HEADER MEMBRANE PROTEIN 01-FEB-17 5MZP TITLE CRYSTAL STRUCTURE OF STABILIZED A2A ADENOSINE RECEPTOR A2AR-STAR2-BRIL TITLE 2 IN COMPLEX WITH CAFFEINE AT 2.1A RESOLUTION 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_VARIANT: TNI PRO; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PFAST-BAC KEYWDS G-PROTEIN-COUPLED RECEPTOR, INTEGRAL MEMBRANE PROTEIN, CHIMERA, KEYWDS 2 THERMOSTABILIZING MUTATIONS, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.Y.R.CHENG,E.SEGALA,N.ROBERTSON,F.DEFLORIAN,A.S.DORE,J.C.ERREY, AUTHOR 2 C.FIEZ-VANDAL,F.H.MARSHALL,R.M.COOKE REVDAT 2 09-AUG-17 5MZP 1 JRNL REVDAT 1 26-JUL-17 5MZP 0 JRNL AUTH R.K.Y.CHENG,E.SEGALA,N.ROBERTSON,F.DEFLORIAN,A.S.DORE, JRNL AUTH 2 J.C.ERREY,C.FIEZ-VANDAL,F.H.MARSHALL,R.M.COOKE JRNL TITL STRUCTURES OF HUMAN A1 AND A2A ADENOSINE RECEPTORS WITH JRNL TITL 2 XANTHINES REVEAL DETERMINANTS OF SELECTIVITY. JRNL REF STRUCTURE V. 25 1275 2017 JRNL REFN ISSN 1878-4186 JRNL PMID 28712806 JRNL DOI 10.1016/J.STR.2017.06.012 REMARK 2 REMARK 2 RESOLUTION. 2.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10.1_2155: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.53 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 3 NUMBER OF REFLECTIONS : 29222 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.197 REMARK 3 R VALUE (WORKING SET) : 0.196 REMARK 3 FREE R VALUE : 0.220 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.060 REMARK 3 FREE R VALUE TEST SET COUNT : 1479 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 38.5331 - 4.6679 0.96 2636 146 0.1930 0.1871 REMARK 3 2 4.6679 - 3.7060 0.97 2521 144 0.1603 0.1967 REMARK 3 3 3.7060 - 3.2378 0.99 2559 134 0.1779 0.2351 REMARK 3 4 3.2378 - 2.9419 0.99 2506 140 0.1964 0.2117 REMARK 3 5 2.9419 - 2.7311 0.98 2507 115 0.1956 0.2439 REMARK 3 6 2.7311 - 2.5701 0.98 2494 120 0.1992 0.2198 REMARK 3 7 2.5701 - 2.4414 0.99 2495 143 0.2115 0.2239 REMARK 3 8 2.4414 - 2.3352 0.99 2485 156 0.2206 0.2269 REMARK 3 9 2.3352 - 2.2453 1.00 2513 130 0.2360 0.2893 REMARK 3 10 2.2453 - 2.1678 0.99 2507 131 0.2572 0.2679 REMARK 3 11 2.1678 - 2.1000 1.00 2520 120 0.2768 0.3416 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL 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) : 0.210 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.330 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 : 0.027 3665 REMARK 3 ANGLE : 0.953 4890 REMARK 3 CHIRALITY : 0.072 545 REMARK 3 PLANARITY : 0.006 576 REMARK 3 DIHEDRAL : 19.655 1224 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 0 THROUGH 186 ) REMARK 3 ORIGIN FOR THE GROUP (A): -26.0404 -3.7278 20.8347 REMARK 3 T TENSOR REMARK 3 T11: 0.1059 T22: 0.1289 REMARK 3 T33: 0.0874 T12: -0.0111 REMARK 3 T13: -0.0110 T23: 0.0118 REMARK 3 L TENSOR REMARK 3 L11: 0.3029 L22: 0.1241 REMARK 3 L33: 0.4225 L12: 0.0241 REMARK 3 L13: 0.0572 L23: 0.2431 REMARK 3 S TENSOR REMARK 3 S11: -0.0406 S12: -0.0612 S13: 0.0316 REMARK 3 S21: -0.0219 S22: 0.0109 S23: 0.0144 REMARK 3 S31: 0.0447 S32: -0.1103 S33: -0.0000 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 187 THROUGH 305 ) REMARK 3 ORIGIN FOR THE GROUP (A): -8.4847 -31.7462 16.2480 REMARK 3 T TENSOR REMARK 3 T11: 0.1614 T22: 0.1053 REMARK 3 T33: 0.2147 T12: 0.0333 REMARK 3 T13: 0.0064 T23: -0.0230 REMARK 3 L TENSOR REMARK 3 L11: 0.0879 L22: 0.1217 REMARK 3 L33: -0.1855 L12: -0.2335 REMARK 3 L13: 0.1358 L23: -0.2596 REMARK 3 S TENSOR REMARK 3 S11: 0.0391 S12: 0.0622 S13: -0.0496 REMARK 3 S21: -0.2691 S22: -0.0010 S23: -0.0860 REMARK 3 S31: -0.0326 S32: 0.0085 S33: -0.0000 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 5MZP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 01-FEB-17. REMARK 100 THE DEPOSITION ID IS D_1200003325. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-MAR-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 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) : 0.96862 REMARK 200 MONOCHROMATOR : DOUBLE SI (111) CRYSTAL REMARK 200 OPTICS : (DOUBLE) KB MIRROR PAIR REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS V1.0 REMARK 200 DATA SCALING SOFTWARE : AIMLESS 6.5.019 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 29678 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.100 REMARK 200 RESOLUTION RANGE LOW (A) : 89.940 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 200 DATA REDUNDANCY : 4.800 REMARK 200 R MERGE (I) : 0.13000 REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.16 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9 REMARK 200 DATA REDUNDANCY IN SHELL : 4.90 REMARK 200 R MERGE FOR SHELL (I) : 0.97700 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.400 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER 2.5.7 REMARK 200 STARTING MODEL: 5IU4 REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 52.36 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.58 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH 5.5, 0.2M K/NA TARTRATE, REMARK 280 27.5-40% PEG400, 0.5-1% (V/V) (+/-)-2-METHYL-2,4-PENTANEDIOL, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -X,Y,-Z+1/2 REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.82000 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 69.82000 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 19.72100 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.93500 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.72100 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.93500 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.82000 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.72100 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.93500 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.82000 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.72100 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.93500 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: 10830 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 21390 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 40.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ASP A -8 REMARK 465 TYR A -7 REMARK 465 LYS A -6 REMARK 465 ASP A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 GLY A -1 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 HIS A 306 REMARK 465 VAL A 307 REMARK 465 LEU A 308 REMARK 465 ARG A 309 REMARK 465 GLN A 310 REMARK 465 GLN A 311 REMARK 465 GLU A 312 REMARK 465 PRO A 313 REMARK 465 PHE A 314 REMARK 465 LYS A 315 REMARK 465 ALA A 316 REMARK 465 ALA A 317 REMARK 465 ALA A 318 REMARK 465 HIS A 319 REMARK 465 HIS A 320 REMARK 465 HIS A 321 REMARK 465 HIS A 322 REMARK 465 HIS A 323 REMARK 465 HIS A 324 REMARK 465 HIS A 325 REMARK 465 HIS A 326 REMARK 465 HIS A 327 REMARK 465 HIS A 328 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: 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 GLY A 162 O HOH A 2501 2.15 REMARK 500 O HOH A 2620 O HOH A 2643 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 -51.71 -121.59 REMARK 500 TYR A1101 -57.00 -134.96 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 2406 REMARK 610 OLA A 2407 REMARK 610 OLA A 2410 REMARK 610 OLA A 2411 REMARK 610 OLA A 2412 REMARK 610 OLA A 2413 REMARK 610 OLA A 2414 REMARK 610 OLA A 2415 REMARK 610 OLA A 2416 REMARK 610 OLA A 2417 REMARK 610 OLA A 2418 REMARK 610 OLA A 2419 REMARK 610 OLA A 2420 REMARK 610 OLA A 2421 REMARK 610 OLA A 2422 REMARK 610 OLA A 2423 REMARK 610 OLC A 2424 REMARK 610 OLC A 2425 REMARK 610 OLC A 2426 REMARK 610 OLC A 2427 REMARK 610 OLC A 2428 REMARK 610 OLC A 2429 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 A2400 NA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 52 OD1 REMARK 620 2 SER A 91 OG 129.2 REMARK 620 3 HOH A2573 O 78.0 123.0 REMARK 620 4 HOH A2507 O 104.3 119.5 90.2 REMARK 620 5 HOH A2546 O 96.5 66.6 170.3 83.5 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 NA A 2400 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CFF A 2401 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2402 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2403 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2404 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 2405 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2406 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2407 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2408 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2410 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2412 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2413 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2414 