ATOM 1739 CG1 ILE A1017 8.094 -57.011 19.659 1.00 48.14 C ANISOU 1739 CG1 ILE A1017 4649 4405 9239 1120 634 -167 C ATOM 1740 CG2 ILE A1017 8.183 -59.306 18.628 1.00 47.08 C ANISOU 1740 CG2 ILE A1017 5042 4252 8594 1462 859 23 C ATOM 1741 CD1 ILE A1017 6.606 -57.003 19.944 1.00 48.64 C ANISOU 1741 CD1 ILE A1017 4926 4456 9099 1036 461 -331 C ATOM 1742 N GLU A1018 10.274 -58.091 15.727 1.00 54.91 N ANISOU 1742 N GLU A1018 5950 4992 9922 1799 1688 626 N ATOM 1743 CA GLU A1018 10.612 -58.945 14.592 1.00 58.44 C ANISOU 1743 CA GLU A1018 6782 5341 10080 2128 1995 828 C ATOM 1744 C GLU A1018 12.109 -59.211 14.513 1.00 64.21 C ANISOU 1744 C GLU A1018 7202 6190 11004 2350 2316 1087 C ATOM 1745 O GLU A1018 12.529 -60.346 14.261 1.00 67.26 O ANISOU 1745 O GLU A1018 7825 6597 11134 2655 2474 1186 O ATOM 1746 CB GLU A1018 10.115 -58.312 13.295 1.00 61.74 C ANISOU 1746 CB GLU A1018 7535 5535 10387 2175 2157 923 C ATOM 1747 CG GLU A1018 8.608 -58.250 13.182 1.00 66.30 C ANISOU 1747 CG GLU A1018 8473 5983 10736 2021 1846 713 C ATOM 1748 CD GLU A1018 8.149 -57.486 11.958 1.00 76.49 C ANISOU 1748 CD GLU A1018 10063 7046 11954 2055 1962 800 C ATOM 1749 OE1 GLU A1018 9.006 -57.109 11.130 1.00 82.32 O ANISOU 1749 OE1 GLU A1018 10799 7716 12765 2228 2327 1037 O ATOM 1750 OE2 GLU A1018 6.928 -57.258 11.827 1.00 77.24 O ANISOU 1750 OE2 GLU A1018 10386 7033 11928 1917 1694 652 O ATOM 1751 N LYS A1019 12.932 -58.184 14.722 1.00 65.66 N ANISOU 1751 N LYS A1019 6853 6442 11653 2208 2406 1218 N ATOM 1752 CA LYS A1019 14.378 -58.327 14.635 1.00 67.94 C ANISOU 1752 CA LYS A1019 6739 6857 12218 2392 2714 1521 C ATOM 1753 C LYS A1019 15.029 -58.515 16.001 1.00 66.83 C ANISOU 1753 C LYS A1019 6106 6923 12365 2262 2443 1441 C ATOM 1754 O LYS A1019 16.245 -58.335 16.132 1.00 69.71 O ANISOU 1754 O LYS A1019 5972 7405 13109 2305 2594 1690 O ATOM 1755 CB LYS A1019 14.988 -57.126 13.911 1.00 74.88 C ANISOU 1755 CB LYS A1019 7313 7663 13474 2316 2998 1795 C ATOM 1756 CG LYS A1019 14.712 -55.787 14.560 1.00 77.92 C ANISOU 1756 CG LYS A1019 7355 8006 14243 1885 2678 1651 C ATOM 1757 CD LYS A1019 15.308 -54.658 13.738 1.00 87.60 C ANISOU 1757 CD LYS A1019 8334 9124 15824 1811 2975 1957 C ATOM 1758 CE LYS A1019 14.792 -54.689 12.308 1.00 92.47 C ANISOU 1758 CE LYS A1019 9502 9555 16077 2051 3331 2079 C ATOM 1759 NZ LYS A1019 15.397 -53.613 11.471 1.00 97.72 N ANISOU 1759 NZ LYS A1019 9954 10108 17069 2001 3670 2413 N ATOM 1760 N ALA A1020 14.251 -58.875 17.017 1.00 65.30 N ANISOU 1760 N ALA A1020 6039 6771 12000 2108 2042 1120 N ATOM 1761 CA ALA A1020 14.812 -59.214 18.315 1.00 70.86 C ANISOU 1761 CA ALA A1020 6396 7650 12879 2039 1770 1026 C ATOM 1762 C ALA A1020 15.463 -60.592 18.264 1.00 74.15 C ANISOU 1762 C ALA A1020 6919 8174 13081 2396 1943 1154 C ATOM 1763 O ALA A1020 15.098 -61.445 17.450 1.00 71.57 O ANISOU 1763 O ALA A1020 7087 7761 12344 2662 2156 1199 O ATOM 1764 CB ALA A1020 13.731 -59.184 19.396 1.00 55.67 C ANISOU 1764 CB ALA A1020 4634 5729 10788 1807 1339 664 C ATOM 1765 N ASP A1021 16.441 -60.807 19.146 1.00 81.19 N ANISOU 1765 N ASP A1021 7371 9233 14246 2411 1819 1211 N ATOM 1766 CA ASP A1021 17.150 -62.077 19.201 1.00 88.63 C ANISOU 1766 CA ASP A1021 8418 10305 14952 2717 1930 1317 C ATOM 1767 C ASP A1021 16.949 -62.844 20.500 1.00 86.31 C ANISOU 1767 C ASP A1021 8135 10090 14567 2727 1575 1091 C ATOM 1768 O ASP A1021 17.326 -64.020 20.562 1.00 89.15 O ANISOU 1768 O ASP A1021 8700 10524 14648 2996 1638 1133 O ATOM 1769 CB ASP A1021 18.656 -61.864 18.975 1.00101.63 C ANISOU 1769 CB ASP A1021 9606 12104 16907 2765 2117 1633 C ATOM 1770 CG ASP A1021 19.307 -61.066 20.087 1.00110.47 C ANISOU 1770 CG ASP A1021 10124 13318 18531 2462 1760 1607 C ATOM 1771 OD1 ASP A1021 18.626 -60.200 20.676 1.00110.24 O ANISOU 1771 OD1 ASP A1021 10003 13194 18690 2167 1457 1397 O ATOM 1772 OD2 ASP A1021 20.502 -61.308 20.373 1.00117.07 O ANISOU 1772 OD2 ASP A1021 10609 14307 19565 2522 1756 1794 O ATOM 1773 N ASN A1022 16.373 -62.228 21.531 1.00 81.68 N ANISOU 1773 N ASN A1022 7458 9504 14073 2391 1168 823 N ATOM 1774 CA ASN A1022 16.108 -62.908 22.790 1.00 78.05 C ANISOU 1774 CA ASN A1022 7109 9120 13426 2359 816 590 C ATOM 1775 C ASN A1022 14.712 -62.545 23.271 1.00 71.38 C ANISOU 1775 C ASN A1022 6578 8190 12354 2102 570 292 C ATOM 1776 O ASN A1022 14.065 -61.633 22.749 1.00 68.34 O ANISOU 1776 O ASN A1022 6236 7698 12030 1927 618 255 O ATOM 1777 CB ASN A1022 17.155 -62.555 23.854 1.00 80.47 C ANISOU 1777 CB ASN A1022 6888 9549 14137 2272 531 610 C ATOM 1778 CG ASN A1022 17.248 -61.068 24.104 1.00 79.75 C ANISOU 1778 CG ASN A1022 6434 9395 14471 1934 330 574 C ATOM 1779 OD1 ASN A1022 16.455 -60.504 24.856 1.00 76.51 O ANISOU 1779 OD1 ASN A1022 6167 8919 13985 1701 21 303 O ATOM 1780 ND2 ASN A1022 18.221 -60.421 23.474 1.00 84.04 N ANISOU 1780 ND2 ASN A1022 6519 9948 15465 1918 515 866 N ATOM 1781 N ALA A1023 14.252 -63.271 24.292 1.00 67.10 N ANISOU 1781 N ALA A1023 6248 7699 11548 2099 321 98 N ATOM 1782 CA ALA A1023 12.909 -63.059 24.821 1.00 62.00 C ANISOU 1782 CA ALA A1023 5884 7001 10673 1901 132 -144 C ATOM 1783 C ALA A1023 12.801 -61.772 25.627 1.00 61.96 C ANISOU 1783 C ALA A1023 5622 6989 10932 1651 -129 -302 C ATOM 1784 O ALA A1023 11.711 -61.197 25.717 1.00 63.29 O ANISOU 1784 O ALA A1023 5956 7093 10999 1497 -189 -448 O ATOM 1785 CB ALA A1023 12.486 -64.250 25.679 1.00 60.23 C ANISOU 1785 CB ALA A1023 5965 6831 10088 1987 -16 -259 C ATOM 1786 N ALA A1024 13.905 -61.303 26.212 1.00 61.52 N ANISOU 1786 N ALA A1024 5175 6981 11218 1618 -305 -265 N ATOM 1787 CA ALA A1024 13.850 -60.082 27.010 1.00 60.12 C ANISOU 1787 CA ALA A1024 4826 6746 11272 1386 -616 -426 C ATOM 1788 C ALA A1024 13.561 -58.865 26.142 1.00 59.64 C ANISOU 1788 C ALA A1024 4666 6557 11438 1217 -491 -375 C ATOM 1789 O ALA A1024 12.828 -57.959 26.558 1.00 60.66 O ANISOU 1789 O ALA A1024 4895 6595 11557 1054 -664 -560 O ATOM 1790 CB ALA A1024 15.156 -59.893 27.780 1.00 63.32 C ANISOU 1790 CB ALA A1024 4842 7195 12021 1369 -900 -375 C ATOM 1791 N GLN A1025 14.133 -58.821 24.936 1.00 58.65 N ANISOU 1791 N GLN A1025 4373 6414 11498 1282 -174 -114 N ATOM 1792 CA GLN A1025 13.860 -57.708 24.033 1.00 57.55 C ANISOU 1792 CA GLN A1025 4178 6138 11549 1137 -26 -41 C ATOM 1793 C GLN A1025 12.413 -57.728 23.563 1.00 55.99 C ANISOU 1793 C GLN A1025 4411 5868 10996 1131 80 -177 C ATOM 1794 O GLN A1025 11.782 -56.673 23.428 1.00 54.42 O ANISOU 1794 O GLN A1025 4251 5552 10873 968 18 -268 O ATOM 1795 CB GLN A1025 14.814 -57.752 22.840 1.00 59.08 C ANISOU 1795 CB GLN A1025 4130 6335 11983 1255 341 303 C ATOM 1796 CG GLN A1025 16.273 -57.554 23.211 1.00 68.43 C ANISOU 1796 CG GLN A1025 4774 7594 13633 1229 247 505 C ATOM 1797 CD GLN A1025 17.204 -57.698 22.023 1.00 75.41 C ANISOU 1797 CD GLN A1025 5401 8512 14738 1404 693 899 C ATOM 1798 OE1 GLN A1025 16.774 -58.026 20.918 1.00 77.68 O ANISOU 1798 OE1 GLN A1025 5994 8754 14767 1583 1073 1000 O ATOM 1799 NE2 GLN A1025 18.488 -57.452 22.246 1.00 80.84 N ANISOU 1799 NE2 GLN A1025 5606 9279 15831 1343 636 1128 N ATOM 1800 N VAL A1026 11.869 -58.920 23.310 1.00 56.75 N ANISOU 1800 N VAL A1026 4833 6016 10715 1303 213 -179 N ATOM 1801 CA VAL A1026 10.464 -59.026 22.933 1.00 52.88 C ANISOU 1801 CA VAL A1026 4718 5456 9917 1273 252 -286 C ATOM 1802 C VAL A1026 9.575 -58.555 24.074 1.00 53.34 C ANISOU 1802 C VAL A1026 4830 5536 9900 1130 -24 -535 C ATOM 1803 O VAL A1026 8.580 -57.852 23.855 1.00 55.76 O ANISOU 1803 O VAL A1026 5251 5766 10169 1032 -36 -618 O ATOM 1804 CB VAL A1026 10.135 -60.469 22.510 1.00 51.59 C ANISOU 1804 CB VAL A1026 4900 5314 9387 1460 382 -221 C ATOM 1805 CG1 VAL A1026 8.670 -60.593 22.146 1.00 44.65 C ANISOU 1805 CG1 VAL A1026 4367 4353 8244 1388 359 -303 C ATOM 1806 CG2 VAL A1026 11.016 -60.887 21.342 1.00 48.59 C ANISOU 1806 CG2 VAL A1026 4534 4891 9035 1670 690 29 C ATOM 1807 N LYS A1027 9.928 -58.914 25.311 1.00 54.18 N ANISOU 1807 N LYS A1027 4871 5743 9972 1149 -241 -648 N ATOM 1808 CA LYS A1027 9.147 -58.467 26.460 1.00 58.66 C ANISOU 1808 CA LYS A1027 5534 6325 10429 1071 -473 -874 C ATOM 1809 C LYS A1027 9.172 -56.949 26.593 1.00 59.60 C ANISOU 1809 C LYS A1027 5509 6325 10810 924 -610 -965 C ATOM 1810 O LYS A1027 8.141 -56.327 26.871 1.00 59.36 O ANISOU 1810 O LYS A1027 5631 6252 10672 883 -659 -1103 O ATOM 1811 CB LYS A1027 9.665 -59.124 27.739 1.00 63.17 C ANISOU 1811 CB LYS A1027 6104 6998 10898 1148 -687 -966 C ATOM 1812 CG LYS A1027 8.974 -58.631 29.002 1.00 66.40 C ANISOU 1812 CG LYS A1027 6657 7410 11162 1120 -912 -1192 C ATOM 1813 CD LYS A1027 9.585 -59.249 30.243 1.00 69.99 C ANISOU 1813 CD LYS A1027 7150 7939 11503 1215 -1143 -1277 C ATOM 1814 CE LYS A1027 8.887 -58.765 31.502 1.00 71.54 C ANISOU 1814 CE LYS A1027 7568 8119 11495 1242 -1336 -1494 C ATOM 1815 NZ LYS A1027 9.473 -59.385 32.722 1.00 73.52 N ANISOU 1815 NZ LYS A1027 7920 8421 11592 1356 -1577 -1581 N ATOM 1816 N ASP A1028 10.342 -56.336 26.391 1.00 64.71 N ANISOU 1816 N ASP A1028 5860 6911 11818 850 -675 -869 N ATOM 1817 CA ASP A1028 10.459 -54.888 26.538 1.00 67.10 C ANISOU 1817 CA ASP A1028 6046 7057 12393 682 -856 -944 C ATOM 1818 C ASP A1028 9.560 -54.152 25.553 1.00 60.60 C ANISOU 1818 C ASP A1028 5345 6123 11558 629 -664 -921 C ATOM 1819 O ASP A1028 8.886 -53.183 25.922 1.00 60.23 O ANISOU 1819 O ASP A1028 5416 5969 11499 563 -805 -1082 O ATOM 1820 CB ASP A1028 11.914 -54.457 26.355 1.00 77.93 C ANISOU 1820 CB ASP A1028 7026 8376 14208 578 -944 -771 C ATOM 1821 CG ASP A1028 12.717 -54.548 27.639 1.00 87.43 C ANISOU 1821 CG ASP A1028 8104 9602 15513 556 -1333 -871 C ATOM 1822 OD1 ASP A1028 12.302 -53.935 28.645 1.00 90.86 O ANISOU 1822 OD1 ASP A1028 8726 9945 15852 506 -1650 -1111 O ATOM 1823 OD2 ASP A1028 13.760 -55.237 27.643 1.00 90.92 O ANISOU 1823 OD2 ASP A1028 8285 10146 16114 616 -1328 -707 O ATOM 1824 N ALA A1029 9.537 -54.593 24.294 1.00 57.18 N ANISOU 1824 N ALA A1029 4926 5696 11106 684 -352 -724 N ATOM 1825 CA ALA A1029 8.710 -53.920 23.298 1.00 54.83 C ANISOU 1825 CA ALA A1029 4769 5276 10788 646 -193 -692 C ATOM 1826 C ALA A1029 7.227 -54.165 23.550 1.00 51.13 C ANISOU 1826 C ALA A1029 4587 4848 9994 698 -214 -844 C ATOM 1827 O ALA A1029 6.401 -53.271 23.335 1.00 54.40 O ANISOU 1827 O ALA A1029 5092 5162 10414 651 -234 -916 O ATOM 1828 CB ALA A1029 9.104 -54.378 21.895 1.00 54.21 C ANISOU 1828 CB ALA A1029 4698 5171 10730 728 133 -437 C ATOM 1829 N LEU A1030 6.871 -55.365 24.013 1.00 49.23 N ANISOU 1829 N LEU A1030 4472 4749 9485 796 -209 -870 N ATOM 1830 CA LEU A1030 5.467 -55.680 24.257 1.00 48.11 C ANISOU 1830 CA LEU A1030 4542 4661 9077 828 -216 -954 C ATOM 1831 C LEU A1030 4.910 -54.884 25.430 1.00 50.49 C ANISOU 1831 C LEU A1030 4854 4976 9352 821 -394 -1154 C ATOM 1832 O LEU A1030 3.751 -54.451 25.398 1.00 48.10 O ANISOU 1832 O LEU A1030 4650 4664 8962 836 -369 -1202 O ATOM 1833 CB LEU A1030 5.304 -57.179 24.506 1.00 46.98 C ANISOU 1833 CB LEU A1030 4529 4645 8677 910 -179 -903 C ATOM 1834 CG LEU A1030 5.391 -58.103 23.294 1.00 46.83 C ANISOU 1834 CG LEU A1030 4657 4579 8557 965 -9 -721 C ATOM 1835 CD1 LEU A1030 5.585 -59.538 23.751 1.00 47.29 C ANISOU 1835 CD1 LEU A1030 4839 4736 8392 1052 -24 -687 C ATOM 1836 CD2 LEU A1030 4.138 -57.977 22.438 1.00 40.49 C ANISOU 1836 CD2 LEU A1030 4037 3690 7658 921 33 -677 C ATOM 1837 N THR A1031 5.716 -54.684 26.477 1.00 54.56 N ANISOU 1837 N THR A1031 5290 5506 9933 824 -583 -1264 N ATOM 1838 CA THR A1031 5.265 -53.887 27.614 1.00 57.68 C ANISOU 1838 CA THR A1031 5784 5874 10259 862 -768 -1467 C ATOM 1839 C THR A1031 5.009 -52.442 27.205 1.00 56.48 C ANISOU 1839 C THR A1031 5634 5540 10285 797 -813 -1523 C ATOM 1840 O THR A1031 4.074 -51.804 27.705 1.00 56.09 O ANISOU 1840 O THR A1031 5739 5466 10108 883 -846 -1650 O ATOM 1841 CB THR A1031 6.290 -53.950 28.745 1.00 62.70 C ANISOU 1841 CB THR A1031 6385 6510 10929 875 -1026 -1574 C ATOM 1842 OG1 THR A1031 7.578 -53.573 28.245 1.00 71.01 O ANISOU 1842 OG1 THR A1031 7192 7462 12327 745 -1114 -1478 O ATOM 1843 CG2 THR A1031 6.365 -55.359 29.320 1.00 58.16 C ANISOU 1843 CG2 THR A1031 5872 6112 10116 977 -992 -1543 C ATOM 1844 N LYS A1032 5.824 -51.909 26.291 1.00 56.98 N ANISOU 1844 N LYS A1032 5536 5472 10641 667 -792 -1410 N ATOM 1845 CA LYS A1032 5.570 -50.566 25.782 1.00 59.52 C ANISOU 1845 CA LYS A1032 5884 5598 11133 593 -822 -1437 C ATOM 1846 C LYS A1032 4.337 -50.530 24.889 1.00 57.86 C ANISOU 1846 C LYS A1032 5791 5398 10795 652 -610 -1378 C ATOM 1847 O LYS A1032 3.635 -49.513 24.846 1.00 59.47 O ANISOU 1847 O LYS A1032 6102 5486 11009 676 -649 -1463 O ATOM 1848 CB LYS A1032 6.791 -50.046 25.024 1.00 62.38 C ANISOU 1848 CB LYS A1032 6025 5817 11861 427 -828 -1283 C ATOM 1849 CG LYS A1032 8.023 -49.846 25.890 1.00 67.44 C ANISOU 1849 CG LYS A1032 6497 6407 12721 327 -1114 -1321 C ATOM 1850 CD LYS A1032 9.179 -49.289 25.076 1.00 72.95 C ANISOU 1850 CD LYS A1032 6906 6970 13842 142 -1090 -1104 C ATOM 1851 CE LYS A1032 10.413 -49.084 25.936 1.00 79.13 C ANISOU 1851 CE LYS A1032 7465 7694 14906 10 -1431 -1108 C ATOM 1852 NZ LYS A1032 11.552 -48.535 25.149 1.00 84.21 N ANISOU 1852 NZ LYS A1032 7753 8219 16024 -191 -1391 -837 N ATOM 1853 N MET A1033 4.054 -51.619 24.170 1.00 54.01 N ANISOU 1853 N MET A1033 5310 5027 10187 684 -417 -1232 N ATOM 1854 CA MET A1033 2.864 -51.649 23.326 1.00 50.83 C ANISOU 1854 CA MET A1033 5024 4616 9673 723 -285 -1165 C ATOM 1855 C MET A1033 1.597 -51.768 24.161 1.00 47.31 C ANISOU 1855 C MET A1033 4660 4294 9022 830 -318 -1265 C ATOM 1856 O MET A1033 0.563 -51.184 23.816 1.00 44.84 O ANISOU 1856 O MET A1033 4400 3942 8695 875 -288 -1266 O ATOM 1857 CB MET A1033 2.949 -52.801 22.326 1.00 52.26 C ANISOU 1857 CB MET A1033 5251 4838 9766 725 -128 -981 C ATOM 1858 CG MET A1033 4.029 -52.627 21.285 1.00 56.71 C ANISOU 1858 CG MET A1033 5763 5277 10507 680 -5 -831 C ATOM 1859 SD MET A1033 4.232 -54.080 20.242 1.00 58.33 S ANISOU 1859 SD MET A1033 6124 5510 10528 765 180 -632 S ATOM 1860 CE MET A1033 2.695 -54.050 19.331 1.00 58.52 C ANISOU 1860 CE MET A1033 6403 5446 10388 776 171 -600 C ATOM 1861 N ARG A1034 1.657 -52.524 25.259 1.00 47.35 N ANISOU 1861 N ARG A1034 4668 4451 8870 891 -365 -1328 N ATOM 1862 CA ARG A1034 0.465 -52.730 26.074 1.00 50.01 C ANISOU 1862 CA ARG A1034 5067 4928 9008 1013 -335 -1371 C ATOM 1863 C ARG A1034 0.038 -51.440 26.763 1.00 53.80 C ANISOU 1863 C ARG A1034 5621 5332 9488 1132 -406 -1533 C ATOM 1864 O ARG A1034 -1.152 -51.104 26.781 1.00 55.78 O ANISOU 1864 O ARG A1034 5892 5631 9672 1245 -319 -1512 O ATOM 1865 CB ARG A1034 0.716 -53.831 27.102 1.00 48.97 C ANISOU 1865 CB ARG A1034 4961 4956 8689 1062 -352 -1386 C ATOM 1866 CG ARG A1034 -0.556 -54.355 27.741 1.00 50.37 C ANISOU 1866 CG ARG A1034 5172 5302 8666 1168 -248 -1334 C ATOM 1867 CD ARG A1034 -0.264 -55.333 28.858 1.00 55.15 C ANISOU 1867 CD ARG A1034 5844 6043 9068 1231 -261 -1354 C ATOM 1868 NE ARG A1034 -1.481 -56.012 29.292 1.00 62.22 N ANISOU 1868 NE ARG A1034 6735 7103 9802 1295 -118 -1225 N ATOM 1869 CZ ARG A1034 -2.338 -55.519 30.179 1.00 68.61 C ANISOU 1869 CZ ARG A1034 7578 7999 10492 1476 -22 -1257 C ATOM 1870 NH1 ARG A1034 -2.112 -54.337 30.736 1.00 72.56 N ANISOU 1870 NH1 ARG A1034 8186 8406 10976 1626 -89 -1450 N ATOM 1871 NH2 ARG A1034 -3.423 -56.208 30.508 1.00 70.40 N ANISOU 1871 NH2 ARG A1034 7741 8391 10617 1517 141 -1076 N ATOM 1872 N ALA A1035 0.995 -50.706 27.334 1.00 57.53 N ANISOU 1872 N ALA A1035 6144 5673 10041 1119 -581 -1683 N ATOM 1873 CA ALA A1035 0.674 -49.430 27.966 1.00 57.67 C ANISOU 1873 CA ALA A1035 6319 5557 10036 1245 -692 -1854 C ATOM 1874 C ALA A1035 0.194 -48.410 26.940 1.00 57.45 C ANISOU 1874 C ALA A1035 6290 5372 10166 1215 -649 -1817 C ATOM 1875 O ALA A1035 -0.712 -47.618 27.223 1.00 59.86 O ANISOU 1875 O ALA A1035 6719 5639 10385 1390 -627 -1893 O ATOM 1876 CB ALA A1035 1.892 -48.903 28.725 1.00 56.65 C ANISOU 1876 CB ALA A1035 6270 5267 9986 1190 -971 -2011 C ATOM 1877 N ALA A1036 0.786 -48.414 25.742 1.00 58.44 N ANISOU 1877 N ALA A1036 6298 5402 10506 1027 -617 -1689 N ATOM 1878 CA ALA A1036 0.356 -47.484 24.704 1.00 59.67 C ANISOU 1878 CA ALA A1036 6485 5393 10795 1001 -574 -1639 C ATOM 1879 C ALA A1036 -0.989 -47.882 24.109 1.00 64.70 C ANISOU 1879 C ALA A1036 7104 6154 11324 1096 -414 -1524 C ATOM 1880 O ALA A1036 -1.749 -47.013 23.667 1.00 66.45 O ANISOU 1880 O ALA A1036 7390 6278 11582 1175 -402 -1529 O ATOM 1881 CB ALA A1036 1.411 -47.393 23.602 1.00 55.46 C ANISOU 1881 CB ALA A1036 5856 4716 10500 798 -552 -1506 C ATOM 1882 N ALA A1037 -1.297 -49.183 24.079 1.00 64.80 N ANISOU 1882 N ALA A1037 7033 6364 11222 1082 -321 -1408 N ATOM 1883 CA ALA A1037 -2.598 -49.615 23.580 1.00 64.26 C ANISOU 1883 CA ALA A1037 6922 6404 11089 1136 -231 -1274 C ATOM 1884 C ALA A1037 -3.719 -49.149 24.500 1.00 67.79 C ANISOU 1884 C ALA A1037 7360 6963 11435 1349 -192 -1333 C ATOM 1885 O ALA A1037 -4.809 -48.802 24.033 1.00 68.44 O ANISOU 1885 O ALA A1037 7391 7059 11553 1431 -150 -1246 O ATOM 1886 CB ALA A1037 -2.627 -51.135 23.425 1.00 61.76 C ANISOU 1886 CB ALA A1037 6551 6238 10678 1049 -185 -1132 C ATOM 1887 N LEU A1038 -3.469 -49.135 25.810 1.00 71.55 N ANISOU 1887 N LEU A1038 7895 7515 11775 1470 -201 -1466 N ATOM 1888 CA LEU A1038 -4.454 -48.620 26.753 1.00 75.48 C ANISOU 1888 CA LEU A1038 8439 8106 12135 1741 -119 -1520 C ATOM 1889 C LEU A1038 -4.520 -47.099 26.731 1.00 79.72 C ANISOU 1889 C LEU A1038 9141 8429 12718 1881 -194 -1670 C ATOM 1890 O LEU A1038 -5.591 -46.527 26.961 1.00 81.60 O ANISOU 1890 O LEU A1038 9393 8715 12896 2124 -92 -1653 O ATOM 1891 CB LEU A1038 -4.132 -49.111 28.164 1.00 76.48 C ANISOU 1891 CB LEU A1038 8663 8352 12046 1861 -105 -1616 C ATOM 1892 CG LEU A1038 -4.050 -50.628 28.320 1.00 75.46 C ANISOU 1892 CG LEU A1038 8410 8419 11843 1740 -36 -1473 C ATOM 1893 CD1 LEU A1038 -3.684 -50.994 29.746 1.00 76.81 C ANISOU 1893 CD1 LEU A1038 8729 8677 11777 1885 -36 -1583 C ATOM 1894 CD2 LEU A1038 -5.364 -51.272 27.914 1.00 76.34 C ANISOU 1894 CD2 LEU A1038 8317 8711 11977 1746 126 -1229 C ATOM 1895 N ASP A1039 -3.394 -46.434 26.465 1.00 83.38 N ANISOU 1895 N ASP A1039 9727 8652 13302 1737 -370 -1794 N ATOM 1896 CA ASP A1039 -3.403 -44.981 26.337 1.00 87.59 C ANISOU 1896 CA ASP A1039 10449 8930 13900 1826 -478 -1923 C ATOM 1897 C ASP A1039 -4.198 -44.547 25.112 1.00 86.66 C ANISOU 1897 C ASP A1039 10256 8758 13913 1822 -402 -1792 C ATOM 1898 O ASP A1039 -4.922 -43.545 25.156 1.00 88.49 O ANISOU 1898 O ASP A1039 10611 8894 14117 2033 -398 -1849 O ATOM 1899 CB ASP A1039 -1.969 -44.453 26.266 1.00 92.32 C ANISOU 1899 CB ASP A1039 11146 9275 14657 1608 -704 -2031 C ATOM 1900 CG ASP A1039 -1.903 -42.937 26.211 1.00100.95 C ANISOU 1900 CG ASP A1039 12479 10056 15820 1667 -864 -2166 C ATOM 1901 OD1 ASP A1039 -2.086 -42.292 27.266 1.00105.35 O ANISOU 1901 OD1 ASP A1039 13301 10522 16204 1890 -974 -2350 O ATOM 1902 OD2 ASP A1039 -1.665 -42.389 25.113 1.00102.60 O ANISOU 1902 OD2 ASP A1039 12657 10090 16238 1507 -881 -2084 O ATOM 1903 N ALA A1040 -4.081 -45.292 24.009 1.00 84.66 N ANISOU 1903 N ALA A1040 9840 8548 13779 1612 -356 -1618 N ATOM 1904 CA ALA A1040 -4.859 -44.979 22.816 1.00 85.54 C ANISOU 1904 CA ALA A1040 9915 8597 13989 1612 -321 -1487 C ATOM 1905 C ALA A1040 -6.314 -45.406 22.951 1.00 86.30 C ANISOU 1905 C ALA A1040 9853 8920 14017 1790 -215 -1359 C ATOM 1906 O ALA A1040 -7.165 -44.914 22.201 1.00 86.62 O ANISOU 1906 O ALA A1040 9868 8909 14134 1867 -221 -1272 O ATOM 1907 CB ALA A1040 -4.228 -45.636 21.587 1.00 83.45 C ANISOU 1907 CB ALA A1040 9609 8269 13831 1363 -321 -1343 C ATOM 1908 N GLN A1041 -6.618 -46.309 23.886 1.00 85.96 N ANISOU 1908 N GLN A1041 9689 9122 13849 1853 -123 -1322 N ATOM 1909 CA GLN A1041 -7.996 -46.735 24.102 1.00 87.32 C ANISOU 1909 CA GLN A1041 9652 9527 13999 2008 -2 -1150 C ATOM 1910 C GLN A1041 -8.822 -45.659 24.797 1.00 90.96 C ANISOU 1910 C GLN A1041 10161 10005 14394 2364 94 -1216 C ATOM 1911 O GLN A1041 -10.040 -45.598 24.603 1.00 94.11 O ANISOU 1911 O GLN A1041 10361 10537 14861 2518 182 -1045 O ATOM 1912 CB GLN A1041 -8.022 -48.030 24.914 1.00 86.54 C ANISOU 1912 CB GLN A1041 9423 9672 13788 1961 92 -1061 C ATOM 1913 CG GLN A1041 -9.382 -48.706 24.969 1.00 88.78 C ANISOU 1913 CG GLN A1041 9420 10197 14117 2024 206 -802 C ATOM 1914 CD GLN A1041 -9.330 -50.070 25.632 1.00 90.12 C ANISOU 1914 CD GLN A1041 9483 10567 14192 1917 280 -685 C ATOM 1915 OE1 GLN A1041 -8.312 -50.457 26.206 1.00 90.30 O ANISOU 1915 OE1 GLN A1041 9664 10569 14079 1857 264 -825 O ATOM 1916 NE2 GLN A1041 -10.430 -50.808 25.552 1.00 91.89 N ANISOU 1916 NE2 GLN A1041 9430 10978 14508 1884 341 -411 N ATOM 1917 N LYS A1042 -8.185 -44.807 25.595 1.00 91.06 N ANISOU 1917 N LYS A1042 10444 9872 14281 2512 61 -1450 N ATOM 1918 CA LYS A1042 -8.888 -43.734 26.287 1.00 93.00 C ANISOU 1918 CA LYS A1042 10840 10087 14408 2903 146 -1541 C ATOM 1919 C LYS A1042 -9.285 -42.622 25.319 1.00 92.18 C ANISOU 1919 C LYS A1042 10805 9776 14445 2965 63 -1545 C ATOM 1920 O LYS A1042 -10.441 -42.204 25.282 1.00 93.34 O ANISOU 1920 O LYS A1042 10846 10016 14603 3245 182 -1438 O ATOM 1921 CB LYS A1042 -8.023 -43.166 27.413 1.00 95.20 C ANISOU 1921 CB LYS A1042 11482 10208 14482 3030 61 -1809 C ATOM 1922 CG LYS A1042 -7.646 -44.180 28.479 1.00 96.26 C ANISOU 1922 CG LYS A1042 11609 10530 14437 3024 130 -1822 C ATOM 1923 CD LYS A1042 -6.821 -43.536 29.583 1.00 99.25 C ANISOU 1923 CD LYS A1042 12402 10708 14600 3169 -23 -2099 C ATOM 1924 CE LYS A1042 -6.450 -44.550 30.656 1.00 99.80 C ANISOU 1924 CE LYS A1042 12501 10954 14466 3186 29 -2113 C ATOM 1925 NZ LYS A1042 -5.654 -43.932 31.753 1.00102.28 N ANISOU 1925 NZ LYS A1042 13265 11044 14552 3336 -181 -2388 N ATOM 1926 N LYS A1059 -18.438 -50.198 20.153 1.00 96.27 N ANISOU 1926 N LYS A1059 8048 11677 16854 1697 -676 1333 N ATOM 1927 CA LYS A1059 -18.553 -51.652 20.122 1.00 94.96 C ANISOU 1927 CA LYS A1059 7760 11553 16770 1330 -846 1555 C ATOM 1928 C LYS A1059 -17.456 -52.260 19.255 1.00 90.88 C ANISOU 1928 C LYS A1059 7753 10728 16051 1037 -1119 1349 C ATOM 1929 O LYS A1059 -16.636 -53.038 19.741 1.00 89.26 O ANISOU 1929 O LYS A1059 7735 10531 15650 909 -1019 1250 O ATOM 1930 CB LYS A1059 -19.933 -52.066 19.614 1.00 97.55 C ANISOU 1930 CB LYS A1059 7636 11959 17470 1174 -1120 1967 C ATOM 1931 CG LYS A1059 -21.067 -51.550 20.479 1.00101.90 C ANISOU 1931 CG LYS A1059 7818 12846 18055 1426 -772 2160 C ATOM 1932 CD LYS A1059 -22.426 -51.893 19.897 1.00105.77 C ANISOU 1932 CD LYS A1059 7967 13387 18835 1226 -1042 2527 C ATOM 1933 CE LYS A1059 -23.536 -51.321 20.754 1.00109.52 C ANISOU 1933 CE LYS A1059 8063 14193 19355 1522 -668 2722 C ATOM 1934 NZ LYS A1059 -24.871 -51.602 20.176 1.00115.43 N ANISOU 1934 NZ LYS A1059 8447 14982 20431 1333 -933 3093 N ATOM 1935 N ASP A1060 -17.445 -51.903 17.968 1.00 90.70 N ANISOU 1935 N ASP A1060 7972 10428 16061 964 -1450 1296 N ATOM 1936 CA ASP A1060 -16.340 -52.310 17.105 1.00 88.77 C ANISOU 1936 CA ASP A1060 8268 9880 15582 777 -1636 1093 C ATOM 1937 C ASP A1060 -15.034 -51.667 17.548 1.00 85.66 C ANISOU 1937 C ASP A1060 8186 9444 14917 941 -1323 751 C ATOM 1938 O ASP A1060 -13.954 -52.221 17.311 1.00 83.49 O ANISOU 1938 O ASP A1060 8260 9026 14436 809 -1332 608 O ATOM 1939 CB ASP A1060 -16.642 -51.950 15.650 1.00 92.13 C ANISOU 1939 CB ASP A1060 8927 10009 16067 724 -2023 1119 C ATOM 1940 CG ASP A1060 -17.993 -52.463 15.189 1.00 99.95 C ANISOU 1940 CG ASP A1060 9585 11018 17374 561 -2410 1468 C ATOM 1941 OD1 ASP A1060 -18.450 -53.500 15.715 1.00102.35 O ANISOU 1941 OD1 ASP A1060 9605 11472 17810 358 -2465 1699 O ATOM 1942 OD2 ASP A1060 -18.600 -51.826 14.301 1.00103.38 O ANISOU 1942 OD2 ASP A1060 10035 11304 17939 625 -2679 1528 O ATOM 1943 N PHE A1061 -15.114 -50.499 18.188 1.00 86.28 N ANISOU 1943 N PHE A1061 8151 9632 15000 1237 -1063 630 N ATOM 1944 CA PHE A1061 -13.924 -49.862 18.742 1.00 82.37 C ANISOU 1944 CA PHE A1061 7922 9089 14286 1371 -811 324 C ATOM 1945 C PHE A1061 -13.401 -50.636 19.945 1.00 78.08 C ANISOU 1945 C PHE A1061 7319 8740 13609 1338 -594 285 C ATOM 1946 O PHE A1061 -12.201 -50.917 20.042 1.00 75.81 O ANISOU 1946 O PHE A1061 7304 8358 13144 1250 -548 102 O ATOM 1947 CB PHE A1061 -14.242 -48.413 19.120 1.00 84.64 C ANISOU 1947 CB PHE A1061 8157 9400 14602 1703 -646 212 C ATOM 1948 CG PHE A1061 -13.401 -47.873 20.246 1.00 83.39 C ANISOU 1948 CG PHE A1061 8135 9292 14257 1880 -373 -34 C ATOM 1949 CD1 PHE A1061 -12.124 -47.395 20.008 1.00 78.75 C ANISOU 1949 CD1 PHE A1061 7907 8479 13535 1826 -378 -287 C ATOM 1950 CD2 PHE A1061 -13.897 -47.828 21.540 1.00 86.66 C ANISOU 1950 CD2 PHE A1061 8328 9965 14636 2109 -121 7 C ATOM 1951 CE1 PHE A1061 -11.355 -46.893 21.041 1.00 78.60 C ANISOU 1951 CE1 PHE A1061 8020 8474 13370 1961 -205 -505 C ATOM 1952 CE2 PHE A1061 -13.130 -47.330 22.576 1.00 85.69 C ANISOU 1952 CE2 PHE A1061 8404 9846 14308 2285 73 -232 C ATOM 1953 CZ PHE A1061 -11.858 -46.862 22.326 1.00 81.24 C ANISOU 1953 CZ PHE A1061 8197 9038 13635 2193 -4 -495 C ATOM 1954 N ARG A1062 -14.292 -50.987 20.876 1.00 78.84 N ANISOU 1954 N ARG A1062 7050 9111 13794 1424 -447 478 N ATOM 1955 CA ARG A1062 -13.871 -51.715 22.069 1.00 78.56 C ANISOU 1955 CA ARG A1062 6981 9258 13608 1421 -229 458 C ATOM 1956 C ARG A1062 -13.415 -53.127 21.724 1.00 68.79 C ANISOU 1956 C ARG A1062 5856 7958 12322 1088 -404 540 C ATOM 1957 O ARG A1062 -12.445 -53.630 22.305 1.00 63.81 O ANISOU 1957 O ARG A1062 5414 7337 11495 1047 -302 396 O ATOM 1958 CB ARG A1062 -15.006 -51.744 23.093 1.00 89.84 C ANISOU 1958 CB ARG A1062 7999 10995 15141 1619 11 695 C ATOM 1959 CG ARG A1062 -14.789 -52.724 24.238 1.00 96.56 C ANISOU 1959 CG ARG A1062 8794 12040 15855 1580 214 763 C ATOM 1960 CD ARG A1062 -15.622 -52.358 25.455 1.00105.63 C ANISOU 1960 CD ARG A1062 9660 13474 16999 1921 579 909 C ATOM 1961 NE ARG A1062 -15.192 -51.089 26.036 1.00110.06 N ANISOU 1961 NE ARG A1062 10466 13993 17359 2296 771 617 N ATOM 1962 CZ ARG A1062 -14.178 -50.962 26.886 1.00110.32 C ANISOU 1962 CZ ARG A1062 10835 13982 17098 2407 887 341 C ATOM 1963 NH1 ARG A1062 -13.484 -52.030 27.258 1.00108.91 N ANISOU 1963 NH1 ARG A1062 10765 13824 16792 2193 862 322 N ATOM 1964 NH2 ARG A1062 -13.855 -49.767 27.362 1.00110.77 N ANISOU 1964 NH2 ARG A1062 11144 13955 16989 2733 993 86 N ATOM 1965 N HIS A1063 -14.094 -53.779 20.776 1.00 65.43 N ANISOU 1965 N HIS A1063 5348 7445 12066 858 -698 768 N ATOM 1966 CA HIS A1063 -13.686 -55.121 20.373 1.00 63.08 C ANISOU 