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2415 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2416 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2417 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2418 REMARK 800 REMARK 800 SITE_IDENTIFIER: AD9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2419 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2420 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2421 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2422 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 2423 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2424 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE6 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2425 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE7 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2426 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE8 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2427 REMARK 800 REMARK 800 SITE_IDENTIFIER: AE9 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2428 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2429 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 2430 REMARK 800 REMARK 800 SITE_IDENTIFIER: AF3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue TAR A 2431 DBREF 5MZP A 2 208 UNP P29274 AA2AR_HUMAN 2 208 DBREF 5MZP A 1001 1106 UNP P0ABE7 C562_ECOLX 23 128 DBREF 5MZP A 219 317 UNP P29274 AA2AR_HUMAN 219 317 SEQADV 5MZP ASP A -8 UNP P29274 EXPRESSION TAG SEQADV 5MZP TYR A -7 UNP P29274 EXPRESSION TAG SEQADV 5MZP LYS A -6 UNP P29274 EXPRESSION TAG SEQADV 5MZP ASP A -5 UNP P29274 EXPRESSION TAG SEQADV 5MZP ASP A -4 UNP P29274 EXPRESSION TAG SEQADV 5MZP ASP A -3 UNP P29274 EXPRESSION TAG SEQADV 5MZP ASP A -2 UNP P29274 EXPRESSION TAG SEQADV 5MZP GLY A -1 UNP P29274 EXPRESSION TAG SEQADV 5MZP ALA A 0 UNP P29274 EXPRESSION TAG SEQADV 5MZP PRO A 1 UNP P29274 EXPRESSION TAG SEQADV 5MZP LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION SEQADV 5MZP ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION SEQADV 5MZP ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION SEQADV 5MZP ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION SEQADV 5MZP ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION SEQADV 5MZP ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION SEQADV 5MZP TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION SEQADV 5MZP ILE A 1102 UNP P0ABE7 HIS 124 CONFLICT SEQADV 5MZP LEU A 1106 UNP P0ABE7 ARG 128 CONFLICT SEQADV 5MZP ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION SEQADV 5MZP ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION SEQADV 5MZP ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION SEQADV 5MZP ALA A 318 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 319 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 320 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 321 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 322 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 323 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 324 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 325 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 326 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 327 UNP P29274 EXPRESSION TAG SEQADV 5MZP HIS A 328 UNP P29274 EXPRESSION TAG SEQRES 1 A 433 ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE MET SEQRES 2 A 433 GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE ALA SEQRES 3 A 433 VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP ALA SEQRES 4 A 433 VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN TYR SEQRES 5 A 433 PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL GLY SEQRES 6 A 433 VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR GLY SEQRES 7 A 433 PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA CYS SEQRES 8 A 433 PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER LEU SEQRES 9 A 433 LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA ILE SEQRES 10 A 433 PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG ALA SEQRES 11 A 433 ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE ALA SEQRES 12 A 433 ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS GLY SEQRES 13 A 433 GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS GLY SEQRES 14 A 433 GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL PRO SEQRES 15 A 433 MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS VAL SEQRES 16 A 433 LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU ARG SEQRES 17 A 433 ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU GLU SEQRES 18 A 433 ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL ILE SEQRES 19 A 433 GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA LEU SEQRES 20 A 433 THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS ALA SEQRES 21 A 433 THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER PRO SEQRES 22 A 433 GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU VAL SEQRES 23 A 433 GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU GLY SEQRES 24 A 433 LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU LYS SEQRES 25 A 433 THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU ARG SEQRES 26 A 433 ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SEQRES 27 A 433 SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS TRP SEQRES 28 A 433 LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS SEQRES 29 A 433 PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU SEQRES 30 A 433 ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN PRO SEQRES 31 A 433 PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR SEQRES 32 A 433 PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN SEQRES 33 A 433 GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS HIS SEQRES 34 A 433 HIS HIS HIS HIS HET NA A2400 1 HET CFF A2401 28 HET CLR A2402 28 HET CLR A2403 28 HET CLR A2404 28 HET CLR A2405 28 HET OLA A2406 9 HET OLA A2407 18 HET OLA A2408 20 HET OLA A2409 20 HET OLA A2410 12 HET OLA A2411 8 HET OLA A2412 15 HET OLA A2413 11 HET OLA A2414 19 HET OLA A2415 14 HET OLA A2416 10 HET OLA A2417 13 HET OLA A2418 12 HET OLA A2419 13 HET OLA A2420 13 HET OLA A2421 15 HET OLA A2422 16 HET OLA A2423 16 HET OLC A2424 16 HET OLC A2425 16 HET OLC A2426 23 HET OLC A2427 23 HET OLC A2428 23 HET OLC A2429 18 HET OLC A2430 25 HET TAR A2431 10 HETNAM NA SODIUM ION HETNAM CFF CAFFEINE HETNAM CLR CHOLESTEROL HETNAM OLA OLEIC ACID HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE HETNAM TAR D(-)-TARTARIC ACID HETSYN CFF 3,7-DIHYDRO-1,3,7-TRIMETHYL-1H-PURINE-2,6-DIONE HETSYN OLC 1-OLEOYL-R-GLYCEROL FORMUL 2 NA NA 1+ FORMUL 3 CFF C8 H10 N4 O2 FORMUL 4 CLR 4(C27 H46 O) FORMUL 8 OLA 18(C18 H34 O2) FORMUL 26 OLC 7(C21 H40 O4) FORMUL 33 TAR C4 H6 O6 FORMUL 34 HOH *177(H2 O) HELIX 1 AA1 PRO A 1 ASN A 34 1 34 HELIX 2 AA2 SER A 35 GLN A 38 5 4 HELIX 3 AA3 ASN A 39 LEU A 58 1 20 HELIX 4 AA4 LEU A 58 SER A 67 1 10 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 LEU A 208 1 23 HELIX 13 AB4 ASP A 1002 LYS A 1019 1 18 HELIX 14 AB5 ASN A 1022 LYS A 1042 1 21 HELIX 15 AB6 GLU A 1057 GLU A 1081 1 25 HELIX 16 AB7 LYS A 1083 GLN A 1093 1 11 HELIX 17 AB8 GLN A 1093 TYR A 1101 1 9 HELIX 18 AB9 TYR A 1101 LEU A 1106 1 6 HELIX 19 AC1 ARG A 220 CYS A 259 1 40 HELIX 20 AC2 PRO A 266 ILE A 292 1 27 HELIX 21 AC3 ILE A 292 SER A 305 1 14 SHEET 1 AA1 2 CYS A 71 ALA A 73 0 SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72 SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03 SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03 SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.08 SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03 LINK OD1 ASP A 52 NA NA A2400 1555 1555 2.46 LINK OG SER A 91 NA NA A2400 1555 1555 2.50 LINK NA NA A2400 O HOH A2573 1555 1555 2.40 LINK NA NA A2400 O HOH A2507 1555 1555 2.65 LINK NA NA A2400 O HOH A2546 1555 1555 2.51 SITE 1 AC1 5 ASP A 52 SER A 91 HOH A2507 HOH A2546 SITE 2 AC1 5 HOH A2573 SITE 1 AC2 12 VAL A 84 PHE A 168 GLU A 169 MET A 177 SITE 2 AC2 12 LEU A 249 ASN A 253 MET A 270 ILE A 274 SITE 3 AC2 12 HOH A2527 HOH A2559 HOH A2589 HOH A2668 SITE 1 AC3 7 ALA A 73 HIS A 75 GLY A 76 OLA A2420 SITE 2 AC3 7 OLA A2421 OLC A2424 HOH A2558 SITE 1 AC4 8 ALA A 72 ALA A 73 GLY A 76 ILE A 80 SITE 2 AC4 8 CLR A2405 OLC A2424 OLC A2427 HOH A2544 SITE 1 AC5 7 LEU A 247 PRO A 248 CYS A 262 SER A 263 SITE 2 AC5 7 OLA A2412 OLC A2426 HOH A2570 SITE 1 AC6 7 PHE A 255 PHE A 258 CLR A2403 OLA A2419 SITE 2 AC6 7 OLC A2424 OLC A2427 HOH A2569 SITE 1 AC7 