1966 CA HIS A1063 5239 7033 11694 559 -905 841 C ATOM 1967 C HIS A1063 -12.300 -55.119 19.743 1.00 55.58 C ANISOU 1967 C HIS A1063 4762 5841 10515 523 -952 575 C ATOM 1968 O HIS A1063 -11.530 -56.067 19.935 1.00 54.30 O ANISOU 1968 O HIS A1063 4796 5647 10189 404 -949 533 O ATOM 1969 CB HIS A1063 -14.710 -55.717 19.407 1.00 68.23 C ANISOU 1969 CB HIS A1063 5777 7577 12570 325 -1287 1128 C ATOM 1970 CG HIS A1063 -14.456 -57.153 19.067 1.00 71.54 C ANISOU 1970 CG HIS A1063 6413 7859 12910 23 -1535 1234 C ATOM 1971 ND1 HIS A1063 -14.362 -58.140 20.025 1.00 71.66 N ANISOU 1971 ND1 HIS A1063 6328 8031 12869 -78 -1405 1334 N ATOM 1972 CD2 HIS A1063 -14.273 -57.769 17.874 1.00 72.16 C ANISOU 1972 CD2 HIS A1063 6861 7630 12926 -174 -1913 1252 C ATOM 1973 CE1 HIS A1063 -14.134 -59.301 19.438 1.00 71.61 C ANISOU 1973 CE1 HIS A1063 6610 7816 12783 -337 -1702 1407 C ATOM 1974 NE2 HIS A1063 -14.074 -59.104 18.133 1.00 71.77 N ANISOU 1974 NE2 HIS A1063 6933 7548 12786 -389 -2015 1355 N ATOM 1975 N GLY A1064 -11.963 -54.068 18.993 1.00 51.96 N ANISOU 1975 N GLY A1064 4483 5210 10048 637 -978 417 N ATOM 1976 CA GLY A1064 -10.646 -54.001 18.384 1.00 47.92 C ANISOU 1976 CA GLY A1064 4372 4482 9352 619 -971 215 C ATOM 1977 C GLY A1064 -9.530 -53.912 19.406 1.00 47.55 C ANISOU 1977 C GLY A1064 4365 4540 9162 708 -710 15 C ATOM 1978 O GLY A1064 -8.491 -54.563 19.263 1.00 45.00 O ANISOU 1978 O GLY A1064 4270 4133 8693 631 -698 -57 O ATOM 1979 N PHE A1065 -9.728 -53.112 20.456 1.00 50.05 N ANISOU 1979 N PHE A1065 4481 5026 9508 893 -513 -72 N ATOM 1980 CA PHE A1065 -8.710 -52.984 21.492 1.00 51.68 C ANISOU 1980 CA PHE A1065 4751 5307 9576 981 -327 -267 C ATOM 1981 C PHE A1065 -8.706 -54.171 22.446 1.00 54.33 C ANISOU 1981 C PHE A1065 5003 5830 9811 919 -259 -186 C ATOM 1982 O PHE A1065 -7.656 -54.495 23.012 1.00 56.58 O ANISOU 1982 O PHE A1065 5417 6123 9956 919 -191 -323 O ATOM 1983 CB PHE A1065 -8.904 -51.679 22.263 1.00 55.62 C ANISOU 1983 CB PHE A1065 5173 5866 10094 1229 -181 -407 C ATOM 1984 CG PHE A1065 -8.318 -50.480 21.572 1.00 55.75 C ANISOU 1984 CG PHE A1065 5374 5654 10155 1280 -225 -569 C ATOM 1985 CD1 PHE A1065 -6.963 -50.206 21.670 1.00 52.57 C ANISOU 1985 CD1 PHE A1065 5159 5125 9691 1239 -207 -750 C ATOM 1986 CD2 PHE A1065 -9.117 -49.632 20.821 1.00 57.89 C ANISOU 1986 CD2 PHE A1065 5616 5831 10550 1360 -294 -514 C ATOM 1987 CE1 PHE A1065 -6.416 -49.111 21.034 1.00 52.13 C ANISOU 1987 CE1 PHE A1065 5253 4847 9707 1255 -241 -858 C ATOM 1988 CE2 PHE A1065 -8.573 -48.530 20.184 1.00 55.13 C ANISOU 1988 CE2 PHE A1065 5463 5251 10235 1399 -329 -647 C ATOM 1989 CZ PHE A1065 -7.223 -48.270 20.292 1.00 54.01 C ANISOU 1989 CZ PHE A1065 5501 4979 10040 1335 -295 -811 C ATOM 1990 N ASP A1066 -9.855 -54.826 22.636 1.00 55.12 N ANISOU 1990 N ASP A1066 4874 6074 9996 859 -285 56 N ATOM 1991 CA ASP A1066 -9.874 -56.066 23.406 1.00 55.26 C ANISOU 1991 CA ASP A1066 4840 6234 9923 758 -238 175 C ATOM 1992 C ASP A1066 -9.034 -57.140 22.730 1.00 51.05 C ANISOU 1992 C ASP A1066 4583 5533 9280 553 -407 166 C ATOM 1993 O ASP A1066 -8.318 -57.894 23.401 1.00 52.27 O ANISOU 1993 O ASP A1066 4843 5741 9276 534 -339 113 O ATOM 1994 CB ASP A1066 -11.311 -56.553 23.594 1.00 61.49 C ANISOU 1994 CB ASP A1066 5297 7184 10884 691 -253 495 C ATOM 1995 CG ASP A1066 -12.092 -55.704 24.580 1.00 70.33 C ANISOU 1995 CG ASP A1066 6133 8531 12058 965 15 540 C ATOM 1996 OD1 ASP A1066 -11.459 -55.058 25.443 1.00 72.70 O ANISOU 1996 OD1 ASP A1066 6559 8880 12184 1195 214 314 O ATOM 1997 OD2 ASP A1066 -13.339 -55.689 24.495 1.00 75.49 O ANISOU 1997 OD2 ASP A1066 6451 9305 12928 965 16 814 O ATOM 1998 N ILE A1067 -9.112 -57.229 21.400 1.00 47.03 N ANISOU 1998 N ILE A1067 4233 4809 8829 430 -629 219 N ATOM 1999 CA ILE A1067 -8.254 -58.154 20.669 1.00 44.58 C ANISOU 1999 CA ILE A1067 4263 4306 8370 306 -764 198 C ATOM 2000 C ILE A1067 -6.795 -57.740 20.800 1.00 47.23 C ANISOU 2000 C ILE A1067 4776 4594 8577 430 -604 -38 C ATOM 2001 O ILE A1067 -5.915 -58.577 21.029 1.00 48.98 O ANISOU 2001 O ILE A1067 5159 4804 8648 410 -576 -77 O ATOM 2002 CB ILE A1067 -8.685 -58.229 19.194 1.00 45.20 C ANISOU 2002 CB ILE A1067 4542 4133 8498 200 -1037 301 C ATOM 2003 CG1 ILE A1067 -10.121 -58.742 19.077 1.00 52.90 C ANISOU 2003 CG1 ILE A1067 5309 5141 9649 32 -1269 570 C ATOM 2004 CG2 ILE A1067 -7.738 -59.119 18.411 1.00 44.27 C ANISOU 2004 CG2 ILE A1067 4856 3792 8170 148 -1136 270 C ATOM 2005 CD1 ILE A1067 -10.711 -58.575 17.693 1.00 52.58 C ANISOU 2005 CD1 ILE A1067 5437 4851 9690 -50 -1590 665 C ATOM 2006 N LEU A1068 -6.521 -56.439 20.673 1.00 46.23 N ANISOU 2006 N LEU A1068 4606 4432 8528 557 -512 -181 N ATOM 2007 CA LEU A1068 -5.144 -55.957 20.679 1.00 43.14 C ANISOU 2007 CA LEU A1068 4341 3967 8084 634 -398 -362 C ATOM 2008 C LEU A1068 -4.467 -56.228 22.016 1.00 40.87 C ANISOU 2008 C LEU A1068 3972 3846 7711 693 -281 -472 C ATOM 2009 O LEU A1068 -3.356 -56.767 22.063 1.00 40.09 O ANISOU 2009 O LEU A1068 3991 3715 7525 685 -254 -523 O ATOM 2010 CB LEU A1068 -5.116 -54.464 20.359 1.00 41.44 C ANISOU 2010 CB LEU A1068 4087 3662 7995 730 -354 -469 C ATOM 2011 CG LEU A1068 -3.722 -53.904 20.079 1.00 40.74 C ANISOU 2011 CG LEU A1068 4116 3446 7919 758 -270 -595 C ATOM 2012 CD1 LEU A1068 -3.194 -54.474 18.774 1.00 40.36 C ANISOU 2012 CD1 LEU A1068 4316 3211 7805 706 -293 -493 C ATOM 2013 CD2 LEU A1068 -3.735 -52.386 20.047 1.00 45.66 C ANISOU 2013 CD2 LEU A1068 4691 3983 8676 836 -241 -705 C ATOM 2014 N VAL A1069 -5.123 -55.857 23.118 1.00 41.82 N ANISOU 2014 N VAL A1069 3907 4141 7843 782 -207 -500 N ATOM 2015 CA VAL A1069 -4.521 -56.053 24.433 1.00 44.24 C ANISOU 2015 CA VAL A1069 4197 4582 8031 868 -119 -615 C ATOM 2016 C VAL A1069 -4.381 -57.539 24.742 1.00 44.10 C ANISOU 2016 C VAL A1069 4243 4639 7876 775 -139 -505 C ATOM 2017 O VAL A1069 -3.366 -57.979 25.297 1.00 44.45 O ANISOU 2017 O VAL A1069 4376 4703 7811 804 -126 -600 O ATOM 2018 CB VAL A1069 -5.340 -55.317 25.509 1.00 48.57 C ANISOU 2018 CB VAL A1069 4605 5280 8569 1040 -9 -654 C ATOM 2019 CG1 VAL A1069 -4.736 -55.546 26.889 1.00 49.72 C ANISOU 2019 CG1 VAL A1069 4812 5536 8542 1155 58 -777 C ATOM 2020 CG2 VAL A1069 -5.399 -53.830 25.197 1.00 49.19 C ANISOU 2020 CG2 VAL A1069 4683 5246 8762 1150 -11 -780 C ATOM 2021 N GLY A1070 -5.387 -58.336 24.378 1.00 42.80 N ANISOU 2021 N GLY A1070 4037 4497 7728 656 -202 -293 N ATOM 2022 CA GLY A1070 -5.289 -59.771 24.589 1.00 42.24 C ANISOU 2022 CA GLY A1070 4072 4449 7527 545 -254 -173 C ATOM 2023 C GLY A1070 -4.157 -60.400 23.799 1.00 41.24 C ANISOU 2023 C GLY A1070 4212 4151 7305 504 -337 -221 C ATOM 2024 O GLY A1070 -3.447 -61.276 24.302 1.00 40.68 O ANISOU 2024 O GLY A1070 4260 4109 7086 518 -325 -241 O ATOM 2025 N GLN A1071 -3.978 -59.971 22.548 1.00 40.47 N ANISOU 2025 N GLN A1071 4231 3870 7276 485 -405 -226 N ATOM 2026 CA GLN A1071 -2.895 -60.514 21.736 1.00 39.76 C ANISOU 2026 CA GLN A1071 4412 3616 7079 506 -425 -245 C ATOM 2027 C GLN A1071 -1.532 -60.096 22.268 1.00 39.13 C ANISOU 2027 C GLN A1071 4280 3590 6997 633 -287 -406 C ATOM 2028 O GLN A1071 -0.566 -60.860 22.158 1.00 44.25 O ANISOU 2028 O GLN A1071 5079 4199 7534 684 -263 -402 O ATOM 2029 CB GLN A1071 -3.059 -60.080 20.281 1.00 39.86 C ANISOU 2029 CB GLN A1071 4592 3412 7140 492 -499 -196 C ATOM 2030 CG GLN A1071 -4.190 -60.783 19.550 1.00 48.29 C ANISOU 2030 CG GLN A1071 5812 4354 8182 351 -728 -19 C ATOM 2031 CD GLN A1071 -4.395 -60.249 18.149 1.00 47.29 C ANISOU 2031 CD GLN A1071 5890 3997 8081 364 -829 14 C ATOM 2032 OE1 GLN A1071 -4.215 -59.058 17.895 1.00 47.81 O ANISOU 2032 OE1 GLN A1071 5851 4053 8262 445 -722 -71 O ATOM 2033 NE2 GLN A1071 -4.767 -61.128 17.230 1.00 42.33 N ANISOU 2033 NE2 GLN A1071 5603 3153 7328 289 -1058 139 N ATOM 2034 N ILE A1072 -1.435 -58.897 22.847 1.00 42.17 N ANISOU 2034 N ILE A1072 4461 4050 7513 691 -220 -537 N ATOM 2035 CA ILE A1072 -0.199 -58.492 23.509 1.00 42.09 C ANISOU 2035 CA ILE A1072 4376 4081 7536 774 -163 -680 C ATOM 2036 C ILE A1072 0.058 -59.366 24.730 1.00 39.38 C ANISOU 2036 C ILE A1072 4033 3887 7045 811 -177 -711 C ATOM 2037 O ILE A1072 1.185 -59.820 24.959 1.00 39.41 O ANISOU 2037 O ILE A1072 4069 3895 7009 863 -177 -747 O ATOM 2038 CB ILE A1072 -0.259 -56.997 23.876 1.00 39.95 C ANISOU 2038 CB ILE A1072 3952 3805 7421 814 -152 -816 C ATOM 2039 CG1 ILE A1072 -0.294 -56.140 22.611 1.00 39.56 C ANISOU 2039 CG1 ILE A1072 3932 3582 7515 784 -133 -780 C ATOM 2040 CG2 ILE A1072 0.926 -56.611 24.746 1.00 46.09 C ANISOU 2040 CG2 ILE A1072 4655 4610 8246 868 -178 -960 C ATOM 2041 CD1 ILE A1072 -0.564 -54.670 22.869 1.00 40.25 C ANISOU 2041 CD1 ILE A1072 3918 3629 7745 819 -144 -898 C ATOM 2042 N ASP A1073 -0.985 -59.625 25.526 1.00 43.34 N ANISOU 2042 N ASP A1073 4490 4513 7464 801 -177 -675 N ATOM 2043 CA ASP A1073 -0.837 -60.495 26.688 1.00 42.88 C ANISOU 2043 CA ASP A1073 4473 4585 7234 844 -172 -681 C ATOM 2044 C ASP A1073 -0.427 -61.906 26.276 1.00 41.22 C ANISOU 2044 C ASP A1073 4449 4320 6891 792 -219 -567 C ATOM 2045 O ASP A1073 0.356 -62.559 26.974 1.00 40.90 O ANISOU 2045 O ASP A1073 4482 4331 6728 862 -232 -611 O ATOM 2046 CB ASP A1073 -2.139 -60.528 27.492 1.00 45.84 C ANISOU 2046 CB ASP A1073 4761 5100 7554 851 -108 -599 C ATOM 2047 CG ASP A1073 -2.464 -59.190 28.139 1.00 53.17 C ANISOU 2047 CG ASP A1073 5573 6088 8543 985 -41 -731 C ATOM 2048 OD1 ASP A1073 -1.519 -58.435 28.466 1.00 54.50 O ANISOU 2048 OD1 ASP A1073 5768 6204 8735 1071 -89 -922 O ATOM 2049 OD2 ASP A1073 -3.666 -58.894 28.322 1.00 55.15 O ANISOU 2049 OD2 ASP A1073 5707 6424 8823 1012 47 -630 O ATOM 2050 N ASP A1074 -0.958 -62.398 25.151 1.00 41.16 N ANISOU 2050 N ASP A1074 4561 4187 6890 686 -272 -421 N ATOM 2051 CA ASP A1074 -0.554 -63.708 24.647 1.00 40.60 C ANISOU 2051 CA ASP A1074 4756 4009 6662 665 -339 -322 C ATOM 2052 C ASP A1074 0.938 -63.736 24.343 1.00 39.75 C ANISOU 2052 C ASP A1074 4722 3847 6536 810 -282 -405 C ATOM 2053 O ASP A1074 1.654 -64.654 24.762 1.00 39.72 O ANISOU 2053 O ASP A1074 4840 3864 6389 890 -289 -401 O ATOM 2054 CB ASP A1074 -1.356 -64.066 23.392 1.00 42.92 C ANISOU 2054 CB ASP A1074 5229 4120 6960 542 -456 -171 C ATOM 2055 CG ASP A1074 -2.824 -64.323 23.682 1.00 46.94 C ANISOU 2055 CG ASP A1074 5635 4680 7519 369 -552 -19 C ATOM 2056 OD1 ASP A1074 -3.211 -64.329 24.870 1.00 50.81 O ANISOU 2056 OD1 ASP A1074 5938 5360 8009 370 -472 -12 O ATOM 2057 OD2 ASP A1074 -3.594 -64.519 22.716 1.00 46.15 O ANISOU 2057 OD2 ASP A1074 5644 4425 7465 241 -710 112 O ATOM 2058 N ALA A1075 1.425 -62.736 23.604 1.00 39.15 N ANISOU 2058 N ALA A1075 4557 3700 6618 853 -215 -455 N ATOM 2059 CA ALA A1075 2.842 -62.695 23.265 1.00 49.44 C ANISOU 2059 CA ALA A1075 5859 4966 7961 988 -125 -478 C ATOM 2060 C ALA A1075 3.703 -62.426 24.491 1.00 45.16 C ANISOU 2060 C ALA A1075 5100 4571 7486 1052 -137 -600 C ATOM 2061 O ALA A1075 4.834 -62.918 24.572 1.00 43.57 O ANISOU 2061 O ALA A1075 4897 4385 7272 1169 -108 -584 O ATOM 2062 CB ALA A1075 3.093 -61.641 22.187 1.00 39.44 C ANISOU 2062 CB ALA A1075 4534 3582 6870 998 -34 -463 C ATOM 2063 N ALEU A1076 3.190 -61.647 25.448 0.52 43.06 N ANISOU 2063 N ALEU A1076 4672 4403 7285 1002 -191 -717 N ATOM 2064 N BLEU A1076 3.185 -61.661 25.456 0.48 43.09 N ANISOU 2064 N BLEU A1076 4677 4407 7286 1002 -192 -717 N ATOM 2065 CA ALEU A1076 3.943 -61.366 26.666 0.52 44.13 C ANISOU 2065 CA ALEU A1076 4677 4639 7451 1068 -265 -851 C ATOM 2066 CA BLEU A1076 3.952 -61.367 26.662 0.48 44.14 C ANISOU 2066 CA BLEU A1076 4678 4640 7453 1068 -265 -851 C ATOM 2067 C ALEU A1076 4.159 -62.629 27.489 0.52 44.88 C ANISOU 2067 C ALEU A1076 4909 4820 7323 1137 -313 -832 C ATOM 2068 C BLEU A1076 4.153 -62.618 27.510 0.48 44.88 C ANISOU 2068 C BLEU A1076 4908 4821 7323 1137 -314 -834 C ATOM 2069 O ALEU A1076 5.246 -62.840 28.040 0.52 45.75 O ANISOU 2069 O ALEU A1076 4967 4969 7448 1230 -380 -883 O ATOM 2070 O BLEU A1076 5.224 -62.811 28.096 0.48 45.82 O ANISOU 2070 O BLEU A1076 4973 4982 7456 1229 -385 -890 O ATOM 2071 CB ALEU A1076 3.220 -60.307 27.497 0.52 45.08 C ANISOU 2071 CB ALEU A1076 4704 4810 7613 1046 -311 -981 C ATOM 2072 CB BLEU A1076 3.255 -60.273 27.471 0.48 45.07 C ANISOU 2072 CB BLEU A1076 4698 4804 7621 1045 -312 -983 C ATOM 2073 CG ALEU A1076 3.668 -58.860 27.302 0.52 45.22 C ANISOU 2073 CG ALEU A1076 4564 4743 7875 1024 -351 -1083 C ATOM 2074 CG BLEU A1076 3.965 -59.799 28.740 0.48 46.25 C ANISOU 2074 CG BLEU A1076 4787 5004 7780 1122 -447 -1148 C ATOM 2075 CD1ALEU A1076 2.735 -57.912 28.036 0.52 46.77 C ANISOU 2075 CD1ALEU A1076 4761 4963 8046 1048 -381 -1202 C ATOM 2076 CD1BLEU A1076 5.342 -59.248 28.407 0.48 46.45 C ANISOU 2076 CD1BLEU A1076 4645 4950 8054 1111 -528 -1175 C ATOM 2077 CD2ALEU A1076 5.099 -58.690 27.791 0.52 46.61 C ANISOU 2077 CD2ALEU A1076 4622 4908 8178 1060 -474 -1153 C ATOM 2078 CD2BLEU A1076 3.126 -58.755 29.463 0.48 47.34 C ANISOU 2078 CD2BLEU A1076 4932 5156 7900 1151 -472 -1273 C ATOM 2079 N LYS A1077 3.134 -63.478 27.587 1.00 45.05 N ANISOU 2079 N LYS A1077 5098 4862 7156 1083 -298 -741 N ATOM 2080 CA LYS A1077 3.273 -64.713 28.351 1.00 47.37 C ANISOU 2080 CA LYS A1077 5561 5214 7226 1136 -341 -703 C ATOM 2081 C LYS A1077 4.302 -65.640 27.717 1.00 47.59 C ANISOU 2081 C LYS A1077 5728 5162 7192 1233 -343 -633 C ATOM 2082 O LYS A1077 5.088 -66.280 28.426 1.00 47.64 O ANISOU 2082 O LYS A1077 5785 5221 7095 1351 -397 -662 O ATOM 2083 CB LYS A1077 1.920 -65.413 28.473 1.00 48.11 C ANISOU 2083 CB LYS A1077 5783 5319 7176 1018 -326 -568 C ATOM 2084 CG LYS A1077 1.994 -66.745 29.191 1.00 52.68 C ANISOU 2084 CG LYS A1077 6573 5926 7517 1048 -367 -497 C ATOM 2085 CD LYS A1077 0.643 -67.420 29.268 1.00 57.03 C ANISOU 2085 CD LYS A1077 7211 6474 7983 886 -359 -314 C ATOM 2086 CE LYS A1077 0.767 -68.801 29.896 1.00 61.47 C ANISOU 2086 CE LYS A1077 8023 7025 8307 898 -408 -221 C ATOM 2087 NZ LYS A1077 1.629 -69.713 29.094 1.00 61.31 N ANISOU 2087 NZ LYS A1077 8263 6844 8190 959 -496 -197 N ATOM 2088 N LEU A1078 4.319 -65.718 26.384 1.00 46.75 N ANISOU 2088 N LEU A1078 5712 4921 7129 1221 -279 -536 N ATOM 2089 CA LEU A1078 5.314 -66.543 25.705 1.00 47.27 C ANISOU 2089 CA LEU A1078 5945 4901 7113 1379 -232 -456 C ATOM 2090 C LEU A1078 6.718 -65.983 25.897 1.00 50.12 C ANISOU 2090 C LEU A1078 6040 5335 7667 1521 -186 -507 C ATOM 2091 O LEU A1078 7.683 -66.745 26.031 1.00 52.44 O ANISOU 2091 O LEU A1078 6383 5648 7893 1696 -175 -464 O ATOM 2092 CB LEU A1078 4.976 -66.654 24.218 1.00 46.75 C ANISOU 2092 CB LEU A1078 6096 4650 7016 1370 -167 -341 C ATOM 2093 CG LEU A1078 3.621 -67.272 23.867 1.00 47.18 C ANISOU 2093 CG LEU A1078 6422 4588 6917 1204 -283 -255 C ATOM 2094 CD1 LEU A1078 3.265 -66.997 22.412 1.00 47.33 C ANISOU 2094 CD1 LEU A1078 6624 4410 6948 1187 -266 -177 C ATOM 2095 CD2 LEU A1078 3.616 -68.769 24.145 1.00 44.97 C ANISOU 2095 CD2 LEU A1078 6481 4239 6367 1243 -379 -179 C ATOM 2096 N ALA A1079 6.853 -64.653 25.918 1.00 50.78 N ANISOU 2096 N ALA A1079 5832 5449 8013 1447 -177 -583 N ATOM 2097 CA ALA A1079 8.164 -64.047 26.135 1.00 52.53 C ANISOU 2097 CA ALA A1079 5754 5722 8483 1527 -183 -604 C ATOM 2098 C ALA A1079 8.677 -64.326 27.543 1.00 54.26 C ANISOU 2098 C ALA A1079 5896 6058 8664 1578 -368 -710 C ATOM 2099 O ALA A1079 9.869 -64.598 27.734 1.00 57.00 O ANISOU 2099 O ALA A1079 6095 6448 9113 1708 -404 -668 O ATOM 2100 CB ALA A1079 8.098 -62.543 25.872 1.00 49.65 C ANISOU 2100 CB ALA A1079 5141 5320 8404 1398 -178 -658 C ATOM 2101 N ASN A1080 7.791 -64.265 28.541 1.00 53.03 N ANISOU 2101 N ASN A1080 5842 5951 8356 1501 -483 -832 N ATOM 2102 CA ASN A1080 8.161 -64.564 29.920 1.00 55.63 C ANISOU 2102 CA ASN A1080 6192 6368 8578 1573 -664 -939 C ATOM 2103 C ASN A1080 8.512 -66.030 30.133 1.00 58.28 C ANISOU 2103 C ASN A1080 6740 6729 8674 1713 -667 -858 C ATOM 2104 O ASN A1080 9.105 -66.362 31.165 1.00 61.58 O ANISOU 2104 O ASN A1080 7170 7209 9019 1813 -827 -926 O ATOM 2105 CB ASN A1080 7.028 -64.161 30.864 1.00 54.39 C ANISOU 2105 CB ASN A1080 6147 6251 8269 1503 -716 -1056 C ATOM 2106 CG ASN A1080 6.886 -62.660 30.989 1.00 56.14 C ANISOU 2106 CG ASN A1080 6195 6437 8698 1427 -777 -1180 C ATOM 2107 OD1 ASN A1080 7.878 -61.933 31.006 1.00 61.03 O ANISOU 2107 OD1 ASN A1080 6612 7016 9562 1423 -908 -1234 O ATOM 2108 ND2 ASN A1080 5.650 -62.185 31.078 1.00 52.44 N ANISOU 2108 ND2 ASN A1080 5800 5975 8151 1366 -694 -1207 N ATOM 2109 N GLU A1081 8.155 -66.906 29.198 1.00 56.94 N ANISOU 2109 N GLU A1081 6783 6488 8364 1730 -524 -720 N ATOM 2110 CA GLU A1081 8.532 -68.310 29.244 1.00 57.51 C ANISOU 2110 CA GLU A1081 7112 6539 8201 1881 -527 -632 C ATOM 2111 C GLU A1081 9.770 -68.604 28.407 1.00 57.82 C ANISOU 2111 C GLU A1081 7069 6548 8350 2084 -430 -523 C ATOM 2112 O GLU A1081 10.131 -69.773 28.244 1.00 59.77 O ANISOU 2112 O GLU A1081 7567 6751 8391 2259 -403 -436 O ATOM 2113 CB GLU A1081 7.367 -69.183 28.776 1.00 60.28 C ANISOU 2113 CB GLU A1081 7815 6785 8302 1785 -476 -535 C ATOM 2114 CG GLU A1081 6.142 -69.111 29.663 1.00 65.25 C ANISOU 2114 CG GLU A1081 8502 7469 8819 1614 -531 -574 C ATOM 2115 CD GLU A1081 4.955 -69.841 29.068 1.00 70.62 C ANISOU 2115 CD GLU A1081 9445 8035 9354 1460 -509 -432 C ATOM 2116 OE1 GLU A1081 4.985 -70.134 27.854 1.00 72.31 O ANISOU 2116 OE1 GLU A1081 9808 8100 9567 1465 -476 -344 O ATOM 2117 OE2 GLU A1081 3.992 -70.122 29.813 1.00 72.66 O ANISOU 2117 OE2 GLU A1081 9768 8337 9501 1338 -532 -391 O ATOM 2118 N GLY A1082 10.421 -67.574 27.867 1.00 56.75 N ANISOU 2118 N GLY A1082 6600 6428 8535 2078 -358 -505 N ATOM 2119 CA GLY A1082 11.616 -67.779 27.074 1.00 57.42 C ANISOU 2119 CA GLY A1082 6547 6508 8760 2293 -207 -352 C ATOM 2120 C GLY A1082 11.376 -68.285 25.671 1.00 55.03 C ANISOU 2120 C GLY A1082 6535 6066 8308 2401 31 -205 C ATOM 2121 O GLY A1082 12.319 -68.738 25.018 1.00 60.40 O ANISOU 2121 O GLY A1082 7213 6734 9003 2661 205 -52 O ATOM 2122 N LYS A1083 10.140 -68.217 25.183 1.00 50.60 N ANISOU 2122 N LYS A1083 6235 5391 7598 2230 38 -233 N ATOM 2123 CA LYS A1083 9.787 -68.705 23.849 1.00 49.55 C ANISOU 2123 CA LYS A1083 6471 5076 7281 2319 191 -111 C ATOM 2124 C LYS A1083 9.816 -67.521 22.886 1.00 49.04 C ANISOU 2124 C LYS A1083 6209 4967 7457 2260 353 -63 C ATOM 2125 O LYS A1083 8.805 -66.858 22.655 1.00 47.38 O ANISOU 2125 O LYS A1083 6021 4700 7283 2041 296 -124 O ATOM 2126 CB LYS A1083 8.423 -69.387 23.873 1.00 48.83 C ANISOU 2126 CB LYS A1083 6783 4862 6911 2147 40 -143 C ATOM 2127 CG LYS A1083 8.300 -70.472 24.929 1.00 50.66 C ANISOU 2127 CG LYS A1083 7197 5132 6920 2159 -120 -178 C ATOM 2128 CD LYS A1083 6.908 -71.075 24.944 1.00 53.21 C ANISOU 2128 CD LYS A1083 7853 5330 7034 1939 -268 -159 C ATOM 2129 CE LYS A1083 6.782 -72.147 26.016 1.00 55.32 C ANISOU 2129 CE LYS A1083 8308 5626 7085 1938 -406 -164 C ATOM 2130 NZ LYS A1083 5.436 -72.789 26.007 1.00 53.28 N ANISOU 2130 NZ LYS A1083 8343 5236 6666 1694 -550 -90 N ATOM 2131 N VAL A1084 10.992 -67.264 22.311 1.00 48.54 N ANISOU 2131 N VAL A1084 5942 4932 7569 2472 571 72 N ATOM 2132 CA VAL A1084 11.167 -66.088 21.463 1.00 53.41 C ANISOU 2132 CA VAL A1084 6333 5513 8449 2419 748 148 C ATOM 2133 C VAL A1084 10.422 -66.256 20.144 1.00 48.48 C ANISOU 2133 C VAL A1084 6160 4673 7587 2466 872 219 C ATOM 2134 O VAL A1084 9.655 -65.379 19.732 1.00 47.30 O ANISOU 2134 O VAL A1084 5996 4450 7524 2270 844 174 O ATOM 2135 CB VAL A1084 12.662 -65.811 21.226 1.00 59.86 C ANISOU 2135 CB VAL A1084 6766 6426 9550 2632 973 331 C ATOM 2136 CG1 VAL A1084 12.851 -64.428 20.610 1.00 60.23 C ANISOU 2136 CG1 VAL A1084 6493 6451 9943 2501 1115 410 C ATOM 2137 CG2 VAL A1084 13.442 -65.948 22.522 1.00 63.65 C ANISOU 2137 CG2 VAL A1084 6884 7089 10212 2628 780 274 C ATOM 2138 N LYS A1085 10.650 -67.375 19.451 1.00 53.06 N ANISOU 2138 N LYS A1085 7185 5127 7849 2749 990 331 N ATOM 2139 CA LYS A1085 10.018 -67.580 18.149 1.00 53.69 C ANISOU 2139 CA LYS A1085 7780 4956 7664 2830 1069 401 C ATOM 2140 C LYS A1085 8.499 -67.589 18.264 1.00 47.83 C ANISOU 2140 C LYS A1085 7276 4101 6797 2515 762 265 C ATOM 2141 O LYS A1085 7.800 -67.042 17.404 1.00 47.46 O ANISOU 2141 O LYS A1085 7399 3903 6732 2424 754 278 O ATOM 2142 CB LYS A1085 10.510 -68.884 17.519 1.00 55.53 C ANISOU 2142 CB LYS A1085 8537 5040 7521 3215 1196 523 C ATOM 2143 CG LYS A1085 11.955 -68.854 17.050 1.00 57.80 C ANISOU 2143 CG LYS A1085 8612 5458 7893 3522 1553 713 C ATOM 2144 CD LYS A1085 12.135 -67.964 15.831 1.00 60.07 C ANISOU 2144 CD LYS A1085 8883 5695 8245 3542 1817 846 C ATOM 2145 CE LYS A1085 13.566 -68.034 15.320 1.00 67.56 C ANISOU 2145 CE LYS A1085 9634 6797 9239 3817 2188 1079 C ATOM 2146 NZ LYS A1085 13.744 -67.304 14.039 1.00 73.61 N ANISOU 2146 NZ LYS A1085 10489 7493 9985 3881 2487 1248 N ATOM 2147 N GLU A1086 7.968 -68.207 19.321 1.00 46.69 N ANISOU 2147 N GLU A1086 7135 4029 6576 2353 513 158 N ATOM 2148 CA GLU A1086 6.522 -68.265 19.485 1.00 53.28 C ANISOU 2148 CA GLU A1086 8129 4781 7335 2054 244 83 C ATOM 2149 C GLU A1086 5.951 -66.903 19.861 1.00 48.74 C ANISOU 2149 C GLU A1086 7117 4333 7070 1797 210 -9 C ATOM 2150 O GLU A1086 4.833 -66.569 19.454 1.00 45.88 O ANISOU 2150 O GLU A1086 6856 3869 6706 1610 81 -18 O ATOM 2151 CB GLU A1086 6.158 -69.316 20.534 1.00 56.31 C ANISOU 2151 CB GLU A1086 8625 5213 7559 1968 38 39 C ATOM 2152 CG GLU A1086 4.703 -69.752 20.499 1.00 63.71 C ANISOU 2152 CG GLU A1086 9822 6012 8374 1699 -229 48 C ATOM 2153 CD GLU A1086 4.421 -70.928 21.417 1.00 70.55 C ANISOU 2153 CD GLU A1086 10861 6886 9057 1632 -403 58 C ATOM 2154 OE1 GLU A1086 5.379 -71.631 21.802 1.00 74.06 O ANISOU 2154 OE1 GLU A1086 11395 7370 9374 1858 -331 58 O ATOM 2155 OE2 GLU A1086 3.238 -71.148 21.754 1.00 73.59 O ANISOU 2155 OE2 GLU A1086 11279 7239 9442 1357 -605 86 O ATOM 2156 N ALA A1087 6.705 -66.104 20.621 1.00 47.82 N ANISOU 2156 N ALA A1087 6530 4417 7222 1794 297 -72 N ATOM 2157 CA ALA A1087 6.251 -64.758 20.958 1.00 48.38 C ANISOU 2157 CA ALA A1087 6245 4573 7566 1589 261 -167 C ATOM 2158 C ALA A1087 6.285 -63.842 19.740 1.00 49.39 C ANISOU 2158 C ALA A1087 6383 4570 7812 1609 411 -95 C ATOM 2159 O ALA A1087 5.379 -63.023 19.548 1.00 41.85 O ANISOU 2159 O ALA A1087 5377 3574 6949 1440 335 -146 O ATOM 2160 CB ALA A1087 7.101 -64.183 22.090 1.00 42.69 C ANISOU 2160 CB ALA A1087 5095 4045 7080 1581 251 -256 C ATOM 2161 N GLN A1088 7.320 -63.968 18.904 1.00 44.37 N ANISOU 2161 N GLN A1088 5818 3870 7169 1841 645 41 N ATOM 2162 CA GLN A1088 7.392 -63.154 17.694 1.00 47.19 C ANISOU 2162 CA GLN A1088 6238 4088 7604 1891 828 141 C ATOM 2163 C GLN A1088 6.256 -63.486 16.733 1.00 48.24 C ANISOU 2163 C GLN A1088 6863 3995 7472 1864 716 158 C ATOM 2164 O GLN A1088 5.650 -62.581 16.147 1.00 49.27 O ANISOU 2164 O GLN A1088 6995 4032 7693 1755 699 151 O ATOM 2165 CB GLN A1088 8.746 -63.343 17.011 1.00 47.53 C ANISOU 2165 CB GLN A1088 6272 4118 7668 2191 1154 332 C ATOM 2166 CG GLN A1088 9.912 -62.738 17.767 1.00 48.59 C ANISOU 2166 CG GLN A1088 5835 4453 8173 2181 1249 365 C ATOM 2167 CD GLN A1088 11.251 -63.110 17.159 1.00 61.87 C ANISOU 2167 CD GLN A1088 7460 6156 9893 2506 1589 605 C ATOM 2168 OE1 GLN A1088 11.508 -64.281 16.861 1.00 52.52 O ANISOU 2168 OE1 GLN A1088 6621 4928 8407 2781 1680 679 O ATOM 2169 NE2 GLN A1088 12.110 -62.115 16.965 1.00 53.32 N ANISOU 2169 NE2 GLN A1088 5941 5133 9186 2487 1784 748 N ATOM 2170 N ALA A1089 5.953 -64.775 16.554 1.00 49.41 N ANISOU 2170 N ALA A1089 7451 4029 7295 1956 601 185 N ATOM 2171 CA ALA A1089 4.846 -65.151 15.680 1.00 51.07 C ANISOU 2171 CA ALA A1089 8150 3989 7266 1897 403 207 C ATOM 2172 C ALA A1089 3.515 -64.661 16.235 1.00 51.39 C ANISOU 2172 C ALA A1089 7988 4084 7454 1563 127 108 C ATOM 2173 O ALA A1089 2.644 -64.219 15.475 1.00 52.85 O ANISOU 2173 O ALA A1089 8337 4114 7632 1467 1 127 O ATOM 2174 CB ALA A1089 4.822 -66.665 15.480 1.00 46.45 C ANISOU 2174 CB ALA A1089 8094 3240 6313 2039 281 256 C ATOM 2175 N ALA A1090 3.340 -64.728 17.558 1.00 48.71 N ANISOU 2175 N ALA A1090 7301 3965 7241 1410 38 18 N ATOM 2176 CA ALA A1090 2.127 -64.199 18.176 1.00 45.92 C ANISOU 2176 CA ALA A1090 6708 3702 7040 1146 -151 -48 C ATOM 2177 C ALA A1090 2.038 -62.688 18.009 1.00 47.87 C ANISOU 2177 C ALA A1090 6646 3996 7547 1093 -57 -104 C ATOM 2178 O ALA A1090 0.948 -62.142 17.793 1.00 47.13 O ANISOU 2178 O ALA A1090 6516 3861 7532 950 -192 -109 O ATOM 2179 CB ALA A1090 2.083 -64.577 19.656 1.00 43.88 C ANISOU 2179 CB ALA A1090 6188 3665 6818 1060 -205 -120 C ATOM 2180 N ALA A1091 3.174 -61.995 18.117 1.00 47.51 N ANISOU 2180 N ALA A1091 6364 4029 7657 1204 158 -131 N ATOM 2181 CA ALA A1091 3.194 -60.556 17.901 1.00 48.51 C ANISOU 2181 CA ALA A1091 6243 4157 8031 1150 239 -171 C ATOM 2182 C ALA A1091 2.894 -60.191 16.456 1.00 53.74 C ANISOU 2182 C ALA A1091 7199 4591 8630 1205 287 -74 C ATOM 2183 O ALA A1091 2.435 -59.074 16.196 1.00 56.24 O ANISOU 2183 O ALA A1091 7394 4867 9106 1123 275 -106 O ATOM 2184 CB ALA A1091 4.546 -59.979 18.318 1.00 46.45 C ANISOU 2184 CB ALA A1091 5666 4001 7981 1223 419 -182 C ATOM 2185 N GLU A1092 3.138 -61.104 15.513 1.00 54.19 N ANISOU 2185 N GLU A1092 7686 4476 8427 1367 332 40 N ATOM 2186 CA GLU A1092 2.803 -60.829 14.120 1.00 58.39 C ANISOU 2186 CA GLU A1092 8594 4755 8835 1450 350 130 C ATOM 2187 C GLU A1092 1.294 -60.746 13.917 1.00 55.84 C ANISOU 2187 C GLU A1092 8400 4332 8483 1261 25 97 C ATOM 2188 O GLU A1092 0.828 -60.044 13.011 1.00 52.86 O ANISOU 2188 O GLU A1092 8179 3791 8116 1265 -11 129 O ATOM 2189 CB GLU A1092 3.412 -61.901 13.215 1.00 65.60 C ANISOU 2189 CB GLU A1092 10023 5483 9418 1716 460 254 C ATOM 2190 CG GLU A1092 3.617 -61.461 11.773 1.00 75.74 C ANISOU 2190 CG GLU A1092 11688 6521 10568 1912 630 374 C ATOM 2191 CD GLU A1092 4.694 -60.398 11.629 1.00 83.21 C ANISOU 2191 CD GLU A1092 12292 7559 11764 2007 1008 454 C ATOM 2192 OE1 GLU A1092 5.607 -60.351 12.482 1.00 85.37 O ANISOU 2192 OE1 GLU A1092 12136 8054 12246 2008 1166 453 O ATOM 2193 OE2 GLU A1092 4.626 -59.607 10.663 1.00 86.10 O ANISOU 2193 OE2 GLU A1092 12789 7810 12116 2038 1104 522 O ATOM 2194 N GLN A1093 0.519 -61.444 14.754 1.00 52.64 N ANISOU 2194 N GLN A1093 7912 4026 8062 1098 -211 55 N ATOM 2195 CA GLN A1093 -0.937 -61.369 14.686 1.00 50.86 C ANISOU 2195 CA GLN A1093 7694 3748 7884 900 -518 67 C ATOM 2196 C GLN A1093 -1.459 -59.981 15.025 1.00 51.57 C ANISOU 2196 C GLN A1093 7380 3960 8253 805 -490 -3 C ATOM 2197 O GLN A1093 -2.601 -59.659 14.679 1.00 53.61 O ANISOU 2197 O GLN A1093 7644 4147 8578 696 -704 33 O ATOM 2198 CB GLN A1093 -1.563 -62.394 15.631 1.00 50.07 C ANISOU 2198 CB GLN A1093 7515 3759 7749 742 -716 83 C ATOM 2199 CG GLN A1093 -0.993 -63.793 15.491 1.00 54.80 C ANISOU 2199 CG GLN A1093 8510 4243 8068 839 -751 136 C ATOM 2200 CD GLN A1093 -1.264 -64.397 14.132 1.00 61.96 C ANISOU 2200 CD GLN A1093 10027 4797 8716 910 -948 230 C ATOM 2201 OE1 GLN A1093 -2.336 -64.207 13.559 1.00 64.75 O ANISOU 2201 OE1 GLN A1093 10493 5000 9109 766 -1229 283 O ATOM 2202 NE2 GLN A1093 -0.290 -65.130 13.606 1.00 67.47 N ANISOU 2202 NE2 GLN A1093 11146 5349 9139 1158 -815 258 N ATOM 2203 N LEU A1094 -0.654 -59.158 15.700 1.00 49.34 N ANISOU 2203 N LEU A1094 6761 3843 8141 850 -260 -95 N ATOM 2204 CA LEU A1094 -1.072 -57.797 16.011 1.00 45.39 C ANISOU 2204 CA LEU A1094 5952 3417 7879 792 -239 -175 C ATOM 2205 C LEU A1094 -1.298 -56.974 14.750 1.00 49.57 C ANISOU 2205 C LEU A1094 6684 3728 8424 840 -238 -124 C ATOM 2206 O LEU A1094 -2.104 -56.038 14.763 1.00 48.26 O ANISOU 2206 O LEU A1094 6370 3563 8403 784 -324 -160 O ATOM 2207 CB LEU A1094 -0.031 -57.127 16.905 1.00 42.93 C ANISOU 2207 CB LEU A1094 5325 3260 7728 825 -47 -280 C ATOM 2208 CG LEU A1094 0.135 -57.768 18.283 1.00 44.39 C ANISOU 2208 CG LEU A1094 5309 3662 7896 792 -72 -354 C ATOM 2209 CD1 LEU A1094 1.470 -57.395 18.889 1.00 44.97 C ANISOU 2209 CD1 LEU A1094 5182 3819 8086 849 73 -423 C ATOM 2210 CD2 LEU A1094 -1.002 -57.341 19.196 1.00 45.13 C ANISOU 2210 CD2 LEU A1094 5181 3895 8072 708 -185 -422 C ATOM 2211 N LYS A1095 -0.603 -57.303 13.656 1.00 52.47 N ANISOU 2211 N LYS A1095 7415 3899 8623 975 -128 -31 N ATOM 2212 CA LYS A1095 -0.768 -56.538 12.424 1.00 59.50 C ANISOU 2212 CA LYS A1095 8560 4560 9488 1048 -106 31 C ATOM 2213 C LYS A1095 -2.158 -56.716 11.832 1.00 59.23 C ANISOU 2213 C LYS A1095 8752 4379 9376 971 -447 67 C ATOM 2214 O LYS A1095 -2.707 -55.774 11.249 1.00 61.46 O ANISOU 2214 O LYS A1095 9065 4547 9738 971 -513 72 O ATOM 2215 CB LYS A1095 0.296 -56.935 11.405 1.00 65.48 C ANISOU 2215 CB LYS A1095 9700 5140 10038 1261 129 149 C ATOM 2216 CG LYS A1095 1.691 -56.452 11.751 1.00 71.34 C ANISOU 2216 CG LYS A1095 10159 6002 10945 1338 484 173 C ATOM 2217 CD LYS A1095 2.691 -56.876 10.692 1.00 79.37 C ANISOU 2217 CD LYS A1095 11540 6860 11758 1594 772 343 C ATOM 2218 CE LYS A1095 4.059 -56.280 10.964 1.00 84.60 C ANISOU 2218 CE LYS A1095 11839 7642 12663 1650 1128 425 C ATOM 2219 NZ LYS A1095 5.084 -56.793 10.012 1.00 89.42 N ANISOU 2219 NZ LYS A1095 12742 8163 13070 1932 1463 630 N ATOM 2220 N THR A1096 -2.741 -57.907 11.970 1.00 57.45 N ANISOU 2220 N THR A1096 8678 4138 9011 895 -690 108 N ATOM 2221 CA THR A1096 -4.102 -58.119 11.492 1.00 58.93 C ANISOU 2221 CA THR A1096 9013 4191 9188 774 -1076 173 C ATOM 2222 C THR A1096 -5.094 -57.261 12.267 1.00 55.76 C ANISOU 2222 C THR A1096 8112 3989 9085 639 -1164 135 C ATOM 2223 O THR A1096 -5.996 -56.657 11.676 1.00 55.52 O ANISOU 2223 O THR A1096 8107 3848 9138 612 -1364 177 O ATOM 2224 CB THR A1096 -4.469 -59.598 11.597 1.00 62.71 C ANISOU 2224 CB THR A1096 9724 4607 9498 679 -1338 246 C ATOM 2225 OG1 THR A1096 -3.504 -60.381 10.884 1.00 66.86 O ANISOU 2225 OG1 THR A1096 10740 4967 9697 859 -1214 273 O ATOM 2226 CG2 THR A1096 -5.846 -59.847 11.011 1.00 64.35 C ANISOU 2226 CG2 THR A1096 10087 4635 9730 523 -1798 350 C ATOM 2227 N THR A1097 -4.936 -57.187 13.591 1.00 52.70 N ANISOU 2227 N THR A1097 7293 3889 8843 586 -1014 60 N ATOM 2228 CA THR A1097 -5.801 -56.327 14.392 1.00 51.17 C ANISOU 2228 CA THR A1097 6660 3890 8893 530 -1033 24 C ATOM 2229 C THR A1097 -5.576 -54.858 14.058 1.00 52.60 C ANISOU 2229 C THR A1097 6782 4014 9190 636 -892 -60 C ATOM 2230 O THR A1097 -6.524 -54.065 14.038 1.00 54.01 O ANISOU 2230 O THR A1097 6793 4210 9519 636 -998 -50 O ATOM 2231 CB THR A1097 -5.556 -56.576 15.881 1.00 48.42 C ANISOU 2231 CB THR A1097 5963 3827 8605 502 -879 -47 C ATOM 2232 OG1 THR A1097 -5.590 -57.984 16.143 1.00 51.73 O ANISOU 2232 OG1 THR A1097 6493 4270 8891 409 -986 37 O ATOM 2233 CG2 THR A1097 -6.619 -55.883 16.721 1.00 45.71 C ANISOU 2233 CG2 THR A1097 5224 3680 8461 486 -897 -47 C ATOM 2234 N ARG A1098 -4.324 -54.483 13.789 1.00 51.51 N ANISOU 2234 N ARG A1098 6770 3802 9001 729 -653 -121 N ATOM 2235 CA ARG A1098 -4.007 -53.095 13.471 1.00 51.39 C ANISOU 2235 CA ARG A1098 6716 3703 9109 801 -518 -180 C ATOM 2236 C ARG A1098 -4.669 -52.658 12.170 1.00 53.98 C ANISOU 2236 C ARG A1098 7341 3781 9387 846 -672 -97 C ATOM 2237 O ARG A1098 -5.242 -51.565 12.093 1.00 55.74 O ANISOU 2237 O ARG A1098 7456 3972 9749 872 -716 -131 O ATOM 2238 CB ARG A1098 -2.491 -52.920 13.389 1.00 49.36 C ANISOU 2238 CB ARG A1098 6507 3408 8839 862 -238 -198 C ATOM 2239 CG ARG A1098 -2.039 -51.541 12.952 1.00 52.94 C ANISOU 2239 CG ARG A1098 6954 3730 9432 904 -97 -216 C ATOM 2240 CD ARG A1098 -0.603 -51.579 12.467 1.00 56.62 C ANISOU 2240 CD ARG A1098 7523 4109 9880 963 176 -133 C ATOM 2241 NE ARG A1098 -0.441 -52.497 11.342 1.00 61.53 N ANISOU 2241 NE ARG A1098 8563 4573 10243 1076 214 8 N ATOM 2242 CZ ARG A1098 0.727 -52.808 10.790 1.00 65.36 C ANISOU 2242 CZ ARG A1098 9198 4987 10647 1194 486 129 C ATOM 2243 NH1 ARG A1098 1.848 -52.276 11.260 1.00 65.27 N ANISOU 2243 NH1 ARG A1098 8885 5064 10851 1171 722 148 N ATOM 2244 NH2 ARG A1098 0.775 -53.655 9.770 1.00 68.34 N ANISOU 2244 NH2 ARG A1098 10039 5197 10732 1348 512 247 N ATOM 2245 N ASN A1099 -4.608 -53.504 11.139 1.00 55.63 N ANISOU 2245 N ASN A1099 7972 3790 9376 879 -774 8 N ATOM 2246 CA ASN A1099 -5.156 -53.137 9.839 1.00 59.54 C ANISOU 2246 CA ASN A1099 8839 4007 9776 945 -947 85 C ATOM 2247 C ASN A1099 -6.678 -53.136 9.841 1.00 62.21 C ANISOU 2247 C ASN A1099 9058 4355 10225 850 -1326 127 C ATOM 2248 O ASN A1099 -7.293 -52.374 9.088 1.00 69.27 O ANISOU 2248 O ASN A1099 10062 5146 11111 888 -1445 156 O ATOM 2249 CB ASN A1099 -4.636 -54.091 8.763 1.00 63.60 C ANISOU 2249 CB ASN A1099 9854 4403 9908 1013 -894 182 C ATOM 2250 CG ASN A1099 -3.121 -54.117 8.687 1.00 64.29 C ANISOU 2250 CG ASN A1099 10024 4472 9931 1146 -493 195 C ATOM 2251 OD1 ASN A1099 -2.452 -53.159 9.076 1.00 66.25 O ANISOU 2251 OD1 ASN A1099 10048 4732 10394 1181 -268 151 O ATOM 2252 ND2 ASN A1099 -2.572 -55.213 8.183 1.00 64.51 N ANISOU 2252 ND2 ASN A1099 10338 4479 9692 1216 -431 264 N ATOM 2253 N ALA A1100 -7.303 -53.971 10.672 1.00 58.28 N ANISOU 2253 N ALA A1100 8298 4047 9800 713 -1485 156 N ATOM 2254 CA ALA A1100 -8.751 -54.125 10.645 1.00 58.64 C ANISOU 2254 CA ALA A1100 8183 4109 9989 603 -1853 262 C ATOM 2255 C ALA A1100 -9.480 -53.290 11.689 1.00 59.82 C ANISOU 2255 C ALA A1100 7772 4534 10422 602 -1778 233 C ATOM 2256 O ALA A1100 -10.682 -53.050 11.532 1.00 62.24 O ANISOU 2256 O ALA A1100 7900 4851 10896 570 -2034 340 O ATOM 2257 CB ALA A1100 -9.132 -55.598 10.833 1.00 60.56 C ANISOU 2257 CB ALA A1100 8488 4360 10161 438 -2104 373 C ATOM 2258 N TYR A1101 -8.795 -52.837 12.740 1.00 59.71 N ANISOU 2258 N TYR A1101 7494 4731 10461 658 -1448 102 N ATOM 2259 CA TYR A1101 -9.465 -52.109 13.813 1.00 57.99 C ANISOU 2259 CA TYR A1101 6819 4763 10451 709 -1358 68 C ATOM 2260 C TYR A1101 -8.725 -50.836 14.198 1.00 55.07 C ANISOU 2260 C TYR A1101 6405 4403 10116 849 -1089 -109 C ATOM 2261 O TYR A1101 -9.299 -49.742 14.164 1.00 53.88 O ANISOU 2261 O TYR A1101 6151 4235 10085 963 -1100 -136 O ATOM 2262 CB TYR A1101 -9.616 -52.996 15.053 1.00 58.23 C ANISOU 2262 CB TYR A1101 6552 5066 10509 627 -1286 102 C ATOM 2263 CG TYR A1101 -10.477 -54.224 14.857 1.00 61.03 C ANISOU 2263 CG TYR A1101 6879 5425 10887 450 -1571 307 C ATOM 2264 CD1 TYR A1101 -11.857 -54.160 15.009 1.00 63.19 C ANISOU 2264 CD1 TYR A1101 6817 5808 11384 407 -1756 487 C ATOM 2265 CD2 TYR A1101 -9.908 -55.452 14.536 1.00 59.99 C ANISOU 2265 CD2 TYR A1101 7049 5176 10568 329 -1664 342 C ATOM 2266 CE1 TYR A1101 -12.648 -55.283 14.837 1.00 64.91 C ANISOU 2266 CE1 TYR A1101 6979 6010 11675 198 -2059 709 C ATOM 2267 CE2 TYR A1101 -10.689 -56.577 14.363 1.00 59.38 C ANISOU 2267 CE2 TYR A1101 6988 5056 10516 140 -1974 534 C ATOM 2268 CZ TYR A1101 -12.057 -56.488 14.514 1.00 64.22 C ANISOU 2268 CZ TYR A1101 7242 5771 11389 51 -2185 723 C ATOM 2269 OH TYR A1101 -12.835 -57.609 14.342 1.00 68.26 O ANISOU 2269 OH TYR A1101 7742 6221 11975 -183 -2534 948 O ATOM 2270 N ILE A1102 -7.451 -50.973 14.574 1.00 53.82 N ANISOU 2270 N ILE A1102 6325 4258 9867 841 -873 -217 N ATOM 2271 CA ILE A1102 -6.733 -49.866 15.200 1.00 52.79 C ANISOU 2271 CA ILE A1102 6100 4151 9806 926 -667 -376 C ATOM 2272 C ILE A1102 -6.543 -48.713 14.222 1.00 52.66 C ANISOU 2272 C ILE A1102 6295 3884 9828 994 -658 -394 C ATOM 2273 O ILE A1102 -6.675 -47.543 14.594 1.00 50.36 O ANISOU 2273 O ILE A1102 5915 3576 9642 1083 -612 -490 O ATOM 2274 CB ILE A1102 -5.386 -50.353 15.763 1.00 53.60 C ANISOU 2274 CB ILE A1102 6212 4312 9843 875 -491 -453 C ATOM 2275 CG1 ILE A1102 -5.585 -51.591 16.646 1.00 54.13 C ANISOU 2275 CG1 ILE A1102 6130 4599 9838 813 -513 -421 C ATOM 2276 CG2 ILE A1102 -4.695 -49.229 16.525 1.00 52.94 C ANISOU 2276 CG2 ILE A1102 6016 4236 9862 928 -359 -610 C ATOM 2277 CD1 ILE A1102 -6.585 -51.403 17.773 1.00 54.24 C ANISOU 2277 CD1 ILE A1102 5845 4836 9927 868 -525 -440 C ATOM 2278 N GLN A1103 -6.220 -49.017 12.964 1.00 53.60 N ANISOU 2278 N GLN A1103 6743 3785 9837 972 -698 -298 N ATOM 2279 CA GLN A1103 -6.024 -47.946 11.993 1.00 56.48 C ANISOU 2279 CA GLN A1103 7345 3897 10216 1044 -667 -289 C ATOM 2280 C GLN A1103 -7.332 -47.224 11.689 1.00 53.41 C ANISOU 2280 C GLN A1103 6925 3458 9912 1128 -876 -266 C ATOM 2281 O GLN A1103 -7.327 -46.014 11.430 1.00 51.54 O ANISOU 2281 O GLN A1103 6757 3104 9722 1205 -831 -312 O ATOM 2282 CB GLN A1103 -5.410 -48.494 10.707 1.00 64.47 C ANISOU 2282 CB GLN A1103 8771 4705 11019 1045 -627 -169 C ATOM 2283 CG GLN A1103 -4.737 -47.430 9.855 1.00 72.49 C ANISOU 2283 CG GLN A1103 10025 5579 11938 1088 -439 -134 C ATOM 2284 CD GLN A1103 -4.711 -47.784 8.385 1.00 79.55 C ANISOU 2284 CD GLN A1103 11394 6289 12542 1152 -435 8 C ATOM 2285 OE1 GLN A1103 -5.725 -48.187 7.814 1.00 82.75 O ANISOU 2285 OE1 GLN A1103 11944 6655 12842 1162 -682 57 O ATOM 2286 NE2 GLN A1103 -3.548 -47.635 7.761 1.00 82.12 N ANISOU 2286 NE2 GLN A1103 11957 6496 12748 1204 -165 86 N ATOM 2287 N LYS A1104 -8.457 -47.944 11.713 1.00 51.94 N ANISOU 2287 N LYS A1104 6623 3375 9738 1102 -1111 -175 N ATOM 2288 CA LYS A1104 -9.746 -47.293 11.505 1.00 55.90 C ANISOU 2288 CA LYS A1104 7008 3866 10366 1194 -1318 -123 C ATOM 2289 C LYS A1104 -10.066 -46.333 12.644 1.00 54.54 C ANISOU 2289 C LYS A1104 6504 3876 10343 1320 -1179 -232 C ATOM 2290 O LYS A1104 -10.608 -45.247 12.411 1.00 54.67 O ANISOU 2290 O LYS A1104 6530 3802 10440 1466 -1227 -252 O ATOM 2291 CB LYS A1104 -10.853 -48.336 11.358 1.00 59.43 C ANISOU 2291 CB LYS A1104 7331 4397 10851 1104 -1617 42 C ATOM 2292 CG LYS A1104 -10.742 -49.198 10.113 1.00 65.28 C ANISOU 2292 CG LYS A1104 8504 4886 11415 1014 -1851 147 C ATOM 2293 CD LYS A1104 -11.980 -50.064 9.935 1.00 71.96 C ANISOU 2293 CD LYS A1104 9221 5765 12354 899 -2245 326 C ATOM 2294 CE LYS A1104 -11.855 -50.985 8.730 1.00 75.02 C ANISOU 2294 CE LYS A1104 10130 5852 12521 815 -2537 413 C ATOM 2295 NZ LYS A1104 -10.863 -52.078 8.951 1.00 74.68 N ANISOU 2295 NZ LYS A1104 10283 5819 12274 733 -2384 379 N ATOM 2296 N TYR A1105 -9.743 -46.719 13.882 1.00 53.74 N ANISOU 2296 N TYR A1105 6153 4013 10252 1294 -1015 -305 N ATOM 2297 CA TYR A1105 -9.961 -45.823 15.012 1.00 57.47 C ANISOU 2297 CA TYR A1105 6405 4627 10804 1455 -876 -425 C ATOM 2298 C TYR A1105 -9.067 -44.593 14.918 1.00 54.32 C ANISOU 2298 C TYR A1105 6224 4017 10399 1514 -764 -583 C ATOM 2299 O TYR A1105 -9.497 -43.481 15.244 1.00 55.38 O ANISOU 2299 O TYR A1105 6338 4112 10590 1694 -752 -662 O ATOM 2300 CB TYR A1105 -9.722 -46.555 16.333 1.00 63.57 C ANISOU 2300 CB TYR A1105 6946 5666 11541 1425 -736 -469 C ATOM 2301 CG TYR A1105 -9.613 -45.622 17.522 1.00 75.03 C ANISOU 2301 CG TYR A1105 8310 7203 12997 1611 -578 -635 C ATOM 2302 CD1 TYR A1105 -10.738 -44.996 18.042 1.00 82.48 C ANISOU 2302 CD1 TYR A1105 9068 8266 14003 1849 -555 -608 C ATOM 2303 CD2 TYR A1105 -8.383 -45.359 18.117 1.00 77.50 C ANISOU 2303 CD2 TYR A1105 8744 7456 13246 1567 -470 -809 C ATOM 2304 CE1 TYR A1105 -10.645 -44.136 19.124 1.00 86.39 C ANISOU 2304 CE1 TYR A1105 9576 8803 14446 2069 -417 -769 C ATOM 2305 CE2 TYR A1105 -8.279 -44.499 19.200 1.00 80.53 C ANISOU 2305 CE2 TYR A1105 9130 7865 13605 1741 -391 -975 C ATOM 2306 CZ TYR A1105 -9.414 -43.894 19.700 1.00 86.43 C ANISOU 2306 CZ TYR A1105 9766 8711 14361 2006 -358 -965 C ATOM 2307 OH TYR A1105 -9.322 -43.039 20.776 1.00 91.46 O ANISOU 2307 OH TYR A1105 10493 9340 14918 2228 -282 -1138 O ATOM 2308 N LEU A1106 -7.826 -44.776 14.476 1.00 51.63 N ANISOU 2308 N LEU A1106 6090 3530 9998 1372 -681 -610 N ATOM 2309 CA LEU A1106 -6.881 -43.677 14.313 1.00 53.31 C ANISOU 2309 CA LEU A1106 6484 3535 10235 1363 -582 -705 C ATOM 2310 C LEU A1106 -7.402 -42.627 13.339 1.00 53.05 C ANISOU 2310 C LEU A1106 6669 3339 10147 1435 -652 -651 C ATOM 2311 O LEU A1106 -7.389 -41.435 13.638 1.00 54.88 O ANISOU 2311 O LEU A1106 6959 3505 10386 1510 -628 -739 O ATOM 2312 CB LEU A1106 -5.528 -44.205 13.830 1.00 55.89 C ANISOU 2312 CB LEU A1106 6948 3797 10492 1187 -452 -651 C ATOM 2313 CG LEU A1106 -4.566 -43.155 13.257 1.00 60.26 C ANISOU 2313 CG LEU A1106 7701 4173 11024 1116 -342 -633 C ATOM 2314 CD1 LEU A1106 -4.066 -42.210 14.345 1.00 59.02 C ANISOU 2314 CD1 LEU A1106 7435 4005 10986 1102 -330 -787 C ATOM 2315 CD2 LEU A1106 -3.398 -43.811 12.526 1.00 59.43 C ANISOU 2315 CD2 LEU A1106 7714 4002 10864 1001 -184 -505 C ATOM 2316 N GLU A 219 -7.971 -43.165 12.265 1.00 55.49 N ANISOU 2316 N GLU A 219 9090 3570 8422 1911 -484 -993 N ATOM 2317 CA GLU A 219 -8.428 -42.295 11.188 1.00 55.30 C ANISOU 2317 CA GLU A 219 9058 3677 8276 1852 -374 -1102 C ATOM 2318 C GLU A 219 -9.700 -41.556 11.580 1.00 51.23 C ANISOU 2318 C GLU A 219 8602 3226 7638 1661 -437 -1011 C ATOM 2319 O GLU A 219 -9.868 -40.381 11.249 1.00 50.00 O ANISOU 2319 O GLU A 219 8375 3231 7394 1632 -368 -1034 O ATOM 2320 CB GLU A 219 -8.648 -43.100 9.904 1.00 61.02 C ANISOU 2320 CB GLU A 219 9901 4312 8970 1848 -308 -1260 C ATOM 2321 CG GLU A 219 -7.362 -43.407 9.150 1.00 68.82 C ANISOU 2321 CG GLU A 219 10800 5304 10046 2037 -183 -1392 C ATOM 2322 CD GLU A 219 -7.509 -44.560 8.171 1.00 75.90 C ANISOU 2322 CD GLU A 219 11838 6055 10947 2046 -154 -1524 C ATOM 2323 OE1 GLU A 219 -8.625 -45.111 8.055 1.00 77.91 O ANISOU 2323 OE1 GLU A 219 12258 6209 11136 1901 -236 -1514 O ATOM 2324 OE2 GLU A 219 -6.505 -44.920 7.521 1.00 79.05 O ANISOU 2324 OE2 GLU A 219 12178 6439 11418 2195 -47 -1638 O ATOM 2325 N ARG A 220 -10.599 -42.240 12.296 1.00 49.20 N ANISOU 2325 N ARG A 220 8473 2845 7376 1527 -563 -902 N ATOM 2326 CA ARG A 220 -11.817 -41.577 12.752 1.00 52.37 C ANISOU 2326 CA ARG A 220 8922 3305 7673 1337 -621 -803 C ATOM 2327 C ARG A 220 -11.528 -40.594 13.878 1.00 48.40 C ANISOU 2327 C ARG A 220 8287 2927 7177 1346 -651 -668 C ATOM 2328 O ARG A 220 -12.164 -39.537 13.955 1.00 46.56 O ANISOU 2328 O ARG A 220 7963 2891 6837 1214 -608 -617 O ATOM 2329 CB ARG A 220 -12.858 -42.609 13.178 1.00 58.55 C ANISOU 2329 CB ARG A 220 9863 3933 8448 1177 -732 -723 C ATOM 2330 CG ARG A 220 -13.323 -43.496 12.032 1.00 69.33 C ANISOU 2330 CG ARG A 220 11356 5195 9789 1133 -709 -854 C ATOM 2331 CD ARG A 220 -14.588 -44.256 12.385 1.00 76.96 C ANISOU 2331 CD ARG A 220 12465 6051 10726 932 -813 -772 C ATOM 2332 NE ARG A 220 -14.918 -45.254 11.371 1.00 82.81 N ANISOU 2332 NE ARG A 220 13328 6673 11463 906 -807 -893 N ATOM 2333 CZ ARG A 220 -16.084 -45.884 11.296 1.00 86.12 C ANISOU 2333 CZ ARG A 220 13868 7011 11844 723 -878 -865 C ATOM 2334 NH1 ARG A 220 -17.041 -45.614 12.174 1.00 85.85 N ANISOU 2334 NH1 ARG A 220 13841 7008 11771 548 -949 -718 N ATOM 2335 NH2 ARG A 220 -16.296 -46.779 10.340 1.00 88.55 N ANISOU 2335 NH2 ARG A 220 14282 7211 12150 713 -874 -985 N ATOM 2336 N ALA A 221 -10.572 -40.912 14.752 1.00 48.85 N ANISOU 2336 N ALA A 221 8277 2940 7345 1472 -703 -597 N ATOM 2337 CA ALA A 221 -10.168 -39.946 15.768 1.00 47.63 C ANISOU 2337 CA ALA A 221 7975 2928 7195 1488 -725 -478 C ATOM 2338 C ALA A 221 -9.526 -38.723 15.128 1.00 47.01 C ANISOU 2338 C ALA A 221 7705 3073 7084 1556 -587 -559 C ATOM 2339 O ALA A 221 -9.761 -37.589 15.562 1.00 43.37 O ANISOU 2339 O ALA A 221 7121 2808 6549 1467 -560 -483 O ATOM 2340 CB ALA A 221 -9.212 -40.597 16.765 1.00 48.88 C ANISOU 2340 CB ALA A 221 8097 2996 7478 1611 -814 -392 C ATOM 2341 N ARG A 222 -8.717 -38.938 14.089 1.00 50.22 N ANISOU 2341 N ARG A 222 8088 3450 7542 1710 -495 -715 N ATOM 2342 CA ARG A 222 -8.140 -37.822 13.350 1.00 48.83 C ANISOU 2342 CA ARG A 222 7745 3480 7327 1762 -351 -799 C ATOM 2343 C ARG A 222 -9.223 -37.015 12.646 1.00 47.98 C ANISOU 2343 C ARG A 222 7655 3517 7057 1585 -278 -822 C ATOM 2344 O ARG A 222 -9.183 -35.780 12.643 1.00 46.06 O ANISOU 2344 O ARG A 222 7270 3481 6750 1538 -210 -794 O ATOM 2345 CB ARG A 222 -7.120 -38.346 12.341 1.00 53.52 C ANISOU 2345 CB ARG A 222 8329 4002 8003 1955 -257 -967 C ATOM 2346 CG ARG A 222 -6.296 -37.284 11.641 1.00 56.70 C ANISOU 2346 CG ARG A 222 8550 4603 8390 2035 -102 -1050 C ATOM 2347 CD ARG A 222 -5.551 -37.897 10.472 1.00 63.06 C ANISOU 2347 CD ARG A 222 9352 5370 9238 2151 24 -1209 C ATOM 2348 NE ARG A 222 -4.832 -39.107 10.863 1.00 70.62 N ANISOU 2348 NE ARG A 222 10318 6174 10340 2259 -28 -1196 N ATOM 2349 CZ ARG A 222 -4.516 -40.092 10.027 1.00 77.23 C ANISOU 2349 CZ ARG A 222 11223 6902 11218 2325 36 -1312 C ATOM 2350 NH1 ARG A 222 -4.862 -40.016 8.748 1.00 78.43 N ANISOU 2350 NH1 ARG A 222 11442 7087 11270 2286 150 -1449 N ATOM 2351 NH2 ARG A 222 -3.861 -41.158 10.468 1.00 79.06 N ANISOU 2351 NH2 ARG A 222 11464 6992 11584 2429 -18 -1289 N ATOM 2352 N SER A 223 -10.200 -37.700 12.048 1.00 50.13 N ANISOU 2352 N SER A 223 8102 3677 7267 1484 -302 -871 N ATOM 2353 CA SER A 223 -11.273 -37.007 11.344 1.00 47.08 C ANISOU 2353 CA SER A 223 7738 3416 6733 1318 -250 -895 C ATOM 2354 C SER A 223 -12.087 -36.141 12.296 1.00 44.91 C ANISOU 2354 C SER A 223 7391 3281 6393 1156 -299 -740 C ATOM 2355 O SER A 223 -12.517 -35.039 11.931 1.00 48.09 O ANISOU 2355 O SER A 223 7711 3867 6695 1070 -233 -739 O ATOM 2356 CB SER A 223 -12.167 -38.024 10.634 1.00 51.42 C ANISOU 2356 CB SER A 223 8495 3800 7244 1237 -292 -970 C ATOM 2357 OG SER A 223 -13.288 -37.399 10.034 1.00 57.42 O ANISOU 2357 OG SER A 223 9276 4675 7866 1067 -267 -980 O ATOM 2358 N THR A 224 -12.301 -36.614 13.526 1.00 41.01 N ANISOU 2358 N THR A 224 6930 2700 5951 1116 -415 -608 N ATOM 2359 CA THR A 224 -13.056 -35.826 14.495 1.00 41.52 C ANISOU 2359 CA THR A 224 6930 2895 5951 969 -454 -464 C ATOM 2360 C THR A 224 -12.286 -34.578 14.916 1.00 41.69 C ANISOU 2360 C THR A 224 6758 3109 5972 1030 -398 -425 C ATOM 2361 O THR A 224 -12.864 -33.490 15.012 1.00 38.28 O ANISOU 2361 O THR A 224 6245 2851 5450 923 -361 -382 O ATOM 2362 CB THR A 224 -13.406 -36.683 15.712 1.00 41.73 C ANISOU 2362 CB THR A 224 7052 2777 6026 914 -584 -332 C ATOM 2363 OG1 THR A 224 -14.211 -37.793 15.298 1.00 46.72 O ANISOU 2363 OG1 THR A 224 7865 3230 6655 832 -637 -364 O ATOM 2364 CG2 THR A 224 -14.179 -35.868 16.734 1.00 43.14 C ANISOU 2364 CG2 THR A 224 7166 3097 6130 764 -612 -188 C ATOM 2365 N LEU A 225 -10.979 -34.711 15.163 1.00 42.80 N ANISOU 2365 N LEU A 225 6822 3222 6219 1204 -395 -442 N ATOM 2366 CA LEU A 225 -10.186 -33.551 15.563 1.00 40.43 C ANISOU 2366 CA LEU A 225 6334 3098 5930 1260 -349 -409 C ATOM 2367 C LEU A 225 -10.115 -32.514 14.448 1.00 39.59 C ANISOU 2367 C LEU A 225 6136 3158 5750 1252 -212 -506 C ATOM 2368 O LEU A 225 -10.187 -31.309 14.712 1.00 40.47 O ANISOU 2368 O LEU A 225 6129 3445 5805 1194 -176 -457 O ATOM 2369 CB LEU A 225 -8.782 -33.987 15.982 1.00 44.63 C ANISOU 2369 CB LEU A 225 6796 3557 6605 1452 -380 -415 C ATOM 2370 CG LEU A 225 -8.674 -34.614 17.374 1.00 51.18 C ANISOU 2370 CG LEU A 225 7670 4275 7499 1461 -527 -280 C ATOM 2371 CD1 LEU A 225 -7.299 -35.219 17.602 1.00 54.18 C ANISOU 2371 CD1 LEU A 225 7996 4554 8035 1668 -567 -306 C ATOM 2372 CD2 LEU A 225 -8.979 -33.574 18.441 1.00 52.41 C ANISOU 2372 CD2 LEU A 225 7737 4589 7588 1356 -562 -150 C ATOM 2373 N GLN A 226 -9.976 -32.960 13.198 1.00 40.15 N ANISOU 2373 N GLN A 226 6270 3171 5813 1308 -135 -644 N ATOM 2374 CA GLN A 226 -9.906 -32.017 12.087 1.00 42.19 C ANISOU 2374 CA GLN A 226 6460 3582 5989 1298 -3 -735 C ATOM 2375 C GLN A 226 -11.222 -31.273 11.899 1.00 41.01 C ANISOU 2375 C GLN A 226 6340 3539 5701 1112 -3 -694 C ATOM 2376 O GLN A 226 -11.218 -30.109 11.481 1.00 37.54 O ANISOU 2376 O GLN A 226 5804 3267 5191 1077 77 -704 O ATOM 2377 CB GLN A 226 -9.507 -32.745 10.804 1.00 46.79 C ANISOU 2377 CB GLN A 226 7127 4071 6581 1396 78 -894 C ATOM 2378 CG GLN A 226 -8.091 -33.300 10.839 1.00 57.93 C ANISOU 2378 CG GLN A 226 8472 5405 8134 1600 107 -954 C ATOM 2379 CD GLN A 226 -7.783 -34.209 9.657 1.00 68.06 C ANISOU 2379 CD GLN A 226 9866 6566 9430 1702 179 -1117 C ATOM 2380 OE1 GLN A 226 -8.663 -34.524 8.852 1.00 72.04 O ANISOU 2380 OE1 GLN A 226 10516 7024 9834 1613 190 -1182 O ATOM 2381 NE2 GLN A 226 -6.528 -34.636 9.551 1.00 69.30 N ANISOU 2381 NE2 GLN A 226 9951 6669 9711 1891 227 -1188 N ATOM 2382 N LYS A 227 -12.351 -31.915 12.211 1.00 40.86 N ANISOU 2382 N LYS A 227 6449 3426 5648 992 -93 -645 N ATOM 2383 CA LYS A 227 -13.631 -31.219 12.138 1.00 39.20 C ANISOU 2383 CA LYS A 227 6249 3321 5323 818 -103 -598 C ATOM 2384 C LYS A 227 -13.781 -30.208 13.265 1.00 36.64 C ANISOU 2384 C LYS A 227 5801 3133 4985 758 -128 -469 C ATOM 2385 O LYS A 227 -14.373 -29.143 13.062 1.00 37.30 O ANISOU 2385 O LYS A 227 5824 3366 4983 669 -90 -452 O ATOM 2386 CB LYS A 227 -14.782 -32.224 12.161 1.00 41.69 C ANISOU 2386 CB LYS A 227 6724 3498 5618 701 -190 -582 C ATOM 2387 CG LYS A 227 -14.860 -33.083 10.907 1.00 47.42 C ANISOU 2387 CG LYS A 227 7587 4102 6329 730 -167 -721 C ATOM 2388 CD LYS A 227 -15.977 -34.103 10.994 1.00 53.74 C ANISOU 2388 CD LYS A 227 8543 4754 7120 605 -266 -701 C ATOM 2389 CE LYS A 227 -15.999 -34.985 9.755 1.00 61.80 C ANISOU 2389 CE LYS A 227 9713 5642 8125 638 -250 -849 C ATOM 2390 NZ LYS A 227 -17.084 -36.007 9.806 1.00 67.58 N ANISOU 2390 NZ LYS A 227 10602 6219 8855 506 -354 -834 N ATOM 2391 N GLU A 228 -13.258 -30.518 14.453 1.00 37.09 N ANISOU 2391 N GLU A 228 5830 3140 5123 808 -196 -381 N ATOM 2392 CA GLU A 228 -13.267 -29.540 15.535 1.00 36.67 C ANISOU 2392 CA GLU A 228 5662 3217 5052 765 -217 -270 C ATOM 2393 C GLU A 228 -12.348 -28.364 15.232 1.00 34.53 C ANISOU 2393 C GLU A 228 5238 3098 4783 842 -131 -305 C ATOM 2394 O GLU A 228 -12.669 -27.223 15.588 1.00 33.16 O ANISOU 2394 O GLU A 228 4978 3070 4551 771 -113 -252 O ATOM 2395 CB GLU A 228 -12.872 -30.206 16.851 1.00 44.99 C ANISOU 2395 CB GLU A 228 6738 4173 6183 804 -319 -168 C ATOM 2396 CG GLU A 228 -13.966 -31.070 17.455 1.00 53.20 C ANISOU 2396 CG GLU A 228 7913 5101 7199 681 -407 -90 C ATOM 2397 CD GLU A 228 -13.560 -31.676 18.785 1.00 60.55 C ANISOU 2397 CD GLU A 228 8875 5939 8192 715 -509 22 C ATOM 2398 OE1 GLU A 228 -12.828 -32.691 18.782 1.00 61.06 O ANISOU 2398 OE1 GLU A 228 9003 5846 8352 828 -557 -1 O ATOM 2399 OE2 GLU A 228 -13.963 -31.128 19.836 1.00 63.76 O ANISOU 2399 OE2 GLU A 228 9247 6430 8550 632 -543 132 O ATOM 2400 N VAL A 229 -11.211 -28.615 14.577 1.00 32.95 N ANISOU 2400 N VAL A 229 5001 2866 4654 984 -73 -395 N ATOM 2401 CA VAL A 229 -10.370 -27.509 14.126 1.00 36.66 C ANISOU 2401 CA VAL A 229 5326 3481 5123 1043 25 -437 C ATOM 2402 C VAL A 229 -11.118 -26.659 13.107 1.00 35.31 C ANISOU 2402 C VAL A 229 5162 3423 4832 947 107 -485 C ATOM 2403 O VAL A 229 -11.103 -25.424 13.177 1.00 32.77 O ANISOU 2403 O VAL A 229 4738 3249 4465 905 147 -454 O ATOM 2404 CB VAL A 229 -9.041 -28.037 13.555 1.00 36.36 C ANISOU 2404 CB VAL A 229 5246 3384 5188 1213 84 -532 C ATOM 2405 CG1 VAL A 229 -8.214 -26.892 12.994 1.00 36.02 C ANISOU 2405 CG1 VAL A 229 5051 3495 5138 1257 199 -576 C ATOM 2406 CG2 VAL A 229 -8.263 -28.768 14.625 1.00 37.19 C ANISOU 2406 CG2 VAL A 229 5327 3386 5419 1315 -12 -474 C ATOM 2407 N HIS A 230 -11.799 -27.307 12.157 1.00 37.75 N ANISOU 2407 N HIS A 230 5599 3658 5087 909 122 -559 N ATOM 2408 CA HIS A 230 -12.542 -26.570 11.139 1.00 41.52 C ANISOU 2408 CA HIS A 230 6098 4233 5446 820 185 -605 C ATOM 2409 C HIS A 230 -13.652 -25.733 11.763 1.00 34.60 C ANISOU 2409 C HIS A 230 5195 3453 4499 679 134 -507 C ATOM 2410 O HIS A 230 -13.878 -24.586 11.360 1.00 34.05 O ANISOU 2410 O HIS A 230 5062 3518 4358 631 185 -505 O ATOM 2411 CB HIS A 230 -13.114 -27.541 10.105 1.00 52.13 C ANISOU 2411 CB HIS A 230 7598 5463 6745 800 186 -700 C ATOM 2412 CG HIS A 230 -13.897 -26.878 9.012 1.00 63.25 C ANISOU 2412 CG HIS A 230 9045 6961 8027 709 234 -749 C ATOM 2413 ND1 HIS A 230 -13.300 -26.306 7.909 1.00 66.65 N ANISOU 2413 ND1 HIS A 230 9450 7470 8404 760 347 -835 N ATOM 2414 CD2 HIS A 230 -15.230 -26.700 8.851 1.00 65.14 C ANISOU 2414 CD2 HIS A 230 9344 7223 8181 569 179 -720 C ATOM 2415 CE1 HIS A 230 -14.231 -25.803 7.117 1.00 65.94 C ANISOU 2415 CE1 HIS A 230 9416 7444 8196 658 352 -854 C ATOM 2416 NE2 HIS A 230 -15.411 -26.030 7.665 1.00 65.10 N ANISOU 2416 NE2 HIS A 230 9355 7306 8075 544 248 -787 N ATOM 2417 N ALA A 231 -14.352 -26.287 12.755 1.00 31.32 N ANISOU 2417 N ALA A 231 4826 2970 4103 612 37 -424 N ATOM 2418 CA ALA A 231 -15.423 -25.545 13.409 1.00 34.16 C ANISOU 2418 CA ALA A 231 5156 3422 4402 483 -3 -334 C ATOM 2419 C ALA A 231 -14.879 -24.414 14.272 1.00 33.63 C ANISOU 2419 C ALA A 231 4953 3479 4348 505 10 -265 C ATOM 2420 O ALA A 231 -15.522 -23.364 14.390 1.00 30.57 O ANISOU 2420 O ALA A 231 4510 3209 3895 426 21 -228 O ATOM 2421 CB ALA A 231 -16.280 -26.494 14.249 1.00 38.44 C ANISOU 2421 CB ALA A 231 5786 3858 4960 402 -99 -263 C ATOM 2422 N ALA A 232 -13.708 -24.604 14.885 1.00 33.39 N ANISOU 2422 N ALA A 232 4866 3418 4403 612 1 -249 N ATOM 2423 CA ALA A 232 -13.129 -23.541 15.700 1.00 32.33 C ANISOU 2423 CA ALA A 232 4604 3396 4283 631 4 -188 C ATOM 2424 C ALA A 232 -12.620 -22.399 14.830 1.00 32.40 C ANISOU 2424 C ALA A 232 4521 3526 4263 656 101 -245 C ATOM 2425 O ALA A 232 -12.695 -21.230 15.226 1.00 31.81 O ANISOU 2425 O ALA A 232 4362 3567 4155 614 111 -200 O ATOM 2426 CB ALA A 232 -12.005 -24.094 16.577 1.00 29.05 C ANISOU 2426 CB ALA A 232 4151 2912 3972 738 -47 -155 C ATOM 2427 N LYS A 233 -12.092 -22.715 13.644 1.00 30.91 N ANISOU 2427 N LYS A 233 4352 3309 4082 722 176 -343 N ATOM 2428 CA LYS A 233 -11.678 -21.660 12.726 1.00 32.53 C ANISOU 2428 CA LYS A 233 4486 3627 4245 731 277 -393 C ATOM 2429 C LYS A 233 -12.877 -20.853 12.243 1.00 29.86 C ANISOU 2429 C LYS A 233 4183 3370 3793 611 285 -381 C ATOM 2430 O LYS A 233 -12.812 -19.620 12.172 1.00 26.66 O ANISOU 2430 O LYS A 233 3700 3079 3351 581 323 -360 O ATOM 2431 CB LYS A 233 -10.909 -22.259 11.549 1.00 36.80 C ANISOU 2431 CB LYS A 233 5056 4119 4807 824 364 -504 C ATOM 2432 CG LYS A 233 -9.514 -22.731 11.931 1.00 46.42 C ANISOU 2432 CG LYS A 233 6191 5293 6152 960 378 -521 C ATOM 2433 CD LYS A 233 -8.766 -23.332 10.755 1.00 49.05 C ANISOU 2433 CD LYS A 233 6549 5580 6507 1060 478 -641 C ATOM 2434 CE LYS A 233 -7.362 -23.750 11.155 1.00 50.63 C ANISOU 2434 CE LYS A 233 6644 5745 6849 1204 493 -659 C ATOM 2435 NZ LYS A 233 -6.652 -24.419 10.024 1.00 55.90 N ANISOU 2435 NZ LYS A 233 7336 6362 7543 1311 600 -785 N ATOM 2436 N SER A 234 -13.983 -21.532 11.922 1.00 25.53 N ANISOU 2436 N SER A 234 3750 2757 3193 541 243 -394 N ATOM 2437 CA SER A 234 -15.193 -20.825 11.518 1.00 28.23 C ANISOU 2437 CA SER A 234 4117 3171 3437 430 234 -379 C ATOM 2438 C SER A 234 -15.672 -19.882 12.614 1.00 30.36 C ANISOU 2438 C SER A 234 4307 3528 3700 369 191 -284 C ATOM 2439 O SER A 234 -16.018 -18.726 12.342 1.00 31.68 O ANISOU 2439 O SER A 234 4428 3799 3811 325 217 -271 O ATOM 2440 CB SER A 234 -16.283 -21.828 11.152 1.00 28.57 C ANISOU 2440 CB SER A 234 4285 3123 3446 361 178 -402 C ATOM 2441 OG SER A 234 -15.881 -22.607 10.039 1.00 32.70 O ANISOU 2441 OG SER A 234 4895 3569 3962 416 221 -503 O ATOM 2442 N ALA A 235 -15.689 -20.356 13.863 1.00 28.69 N ANISOU 2442 N ALA A 235 4086 3272 3542 367 126 -217 N ATOM 2443 CA ALA A 235 -16.062 -19.493 14.977 1.00 26.40 C ANISOU 2443 CA ALA A 235 3728 3064 3241 317 92 -133 C ATOM 2444 C ALA A 235 -15.067 -18.352 15.156 1.00 27.82 C ANISOU 2444 C ALA A 235 3797 3335 3440 370 135 -126 C ATOM 2445 O ALA A 235 -15.461 -17.220 15.468 1.00 22.85 O ANISOU 2445 O ALA A 235 3112 2799 2770 322 138 -91 O ATOM 2446 CB ALA A 235 -16.172 -20.324 16.254 1.00 25.54 C ANISOU 2446 CB ALA A 235 3648 2882 3175 308 17 -63 C ATOM 2447 N ALA A 236 -13.776 -18.629 14.960 1.00 28.33 N ANISOU 2447 N ALA A 236 3823 3369 3571 469 168 -162 N ATOM 2448 CA ALA A 236 -12.759 -17.590 15.097 1.00 26.52 C ANISOU 2448 CA ALA A 236 3481 3224 3373 514 209 -157 C ATOM 2449 C ALA A 236 -12.867 -16.541 13.994 1.00 25.76 C ANISOU 2449 C ALA A 236 3362 3214 3213 484 288 -197 C ATOM 2450 O ALA A 236 -12.563 -15.366 14.229 1.00 23.80 O ANISOU 2450 O ALA A 236 3033 3052 2959 469 306 -171 O ATOM 2451 CB ALA A 236 -11.363 -18.216 15.095 1.00 24.76 C ANISOU 2451 CB ALA A 236 3210 2949 3249 628 227 -190 C ATOM 2452 N ILE A 237 -13.281 -16.943 12.789 1.00 23.50 N ANISOU 2452 N ILE A 237 3154 2901 2874 472 331 -260 N ATOM 2453 CA ILE A 237 -13.496 -15.973 11.718 1.00 23.84 C ANISOU 2453 CA ILE A 237 3197 3021 2840 435 397 -289 C ATOM 2454 C ILE A 237 -14.604 -15.004 12.104 1.00 26.56 C ANISOU 2454 C ILE A 237 3535 3432 3125 346 351 -232 C ATOM 2455 O ILE A 237 -14.491 -13.792 11.890 1.00 28.53 O ANISOU 2455 O ILE A 237 3734 3762 3344 325 383 -217 O ATOM 2456 CB ILE A 237 -13.807 -16.699 10.395 1.00 26.17 C ANISOU 2456 CB ILE A 237 3598 3267 3077 436 437 -368 C ATOM 2457 CG1 ILE A 237 -12.547 -17.387 9.857 1.00 26.04 C ANISOU 2457 CG1 ILE A 237 3573 3205 3117 538 512 -438 C ATOM 2458 CG2 ILE A 237 -14.384 -15.734 9.367 1.00 25.13 C ANISOU 2458 CG2 ILE A 237 3495 3210 2843 375 474 -382 C ATOM 2459 CD1 ILE A 237 -12.812 -18.349 8.705 1.00 23.66 C ANISOU 2459 CD1 ILE A 237 3393 2831 2764 551 543 -526 C ATOM 2460 N ILE A 238 -15.681 -15.526 12.700 1.00 23.72 N ANISOU 2460 N ILE A 238 3223 3037 2752 292 278 -199 N ATOM 2461 CA ILE A 238 -16.795 -14.691 13.146 1.00 23.72 C ANISOU 2461 CA ILE A 238 3206 3100 2705 214 236 -149 C ATOM 2462 C ILE A 238 -16.320 -13.673 14.177 1.00 26.73 C ANISOU 2462 C ILE A 238 3495 3544 3116 225 230 -97 C ATOM 2463 O ILE A 238 -16.644 -12.480 14.097 1.00 24.40 O ANISOU 2463 O ILE A 238 3164 3322 2784 193 239 -80 O ATOM 2464 CB ILE A 238 -17.922 -15.576 13.712 1.00 24.52 C ANISOU 2464 CB ILE A 238 3363 3150 2802 156 168 -121 C ATOM 2465 CG1 ILE A 238 -18.459 -16.517 12.631 1.00 32.18 C ANISOU 2465 CG1 ILE A 238 4431 4055 3742 134 164 -178 C ATOM 2466 CG2 ILE A 238 -19.039 -14.725 14.287 1.00 19.34 C ANISOU 2466 CG2 ILE A 238 2672 2565 2110 85 135 -71 C ATOM 2467 CD1 ILE A 238 -19.422 -15.856 11.687 1.00 34.54 C ANISOU 2467 CD1 ILE A 238 4751 4408 3963 73 163 -197 C ATOM 2468 N ALA A 239 -15.550 -14.132 15.165 1.00 24.26 N ANISOU 2468 N ALA A 239 3150 3200 2869 270 206 -71 N ATOM 2469 CA ALA A 239 -15.038 -13.227 16.190 1.00 21.75 C ANISOU 2469 CA ALA A 239 2752 2937 2577 279 189 -26 C ATOM 2470 C ALA A 239 -14.064 -12.216 15.597 1.00 22.56 C ANISOU 2470 C ALA A 239 2785 3094 2693 309 248 -50 C ATOM 2471 O ALA A 239 -14.076 -11.037 15.971 1.00 23.99 O ANISOU 2471 O ALA A 239 2916 3338 2860 284 245 -24 O ATOM 2472 CB ALA A 239 -14.373 -14.028 17.308 1.00 18.74 C ANISOU 2472 CB ALA A 239 2358 2502 2259 323 138 7 C ATOM 2473 N GLY A 240 -13.215 -12.656 14.667 1.00 21.20 N ANISOU 2473 N GLY A 240 2611 2896 2548 361 308 -101 N ATOM 2474 CA GLY A 240 -12.275 -11.737 14.049 1.00 21.63 C ANISOU 2474 CA GLY A 240 2598 3006 2615 381 378 -121 C ATOM 2475 C GLY A 240 -12.959 -10.694 13.187 1.00 21.84 C ANISOU 2475 C GLY A 240 2652 3088 2559 321 412 -125 C ATOM 2476 O GLY A 240 -12.530 -9.539 13.140 1.00 20.22 O ANISOU 2476 O GLY A 240 2391 2939 2354 304 438 -108 O ATOM 2477 N LEU A 241 -14.033 -11.083 12.491 1.00 18.80 N ANISOU 2477 N LEU A 241 2355 2682 2104 284 404 -144 N ATOM 2478 CA LEU A 241 -14.784 -10.113 11.698 1.00 18.63 C ANISOU 2478 CA LEU A 241 2367 2709 2003 230 417 -140 C ATOM 2479 C LEU A 241 -15.512 -9.108 12.584 1.00 17.71 C ANISOU 2479 C LEU A 241 2215 2635 1877 186 360 -87 C ATOM 2480 O LEU A 241 -15.647 -7.939 12.213 1.00 20.18 O ANISOU 2480 O LEU A 241 2518 2995 2157 159 374 -72 O ATOM 2481 CB LEU A 241 -15.777 -10.830 10.781 1.00 22.40 C ANISOU 2481 CB LEU A 241 2945 3154 2413 201 405 -175 C ATOM 2482 CG LEU A 241 -15.169 -11.600 9.601 1.00 26.51 C ANISOU 2482 CG LEU A 241 3522 3638 2911 237 474 -242 C ATOM 2483 CD1 LEU A 241 -16.245 -12.358 8.848 1.00 31.44 C ANISOU 2483 CD1 LEU A 241 4255 4222 3469 200 439 -276 C ATOM 2484 CD2 LEU A 241 -14.422 -10.645 8.662 1.00 25.59 C ANISOU 2484 CD2 LEU A 241 3390 3577 2757 240 560 -256 C ATOM 2485 N PHE A 242 -16.008 -9.545 13.739 1.00 16.43 N ANISOU 2485 N PHE A 242 2045 2457 1743 180 299 -57 N ATOM 2486 CA PHE A 242 -16.564 -8.593 14.692 1.00 17.60 C ANISOU 2486 CA PHE A 242 2155 2647 1885 149 256 -14 C ATOM 2487 C PHE A 242 -15.527 -7.538 15.059 1.00 17.64 C ANISOU 2487 C PHE A 242 2091 2688 1925 167 276 0 C ATOM 2488 O PHE A 242 -15.807 -6.335 15.026 1.00 17.41 O ANISOU 2488 O PHE A 242 2045 2697 1871 141 274 15 O ATOM 2489 CB PHE A 242 -17.064 -9.322 15.944 1.00 15.46 C ANISOU 2489 CB PHE A 242 1887 2354 1633 141 201 16 C ATOM 2490 CG PHE A 242 -17.728 -8.413 16.948 1.00 15.67 C ANISOU 2490 CG PHE A 242 1884 2428 1644 111 167 52 C ATOM 2491 CD1 PHE A 242 -16.980 -7.745 17.904 1.00 17.95 C ANISOU 2491 CD1 PHE A 242 2122 2739 1961 129 154 72 C ATOM 2492 CD2 PHE A 242 -19.100 -8.218 16.925 1.00 17.27 C ANISOU 2492 CD2 PHE A 242 2104 2652 1804 66 147 60 C ATOM 2493 CE1 PHE A 242 -17.585 -6.900 18.822 1.00 20.89 C ANISOU 2493 CE1 PHE A 242 2477 3151 2311 106 127 95 C ATOM 2494 CE2 PHE A 242 -19.711 -7.376 17.838 1.00 20.68 C ANISOU 2494 CE2 PHE A 242 2506 3129 2223 48 126 83 C ATOM 2495 CZ PHE A 242 -18.952 -6.720 18.789 1.00 20.13 C ANISOU 2495 CZ PHE A 242 2399 3077 2172 69 119 98 C ATOM 2496 N ALA A 243 -14.311 -7.976 15.399 1.00 16.30 N ANISOU 2496 N ALA A 243 1876 2500 1818 212 290 -6 N ATOM 2497 CA ALA A 243 -13.260 -7.033 15.771 1.00 19.54 C ANISOU 2497 CA ALA A 243 2210 2943 2273 223 301 7 C ATOM 2498 C ALA A 243 -12.913 -6.099 14.616 1.00 16.96 C ANISOU 2498 C ALA A 243 1875 2646 1922 204 367 -8 C ATOM 2499 O ALA A 243 -12.745 -4.892 14.812 1.00 19.23 O ANISOU 2499 O ALA A 243 2130 2966 2210 176 363 13 O ATOM 2500 CB ALA A 243 -12.024 -7.796 16.241 1.00 20.30 C ANISOU 2500 CB ALA A 243 2250 3013 2450 279 299 1 C ATOM 2501 N ALEU A 244 -12.812 -6.642 13.402 0.58 19.05 N ANISOU 2501 N ALEU A 244 2180 2898 2159 214 429 -43 N ATOM 2502 N BLEU A 244 -12.807 -6.637 13.400 0.42 19.04 N ANISOU 2502 N BLEU A 244 2178 2897 2158 214 429 -43 N ATOM 2503 CA ALEU A 244 -12.466 -5.822 12.247 0.58 19.84 C ANISOU 2503 CA ALEU A 244 2287 3028 2222 191 500 -53 C ATOM 2504 CA BLEU A 244 -12.454 -5.798 12.258 0.42 19.86 C ANISOU 2504 CA BLEU A 244 2289 3031 2226 191 500 -52 C ATOM 2505 C ALEU A 244 -13.525 -4.758 11.981 0.58 18.52 C ANISOU 2505 C ALEU A 244 2169 2882 1986 138 469 -26 C ATOM 2506 C BLEU A 244 -13.528 -4.759 11.957 0.42 18.54 C ANISOU 2506 C BLEU A 244 2172 2885 1987 138 470 -27 C ATOM 2507 O ALEU A 244 -13.196 -3.617 11.640 0.58 18.45 O ANISOU 2507 O ALEU A 244 2145 2899 1967 109 495 -7 O ATOM 2508 O BLEU A 244 -13.205 -3.634 11.563 0.42 18.61 O ANISOU 2508 O BLEU A 244 2169 2919 1983 109 498 -8 O ATOM 2509 CB ALEU A 244 -12.279 -6.711 11.016 0.58 22.45 C ANISOU 2509 CB ALEU A 244 2672 3340 2519 214 570 -102 C ATOM 2510 CB BLEU A 244 -12.197 -6.663 11.023 0.42 22.31 C ANISOU 2510 CB BLEU A 244 2648 3324 2504 214 573 -101 C ATOM 2511 CG ALEU A 244 -11.849 -6.048 9.708 0.58 23.39 C ANISOU 2511 CG ALEU A 244 2813 3489 2583 190 660 -115 C ATOM 2512 CG BLEU A 244 -10.886 -7.451 11.024 0.42 23.95 C ANISOU 2512 CG BLEU A 244 2793 3518 2790 277 630 -135 C ATOM 2513 CD1ALEU A 244 -10.426 -5.517 9.816 0.58 25.82 C ANISOU 2513 CD1ALEU A 244 3019 3829 2963 202 725 -109 C ATOM 2514 CD1BLEU A 244 -10.700 -8.188 9.709 0.42 23.27 C ANISOU 2514 CD1BLEU A 244 2768 3416 2658 300 715 -193 C ATOM 2515 CD2ALEU A 244 -11.975 -7.028 8.549 0.58 25.06 C ANISOU 2515 CD2ALEU A 244 3108 3678 2735 210 715 -170 C ATOM 2516 CD2BLEU A 244 -9.715 -6.515 11.292 0.42 26.25 C ANISOU 2516 CD2BLEU A 244 2977 3852 3146 272 667 -114 C ATOM 2517 N CYS A 245 -14.803 -5.112 12.129 1.00 16.14 N ANISOU 2517 N CYS A 245 1922 2568 1643 124 413 -23 N ATOM 2518 CA CYS A 245 -15.878 -4.182 11.803 1.00 18.03 C ANISOU 2518 CA CYS A 245 2202 2826 1824 85 379 -2 C ATOM 2519 C CYS A 245 -16.069 -3.107 12.867 1.00 19.50 C ANISOU 2519 C CYS A 245 2341 3029 2038 74 332 31 C ATOM 2520 O CYS A 245 -16.522 -2.004 12.544 1.00 21.10 O ANISOU 2520 O CYS A 245 2561 3244 2210 51 319 49 O ATOM 2521 CB CYS A 245 -17.191 -4.942 11.599 1.00 21.27 C ANISOU 2521 CB CYS A 245 2670 3220 2191 73 332 -14 C ATOM 2522 SG CYS A 245 -17.231 -5.973 10.105 1.00 28.20 S ANISOU 2522 SG CYS A 245 3634 4072 3008 72 374 -60 S ATOM 2523 N TRP A 246 -15.755 -3.405 14.132 1.00 15.60 N ANISOU 2523 N TRP A 246 1797 2532 1597 93 303 38 N ATOM 2524 CA TRP A 246 -15.985 -2.456 15.219 1.00 16.94 C ANISOU 2524 CA TRP A 246 1935 2718 1784 84 257 60 C ATOM 2525 C TRP A 246 -14.750 -1.657 15.613 1.00 17.29 C ANISOU 2525 C TRP A 246 1923 2769 1878 83 269 69 C ATOM 2526 O TRP A 246 -14.899 -0.559 16.160 1.00 17.43 O ANISOU 2526 O TRP A 246 1931 2794 1898 67 239 83 O ATOM 2527 CB TRP A 246 -16.513 -3.180 16.463 1.00 19.32 C ANISOU 2527 CB TRP A 246 2228 3015 2096 94 210 66 C ATOM 2528 CG TRP A 246 -17.957 -3.548 16.360 1.00 19.07 C ANISOU 2528 CG TRP A 246 2236 2987 2022 78 186 66 C ATOM 2529 CD1 TRP A 246 -18.470 -4.742 15.961 1.00 17.93 C ANISOU 2529 CD1 TRP A 246 2126 2823 1863 73 187 55 C ATOM 2530 CD2 TRP A 246 -19.077 -2.699 16.640 1.00 17.29 C ANISOU 2530 CD2 TRP A 246 2013 2786 1771 63 157 73 C ATOM 2531 NE1 TRP A 246 -19.843 -4.698 15.986 1.00 20.25 N ANISOU 2531 NE1 TRP A 246 2436 3133 2126 48 157 59 N ATOM 2532 CE2 TRP A 246 -20.242 -3.454 16.401 1.00 20.11 C ANISOU 2532 CE2 TRP A 246 2393 3145 2103 47 141 70 C ATOM 2533 CE3 TRP A 246 -19.206 -1.374 17.074 1.00 16.04 C ANISOU 2533 CE3 TRP A 246 1837 2643 1614 64 141 79 C ATOM 2534 CZ2 TRP A 246 -21.523 -2.929 16.579 1.00 15.38 C ANISOU 2534 CZ2 TRP A 246 1786 2572 1485 35 114 73 C ATOM 2535 CZ3 TRP A 246 -20.483 -0.857 17.258 1.00 12.58 C ANISOU 2535 CZ3 TRP A 246 1400 2224 1154 60 115 79 C ATOM 2536 CH2 TRP A 246 -21.619 -1.633 17.010 1.00 12.88 C ANISOU 2536 CH2 TRP A 246 1447 2272 1173 48 103 76 C ATOM 2537 N LEU A 247 -13.548 -2.173 15.366 1.00 17.55 N ANISOU 2537 N LEU A 247 1915 2797 1955 101 311 59 N ATOM 2538 CA LEU A 247 -12.344 -1.452 15.775 1.00 18.02 C ANISOU 2538 CA LEU A 247 1905 2867 2074 94 316 69 C ATOM 2539 C LEU A 247 -12.224 -0.054 15.180 1.00 20.39 C ANISOU 2539 C LEU A 247 2213 3176 2359 50 338 84 C ATOM 2540 O LEU A 247 -11.808 0.856 15.920 1.00 23.43 O ANISOU 2540 O LEU A 247 2562 3563 2779 30 303 97 O ATOM 2541 CB LEU A 247 -11.094 -2.278 15.446 1.00 19.85 C ANISOU 2541 CB LEU A 247 2080 3099 2365 125 367 52 C ATOM 2542 CG LEU A 247 -10.682 -3.286 16.521 1.00 28.05 C ANISOU 2542 CG LEU A 247 3079 4121 3458 170 318 50 C ATOM 2543 CD1 LEU A 247 -9.537 -4.174 16.015 1.00 31.17 C ANISOU 2543 CD1 LEU A 247 3417 4509 3916 215 372 26 C ATOM 2544 CD2 LEU A 247 -10.291 -2.578 17.814 1.00 24.92 C ANISOU 2544 CD2 LEU A 247 2634 3734 3098 157 247 71 C ATOM 2545 N PRO A 248 -12.542 0.198 13.898 1.00 17.54 N ANISOU 2545 N PRO A 248 1904 2816 1945 30 388 85 N ATOM 2546 CA PRO A 248 -12.409 1.574 13.390 1.00 17.99 C ANISOU 2546 CA PRO A 248 1977 2871 1987 -16 401 110 C ATOM 2547 C PRO A 248 -13.162 2.599 14.219 1.00 15.33 C ANISOU 2547 C PRO A 248 1660 2520 1647 -28 326 125 C ATOM 2548 O PRO A 248 -12.592 3.646 14.543 1.00 16.87 O ANISOU 2548 O PRO A 248 1830 2704 1875 -58 314 140 O ATOM 2549 CB PRO A 248 -12.957 1.466 11.961 1.00 18.64 C ANISOU 2549 CB PRO A 248 2138 2953 1991 -29 447 112 C ATOM 2550 CG PRO A 248 -12.662 0.056 11.578 1.00 17.27 C ANISOU 2550 CG PRO A 248 1958 2787 1815 6 494 78 C ATOM 2551 CD PRO A 248 -12.943 -0.727 12.823 1.00 18.58 C ANISOU 2551 CD PRO A 248 2090 2945 2024 44 432 65 C ATOM 2552 N LEU A 249 -14.416 2.318 14.592 1.00 16.24 N ANISOU 2552 N LEU A 249 1813 2632 1725 -4 278 117 N ATOM 2553 CA LEU A 249 -15.153 3.228 15.467 1.00 17.64 C ANISOU 2553 CA LEU A 249 2001 2798 1902 -3 215 121 C ATOM 2554 C LEU A 249 -14.385 3.491 16.758 1.00 20.21 C ANISOU 2554 C LEU A 249 2274 3123 2281 -3 183 114 C ATOM 2555 O LEU A 249 -14.187 4.645 17.155 1.00 18.14 O ANISOU 2555 O LEU A 249 2012 2842 2036 -24 155 119 O ATOM 2556 CB LEU A 249 -16.531 2.648 15.789 1.00 17.57 C ANISOU 2556 CB LEU A 249 2019 2799 1857 24 181 109 C ATOM 2557 CG LEU A 249 -17.698 2.985 14.860 1.00 17.23 C ANISOU 2557 CG LEU A 249 2030 2751 1764 24 168 116 C ATOM 2558 CD1 LEU A 249 -18.917 2.172 15.255 1.00 17.67 C ANISOU 2558 CD1 LEU A 249 2088 2827 1802 45 140 102 C ATOM 2559 CD2 LEU A 249 -18.003 4.474 14.910 1.00 14.74 C ANISOU 2559 CD2 LEU A 249 1737 2412 1452 18 135 129 C ATOM 2560 N HIS A 250 -13.952 2.422 17.430 1.00 15.36 N ANISOU 2560 N HIS A 250 1620 2525 1691 19 179 104 N ATOM 2561 CA HIS A 250 -13.263 2.575 18.706 1.00 17.25 C ANISOU 2561 CA HIS A 250 1816 2766 1973 20 134 100 C ATOM 2562 C HIS A 250 -11.933 3.298 18.538 1.00 15.22 C ANISOU 2562 C HIS A 250 1507 2503 1774 -13 145 108 C ATOM 2563 O HIS A 250 -11.546 4.105 19.392 1.00 16.95 O ANISOU 2563 O HIS A 250 1709 2711 2019 -33 96 105 O ATOM 2564 CB HIS A 250 -13.056 1.205 19.347 1.00 17.93 C ANISOU 2564 CB HIS A 250 1878 2862 2071 53 121 95 C ATOM 2565 CG HIS A 250 -14.321 0.578 19.844 1.00 18.33 C ANISOU 2565 CG HIS A 250 1975 2920 2071 71 100 92 C ATOM 2566 ND1 HIS A 250 -15.027 1.078 20.917 1.00 18.86 N ANISOU 2566 ND1 HIS A 250 2063 2994 2108 71 57 87 N ATOM 2567 CD2 HIS A 250 -15.005 -0.510 19.417 1.00 17.24 C ANISOU 2567 CD2 HIS A 250 1862 2781 1906 86 120 91 C ATOM 2568 CE1 HIS A 250 -16.093 0.325 21.128 1.00 19.62 C ANISOU 2568 CE1 HIS A 250 2188 3101 2165 82 58 87 C ATOM 2569 NE2 HIS A 250 -16.101 -0.647 20.232 1.00 18.24 N ANISOU 2569 NE2 HIS A 250 2017 2919 1994 87 91 92 N ATOM 2570 N ILE A 251 -11.221 3.023 17.447 1.00 14.79 N ANISOU 2570 N ILE A 251 1426 2455 1740 -24 213 115 N ATOM 2571 CA ILE A 251 -9.960 3.715 17.201 1.00 15.88 C ANISOU 2571 CA ILE A 251 1501 2593 1938 -66 237 126 C ATOM 2572 C ILE A 251 -10.206 5.203 16.968 1.00 15.60 C ANISOU 2572 C ILE A 251 1510 2530 1888 -116 223 143 C ATOM 2573 O ILE A 251 -9.466 6.054 17.476 1.00 17.72 O ANISOU 2573 O ILE A 251 1742 2785 2206 -156 192 148 O ATOM 2574 CB ILE A 251 -9.215 3.061 16.022 1.00 18.46 C ANISOU 2574 CB ILE A 251 1793 2941 2282 -64 330 127 C ATOM 2575 CG1 ILE A 251 -8.746 1.651 16.409 1.00 21.66 C ANISOU 2575 CG1 ILE A 251 2144 3360 2726 -8 332 107 C ATOM 2576 CG2 ILE A 251 -8.024 3.917 15.592 1.00 19.06 C ANISOU 2576 CG2 ILE A 251 1806 3023 2414 -122 374 144 C ATOM 2577 CD1 ILE A 251 -8.252 0.819 15.238 1.00 21.84 C ANISOU 2577 CD1 ILE A 251 2149 3398 2752 13 429 92 C ATOM 2578 N ILE A 252 -11.256 5.540 16.215 1.00 15.31 N ANISOU 2578 N ILE A 252 1554 2478 1785 -116 237 152 N ATOM 2579 CA ILE A 252 -11.603 6.945 16.009 1.00 20.10 C ANISOU 2579 CA ILE A 252 2215 3045 2378 -153 213 170 C ATOM 2580 C ILE A 252 -11.907 7.622 17.339 1.00 17.16 C ANISOU 2580 C ILE A 252 1848 2649 2022 -145 131 150 C ATOM 2581 O ILE A 252 -11.442 8.736 17.604 1.00 18.13 O ANISOU 2581 O ILE A 252 1975 2736 2178 -188 101 157 O ATOM 2582 CB ILE A 252 -12.781 7.075 15.027 1.00 21.17 C ANISOU 2582 CB ILE A 252 2435 3169 2441 -140 225 184 C ATOM 2583 CG1 ILE A 252 -12.347 6.655 13.619 1.00 18.18 C ANISOU 2583 CG1 ILE A 252 2068 2807 2032 -163 309 204 C ATOM 2584 CG2 ILE A 252 -13.313 8.507 15.019 1.00 15.46 C ANISOU 2584 CG2 ILE A 252 1774 2393 1709 -161 179 200 C ATOM 2585 CD1 ILE A 252 -13.504 6.510 12.646 1.00 16.60 C ANISOU 2585 CD1 ILE A 252 1953 2603 1752 -146 310 213 C ATOM 2586 N ASN A 253 -12.686 6.961 18.201 1.00 16.28 N ANISOU 2586 N ASN A 253 1745 2556 1886 -95 94 125 N ATOM 2587 CA ASN A 253 -12.955 7.533 19.516 1.00 18.75 C ANISOU 2587 CA ASN A 253 2070 2853 2202 -85 25 99 C ATOM 2588 C ASN A 253 -11.672 7.737 20.310 1.00 19.77 C ANISOU 2588 C ASN A 253 2141 2981 2390 -118 -9 94 C ATOM 2589 O ASN A 253 -11.544 8.730 21.036 1.00 21.12 O ANISOU 2589 O ASN A 253 2332 3119 2574 -139 -63 78 O ATOM 2590 CB ASN A 253 -13.935 6.651 20.291 1.00 14.22 C ANISOU 2590 CB ASN A 253 1509 2309 1585 -33 8 77 C ATOM 2591 CG ASN A 253 -15.366 6.781 19.781 1.00 17.63 C ANISOU 2591 CG ASN A 253 1993 2738 1968 -4 18 75 C ATOM 2592 OD1 ASN A 253 -15.700 7.739 19.086 1.00 18.98 O ANISOU 2592 OD1 ASN A 253 2202 2875 2135 -14 17 85 O ATOM 2593 ND2 ASN A 253 -16.217 5.826 20.140 1.00 18.38 N ANISOU 2593 ND2 ASN A 253 2089 2866 2030 30 22 65 N ATOM 2594 N CYS A 254 -10.705 6.824 20.175 1.00 16.41 N ANISOU 2594 N CYS A 254 1644 2587 2005 -120 17 103 N ATOM 2595 CA CYS A 254 -9.426 7.022 20.849 1.00 17.11 C ANISOU 2595 CA CYS A 254 1661 2677 2162 -153 -22 101 C ATOM 2596 C CYS A 254 -8.723 8.282 20.346 1.00 16.73 C ANISOU 2596 C CYS A 254 1601 2595 2159 -224 -15 117 C ATOM 2597 O CYS A 254 -8.143 9.031 21.139 1.00 18.48 O ANISOU 2597 O CYS A 254 1807 2795 2420 -262 -80 106 O ATOM 2598 CB CYS A 254 -8.539 5.789 20.674 1.00 17.47 C ANISOU 2598 CB CYS A 254 1622 2762 2255 -131 8 109 C ATOM 2599 SG CYS A 254 -9.090 4.340 21.636 1.00 19.30 S ANISOU 2599 SG CYS A 254 1866 3017 2449 -60 -30 97 S ATOM 2600 N PHE A 255 -8.762 8.539 19.033 1.00 18.64 N ANISOU 2600 N PHE A 255 1859 2831 2393 -249 60 144 N ATOM 2601 CA PHE A 255 -8.146 9.759 18.510 1.00 19.96 C ANISOU 2601 CA PHE A 255 2028 2960 2597 -327 71 169 C ATOM 2602 C PHE A 255 -8.866 11.004 19.014 1.00 22.62 C ANISOU 2602 C PHE A 255 2453 3232 2910 -340 3 158 C ATOM 2603 O PHE A 255 -8.222 11.985 19.405 1.00 22.29 O ANISOU 2603 O PHE A 255 2403 3149 2916 -401 -41 158 O ATOM 2604 CB PHE A 255 -8.135 9.743 16.982 1.00 17.79 C ANISOU 2604 CB PHE A 255 1771 2690 2297 -351 168 206 C ATOM 2605 CG PHE A 255 -6.931 9.068 16.395 1.00 22.36 C ANISOU 2605 CG PHE A 255 2248 3318 2929 -375 247 218 C ATOM 2606 CD1 PHE A 255 -5.747 9.767 16.205 1.00 21.89 C ANISOU 2606 CD1 PHE A 255 2119 3255 2943 -456 270 240 C ATOM 2607 CD2 PHE A 255 -6.979 7.727 16.047 1.00 21.83 C ANISOU 2607 CD2 PHE A 255 2151 3299 2845 -315 300 203 C ATOM 2608 CE1 PHE A 255 -4.637 9.140 15.671 1.00 24.02 C ANISOU 2608 CE1 PHE A 255 2280 3578 3270 -472 352 246 C ATOM 2609 CE2 PHE A 255 -5.880 7.100 15.510 1.00 23.97 C ANISOU 2609 CE2 PHE A 255 2326 3614 3169 -323 378 206 C ATOM 2610 CZ PHE A 255 -4.705 7.805 15.323 1.00 24.22 C ANISOU 2610 CZ PHE A 255 2276 3650 3276 -399 408 226 C ATOM 2611 N THR A 256 -10.198 10.990 18.983 1.00 16.94 N ANISOU 2611 N THR A 256 1815 2500 2123 -284 -7 146 N ATOM 2612 CA THR A 256 -10.974 12.099 19.526 1.00 24.61 C ANISOU 2612 CA THR A 256 2866 3410 3074 -276 -70 125 C ATOM 2613 C THR A 256 -10.613 12.358 20.982 1.00 22.88 C ANISOU 2613 C THR A 256 2633 3182 2878 -278 -147 81 C ATOM 2614 O THR A 256 -10.382 13.505 21.382 1.00 25.63 O ANISOU 2614 O THR A 256 3018 3469 3252 -318 -200 68 O ATOM 2615 CB THR A 256 -12.468 11.791 19.395 1.00 22.02 C ANISOU 2615 CB THR A 256 2599 3090 2679 -202 -66 111 C ATOM 2616 OG1 THR A 256 -12.793 11.588 18.015 1.00 22.15 O ANISOU 2616 OG1 THR A 256 2637 3110 2667 -204 -7 151 O ATOM 2617 CG2 THR A 256 -13.313 12.931 19.959 1.00 21.98 C ANISOU 2617 CG2 THR A 256 2669 3021 2660 -178 -124 82 C ATOM 2618 N PHE A 257 -10.543 11.296 21.783 1.00 19.83 N ANISOU 2618 N PHE A 257 2203 2852 2480 -239 -160 60 N ATOM 2619 CA PHE A 257 -10.343 11.425 23.221 1.00 22.20 C ANISOU 2619 CA PHE A 257 2507 3150 2778 -234 -239 19 C ATOM 2620 C PHE A 257 -8.898 11.776 23.558 1.00 24.06 C ANISOU 2620 C PHE A 257 2676 3377 3089 -304 -284 24 C ATOM 2621 O PHE A 257 -8.644 12.718 24.317 1.00 23.27 O ANISOU 2621 O PHE A 257 2609 3231 3003 -339 -356 -5 O ATOM 2622 CB PHE A 257 -10.758 10.124 23.913 1.00 19.43 C ANISOU 2622 CB PHE A 257 2140 2861 2382 -174 -239 6 C ATOM 2623 CG PHE A 257 -10.660 10.170 25.409 1.00 20.91 C ANISOU 2623 CG PHE A 257 2347 3052 2544 -165 -318 -33 C ATOM 2624 CD1 PHE A 257 -11.487 11.006 26.145 1.00 19.52 C ANISOU 2624 CD1 PHE A 257 2255 2843 2317 -146 -352 -78 C ATOM 2625 CD2 PHE A 257 -9.757 9.364 26.083 1.00 22.31 C ANISOU 2625 CD2 PHE A 257 2467 3267 2745 -171 -359 -27 C ATOM 2626 CE1 PHE A 257 -11.405 11.046 27.521 1.00 22.61 C ANISOU 2626 CE1 PHE A 257 2679 3242 2668 -140 -420 -119 C ATOM 2627 CE2 PHE A 257 -9.673 9.401 27.462 1.00 27.09 C ANISOU 2627 CE2 PHE A 257 3105 3877 3312 -166 -440 -59 C ATOM 2628 CZ PHE A 257 -10.497 10.247 28.182 1.00 26.03 C ANISOU 2628 CZ PHE A 257 3062 3713 3113 -154 -467 -106 C ATOM 2629 N PHE A 258 -7.939 11.034 23.001 1.00 18.10 N ANISOU 2629 N PHE A 258 1824 2664 2388 -325 -243 56 N ATOM 2630 CA PHE A 258 -6.543 11.172 23.400 1.00 20.05 C ANISOU 2630 CA PHE A 258 1981 2918 2720 -384 -289 60 C ATOM 2631 C PHE A 258 -5.790 12.277 22.667 1.00 24.33 C ANISOU 2631 C PHE A 258 2500 3417 3328 -477 -271 86 C ATOM 2632 O PHE A 258 -4.714 12.675 23.130 1.00 23.77 O ANISOU 2632 O PHE A 258 2362 3339 3331 -540 -326 83 O ATOM 2633 CB PHE A 258 -5.797 9.850 23.195 1.00 20.58 C ANISOU 2633 CB PHE A 258 1940 3051 2829 -357 -254 79 C ATOM 2634 CG PHE A 258 -6.175 8.785 24.177 1.00 21.62 C ANISOU 2634 CG PHE A 258 2083 3217 2916 -286 -301 60 C ATOM 2635 CD1 PHE A 258 -6.010 8.995 25.538 1.00 25.23 C ANISOU 2635 CD1 PHE A 258 2560 3667 3359 -289 -408 32 C ATOM 2636 CD2 PHE A 258 -6.682 7.570 23.745 1.00 19.97 C ANISOU 2636 CD2 PHE A 258 1872 3044 2674 -222 -240 72 C ATOM 2637 CE1 PHE A 258 -6.357 8.018 26.450 1.00 24.77 C ANISOU 2637 CE1 PHE A 258 2523 3638 3248 -231 -450 23 C ATOM 2638 CE2 PHE A 258 -7.030 6.588 24.655 1.00 20.37 C ANISOU 2638 CE2 PHE A 258 1939 3118 2682 -165 -284 63 C ATOM 2639 CZ PHE A 258 -6.872 6.813 26.009 1.00 20.59 C ANISOU 2639 CZ PHE A 258 1991 3141 2691 -170 -386 42 C ATOM 2640 N CYS A 259 -6.302 12.779 21.538 1.00 27.90 N ANISOU 2640 N CYS A 259 3006 3838 3757 -492 -200 114 N ATOM 2641 CA CYS A 259 -5.627 13.827 20.767 1.00 27.42 C ANISOU 2641 CA CYS A 259 2937 3732 3750 -588 -174 150 C ATOM 2642 C CYS A 259 -6.573 15.004 20.551 1.00 30.97 C ANISOU 2642 C CYS A 259 3518 4094 4154 -595 -196 150 C ATOM 2643 O CYS A 259 -7.088 15.202 19.440 1.00 28.93 O ANISOU 2643 O CYS A 259 3312 3819 3861 -595 -130 188 O ATOM 2644 CB CYS A 259 -5.113 13.307 19.424 1.00 30.74 C ANISOU 2644 CB CYS A 259 3292 4197 4190 -612 -57 199 C ATOM 2645 SG CYS A 259 -4.041 14.523 18.575 1.00 39.94 S ANISOU 2645 SG CYS A 259 4426 5319 5431 -751 -17 251 S ATOM 2646 N PRO A 260 -6.809 15.824 21.582 1.00 31.83 N ANISOU 2646 N PRO A 260 3688 4144 4261 -600 -291 107 N ATOM 2647 CA PRO A 260 -7.624 17.034 21.379 1.00 34.94 C ANISOU 2647 CA PRO A 260 4206 4441 4627 -604 -316 103 C ATOM 2648 C PRO A 260 -6.975 18.055 20.460 1.00 37.84 C ANISOU 2648 C PRO A 260 4587 4742 5048 -709 -294 158 C ATOM 2649 O PRO A 260 -7.666 18.973 20.000 1.00 37.85 O ANISOU 2649 O PRO A 260 4695 4660 5026 -709 -302 172 O ATOM 2650 CB PRO A 260 -7.793 17.590 22.800 1.00 36.29 C ANISOU 2650 CB PRO A 260 4428 4569 4793 -589 -422 34 C ATOM 2651 CG PRO A 260 -6.608 17.064 23.548 1.00 36.81 C ANISOU 2651 CG PRO A 260 4388 4688 4910 -632 -464 22 C ATOM 2652 CD PRO A 260 -6.351 15.694 22.976 1.00 32.89 C ANISOU 2652 CD PRO A 260 3792 4291 4414 -598 -384 57 C ATOM 2653 N ASP A 261 -5.674 17.932 20.185 1.00 36.03 N ANISOU 2653 N ASP A 261 4252 4546 4892 -798 -266 190 N ATOM 2654 CA ASP A 261 -5.003 18.777 19.205 1.00 37.47 C ANISOU 2654 CA ASP A 261 4436 4680 5123 -910 -222 253 C ATOM 2655 C ASP A 261 -5.188 18.280 17.776 1.00 33.49 C ANISOU 2655 C ASP A 261 3929 4218 4576 -904 -101 314 C ATOM 2656 O ASP A 261 -4.822 18.994 16.836 1.00 32.04 O ANISOU 2656 O ASP A 261 3774 3993 4407 -993 -52 375 O ATOM 2657 CB ASP A 261 -3.507 18.870 19.522 1.00 45.34 C ANISOU 2657 CB ASP A 261 5304 5700 6223 -1016 -238 261 C ATOM 2658 CG ASP A 261 -3.234 19.434 20.908 1.00 56.30 C ANISOU 2658 CG ASP A 261 6702 7040 7650 -1038 -371 201 C ATOM 2659 OD1 ASP A 261 -4.072 20.208 21.419 1.00 58.37 O ANISOU 2659 OD1 ASP A 261 7093 7215 7870 -1007 -442 164 O ATOM 2660 OD2 ASP A 261 -2.174 19.102 21.485 1.00 60.51 O ANISOU 2660 OD2 ASP A 261 7114 7622 8257 -1083 -408 188 O ATOM 2661 N CYS A 262 -5.729 17.078 17.596 1.00 32.28 N ANISOU 2661 N CYS A 262 3751 4146 4367 -809 -52 300 N ATOM 2662 CA CYS A 262 -6.062 16.558 16.278 1.00 32.26 C ANISOU 2662 CA CYS A 262 