4 PHE A 44 ALA A 97 ILE A 124 HOH A2584 SITE 1 AC8 2 OLA A2417 HOH A2515 SITE 1 AC9 5 ILE A 127 PRO A 189 LEU A 192 ARG A 199 SITE 2 AC9 5 OLA A2415 SITE 1 AD1 5 SER A 7 LEU A 19 GLY A 23 LEU A 26 SITE 2 AD1 5 PHE A 286 SITE 1 AD2 1 CLR A2404 SITE 1 AD3 3 SER A 7 THR A 11 LEU A 14 SITE 1 AD4 6 VAL A 25 TRP A 29 TRP A 32 PHE A 201 SITE 2 AD4 6 LYS A 233 OLA A2419 SITE 1 AD5 4 ARG A 120 GLY A 123 VAL A 130 OLA A2408 SITE 1 AD6 2 ILE A 287 OLA A2417 SITE 1 AD7 6 VAL A 12 LEU A 19 THR A 279 PHE A 286 SITE 2 AD7 6 OLA A2407 OLA A2416 SITE 1 AD8 1 GLY A 240 SITE 1 AD9 5 LEU A 194 PHE A 201 ALA A 239 CLR A2405 SITE 2 AD9 5 OLA A2414 SITE 1 AE1 5 HIS A 75 MET A 140 CLR A2402 OLA A2422 SITE 2 AE1 5 OLA A2423 SITE 1 AE2 5 TYR A 179 PHE A 258 CLR A2402 OLA A2422 SITE 2 AE2 5 OLC A2424 SITE 1 AE3 10 HIS A 75 MET A 140 LEU A 141 GLY A 142 SITE 2 AE3 10 ASN A 144 ASN A 175 TYR A 179 OLA A2420 SITE 3 AE3 10 OLA A2421 HOH A2525 SITE 1 AE4 3 PHE A 133 OLA A2420 OLC A2428 SITE 1 AE5 5 PHE A 258 CLR A2402 CLR A2403 CLR A2405 SITE 2 AE5 5 OLA A2421 SITE 1 AE6 3 SER A 6 ILE A 10 HOH A2601 SITE 1 AE7 9 ASP A 261 CYS A 262 LYS A1085 CLR A2404 SITE 2 AE7 9 OLC A2427 OLC A2430 HOH A2533 HOH A2570 SITE 3 AE7 9 HOH A2586 SITE 1 AE8 12 VAL A 57 LEU A 58 PRO A 61 THR A 65 SITE 2 AE8 12 PHE A 70 CYS A 71 GLN A 163 CYS A 259 SITE 3 AE8 12 ASP A 261 CLR A2403 CLR A2405 OLC A2426 SITE 1 AE9 6 TYR A 43 SER A 47 GLY A 118 TRP A 129 SITE 2 AE9 6 PHE A 133 OLA A2423 SITE 1 AF1 5 CYS A 28 TRP A 32 TYR A 43 VAL A 46 SITE 2 AF1 5 ALA A 50 SITE 1 AF2 4 THR A 65 THR A 68 OLC A2426 HOH A2595 SITE 1 AF3 6 GLY A 142 TRP A 143 ASN A 144 ASN A 145 SITE 2 AF3 6 ASN A 175 HOH A2617 CRYST1 39.442 179.870 139.640 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 0.025354 0.000000 0.000000 0.00000 SCALE2 0.000000 0.005560 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007161 0.00000 ATOM 1 N ALA A 0 -22.591 22.161 0.758 1.00 76.22 N ANISOU 1 N ALA A 0 10419 8963 9577 -53 -527 445 N ATOM 2 CA ALA A 0 -23.668 21.365 0.180 1.00 81.95 C ANISOU 2 CA ALA A 0 11127 9736 10275 -30 -546 452 C ATOM 3 C ALA A 0 -24.760 21.105 1.213 1.00 92.37 C ANISOU 3 C ALA A 0 12390 11094 11613 28 -569 417 C ATOM 4 O ALA A 0 -24.472 21.014 2.407 1.00 87.56 O ANISOU 4 O ALA A 0 11741 10496 11033 36 -554 384 O ATOM 5 CB ALA A 0 -23.125 20.053 -0.363 1.00 74.48 C ANISOU 5 CB ALA A 0 10161 8837 9302 -77 -505 457 C ATOM 6 N PRO A 1 -26.006 21.000 0.756 1.00 98.36 N ANISOU 6 N PRO A 1 13145 11874 12353 67 -606 423 N ATOM 7 CA PRO A 1 -27.118 20.718 1.672 1.00 96.31 C ANISOU 7 CA PRO A 1 12829 11656 12107 119 -628 387 C ATOM 8 C PRO A 1 -26.875 19.437 2.448 1.00 94.94 C ANISOU 8 C PRO A 1 12594 11542 11938 100 -588 359 C ATOM 9 O PRO A 1 -26.466 18.418 1.871 1.00 93.09 O ANISOU 9 O PRO A 1 12355 11336 11681 60 -557 371 O ATOM 10 CB PRO A 1 -28.324 20.581 0.731 1.00 98.98 C ANISOU 10 CB PRO A 1 13177 12016 12414 149 -665 402 C ATOM 11 CG PRO A 1 -27.957 21.395 -0.460 1.00 99.85 C ANISOU 11 CG PRO A 1 13362 12072 12507 132 -679 446 C ATOM 12 CD PRO A 1 -26.471 21.235 -0.623 1.00 98.65 C ANISOU 12 CD PRO A 1 13231 11896 12355 66 -631 461 C ATOM 13 N PRO A 2 -27.089 19.490 3.747 1.00 94.15 N ANISOU 13 N PRO A 2 12450 11459 11866 128 -589 323 N ATOM 14 CA PRO A 2 -26.869 18.339 4.622 1.00 90.08 C ANISOU 14 CA PRO A 2 11876 10994 11355 113 -554 296 C ATOM 15 C PRO A 2 -27.667 17.087 4.262 1.00 81.70 C ANISOU 15 C PRO A 2 10783 9994 10266 111 -549 294 C ATOM 16 O PRO A 2 -27.156 15.993 4.389 1.00 77.23 O ANISOU 16 O PRO A 2 10193 9457 9692 77 -512 290 O ATOM 17 CB PRO A 2 -27.299 18.865 5.994 1.00 91.44 C ANISOU 17 CB PRO A 2 12012 11173 11559 156 -571 259 C ATOM 18 CG PRO A 2 -28.264 19.964 5.694 1.00 91.49 C ANISOU 18 CG PRO A 2 12041 11152 11569 205 -623 262 C ATOM 19 CD PRO A 2 -27.771 20.599 4.433 1.00 92.39 C ANISOU 19 CD PRO A 2 12224 11212 11669 182 -630 304 C ATOM 20 N ILE A 3 -28.858 17.240 3.703 1.00 78.17 N ANISOU 20 N ILE A 3 10338 9562 9803 144 -586 298 N ATOM 21 CA ILE A 3 -29.729 16.110 3.397 1.00 75.31 C ANISOU 21 CA ILE A 3 9942 9259 9415 144 -584 291 C ATOM 22 C ILE A 3 -29.186 15.266 2.249 1.00 68.09 C ANISOU 22 C ILE A 3 9049 8350 8471 96 -557 320 C ATOM 23 O ILE A 3 -29.576 14.102 2.104 1.00 67.53 O ANISOU 23 O ILE A 3 8948 8328 8382 82 -541 312 O ATOM 24 CB ILE A 3 -31.154 16.606 3.082 1.00 75.92 C ANISOU 24 CB ILE A 3 10015 9350 9481 196 -633 284 C ATOM 25 CG1 ILE A 3 -32.158 15.452 3.150 1.00 76.38 C ANISOU 25 CG1 ILE A 3 10023 9479 9520 200 -630 263 C ATOM 26 CG2 ILE A 3 -31.198 17.261 1.716 1.00 75.84 C ANISOU 26 CG2 ILE A 3 10064 9303 9450 196 -659 321 C ATOM 27 CD1 ILE A 3 -33.561 15.834 2.728 1.00 76.76 C ANISOU 27 CD1 ILE A 3 10063 9548 9552 248 -677 254 C ATOM 28 N MET A 4 -28.321 15.795 1.393 1.00 60.62 N ANISOU 28 N MET A 4 8156 7358 7518 68 -551 351 N ATOM 29 CA MET A 4 -27.731 15.015 0.327 1.00 59.47 C ANISOU 29 CA MET A 4 8030 7221 7344 20 -524 375 C ATOM 30 C MET A 4 -26.775 13.969 0.893 1.00 55.22 C ANISOU 30 C MET A 4 7462 6704 6814 -19 -476 361 C ATOM 31 O MET A 4 -26.908 12.801 0.616 1.00 53.76 O ANISOU 31 O MET A 4 7255 6559 6612 -39 -456 357 O ATOM 32 CB MET A 4 -27.000 15.923 -0.653 1.00 59.89 C ANISOU 32 CB MET A 4 8147 7219 7388 -2 -529 411 C ATOM 33 CG MET A 4 -27.913 16.863 -1.398 1.00 60.64 C ANISOU 33 CG MET A 4 8279 7292 7469 35 -577 431 C ATOM 34 SD MET A 4 -27.017 17.852 -2.576 1.00 64.01 S ANISOU 34 SD MET A 4 8787 7655 7880 2 -580 477 S ATOM 35 CE MET A 4 -26.503 16.675 -3.808 1.00 63.12 C ANISOU 35 CE MET A 4 8680 7577 7727 -55 -545 497 C ATOM 36 N GLY A 5 -25.828 14.403 1.713 1.00 50.80 N ANISOU 36 N GLY A 5 6904 6117 6282 -28 -458 351 N ATOM 37 CA GLY A 5 -24.882 13.512 2.360 1.00 49.41 C ANISOU 37 CA GLY A 5 6700 5958 6115 -59 -416 334 C ATOM 38 C GLY A 5 -25.605 12.549 3.284 1.00 50.20 C ANISOU 38 C GLY A 5 6746 6109 6220 -40 -411 307 C ATOM 39 O GLY A 5 -25.280 11.379 3.351 1.00 47.12 O ANISOU 39 O GLY A 5 6333 5748 5821 -65 -382 300 O ATOM 40 N SER A 6 -26.609 13.049 3.990 1.00 46.85 N ANISOU 40 N SER A 6 6300 5695 5808 5 -441 289 N ATOM 41 CA SER A 6 -27.427 12.231 4.840 1.00 45.31 C ANISOU 41 CA SER A 6 6053 5549 5613 23 -439 263 C ATOM 42 C SER A 6 -28.154 11.191 4.023 1.00 36.37 C ANISOU 42 C SER A 6 4912 4456 4452 11 -437 270 C ATOM 43 O SER A 6 -28.246 10.084 4.442 1.00 33.59 O ANISOU 43 O SER A 6 4527 4140 4095 -3 -415 256 O ATOM 44 CB SER A 6 -28.470 13.066 5.555 1.00 50.09 C ANISOU 44 CB SER A 6 6639 6160 6233 74 -476 243 C ATOM 45 OG SER A 6 -27.876 14.071 6.311 1.00 59.57 O ANISOU 45 OG SER A 6 7848 7324 7462 88 -480 234 O ATOM 46 N SER A 7 -28.645 11.545 2.842 1.00 36.01 N ANISOU 46 N SER A 7 4895 4402 4385 15 -460 291 N ATOM 47 CA SER A 7 -29.382 10.594 2.038 1.00 38.84 C ANISOU 47 CA SER A 7 5242 4800 4715 4 -460 294 C ATOM 48 C SER A 7 -28.539 9.386 1.704 1.00 36.14 C ANISOU 48 C SER A 7 4898 4471 4362 -43 -419 300 C ATOM 49 O SER A 7 -29.030 8.294 1.798 1.00 33.01 O ANISOU 49 O SER A 7 4471 4115 3955 -53 -407 287 O ATOM 50 CB SER A 7 -29.883 11.216 0.743 1.00 42.98 C ANISOU 50 CB SER A 7 5803 5310 5216 15 -491 318 C ATOM 51 OG SER A 7 -30.888 12.157 1.012 1.00 44.28 O ANISOU 51 OG SER A 7 5964 5473 5388 65 -534 309 O ATOM 52 N VAL A 8 -27.285 9.577 1.343 1.00 22.41 N ANISOU 52 N VAL A 8 3190 2698 2627 -74 -398 316 N ATOM 53 CA VAL A 8 -26.448 8.446 1.043 1.00 25.20 C ANISOU 53 CA VAL A 8 3540 3064 2971 -117 -361 318 C ATOM 54 C VAL A 8 -26.233 7.554 2.277 1.00 29.74 C ANISOU 54 C VAL A 8 4076 3662 3563 -119 -336 292 C ATOM 55 O VAL A 8 -26.356 6.356 2.190 1.00 25.23 O ANISOU 55 O VAL A 8 3486 3121 2981 -137 -318 285 O ATOM 56 CB VAL A 8 -25.091 8.865 0.513 1.00 25.76 C ANISOU 56 CB VAL A 8 3648 3097 3043 -149 -342 335 C ATOM 57 CG1 VAL A 8 -24.209 7.659 0.375 1.00 22.83 C ANISOU 57 CG1 VAL A 8 3266 2742 2665 -188 -304 329 C ATOM 58 CG2 VAL A 8 -25.229 9.581 -0.809 1.00 32.15 C ANISOU 58 CG2 VAL A 8 4500 3885 3829 -155 -362 364 C ATOM 59 N TYR A 9 -25.946 8.172 3.421 1.00 30.23 N ANISOU 59 N TYR A 9 4127 3709 3651 -99 -338 279 N ATOM 60 CA TYR A 9 -25.732 7.453 4.661 1.00 23.94 C ANISOU 60 CA TYR A 9 3294 2932 2868 -98 -317 256 C ATOM 61 C TYR A 9 -26.994 6.734 5.083 1.00 21.12 C ANISOU 61 C TYR A 9 2902 2620 2503 -82 -326 241 C ATOM 62 O TYR A 9 -26.944 5.605 5.474 1.00 19.48 O ANISOU 62 O TYR A 9 2673 2437 2291 -98 -304 231 O ATOM 63 CB TYR A 9 -25.211 8.387 5.768 1.00 25.05 C ANISOU 63 CB TYR A 9 3431 3050 3038 -78 -320 243 C ATOM 64 CG TYR A 9 -25.364 7.842 7.176 1.00 24.94 C ANISOU 64 CG TYR A 9 3376 3063 3037 -64 -309 218 C ATOM 65 CD1 TYR A 9 -24.577 6.802 