3768 4182 4307 -791 53 346 C ATOM 2663 C CYS A 262 -7.474 16.981 15.899 1.00 29.98 C ANISOU 2663 C CYS A 262 3620 3836 3936 -730 29 352 C ATOM 2664 O CYS A 262 -8.390 16.936 16.725 1.00 30.26 O ANISOU 2664 O CYS A 262 3699 3853 3943 -648 -40 302 O ATOM 2665 CB CYS A 262 -5.971 15.029 16.252 1.00 34.85 C ANISOU 2665 CB CYS A 262 4007 4616 4619 -719 110 323 C ATOM 2666 SG CYS A 262 -4.357 14.273 16.578 1.00 44.11 S ANISOU 2666 SG CYS A 262 4996 5871 5894 -761 146 315 S ATOM 2667 N SER A 263 -7.649 17.389 14.644 1.00 27.80 N ANISOU 2667 N SER A 263 3412 3532 3620 -769 87 414 N ATOM 2668 CA SER A 263 -8.991 17.665 14.146 1.00 29.87 C ANISOU 2668 CA SER A 263 3797 3749 3804 -703 63 426 C ATOM 2669 C SER A 263 -9.852 16.414 14.257 1.00 27.20 C ANISOU 2669 C SER A 263 3437 3488 3409 -593 76 386 C ATOM 2670 O SER A 263 -9.381 15.294 14.042 1.00 22.30 O ANISOU 2670 O SER A 263 2734 2954 2784 -583 144 379 O ATOM 2671 CB SER A 263 -8.944 18.143 12.694 1.00 32.34 C ANISOU 2671 CB SER A 263 4186 4032 4071 -766 125 508 C ATOM 2672 OG SER A 263 -8.304 19.400 12.596 1.00 41.42 O ANISOU 2672 OG SER A 263 5375 5092 5269 -872 104 552 O ATOM 2673 N HIS A 264 -11.119 16.610 14.616 1.00 26.31 N ANISOU 2673 N HIS A 264 3395 3340 3260 -510 11 358 N ATOM 2674 CA HIS A 264 -12.035 15.485 14.736 1.00 26.29 C ANISOU 2674 CA HIS A 264 3375 3406 3208 -414 20 323 C ATOM 2675 C HIS A 264 -12.164 14.780 13.392 1.00 27.46 C ANISOU 2675 C HIS A 264 3539 3602 3295 -418 96 365 C ATOM 2676 O HIS A 264 -12.163 15.423 12.339 1.00 25.72 O ANISOU 2676 O HIS A 264 3391 3340 3043 -464 116 423 O ATOM 2677 CB HIS A 264 -13.396 15.980 15.219 1.00 24.08 C ANISOU 2677 CB HIS A 264 3166 3078 2906 -333 -56 291 C ATOM 2678 CG HIS A 264 -14.284 14.902 15.758 1.00 22.13 C ANISOU 2678 CG HIS A 264 2882 2899 2626 -244 -59 243 C ATOM 2679 ND1 HIS A 264 -14.815 13.910 14.964 1.00 24.36 N ANISOU 2679 ND1 HIS A 264 3158 3241 2856 -213 -16 258 N ATOM 2680 CD2 HIS A 264 -14.762 14.680 17.006 1.00 21.75 C ANISOU 2680 CD2 HIS A 264 2809 2868 2587 -187 -99 183 C ATOM 2681 CE1 HIS A 264 -15.566 13.111 15.702 1.00 22.51 C ANISOU 2681 CE1 HIS A 264 2890 3055 2609 -145 -30 212 C ATOM 2682 NE2 HIS A 264 -15.550 13.557 16.945 1.00 23.50 N ANISOU 2682 NE2 HIS A 264 3003 3158 2766 -128 -76 168 N ATOM 2683 N ALA A 265 -12.235 13.450 13.429 1.00 23.64 N ANISOU 2683 N ALA A 265 2993 3199 2788 -373 137 338 N ATOM 2684 CA ALA A 265 -12.484 12.690 12.214 1.00 23.27 C ANISOU 2684 CA ALA A 265 2971 3196 2674 -366 203 363 C ATOM 2685 C ALA A 265 -13.689 13.280 11.488 1.00 24.52 C ANISOU 2685 C ALA A 265 3239 3306 2770 -339 158 392 C ATOM 2686 O ALA A 265 -14.681 13.643 12.135 1.00 21.02 O ANISOU 2686 O ALA A 265 2822 2831 2335 -279 81 366 O ATOM 2687 CB ALA A 265 -12.739 11.215 12.539 1.00 22.08 C ANISOU 2687 CB ALA A 265 2760 3120 2509 -303 225 318 C ATOM 2688 N PRO A 266 -13.635 13.416 10.165 1.00 24.21 N ANISOU 2688 N PRO A 266 3267 3262 2669 -379 202 446 N ATOM 2689 CA PRO A 266 -14.720 14.093 9.445 1.00 25.27 C ANISOU 2689 CA PRO A 266 3512 3342 2747 -357 143 483 C ATOM 2690 C PRO A 266 -16.001 13.271 9.467 1.00 24.11 C ANISOU 2690 C PRO A 266 3368 3232 2561 -270 101 448 C ATOM 2691 O PRO A 266 -15.996 12.064 9.708 1.00 24.20 O ANISOU 2691 O PRO A 266 3315 3313 2566 -241 137 406 O ATOM 2692 CB PRO A 266 -14.171 14.237 8.021 1.00 23.54 C ANISOU 2692 CB PRO A 266 3363 3124 2459 -432 214 550 C ATOM 2693 CG PRO A 266 -13.160 13.143 7.899 1.00 27.26 C ANISOU 2693 CG PRO A 266 3747 3679 2932 -458 321 525 C ATOM 2694 CD PRO A 266 -12.569 12.943 9.266 1.00 24.25 C ANISOU 2694 CD PRO A 266 3250 3313 2649 -444 310 474 C ATOM 2695 N LEU A 267 -17.115 13.959 9.207 1.00 24.18 N ANISOU 2695 N LEU A 267 3451 3189 2549 -229 19 467 N ATOM 2696 CA LEU A 267 -18.427 13.329 9.338 1.00 27.62 C ANISOU 2696 CA LEU A 267 3873 3655 2964 -147 -33 432 C ATOM 2697 C LEU A 267 -18.569 12.127 8.412 1.00 23.34 C ANISOU 2697 C LEU A 267 3339 3181 2348 -152 11 434 C ATOM 2698 O LEU A 267 -19.145 11.106 8.801 1.00 22.65 O ANISOU 2698 O LEU A 267 3197 3148 2262 -107 7 388 O ATOM 2699 CB LEU A 267 -19.536 14.351 9.067 1.00 32.34 C ANISOU 2699 CB LEU A 267 4545 4182 3559 -102 -131 459 C ATOM 2700 CG LEU A 267 -20.978 13.842 9.168 1.00 38.08 C ANISOU 2700 CG LEU A 267 5249 4940 4280 -17 -195 427 C ATOM 2701 CD1 LEU A 267 -21.275 13.296 10.560 1.00 37.75 C ANISOU 2701 CD1 LEU A 267 5104 4942 4296 33 -189 353 C ATOM 2702 CD2 LEU A 267 -21.972 14.939 8.800 1.00 40.59 C ANISOU 2702 CD2 LEU A 267 5636 5181 4604 31 -295 458 C ATOM 2703 N TRP A 268 -18.047 12.222 7.184 1.00 22.71 N ANISOU 2703 N TRP A 268 3333 3098 2199 -212 57 486 N ATOM 2704 CA TRP A 268 -18.183 11.103 6.256 1.00 24.70 C ANISOU 2704 CA TRP A 268 3608 3409 2369 -216 99 479 C ATOM 2705 C TRP A 268 -17.455 9.865 6.763 1.00 25.42 C ANISOU 2705 C TRP A 268 3605 3566 2487 -215 181 425 C ATOM 2706 O TRP A 268 -17.897 8.736 6.513 1.00 22.65 O ANISOU 2706 O TRP A 268 3246 3261 2100 -188 189 391 O ATOM 2707 CB TRP A 268 -17.673 11.494 4.866 1.00 24.76 C ANISOU 2707 CB TRP A 268 3722 3402 2285 -285 145 544 C ATOM 2708 CG TRP A 268 -16.199 11.771 4.786 1.00 26.09 C ANISOU 2708 CG TRP A 268 3869 3574 2471 -361 251 565 C ATOM 2709 CD1 TRP A 268 -15.589 12.990 4.859 1.00 30.50 C ANISOU 2709 CD1 TRP A 268 4453 4071 3063 -418 252 616 C ATOM 2710 CD2 TRP A 268 -15.150 10.810 4.597 1.00 27.23 C ANISOU 2710 CD2 TRP A 268 3954 3784 2607 -391 370 536 C ATOM 2711 NE1 TRP A 268 -14.228 12.847 4.733 1.00 28.00 N ANISOU 2711 NE1 TRP A 268 4088 3787 2763 -488 367 623 N ATOM 2712 CE2 TRP A 268 -13.933 11.520 4.573 1.00 26.81 C ANISOU 2712 CE2 TRP A 268 3882 3717 2590 -467 442 572 C ATOM 2713 CE3 TRP A 268 -15.123 9.419 4.449 1.00 26.32 C ANISOU 2713 CE3 TRP A 268 3800 3734 2465 -360 421 481 C ATOM 2714 CZ2 TRP A 268 -12.704 10.886 4.413 1.00 28.17 C ANISOU 2714 CZ2 TRP A 268 3982 3946 2775 -506 567 553 C ATOM 2715 CZ3 TRP A 268 -13.903 8.792 4.289 1.00 25.26 C ANISOU 2715 CZ3 TRP A 268 3608 3648 2343 -391 542 460 C ATOM 2716 CH2 TRP A 268 -12.710 9.524 4.271 1.00 25.63 C ANISOU 2716 CH2 TRP A 268 3622 3688 2428 -461 616 495 C ATOM 2717 N LEU A 269 -16.345 10.056 7.482 1.00 22.67 N ANISOU 2717 N LEU A 269 3187 3219 2207 -244 233 415 N ATOM 2718 CA LEU A 269 -15.622 8.921 8.041 1.00 18.39 C ANISOU 2718 CA LEU A 269 2551 2732 1702 -235 298 367 C ATOM 2719 C LEU A 269 -16.377 8.319 9.221 1.00 19.01 C ANISOU 2719 C LEU A 269 2567 2827 1828 -169 240 316 C ATOM 2720 O LEU A 269 -16.416 7.093 9.375 1.00 19.59 O ANISOU 2720 O LEU A 269 2602 2944 1899 -143 265 279 O ATOM 2721 CB LEU A 269 -14.210 9.351 8.451 1.00 18.27 C ANISOU 2721 CB LEU A 269 2474 2715 1753 -287 358 376 C ATOM 2722 CG LEU A 269 -13.290 8.243 8.969 1.00 21.13 C ANISOU 2722 CG LEU A 269 2733 3131 2163 -275 423 332 C ATOM 2723 CD1 LEU A 269 -13.231 7.089 7.981 1.00 20.99 C ANISOU 2723 CD1 LEU A 269 2737 3158 2079 -265 495 314 C ATOM 2724 CD2 LEU A 269 -11.883 8.786 9.242 1.00 22.74 C ANISOU 2724 CD2 LEU A 269 2869 3335 2438 -334 476 347 C ATOM 2725 N MET A 270 -16.984 9.164 10.059 1.00 20.25 N ANISOU 2725 N MET A 270 2720 2947 2028 -143 165 314 N ATOM 2726 CA MET A 270 -17.872 8.664 11.105 1.00 20.80 C ANISOU 2726 CA MET A 270 2740 3036 2126 -83 115 270 C ATOM 2727 C MET A 270 -18.972 7.793 10.512 1.00 19.77 C ANISOU 2727 C MET A 270 2634 2936 1944 -52 94 259 C ATOM 2728 O MET A 270 -19.218 6.678 10.983 1.00 19.70 O ANISOU 2728 O MET A 270 2577 2966 1942 -30 104 224 O ATOM 2729 CB MET A 270 -18.484 9.829 11.887 1.00 18.72 C ANISOU 2729 CB MET A 270 2486 2725 1903 -55 44 266 C ATOM 2730 CG MET A 270 -17.470 10.764 12.526 1.00 23.21 C ANISOU 2730 CG MET A 270 3040 3252 2524 -91 49 272 C ATOM 2731 SD MET A 270 -16.293 9.878 13.564 1.00 27.30 S ANISOU 2731 SD MET A 270 3463 3819 3091 -107 96 236 S ATOM 2732 CE MET A 270 -17.405 9.043 14.700 1.00 26.66 C ANISOU 2732 CE MET A 270 3341 3777 3010 -35 58 184 C ATOM 2733 N TYR A 271 -19.647 8.292 9.471 1.00 17.91 N ANISOU 2733 N TYR A 271 2473 2676 1655 -55 56 293 N ATOM 2734 CA TYR A 271 -20.706 7.516 8.828 1.00 18.04 C ANISOU 2734 CA TYR A 271 2514 2719 1621 -33 22 284 C ATOM 2735 C TYR A 271 -20.170 6.203 8.277 1.00 20.49 C ANISOU 2735 C TYR A 271 2825 3070 1888 -56 90 264 C ATOM 2736 O TYR A 271 -20.819 5.157 8.399 1.00 22.16 O ANISOU 2736 O TYR A 271 3014 3312 2094 -36 74 232 O ATOM 2737 CB TYR A 271 -21.353 8.322 7.699 1.00 21.12 C ANISOU 2737 CB TYR A 271 2996 3074 1954 -38 -36 331 C ATOM 2738 CG TYR A 271 -22.278 9.428 8.153 1.00 27.76 C ANISOU 2738 CG TYR A 271 3837 3871 2839 8 -125 342 C ATOM 2739 CD1 TYR A 271 -22.761 9.469 9.455 1.00 29.72 C ANISOU 2739 CD1 TYR A 271 4003 4129 3161 56 -147 300 C ATOM 2740 CD2 TYR A 271 -22.674 10.432 7.272 1.00 34.83 C ANISOU 2740 CD2 TYR A 271 4819 4715 3700 6 -187 395 C ATOM 2741 CE1 TYR A 271 -23.608 10.482 9.870 1.00 32.38 C ANISOU 2741 CE1 TYR A 271 4337 4425 3541 108 -219 301 C ATOM 2742 CE2 TYR A 271 -23.523 11.447 7.674 1.00 34.97 C ANISOU 2742 CE2 TYR A 271 4836 4684 3767 61 -271 402 C ATOM 2743 CZ TYR A 271 -23.987 11.466 8.978 1.00 37.47 C ANISOU 2743 CZ TYR A 271 5063 5013 4163 114 -283 349 C ATOM 2744 OH TYR A 271 -24.833 12.476 9.395 1.00 41.88 O ANISOU 2744 OH TYR A 271 5616 5523 4773 178 -359 346 O ATOM 2745 N LEU A 272 -18.996 6.246 7.642 1.00 17.14 N ANISOU 2745 N LEU A 272 2429 2646 1437 -100 167 281 N ATOM 2746 CA LEU A 272 -18.414 5.033 7.082 1.00 19.71 C ANISOU 2746 CA LEU A 272 2758 3006 1725 -113 241 254 C ATOM 2747 C LEU A 272 -18.106 4.020 8.176 1.00 19.53 C ANISOU 2747 C LEU A 272 2645 3007 1769 -84 263 207 C ATOM 2748 O LEU A 272 -18.369 2.822 8.019 1.00 19.87 O ANISOU 2748 O LEU A 272 2688 3069 1793 -70 272 174 O ATOM 2749 CB LEU A 272 -17.154 5.384 6.290 1.00 22.54 C ANISOU 2749 CB LEU A 272 3148 3364 2052 -163 333 279 C ATOM 2750 CG LEU A 272 -16.476 4.223 5.563 1.00 28.10 C ANISOU 2750 CG LEU A 272 3863 4102 2711 -171 424 246 C ATOM 2751 CD1 LEU A 272 -17.446 3.571 4.590 1.00 28.94 C ANISOU 2751 CD1 LEU A 272 4059 4215 2723 -164 389 233 C ATOM 2752 CD2 LEU A 272 -15.217 4.702 4.839 1.00 29.70 C ANISOU 2752 CD2 LEU A 272 4083 4313 2890 -222 528 273 C ATOM 2753 N ALA A 273 -17.561 4.488 9.302 1.00 16.74 N ANISOU 2753 N ALA A 273 2221 2647 1492 -78 263 207 N ATOM 2754 CA ALA A 273 -17.247 3.595 10.413 1.00 14.76 C ANISOU 2754 CA ALA A 273 1893 2416 1301 -52 272 171 C ATOM 2755 C ALA A 273 -18.508 2.999 11.030 1.00 16.63 C ANISOU 2755 C ALA A 273 2118 2662 1539 -19 210 150 C ATOM 2756 O ALA A 273 -18.500 1.839 11.462 1.00 16.80 O ANISOU 2756 O ALA A 273 2110 2699 1575 -3 221 124 O ATOM 2757 CB ALA A 273 -16.441 4.349 11.472 1.00 14.65 C ANISOU 2757 CB ALA A 273 1819 2392 1357 -58 270 177 C ATOM 2758 N ILE A 274 -19.589 3.780 11.093 1.00 14.55 N ANISOU 2758 N ILE A 274 1874 2388 1266 -7 146 163 N ATOM 2759 CA ILE A 274 -20.856 3.278 11.615 1.00 15.25 C ANISOU 2759 CA ILE A 274 1940 2493 1360 20 94 145 C ATOM 2760 C ILE A 274 -21.451 2.233 10.675 1.00 16.22 C ANISOU 2760 C ILE A 274 2101 2629 1433 10 88 134 C ATOM 2761 O ILE A 274 -21.909 1.173 11.115 1.00 18.08 O ANISOU 2761 O ILE A 274 2309 2882 1680 15 82 111 O ATOM 2762 CB ILE A 274 -21.825 4.453 11.849 1.00 15.65 C ANISOU 2762 CB ILE A 274 1994 2530 1424 43 30 157 C ATOM 2763 CG1 ILE A 274 -21.369 5.295 13.045 1.00 15.21 C ANISOU 2763 CG1 ILE A 274 1900 2460 1420 56 30 151 C ATOM 2764 CG2 ILE A 274 -23.255 3.945 12.045 1.00 15.23 C ANISOU 2764 CG2 ILE A 274 1914 2502 1371 65 -19 141 C ATOM 2765 CD1 ILE A 274 -22.174 6.591 13.234 1.00 18.97 C ANISOU 2765 CD1 ILE A 274 2387 2906 1913 87 -27 158 C ATOM 2766 N AVAL A 275 -21.481 2.538 9.376 0.66 15.19 N ANISOU 2766 N AVAL A 275 2042 2487 1241 -9 85 153 N ATOM 2767 N BVAL A 275 -21.452 2.501 9.367 0.34 16.10 N ANISOU 2767 N BVAL A 275 2159 2603 1357 -10 88 152 N ATOM 2768 CA AVAL A 275 -21.978 1.593 8.380 0.66 17.27 C ANISOU 2768 CA AVAL A 275 2358 2758 1444 -24 75 138 C ATOM 2769 CA BVAL A 275 -22.041 1.527 8.450 0.34 17.19 C ANISOU 2769 CA BVAL A 275 2344 2751 1439 -22 72 136 C ATOM 2770 C AVAL A 275 -21.193 0.288 8.447 0.66 17.63 C ANISOU 2770 C AVAL A 275 2396 2810 1494 -29 140 103 C ATOM 2771 C BVAL A 275 -21.184 0.267 8.374 0.34 17.81 C ANISOU 2771 C BVAL A 275 2422 2832 1512 -30 142 103 C ATOM 2772 O AVAL A 275 -21.768 -0.805 8.392 0.66 19.34 O ANISOU 2772 O AVAL A 275 2617 3030 1701 -31 121 76 O ATOM 2773 O BVAL A 275 -21.706 -0.827 8.136 0.34 19.13 O ANISOU 2773 O BVAL A 275 2606 3002 1661 -34 126 76 O ATOM 2774 CB AVAL A 275 -21.914 2.231 6.976 0.66 19.47 C ANISOU 2774 CB AVAL A 275 2732 3024 1643 -47 69 167 C ATOM 2775 CB BVAL A 275 -22.280 2.141 7.053 0.34 19.62 C ANISOU 2775 CB BVAL A 275 2744 3045 1665 -42 47 164 C ATOM 2776 CG1AVAL A 275 -21.916 1.173 5.887 0.66 20.59 C ANISOU 2776 CG1AVAL A 275 2943 3172 1708 -69 89 142 C ATOM 2777 CG1BVAL A 275 -23.208 3.348 7.148 0.34 20.13 C ANISOU 2777 CG1BVAL A 275 2808 3096 1746 -23 -36 197 C ATOM 2778 CG2AVAL A 275 -23.074 3.203 6.778 0.66 20.24 C ANISOU 2778 CG2AVAL A 275 2846 3110 1735 -33 -26 197 C ATOM 2779 CG2BVAL A 275 -20.973 2.514 6.376 0.34 18.73 C ANISOU 2779 CG2BVAL A 275 2679 2923 1515 -69 129 181 C ATOM 2780 N LEU A 276 -19.869 0.384 8.585 1.00 17.37 N ANISOU 2780 N LEU A 276 2345 2774 1482 -30 214 103 N ATOM 2781 CA LEU A 276 -19.033 -0.812 8.661 1.00 19.64 C ANISOU 2781 CA LEU A 276 2616 3061 1784 -21 276 69 C ATOM 2782 C LEU A 276 -19.401 -1.670 9.868 1.00 17.12 C ANISOU 2782 C LEU A 276 2239 2742 1525 -1 247 52 C ATOM 2783 O LEU A 276 -19.560 -2.891 9.747 1.00 17.13 O ANISOU 2783 O LEU A 276 2257 2732 1519 3 251 23 O ATOM 2784 CB LEU A 276 -17.555 -0.416 8.712 1.00 21.16 C ANISOU 2784 CB LEU A 276 2775 3256 2007 -23 355 75 C ATOM 2785 CG LEU A 276 -16.552 -1.544 8.991 1.00 21.91 C ANISOU 2785 CG LEU A 276 2829 3350 2145 1 416 41 C ATOM 2786 CD1 LEU A 276 -16.595 -2.603 7.888 1.00 22.27 C ANISOU 2786 CD1 LEU A 276 2945 3388 2130 4 454 2 C ATOM 2787 CD2 LEU A 276 -15.145 -0.977 9.129 1.00 23.16 C ANISOU 2787 CD2 LEU A 276 2930 3518 2350 -3 483 52 C ATOM 2788 N ALA A 277 -19.548 -1.045 11.040 1.00 15.57 N ANISOU 2788 N ALA A 277 1983 2553 1379 10 217 69 N ATOM 2789 CA ALA A 277 -19.968 -1.780 12.227 1.00 18.21 C ANISOU 2789 CA ALA A 277 2273 2892 1756 23 190 60 C ATOM 2790 C ALA A 277 -21.304 -2.478 12.000 1.00 19.03 C ANISOU 2790 C ALA A 277 2398 2999 1834 9 144 50 C ATOM 2791 O ALA A 277 -21.470 -3.650 12.357 1.00 17.84 O ANISOU 2791 O ALA A 277 2244 2837 1696 5 142 36 O ATOM 2792 CB ALA A 277 -20.060 -0.833 13.420 1.00 14.36 C ANISOU 2792 CB ALA A 277 1734 2416 1307 33 164 76 C ATOM 2793 N HIS A 278 -22.268 -1.775 11.397 1.00 17.92 N ANISOU 2793 N HIS A 278 2279 2869 1662 0 100 61 N ATOM 2794 CA HIS A 278 -23.571 -2.378 11.126 1.00 17.72 C ANISOU 2794 CA HIS A 278 2261 2852 1620 -18 47 52 C ATOM 2795 C HIS A 278 -23.479 -3.530 10.131 1.00 17.80 C ANISOU 2795 C HIS A 278 2335 2840 1588 -40 55 27 C ATOM 2796 O HIS A 278 -24.250 -4.490 10.235 1.00 20.14 O ANISOU 2796 O HIS A 278 2630 3133 1889 -62 24 13 O ATOM 2797 CB HIS A 278 -24.549 -1.319 10.616 1.00 17.90 C ANISOU 2797 CB HIS A 278 2289 2889 1625 -15 -12 70 C ATOM 2798 CG HIS A 278 -24.945 -0.314 11.652 1.00 15.34 C ANISOU 2798 CG HIS A 278 1901 2581 1347 12 -29 83 C ATOM 2799 ND1 HIS A 278 -25.425 0.937 11.331 1.00 15.77 N ANISOU 2799 ND1 HIS A 278 1959 2633 1398 32 -71 101 N ATOM 2800 CD2 HIS A 278 -24.925 -0.373 13.005 1.00 18.33 C ANISOU 2800 CD2 HIS A 278 2220 2975 1771 25 -11 79 C ATOM 2801 CE1 HIS A 278 -25.694 1.602 12.441 1.00 19.08 C ANISOU 2801 CE1 HIS A 278 2321 3063 1865 60 -73 100 C ATOM 2802 NE2 HIS A 278 -25.392 0.833 13.471 1.00 17.44 N ANISOU 2802 NE2 HIS A 278 2076 2870 1681 54 -35 86 N ATOM 2803 N ATHR A 279 -22.560 -3.449 9.165 0.58 19.38 N ANISOU 2803 N ATHR A 279 2594 3026 1744 -38 101 18 N ATOM 2804 N BTHR A 279 -22.558 -3.459 9.159 0.42 19.46 N ANISOU 2804 N BTHR A 279 2604 3036 1754 -38 101 18 N ATOM 2805 CA ATHR A 279 -22.400 -4.523 8.191 0.58 21.20 C ANISOU 2805 CA ATHR A 279 2896 3233 1926 -52 118 -18 C ATOM 2806 CA BTHR A 279 -22.428 -4.548 8.193 0.42 21.16 C ANISOU 2806 CA BTHR A 279 2891 3228 1921 -53 116 -18 C ATOM 2807 C ATHR A 279 -22.008 -5.835 8.854 0.58 21.54 C ANISOU 2807 C ATHR A 279 2922 3249 2014 -44 144 -44 C ATOM 2808 C BTHR A 279 -21.996 -5.847 8.850 0.42 21.35 C ANISOU 2808 C BTHR A 279 2898 3224 1989 -43 145 -44 C ATOM 2809 O ATHR A 279 -22.282 -6.905 8.302 0.58 21.24 O ANISOU 2809 O ATHR A 279 2938 3182 1950 -59 133 -78 O ATOM 2810 O BTHR A 279 -22.193 -6.916 8.266 0.42 21.25 O ANISOU 2810 O BTHR A 279 2942 3182 1949 -58 138 -79 O ATOM 2811 CB ATHR A 279 -21.360 -4.122 7.138 0.58 22.54 C ANISOU 2811 CB ATHR A 279 3125 3399 2039 -48 184 -23 C ATOM 2812 CB BTHR A 279 -21.424 -4.218 7.080 0.42 22.40 C ANISOU 2812 CB BTHR A 279 3112 3380 2017 -50 181 -26 C ATOM 2813 OG1ATHR A 279 -21.738 -2.869 6.552 0.58 22.10 O ANISOU 2813 OG1ATHR A 279 3096 3360 1940 -60 152 12 O ATOM 2814 OG1BTHR A 279 -20.195 -3.740 7.646 0.42 22.01 O ANISOU 2814 OG1BTHR A 279 3012 3336 2015 -26 249 -14 O ATOM 2815 CG2ATHR A 279 -21.252 -5.171 6.036 0.58 21.85 C ANISOU 2815 CG2ATHR A 279 3127 3290 1886 -60 205 -70 C ATOM 2816 CG2BTHR A 279 -21.996 -3.199 6.102 0.42 21.83 C ANISOU 2816 CG2BTHR A 279 3097 3322 1875 -70 139 0 C ATOM 2817 N ASN A 280 -21.393 -5.780 10.038 1.00 18.16 N ANISOU 2817 N ASN A 280 2427 2822 1650 -20 169 -29 N ATOM 2818 CA ASN A 280 -21.070 -7.011 10.748 1.00 21.41 C ANISOU 2818 CA ASN A 280 2827 3202 2106 -9 180 -44 C ATOM 2819 C ASN A 280 -22.325 -7.805 11.086 1.00 20.47 C ANISOU 2819 C ASN A 280 2712 3072 1992 -46 120 -44 C ATOM 2820 O ASN A 280 -22.262 -9.031 11.243 1.00 21.02 O ANISOU 2820 O ASN A 280 2808 3098 2079 -51 119 -61 O ATOM 2821 CB ASN A 280 -20.292 -6.715 12.024 1.00 22.38 C ANISOU 2821 CB ASN A 280 2880 3333 2291 19 199 -21 C ATOM 2822 CG ASN A 280 -19.894 -7.977 12.742 1.00 24.34 C ANISOU 2822 CG ASN A 280 3125 3541 2582 34 201 -28 C ATOM 2823 OD1 ASN A 280 -19.011 -8.701 12.287 1.00 27.16 O ANISOU 2823 OD1 ASN A 280 3506 3862 2950 62 240 -57 O ATOM 2824 ND2 ASN A 280 -20.561 -8.269 13.845 1.00 22.28 N ANISOU 2824 ND2 ASN A 280 2838 3283 2345 17 162 -3 N ATOM 2825 N SER A 281 -23.468 -7.133 11.202 1.00 19.06 N ANISOU 2825 N SER A 281 2505 2930 1805 -71 70 -23 N ATOM 2826 CA SER A 281 -24.720 -7.842 11.432 1.00 23.80 C ANISOU 2826 CA SER A 281 3098 3531 2415 -115 17 -22 C ATOM 2827 C SER A 281 -25.237 -8.541 10.182 1.00 26.05 C ANISOU 2827 C SER A 281 3456 3789 2654 -149 -18 -54 C ATOM 2828 O SER A 281 -26.250 -9.243 10.264 1.00 27.23 O ANISOU 2828 O SER A 281 3601 3932 2815 -196 -68 -57 O ATOM 2829 CB SER A 281 -25.773 -6.876 11.972 1.00 23.32 C ANISOU 2829 CB SER A 281 2967 3523 2370 -123 -20 6 C ATOM 2830 OG SER A 281 -25.451 -6.475 13.297 1.00 24.76 O ANISOU 2830 OG SER A 281 3091 3726 2592 -101 8 29 O ATOM 2831 N VAL A 282 -24.569 -8.369 9.044 1.00 26.02 N ANISOU 2831 N VAL A 282 3520 3771 2594 -132 7 -80 N ATOM 2832 CA VAL A 282 -24.932 -9.057 7.813 1.00 24.78 C ANISOU 2832 CA VAL A 282 3453 3586 2378 -162 -24 -119 C ATOM 2833 C VAL A 282 -24.045 -10.272 7.542 1.00 24.80 C ANISOU 2833 C VAL A 282 3521 3525 2376 -147 25 -165 C ATOM 2834 O VAL A 282 -24.509 -11.221 6.889 1.00 25.71 O ANISOU 2834 O VAL A 282 3707 3599 2461 -180 -11 -204 O ATOM 2835 CB VAL A 282 -24.891 -8.086 6.607 1.00 22.37 C ANISOU 2835 CB VAL A 282 3201 3306 1994 -157 -30 -120 C ATOM 2836 CG1 VAL A 282 -25.435 -8.742 5.336 1.00 21.34 C ANISOU 2836 CG1 VAL A 282 3171 3151 1786 -195 -79 -160 C ATOM 2837 CG2 VAL A 282 -25.660 -6.804 6.921 1.00 19.72 C ANISOU 2837 CG2 VAL A 282 2799 3020 1674 -157 -79 -73 C ATOM 2838 N VAL A 283 -22.805 -10.293 8.044 1.00 20.93 N ANISOU 2838 N VAL A 283 3008 3024 1922 -96 99 -165 N ATOM 2839 CA VAL A 283 -21.819 -11.235 7.517 1.00 23.60 C ANISOU 2839 CA VAL A 283 3409 3307 2250 -63 156 -217 C ATOM 2840 C VAL A 283 -21.957 -12.641 8.105 1.00 23.06 C ANISOU 2840 C VAL A 283 3360 3170 2234 -70 133 -234 C ATOM 2841 O VAL A 283 -21.649 -13.622 7.419 1.00 25.45 O ANISOU 2841 O VAL A 283 3743 3411 2515 -59 149 -290 O ATOM 2842 CB VAL A 283 -20.391 -10.694 7.721 1.00 26.36 C ANISOU 2842 CB VAL A 283 3716 3673 2625 -4 243 -212 C ATOM 2843 CG1 VAL A 283 -20.219 -9.367 7.000 1.00 27.79 C ANISOU 2843 CG1 VAL A 283 3899 3911 2750 -8 269 -195 C ATOM 2844 CG2 VAL A 283 -20.066 -10.553 9.202 1.00 29.67 C ANISOU 2844 CG2 VAL A 283 4041 4100 3131 18 239 -168 C ATOM 2845 N ASN A 284 -22.399 -12.781 9.357 1.00 22.81 N ANISOU 2845 N ASN A 284 3263 3139 2264 -87 99 -189 N ATOM 2846 CA ASN A 284 -22.408 -14.105 9.981 1.00 26.29 C ANISOU 2846 CA ASN A 284 3728 3506 2754 -94 80 -194 C ATOM 2847 C ASN A 284 -23.234 -15.147 9.227 1.00 27.32 C ANISOU 2847 C ASN A 284 3947 3578 2857 -149 29 -235 C ATOM 2848 O ASN A 284 -22.730 -16.270 9.048 1.00 27.79 O ANISOU 2848 O ASN A 284 4073 3552 2933 -127 40 -275 O ATOM 2849 CB ASN A 284 -22.874 -13.993 11.440 1.00 28.23 C ANISOU 2849 CB ASN A 284 3898 3774 3054 -118 52 -130 C ATOM 2850 CG ASN A 284 -21.870 -13.260 12.318 1.00 30.72 C ANISOU 2850 CG ASN A 284 4144 4124 3404 -60 95 -98 C ATOM 2851 OD1 ASN A 284 -20.827 -12.798 11.841 1.00 28.18 O ANISOU 2851 OD1 ASN A 284 3818 3813 3077 -7 146 -120 O ATOM 2852 ND2 ASN A 284 -22.186 -13.136 13.601 1.00 33.70 N ANISOU 2852 ND2 ASN A 284 4468 4522 3814 -77 75 -46 N ATOM 2853 N PRO A 285 -24.459 -14.873 8.759 1.00 25.77 N ANISOU 2853 N PRO A 285 3755 3415 2623 -216 -32 -231 N ATOM 2854 CA PRO A 285 -25.161 -15.893 7.959 1.00 25.88 C ANISOU 2854 CA PRO A 285 3858 3367 2608 -272 -88 -278 C ATOM 2855 C PRO A 285 -24.352 -16.382 6.769 1.00 28.68 C ANISOU 2855 C PRO A 285 4324 3668 2906 -231 -50 -355 C ATOM 2856 O PRO A 285 -24.452 -17.560 6.407 1.00 30.24 O ANISOU 2856 O PRO A 285 4609 3779 3103 -251 -75 -403 O ATOM 2857 CB PRO A 285 -26.440 -15.173 7.514 1.00 26.54 C ANISOU 2857 CB PRO A 285 3911 3517 2656 -335 -159 -260 C ATOM 2858 CG PRO A 285 -26.671 -14.153 8.564 1.00 27.73 C ANISOU 2858 CG PRO A 285 3942 3745 2849 -325 -147 -194 C ATOM 2859 CD PRO A 285 -25.298 -13.679 8.970 1.00 26.22 C ANISOU 2859 CD PRO A 285 3733 3560 2671 -243 -63 -186 C ATOM 2860 N PHE A 286 -23.528 -15.517 6.167 1.00 27.59 N ANISOU 2860 N PHE A 286 4187 3577 2720 -175 15 -368 N ATOM 2861 CA PHE A 286 -22.717 -15.932 5.027 1.00 27.23 C ANISOU 2861 CA PHE A 286 4243 3492 2611 -134 71 -445 C ATOM 2862 C PHE A 286 -21.568 -16.832 5.454 1.00 30.01 C ANISOU 2862 C PHE A 286 4605 3771 3027 -62 137 -476 C ATOM 2863 O PHE A 286 -21.208 -17.769 4.731 1.00 31.20 O ANISOU 2863 O PHE A 286 4854 3848 3151 -40 158 -552 O ATOM 2864 CB PHE A 286 -22.192 -14.704 4.287 1.00 30.06 C ANISOU 2864 CB PHE A 286 4595 3927 2899 -106 129 -440 C ATOM 2865 CG PHE A 286 -23.228 -14.028 3.457 1.00 34.07 C ANISOU 2865 CG PHE A 286 5140 4482 3322 -165 59 -431 C ATOM 2866 CD1 PHE A 286 -24.044 -13.054 4.007 1.00 33.70 C ANISOU 2866 CD1 PHE A 286 5005 4500 3300 -197 2 -361 C ATOM 2867 CD2 PHE A 286 -23.411 -14.388 2.131 1.00 35.05 C ANISOU 2867 CD2 PHE A 286 5391 4584 3342 -187 44 -493 C ATOM 2868 CE1 PHE A 286 -25.017 -12.443 3.246 1.00 36.31 C ANISOU 2868 CE1 PHE A 286 5364 4870 3563 -244 -75 -350 C ATOM 2869 CE2 PHE A 286 -24.378 -13.776 1.363 1.00 37.98 C ANISOU 2869 CE2 PHE A 286 5799 4997 3633 -242 -37 -480 C ATOM 2870 CZ PHE A 286 -25.185 -12.805 1.922 1.00 37.60 C ANISOU 2870 CZ PHE A 286 5654 5011 3622 -268 -100 -406 C ATOM 2871 N ILE A 287 -20.972 -16.564 6.618 1.00 31.18 N ANISOU 2871 N ILE A 287 4654 3936 3257 -22 165 -423 N ATOM 2872 CA ILE A 287 -19.931 -17.454 7.116 1.00 32.69 C ANISOU 2872 CA ILE A 287 4846 4053 3520 50 208 -445 C ATOM 2873 C ILE A 287 -20.509 -18.831 7.425 1.00 30.65 C ANISOU 2873 C ILE A 287 4657 3689 3300 16 142 -460 C ATOM 2874 O ILE A 287 -19.910 -19.858 7.083 1.00 33.76 O ANISOU 2874 O ILE A 287 5124 3990 3712 65 164 -522 O ATOM 2875 CB ILE A 287 -19.239 -16.839 8.343 1.00 30.55 C ANISOU 2875 CB ILE A 287 4456 3825 3325 92 232 -379 C ATOM 2876 CG1 ILE A 287 -18.729 -15.433 8.022 1.00 31.00 C ANISOU 2876 CG1 ILE A 287 4449 3981 3348 110 290 -362 C ATOM 2877 CG2 ILE A 287 -18.096 -17.736 8.811 1.00 29.84 C ANISOU 2877 CG2 ILE A 287 4362 3660 3315 175 266 -401 C ATOM 2878 CD1 ILE A 287 -17.661 -15.396 6.947 1.00 32.02 C ANISOU 2878 CD1 ILE A 287 4613 4112 3441 169 385 -427 C ATOM 2879 N TYR A 288 -21.682 -18.878 8.066 1.00 24.83 N ANISOU 2879 N TYR A 288 3897 2960 2577 -68 62 -405 N ATOM 2880 CA TYR A 288 -22.304 -20.168 8.356 1.00 29.11 C ANISOU 2880 CA TYR A 288 4506 3399 3155 -119 -3 -411 C ATOM 2881 C TYR A 288 -22.618 -20.927 7.072 1.00 30.86 C ANISOU 2881 C TYR A 288 4856 3552 3317 -144 -25 -500 C ATOM 2882 O TYR A 288 -22.401 -22.141 6.990 1.00 32.49 O ANISOU 2882 O TYR A 288 5150 3641 3555 -131 -40 -544 O ATOM 2883 CB TYR A 288 -23.578 -19.975 9.181 1.00 29.68 C ANISOU 2883 CB TYR A 288 4519 3510 3246 -217 -73 -337 C ATOM 2884 CG TYR A 288 -23.382 -19.246 10.493 1.00 29.38 C ANISOU 2884 CG TYR A 288 4369 3539 3254 -200 -54 -254 C ATOM 2885 CD1 TYR A 288 -22.263 -19.478 11.286 1.00 32.69 C ANISOU 2885 CD1 TYR A 288 4768 3926 3729 -123 -16 -234 C ATOM 2886 CD2 TYR A 288 -24.321 -18.323 10.936 1.00 25.98 C ANISOU 2886 CD2 TYR A 288 3855 3205 2811 -258 -78 -200 C ATOM 2887 CE1 TYR A 288 -22.087 -18.809 12.488 1.00 31.67 C ANISOU 2887 CE1 TYR A 288 4547 3857 3630 -112 -7 -163 C ATOM 2888 CE2 TYR A 288 -24.154 -17.647 12.125 1.00 25.53 C ANISOU 2888 CE2 TYR A 288 3706 3207 2785 -241 -58 -135 C ATOM 2889 CZ TYR A 288 -23.039 -17.893 12.901 1.00 31.35 C ANISOU 2889 CZ TYR A 288 4435 3910 3566 -172 -25 -116 C ATOM 2890 OH TYR A 288 -22.881 -17.210 14.089 1.00 31.82 O ANISOU 2890 OH TYR A 288 4414 4028 3647 -161 -14 -54 O ATOM 2891 N ALA A 289 -23.110 -20.222 6.049 1.00 31.47 N ANISOU 2891 N ALA A 289 4954 3696 3306 -177 -34 -527 N ATOM 2892 CA ALA A 289 -23.497 -20.881 4.806 1.00 31.86 C ANISOU 2892 CA ALA A 289 5135 3688 3282 -211 -67 -612 C ATOM 2893 C ALA A 289 -22.290 -21.398 4.033 1.00 36.77 C ANISOU 2893 C ALA A 289 5845 4249 3876 -117 18 -703 C ATOM 2894 O ALA A 289 -22.374 -22.449 3.386 1.00 37.80 O ANISOU 2894 O ALA A 289 6099 4279 3984 -125 -5 -782 O ATOM 2895 CB ALA A 289 -24.310 -19.923 3.935 1.00 27.98 C ANISOU 2895 CB ALA A 289 4645 3290 2697 -268 -106 -611 C ATOM 2896 N TYR A 290 -21.164 -20.683 4.076 1.00 38.53 N ANISOU 2896 N TYR A 290 6007 4531 4103 -28 118 -698 N ATOM 2897 CA TYR A 290 -19.990 -21.089 3.317 1.00 40.39 C ANISOU 2897 CA TYR A 290 6307 4725 4315 65 215 -787 C ATOM 2898 C TYR A 290 -19.111 -22.089 4.053 1.00 40.22 C ANISOU 2898 C TYR A 290 6276 4603 4402 148 243 -803 C ATOM 2899 O TYR A 290 -18.372 -22.835 3.400 1.00 40.63 O ANISOU 2899 O TYR A 290 6408 4582 4447 220 302 -895 O ATOM 2900 CB TYR A 290 -19.152 -19.863 2.936 1.00 47.16 C ANISOU 2900 CB TYR A 290 7097 5694 5128 116 316 -776 C ATOM 2901 CG TYR A 290 -19.636 -19.166 1.685 1.00 57.00 C ANISOU 2901 CG TYR A 290 8417 7006 6236 66 318 -803 C ATOM 2902 CD1 TYR A 290 -19.374 -19.698 0.429 1.00 62.66 C ANISOU 2902 CD1 TYR A 290 9269 7683 6855 84 362 -906 C ATOM 2903 CD2 TYR A 290 -20.356 -17.980 1.758 1.00 62.43 C ANISOU 2903 CD2 TYR A 290 9046 7791 6886 4 272 -728 C ATOM 2904 CE1 TYR A 290 -19.816 -19.073 -0.722 1.00 66.14 C ANISOU 2904 CE1 TYR A 290 9791 8183 7155 36 356 -927 C ATOM 2905 CE2 TYR A 290 -20.803 -17.345 0.611 1.00 66.22 C ANISOU 2905 CE2 TYR A 290 9600 8323 7237 -39 261 -746 C ATOM 2906 CZ TYR A 290 -20.530 -17.897 -0.625 1.00 68.49 C ANISOU 2906 CZ TYR A 290 10028 8574 7420 -26 301 -842 C ATOM 2907 OH TYR A 290 -20.973 -17.274 -1.768 1.00 72.21 O ANISOU 2907 OH TYR A 290 10588 9098 7751 -73 282 -855 O ATOM 2908 N ARG A 291 -19.183 -22.140 5.386 1.00 36.62 N ANISOU 2908 N ARG A 291 5730 4137 4045 142 201 -718 N ATOM 2909 CA ARG A 291 -18.265 -22.954 6.171 1.00 37.51 C ANISOU 2909 CA ARG A 291 5824 4163 4265 229 220 -718 C ATOM 2910 C ARG A 291 -18.913 -24.104 6.931 1.00 37.61 C ANISOU 2910 C ARG A 291 5892 4056 4343 182 125 -689 C ATOM 2911 O ARG A 291 -18.192 -25.019 7.344 1.00 43.07 O ANISOU 2911 O ARG A 291 6609 4642 5114 258 129 -707 O ATOM 2912 CB ARG A 291 -17.498 -22.077 7.175 1.00 37.26 C ANISOU 2912 CB ARG A 291 5645 4214 4298 280 258 -640 C ATOM 2913 CG ARG A 291 -16.611 -21.020 6.526 1.00 37.28 C ANISOU 2913 CG ARG A 291 5585 4321 4260 336 363 -665 C ATOM 2914 CD ARG A 291 -15.568 -20.504 7.499 1.00 39.72 C ANISOU 2914 CD ARG A 291 5760 4673 4658 406 400 -610 C ATOM 2915 NE ARG A 291 -14.840 -21.599 8.136 1.00 45.04 N ANISOU 2915 NE ARG A 291 6437 5240 5437 489 387 -622 N ATOM 2916 CZ ARG A 291 -13.700 -22.111 7.683 1.00 47.49 C ANISOU 2916 CZ ARG A 291 6747 5505 5791 599 462 -696 C ATOM 2917 NH1 ARG A 291 -13.145 -21.625 6.580 1.00 46.47 N ANISOU 2917 NH1 ARG A 291 6617 5437 5603 631 567 -765 N ATOM 2918 NH2 ARG A 291 -13.113 -23.111 8.333 1.00 47.15 N ANISOU 2918 NH2 ARG A 291 6706 5357 5852 677 432 -700 N ATOM 2919 N ILE A 292 -20.227 -24.095 7.134 1.00 33.14 N ANISOU 2919 N ILE A 292 5341 3500 3750 61 39 -643 N ATOM 2920 CA ILE A 292 -20.908 -25.127 7.913 1.00 34.61 C ANISOU 2920 CA ILE A 292 5573 3580 3997 -4 -47 -601 C ATOM 2921 C ILE A 292 -21.943 -25.785 7.014 1.00 36.06 C ANISOU 2921 C ILE A 292 5875 3701 4125 -99 -113 -660 C ATOM 2922 O ILE A 292 -22.958 -25.168 6.667 1.00 35.34 O ANISOU 2922 O ILE A 292 5762 3692 3974 -193 -153 -642 O ATOM 2923 CB ILE A 292 -21.560 -24.562 9.182 1.00 36.70 C ANISOU 2923 CB ILE A 292 5731 3918 4295 -74 -88 -482 C ATOM 2924 CG1 ILE A 292 -20.539 -23.756 9.991 1.00 36.93 C ANISOU 2924 CG1 ILE A 292 5645 4022 4364 15 -29 -430 C ATOM 2925 CG2 ILE A 292 -22.141 -25.694 10.027 1.00 37.53 C ANISOU 2925 CG2 ILE A 292 5889 3907 4462 -141 -164 -433 C ATOM 2926 CD1 ILE A 292 -21.126 -23.056 11.196 1.00 36.69 C ANISOU 2926 CD1 ILE A 292 5515 4076 4349 -46 -58 -323 C ATOM 2927 N ARG A 293 -21.700 -27.048 6.655 1.00 38.45 N ANISOU 2927 N ARG A 293 6304 3853 4454 -74 -133 -732 N ATOM 2928 CA ARG A 293 -22.557 -27.731 5.689 1.00 42.08 C ANISOU 2928 CA ARG A 293 6894 4239 4857 -158 -196 -806 C ATOM 2929 C ARG A 293 -23.985 -27.875 6.204 1.00 38.41 C ANISOU 2929 C ARG A 293 6410 3777 4405 -314 -300 -732 C ATOM 2930 O ARG A 293 -24.943 -27.731 5.436 1.00 38.19 O ANISOU 2930 O ARG A 293 6418 3781 4311 -408 -356 -762 O ATOM 2931 CB ARG A 293 -21.968 -29.100 5.348 1.00 48.00 C ANISOU 2931 CB ARG A 293 7785 4809 5645 -95 -199 -896 C ATOM 2932 CG ARG A 293 -22.791 -29.905 4.362 1.00 58.79 C ANISOU 2932 CG ARG A 293 9304 6080 6954 -181 -272 -983 C ATOM 2933 CD ARG A 293 -22.134 -31.244 4.053 1.00 68.90 C ANISOU 2933 CD ARG A 293 10731 7171 8278 -105 -269 -1080 C ATOM 2934 NE ARG A 293 -20.881 -31.084 3.319 1.00 77.93 N ANISOU 2934 NE ARG A 293 11895 8327 9389 49 -153 -1179 N ATOM 2935 CZ ARG A 293 -19.673 -31.137 3.873 1.00 83.56 C ANISOU 2935 CZ ARG A 293 12544 9021 10182 188 -77 -1170 C ATOM 2936 NH1 ARG A 293 -19.543 -31.353 5.176 1.00 83.19 N ANISOU 2936 NH1 ARG A 293 12424 8939 10246 195 -114 -1064 N ATOM 2937 NH2 ARG A 293 -18.592 -30.977 3.120 1.00 87.29 N ANISOU 2937 NH2 ARG A 293 13027 9515 10625 319 36 -1266 N ATOM 2938 N GLU A 294 -24.151 -28.152 7.500 1.00 38.24 N ANISOU 2938 N GLU A 294 6332 3730 4469 -345 -328 -633 N ATOM 2939 CA GLU A 294 -25.493 -28.344 8.041 1.00 40.59 C ANISOU 2939 CA GLU A 294 6604 4033 4786 -497 -413 -560 C ATOM 2940 C GLU A 294 -26.317 -27.063 7.952 1.00 39.00 C ANISOU 2940 C GLU A 294 6282 4005 4532 -560 -415 -517 C ATOM 2941 O GLU A 294 -27.525 -27.115 7.691 1.00 37.43 O ANISOU 2941 O GLU A 294 6079 3827 4317 -684 -488 -509 O ATOM 2942 CB GLU A 294 -25.413 -28.842 9.485 1.00 44.96 C ANISOU 2942 CB GLU A 294 7124 4531 5428 -513 -426 -458 C ATOM 2943 CG GLU A 294 -26.720 -29.418 10.015 1.00 49.50 C ANISOU 2943 CG GLU A 294 7706 5068 6033 -677 -508 -392 C ATOM 2944 CD GLU A 294 -27.101 -30.728 9.351 1.00 56.71 C ANISOU 2944 CD GLU A 294 8775 5813 6961 -742 -581 -460 C ATOM 2945 OE1 GLU A 294 -26.191 -31.475 8.934 1.00 60.31 O ANISOU 2945 OE1 GLU A 294 9345 6139 7431 -645 -568 -535 O ATOM 2946 OE2 GLU A 294 -28.312 -31.013 9.244 1.00 59.40 O ANISOU 2946 OE2 GLU A 294 9120 6148 7301 -891 -654 -443 O ATOM 2947 N PHE A 295 -25.683 -25.900 8.165 1.00 32.58 N ANISOU 2947 N PHE A 295 5366 3315 3699 -477 -341 -490 N ATOM 2948 CA PHE A 295 -26.385 -24.636 7.954 1.00 32.97 C ANISOU 2948 CA PHE A 295 5314 3518 3697 -519 -344 -460 C ATOM 2949 C PHE A 295 -26.684 -24.415 6.477 1.00 34.84 C ANISOU 2949 C PHE A 295 5621 3774 3842 -534 -367 -547 C ATOM 2950 O PHE A 295 -27.796 -24.013 6.113 1.00 34.11 O ANISOU 2950 O PHE A 295 5498 3746 3718 -626 -432 -535 O ATOM 2951 CB PHE A 295 -25.564 -23.462 8.494 1.00 30.85 C ANISOU 2951 CB PHE A 295 4935 3360 3429 -426 -263 -415 C ATOM 2952 CG PHE A 295 -25.869 -23.107 9.921 1.00 31.12 C ANISOU 2952 CG PHE A 295 4858 3446 3518 -456 -262 -311 C ATOM 2953 CD1 PHE A 295 -27.073 -22.511 10.260 1.00 29.33 C ANISOU 2953 CD1 PHE A 295 4545 3311 3287 -550 -300 -256 C ATOM 2954 CD2 PHE A 295 -24.943 -23.354 10.921 1.00 31.55 C ANISOU 2954 CD2 PHE A 295 4895 3463 3628 -386 -225 -269 C ATOM 2955 CE1 PHE A 295 -27.354 -22.181 11.576 1.00 26.47 C ANISOU 2955 CE1 PHE A 295 4089 3003 2966 -576 -287 -167 C ATOM 2956 CE2 PHE A 295 -25.216 -23.023 12.238 1.00 30.91 C ANISOU 2956 CE2 PHE A 295 4729 3434 3582 -416 -224 -175 C ATOM 2957 CZ PHE A 295 -26.423 -22.435 12.565 1.00 27.10 C ANISOU 2957 CZ PHE A 295 4168 3044 3086 -512 -249 -126 C ATOM 2958 N ARG A 296 -25.698 -24.666 5.615 1.00 33.97 N ANISOU 2958 N ARG A 296 5605 3613 3688 -442 -314 -635 N ATOM 2959 CA ARG A 296 -25.874 -24.449 4.183 1.00 32.81 C ANISOU 2959 CA ARG A 296 5545 3486 3436 -451 -327 -721 C ATOM 2960 C ARG A 296 -27.025 -25.283 3.634 1.00 36.68 C ANISOU 2960 C ARG A 296 6126 3903 3907 -571 -441 -760 C ATOM 2961 O ARG A 296 -27.878 -24.776 2.896 1.00 36.56 O ANISOU 2961 O ARG A 296 6113 3956 3824 -640 -504 -771 O ATOM 2962 CB ARG A 296 -24.568 -24.773 3.458 1.00 32.38 C ANISOU 2962 CB ARG A 296 5584 3375 3344 -331 -237 -814 C ATOM 2963 CG ARG A 296 -24.656 -24.696 1.956 1.00 39.46 C ANISOU 2963 CG ARG A 296 6598 4279 4115 -337 -239 -912 C ATOM 2964 CD ARG A 296 -23.279 -24.796 1.318 1.00 41.88 C ANISOU 2964 CD ARG A 296 6968 4561 4382 -209 -119 -997 C ATOM 2965 NE ARG A 296 -22.592 -26.052 1.609 1.00 43.13 N ANISOU 2965 NE ARG A 296 7197 4573 4616 -144 -96 -1051 N ATOM 2966 CZ ARG A 296 -21.542 -26.164 2.417 1.00 43.16 C ANISOU 2966 CZ ARG A 296 7130 4554 4712 -42 -21 -1025 C ATOM 2967 NH1 ARG A 296 -20.975 -27.347 2.614 1.00 45.12 N ANISOU 2967 NH1 ARG A 296 7453 4658 5030 21 -14 -1077 N ATOM 2968 NH2 ARG A 296 -21.053 -25.095 3.030 1.00 40.40 N ANISOU 2968 NH2 ARG A 296 6639 4322 4389 0 38 -948 N ATOM 2969 N GLN A 297 -27.072 -26.570 3.997 1.00 37.38 N ANISOU 2969 N GLN A 297 6293 3849 4061 -601 -478 -777 N ATOM 2970 CA GLN A 297 -28.131 -27.440 3.496 1.00 40.62 C ANISOU 2970 CA GLN A 297 6796 4176 4462 -726 -592 -816 C ATOM 2971 C GLN A 297 -29.489 -27.034 4.052 1.00 39.23 C ANISOU 2971 C GLN A 297 6500 4082 4322 -858 -674 -727 C ATOM 2972 O GLN A 297 -30.501 -27.105 3.347 1.00 38.40 O ANISOU 2972 O GLN A 297 6423 3988 4179 -961 -770 -755 O ATOM 2973 CB GLN A 297 -27.817 -28.897 3.839 1.00 46.93 C ANISOU 2973 CB GLN A 297 7707 4792 5332 -727 -611 -848 C ATOM 2974 CG GLN A 297 -26.577 -29.444 3.141 1.00 53.57 C ANISOU 2974 CG GLN A 297 8679 5535 6141 -595 -539 -958 C ATOM 2975 CD GLN A 297 -26.228 -30.857 3.578 1.00 62.11 C ANISOU 2975 CD GLN A 297 9866 6424 7307 -581 -561 -983 C ATOM 2976 OE1 GLN A 297 -26.701 -31.337 4.610 1.00 65.86 O ANISOU 2976 OE1 GLN A 297 10304 6848 7873 -654 -611 -896 O ATOM 2977 NE2 GLN A 297 -25.396 -31.532 2.790 1.00 61.89 N ANISOU 2977 NE2 GLN A 297 9977 6287 7251 -486 -522 -1102 N ATOM 2978 N THR A 298 -29.530 -26.599 5.313 1.00 36.33 N ANISOU 2978 N THR A 298 5998 3778 4029 -857 -637 -621 N ATOM 2979 CA THR A 298 -30.793 -26.162 5.899 1.00 36.57 C ANISOU 2979 CA THR A 298 5900 3898 4098 -973 -695 -538 C ATOM 2980 C THR A 298 -31.264 -24.852 5.277 1.00 37.81 C ANISOU 2980 C THR A 298 5973 4205 4189 -969 -708 -536 C ATOM 2981 O THR A 298 -32.466 -24.659 5.063 1.00 35.18 O ANISOU 2981 O THR A 298 5583 3926 3860 -1073 -794 -519 O ATOM 2982 CB THR A 298 -30.649 -26.018 7.413 1.00 35.90 C ANISOU 2982 CB THR A 298 5706 3842 4094 -965 -641 -433 C ATOM 2983 OG1 THR A 298 -30.028 -27.195 7.943 1.00 36.94 O ANISOU 2983 OG1 THR A 298 5931 3825 4279 -948 -629 -433 O ATOM 2984 CG2 THR A 298 -32.016 -25.847 8.057 1.00 36.69 C ANISOU 2984 CG2 THR A 298 5686 4012 4241 -1099 -695 -355 C ATOM 2985 N PHE A 299 -30.329 -23.940 4.987 1.00 39.36 N ANISOU 2985 N PHE A 299 6156 4468 4329 -850 -627 -551 N ATOM 2986 CA PHE A 299 -30.685 -22.708 4.289 1.00 36.90 C ANISOU 2986 CA PHE A 299 5791 4282 3947 -839 -642 -550 C ATOM 2987 C PHE A 299 -31.329 -23.011 2.941 1.00 40.30 C ANISOU 2987 C PHE A 299 6328 4686 4297 -902 -740 -627 C ATOM 2988 O PHE A 299 -32.332 -22.390 2.572 1.00 39.83 O ANISOU 2988 O PHE A 299 6208 4709 4217 -966 -821 -607 O ATOM 2989 CB PHE A 299 -29.448 -21.824 4.101 1.00 32.11 C ANISOU 2989 CB PHE A 299 5182 3729 3290 -707 -534 -560 C ATOM 2990 CG PHE A 299 -28.929 -21.207 5.377 1.00 33.79 C ANISOU 2990 CG PHE A 299 5270 3998 3570 -649 -455 -479 C ATOM 2991 CD1 PHE A 299 -29.695 -21.210 6.533 1.00 31.31 C ANISOU 2991 CD1 PHE A 299 4846 3713 3336 -713 -480 -400 C ATOM 2992 CD2 PHE A 299 -27.672 -20.618 5.415 1.00 34.53 C ANISOU 2992 CD2 PHE A 299 5357 4118 3645 -535 -355 -485 C ATOM 2993 CE1 PHE A 299 -29.215 -20.643 7.704 1.00 30.99 C ANISOU 2993 CE1 PHE A 299 4707 3724 3345 -661 -411 -331 C ATOM 2994 CE2 PHE A 299 -27.187 -20.046 6.585 1.00 31.72 C ANISOU 2994 CE2 PHE A 299 4892 3811 3348 -486 -294 -414 C ATOM 2995 CZ PHE A 299 -27.960 -20.063 7.729 1.00 30.35 C ANISOU 2995 CZ PHE A 299 4625 3663 3243 -548 -325 -339 C ATOM 2996 N AARG A 300 -30.768 -23.967 2.194 0.45 43.67 N ANISOU 2996 N AARG A 300 6917 4996 4677 -884 -738 -719 N ATOM 2997 N BARG A 300 -30.770 -23.969 2.197 0.55 43.61 N ANISOU 2997 N BARG A 300 6910 4989 4671 -884 -738 -719 N ATOM 2998 CA AARG A 300 -31.329 -24.314 0.892 0.45 46.82 C ANISOU 2998 CA AARG A 300 7440 5362 4987 -946 -834 -802 C ATOM 2999 CA BARG A 300 -31.329 -24.314 0.893 0.55 46.84 C ANISOU 2999 CA BARG A 300 7442 5365 4989 -945 -834 -802 C ATOM 3000 C AARG A 300 -32.737 -24.882 1.025 0.45 46.55 C ANISOU 3000 C AARG A 300 7373 5304 5008 -1096 -970 -782 C ATOM 3001 C BARG A 300 -32.736 -24.884 1.023 0.55 46.50 C ANISOU 3001 C BARG A 300 7367 5297 5002 -1096 -970 -782 C ATOM 3002 O AARG A 300 -33.622 -24.548 0.230 0.45 46.56 O ANISOU 3002 O AARG A 300 7378 5356 4956 -1165 -1075 -799 O ATOM 3003 O BARG A 300 -33.620 -24.553 0.225 0.55 46.50 O ANISOU 3003 O BARG A 300 7371 5348 4948 -1165 -1075 -800 O ATOM 3004 CB AARG A 300 -30.418 -25.306 0.168 0.45 50.48 C ANISOU 3004 CB AARG A 300 8089 5695 5395 -891 -795 -913 C ATOM 3005 CB BARG A 300 -30.413 -25.302 0.172 0.55 50.48 C ANISOU 3005 CB BARG A 300 8088 5695 5395 -890 -794 -913 C ATOM 3006 CG AARG A 300 -29.187 -24.673 -0.463 0.45 52.56 C ANISOU 3006 CG AARG A 300 8404 5999 5566 -759 -676 -959 C ATOM 3007 CG BARG A 300 -29.081 -24.706 -0.251 0.55 52.38 C ANISOU 3007 CG BARG A 300 8366 5973 5564 -750 -662 -949 C ATOM 3008 CD AARG A 300 -28.514 -25.631 -1.437 0.45 55.28 C ANISOU 3008 CD AARG A 300 8943 6226 5836 -718 -651 -1088 C ATOM 3009 CD BARG A 300 -28.294 -25.674 -1.118 0.55 55.13 C ANISOU 3009 CD BARG A 300 8900 6200 5848 -697 -624 -1073 C ATOM 3010 NE AARG A 300 -27.821 -26.719 -0.753 0.45 56.13 N ANISOU 3010 NE AARG A 300 9088 6202 6038 -669 -600 -1110 N ATOM 3011 NE BARG A 300 -27.071 -25.069 -1.638 0.55 55.02 N ANISOU 3011 NE BARG A 300 8914 6234 5757 -571 -492 -1113 N ATOM 3012 CZ AARG A 300 -26.506 -26.762 -0.563 0.45 55.17 C ANISOU 3012 CZ AARG A 300 8973 6057 5933 -538 -471 -1135 C ATOM 3013 CZ BARG A 300 -27.001 -24.390 -2.778 0.55 54.78 C ANISOU 3013 CZ BARG A 300 8952 6274 5586 -560 -480 -1157 C ATOM 3014 NH1AARG A 300 -25.737 -25.780 -1.013 0.45 55.41 N ANISOU 3014 NH1AARG A 300 8974 6190 5889 -451 -370 -1141 N ATOM 3015 NH1BARG A 300 -28.085 -24.227 -3.524 0.55 52.64 N ANISOU 3015 NH1BARG A 300 8732 6032 5237 -660 -605 -1168 N ATOM 3016 NH2AARG A 300 -25.960 -27.790 0.071 0.45 53.58 N ANISOU 3016 NH2AARG A 300 8805 5726 5825 -494 -445 -1151 N ATOM 3017 NH2BARG A 300 -25.847 -23.876 -3.175 0.55 57.72 N ANISOU 3017 NH2BARG A 300 9343 6690 5898 -452 -345 -1186 N ATOM 3018 N LYS A 301 -32.965 -25.738 2.024 1.00 47.26 N ANISOU 3018 N LYS A 301 7430 5318 5208 -1153 -975 -741 N ATOM 3019 CA LYS A 301 -34.295 -26.310 2.213 1.00 49.06 C ANISOU 3019 CA LYS A 301 7617 5525 5501 -1309 -1095 -715 C ATOM 3020 C LYS A 301 -35.320 -25.233 2.549 1.00 44.64 C ANISOU 3020 C LYS A 301 6869 5119 4972 -1359 -1136 -635 C ATOM 3021 O LYS A 301 -36.436 -25.245 2.020 1.00 43.90 O ANISOU 3021 O LYS A 301 6748 5055 4878 -1464 -1258 -644 O ATOM 3022 CB LYS A 301 -34.260 -27.380 3.305 1.00 53.61 C ANISOU 3022 CB LYS A 301 8193 5990 6185 -1359 -1075 -673 C ATOM 3023 CG LYS A 301 -33.582 -28.673 2.884 1.00 63.00 C ANISOU 3023 CG LYS A 301 9578 6998 7363 -1343 -1079 -761 C ATOM 3024 CD LYS A 301 -33.735 -29.755 3.947 1.00 69.07 C ANISOU 3024 CD LYS A 301 10353 7649 8243 -1415 -1084 -707 C ATOM 3025 CE LYS A 301 -33.092 -31.061 3.502 1.00 74.54 C ANISOU 3025 CE LYS A 301 11246 8143 8930 -1393 -1099 -798 C ATOM 3026 NZ LYS A 301 -33.250 -32.139 4.522 1.00 78.35 N ANISOU 3026 NZ LYS A 301 11751 8497 9522 -1468 -1115 -738 N ATOM 3027 N ILE A 302 -34.955 -24.290 3.420 1.00 43.79 N ANISOU 3027 N ILE A 302 6631 5110 4895 -1281 -1040 -559 N ATOM 3028 CA ILE A 302 -35.863 -23.198 3.760 1.00 46.50 C ANISOU 3028 CA ILE A 302 6798 5600 5271 -1308 -1068 -489 C ATOM 3029 C ILE A 302 -36.144 -22.333 2.538 1.00 50.90 C ANISOU 3029 C ILE A 302 7376 6230 5733 -1284 -1138 -529 C ATOM 3030 O ILE A 302 -37.291 -21.949 2.281 1.00 51.22 O ANISOU 3030 O ILE A 302 7325 6342 5794 -1359 -1241 -509 O ATOM 3031 CB ILE A 302 -35.281 -22.362 4.914 1.00 43.14 C ANISOU 3031 CB ILE A 302 6254 5252 4886 -1217 -946 -413 C ATOM 3032 CG1 ILE A 302 -35.140 -23.212 6.177 1.00 42.28 C ANISOU 3032 CG1 ILE A 302 6123 5077 4866 -1254 -892 -362 C ATOM 3033 CG2 ILE A 302 -36.145 -21.139 5.171 1.00 41.43 C ANISOU 3033 CG2 ILE A 302 5865 5181 4694 -1224 -968 -355 C ATOM 3034 CD1 ILE A 302 -34.381 -22.522 7.288 1.00 38.42 C ANISOU 3034 CD1 ILE A 302 5552 4645 4400 -1159 -774 -298 C ATOM 3035 N ILE A 303 -35.104 -22.017 1.765 1.00 50.67 N ANISOU 3035 N ILE A 303 7466 6186 5600 -1181 -1084 -583 N ATOM 3036 CA ILE A 303 -35.260 -21.117 0.627 1.00 52.24 C ANISOU 3036 CA ILE A 303 7700 6455 5693 -1153 -1139 -610 C ATOM 3037 C ILE A 303 -36.049 -21.793 -0.490 1.00 55.50 C ANISOU 3037 C ILE A 303 8221 6817 6049 -1252 -1286 -679 C ATOM 3038 O ILE A 303 -36.966 -21.201 -1.068 1.00 54.66 O ANISOU 3038 O ILE A 303 8067 6783 5918 -1298 -1400 -668 O ATOM 3039 CB ILE A 303 -33.880 -20.635 0.144 1.00 50.94 C ANISOU 3039 CB ILE A 303 7636 6289 5430 -1025 -1025 -645 C ATOM 3040 CG1 ILE A 303 -33.285 -19.648 1.152 1.00 46.55 C ANISOU 3040 CG1 ILE A 303 6949 5812 4926 -935 -910 -568 C ATOM 3041 CG2 ILE A 303 -33.974 -20.017 -1.244 1.00 52.61 C ANISOU 3041 CG2 ILE A 303 7944 6540 5504 -1013 -1088 -689 C ATOM 3042 CD1 ILE A 303 -31.778 -19.575 1.118 1.00 45.69 C ANISOU 3042 CD1 ILE A 303 6915 5672 4772 -822 -774 -596 C ATOM 3043 N ARG A 304 -35.709 -23.045 -0.808 1.00 61.25 N ANISOU 3043 N ARG A 304 9099 7414 6759 -1286 -1293 -755 N ATOM 3044 CA ARG A 304 -36.399 -23.738 -1.894 1.00 64.13 C ANISOU 3044 CA ARG A 304 9587 7718 7062 -1383 -1436 -832 C ATOM 3045 C ARG A 304 -37.864 -23.994 -1.569 1.00 67.83 C ANISOU 3045 C ARG A 304 9930 8211 7630 -1527 -1574 -789 C ATOM 3046 O ARG A 304 -38.710 -23.958 -2.468 1.00 71.75 O ANISOU 3046 O ARG A 304 10422 8736 8103 -1565 -1680 -806 O ATOM 3047 CB ARG A 304 -35.698 -25.057 -2.217 1.00 66.20 C ANISOU 3047 CB ARG A 304 10039 7822 7294 -1383 -1409 -927 C ATOM 3048 CG ARG A 304 -34.334 -24.906 -2.871 1.00 71.30 C ANISOU 3048 CG ARG A 304 10829 8440 7820 -1251 -1291 -996 C ATOM 3049 CD ARG A 304 -33.668 -26.261 -3.063 1.00 78.12 C ANISOU 3049 CD ARG A 304 11865 9140 8678 -1241 -1258 -1092 C ATOM 3050 NE ARG A 304 -32.281 -26.130 -3.502 1.00 83.37 N ANISOU 3050 NE ARG A 304 12637 9786 9255 -1101 -1118 -1153 N ATOM 3051 CZ ARG A 304 -31.444 -27.152 -3.650 1.00 86.32 C ANISOU 3051 CZ ARG A 304 13148 10027 9623 -1048 -1054 -1239 C ATOM 3052 NH1 ARG A 304 -30.199 -26.937 -4.054 1.00 85.76 N ANISOU 3052 NH1 ARG A 304 13151 9956 9476 -919 -920 -1294 N ATOM 3053 NH2 ARG A 304 -31.849 -28.388 -3.393 1.00 88.45 N ANISOU 3053 NH2 ARG A 304 13463 10169 9977 -1118 -1116 -1262 N ATOM 3054 N SER A 305 -38.189 -24.241 -0.303 1.00 72.00 N ANISOU 3054 N SER A 305 10317 8743 8295 -1569 -1531 -715 N ATOM 3055 CA SER A 305 -39.541 -24.640 0.062 1.00 79.64 C ANISOU 3055 CA SER A 305 11164 9726 9369 -1717 -1645 -677 C ATOM 3056 C SER A 305 -40.443 -23.474 0.445 1.00 84.91 C ANISOU 3056 C SER A 305 11615 10552 10096 -1723 -1677 -596 C ATOM 3057 O SER A 305 -41.669 -23.615 0.373 1.00 88.49 O ANISOU 3057 O SER A 305 11955 11043 10624 -1818 -1777 -575 O ATOM 3058 CB SER A 305 -39.503 -25.641 1.223 1.00 80.39 C ANISOU 3058 CB SER A 305 11231 9735 9579 -1780 -1584 -639 C ATOM 3059 OG SER A 305 -38.758 -26.797 0.879 1.00 81.56 O ANISOU 3059 OG SER A 305 11579 9721 9688 -1778 -1571 -716 O ATOM 3060 N HIS A 306 -39.880 -22.332 0.846 1.00 87.32 N ANISOU 3060 N HIS A 306 11842 10950 10384 -1598 -1572 -549 N ATOM 3061 CA HIS A 306 -40.683 -21.244 1.387 1.00 91.53 C ANISOU 3061 CA HIS A 306 12164 11622 10989 -1590 -1584 -472 C ATOM 3062 C HIS A 306 -40.541 -19.915 0.653 1.00 90.55 C ANISOU 3062 C HIS A 306 12035 11591 10781 -1489 -1607 -469 C ATOM 3063 O HIS A 306 -41.389 -19.038 0.849 1.00 91.61 O ANISOU 3063 O HIS A 306 12005 11831 10971 -1489 -1657 -418 O ATOM 3064 CB HIS A 306 -40.358 -21.027 2.874 1.00 94.28 C ANISOU 3064 CB HIS A 306 12388 12006 11428 -1549 -1438 -397 C ATOM 3065 CG HIS A 306 -40.694 -22.201 3.742 1.00 98.00 C ANISOU 3065 CG HIS A 306 12834 12405 11995 -1660 -1421 -374 C ATOM 3066 ND1 HIS A 306 -39.742 -23.084 4.205 1.00 98.50 N ANISOU 3066 ND1 HIS A 306 13018 12354 12052 -1642 -1332 -386 N ATOM 3067 CD2 HIS A 306 -41.881 -22.642 4.223 1.00 99.70 C ANISOU 3067 CD2 HIS A 306 12921 12645 12317 -1794 -1482 -337 C ATOM 3068 CE1 HIS A 306 -40.327 -24.014 4.939 1.00 99.28 C ANISOU 3068 CE1 HIS A 306 13075 12403 12243 -1762 -1343 -352 C ATOM 3069 NE2 HIS A 306 -41.624 -23.770 4.965 1.00100.07 N ANISOU 3069 NE2 HIS A 306 13021 12588 12411 -1861 -1427 -322 N ATOM 3070 N VAL A 307 -39.510 -19.731 -0.167 1.00 87.71 N ANISOU 3070 N VAL A 307 11845 11192 10290 -1403 -1568 -519 N ATOM 3071 CA VAL A 307 -39.405 -18.517 -0.976 1.00 85.87 C ANISOU 3071 CA VAL A 307 11629 11035 9964 -1323 -1601 -513 C ATOM 3072 C VAL A 307 -39.221 -18.878 -2.448 1.00 85.39 C ANISOU 3072 C VAL A 307 11768 10917 9758 -1337 -1687 -593 C ATOM 3073 O VAL A 307 -39.173 -20.053 -2.814 1.00 85.60 O ANISOU 3073 O VAL A 307 11905 10845 9774 -1390 -1703 -655 O ATOM 3074 CB VAL A 307 -38.254 -17.596 -0.499 1.00 85.33 C ANISOU 3074 CB VAL A 307 11552 11002 9866 -1187 -1443 -478 C ATOM 3075 CG1 VAL A 307 -38.156 -17.579 1.021 1.00 84.63 C ANISOU 3075 CG1 VAL A 307 11314 10937 9905 -1172 -1331 -417 C ATOM 3076 CG2 VAL A 307 -36.934 -18.004 -1.132 1.00 85.09 C ANISOU 3076 CG2 VAL A 307 11720 10893 9718 -1127 -1356 -543 C TER 3077 VAL A 307 HETATM 3078 N2 T4E A1201 -20.342 8.173 17.331 1.00 24.44 N ANISOU 3078 N2 T4E A1201 2995 3567 2725 104 -20 84 N HETATM 3079 N1 T4E A1201 -21.233 7.324 17.048 1.00 21.76 N ANISOU 3079 N1 T4E A1201 2640 3265 2363 122 -15 82 N HETATM 3080 C6 T4E A1201 -21.210 5.991 17.439 1.00 18.93 C ANISOU 3080 C6 T4E A1201 2247 2953 1994 115 12 74 C HETATM 3081 C5 T4E A1201 -20.047 5.587 18.213 1.00 17.27 C ANISOU 3081 C5 T4E A1201 2016 2748 1799 95 31 69 C HETATM 3082 N4 T4E A1201 -19.065 6.504 18.525 1.00 20.77 N ANISOU 3082 N4 T4E A1201 2465 3158 2268 78 22 69 N HETATM 3083 C3 T4E A1201 -19.204 7.811 18.074 1.00 18.07 C ANISOU 3083 C3 T4E A1201 2161 2770 1936 78 -1 77 C HETATM 3084 C10 T4E A1201 -24.423 3.279 16.149 1.00 14.30 C ANISOU 3084 C10 T4E A1201 1618 2461 1355 121 -7 73 C HETATM 3085 C11 T4E A1201 -24.732 4.524 16.749 1.00 16.39 C ANISOU 3085 C11 T4E A1201 1872 2715 1641 157 -26 61 C HETATM 3086 C12 T4E A1201 -23.689 5.416 17.181 1.00 16.22 C ANISOU 3086 C12 T4E A1201 1873 2658 1632 159 -19 60 C HETATM 3087 C7 T4E A1201 -22.313 5.082 17.016 1.00 17.32 C ANISOU 3087 C7 T4E A1201 2030 2782 1768 125 10 74 C HETATM 3088 C8 T4E A1201 -22.055 3.831 16.387 1.00 13.55 C ANISOU 3088 C8 T4E A1201 1556 2322 1272 99 35 84 C HETATM 3089 C9 T4E A1201 -23.090 2.989 15.993 1.00 13.50 C ANISOU 3089 C9 T4E A1201 1542 2341 1249 99 25 82 C HETATM 3090 C16 T4E A1201 -19.306 1.546 19.719 1.00 17.30 C ANISOU 3090 C16 T4E A1201 1956 2825 1791 82 77 71 C HETATM 3091 C17 T4E A1201 -20.616 2.085 19.745 1.00 16.21 C ANISOU 3091 C17 T4E A1201 1825 2702 1633 94 66 60 C HETATM 3092 C18 T4E A1201 -20.842 3.400 19.269 1.00 15.61 C ANISOU 3092 C18 T4E A1201 1763 2606 1563 104 51 56 C HETATM 3093 C13 T4E A1201 -19.801 4.182 18.733 1.00 18.84 C ANISOU 3093 C13 T4E A1201 2186 2981 1992 89 52 66 C HETATM 3094 C14 T4E A1201 -18.518 3.629 18.718 1.00 17.17 C ANISOU 3094 C14 T4E A1201 1958 2766 1800 70 72 76 C HETATM 3095 C15 T4E A1201 -18.266 2.321 19.194 1.00 13.74 C ANISOU 3095 C15 T4E A1201 1503 2351 1366 72 83 76 C HETATM 3096 N3 T4E A1201 -18.224 8.754 18.366 1.00 20.02 N ANISOU 3096 N3 T4E A1201 2417 2976 2213 50 -14 78 N HETATM 3097 CL1 T4E A1201 -22.628 1.483 15.270 1.00 16.71 CL ANISOU 3097 CL1 T4E A1201 1966 2750 1633 68 54 86 CL HETATM 3098 O1 T4E A1201 -25.385 2.428 15.748 1.00 16.57 O ANISOU 3098 O1 T4E A1201 1889 2774 1632 110 -21 72 O HETATM 3099 NA NA A1202 -23.509 -8.331 16.493 1.00 41.20 NA HETATM 3100 C1 CLR A1203 -36.798 9.691 28.320 1.00 88.00 C HETATM 3101 C2 CLR A1203 -36.421 11.132 28.737 1.00 88.20 C HETATM 3102 C3 CLR A1203 -37.248 11.681 29.872 1.00 90.40 C HETATM 3103 C4 CLR A1203 -37.405 10.670 31.024 1.00 91.97 C HETATM 3104 C5 CLR A1203 -37.762 9.292 30.525 1.00 92.01 C HETATM 3105 C6 CLR A1203 -38.874 8.704 31.003 1.00 93.51 C HETATM 3106 C7 CLR A1203 -39.312 7.298 30.643 1.00 92.30 C HETATM 3107 C8 CLR A1203 -38.133 6.518 30.081 1.00 89.41 C HETATM 3108 C9 CLR A1203 -37.405 7.318 28.993 1.00 86.96 C HETATM 3109 C10 CLR A1203 -36.865 8.681 29.467 1.00 89.11 C HETATM 3110 C11 CLR A1203 -36.335 6.433 28.346 1.00 83.27 C HETATM 3111 C12 CLR A1203 -36.788 5.010 27.976 1.00 85.13 C HETATM 3112 C13 CLR A1203 -37.550 4.266 29.041 1.00 88.53 C HETATM 3113 C14 CLR A1203 -38.643 5.229 29.482 1.00 89.99 C HETATM 3114 C15 CLR A1203 -39.577 4.393 30.351 1.00 91.67 C HETATM 3115 C16 CLR A1203 -39.467 3.000 29.740 1.00 90.64 C HETATM 3116 C17 CLR A1203 -38.379 3.026 28.665 1.00 89.12 C HETATM 3117 C18 CLR A1203 -36.579 3.868 30.188 1.00 89.13 C HETATM 3118 C19 CLR A1203 -35.437 8.520 30.059 1.00 89.72 C HETATM 3119 C20 CLR A1203 -37.687 1.661 28.512 1.00 87.23 C HETATM 3120 C21 CLR A1203 -37.651 1.208 27.052 1.00 85.77 C HETATM 3121 C22 CLR A1203 -38.349 0.558 29.374 1.00 86.76 C HETATM 3122 C23 CLR A1203 -37.526 -0.731 29.520 1.00 85.21 C HETATM 3123 C24 CLR A1203 -36.504 -0.608 30.656 1.00 82.60 C HETATM 3124 C25 CLR A1203 -35.100 -1.147 30.330 1.00 77.34 C HETATM 3125 C26 CLR A1203 -35.103 -2.151 29.177 1.00 73.83 C HETATM 3126 C27 CLR A1203 -34.113 -0.020 30.041 1.00 75.14 C HETATM 3127 O1 CLR A1203 -36.620 12.863 30.396 1.00 90.14 O HETATM 3128 C1 CLR A1204 -38.098 10.719 21.611 1.00 26.20 C HETATM 3129 C2 CLR A1204 -37.826 12.212 21.904 1.00 28.46 C HETATM 3130 C3 CLR A1204 -38.146 12.567 23.333 1.00 30.61 C HETATM 3131 C4 CLR A1204 -37.352 11.671 24.300 1.00 29.68 C HETATM 3132 C5 CLR A1204 -37.561 10.207 23.998 1.00 28.80 C HETATM 3133 C6 CLR A1204 -37.902 9.402 25.021 1.00 26.78 C HETATM 3134 C7 CLR A1204 -38.160 7.910 24.907 1.00 29.78 C HETATM 3135 C8 CLR A1204 -37.754 7.358 23.544 1.00 29.23 C HETATM 3136 C9 CLR A1204 -38.109 8.348 22.428 1.00 27.81 C HETATM 3137 C10 CLR A1204 -37.428 9.717 22.564 1.00 26.52 C HETATM 3138 C11 CLR A1204 -37.903 7.691 21.059 1.00 28.48 C HETATM 3139 C12 CLR A1204 -38.592 6.325 20.931 1.00 27.22 C HETATM 3140 C13 CLR A1204 -38.235 5.340 22.015 1.00 27.23 C HETATM 3141 C14 CLR A1204 -38.519 6.068 23.321 1.00 30.34 C HETATM 3142 C15 CLR A1204 -38.357 4.987 24.386 1.00 32.24 C HETATM 3143 C16 CLR A1204 -38.856 3.731 23.675 1.00 33.26 C HETATM 3144 C17 CLR A1204 -39.064 4.055 22.193 1.00 31.10 C HETATM 3145 C18 CLR A1204 -36.748 4.904 21.890 1.00 24.54 C HETATM 3146 C19 CLR A1204 -35.914 9.601 22.204 1.00 25.40 C HETATM 3147 C20 CLR A1204 -38.793 2.807 21.342 1.00 33.14 C HETATM 3148 C21 CLR A1204 -39.021 3.040 19.845 1.00 32.70 C HETATM 3149 C22 CLR A1204 -39.691 1.639 21.817 1.00 38.28 C HETATM 3150 C23 CLR A1204 -39.536 0.313 21.055 1.00 41.77 C HETATM 3151 