7.625 1.00 22.25 C ANISOU 65 CD1 TYR A 9 3023 2733 2696 -87 -278 211 C ATOM 66 CD2 TYR A 9 -26.305 8.349 8.038 1.00 24.33 C ANISOU 66 CD2 TYR A 9 3273 3001 2969 -28 -332 201 C ATOM 67 CE1 TYR A 9 -24.719 6.290 8.885 1.00 20.39 C ANISOU 67 CE1 TYR A 9 2755 2522 2469 -76 -268 192 C ATOM 68 CE2 TYR A 9 -26.446 7.851 9.311 1.00 25.41 C ANISOU 68 CE2 TYR A 9 3374 3166 3115 -19 -321 179 C ATOM 69 CZ TYR A 9 -25.649 6.818 9.723 1.00 28.28 C ANISOU 69 CZ TYR A 9 3730 3538 3476 -43 -289 176 C ATOM 70 OH TYR A 9 -25.783 6.288 10.952 1.00 30.62 O ANISOU 70 OH TYR A 9 3995 3862 3778 -35 -279 158 O ATOM 71 N ILE A 10 -28.125 7.397 4.952 1.00 19.27 N ANISOU 71 N ILE A 10 2662 2395 2264 -51 -359 238 N ATOM 72 CA ILE A 10 -29.381 6.813 5.352 1.00 24.51 C ANISOU 72 CA ILE A 10 3289 3104 2919 -36 -368 220 C ATOM 73 C ILE A 10 -29.769 5.643 4.473 1.00 25.73 C ANISOU 73 C ILE A 10 3441 3288 3049 -63 -356 226 C ATOM 74 O ILE A 10 -30.230 4.649 4.953 1.00 27.30 O ANISOU 74 O ILE A 10 3610 3520 3241 -73 -342 211 O ATOM 75 CB ILE A 10 -30.519 7.851 5.424 1.00 25.76 C ANISOU 75 CB ILE A 10 3440 3270 3080 7 -409 211 C ATOM 76 CG1 ILE A 10 -30.292 8.819 6.574 1.00 29.79 C ANISOU 76 CG1 ILE A 10 3940 3760 3616 36 -419 196 C ATOM 77 CG2 ILE A 10 -31.858 7.188 5.595 1.00 22.28 C ANISOU 77 CG2 ILE A 10 2960 2881 2622 18 -418 190 C ATOM 78 CD1 ILE A 10 -31.343 9.881 6.721 1.00 31.21 C ANISOU 78 CD1 ILE A 10 4112 3944 3801 83 -461 183 C ATOM 79 N THR A 11 -29.587 5.789 3.176 1.00 27.47 N ANISOU 79 N THR A 11 3692 3493 3253 -77 -361 247 N ATOM 80 CA THR A 11 -29.921 4.713 2.248 1.00 23.50 C ANISOU 80 CA THR A 11 3187 3017 2725 -103 -351 251 C ATOM 81 C THR A 11 -29.063 3.479 2.505 1.00 21.25 C ANISOU 81 C THR A 11 2897 2736 2443 -140 -312 248 C ATOM 82 O THR A 11 -29.567 2.349 2.489 1.00 20.74 O ANISOU 82 O THR A 11 2811 2702 2366 -156 -299 238 O ATOM 83 CB THR A 11 -29.759 5.195 0.805 1.00 23.43 C ANISOU 83 CB THR A 11 3216 2989 2698 -112 -364 275 C ATOM 84 OG1 THR A 11 -30.575 6.356 0.594 1.00 24.99 O ANISOU 84 OG1 THR A 11 3422 3181 2893 -73 -403 279 O ATOM 85 CG2 THR A 11 -30.187 4.112 -0.172 1.00 25.22 C ANISOU 85 CG2 THR A 11 3437 3248 2899 -137 -355 277 C ATOM 86 N VAL A 12 -27.767 3.677 2.753 1.00 23.16 N ANISOU 86 N VAL A 12 3156 2944 2698 -153 -293 254 N ATOM 87 CA VAL A 12 -26.884 2.556 3.055 1.00 23.69 C ANISOU 87 CA VAL A 12 3218 3013 2769 -182 -260 249 C ATOM 88 C VAL A 12 -27.295 1.889 4.362 1.00 24.37 C ANISOU 88 C VAL A 12 3271 3123 2866 -173 -250 229 C ATOM 89 O VAL A 12 -27.278 0.657 4.477 1.00 24.01 O ANISOU 89 O VAL A 12 3215 3095 2814 -194 -230 223 O ATOM 90 CB VAL A 12 -25.418 3.027 3.092 1.00 27.72 C ANISOU 90 CB VAL A 12 3752 3487 3294 -194 -244 256 C ATOM 91 CG1 VAL A 12 -24.507 1.915 3.600 1.00 25.30 C ANISOU 91 CG1 VAL A 12 3436 3183 2993 -215 -213 245 C ATOM 92 CG2 VAL A 12 -24.973 3.491 1.709 1.00 24.55 C ANISOU 92 CG2 VAL A 12 3385 3067 2877 -212 -248 276 C ATOM 93 N GLU A 13 -27.677 2.687 5.363 1.00 21.53 N ANISOU 93 N GLU A 13 2896 2764 2521 -142 -266 219 N ATOM 94 CA GLU A 13 -28.105 2.122 6.640 1.00 18.61 C ANISOU 94 CA GLU A 13 2494 2420 2157 -135 -257 201 C ATOM 95 C GLU A 13 -29.340 1.245 6.472 1.00 18.42 C ANISOU 95 C GLU A 13 2447 2436 2114 -142 -259 192 C ATOM 96 O GLU A 13 -29.410 0.145 7.033 1.00 20.20 O ANISOU 96 O GLU A 13 2658 2681 2337 -159 -239 184 O ATOM 97 CB GLU A 13 -28.375 3.243 7.646 1.00 21.41 C ANISOU 97 CB GLU A 13 2834 2772 2530 -99 -276 189 C ATOM 98 CG GLU A 13 -27.120 3.907 8.199 1.00 22.80 C ANISOU 98 CG GLU A 13 3023 2912 2727 -94 -268 190 C ATOM 99 CD GLU A 13 -26.526 3.156 9.381 1.00 27.40 C ANISOU 99 CD GLU A 13 3589 3504 3319 -101 -244 179 C ATOM 100 OE1 GLU A 13 -26.449 3.742 10.481 1.00 29.44 O ANISOU 100 OE1 GLU A 13 3831 3763 3593 -78 -248 165 O ATOM 101 OE2 GLU A 13 -26.145 1.978 9.214 1.00 29.58 O ANISOU 101 OE2 GLU A 13 3868 3786 3585 -127 -221 182 O ATOM 102 N LEU A 14 -30.300 1.706 5.689 1.00 19.18 N ANISOU 102 N LEU A 14 2542 2547 2198 -130 -284 193 N ATOM 103 CA LEU A 14 -31.515 0.941 5.450 1.00 24.94 C ANISOU 103 CA LEU A 14 3249 3319 2908 -137 -287 181 C ATOM 104 C LEU A 14 -31.232 -0.344 4.694 1.00 25.63 C ANISOU 104 C LEU A 14 3345 3411 2982 -176 -263 188 C ATOM 105 O LEU A 14 -31.771 -1.362 5.001 1.00 27.49 O ANISOU 105 O LEU A 14 3561 3673 3209 -193 -249 176 O ATOM 106 CB LEU A 14 -32.569 1.769 4.752 1.00 21.88 C ANISOU 106 CB LEU A 14 2857 2946 2509 -112 -321 178 C ATOM 107 CG LEU A 14 -33.011 2.950 5.591 1.00 27.80 C ANISOU 107 CG LEU A 14 3593 3696 3274 -71 -347 166 C ATOM 108 CD1 LEU A 14 -33.798 3.945 4.790 1.00 30.13 C ANISOU 108 CD1 LEU A 14 3895 3993 3560 -40 -385 167 C ATOM 109 CD2 LEU A 14 -33.752 2.524 6.829 1.00 27.64 C ANISOU 109 CD2 LEU A 14 3531 3714 3255 -65 -341 140 C ATOM 110 N ALA A 15 -30.343 -0.280 3.721 1.00 26.55 N ANISOU 110 N ALA A 15 3492 3499 3096 -191 -257 205 N ATOM 111 CA ALA A 15 -29.947 -1.480 2.994 1.00 26.21 C ANISOU 111 CA ALA A 15 3458 3458 3041 -227 -234 209 C ATOM 112 C ALA A 15 -29.258 -2.483 3.911 1.00 25.32 C ANISOU 112 C ALA A 15 3341 3339 2939 -244 -205 203 C ATOM 113 O ALA A 15 -29.427 -3.696 3.747 1.00 26.27 O ANISOU 113 O ALA A 15 3457 3474 3052 -269 -188 197 O ATOM 114 CB ALA A 15 -29.032 -1.109 1.828 1.00 18.56 C ANISOU 114 CB ALA A 15 2522 2462 2067 -238 -233 227 C ATOM 115 N ILE A 16 -28.468 -2.013 4.866 1.00 24.79 N ANISOU 115 N ILE A 16 3276 3251 2891 -230 -201 203 N ATOM 116 CA ILE A 16 -27.821 -2.889 5.821 1.00 24.79 C ANISOU 116 CA ILE A 16 3273 3246 2901 -241 -177 197 C ATOM 117 C ILE A 16 -28.862 -3.509 6.754 1.00 22.82 C ANISOU 117 C ILE A 16 2996 3029 2647 -241 -175 184 C ATOM 118 O ILE A 16 -28.831 -4.681 7.022 1.00 21.14 O ANISOU 118 O ILE A 16 2781 2821 2428 -262 -155 181 O ATOM 119 CB ILE A 16 -26.722 -2.158 6.609 1.00 25.17 C ANISOU 119 CB ILE A 16 3328 3266 2968 -225 -174 198 C ATOM 120 CG1 ILE A 16 -25.557 -1.853 5.678 1.00 22.34 C ANISOU 120 CG1 ILE A 16 2997 2878 2612 -236 -168 209 C ATOM 121 CG2 ILE A 16 -26.254 -2.980 7.793 1.00 23.48 C ANISOU 121 CG2 ILE A 16 3105 3053 2762 -228 -155 191 C ATOM 122 CD1 ILE A 16 -24.586 -0.867 6.232 1.00 19.68 C ANISOU 122 CD1 ILE A 16 2667 2515 2294 -220 -170 209 C ATOM 123 N ALA A 17 -29.821 -2.706 7.167 1.00 22.86 N ANISOU 123 N ALA A 17 2980 3055 2650 -217 -195 176 N ATOM 124 CA ALA A 17 -30.853 -3.169 8.065 1.00 23.47 C ANISOU 124 CA ALA A 17 3028 3167 2721 -217 -193 160 C ATOM 125 C ALA A 17 -31.674 -4.297 7.450 1.00 24.17 C ANISOU 125 C ALA A 17 3110 3282 2790 -247 -184 155 C ATOM 126 O ALA A 17 -31.954 -5.271 8.101 1.00 27.33 O ANISOU 126 O ALA A 17 3501 3697 3185 -266 -166 149 O ATOM 127 CB ALA A 17 -31.744 -2.029 8.485 1.00 14.43 C ANISOU 127 CB ALA A 17 1861 2044 1579 -184 -220 148 C ATOM 128 N VAL A 18 -32.011 -4.161 6.177 1.00 29.98 N ANISOU 128 N VAL A 18 3853 4022 3515 -251 -195 159 N ATOM 129 CA VAL A 18 -32.770 -5.176 5.488 1.00 29.73 C ANISOU 129 CA VAL A 18 3815 4016 3465 -279 -187 152 C ATOM 130 C VAL A 18 -32.016 -6.495 5.431 1.00 24.21 C ANISOU 130 C VAL A 18 3133 3298 2767 -313 -158 157 C ATOM 131 O VAL A 18 -32.563 -7.521 5.720 1.00 22.68 O ANISOU 131 O VAL A 18 2929 3123 2565 -337 -144 148 O ATOM 132 CB VAL A 18 -33.067 -4.749 4.033 1.00 29.34 C ANISOU 132 CB VAL A 18 3774 3970 3403 -277 -205 156 C ATOM 133 CG1 VAL A 18 -33.624 -5.907 3.250 1.00 28.64 C ANISOU 133 CG1 VAL A 18 3681 3904 3298 -309 -193 148 C ATOM 134 CG2 VAL A 18 -34.037 -3.596 3.990 1.00 31.92 C ANISOU 134 CG2 VAL A 18 4083 4320 3726 -243 -236 148 C ATOM 135 N LEU A 19 -30.748 -6.426 5.072 1.00 24.08 N ANISOU 135 N LEU A 19 3143 3245 2761 -314 -151 171 N ATOM 136 CA LEU A 19 -29.901 -7.593 4.969 1.00 24.82 C ANISOU 136 CA LEU A 19 3255 3319 2858 -340 -127 174 C ATOM 137 C LEU A 19 -29.667 -8.279 6.309 1.00 29.28 C ANISOU 137 C LEU A 19 3817 3878 3430 -344 -111 171 C ATOM 138 O LEU A 19 -29.629 -9.476 6.381 1.00 26.00 O ANISOU 138 O LEU A 19 3409 3460 3011 -369 -94 169 O ATOM 139 CB LEU A 19 -28.588 -7.264 4.287 1.00 24.91 C ANISOU 139 CB LEU A 19 3291 3297 2877 -339 -125 185 C ATOM 140 CG LEU A 19 -28.700 -6.842 2.835 1.00 27.30 C ANISOU 140 CG LEU A 19 3602 3602 3168 -343 -137 190 C ATOM 141 CD1 LEU A 19 -27.440 -6.183 2.331 1.00 25.47 C ANISOU 141 CD1 LEU A 19 3393 3340 2943 -339 -137 201 C ATOM 142 CD2 LEU A 19 -29.103 -8.009 1.965 1.00 28.85 C ANISOU 142 CD2 LEU A 19 3798 3813 3350 -374 -126 183 C ATOM 143 N ALA A 20 -29.488 -7.479 7.347 1.00 23.42 N ANISOU 143 N ALA A 20 3066 3133 2698 -319 -118 172 N ATOM 144 CA ALA A 20 -29.268 -7.981 8.679 1.00 22.82 C ANISOU 144 CA ALA A 20 2988 3056 2628 -318 -105 170 C ATOM 