C24 CLR A1204 -40.597 -0.689 21.524 1.00 50.36 C HETATM 3152 C25 CLR A1204 -40.297 -2.155 21.174 1.00 56.70 C HETATM 3153 C26 CLR A1204 -41.226 -3.104 21.928 1.00 62.18 C HETATM 3154 C27 CLR A1204 -40.412 -2.425 19.675 1.00 57.12 C HETATM 3155 O1 CLR A1204 -37.809 13.939 23.590 1.00 31.81 O HETATM 3156 C1 CLR A1205 -8.358 10.911 13.240 1.00 28.44 C HETATM 3157 C2 CLR A1205 -8.403 12.451 13.251 1.00 31.07 C HETATM 3158 C3 CLR A1205 -7.045 13.045 12.990 1.00 32.49 C HETATM 3159 C4 CLR A1205 -6.441 12.513 11.676 1.00 31.69 C HETATM 3160 C5 CLR A1205 -6.501 11.005 11.586 1.00 29.15 C HETATM 3161 C6 CLR A1205 -5.407 10.330 11.178 1.00 28.76 C HETATM 3162 C7 CLR A1205 -5.352 8.833 10.939 1.00 30.78 C HETATM 3163 C8 CLR A1205 -6.745 8.208 10.962 1.00 30.11 C HETATM 3164 C9 CLR A1205 -7.582 8.814 12.093 1.00 28.10 C HETATM 3165 C10 CLR A1205 -7.804 10.324 11.937 1.00 30.11 C HETATM 3166 C11 CLR A1205 -8.891 8.051 12.260 1.00 27.92 C HETATM 3167 C12 CLR A1205 -8.712 6.529 12.303 1.00 29.68 C HETATM 3168 C13 CLR A1205 -7.927 5.949 11.159 1.00 30.12 C HETATM 3169 C14 CLR A1205 -6.612 6.714 11.168 1.00 30.71 C HETATM 3170 C15 CLR A1205 -5.732 5.949 10.181 1.00 31.47 C HETATM 3171 C16 CLR A1205 -6.153 4.499 10.399 1.00 31.94 C HETATM 3172 C17 CLR A1205 -7.425 4.494 11.253 1.00 28.97 C HETATM 3173 C18 CLR A1205 -8.714 6.152 9.830 1.00 28.95 C HETATM 3174 C19 CLR A1205 -8.799 10.614 10.776 1.00 31.09 C HETATM 3175 C20 CLR A1205 -8.330 3.309 10.882 1.00 30.71 C HETATM 3176 C21 CLR A1205 -9.584 3.228 11.755 1.00 32.34 C HETATM 3177 C22 CLR A1205 -7.564 1.976 11.011 1.00 31.27 C HETATM 3178 C23 CLR A1205 -8.453 0.735 11.185 1.00 32.11 C HETATM 3179 C24 CLR A1205 -7.600 -0.534 11.126 1.00 35.86 C HETATM 3180 C25 CLR A1205 -8.410 -1.829 10.971 1.00 37.98 C HETATM 3181 C26 CLR A1205 -7.528 -2.962 10.450 1.00 42.11 C HETATM 3182 C27 CLR A1205 -9.064 -2.251 12.285 1.00 33.95 C HETATM 3183 O1 CLR A1205 -7.160 14.473 12.910 1.00 33.89 O HETATM 3184 C1 CLR A1206 -3.037 8.351 21.083 1.00 21.56 C HETATM 3185 C2 CLR A1206 -2.782 9.870 21.033 1.00 21.30 C HETATM 3186 C3 CLR A1206 -1.877 10.266 19.897 1.00 26.12 C HETATM 3187 C4 CLR A1206 -2.343 9.678 18.550 1.00 26.43 C HETATM 3188 C5 CLR A1206 -2.603 8.193 18.642 1.00 23.58 C HETATM 3189 C6 CLR A1206 -2.042 7.362 17.736 1.00 23.16 C HETATM 3190 C7 CLR A1206 -2.323 5.870 17.646 1.00 25.56 C HETATM 3191 C8 CLR A1206 -3.503 5.472 18.533 1.00 25.68 C HETATM 3192 C9 CLR A1206 -3.417 6.190 19.884 1.00 22.44 C HETATM 3193 C10 CLR A1206 -3.495 7.716 19.766 1.00 22.12 C HETATM 3194 C11 CLR A1206 -4.438 5.629 20.879 1.00 21.45 C HETATM 3195 C12 CLR A1206 -4.525 4.103 20.923 1.00 23.00 C HETATM 3196 C13 CLR A1206 -4.628 3.423 19.580 1.00 27.14 C HETATM 3197 C14 CLR A1206 -3.463 3.979 18.773 1.00 26.49 C HETATM 3198 C15 CLR A1206 -3.389 3.091 17.535 1.00 28.58 C HETATM 3199 C16 CLR A1206 -3.877 1.741 18.050 1.00 29.98 C HETATM 3200 C17 CLR A1206 -4.367 1.912 19.488 1.00 32.13 C HETATM 3201 C18 CLR A1206 -6.018 3.713 18.940 1.00 22.01 C HETATM 3202 C19 CLR A1206 -4.947 8.188 19.445 1.00 21.89 C HETATM 3203 C20 CLR A1206 -5.480 0.900 19.802 1.00 33.63 C HETATM 3204 C21 CLR A1206 -5.920 0.909 21.268 1.00 29.09 C HETATM 3205 C22 CLR A1206 -5.004 -0.521 19.431 1.00 38.68 C HETATM 3206 C23 CLR A1206 -5.974 -1.653 19.791 1.00 40.79 C HETATM 3207 C24 CLR A1206 -5.185 -2.946 20.010 1.00 48.34 C HETATM 3208 C25 CLR A1206 -5.791 -4.169 19.311 1.00 51.40 C HETATM 3209 C26 CLR A1206 -6.168 -3.848 17.867 1.00 52.28 C HETATM 3210 C27 CLR A1206 -4.848 -5.368 19.353 1.00 53.45 C HETATM 3211 O1 CLR A1206 -1.860 11.696 19.791 1.00 26.76 O HETATM 3212 C1 OLA A1207 -36.381 14.739 12.746 1.00 64.92 C HETATM 3213 O1 OLA A1207 -35.751 15.811 12.518 1.00 66.85 O HETATM 3214 O2 OLA A1207 -37.340 14.786 13.532 1.00 66.84 O HETATM 3215 C2 OLA A1207 -35.997 13.427 12.091 1.00 59.65 C HETATM 3216 C3 OLA A1207 -36.590 12.229 12.835 1.00 54.57 C HETATM 3217 C4 OLA A1207 -35.892 10.915 12.504 1.00 47.81 C HETATM 3218 C5 OLA A1207 -36.838 9.819 12.061 1.00 42.63 C HETATM 3219 C6 OLA A1207 -36.369 8.411 12.399 1.00 41.06 C HETATM 3220 C7 OLA A1207 -36.375 7.499 11.178 1.00 41.08 C HETATM 3221 C8 OLA A1207 -36.485 6.020 11.498 1.00 41.57 C HETATM 3222 C9 OLA A1207 -35.851 5.227 10.367 1.00 45.21 C HETATM 3223 C10 OLA A1207 -36.454 4.263 9.632 1.00 49.94 C HETATM 3224 C11 OLA A1207 -37.886 3.819 9.828 1.00 52.91 C HETATM 3225 C12 OLA A1207 -38.009 2.284 9.812 1.00 56.86 C HETATM 3226 C13 OLA A1207 -38.400 1.690 11.181 1.00 59.78 C HETATM 3227 C14 OLA A1207 -39.358 0.493 11.074 1.00 62.99 C HETATM 3228 C15 OLA A1207 -39.172 -0.549 12.193 1.00 62.91 C HETATM 3229 C16 OLA A1207 -38.824 -1.953 11.668 1.00 62.79 C HETATM 3230 C17 OLA A1207 -39.966 -2.969 11.825 1.00 64.39 C HETATM 3231 C18 OLA A1207 -39.784 -4.207 10.933 1.00 64.68 C HETATM 3232 C1 OLA A1208 -34.174 8.634 1.893 0.56 59.02 C HETATM 3233 O1 OLA A1208 -33.725 9.132 0.823 0.56 60.13 O HETATM 3234 O2 OLA A1208 -34.191 9.356 2.904 0.56 58.51 O HETATM 3235 C2 OLA A1208 -34.681 7.207 1.955 0.56 58.32 C HETATM 3236 C3 OLA A1208 -35.387 6.809 0.656 0.56 59.37 C HETATM 3237 C4 OLA A1208 -35.798 5.342 0.605 0.56 59.09 C HETATM 3238 C5 OLA A1208 -34.627 4.385 0.704 0.56 58.18 C HETATM 3239 C6 OLA A1208 -34.972 2.926 0.437 0.56 58.72 C HETATM 3240 C7 OLA A1208 -33.763 2.014 0.631 0.56 57.95 C HETATM 3241 C8 OLA A1208 -33.696 0.836 -0.324 0.56 58.86 C HETATM 3242 C9 OLA A1208 -32.840 -0.252 0.306 0.56 57.78 C HETATM 3243 C10 OLA A1208 -33.101 -1.577 0.281 0.56 58.10 C HETATM 3244 C11 OLA A1208 -34.313 -2.179 -0.397 0.56 58.91 C HETATM 3245 C12 OLA A1208 -34.071 -3.644 -0.807 0.56 58.55 C HETATM 3246 C13 OLA A1208 -35.271 -4.571 -0.528 0.56 58.78 C HETATM 3247 C14 OLA A1208 -35.323 -5.784 -1.471 0.56 59.79 C HETATM 3248 C15 OLA A1208 -35.191 -7.141 -0.753 0.56 59.55 C HETATM 3249 C16 OLA A1208 -34.241 -8.116 -1.470 0.56 60.28 C HETATM 3250 C17 OLA A1208 -34.947 -9.350 -2.057 0.56 61.28 C HETATM 3251 C18 OLA A1208 -34.002 -10.224 -2.896 0.56 61.56 C HETATM 3252 C1 OLA A1209 -20.313 -22.082 27.898 1.00 54.61 C HETATM 3253 O1 OLA A1209 -20.594 -21.746 26.720 1.00 58.60 O HETATM 3254 O2 OLA A1209 -20.551 -23.252 28.237 1.00 60.26 O HETATM 3255 C2 OLA A1209 -19.708 -21.106 28.882 1.00 49.08 C HETATM 3256 C3 OLA A1209 -20.224 -19.681 28.667 1.00 45.01 C HETATM 3257 C4 OLA A1209 -19.390 -18.631 29.390 1.00 41.18 C HETATM 3258 C5 OLA A1209 -19.965 -17.233 29.303 1.00 40.49 C HETATM 3259 C6 OLA A1209 -18.998 -16.182 28.780 1.00 39.94 C HETATM 3260 C7 OLA A1209 -19.598 -14.782 28.875 1.00 42.03 C HETATM 3261 C1 OLA A1210 -28.657 -21.215 34.896 1.00 79.78 C HETATM 3262 O1 OLA A1210 -27.518 -20.668 34.836 1.00 77.94 O HETATM 3263 O2 OLA A1210 -28.705 -22.456 34.829 1.00 80.22 O HETATM 3264 C2 OLA A1210 -29.937 -20.413 35.044 1.00 80.35 C HETATM 3265 C3 OLA A1210 -29.715 -19.060 35.728 1.00 78.44 C HETATM 3266 C4 OLA A1210 -30.983 -18.220 35.823 1.00 77.47 C HETATM 3267 C5 OLA A1210 -30.719 -16.741 36.030 1.00 77.13 C HETATM 3268 C6 OLA A1210 -31.381 -15.813 35.018 1.00 75.89 C HETATM 3269 C7 OLA A1210 -31.565 -14.404 35.581 1.00 75.53 C HETATM 3270 C8 OLA A1210 -30.348 -13.502 35.470 1.00 75.32 C HETATM 3271 C9 OLA A1210 -30.272 -12.601 36.695 1.00 74.64 C HETATM 3272 C10 OLA A1210 -29.337 -11.650 36.927 1.00 73.55 C HETATM 3273 C11 OLA A1210 -28.201 -11.337 35.975 1.00 72.61 C HETATM 3274 C12 OLA A1210 -26.947 -10.817 36.708 1.00 71.65 C HETATM 3275 C13 OLA A1210 -27.206 -9.561 37.563 1.00 72.59 C HETATM 3276 C14 OLA A1210 -26.716 -8.262 36.900 1.00 69.48 C HETATM 3277 C15 OLA A1210 -26.707 -7.039 37.839 1.00 64.42 C HETATM 3278 C16 OLA A1210 -26.865 -5.699 37.099 1.00 56.32 C HETATM 3279 C17 OLA A1210 -28.222 -5.550 36.396 1.00 53.00 C HETATM 3280 C18 OLA A1210 -29.001 -4.313 36.867 1.00 53.74 C HETATM 3281 C1 OLA A1211 -21.488 12.595 4.036 1.00 71.78 C HETATM 3282 O1 OLA A1211 -20.803 13.181 3.178 1.00 74.34 O HETATM 3283 O2 OLA A1211 -21.504 13.073 5.206 1.00 72.04 O HETATM 3284 C2 OLA A1211 -22.273 11.351 3.668 1.00 66.73 C HETATM 3285 C3 OLA A1211 -21.437 10.379 2.834 1.00 62.81 C HETATM 3286 C4 OLA A1211 -21.785 8.921 3.103 1.00 59.50 C HETATM 3287 C5 OLA A1211 -20.582 8.061 3.432 1.00 57.98 C HETATM 3288 C6 OLA A1211 -20.884 6.864 4.323 1.00 56.56 C HETATM 3289 C7 OLA A1211 -22.056 6.049 3.781 1.00 56.08 C HETATM 3290 C8 OLA A1211 -21.695 4.654 3.306 1.00 57.27 C HETATM 3291 C9 OLA A1211 -20.912 4.754 2.005 1.00 59.51 C HETATM 3292 C10 OLA A1211 -20.571 3.713 1.213 1.00 60.70 C HETATM 3293 C11 OLA A1211 -20.935 2.275 1.520 1.00 62.55 C HETATM 3294 C12 OLA A1211 -19.746 1.487 2.103 1.00 65.92 C HETATM 3295 C13 OLA A1211 -20.166 0.269 2.956 1.00 67.36 C HETATM 3296 C14 OLA A1211 -19.132 -0.124 4.025 1.00 65.75 C HETATM 3297 C15 OLA A1211 -18.969 -1.646 4.208 1.00 65.66 C HETATM 3298 C16 OLA A1211 -17.682 -2.211 3.580 1.00 65.82 C HETATM 3299 C1 OLA A1212 -1.620 -22.346 24.948 1.00 95.14 C HETATM 3300 O1 OLA A1212 -1.563 -22.302 23.688 1.00 95.54 O HETATM 3301 O2 OLA A1212 -1.443 -23.447 25.500 1.00 96.60 O HETATM 3302 C2 OLA A1212 -1.892 -21.105 25.776 1.00 91.68 C HETATM 3303 C3 OLA A1212 -0.914 -19.978 25.439 1.00 89.44 C HETATM 3304 C4 OLA A1212 -1.594 -18.717 24.921 1.00 86.18 C HETATM 3305 C5 OLA A1212 -2.741 -18.246 25.794 1.00 83.68 C HETATM 3306 C6 OLA A1212 -2.574 -16.848 26.374 1.00 81.83 C HETATM 3307 C7 OLA A1212 -2.534 -15.781 25.282 1.00 78.49 C HETATM 3308 C8 OLA A1212 -2.784 -14.362 25.760 1.00 75.29 C HETATM 3309 C9 OLA A1212 -3.690 -13.661 24.759 1.00 71.36 C HETATM 3310 C10 OLA A1212 -3.749 -12.328 24.541 1.00 69.01 C HETATM 3311 C11 OLA A1212 -2.901 -11.318 25.281 1.00 68.58 C HETATM 3312 C12 OLA A1212 -2.394 -10.196 24.354 1.00 67.43 C HETATM 3313 C6 OLA A1213 -20.953 -12.563 0.361 1.00 62.32 C HETATM 3314 C7 OLA A1213 -21.335 -11.085 0.432 1.00 60.41 C HETATM 3315 C8 OLA A1213 -20.725 -10.310 1.587 1.00 57.36 C HETATM 3316 C9 OLA A1213 -21.755 -10.185 2.700 1.00 57.17 C HETATM 3317 C10 OLA A1213 -21.943 -9.103 3.490 1.00 55.04 C HETATM 3318 C11 OLA A1213 -21.131 -7.832 3.375 1.00 52.19 C HETATM 3319 C12 OLA A1213 -21.772 -6.826 2.401 1.00 51.00 C HETATM 3320 C13 OLA A1213 -22.954 -6.045 3.013 1.00 47.26 C HETATM 3321 C14 OLA A1213 -23.062 -4.605 2.489 1.00 46.95 C HETATM 3322 C15 OLA A1213 -24.476 -4.006 2.609 1.00 50.15 C HETATM 3323 C16 OLA A1213 -24.576 -2.568 2.070 1.00 53.95 C HETATM 3324 C17 OLA A1213 -23.296 -2.101 1.357 1.00 59.35 C HETATM 3325 C18 OLA A1213 -23.014 -0.602 1.547 1.00 60.69 C HETATM 3326 C1 OLA A1214 -36.310 -15.571 5.116 1.00 73.25 C HETATM 3327 O1 OLA A1214 -36.685 -14.496 5.660 1.00 74.05 O HETATM 3328 O2 OLA A1214 -36.405 -16.617 5.780 1.00 74.72 O HETATM 3329 C2 OLA A1214 -35.764 -15.607 3.702 1.00 70.56 C HETATM 3330 C3 OLA A1214 -34.238 -15.494 3.666 1.00 66.91 C HETATM 3331 C4 OLA A1214 -33.654 -15.771 2.286 1.00 64.69 C HETATM 3332 C5 OLA A1214 -33.058 -14.548 1.621 1.00 59.64 C HETATM 3333 C6 OLA A1214 -31.547 -14.432 1.756 1.00 53.20 C HETATM 3334 C7 OLA A1214 -31.152 -13.411 2.817 1.00 47.32 C HETATM 3335 C8 OLA A1214 -29.679 -13.425 3.180 1.00 43.96 C HETATM 3336 C9 OLA A1214 -29.119 -12.022 3.012 1.00 40.51 C HETATM 3337 C10 OLA A1214 -28.182 -11.449 3.801 1.00 38.65 C HETATM 3338 C1 OLA A1215 -15.806 13.083 0.897 1.00 63.71 C HETATM 3339 O1 OLA A1215 -14.598 12.791 0.670 1.00 63.67 O HETATM 3340 O2 OLA A1215 -16.049 14.207 1.369 1.00 62.96 O HETATM 3341 C2 OLA A1215 -16.934 12.111 0.606 1.00 63.98 C HETATM 3342 C3 OLA A1215 -16.808 10.830 1.434 1.00 64.04 C HETATM 3343 C4 OLA A1215 -17.308 9.581 0.719 1.00 64.00 C HETATM 3344 C5 OLA A1215 -16.222 8.546 0.504 1.00 63.94 C HETATM 3345 C6 OLA A1215 -16.525 7.160 1.058 1.00 63.59 C HETATM 3346 C7 OLA A1215 -15.650 6.095 0.399 1.00 66.46 C HETATM 3347 C8 OLA A1215 -15.303 4.906 1.278 1.00 66.79 C HETATM 3348 C9 OLA A1215 -15.809 3.631 0.616 1.00 66.40 C HETATM 3349 C10 OLA A1215 -15.213 2.418 0.677 1.00 65.28 C HETATM 3350 C3 OLA A1216 -17.048 -16.126 2.751 1.00 71.93 C HETATM 3351 C4 OLA A1216 -18.037 -14.978 2.586 1.00 70.57 C HETATM 3352 C5 OLA A1216 -17.938 -13.931 3.678 1.00 69.70 C HETATM 3353 C6 OLA A1216 -18.020 -12.488 3.198 1.00 69.22 C HETATM 3354 C7 OLA A1216 -17.872 -11.498 4.353 1.00 67.93 C HETATM 3355 C8 OLA A1216 -16.475 -10.937 4.554 1.00 68.24 C HETATM 3356 C9 OLA A1216 -16.319 -9.670 3.725 1.00 68.27 C HETATM 3357 C10 OLA A1216 -16.375 -8.399 4.185 1.00 67.49 C HETATM 3358 C11 OLA A1216 -16.607 -8.031 5.635 1.00 65.22 C HETATM 3359 C12 OLA A1216 -16.657 -6.505 5.849 1.00 62.06 C HETATM 3360 C1 OLA A1217 -37.641 15.690 9.152 1.00 84.28 C HETATM 3361 O1 OLA A1217 -38.449 16.307 8.400 1.00 85.73 O HETATM 3362 O2 OLA A1217 -36.569 16.253 9.438 1.00 83.33 O HETATM 3363 C2 OLA A1217 -37.945 14.309 9.700 1.00 82.35 C HETATM 3364 C3 OLA A1217 -39.236 13.726 9.120 1.00 81.80 C HETATM 3365 C4 OLA A1217 -39.138 12.236 8.815 1.00 78.23 C HETATM 3366 C5 OLA A1217 -40.450 11.496 8.983 1.00 76.89 C HETATM 3367 C6 OLA A1217 -40.312 10.031 9.375 1.00 73.61 C HETATM 3368 C7 OLA A1217 -40.582 9.107 8.190 1.00 72.64 C HETATM 3369 C8 OLA A1217 -40.808 7.649 8.544 1.00 71.09 C HETATM 3370 C9 OLA A1217 -41.952 7.126 7.688 1.00 72.19 C HETATM 3371 C10 OLA A1217 -42.237 5.826 7.455 1.00 71.48 C HETATM 3372 C11 OLA A1217 -41.433 4.682 8.032 1.00 71.99 C HETATM 3373 C12 OLA A1217 -41.848 3.331 7.418 1.00 74.49 C HETATM 3374 C13 OLA A1217 -42.860 2.548 8.279 1.00 75.46 C HETATM 3375 C14 OLA A1217 -42.241 1.325 8.973 1.00 74.30 C HETATM 3376 C15 OLA A1217 -43.217 0.587 9.909 1.00 75.35 C HETATM 3377 C16 OLA A1217 -43.471 -0.874 9.497 1.00 75.92 C HETATM 3378 C17 OLA A1217 -42.190 -1.629 9.107 1.00 76.78 C HETATM 3379 C18 OLA A1217 -42.396 -3.150 9.040 1.00 77.54 C HETATM 3380 C2 OLA A1218 -8.583 -15.394 16.678 1.00 41.31 C HETATM 3381 C3 OLA A1218 -10.037 -14.920 16.753 1.00 42.85 C HETATM 3382 C4 OLA A1218 -10.284 -13.884 17.841 1.00 45.30 C HETATM 3383 C5 OLA A1218 -9.887 -12.484 17.423 1.00 46.89 C HETATM 3384 C6 OLA A1218 -10.143 -11.409 18.466 1.00 47.06 C HETATM 3385 C7 OLA A1218 -9.556 -10.072 18.027 1.00 51.10 C HETATM 3386 C8 OLA A1218 -8.271 -9.678 18.731 1.00 53.87 C HETATM 3387 C9 OLA A1218 -8.110 -8.168 18.639 1.00 55.63 C HETATM 3388 C10 OLA A1218 -8.365 -7.285 19.631 1.00 56.24 C HETATM 3389 C1 OLA A1219 -43.565 -24.226 13.205 1.00 71.64 C HETATM 3390 O1 OLA A1219 -44.057 -24.959 12.304 1.00 73.61 O HETATM 3391 O2 OLA A1219 -42.662 -24.704 13.912 1.00 72.00 O HETATM 3392 C2 OLA A1219 -44.046 -22.808 13.430 1.00 69.82 C HETATM 3393 C3 OLA A1219 -43.082 -22.009 14.311 1.00 68.01 C HETATM 3394 C4 OLA A1219 -43.462 -20.538 14.428 1.00 69.24 C HETATM 3395 C5 OLA A1219 -42.439 -19.707 15.176 1.00 69.00 C HETATM 3396 C6 OLA A1219 -41.058 -20.342 15.285 1.00 70.39 C HETATM 3397 C7 OLA A1219 -40.202 -19.669 16.356 1.00 70.80 C HETATM 3398 C8 OLA A1219 -39.384 -18.482 15.876 1.00 69.52 C HETATM 3399 C9 OLA A1219 -38.165 -18.986 15.115 1.00 66.76 C HETATM 3400 C10 OLA A1219 -37.551 -18.353 14.089 1.00 64.23 C HETATM 3401 C11 OLA A1219 -37.996 -17.016 13.531 1.00 61.97 C HETATM 3402 C12 OLA A1219 -37.352 -15.824 14.268 1.00 58.34 C HETATM 3403 C13 OLA A1219 -37.859 -14.454 13.771 1.00 58.14 C HETATM 3404 C14 OLA A1219 -37.519 -13.282 14.707 1.00 58.42 C HETATM 3405 C15 OLA A1219 -37.967 -11.910 14.160 1.00 61.55 C HETATM 3406 C16 OLA A1219 -38.041 -10.802 15.229 1.00 61.23 C HETATM 3407 C17 OLA A1219 -38.402 -9.418 14.665 1.00 58.07 C HETATM 3408 C1 OLA A1220 -8.272 -18.984 11.939 1.00 64.86 C HETATM 3409 C2 OLA A1220 -8.928 -17.761 11.327 1.00 62.84 C HETATM 3410 C3 OLA A1220 -8.440 -16.459 11.974 1.00 62.21 C HETATM 3411 C4 OLA A1220 -9.543 -15.428 12.187 1.00 62.06 C HETATM 3412 C5 OLA A1220 -9.206 -14.039 11.673 1.00 61.49 C HETATM 3413 C6 OLA A1220 -10.156 -13.488 10.616 1.00 60.50 C HETATM 3414 C7 OLA A1220 -9.982 -11.982 10.420 1.00 59.95 C HETATM 3415 C8 OLA A1220 -9.773 -11.195 11.702 1.00 60.76 C HETATM 3416 C9 OLA A1220 -8.612 -10.229 11.520 1.00 61.54 C HETATM 3417 C10 OLA A1220 -8.120 -9.396 12.467 1.00 60.61 C HETATM 3418 C11 OLA A1220 -8.666 -9.306 13.875 1.00 58.76 C HETATM 3419 C12 OLA A1220 -8.112 -8.081 14.628 1.00 57.72 C HETATM 3420 C10 OLA A1221 -12.612 -3.809 7.140 1.00 62.69 C HETATM 3421 C11 OLA A1221 -11.944 -2.865 8.118 1.00 62.52 C HETATM 3422 C12 OLA A1221 -10.620 -2.302 7.569 1.00 64.76 C HETATM 3423 C13 OLA A1221 -10.326 -0.858 8.027 1.00 66.07 C HETATM 3424 C14 OLA A1221 -11.160 0.197 7.282 1.00 64.94 C HETATM 3425 C15 OLA A1221 -10.558 1.617 7.309 1.00 62.33 C HETATM 3426 C16 OLA A1221 -11.485 2.660 7.960 1.00 56.51 C HETATM 3427 C17 OLA A1221 -12.980 2.354 7.781 1.00 51.02 C HETATM 3428 C18 OLA A1221 -13.878 3.353 8.527 1.00 47.12 C HETATM 3429 C1 OLA A1222 -8.710 14.627 8.130 1.00 69.03 C HETATM 3430 O1 OLA A1222 -8.884 15.575 7.316 1.00 72.09 O HETATM 3431 O2 OLA A1222 -8.995 14.823 9.325 1.00 71.13 O HETATM 3432 C2 OLA A1222 -8.175 13.284 7.680 1.00 63.18 C HETATM 3433 C3 OLA A1222 -9.088 12.656 6.626 1.00 59.47 C HETATM 3434 C4 OLA A1222 -9.437 11.206 6.928 1.00 57.48 C HETATM 3435 C5 OLA A1222 -8.530 10.209 6.234 1.00 57.79 C HETATM 3436 C6 OLA A1222 -9.224 8.951 5.732 1.00 58.97 C HETATM 3437 C7 OLA A1222 -8.623 7.690 6.352 1.00 60.48 C HETATM 3438 C8 OLA A1222 -9.104 6.383 5.748 1.00 61.98 C HETATM 3439 C9 OLA A1222 -10.564 6.541 5.348 1.00 64.42 C HETATM 3440 C10 OLA A1222 -11.232 5.765 4.465 1.00 66.52 C HETATM 3441 C11 OLA A1222 -10.605 4.598 3.734 1.00 68.97 C HETATM 3442 C12 OLA A1222 -11.458 4.148 2.531 1.00 71.10 C HETATM 3443 C13 OLA A1222 -11.999 2.712 2.673 1.00 72.77 C HETATM 3444 C14 OLA A1222 -11.844 1.875 1.394 1.00 75.79 C HETATM 3445 C15 OLA A1222 -10.642 0.911 1.423 1.00 77.27 C HETATM 3446 C16 OLA A1222 -10.032 0.735 2.825 1.00 76.78 C HETATM 3447 C17 OLA A1222 -8.838 -0.232 2.855 1.00 77.00 C HETATM 3448 C18 OLA A1222 -9.200 -1.590 3.474 1.00 76.48 C HETATM 3449 C10 OLC A1223 -3.550 1.617 25.761 1.00 51.42 C HETATM 3450 C9 OLC A1223 -3.436 2.931 25.805 1.00 50.02 C HETATM 3451 C11 OLC A1223 -3.399 0.804 24.523 1.00 52.10 C HETATM 3452 C8 OLC A1223 -3.153 3.812 24.635 1.00 47.13 C HETATM 3453 C24 OLC A1223 -0.069 16.617 24.886 1.00 64.16 C HETATM 3454 C12 OLC A1223 -4.092 -0.534 24.736 1.00 51.59 C HETATM 3455 C7 OLC A1223 -3.648 5.214 24.925 1.00 42.20 C HETATM 3456 C6 OLC A1223 -2.613 6.171 25.423 1.00 36.92 C HETATM 3457 C5 OLC A1223 -2.834 7.551 24.893 1.00 33.80 C HETATM 3458 C4 OLC A1223 -2.544 8.550 25.963 1.00 35.87 C HETATM 3459 C3 OLC A1223 -1.697 9.673 25.447 1.00 36.16 C HETATM 3460 C2 OLC A1223 -2.453 10.942 25.201 1.00 42.51 C HETATM 3461 C21 OLC A1223 -0.894 14.314 25.022 1.00 56.36 C HETATM 3462 C1 OLC A1223 -1.724 12.145 25.711 1.00 47.47 C HETATM 3463 C22 OLC A1223 -1.272 15.762 25.245 1.00 59.80 C HETATM 3464 O19 OLC A1223 -0.899 12.065 26.558 1.00 49.30 O HETATM 3465 O25 OLC A1223 0.559 17.073 26.077 1.00 65.72 O HETATM 3466 O23 OLC A1223 -2.415 16.114 24.461 1.00 58.35 O HETATM 3467 O20 OLC A1223 -1.980 13.451 25.199 1.00 50.22 O HETATM 3468 C9 OLC A1224 -30.755 -1.818 38.422 1.00 46.86 C HETATM 3469 C8 OLC A1224 -30.301 -0.414 38.201 1.00 45.00 C HETATM 3470 C24 OLC A1224 -28.619 9.954 37.438 1.00 64.21 C HETATM 3471 C7 OLC A1224 -31.480 0.523 38.325 1.00 48.29 C HETATM 3472 C6 OLC A1224 -31.164 1.868 37.733 1.00 49.93 C HETATM 3473 C5 OLC A1224 -32.293 2.860 37.839 1.00 50.88 C HETATM 3474 C4 OLC A1224 -32.205 3.829 36.692 1.00 49.53 C HETATM 3475 C3 OLC A1224 -32.390 5.251 37.131 1.00 50.36 C HETATM 3476 C2 OLC A1224 -31.603 6.126 36.207 1.00 51.65 C HETATM 3477 C21 OLC A1224 -30.842 9.795 36.233 1.00 60.98 C HETATM 3478 C1 OLC A1224 -31.870 7.556 36.494 1.00 57.47 C HETATM 3479 C22 OLC A1224 -29.421 10.335 36.198 1.00 61.58 C HETATM 3480 O19 OLC A1224 -32.984 7.962 36.632 1.00 60.04 O HETATM 3481 O25 OLC A1224 -27.971 11.117 37.950 1.00 65.53 O HETATM 3482 O23 OLC A1224 -28.749 9.905 35.016 1.00 58.11 O HETATM 3483 O20 OLC A1224 -30.757 8.449 36.587 1.00 61.33 O HETATM 3484 C10 OLC A1225 -42.168 4.037 12.625 1.00 47.18 C HETATM 3485 C9 OLC A1225 -41.346 5.042 12.426 1.00 49.19 C HETATM 3486 C11 OLC A1225 -43.091 3.985 13.779 1.00 44.08 C HETATM 3487 C8 OLC A1225 -41.250 6.188 13.359 1.00 49.35 C HETATM 3488 C24 OLC A1225 -42.199 19.414 14.183 1.00 92.25 C HETATM 3489 C12 OLC A1225 -43.886 2.726 13.607 1.00 46.53 C HETATM 3490 C7 OLC A1225 -40.778 7.387 12.588 1.00 50.61 C HETATM 3491 C15 OLC A1225 -43.741 -0.925 14.406 1.00 45.98 C HETATM 3492 C13 OLC A1225 -43.245 1.511 14.222 1.00 44.40 C HETATM 3493 C6 OLC A1225 -40.669 8.585 13.492 1.00 49.33 C HETATM 3494 C14 OLC A1225 -43.678 0.277 13.487 1.00 46.15 C HETATM 3495 C5 OLC A1225 -41.214 9.823 12.817 1.00 49.47 C HETATM 3496 C4 OLC A1225 -41.173 10.987 13.764 1.00 51.93 C HETATM 3497 C3 OLC A1225 -41.705 12.235 13.119 1.00 58.10 C HETATM 3498 C2 OLC A1225 -40.918 13.383 13.685 1.00 65.19 C HETATM 3499 C21 OLC A1225 -41.794 17.066 13.615 1.00 82.80 C HETATM 3500 C1 OLC A1225 -41.704 14.647 13.575 1.00 72.60 C HETATM 3501 C22 OLC A1225 -41.233 18.255 14.359 1.00 86.73 C HETATM 3502 O19 OLC A1225 -42.785 14.655 13.064 1.00 73.97 O HETATM 3503 O25 OLC A1225 -41.578 20.632 14.614 1.00 94.73 O HETATM 3504 O23 OLC A1225 -41.101 17.937 15.735 1.00 85.12 O HETATM 3505 O20 OLC A1225 -41.180 15.885 14.084 1.00 77.79 O HETATM 3506 C18 OLC A1226 -21.631 -3.436 35.446 1.00 44.33 C HETATM 3507 C10 OLC A1226 -23.255 -11.368 38.483 1.00 66.93 C HETATM 3508 C9 OLC A1226 -23.505 -12.668 38.292 1.00 67.73 C HETATM 3509 C17 OLC A1226 -22.707 -4.111 36.230 1.00 47.63 C HETATM 3510 C11 OLC A1226 -24.210 -10.399 39.130 1.00 65.56 C HETATM 3511 C8 OLC A1226 -24.794 -13.357 38.669 1.00 67.95 C HETATM 3512 C24 OLC A1226 -25.373 -24.580 38.570 1.00 90.70 C HETATM 3513 C16 OLC A1226 -22.228 -5.456 36.743 1.00 50.30 C HETATM 3514 C12 OLC A1226 -23.969 -9.013 38.540 1.00 62.07 C HETATM 3515 C7 OLC A1226 -24.662 -14.848 38.388 1.00 69.24 C HETATM 3516 C15 OLC A1226 -23.190 -6.090 37.737 1.00 51.32 C HETATM 3517 C13 OLC A1226 -23.417 -7.941 39.477 1.00 57.09 C HETATM 3518 C6 OLC A1226 -26.028 -15.495 38.281 1.00 69.57 C HETATM 3519 C14 OLC A1226 -22.491 -6.947 38.789 1.00 53.13 C HETATM 3520 C5 OLC A1226 -26.459 -16.378 39.433 1.00 73.03 C HETATM 3521 C4 OLC A1226 -27.857 -16.901 39.118 1.00 75.68 C HETATM 3522 C3 OLC A1226 -28.155 -18.283 39.694 1.00 79.07 C HETATM 3523 C2 OLC A1226 -27.339 -19.393 39.049 1.00 79.78 C HETATM 3524 C21 OLC A1226 -26.945 -23.152 39.870 1.00 86.52 C HETATM 3525 C1 OLC A1226 -27.596 -20.735 39.699 1.00 81.17 C HETATM 3526 C22 OLC A1226 -26.818 -24.170 38.742 1.00 90.36 C HETATM 3527 O19 OLC A1226 -28.505 -20.893 40.472 1.00 80.31 O HETATM 3528 O25 OLC A1226 -25.377 -25.677 37.663 1.00 91.63 O HETATM 3529 O23 OLC A1226 -27.616 -25.336 39.013 1.00 92.86 O HETATM 3530 O20 OLC A1226 -26.722 -21.843 39.380 1.00 84.16 O HETATM 3531 C18 OLC A1227 -41.832 -4.921 15.283 1.00 69.16 C HETATM 3532 C10 OLC A1227 -38.386 3.215 14.732 1.00 43.28 C HETATM 3533 C9 OLC A1227 -37.802 4.379 14.849 1.00 40.09 C HETATM 3534 C17 OLC A1227 -40.498 -4.324 15.647 1.00 67.01 C HETATM 3535 C11 OLC A1227 -38.666 2.374 15.926 1.00 47.03 C HETATM 3536 C8 OLC A1227 -37.376 4.892 16.174 1.00 39.15 C HETATM 3537 C24 OLC A1227 -37.789 16.291 17.951 1.00 82.28 C HETATM 3538 C16 OLC A1227 -40.630 -3.369 16.815 1.00 65.91 C HETATM 3539 C12 OLC A1227 -39.164 1.020 15.485 1.00 51.19 C HETATM 3540 C7 OLC A1227 -37.191 6.375 16.048 1.00 40.95 C HETATM 3541 C15 OLC A1227 -40.825 -1.941 16.354 1.00 64.20 C HETATM 3542 C13 OLC A1227 -39.633 0.284 16.715 1.00 56.51 C HETATM 3543 C6 OLC A1227 -37.455 6.999 17.389 1.00 42.62 C HETATM 3544 C14 OLC A1227 -39.514 -1.210 16.524 1.00 60.70 C HETATM 3545 C5 OLC A1227 -37.114 8.452 17.442 1.00 39.78 C HETATM 3546 C4 OLC A1227 -38.026 9.311 16.632 1.00 40.74 C HETATM 3547 C3 OLC A1227 -37.891 10.703 17.173 1.00 43.34 C HETATM 3548 C2 OLC A1227 -38.423 11.797 16.265 1.00 51.68 C HETATM 3549 C21 OLC A1227 -39.938 15.067 17.646 1.00 73.14 C HETATM 3550 C1 OLC A1227 -39.114 12.832 17.110 1.00 57.85 C HETATM 3551 C22 OLC A1227 -38.921 15.569 18.655 1.00 80.96 C HETATM 3552 O19 OLC A1227 -39.538 12.510 18.161 1.00 57.88 O HETATM 3553 O25 OLC A1227 -37.942 17.705 17.949 1.00 84.56 O HETATM 3554 O23 OLC A1227 -39.542 16.441 19.604 1.00 83.42 O HETATM 3555 O20 OLC A1227 -39.274 14.208 16.756 1.00 65.08 O HETATM 3556 C10 OLC A1228 -33.631 -8.380 24.568 1.00 54.25 C HETATM 3557 C9 OLC A1228 -33.284 -9.652 24.520 1.00 50.46 C HETATM 3558 C17 OLC A1228 -36.766 -0.866 24.030 1.00 68.41 C HETATM 3559 C11 OLC A1228 -34.609 -7.771 23.615 1.00 58.82 C HETATM 3560 C8 OLC A1228 -33.760 -10.655 23.515 1.00 46.51 C HETATM 3561 C24 OLC A1228 -31.862 -23.698 24.823 1.00 71.07 C HETATM 3562 C16 OLC A1228 -35.954 -2.003 23.442 1.00 67.09 C HETATM 3563 C12 OLC A1228 -35.068 -6.384 24.065 1.00 61.89 C HETATM 3564 C7 OLC A1228 -32.873 -11.869 23.678 1.00 45.15 C HETATM 3565 C15 OLC A1228 -36.553 -3.371 23.738 1.00 67.60 C HETATM 3566 C13 OLC A1228 -36.234 -5.860 23.225 1.00 63.08 C HETATM 3567 C6 OLC A1228 -33.298 -13.043 22.837 1.00 46.33 C HETATM 3568 C14 OLC A1228 -36.004 -4.429 22.787 1.00 65.44 C HETATM 3569 C5 OLC A1228 -32.315 -14.174 23.008 1.00 48.53 C HETATM 3570 C4 OLC A1228 -32.746 -15.441 22.309 1.00 51.20 C HETATM 3571 C3 OLC A1228 -31.791 -16.600 22.516 1.00 52.02 C HETATM 3572 C2 OLC A1228 -32.608 -17.874 22.527 1.00 58.64 C HETATM 3573 C21 OLC A1228 -31.698 -21.353 23.868 1.00 69.20 C HETATM 3574 C1 OLC A1228 -31.777 -19.101 22.689 1.00 63.35 C HETATM 3575 C22 OLC A1228 -32.495 -22.657 23.912 1.00 70.91 C HETATM 3576 O19 OLC A1228 -30.611 -19.012 22.501 1.00 63.70 O HETATM 3577 O25 OLC A1228 -32.787 -24.734 25.159 1.00 70.90 O HETATM 3578 O23 OLC A1228 -33.791 -22.415 24.414 1.00 72.49 O HETATM 3579 O20 OLC A1228 -32.350 -20.384 23.058 1.00 67.95 O HETATM 3580 C10 OLC A1229 -36.188 -10.459 18.658 1.00 58.99 C HETATM 3581 C9 OLC A1229 -35.315 -11.274 18.114 1.00 56.21 C HETATM 3582 C8 OLC A1229 -35.722 -12.679 17.816 1.00 55.16 C HETATM 3583 C24 OLC A1229 -35.046 -24.967 20.384 1.00 72.68 C HETATM 3584 C7 OLC A1229 -34.618 -13.550 18.351 1.00 53.49 C HETATM 3585 C6 OLC A1229 -35.120 -14.803 19.039 1.00 51.95 C HETATM 3586 C5 OLC A1229 -35.350 -15.888 18.030 1.00 51.51 C HETATM 3587 C4 OLC A1229 -35.545 -17.206 18.739 1.00 53.19 C HETATM 3588 C3 OLC A1229 -35.405 -18.397 17.823 1.00 53.93 C HETATM 