145 C ALA A 20 -30.486 -8.738 9.166 1.00 24.95 C ANISOU 145 C ALA A 20 3239 3359 2883 -338 -98 161 C ATOM 146 O ALA A 20 -30.359 -9.777 9.749 1.00 25.23 O ANISOU 146 O ALA A 20 3282 3388 2915 -357 -80 162 O ATOM 147 CB ALA A 20 -28.947 -6.846 9.624 1.00 26.15 C ANISOU 147 CB ALA A 20 3399 3473 3062 -286 -116 169 C ATOM 148 N ILE A 21 -31.659 -8.184 8.941 1.00 21.28 N ANISOU 148 N ILE A 21 2749 2928 2408 -332 -113 150 N ATOM 149 CA ILE A 21 -32.861 -8.852 9.343 1.00 23.94 C ANISOU 149 CA ILE A 21 3065 3302 2730 -353 -106 137 C ATOM 150 C ILE A 21 -33.115 -10.140 8.596 1.00 26.51 C ANISOU 150 C ILE A 21 3402 3627 3044 -392 -90 136 C ATOM 151 O ILE A 21 -33.314 -11.149 9.188 1.00 28.00 O ANISOU 151 O ILE A 21 3594 3819 3227 -417 -71 135 O ATOM 152 CB ILE A 21 -34.079 -7.947 9.191 1.00 24.95 C ANISOU 152 CB ILE A 21 3161 3470 2849 -336 -128 121 C ATOM 153 CG1 ILE A 21 -34.043 -6.842 10.224 1.00 20.93 C ANISOU 153 CG1 ILE A 21 2636 2968 2350 -301 -142 117 C ATOM 154 CG2 ILE A 21 -35.353 -8.738 9.362 1.00 27.83 C ANISOU 154 CG2 ILE A 21 3502 3878 3194 -364 -119 103 C ATOM 155 CD1 ILE A 21 -34.913 -5.673 9.888 1.00 23.41 C ANISOU 155 CD1 ILE A 21 2926 3308 2661 -272 -171 103 C ATOM 156 N LEU A 22 -32.974 -10.117 7.289 1.00 28.47 N ANISOU 156 N LEU A 22 3659 3868 3290 -396 -96 138 N ATOM 157 CA LEU A 22 -33.258 -11.279 6.495 1.00 26.94 C ANISOU 157 CA LEU A 22 3472 3676 3086 -432 -82 133 C ATOM 158 C LEU A 22 -32.325 -12.411 6.765 1.00 27.01 C ANISOU 158 C LEU A 22 3510 3650 3103 -452 -60 142 C ATOM 159 O LEU A 22 -32.745 -13.525 6.943 1.00 28.72 O ANISOU 159 O LEU A 22 3730 3870 3312 -483 -44 137 O ATOM 160 CB LEU A 22 -33.202 -10.950 5.011 1.00 27.10 C ANISOU 160 CB LEU A 22 3499 3697 3103 -430 -94 133 C ATOM 161 CG LEU A 22 -34.330 -10.090 4.476 1.00 30.66 C ANISOU 161 CG LEU A 22 3922 4186 3540 -415 -116 122 C ATOM 162 CD1 LEU A 22 -34.100 -9.716 3.029 1.00 28.97 C ANISOU 162 CD1 LEU A 22 3720 3967 3321 -410 -129 127 C ATOM 163 CD2 LEU A 22 -35.672 -10.739 4.709 1.00 35.95 C ANISOU 163 CD2 LEU A 22 4565 4899 4194 -438 -110 101 C ATOM 164 N GLY A 23 -31.054 -12.092 6.834 1.00 21.81 N ANISOU 164 N GLY A 23 2872 2955 2458 -433 -61 154 N ATOM 165 CA GLY A 23 -30.051 -13.131 6.987 1.00 20.11 C ANISOU 165 CA GLY A 23 2685 2705 2252 -447 -44 161 C ATOM 166 C GLY A 23 -30.129 -13.827 8.331 1.00 25.55 C ANISOU 166 C GLY A 23 3378 3389 2940 -455 -30 164 C ATOM 167 O GLY A 23 -30.016 -15.053 8.414 1.00 24.55 O ANISOU 167 O GLY A 23 3271 3247 2811 -480 -15 165 O ATOM 168 N ASN A 24 -30.331 -13.060 9.400 1.00 26.67 N ANISOU 168 N ASN A 24 3505 3546 3082 -434 -37 165 N ATOM 169 CA ASN A 24 -30.319 -13.649 10.731 1.00 28.15 C ANISOU 169 CA ASN A 24 3698 3730 3267 -439 -25 170 C ATOM 170 C ASN A 24 -31.661 -14.266 11.100 1.00 25.32 C ANISOU 170 C ASN A 24 3324 3406 2891 -471 -15 162 C ATOM 171 O ASN A 24 -31.705 -15.202 11.907 1.00 27.89 O ANISOU 171 O ASN A 24 3664 3723 3209 -491 0 168 O ATOM 172 CB ASN A 24 -29.888 -12.597 11.748 1.00 24.49 C ANISOU 172 CB ASN A 24 3224 3269 2812 -404 -35 174 C ATOM 173 CG ASN A 24 -28.445 -12.182 11.554 1.00 23.29 C ANISOU 173 CG ASN A 24 3090 3082 2677 -379 -39 180 C ATOM 174 OD1 ASN A 24 -27.526 -12.894 11.959 1.00 28.00 O ANISOU 174 OD1 ASN A 24 3710 3650 3279 -379 -29 187 O ATOM 175 ND2 ASN A 24 -28.237 -11.040 10.910 1.00 22.12 N ANISOU 175 ND2 ASN A 24 2932 2935 2537 -358 -54 178 N ATOM 176 N VAL A 25 -32.757 -13.769 10.524 1.00 27.96 N ANISOU 176 N VAL A 25 3630 3777 3215 -475 -25 148 N ATOM 177 CA VAL A 25 -34.028 -14.477 10.636 1.00 30.17 C ANISOU 177 CA VAL A 25 3894 4091 3477 -511 -14 136 C ATOM 178 C VAL A 25 -33.905 -15.867 10.023 1.00 29.55 C ANISOU 178 C VAL A 25 3843 3990 3396 -549 4 138 C ATOM 179 O VAL A 25 -34.439 -16.848 10.553 1.00 33.09 O ANISOU 179 O VAL A 25 4296 4443 3832 -584 22 137 O ATOM 180 CB VAL A 25 -35.154 -13.653 9.982 1.00 27.18 C ANISOU 180 CB VAL A 25 3480 3759 3090 -504 -30 116 C ATOM 181 CG1 VAL A 25 -36.308 -14.540 9.554 1.00 29.78 C ANISOU 181 CG1 VAL A 25 3795 4119 3401 -546 -18 100 C ATOM 182 CG2 VAL A 25 -35.640 -12.579 10.943 1.00 24.06 C ANISOU 182 CG2 VAL A 25 3055 3396 2692 -477 -43 109 C ATOM 183 N LEU A 26 -33.166 -15.976 8.918 1.00 30.10 N ANISOU 183 N LEU A 26 3929 4032 3476 -544 0 141 N ATOM 184 CA LEU A 26 -32.925 -17.275 8.301 1.00 31.18 C ANISOU 184 CA LEU A 26 4091 4142 3613 -577 15 140 C ATOM 185 C LEU A 26 -32.093 -18.179 9.208 1.00 30.29 C ANISOU 185 C LEU A 26 4013 3989 3506 -583 29 155 C ATOM 186 O LEU A 26 -32.311 -19.395 9.247 1.00 33.01 O ANISOU 186 O LEU A 26 4377 4319 3846 -617 45 155 O ATOM 187 CB LEU A 26 -32.237 -17.082 6.950 1.00 35.22 C ANISOU 187 CB LEU A 26 4611 4637 4134 -566 6 138 C ATOM 188 CG LEU A 26 -31.985 -18.324 6.101 1.00 44.72 C ANISOU 188 CG LEU A 26 5837 5817 5339 -597 19 133 C ATOM 189 CD1 LEU A 26 -33.300 -18.935 5.645 1.00 45.16 C ANISOU 189 CD1 LEU A 26 5875 5905 5379 -635 27 116 C ATOM 190 CD2 LEU A 26 -31.105 -17.977 4.913 1.00 46.41 C ANISOU 190 CD2 LEU A 26 6057 6015 5561 -581 10 132 C ATOM 191 N VAL A 27 -31.133 -17.606 9.938 1.00 26.38 N ANISOU 191 N VAL A 27 3526 3474 3022 -549 22 168 N ATOM 192 CA VAL A 27 -30.349 -18.393 10.889 1.00 27.96 C ANISOU 192 CA VAL A 27 3759 3639 3227 -548 32 182 C ATOM 193 C VAL A 27 -31.252 -18.962 11.977 1.00 28.19 C ANISOU 193 C VAL A 27 3787 3685 3238 -575 45 185 C ATOM 194 O VAL A 27 -31.192 -20.154 12.300 1.00 27.99 O ANISOU 194 O VAL A 27 3792 3635 3209 -602 60 193 O ATOM 195 CB VAL A 27 -29.216 -17.540 11.492 1.00 28.28 C ANISOU 195 CB VAL A 27 3802 3663 3279 -505 21 190 C ATOM 196 CG1 VAL A 27 -28.600 -18.246 12.691 1.00 26.80 C ANISOU 196 CG1 VAL A 27 3643 3449 3092 -501 29 204 C ATOM 197 CG2 VAL A 27 -28.152 -17.245 10.447 1.00 30.19 C ANISOU 197 CG2 VAL A 27 4053 3882 3537 -486 13 187 C ATOM 198 N CYS A 28 -32.103 -18.110 12.560 1.00 25.16 N ANISOU 198 N CYS A 28 3370 3345 2844 -569 41 180 N ATOM 199 CA CYS A 28 -32.999 -18.557 13.623 1.00 29.58 C ANISOU 199 CA CYS A 28 3925 3930 3386 -597 54 181 C ATOM 200 C CYS A 28 -33.990 -19.594 13.111 1.00 32.73 C ANISOU 200 C CYS A 28 4325 4339 3770 -648 70 171 C ATOM 201 O CYS A 28 -34.318 -20.553 13.819 1.00 31.86 O ANISOU 201 O CYS A 28 4235 4222 3648 -682 88 179 O ATOM 202 CB CYS A 28 -33.741 -17.362 14.223 1.00 32.27 C ANISOU 202 CB CYS A 28 4222 4320 3718 -578 44 170 C ATOM 203 SG CYS A 28 -32.683 -16.121 15.004 1.00 31.98 S ANISOU 203 SG CYS A 28 4180 4274 3696 -521 27 179 S ATOM 204 N ATRP A 29 -34.465 -19.422 11.876 0.54 37.98 N ANISOU 204 N ATRP A 29 4972 5021 4438 -656 65 154 N ATOM 205 N BTRP A 29 -34.493 -19.414 11.887 0.46 37.98 N ANISOU 205 N BTRP A 29 4971 5022 4438 -656 65 154 N ATOM 206 CA ATRP A 29 -35.411 -20.364 11.288 0.54 39.70 C ANISOU 206 CA ATRP A 29 5188 5253 4644 -704 79 140 C ATOM 207 CA BTRP A 29 -35.416 -20.397 11.326 0.46 39.71 C ANISOU 207 CA BTRP A 29 5190 5253 4645 -705 80 141 C ATOM 208 C ATRP A 29 -34.754 -21.705 10.984 0.54 38.14 C ANISOU 208 C ATRP A 29 5036 5001 4453 -728 93 150 C ATOM 209 C BTRP A 29 -34.724 -21.732 11.089 0.46 38.17 C ANISOU 209 C BTRP A 29 5042 5004 4457 -728 93 152 C ATOM 210 O ATRP A 29 -35.418 -22.746 11.038 0.54 38.45 O ANISOU 210 O ATRP A 29 5087 5040 4482 -775 111 146 O ATOM 211 O BTRP A 29 -35.328 -22.793 11.284 0.46 37.85 O ANISOU 211 O BTRP A 29 5016 4960 4406 -774 112 150 O ATOM 212 CB ATRP A 29 -36.015 -19.746 10.024 0.54 43.59 C ANISOU 212 CB ATRP A 29 5648 5778 5136 -699 67 119 C ATOM 213 CB BTRP A 29 -36.028 -19.876 10.025 0.46 43.57 C ANISOU 213 CB BTRP A 29 5648 5774 5133 -703 69 119 C ATOM 214 CG ATRP A 29 -37.216 -20.451 9.462 0.54 48.82 C ANISOU 214 CG ATRP A 29 6294 6472 5783 -746 79 97 C ATOM 215 CG BTRP A 29 -37.244 -19.023 10.224 0.46 47.82 C ANISOU 215 CG BTRP A 29 6140 6375 5657 -701 61 99 C ATOM 216 CD1ATRP A 29 -37.368 -20.910 8.188 0.54 51.09 C ANISOU 216 CD1ATRP A 29 6582 6757 6073 -763 80 83 C ATOM 217 CD1BTRP A 29 -37.308 -17.664 10.160 0.46 49.94 C ANISOU 217 CD1BTRP A 29 6378 6669 5928 -659 39 94 C ATOM 218 CD2ATRP A 29 -38.436 -20.761 10.148 0.54 53.81 C ANISOU 218 CD2ATRP A 29 6905 7146 6394 -782 94 83 C ATOM 219 CD2BTRP A 29 -38.572 -19.473 10.520 0.46 52.87 C ANISOU 219 CD2BTRP A 29 6755 7058 6274 -743 75 80 C ATOM 220 NE1ATRP A 29 -38.603 -21.489 8.035 0.54 52.12 N ANISOU 220 NE1ATRP A 29 6693 6925 6187 -807 94 62 N ATOM 221 NE1BTRP A 29 -38.592 -17.236 10.396 0.46 51.24 N ANISOU 221 NE1BTRP A 29 6502 6892 6076 -668 36 72 N ATOM 222 CE2ATRP A 29 -39.278 -21.412 9.224 0.54 54.67 C ANISOU 222 CE2ATRP A 29 7003 7276 6495 -821 103 61 C ATOM 223 CE2BTRP A 29 -39.388 -18.328 10.620 0.46 54.12 C ANISOU 223 CE2BTRP A 29 6867 7271 6424 -720 59 61 C ATOM 224 CE3ATRP A 29 -38.898 -20.555 11.451 0.54 55.42 C ANISOU 224 CE3ATRP A 29 7097 7375 6584 -788 100 86 C ATOM 225 CE3BTRP A 29 -39.150 -20.732 10.709 0.46 55.40 C ANISOU 225 CE3BTRP A 29 7089 7378 6582 -798 100 75 C ATOM 226 CZ2ATRP A 29 -40.554 -21.861 9.563 0.54 56.00 C ANISOU 226 CZ2ATRP A 29 7147 7488 6641 -866 119 40 C ATOM 227 CZ2BTRP A 29 -40.750 -18.404 10.901 0.46 55.74 C ANISOU 227 CZ2BTRP A 29 7036 7534 6607 -750 67 35 C ATOM 228 CZ3ATRP A 29 -40.164 -21.001 11.785 0.54 55.96 C ANISOU 228 CZ3ATRP A 29 7143 7489 6631 -834 117 67 C ATOM 229 CZ3BTRP A 29 -40.503 -20.805 10.988 0.46 55.94 C ANISOU 229 CZ3BTRP A 29 7123 7503 6628 -832 110 51 C ATOM 230 CH2ATRP A 29 -40.977 -21.646 10.845 0.54 55.59 C ANISOU 230 CH2ATRP A 29 7084 7461 6576 -873 126 43 C ATOM 231 CH2BTRP A 29 -41.288 -19.649 11.082 0.46 55.84 C ANISOU 231 CH2BTRP A 29 7061 7549 6607 -807 93 30 C ATOM 232 N ALA A 30 -33.455 -21.704 10.674 1.00 34.88 N ANISOU 232 N ALA A 30 4649 4544 4059 -698 84 162 N ATOM 233 CA ALA A 30 -32.748 -22.952 10.406 1.00 36.32 C ANISOU 233 CA ALA A 30 4875 4674 4251 -715 93 169 C ATOM 234 C ALA A 30 -32.518 -23.746 11.687 1.00 40.75 C ANISOU 234 C ALA A 30 5471 5206 4805 -727 105 188 C ATOM 235 O ALA A 30 -32.671 -24.973 11.699 1.00 38.81 O ANISOU 235 O ALA A 30 5256 4932 4556 -763 119 191 O ATOM 236 CB ALA A 30 -31.420 -22.664 9.707 1.00 30.30 C ANISOU 236 CB ALA A 30 4126 3879 3509 -677 80 171 C ATOM 237 N VAL A 31 -32.148 -23.064 12.773 1.00 38.03 N ANISOU 237 N VAL A 31 5123 4868 4458 -697 99 202 N ATOM 238 CA VAL A 31 -31.937 -23.748 14.044 1.00 35.06 C ANISOU 238 CA VAL A 31 4780 4468 4072 -706 108 223 C ATOM 239 C VAL A 31 -33.258 -24.272 14.595 1.00 37.26 C ANISOU 239 C VAL A 31 5052 4777 4327 -757 127 221 C ATOM 240 O VAL A 31 -33.319 -25.369 15.163 1.00 36.49 O ANISOU 240 O VAL A 31 4993 4651 4220 -789 142 235 O ATOM 241 CB VAL A 31 -31.234 -22.810 15.043 1.00 32.75 C ANISOU 241 CB VAL A 31 4480 4181 3782 -660 96 235 C ATOM 242 CG1 VAL A 31 -31.031 -23.505 16.381 1.00 31.29 C ANISOU 242 CG1 VAL A 31 4330 3976 3584 -668 105 257 C ATOM 243 CG2 VAL A 31 -29.902 -22.335 14.476 1.00 31.86 C ANISOU 243 CG2 VAL A 31 4374 4040 3693 -614 80 234 C ATOM 244 N TRP A 32 -34.337 -23.504 14.426 1.00 37.20 N ANISOU 244 N TRP A 32 4996 4828 4309 -767 127 202 N ATOM 245 CA TRP A 32 -35.640 -23.936 14.923 1.00 39.69 C ANISOU 245 CA TRP A 32 5299 5181 4600 -818 146 195 C ATOM 246 C TRP A 32 -36.117 -25.197 14.211 1.00 43.43 C ANISOU 246 C TRP A 32 5795 5634 5071 -870 163 187 C ATOM 247 O TRP A 32 -36.725 -26.076 14.833 1.00 43.17 O ANISOU 247 O TRP A 32 5782 5600 5020 -918 184 193 O ATOM 248 CB TRP A 32 -36.659 -22.806 14.758 1.00 44.07 C ANISOU 248 CB TRP A 32 5795 5805 5146 -812 139 170 C ATOM 249 CG TRP A 32 -38.068 -23.173 15.148 1.00 55.37 C ANISOU 249 CG TRP A 32 7203 7284 6550 -864 158 155 C ATOM 250 CD1 TRP A 32 -38.973 -23.874 14.401 1.00 56.21 C ANISOU 250 CD1 TRP A 32 7302 7406 6649 -912 172 135 C ATOM 251 CD2 TRP A 32 -38.737 -22.835 16.371 1.00 61.43 C ANISOU 251 CD2 TRP A 32 7949 8095 7296 -875 165 154 C ATOM 252 NE1 TRP A 32 -40.155 -24.005 15.088 1.00 58.96 N ANISOU 252 NE1 TRP A 32 7626 7805 6971 -954 188 121 N ATOM 253 CE2 TRP A 32 -40.037 -23.374 16.298 1.00 62.59 C ANISOU 253 CE2 TRP A 32 8077 8284 7421 -932 185 133 C ATOM 254 CE3 TRP A 32 -38.360 -22.135 17.521 1.00 60.85 C ANISOU 254 CE3 TRP A 32 7870 8032 7218 -843 158 167 C ATOM 255 CZ2 TRP A 32 -40.962 -23.234 17.332 1.00 64.07 C ANISOU 255 CZ2 TRP A 32 8239 8524 7582 -960 198 124 C ATOM 256 CZ3 TRP A 32 -39.280 -21.996 18.545 1.00 61.29 C ANISOU 256 CZ3 TRP A 32 7901 8139 7247 -869 170 159 C ATOM 257 CH2 TRP A 32 -40.565 -22.542 18.443 1.00 63.10 C ANISOU 257 CH2 TRP A 32 8111 8410 7454 -927 190 137 C ATOM 258 N LEU A 33 -35.845 -25.309 12.911 1.00 48.32 N ANISOU 258 N LEU A 33 6413 6238 5706 -864 156 174 N ATOM 259 CA LEU A 33 -36.396 -26.398 12.112 1.00 52.79 C ANISOU 259 CA LEU A 33 6992 6793 6271 -914 171 160 C ATOM 260 C LEU A 33 -35.524 -27.646 12.098 1.00 52.66 C ANISOU 260 C LEU A 33 7036 6706 6268 -924 177 177 C ATOM 261 O LEU A 33 -36.056 -28.757 11.990 1.00 54.51 O ANISOU 261 O LEU A 33 7293 6923 6495 -975 196 173 O ATOM 262 CB LEU A 33 -36.623 -25.931 10.671 1.00 53.87 C ANISOU 262 CB LEU A 33 7096 6954 6417 -904 160 135 C ATOM 263 CG LEU A 33 -37.745 -24.918 10.433 1.00 60.78 C ANISOU 263 CG LEU A 33 7913 7902 7279 -903 155 111 C ATOM 264 CD1 LEU A 33 -37.817 -24.556 8.958 1.00 64.38 C ANISOU 264 CD1 LEU A 33 8345 8373 7744 -891 142 90 C ATOM 265 CD2 LEU A 33 -39.082 -25.459 10.921 1.00 63.85 C ANISOU 265 CD2 LEU A 33 8286 8330 7644 -959 176 97 C ATOM 266 N ASN A 34 -34.204 -27.502 12.195 1.00 46.64 N ANISOU 266 N ASN A 34 6299 5900 5522 -878 162 193 N ATOM 267 CA ASN A 34 -33.282 -28.627 12.071 1.00 45.03 C ANISOU 267 CA ASN A 34 6150 5628 5332 -879 163 205 C ATOM 268 C ASN A 34 -32.809 -29.046 13.460 1.00 46.81 C ANISOU 268 C ASN A 34 6416 5820 5548 -873 166 235 C ATOM 269 O ASN A 34 -32.100 -28.293 14.135 1.00 40.52 O ANISOU 269 O ASN A 34 5615 5025 4754 -828 153 248 O ATOM 270 CB ASN A 34 -32.098 -28.260 11.178 1.00 45.68 C ANISOU 270 CB ASN A 34 6233 5686 5439 -831 144 198 C ATOM 271 CG ASN A 34 -31.289 -29.473 10.752 1.00 46.83 C ANISOU 271 CG ASN A 34 6426 5767 5599 -836 144 199 C ATOM 272 OD1 ASN A 34 -31.444 -30.564 11.301 1.00 47.64 O ANISOU 272 OD1 ASN A 34 6571 5834 5697 -867 156 211 O ATOM 273 ND2 ASN A 34 -30.414 -29.284 9.772 1.00 47.47 N ANISOU 273 ND2 ASN A 34 6503 5834 5700 -805 130 186 N ATOM 274 N SER A 35 -33.188 -30.258 13.876 1.00 47.74 N ANISOU 274 N SER A 35 6573 5908 5658 -914 182 243 N ATOM 275 CA SER A 35 -32.736 -30.774 15.164 1.00 49.25 C ANISOU 275 CA SER A 35 6805 6066 5841 -902 181 270 C ATOM 276 C SER A 35 -31.240 -31.061 15.175 1.00 49.28 C ANISOU 276 C SER A 35 6853 6008 5863 -859 165 286 C ATOM 277 O SER A 35 -30.629 -31.049 16.250 1.00 49.39 O ANISOU 277 O SER A 35 6893 6002 5869 -834 158 309 O ATOM 278 CB SER A 35 -33.517 -32.037 15.536 1.00 53.44 C ANISOU 278 CB SER A 35 7362 6580 6362 -943 197 269 C ATOM 279 OG SER A 35 -33.262 -33.093 14.626 1.00 55.99 O ANISOU 279 OG SER A 35 7714 6857 6704 -954 197 257 O ATOM 280 N ASN A 36 -30.636 -31.312 14.009 1.00 46.65 N ANISOU 280 N ASN A 36 6527 5647 5551 -850 157 271 N ATOM 281 CA ASN A 36 -29.187 -31.466 13.938 1.00 47.56 C ANISOU 281 CA ASN A 36 6671 5713 5686 -799 137 275 C ATOM 282 C ASN A 36 -28.456 -30.158 14.204 1.00 48.41 C ANISOU 282 C ASN A 36 6745 5849 5799 -742 121 276 C ATOM 283 O ASN A 36 -27.249 -30.179 14.468 1.00 49.69 O ANISOU 283 O ASN A 36 6930 5979 5973 -697 105 282 O ATOM 284 CB ASN A 36 -28.778 -32.020 12.572 1.00 54.05 C ANISOU 284 CB ASN A 36 7499 6508 6531 -799 132 251 C ATOM 285 CG ASN A 36 -29.360 -33.392 12.300 1.00 59.43 C ANISOU 285 CG ASN A 36 8217 7154 7212 -849 147 248 C ATOM 286 OD1 ASN A 36 -29.570 -34.184 13.219 1.00 60.27 O ANISOU 286 OD1 ASN A 36 8356 7236 7309 -859 152 264 O ATOM 287 ND2 ASN A 36 -29.627 -33.680 11.032 1.00 61.31 N ANISOU 287 ND2 ASN A 36 8439 7394 7461 -870 150 221 N ATOM 288 N LEU A 37 -29.153 -29.025 14.135 1.00 41.37 N ANISOU 288 N LEU A 37 5801 5018 4899 -743 123 267 N ATOM 289 CA LEU A 37 -28.582 -27.732 14.486 1.00 40.75 C ANISOU 289 CA LEU A 37 5691 4968 4824 -694 109 268 C ATOM 290 C LEU A 37 -28.934 -27.300 15.903 1.00 40.31 C ANISOU 290 C LEU A 37 5630 4937 4748 -691 112 287 C ATOM 291 O LEU A 37 -28.553 -26.203 16.312 1.00 38.66 O ANISOU 291 O LEU A 37 5394 4754 4541 -652 102 287 O ATOM 292 CB LEU A 37 -29.044 -26.659 13.493 1.00 37.12 C ANISOU 292 CB LEU A 37 5177 4557 4370 -689 105 246 C ATOM 293 CG LEU A 37 -28.507 -26.750 12.062 1.00 36.43 C ANISOU 293 CG LEU A 37 5085 4455 4303 -680 97 225 C ATOM 294 CD1 LEU A 37 -29.150 -25.694 11.177 1.00 37.86 C ANISOU 294 CD1 LEU A 37 5214 4687 4483 -681 94 207 C ATOM 295 CD2 LEU A 37 -26.991 -26.610 12.048 1.00 33.56 C ANISOU 295 CD2 LEU A 37 4738 4056 3956 -631 81 226 C ATOM 296 N GLN A 38 -29.648 -28.133 16.660 1.00 42.65 N ANISOU 296 N GLN A 38 5955 5227 5025 -733 128 303 N ATOM 297 CA GLN A 38 -30.103 -27.772 18.001 1.00 41.33 C ANISOU 297 CA GLN A 38 5781 5088 4833 -737 134 320 C ATOM 298 C GLN A 38 -29.107 -28.323 19.017 1.00 44.74 C ANISOU 298 C GLN A 38 6263 5474 5261 -711 127 346 C ATOM 299 O GLN A 38 -29.265 -29.411 19.566 1.00 48.19 O ANISOU 299 O GLN A 38 6748 5877 5685 -740 137 366 O ATOM 300 CB GLN A 38 -31.515 -28.286 18.245 1.00 42.65 C ANISOU 300 CB GLN A 38 5945 5283 4977 -802 158 321 C ATOM 301 