3589 C2 OLC A1229 -35.411 -19.654 18.654 1.00 55.98 C HETATM 3590 C21 OLC A1229 -34.863 -22.791 19.214 1.00 65.56 C HETATM 3591 C1 OLC A1229 -34.466 -20.652 18.082 1.00 58.36 C HETATM 3592 C22 OLC A1229 -34.158 -23.775 20.102 1.00 69.78 C HETATM 3593 O19 OLC A1229 -34.118 -20.558 16.944 1.00 60.81 O HETATM 3594 O25 OLC A1229 -34.331 -25.857 21.236 1.00 74.00 O HETATM 3595 O23 OLC A1229 -33.020 -24.228 19.396 1.00 71.82 O HETATM 3596 O20 OLC A1229 -33.979 -21.753 18.869 1.00 59.70 O HETATM 3597 C10 OLC A1230 -34.400 -10.592 28.436 1.00 57.76 C HETATM 3598 C9 OLC A1230 -34.338 -11.805 27.901 1.00 55.98 C HETATM 3599 C17 OLC A1230 -31.675 -4.184 32.992 1.00 52.41 C HETATM 3600 C11 OLC A1230 -33.359 -9.799 29.155 1.00 53.85 C HETATM 3601 C8 OLC A1230 -33.186 -12.740 27.897 1.00 49.39 C HETATM 3602 C16 OLC A1230 -32.502 -5.423 32.665 1.00 53.47 C HETATM 3603 C12 OLC A1230 -33.977 -8.416 29.341 1.00 54.10 C HETATM 3604 C7 OLC A1230 -33.563 -13.847 26.938 1.00 45.33 C HETATM 3605 C15 OLC A1230 -33.391 -5.215 31.454 1.00 51.33 C HETATM 3606 C13 OLC A1230 -33.226 -7.479 30.278 1.00 52.92 C HETATM 3607 C6 OLC A1230 -33.007 -15.205 27.296 1.00 44.40 C HETATM 3608 C14 OLC A1230 -34.099 -6.486 31.024 1.00 52.94 C HETATM 3609 C5 OLC A1230 -33.927 -16.304 26.812 1.00 46.41 C HETATM 3610 C4 OLC A1230 -33.391 -17.677 27.130 1.00 46.27 C HETATM 3611 C18 OLC A1231 -38.577 1.793 5.952 1.00 78.29 C HETATM 3612 C10 OLC A1231 -36.327 10.085 8.191 1.00 76.95 C HETATM 3613 C9 OLC A1231 -35.757 11.231 8.539 1.00 79.35 C HETATM 3614 C17 OLC A1231 -38.460 3.301 6.024 1.00 77.63 C HETATM 3615 C11 OLC A1231 -35.786 9.210 7.099 1.00 74.71 C HETATM 3616 C8 OLC A1231 -34.521 11.695 7.840 1.00 81.62 C HETATM 3617 C24 OLC A1231 -27.525 18.052 13.090 1.00 89.89 C HETATM 3618 C16 OLC A1231 -38.463 3.934 4.647 1.00 77.05 C HETATM 3619 C12 OLC A1231 -36.514 7.885 7.170 1.00 74.27 C HETATM 3620 C7 OLC A1231 -34.480 13.216 7.771 1.00 82.69 C HETATM 3621 C15 OLC A1231 -37.738 5.278 4.615 1.00 75.44 C HETATM 3622 C13 OLC A1231 -36.655 7.180 5.839 1.00 72.73 C HETATM 3623 C6 OLC A1231 -33.119 13.647 7.247 1.00 83.44 C HETATM 3624 C14 OLC A1231 -37.470 5.901 5.978 1.00 74.39 C HETATM 3625 C5 OLC A1231 -32.758 15.032 7.745 1.00 85.21 C HETATM 3626 C4 OLC A1231 -31.299 15.093 8.153 1.00 85.92 C HETATM 3627 C3 OLC A1231 -30.851 16.527 8.305 1.00 87.83 C HETATM 3628 C2 OLC A1231 -29.449 16.725 7.778 1.00 90.10 C HETATM 3629 C21 OLC A1231 -27.410 16.749 11.023 1.00 90.33 C HETATM 3630 C1 OLC A1231 -28.406 16.467 8.830 1.00 91.36 C HETATM 3631 C22 OLC A1231 -26.638 17.683 11.917 1.00 88.92 C HETATM 3632 O19 OLC A1231 -27.767 15.453 8.760 1.00 91.34 O HETATM 3633 O25 OLC A1231 -26.875 18.977 13.952 1.00 88.59 O HETATM 3634 O23 OLC A1231 -25.477 16.974 12.364 1.00 87.24 O HETATM 3635 O20 OLC A1231 -28.085 17.370 9.928 1.00 92.39 O HETATM 3636 C10 OLC A1232 -30.670 -0.633 33.296 1.00 49.91 C HETATM 3637 C9 OLC A1232 -30.855 0.651 33.520 1.00 51.10 C HETATM 3638 C8 OLC A1232 -31.488 1.552 32.509 1.00 52.55 C HETATM 3639 C24 OLC A1232 -34.390 14.068 33.941 1.00 86.45 C HETATM 3640 C7 OLC A1232 -32.445 2.531 33.161 1.00 57.03 C HETATM 3641 C6 OLC A1232 -33.387 3.192 32.158 1.00 60.09 C HETATM 3642 C5 OLC A1232 -34.231 4.318 32.764 1.00 62.74 C HETATM 3643 C4 OLC A1232 -33.572 5.683 32.759 1.00 63.67 C HETATM 3644 C3 OLC A1232 -34.564 6.814 32.927 1.00 65.73 C HETATM 3645 C2 OLC A1232 -33.978 8.172 32.573 1.00 70.12 C HETATM 3646 C21 OLC A1232 -34.225 11.645 33.465 1.00 82.02 C HETATM 3647 C1 OLC A1232 -34.691 9.252 33.361 1.00 78.66 C HETATM 3648 C22 OLC A1232 -35.101 12.730 34.067 1.00 84.67 C HETATM 3649 O19 OLC A1232 -35.052 9.042 34.476 1.00 84.59 O HETATM 3650 O25 OLC A1232 -34.896 14.991 34.911 1.00 89.47 O HETATM 3651 O23 OLC A1232 -36.368 12.770 33.407 1.00 85.72 O HETATM 3652 O20 OLC A1232 -34.980 10.585 32.901 1.00 80.19 O HETATM 3653 C10 OLC A1233 -6.338 -3.879 27.630 1.00 64.00 C HETATM 3654 C9 OLC A1233 -6.433 -2.752 28.314 1.00 64.72 C HETATM 3655 C8 OLC A1233 -5.445 -1.656 28.013 1.00 66.98 C HETATM 3656 C24 OLC A1233 -4.109 10.202 28.602 1.00 68.52 C HETATM 3657 C7 OLC A1233 -5.630 -0.499 28.983 1.00 68.98 C HETATM 3658 C6 OLC A1233 -4.370 0.311 29.285 1.00 68.73 C HETATM 3659 C5 OLC A1233 -4.740 1.779 29.168 1.00 66.23 C HETATM 3660 C4 OLC A1233 -4.017 2.701 30.127 1.00 64.99 C HETATM 3661 C3 OLC A1233 -4.076 4.123 29.604 1.00 61.78 C HETATM 3662 C2 OLC A1233 -3.705 5.118 30.675 1.00 63.52 C HETATM 3663 C21 OLC A1233 -4.149 8.809 30.553 1.00 66.52 C HETATM 3664 C1 OLC A1233 -3.701 6.504 30.113 1.00 66.97 C HETATM 3665 C22 OLC A1233 -3.333 9.841 29.839 1.00 66.79 C HETATM 3666 O19 OLC A1233 -4.003 6.686 28.991 1.00 71.15 O HETATM 3667 O25 OLC A1233 -5.317 10.858 28.973 1.00 69.25 O HETATM 3668 O23 OLC A1233 -3.275 10.999 30.635 1.00 65.02 O HETATM 3669 O20 OLC A1233 -3.361 7.689 30.849 1.00 68.01 O HETATM 3670 O HOH A1301 1.649 -46.932 20.472 1.00 68.13 O HETATM 3671 O HOH A1302 14.893 -61.764 15.141 1.00 54.27 O HETATM 3672 O HOH A1303 2.274 17.639 27.609 1.00 49.87 O HETATM 3673 O HOH A1304 -13.336 17.304 11.370 1.00 43.19 O HETATM 3674 O HOH A1305 11.295 -64.771 14.490 1.00 67.54 O HETATM 3675 O HOH A1306 -24.907 13.393 11.645 1.00 38.78 O HETATM 3676 O HOH A1307 -27.894 3.367 19.551 1.00 21.91 O HETATM 3677 O HOH A1308 -20.834 16.708 18.840 1.00 56.03 O HETATM 3678 O HOH A1309 -28.776 12.499 8.843 1.00 52.53 O HETATM 3679 O HOH A1310 7.670 -72.582 21.787 1.00 59.13 O HETATM 3680 O HOH A1311 -4.314 -63.360 26.888 1.00 48.83 O HETATM 3681 O HOH A1312 -22.637 -27.953 21.576 1.00 50.40 O HETATM 3682 O HOH A1313 -34.330 13.822 29.946 1.00 42.95 O HETATM 3683 O HOH A1314 -14.428 -26.786 17.370 1.00 36.50 O HETATM 3684 O HOH A1315 -25.345 -13.230 13.591 1.00 26.76 O HETATM 3685 O HOH A1316 -23.792 -11.058 11.456 1.00 30.88 O HETATM 3686 O HOH A1317 3.506 -72.570 23.872 1.00 46.03 O HETATM 3687 O HOH A1318 -27.624 3.028 16.878 1.00 15.31 O HETATM 3688 O HOH A1319 -19.389 -35.174 26.789 1.00 62.46 O HETATM 3689 O HOH A1320 -18.252 12.785 23.567 1.00 32.11 O HETATM 3690 O HOH A1321 -16.369 -16.769 19.161 1.00 23.26 O HETATM 3691 O HOH A1322 -4.664 -37.453 21.227 1.00 44.05 O HETATM 3692 O HOH A1323 -18.739 -11.381 12.988 1.00 22.55 O HETATM 3693 O HOH A1324 -36.831 17.557 14.136 1.00 57.94 O HETATM 3694 O HOH A1325 0.514 -67.011 25.037 1.00 41.30 O HETATM 3695 O HOH A1326 14.075 -64.833 16.653 1.00 58.49 O HETATM 3696 O HOH A1327 -14.016 -27.825 19.882 1.00 47.51 O HETATM 3697 O HOH A1328 -26.364 18.321 22.001 1.00 21.50 O HETATM 3698 O HOH A1329 -30.876 8.162 32.376 1.00 59.20 O HETATM 3699 O HOH A1330 -13.137 -33.321 21.371 1.00 42.63 O HETATM 3700 O HOH A1331 -16.952 16.598 8.898 1.00 37.11 O HETATM 3701 O HOH A1332 -24.602 16.667 2.149 1.00 35.96 O HETATM 3702 O HOH A1333 7.234 -60.577 15.375 1.00 44.78 O HETATM 3703 O HOH A1334 -25.131 -15.937 14.781 1.00 30.05 O HETATM 3704 O HOH A1335 -18.871 10.158 22.909 1.00 29.01 O HETATM 3705 O HOH A1336 0.287 13.706 28.303 1.00 56.58 O HETATM 3706 O HOH A1337 -16.576 -29.098 11.548 1.00 45.74 O HETATM 3707 O HOH A1338 -44.508 16.629 12.509 1.00 66.24 O HETATM 3708 O HOH A1339 -24.386 23.527 29.926 1.00 44.46 O HETATM 3709 O HOH A1340 -16.305 0.666 12.806 1.00 17.13 O HETATM 3710 O HOH A1341 -25.715 -14.365 24.663 1.00 29.03 O HETATM 3711 O HOH A1342 -23.502 15.423 33.106 1.00 40.00 O HETATM 3712 O HOH A1343 0.575 -61.764 29.546 1.00 45.24 O HETATM 3713 O HOH A1344 -15.102 10.195 17.835 1.00 22.52 O HETATM 3714 O HOH A1345 -7.770 10.501 30.745 1.00 44.73 O HETATM 3715 O HOH A1346 -10.114 14.845 25.120 1.00 32.74 O HETATM 3716 O HOH A1347 -25.835 -11.927 21.499 1.00 24.37 O HETATM 3717 O HOH A1348 4.199 -47.310 26.319 1.00 44.84 O HETATM 3718 O HOH A1349 -25.756 7.903 13.243 1.00 29.60 O HETATM 3719 O HOH A1350 -14.169 -58.068 22.733 1.00 56.19 O HETATM 3720 O HOH A1351 -4.496 -63.773 17.797 1.00 43.54 O HETATM 3721 O HOH A1352 -20.711 -2.493 24.373 1.00 23.08 O HETATM 3722 O HOH A1353 3.281 -43.328 22.016 1.00 55.25 O HETATM 3723 O HOH A1354 -39.649 15.317 22.099 1.00 61.60 O HETATM 3724 O HOH A1355 -9.710 15.109 18.646 1.00 35.65 O HETATM 3725 O HOH A1356 -38.508 20.908 20.323 1.00 55.22 O HETATM 3726 O HOH A1357 14.998 -55.629 18.543 1.00 43.11 O HETATM 3727 O HOH A1358 -23.406 -28.652 0.578 1.00 57.77 O HETATM 3728 O HOH A1359 -22.008 -6.522 15.387 1.00 24.86 O HETATM 3729 O HOH A1360 -11.292 12.105 15.774 1.00 22.64 O HETATM 3730 O HOH A1361 -22.406 17.919 25.518 1.00 65.21 O HETATM 3731 O HOH A1362 -24.455 11.330 16.592 1.00 23.70 O HETATM 3732 O HOH A1363 -4.307 -25.724 25.034 1.00 43.54 O HETATM 3733 O HOH A1364 -18.124 -2.513 20.124 1.00 19.19 O HETATM 3734 O HOH A1365 -23.335 -4.853 13.997 1.00 18.95 O HETATM 3735 O HOH A1366 2.661 -67.980 18.473 1.00 43.74 O HETATM 3736 O HOH A1367 -10.815 -33.661 21.681 1.00 52.84 O HETATM 3737 O HOH A1368 -7.411 12.333 27.875 1.00 57.81 O HETATM 3738 O HOH A1369 -19.441 -1.483 22.147 1.00 20.81 O HETATM 3739 O HOH A1370 -2.246 13.347 22.019 1.00 32.89 O HETATM 3740 O HOH A1371 -11.416 15.342 23.225 1.00 35.95 O HETATM 3741 O HOH A1372 -0.795 -62.768 19.909 1.00 41.82 O HETATM 3742 O HOH A1373 -22.574 -9.960 15.077 1.00 39.11 O HETATM 3743 O HOH A1374 -15.111 3.720 21.891 1.00 18.13 O HETATM 3744 O HOH A1375 9.328 -70.283 20.654 1.00 34.73 O HETATM 3745 O HOH A1376 -22.276 12.359 17.683 1.00 31.39 O HETATM 3746 O HOH A1377 -25.690 18.684 24.640 1.00 24.06 O HETATM 3747 O HOH A1378 5.720 -75.558 26.500 1.00 32.39 O HETATM 3748 O HOH A1379 -19.842 -30.471 21.052 1.00 63.10 O HETATM 3749 O HOH A1380 -17.964 -17.224 16.838 1.00 26.26 O HETATM 3750 O HOH A1381 -20.360 10.817 16.255 1.00 32.32 O HETATM 3751 O HOH A1382 -24.959 -6.592 17.647 1.00 45.04 O HETATM 3752 O HOH A1383 -26.099 -11.848 25.660 1.00 32.40 O HETATM 3753 O HOH A1384 -32.304 23.646 25.516 1.00 56.19 O HETATM 3754 O HOH A1385 -17.011 15.282 12.427 1.00 52.22 O HETATM 3755 O HOH A1386 -27.362 -11.511 6.820 1.00 40.98 O HETATM 3756 O HOH A1387 -35.201 -31.671 12.739 1.00 42.99 O HETATM 3757 O HOH A1388 -22.632 -31.494 35.614 1.00 60.73 O HETATM 3758 O HOH A1389 -27.725 20.628 22.182 1.00 25.34 O HETATM 3759 O HOH A1390 -12.326 -35.581 28.407 1.00 51.83 O HETATM 3760 O HOH A1391 -30.006 18.055 29.584 1.00 46.16 O HETATM 3761 O HOH A1392 -31.209 20.954 28.057 1.00 55.17 O HETATM 3762 O HOH A1393 -11.984 19.345 15.109 1.00 36.83 O HETATM 3763 O HOH A1394 8.707 -66.179 14.767 1.00 59.92 O HETATM 3764 O HOH A1395 -25.723 16.836 26.633 1.00 32.84 O HETATM 3765 O HOH A1396 -20.609 -11.224 15.160 1.00 46.37 O HETATM 3766 O HOH A1397 -10.190 -28.807 9.066 1.00 56.37 O HETATM 3767 O HOH A1398 -28.034 -31.287 21.641 1.00 58.66 O HETATM 3768 O HOH A1399 -21.760 -29.064 8.977 1.00 37.49 O HETATM 3769 O HOH A1400 -21.292 12.304 34.893 1.00 50.05 O HETATM 3770 O HOH A1401 -17.540 13.727 29.354 1.00 39.60 O HETATM 3771 O HOH A1402 0.807 -72.852 21.677 1.00 59.39 O HETATM 3772 O HOH A1403 -30.182 -28.881 24.266 1.00 56.46 O HETATM 3773 O HOH A1404 -35.951 18.774 16.007 1.00 44.18 O HETATM 3774 O HOH A1405 -5.383 18.829 12.745 1.00 61.77 O HETATM 3775 O HOH A1406 -3.492 16.346 21.690 1.00 34.67 O HETATM 3776 O HOH A1407 -17.388 13.577 26.246 1.00 28.13 O HETATM 3777 O HOH A1408 -2.779 -64.424 19.812 1.00 52.82 O HETATM 3778 O HOH A1409 -20.122 17.343 28.905 1.00 56.55 O HETATM 3779 O HOH A1410 -15.156 12.448 28.449 1.00 24.27 O HETATM 3780 O HOH A1411 -24.866 -29.438 22.954 1.00 47.84 O HETATM 3781 O HOH A1412 -18.814 -28.000 6.737 1.00 41.86 O HETATM 3782 O HOH A1413 -23.707 8.594 15.818 1.00 29.94 O HETATM 3783 O HOH A1414 -5.768 -61.106 28.164 1.00 59.97 O HETATM 3784 O HOH A1415 -17.913 16.068 19.470 1.00 54.59 O HETATM 3785 O HOH A1416 -17.579 15.102 6.118 1.00 33.55 O HETATM 3786 O HOH A1417 -32.700 18.522 12.976 1.00 61.02 O HETATM 3787 O HOH A1418 -21.822 22.833 26.957 1.00 48.83 O HETATM 3788 O HOH A1419 -4.903 -31.204 24.436 1.00 63.04 O HETATM 3789 O HOH A1420 -17.459 12.169 32.438 1.00 40.55 O HETATM 3790 O HOH A1421 -23.227 -15.491 26.396 1.00 48.01 O HETATM 3791 O HOH A1422 -23.611 -26.849 13.777 1.00 58.40 O HETATM 3792 O HOH A1423 18.761 -58.908 26.359 1.00 53.06 O HETATM 3793 O HOH A1424 -9.270 13.514 16.806 1.00 29.23 O HETATM 3794 O HOH A1425 -19.712 12.451 32.754 1.00 47.95 O HETATM 3795 O HOH A1426 -36.622 -30.773 17.412 1.00 55.25 O HETATM 3796 O HOH A1427 -11.685 14.922 4.779 1.00 58.99 O HETATM 3797 O HOH A1428 -17.985 -26.416 4.335 1.00 54.39 O HETATM 3798 O HOH A1429 -31.070 -29.990 6.416 1.00 57.13 O HETATM 3799 O HOH A1430 -13.407 13.521 29.891 1.00 61.92 O HETATM 3800 O HOH A1431 -12.811 -34.186 8.668 1.00 56.14 O HETATM 3801 O HOH A1432 -30.811 20.179 3.463 1.00 44.91 O HETATM 3802 O HOH A1433 -29.651 19.788 32.898 1.00 61.80 O HETATM 3803 O HOH A1434 11.603 -51.868 23.912 1.00 59.94 O HETATM 3804 O HOH A1435 -24.052 15.391 5.296 1.00 56.43 O HETATM 3805 O HOH A1436 -16.588 -30.615 15.481 1.00 51.17 O HETATM 3806 O HOH A1437 -19.257 -28.249 8.856 1.00 44.15 O HETATM 3807 O HOH A1438 -31.375 16.375 31.164 1.00 55.51 O HETATM 3808 O HOH A1439 -8.087 -29.144 9.918 1.00 59.55 O HETATM 3809 O HOH A1440 -19.941 -18.588 15.744 1.00 45.20 O HETATM 3810 O HOH A1441 -1.669 -27.889 24.627 1.00 61.85 O HETATM 3811 O HOH A1442 6.386 -75.767 24.102 1.00 34.26 O HETATM 3812 O HOH A1443 -27.494 29.278 27.030 1.00 56.25 O HETATM 3813 O HOH A1444 8.266 -74.919 27.240 1.00 44.55 O HETATM 3814 O HOH A1445 8.861 -61.972 13.556 1.00 54.02 O HETATM 3815 O HOH A1446 -15.068 -29.870 7.775 1.00 66.87 O HETATM 3816 O HOH A1447 6.148 -65.179 12.668 1.00 55.92 O HETATM 3817 O HOH A1448 4.083 -75.191 22.906 1.00 54.12 O HETATM 3818 O HOH A1449 -31.470 -22.351 -2.612 1.00 39.55 O HETATM 3819 O HOH A1450 -18.104 -27.228 11.026 1.00 51.35 O HETATM 3820 O HOH A1451 -24.199 10.200 13.227 1.00 53.57 O HETATM 3821 O HOH A1452 -21.539 14.805 17.098 1.00 42.46 O HETATM 3822 O HOH A1453 -23.526 12.785 13.808 1.00 48.20 O HETATM 3823 O HOH A1454 -3.123 -29.498 25.500 1.00 64.07 O HETATM 3824 O HOH A1455 -21.558 10.650 13.446 1.00 48.32 O HETATM 3825 O HOH A1456 -20.212 -21.295 15.138 1.00 45.35 O CONECT 417 3099 CONECT 553 1209 CONECT 569 1118 CONECT 589 1253 CONECT 694 3099 CONECT 1118 569 CONECT 1209 553 CONECT 1253 589 CONECT 2645 2666 CONECT 2666 2645 CONECT 3078 3079 3083 CONECT 3079 3078 3080 CONECT 3080 3079 3081 3087 CONECT 3081 3080 3082 3093 CONECT 3082 3081 3083 CONECT 3083 3078 3082 3096 CONECT 3084 3085 3089 3098 CONECT 3085 3084 3086 CONECT 3086 3085 3087 CONECT 3087 3080 3086 3088 CONECT 3088 3087 3089 CONECT 3089 3084 3088 3097 CONECT 3090 3091 3095 CONECT 3091 3090 3092 CONECT 3092 3091 3093 CONECT 3093 3081 3092 3094 CONECT 3094 3093 3095 CONECT 3095 3090 3094 CONECT 3096 3083 CONECT 3097 3089 CONECT 3098 3084 CONECT 3099 417 694 3728 3742 CONECT 3099 3751 CONECT 3100 3101 3109 CONECT 3101 3100 3102 CONECT 3102 3101 3103 3127 CONECT 3103 3102 3104 CONECT 3104 3103 3105 3109 CONECT 3105 3104 3106 CONECT 3106 3105 3107 CONECT 3107 3106 3108 3113 CONECT 3108 3107 3109 3110 CONECT 3109 3100 3104 3108 3118 CONECT 3110 3108 3111 CONECT 3111 3110 3112 CONECT 3112 3111 3113 3116 3117 CONECT 3113 3107 3112 3114 CONECT 3114 3113 3115 CONECT 3115 3114 3116 CONECT 3116 3112 3115 3119 CONECT 3117 3112 CONECT 3118 3109 CONECT 3119 3116 3120 3121 CONECT 3120 3119 CONECT 3121 3119 3122 CONECT 3122 3121 3123 CONECT 3123 3122 3124 CONECT 3124 3123 3125 3126 CONECT 3125 3124 CONECT 3126 3124 CONECT 3127 3102 CONECT 3128 3129 3137 CONECT 3129 3128 3130 CONECT 3130 3129 3131 3155 CONECT 3131 3130 3132 CONECT 3132 3131 3133 3137 CONECT 3133 3132 3134 CONECT 3134 3133 3135 CONECT 3135 3134 3136 3141 CONECT 3136 3135 3137 3138 CONECT 3137 3128 3132 3136 3146 CONECT 3138 3136 3139 CONECT 3139 3138 3140 CONECT 3140 3139 3141 3144 3145 CONECT 3141 3135 3140 3142 CONECT 3142 3141 3143 CONECT 3143 3142 3144 CONECT 3144 3140 3143 3147 CONECT 3145 3140 CONECT 3146 3137 CONECT 3147 3144 3148 3149 CONECT 3148 3147 CONECT 3149 3147 3150 CONECT 3150 3149 3151 CONECT 3151 3150 3152 CONECT 3152 3151 3153 3154 CONECT 3153 3152 CONECT 3154 3152 CONECT 3155 3130 CONECT 3156 3157 3165 CONECT 3157 3156 3158 CONECT 3158 3157 3159 3183 CONECT 3159 3158 3160 CONECT 3160 3159 3161 3165 CONECT 3161 3160 3162 CONECT 3162 3161 3163 CONECT 3163 3162 3164 3169 CONECT 3164 3163 3165 3166 CONECT 3165 3156 3160 3164 3174 CONECT 3166 3164 3167 CONECT 3167 3166 3168 CONECT 3168 3167 3169 3172 3173 CONECT 3169 3163 3168 3170 CONECT 3170 3169 3171 CONECT 3171 3170 3172 CONECT 3172 3168 3171 3175 CONECT 3173 3168 CONECT 3174 3165 CONECT 3175 3172 3176 3177 CONECT 3176 3175 CONECT 3177 3175 3178 CONECT 3178 3177 3179 CONECT 3179 3178 3180 CONECT 3180 3179 3181 3182 CONECT 3181 3180 CONECT 3182 3180 CONECT 3183 3158 CONECT 3184 3185 3193 CONECT 3185 3184 3186 CONECT 3186 3185 3187 3211 CONECT 3187 3186 3188 CONECT 3188 3187 3189 3193 CONECT 3189 3188 3190 CONECT 3190 3189 3191 CONECT 3191 3190 3192 3197 CONECT 3192 3191 3193 3194 CONECT 3193 3184 3188 3192 3202 CONECT 3194 3192 3195 CONECT 3195 3194 3196 CONECT 3196 3195 3197 3200 3201 CONECT 3197 3191 3196 3198 CONECT 3198 3197 3199 CONECT 3199 3198 3200 CONECT 3200 3196 3199 3203 CONECT 3201 3196 CONECT 3202 3193 CONECT 3203 3200 3204 3205 CONECT 3204 3203 CONECT 3205 3203 3206 CONECT 3206 3205 3207 CONECT 3207 3206 3208 CONECT 3208 3207 3209 3210 CONECT 3209 3208 CONECT 3210 3208 CONECT 3211 3186 CONECT 3212 3213 3214 3215 CONECT 3213 3212 CONECT 3214 3212 CONECT 3215 3212 3216 CONECT 3216 3215 3217 CONECT 3217 3216 3218 CONECT 3218 3217 3219 CONECT 3219 3218 3220 CONECT 3220 3219 3221 CONECT 3221 3220 3222 CONECT 3222 3221 3223 CONECT 3223 3222 3224 CONECT 3224 3223 3225 CONECT 3225 3224 3226 CONECT 3226 3225 3227 CONECT 3227 3226 3228 CONECT 3228 3227 3229 CONECT 3229 3228 3230 CONECT 3230 3229 3231 CONECT 3231 3230 CONECT 3232 3233 3234 3235 CONECT 3233 3232 CONECT 3234 3232 CONECT 3235 3232 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 3245 CONECT 3245 3244 3246 CONECT 3246 3245 3247 CONECT 3247 3246 3248 CONECT 3248 3247 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 CONECT 3252 3253 3254 3255 CONECT 3253 3252 CONECT 3254 3252 CONECT 3255 3252 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 CONECT 3261 3262 3263 3264 CONECT 3262 3261 CONECT 3263 3261 CONECT 3264 3261 3265 CONECT 3265 3264 3266 CONECT 3266 3265 3267 CONECT 3267 3266 3268 CONECT 3268 3267 3269 CONECT 3269 3268 3270 CONECT 3270 3269 3271 CONECT 3271 3270 3272 CONECT 3272 3271 3273 CONECT 3273 3272 3274 CONECT 3274 3273 3275 CONECT 3275 3274 3276 CONECT 3276 3275 3277 CONECT 3277 3276 3278 CONECT 3278 3277 3279 CONECT 3279 3278 3280 CONECT 3280 3279 CONECT 3281 3282 3283 3284 CONECT 3282 3281 CONECT 3283 3281 CONECT 3284 3281 3285 CONECT 3285 3284 3286 CONECT 3286 3285 3287 CONECT 3287 3286 3288 CONECT 3288 3287 3289 CONECT 3289 3288 3290 CONECT 3290 3289 3291 CONECT 3291 3290 3292 CONECT 3292 3291 3293 CONECT 3293 3292 3294 CONECT 3294 3293 3295 CONECT 3295 3294 3296 CONECT 3296 3295 3297 CONECT 3297 3296 3298 CONECT 3298 3297 CONECT 3299 3300 3301 3302 CONECT 3300 3299 CONECT 3301 3299 CONECT 3302 3299 3303 CONECT 3303 3302 3304 CONECT 3304 3303 3305 CONECT 3305 3304 3306 CONECT 3306 3305 3307 CONECT 3307 3306 3308 CONECT 3308 3307 3309 CONECT 3309 3308 3310 CONECT 3310 3309 3311 CONECT 3311 3310 3312 CONECT 3312 3311 CONECT 3313 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 3322 CONECT 3322 3321 3323 CONECT 3323 3322 3324 CONECT 3324 3323 3325 CONECT 3325 3324 CONECT 3326 3327 3328 3329 CONECT 3327 3326 CONECT 3328 3326 CONECT 3329 3326 3330 CONECT 3330 3329 3331 CONECT 3331 3330 3332 CONECT 3332 3331 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 CONECT 3338 3339 3340 3341 CONECT 3339 3338 CONECT 3340 3338 CONECT 3341 3338 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 CONECT 3350 3351 CONECT 3351 3350 3352 CONECT 3352 3351 3353 CONECT 3353 3352 3354 CONECT 3354 3353 3355 CONECT 3355 3354 3356 CONECT 3356 3355 3357 CONECT 3357 3356 3358 CONECT 3358 3357 3359 CONECT 3359 3358 CONECT 3360 3361 3362 3363 CONECT 3361 3360 CONECT 3362 3360 CONECT 3363 3360 3364 CONECT 3364 3363 3365 CONECT 3365 3364 3366 CONECT 3366 3365 3367 CONECT 3367 3366 3368 CONECT 3368 3367 3369 CONECT 3369 3368 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 CONECT 3374 3373 3375 CONECT 3375 3374 3376 CONECT 3376 3375 3377 CONECT 3377 3376 3378 CONECT 3378 3377 3379 CONECT 3379 3378 CONECT 3380 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 CONECT 3389 3390 3391 3392 CONECT 3390 3389 CONECT 3391 3389 CONECT 3392 3389 3393 CONECT 3393 3392 3394 CONECT 3394 3393 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 CONECT 3403 3402 3404 CONECT 3404 3403 3405 CONECT 3405 3404 3406 CONECT 3406 3405 3407 CONECT 3407 3406 CONECT 3408 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 3417 CONECT 3417 3416 3418 CONECT 3418 3417 3419 CONECT 3419 3418 CONECT 3420 3421 CONECT 3421 3420 3422 CONECT 3422 3421 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 3428 CONECT 3428 3427 CONECT 3429 3430 3431 3432 CONECT 3430 3429 CONECT 3431 3429 CONECT 3432 3429 3433 CONECT 3433 3432 3434 CONECT 3434 3433 3435 CONECT 3435 3434 3436 CONECT 3436 3435 3437 CONECT 3437 3436 3438 CONECT 3438 3437 3439 CONECT 3439 3438 3440 CONECT 3440 3439 3441 CONECT 3441 3440 3442 CONECT 3442 3441 3443 CONECT 3443 3442 3444 CONECT 3444 3443 3445 CONECT 3445 3444 3446 CONECT 3446 3445 3447 CONECT 3447 3446 3448 CONECT 3448 3447 CONECT 3449 3450 3451 CONECT 3450 3449 3452 CONECT 3451 3449 3454 CONECT 3452 3450 3455 CONECT 3453 3463 3465 CONECT 3454 3451 CONECT 3455 3452 3456 CONECT 3456 3455 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3459 CONECT 3459 3458 3460 CONECT 3460 3459 3462 CONECT 3461 3463 3467 CONECT 3462 3460 3464 3467 CONECT 3463 3453 3461 3466 CONECT 3464 3462 CONECT 3465 3453 CONECT 3466 3463 CONECT 3467 3461 3462 CONECT 3468 3469 CONECT 3469 3468 3471 CONECT 3470 3479 3481 CONECT 3471 3469 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 3475 CONECT 3475 3474 3476 CONECT 3476 3475 3478 CONECT 3477 3479 3483 CONECT 3478 3476 3480 3483 CONECT 3479 3470 3477 3482 CONECT 3480 3478 CONECT 3481 3470 CONECT 3482 3479 CONECT 3483 3477 3478 CONECT 3484 3485 3486 CONECT 3485 3484 3487 CONECT 3486 3484 3489 CONECT 3487 3485 3490 CONECT 3488 3501 3503 CONECT 3489 3486 3492 CONECT 3490 3487 3493 CONECT 3491 3494 CONECT 3492 3489 3494 CONECT 3493 3490 3495 CONECT 3494 3491 3492 CONECT 3495 3493 3496 CONECT 3496 3495 3497 CONECT 3497 3496 3498 CONECT 3498 3497 3500 CONECT 3499 3501 3505 CONECT 3500 3498 3502 3505 CONECT 3501 3488 3499 3504 CONECT 3502 3500 CONECT 3503 3488 CONECT 3504 3501 CONECT 3505 3499 3500 CONECT 3506 3509 CONECT 3507 3508 3510 CONECT 3508 3507 3511 CONECT 3509 3506 3513 CONECT 3510 3507 3514 CONECT 3511 3508 3515 CONECT 3512 3526 3528 CONECT 3513 3509 3516 CONECT 3514 3510 3517 CONECT 3515 3511 3518 CONECT 3516 3513 3519 CONECT 3517 3514 3519 CONECT 3518 3515 3520 CONECT 3519 3516 3517 CONECT 3520 3518 3521 CONECT 3521 3520 3522 CONECT 3522 3521 3523 CONECT 3523 3522 3525 CONECT 3524 3526 3530 CONECT 3525 3523 3527 3530 CONECT 3526 3512 3524 3529 CONECT 3527 3525 CONECT 3528 3512 CONECT 3529 3526 CONECT 3530 3524 3525 CONECT 3531 3534 CONECT 3532 3533 3535 CONECT 3533 3532 3536 CONECT 3534 3531 3538 CONECT 3535 3532 3539 CONECT 3536 3533 3540 CONECT 3537 3551 3553 CONECT 3538 3534 3541 CONECT 3539 3535 3542 CONECT 3540 3536 3543 CONECT 3541 3538 3544 CONECT 3542 3539 3544 CONECT 3543 3540 3545 CONECT 3544 3541 3542 CONECT 3545 3543 3546 CONECT 3546 3545 3547 CONECT 3547 3546 3548 CONECT 3548 3547 3550 CONECT 3549 3551 3555 CONECT 3550 3548 3552 3555 CONECT 3551 3537 3549 3554 CONECT 3552 3550 CONECT 3553 3537 CONECT 3554 3551 CONECT 3555 3549 3550 CONECT 3556 3557 3559 CONECT 3557 3556 3560 CONECT 3558 3562 CONECT 3559 3556 3563 CONECT 3560 3557 3564 CONECT 3561 3575 3577 CONECT 3562 3558 3565 CONECT 3563 3559 3566 CONECT 3564 3560 3567 CONECT 3565 3562 3568 CONECT 3566 3563 3568 CONECT 3567 3564 3569 CONECT 3568 3565 3566 CONECT 3569 3567 3570 CONECT 3570 3569 3571 CONECT 3571 3570 3572 CONECT 3572 3571 3574 CONECT 3573 3575 3579 CONECT 3574 3572 3576 3579 CONECT 3575 3561 3573 3578 CONECT 3576 3574 CONECT 3577 3561 CONECT 3578 3575 CONECT 3579 3573 3574 CONECT 3580 3581 CONECT 3581 3580 3582 CONECT 3582 3581 3584 CONECT 3583 3592 3594 CONECT 3584 3582 3585 CONECT 3585 3584 3586 CONECT 3586 3585 3587 CONECT 3587 3586 3588 CONECT 3588 3587 3589 CONECT 3589 3588 3591 CONECT 3590 3592 3596 CONECT 3591 3589 3593 3596 CONECT 3592 3583 3590 3595 CONECT 3593 3591 CONECT 3594 3583 CONECT 3595 3592 CONECT 3596 3590 3591 CONECT 3597 3598 3600 CONECT 3598 3597 3601 CONECT 3599 3602 CONECT 3600 3597 3603 CONECT 3601 3598 3604 CONECT 3602 3599 3605 CONECT 3603 3600 3606 CONECT 3604 3601 3607 CONECT 3605 3602 3608 CONECT 3606 3603 3608 CONECT 3607 3604 3609 CONECT 3608 3605 3606 CONECT 3609 3607 3610 CONECT 3610 3609 CONECT 3611 3614 CONECT 3612 3613 3615 CONECT 3613 3612 3616 CONECT 3614 3611 3618 CONECT 3615 3612 3619 CONECT 3616 3613 3620 CONECT 3617 3631 3633 CONECT 3618 3614 3621 CONECT 3619 3615 3622 CONECT 3620 3616 3623 CONECT 3621 3618 3624 CONECT 3622 3619 3624 CONECT 3623 3620 3625 CONECT 3624 3621 3622 CONECT 3625 3623 3626 CONECT 3626 3625 3627 CONECT 3627 3626 3628 CONECT 3628 3627 3630 CONECT 3629 3631 3635 CONECT 3630 3628 3632 3635 CONECT 3631 3617 3629 3634 CONECT 3632 3630 CONECT 3633 3617 CONECT 3634 3631 CONECT 3635 3629 3630 CONECT 3636 3637 CONECT 3637 3636 3638 CONECT 3638 3637 3640 CONECT 3639 3648 3650 CONECT 3640 3638 3641 CONECT 3641 3640 3642 CONECT 3642 3641 3643 CONECT 3643 3642 3644 CONECT 3644 3643 3645 CONECT 3645 3644 3647 CONECT 3646 3648 3652 CONECT 3647 3645 3649 3652 CONECT 3648 3639 3646 3651 CONECT 3649 3647 CONECT 3650 3639 CONECT 3651 3648 CONECT 3652 3646 3647 CONECT 3653 3654 CONECT 3654 3653 3655 CONECT 3655 3654 3657 CONECT 3656 3665 3667 CONECT 3657 3655 3658 CONECT 3658 3657 3659 CONECT 3659 3658 3660 CONECT 3660 3659 3661 CONECT 3661 3660 3662 CONECT 3662 3661 3664 CONECT 3663 3665 3669 CONECT 3664 3662 3666 3669 CONECT 3665 3656 3663 3668 CONECT 3666 3664 CONECT 3667 3656 CONECT 3668 3665 CONECT 3669 3663 3664 CONECT 3728 3099 CONECT 3742 3099 CONECT 3751 3099 MASTER 514 0 33 19 2 0 52 6 3755 1 606 34 END