CG GLN A 38 -32.559 -27.644 17.353 1.00 44.53 C ANISOU 301 CG GLN A 38 6129 5576 5216 -824 163 292 C ATOM 302 CD GLN A 38 -33.925 -28.282 17.505 1.00 49.38 C ANISOU 302 CD GLN A 38 6740 6216 5807 -892 187 287 C ATOM 303 OE1 GLN A 38 -34.069 -29.327 18.139 1.00 50.72 O ANISOU 303 OE1 GLN A 38 6945 6357 5970 -910 195 298 O ATOM 304 NE2 GLN A 38 -34.937 -27.656 16.918 1.00 51.83 N ANISOU 304 NE2 GLN A 38 6997 6582 6112 -910 191 261 N ATOM 305 N ASN A 39 -28.053 -27.546 19.253 1.00 45.74 N ANISOU 305 N ASN A 39 6379 5600 5400 -653 109 346 N ATOM 306 CA ASN A 39 -27.045 -27.858 20.254 1.00 44.20 C ANISOU 306 CA ASN A 39 6223 5371 5201 -617 98 367 C ATOM 307 C ASN A 39 -26.717 -26.578 21.010 1.00 45.12 C ANISOU 307 C ASN A 39 6301 5528 5313 -576 88 365 C ATOM 308 O ASN A 39 -27.183 -25.490 20.658 1.00 44.41 O ANISOU 308 O ASN A 39 6159 5486 5228 -572 88 348 O ATOM 309 CB ASN A 39 -25.787 -28.464 19.616 1.00 43.86 C ANISOU 309 CB ASN A 39 6213 5270 5181 -584 82 361 C ATOM 310 CG ASN A 39 -25.305 -27.675 18.413 1.00 48.81 C ANISOU 310 CG ASN A 39 6801 5911 5833 -558 72 333 C ATOM 311 OD1 ASN A 39 -24.733 -26.593 18.554 1.00 49.09 O ANISOU 311 OD1 ASN A 39 6805 5972 5877 -517 61 325 O ATOM 312 ND2 ASN A 39 -25.537 -28.213 17.220 1.00 47.78 N ANISOU 312 ND2 ASN A 39 6673 5764 5715 -582 77 317 N ATOM 313 N VAL A 40 -25.905 -26.714 22.061 1.00 42.92 N ANISOU 313 N VAL A 40 6050 5231 5027 -543 79 383 N ATOM 314 CA VAL A 40 -25.571 -25.561 22.896 1.00 41.04 C ANISOU 314 CA VAL A 40 5779 5031 4785 -504 70 381 C ATOM 315 C VAL A 40 -24.836 -24.504 22.084 1.00 40.51 C ANISOU 315 C VAL A 40 5672 4976 4745 -462 56 356 C ATOM 316 O VAL A 40 -25.086 -23.301 22.232 1.00 42.42 O ANISOU 316 O VAL A 40 5866 5262 4988 -448 54 344 O ATOM 317 CB VAL A 40 -24.744 -26.006 24.115 1.00 39.58 C ANISOU 317 CB VAL A 40 5633 4820 4585 -474 62 404 C ATOM 318 CG1 VAL A 40 -24.210 -24.790 24.848 1.00 37.77 C ANISOU 318 CG1 VAL A 40 5367 4628 4356 -427 51 396 C ATOM 319 CG2 VAL A 40 -25.588 -26.864 25.037 1.00 39.53 C ANISOU 319 CG2 VAL A 40 5662 4812 4547 -519 77 432 C ATOM 320 N THR A 41 -23.916 -24.935 21.218 1.00 35.24 N ANISOU 320 N THR A 41 5024 4267 4099 -443 47 346 N ATOM 321 CA THR A 41 -23.148 -23.987 20.418 1.00 33.57 C ANISOU 321 CA THR A 41 4780 4065 3912 -407 35 322 C ATOM 322 C THR A 41 -24.065 -23.097 19.590 1.00 37.50 C ANISOU 322 C THR A 41 5229 4604 4414 -429 41 307 C ATOM 323 O THR A 41 -23.870 -21.877 19.527 1.00 37.57 O ANISOU 323 O THR A 41 5199 4643 4431 -403 34 294 O ATOM 324 CB THR A 41 -22.175 -24.738 19.511 1.00 35.61 C ANISOU 324 CB THR A 41 5066 4276 4189 -392 26 311 C ATOM 325 OG1 THR A 41 -21.493 -25.747 20.267 1.00 40.17 O ANISOU 325 OG1 THR A 41 5694 4811 4760 -376 19 327 O ATOM 326 CG2 THR A 41 -21.154 -23.778 18.923 1.00 36.43 C ANISOU 326 CG2 THR A 41 5139 4388 4313 -351 14 288 C ATOM 327 N ASN A 42 -25.082 -23.685 18.964 1.00 33.24 N ANISOU 327 N ASN A 42 4693 4067 3869 -475 54 306 N ATOM 328 CA ASN A 42 -25.982 -22.924 18.113 1.00 26.99 C ANISOU 328 CA ASN A 42 3859 3315 3081 -495 58 290 C ATOM 329 C ASN A 42 -27.022 -22.133 18.895 1.00 25.15 C ANISOU 329 C ASN A 42 3591 3134 2831 -507 63 292 C ATOM 330 O ASN A 42 -27.698 -21.284 18.305 1.00 28.01 O ANISOU 330 O ASN A 42 3912 3533 3196 -512 62 277 O ATOM 331 CB ASN A 42 -26.669 -23.858 17.117 1.00 25.62 C ANISOU 331 CB ASN A 42 3699 3127 2909 -540 69 285 C ATOM 332 CG ASN A 42 -25.716 -24.369 16.051 1.00 33.14 C ANISOU 332 CG ASN A 42 4672 4039 3882 -526 61 274 C ATOM 333 OD1 ASN A 42 -24.616 -23.838 15.882 1.00 32.39 O ANISOU 333 OD1 ASN A 42 4572 3935 3802 -485 48 266 O ATOM 334 ND2 ASN A 42 -26.137 -25.393 15.319 1.00 28.39 N ANISOU 334 ND2 ASN A 42 4091 3415 3281 -563 70 270 N ATOM 335 N TYR A 43 -27.169 -22.377 20.199 1.00 27.38 N ANISOU 335 N TYR A 43 3887 3422 3094 -510 68 309 N ATOM 336 CA TYR A 43 -28.034 -21.519 21.002 1.00 31.26 C ANISOU 336 CA TYR A 43 4341 3968 3570 -514 72 307 C ATOM 337 C TYR A 43 -27.404 -20.145 21.192 1.00 27.47 C ANISOU 337 C TYR A 43 3825 3509 3103 -465 56 295 C ATOM 338 O TYR A 43 -28.101 -19.124 21.158 1.00 24.86 O ANISOU 338 O TYR A 43 3451 3222 2772 -463 54 281 O ATOM 339 CB TYR A 43 -28.331 -22.179 22.349 1.00 38.63 C ANISOU 339 CB TYR A 43 5300 4903 4476 -533 83 329 C ATOM 340 CG TYR A 43 -29.047 -23.505 22.216 1.00 50.73 C ANISOU 340 CG TYR A 43 6867 6415 5992 -588 100 341 C ATOM 341 CD1 TYR A 43 -29.815 -23.791 21.093 1.00 56.45 C ANISOU 341 CD1 TYR A 43 7582 7144 6723 -624 108 326 C ATOM 342 CD2 TYR A 43 -28.948 -24.475 23.205 1.00 52.70 C ANISOU 342 CD2 TYR A 43 7163 6639 6220 -604 108 366 C ATOM 343 CE1 TYR A 43 -30.464 -25.000 20.958 1.00 59.13 C ANISOU 343 CE1 TYR A 43 7954 7465 7050 -676 125 335 C ATOM 344 CE2 TYR A 43 -29.595 -25.690 23.080 1.00 57.25 C ANISOU 344 CE2 TYR A 43 7776 7193 6784 -657 125 378 C ATOM 345 CZ TYR A 43 -30.353 -25.947 21.954 1.00 59.31 C ANISOU 345 CZ TYR A 43 8024 7459 7052 -694 134 361 C ATOM 346 OH TYR A 43 -31.003 -27.153 21.821 1.00 59.14 O ANISOU 346 OH TYR A 43 8037 7415 7018 -750 151 370 O ATOM 347 N PHE A 44 -26.083 -20.097 21.382 1.00 21.01 N ANISOU 347 N PHE A 44 3026 2660 2298 -424 45 298 N ATOM 348 CA PHE A 44 -25.387 -18.816 21.387 1.00 22.91 C ANISOU 348 CA PHE A 44 3235 2915 2555 -380 31 284 C ATOM 349 C PHE A 44 -25.353 -18.195 19.996 1.00 22.84 C ANISOU 349 C PHE A 44 3205 2908 2567 -378 25 266 C ATOM 350 O PHE A 44 -25.306 -16.967 19.869 1.00 27.60 O ANISOU 350 O PHE A 44 3772 3534 3180 -355 16 253 O ATOM 351 CB PHE A 44 -23.971 -18.988 21.935 1.00 21.53 C ANISOU 351 CB PHE A 44 3085 2710 2387 -340 22 289 C ATOM 352 CG PHE A 44 -23.932 -19.421 23.372 1.00 26.45 C ANISOU 352 CG PHE A 44 3726 3335 2987 -335 24 307 C ATOM 353 CD1 PHE A 44 -24.235 -18.525 24.385 1.00 32.51 C ANISOU 353 CD1 PHE A 44 4463 4144 3744 -321 23 305 C ATOM 354 CD2 PHE A 44 -23.605 -20.722 23.710 1.00 26.33 C ANISOU 354 CD2 PHE A 44 3761 3281 2961 -344 28 326 C ATOM 355 CE1 PHE A 44 -24.207 -18.921 25.711 1.00 32.96 C ANISOU 355 CE1 PHE A 44 4537 4208 3778 -318 26 321 C ATOM 356 CE2 PHE A 44 -23.573 -21.123 25.033 1.00 26.71 C ANISOU 356 CE2 PHE A 44 3831 3332 2985 -340 29 345 C ATOM 357 CZ PHE A 44 -23.874 -20.223 26.034 1.00 26.52 C ANISOU 357 CZ PHE A 44 3774 3353 2949 -328 29 343 C ATOM 358 N VAL A 45 -25.374 -19.022 18.946 1.00 22.03 N ANISOU 358 N VAL A 45 3122 2778 2470 -401 30 265 N ATOM 359 CA VAL A 45 -25.470 -18.502 17.583 1.00 21.23 C ANISOU 359 CA VAL A 45 3002 2682 2384 -404 25 250 C ATOM 360 C VAL A 45 -26.807 -17.803 17.375 1.00 21.29 C ANISOU 360 C VAL A 45 2972 2735 2383 -424 27 242 C ATOM 361 O VAL A 45 -26.883 -16.751 16.726 1.00 21.61 O ANISOU 361 O VAL A 45 2984 2793 2434 -409 17 230 O ATOM 362 CB VAL A 45 -25.258 -19.639 16.563 1.00 24.72 C ANISOU 362 CB VAL A 45 3473 3087 2831 -426 30 249 C ATOM 363 CG1 VAL A 45 -25.630 -19.183 15.157 1.00 18.33 C ANISOU 363 CG1 VAL A 45 2642 2291 2031 -438 28 234 C ATOM 364 CG2 VAL A 45 -23.818 -20.130 16.606 1.00 28.19 C ANISOU 364 CG2 VAL A 45 3943 3484 3282 -397 24 249 C ATOM 365 N VAL A 46 -27.880 -18.376 17.924 1.00 21.43 N ANISOU 365 N VAL A 46 2990 2772 2381 -458 39 248 N ATOM 366 CA VAL A 46 -29.199 -17.758 17.819 1.00 24.64 C ANISOU 366 CA VAL A 46 3358 3226 2776 -477 40 236 C ATOM 367 C VAL A 46 -29.251 -16.463 18.619 1.00 24.44 C ANISOU 367 C VAL A 46 3299 3235 2752 -444 30 230 C ATOM 368 O VAL A 46 -29.787 -15.451 18.151 1.00 21.41 O ANISOU 368 O VAL A 46 2880 2881 2373 -435 20 215 O ATOM 369 CB VAL A 46 -30.286 -18.750 18.272 1.00 28.13 C ANISOU 369 CB VAL A 46 3809 3683 3195 -525 58 242 C ATOM 370 CG1 VAL A 46 -31.613 -18.033 18.491 1.00 24.61 C ANISOU 370 CG1 VAL A 46 3318 3296 2735 -539 59 227 C ATOM 371 CG2 VAL A 46 -30.442 -19.860 17.244 1.00 28.56 C ANISOU 371 CG2 VAL A 46 3889 3710 3252 -559 67 242 C ATOM 372 N SER A 47 -28.709 -16.474 19.840 1.00 24.24 N ANISOU 372 N SER A 47 3283 3206 2721 -426 30 240 N ATOM 373 CA SER A 47 -28.622 -15.237 20.611 1.00 27.12 C ANISOU 373 CA SER A 47 3615 3600 3088 -392 20 232 C ATOM 374 C SER A 47 -27.838 -14.179 19.849 1.00 26.92 C ANISOU 374 C SER A 47 3578 3563 3089 -357 4 221 C ATOM 375 O SER A 47 -28.212 -12.999 19.840 1.00 25.57 O ANISOU 375 O SER A 47 3372 3420 2923 -339 -7 207 O ATOM 376 CB SER A 47 -27.974 -15.502 21.971 1.00 26.34 C ANISOU 376 CB SER A 47 3533 3494 2980 -376 22 245 C ATOM 377 OG SER A 47 -27.849 -14.300 22.711 1.00 26.19 O ANISOU 377 OG SER A 47 3481 3504 2965 -343 12 234 O ATOM 378 N LEU A 48 -26.752 -14.590 19.195 1.00 20.72 N ANISOU 378 N LEU A 48 2820 2736 2318 -347 2 226 N ATOM 379 CA LEU A 48 -25.980 -13.671 18.368 1.00 20.04 C ANISOU 379 CA LEU A 48 2724 2637 2252 -320 -10 216 C ATOM 380 C LEU A 48 -26.812 -13.160 17.196 1.00 22.35 C ANISOU 380 C LEU A 48 2996 2946 2548 -334 -15 206 C ATOM 381 O LEU A 48 -26.761 -11.970 16.861 1.00 21.33 O ANISOU 381 O LEU A 48 2845 2828 2430 -312 -28 196 O ATOM 382 CB LEU A 48 -24.716 -14.377 17.880 1.00 21.20 C ANISOU 382 CB LEU A 48 2904 2740 2411 -313 -8 220 C ATOM 383 CG LEU A 48 -23.653 -13.591 17.126 1.00 30.73 C ANISOU 383 CG LEU A 48 4107 3930 3638 -287 -18 209 C ATOM 384 CD1 LEU A 48 -23.126 -12.462 17.984 1.00 25.06 C ANISOU 384 CD1 LEU A 48 3370 3225 2928 -252 -26 202 C ATOM 385 CD2 LEU A 48 -22.527 -14.532 16.726 1.00 35.30 C ANISOU 385 CD2 LEU A 48 4719 4471 4224 -284 -14 210 C ATOM 386 N ALA A 49 -27.597 -14.042 16.570 1.00 21.59 N ANISOU 386 N ALA A 49 2908 2852 2441 -370 -6 208 N ATOM 387 CA ALA A 49 -28.470 -13.613 15.482 1.00 21.15 C ANISOU 387 CA ALA A 49 2832 2817 2385 -383 -12 197 C ATOM 388 C ALA A 49 -29.588 -12.705 15.980 1.00 18.39 C ANISOU 388 C ALA A 49 2446 2514 2028 -378 -19 187 C ATOM 389 O ALA A 49 -29.994 -11.781 15.269 1.00 19.50 O ANISOU 389 O ALA A 49 2564 2671 2173 -367 -33 176 O ATOM 390 CB ALA A 49 -29.055 -14.830 14.764 1.00 22.20 C ANISOU 390 CB ALA A 49 2982 2945 2509 -424 1 199 C ATOM 391 N ALA A 50 -30.098 -12.951 17.189 1.00 20.31 N ANISOU 391 N ALA A 50 2681 2780 2256 -386 -12 188 N ATOM 392 CA ALA A 50 -31.123 -12.075 17.751 1.00 23.41 C ANISOU 392 CA ALA A 50 3034 3221 2641 -379 -20 173 C ATOM 393 C ALA A 50 -30.594 -10.658 17.934 1.00 23.07 C ANISOU 393 C ALA A 50 2972 3179 2614 -334 -38 166 C ATOM 394 O ALA A 50 -31.311 -9.682 17.686 1.00 23.04 O ANISOU 394 O ALA A 50 2938 3204 2613 -321 -53 151 O ATOM 395 CB ALA A 50 -31.622 -12.633 19.083 1.00 26.63 C ANISOU 395 CB ALA A 50 3438 3652 3028 -396 -6 177 C ATOM 396 N ALA A 51 -29.341 -10.527 18.373 1.00 20.51 N ANISOU 396 N ALA A 51 2666 2825 2304 -311 -39 175 N ATOM 397 CA ALA A 51 -28.743 -9.205 18.512 1.00 22.14 C ANISOU 397 CA ALA A 51 2857 3028 2528 -271 -55 167 C ATOM 398 C ALA A 51 -28.601 -8.522 17.159 1.00 23.37 C ANISOU 398 C ALA A 51 3013 3168 2698 -263 -67 163 C ATOM 399 O ALA A 51 -28.760 -7.301 17.052 1.00 29.70 O ANISOU 399 O ALA A 51 3794 3980 3510 -239 -84 153 O ATOM 400 CB ALA A 51 -27.385 -9.313 19.207 1.00 19.08 C ANISOU 400 CB ALA A 51 2488 2611 2149 -251 -51 174 C ATOM 401 N ASP A 52 -28.307 -9.296 16.113 1.00 17.28 N ANISOU 401 N ASP A 52 2266 2373 1927 -284 -60 171 N ATOM 402 CA ASP A 52 -28.165 -8.717 14.784 1.00 19.96 C ANISOU 402 CA ASP A 52 2608 2700 2276 -280 -71 170 C ATOM 403 C ASP A 52 -29.516 -8.329 14.194 1.00 20.64 C ANISOU 403 C ASP A 52 2670 2819 2352 -288 -82 160 C ATOM 404 O ASP A 52 -29.606 -7.340 13.458 1.00 22.24 O ANISOU 404 O ASP A 52 2866 3021 2562 -272 -99 156 O ATOM 405 CB ASP A 52 -27.424 -9.693 13.869 1.00 22.07 C ANISOU 405 CB ASP A 52 2906 2935 2545 -300 -60 178 C ATOM 406 CG ASP A 52 -25.957 -9.844 14.247 1.00 33.11 C ANISOU 406 CG ASP A 52 4325 4300 3955 -284 -55 183 C ATOM 407 OD1 ASP A 52 -25.401 -8.909 14.864 1.00 37.41 O ANISOU 407 OD1 ASP A 52 4860 4843 4511 -256 -62 179 O ATOM 408 OD2 ASP A 52 -25.358 -10.894 13.925 1.00 35.52 O ANISOU 408 OD2 ASP A 52 4655 4582 4260 -298 -44 188 O ATOM 409 N ILE A 53 -30.573 -9.081 14.510 1.00 22.16 N ANISOU 409 N ILE A 53 2853 3041 2528 -314 -73 155 N ATOM 410 CA ILE A 53 -31.914 -8.691 14.079 1.00 26.39 C ANISOU 410 CA ILE A 53 3360 3615 3052 -319 -84 141 C ATOM 411 C ILE A 53 -32.314 -7.369 14.725 1.00 24.48 C ANISOU 411 C ILE A 53 3087 3398 2815 -285 -103 127 C ATOM 412 O ILE A 53 -32.915 -6.502 14.081 1.00 24.33 O ANISOU 412 O ILE A 53 3052 3394 2798 -269 -123 117 O ATOM 413 CB ILE A 53 -32.926 -9.809 14.396 1.00 27.77 C ANISOU 413 CB ILE A 53 3527 3819 3206 -357 -67 136 C ATOM 414 CG1 ILE A 53 -32.605 -11.069 13.588 1.00 26.85 C ANISOU 414 CG1 ILE A 53 3440 3675 3085 -391 -51 146 C ATOM 415 CG2 ILE A 53 -34.349 -9.344 14.111 1.00 27.89 C ANISOU 415 CG2 ILE A 53 3506 3882 3208 -360 -79 114 C ATOM 416 CD1 ILE A 53 -33.460 -12.270 13.956 1.00 26.38 C ANISOU 416 CD1 ILE A 53 3381 3636 3007 -433 -32 143 C ATOM 417 N LEU A 54 -31.975 -7.188 16.005 1.00 22.34 N ANISOU 417 N LEU A 54 2810 3132 2547 -272 -99 127 N ATOM 418 CA LEU A 54 -32.292 -5.945 16.699 1.00 22.52 C ANISOU 418 CA LEU A 54 2803 3176 2576 -238 -117 111 C ATOM 419 C LEU A 54 -31.457 -4.775 16.195 1.00 20.41 C ANISOU 419 C LEU A 54 2545 2879 2332 -205 -135 114 C ATOM 420 O LEU A 54 -31.890 -3.623 16.315 1.00 20.53 O ANISOU 420 O LEU A 54 2538 2908 2354 -177 -156 100 O ATOM 421 CB LEU A 54 -32.103 -6.118 18.208 1.00 19.62 C ANISOU 421 CB LEU A 54 2427 2824 2204 -235 -106 109 C ATOM 422 CG LEU A 54 -33.070 -7.088 18.889 1.00 23.10 C ANISOU 422 CG LEU A 54 2855 3302 2620 -268 -90 104 C ATOM 423 CD1 LEU A 54 -32.699 -7.286 20.356 1.00 28.99 C ANISOU 423 CD1 LEU A 54 3598 4057 3359 -264 -79 107 C ATOM 424 CD2 LEU A 54 -34.507 -6.591 18.760 1.00 26.34 C ANISOU 424 CD2 LEU A 54 3226 3764 3019 -269 -102 80 C ATOM 425 N VAL A 55 -30.269 -5.038 15.643 1.00 18.65 N ANISOU 425 N VAL A 55 2354 2613 2120 -208 -127 130 N ATOM 426 CA VAL A 55 -29.510 -3.971 14.995 1.00 17.65 C ANISOU 426 CA VAL A 55 2238 2457 2012 -184 -142 133 C ATOM 427 C VAL A 55 -30.298 -3.406 13.821 1.00 18.37 C ANISOU 427 C VAL A 55 2325 2556 2100 -182 -160 130 C ATOM 428 O VAL A 55 -30.403 -2.185 13.651 1.00 22.93 O ANISOU 428 O VAL A 55 2894 3130 2688 -154 -182 124 O ATOM 429 CB VAL A 55 -28.122 -4.477 14.554 1.00 21.97 C ANISOU 429 CB VAL A 55 2818 2962 2568 -193 -128 148 C ATOM 430 CG1 VAL A 55 -27.473 -3.494 13.581 1.00 16.97 C ANISOU 430 CG1 VAL A 55 2198 2301 1949 -179 -141 152 C ATOM 431 CG2 VAL A 55 -27.223 -4.690 15.761 1.00 18.88 C ANISOU 431 CG2 VAL A 55 2429 2562 2183 -183 -117 148 C ATOM 432 N GLY A 56 -30.892 -4.283 13.011 1.00 22.42 N ANISOU 432 N GLY A 56 2841 3078 2597 -209 -154 133 N ATOM 433 CA GLY A 56 -31.646 -3.813 11.861 1.00 20.30 C ANISOU 433 CA GLY A 56 2569 2820 2323 -207 -172 130 C ATOM 434 C GLY A 56 -32.975 -3.191 12.241 1.00 21.05 C ANISOU 434 C GLY A 56 2629 2959 2411 -190 -190 110 C ATOM 435 O GLY A 56 -33.400 -2.199 11.644 1.00 21.07 O ANISOU 435 O GLY A 56 2626 2964 2416 -166 -215 104 O ATOM 436 N VAL A 57 -33.644 -3.755 13.246 1.00 23.06 N ANISOU 436 N VAL A 57 2860 3248 2654 -201 -180 97 N ATOM 437 CA VAL A 57 -34.974 -3.281 13.614 1.00 22.68 C ANISOU 437 CA VAL A 57 2773 3248 2595 -189 -195 72 C ATOM 438 C VAL A 57 -34.894 -2.011 14.458 1.00 19.69 C ANISOU 438 C VAL A 57 2376 2872 2231 -148 -215 60 C ATOM 439 O VAL A 57 -35.720 -1.103 14.307 1.00 20.65 O ANISOU 439 O VAL A 57 2476 3017 2354 -122 -241 41 O ATOM 440 CB VAL A 57 -35.748 -4.400 14.337 1.00 28.63 C ANISOU 440 CB VAL A 57 3509 4041 3329 -223 -174 61 C ATOM 441 CG1 VAL A 57 -37.095 -3.895 14.819 1.00 33.11 C ANISOU 441 CG1 VAL A 57 4031 4665 3884 -211 -189 31 C ATOM 442 CG2 VAL A 57 -35.933 -5.597 13.418 1.00 31.14 C ANISOU 442 CG2 VAL A 57 3843 4356 3634 -262 -157 70 C ATOM 443 N LEU A 58 -33.906 -1.910 15.347 1.00 23.32 N ANISOU 443 N LEU A 58 2847 3310 2705 -141 -204 67 N ATOM 444 CA LEU A 58 -33.867 -0.812 16.309 1.00 24.61 C ANISOU 444 CA LEU A 58 2988 3481 2881 -105 -220 52 C ATOM 445 C LEU A 58 -32.606 0.034 16.222 1.00 23.54 C ANISOU 445 C LEU A 58 2877 3296 2770 -82 -226 64 C ATOM 446 O LEU A 58 -32.703 1.263 16.130 1.00 19.90 O ANISOU 446 O LEU A 58 2409 2828 2323 -49 -251 54 O ATOM 447 CB LEU A 58 -34.032 -1.361 17.736 1.00 29.09 C ANISOU 447 CB LEU A 58 3535 4080 3439 -115 -202 42 C ATOM 448 CG LEU A 58 -35.412 -1.918 18.101 1.00 29.50 C ANISOU 448 CG LEU A 58 3553 4189 3466 -135 -198 22 C ATOM 449 CD1 LEU A 58 -35.401 -2.515 19.499 1.00 20.72 C ANISOU 449 CD1 LEU A 58 2427 3102 2342 -150 -178 18 C ATOM 450 CD2 LEU A 58 -36.484 -0.840 17.989 1.00 29.17 C ANISOU 450 CD2 LEU A 58 3476 4181 3425 -104 -228 -7 C ATOM 451 N ALA A 59 -31.418 -0.579 16.256 1.00 19.88 N ANISOU 451 N ALA A 59 2441 2800 2312 -98 -205 83 N ATOM 452 CA ALA A 59 -30.192 0.210 16.368 1.00 21.24 C ANISOU 452 CA ALA A 59 2631 2933 2506 -78 -209 89 C ATOM 453 C ALA A 59 -29.954 1.069 15.131 1.00 23.62 C ANISOU 453 C ALA A 59 2954 3203 2819 -67 -227 98 C ATOM 454 O ALA A 59 -29.461 2.198 15.241 1.00 23.17 O ANISOU 454 O ALA A 59 2900 3122 2780 -42 -241 94 O ATOM 455 CB ALA A 59 -28.992 -0.704 16.623 1.00 19.01 C ANISOU 455 CB ALA A 59 2371 2625 2225 -97 -183 104 C ATOM 456 N ILE A 60 -30.290 0.562 13.949 1.00 22.07 N ANISOU 456 N ILE A 60 2772 3003 2610 -87 -226 109 N ATOM 457 CA ILE A 60 -30.058 1.315 12.718 1.00 22.29 C ANISOU 457 CA ILE A 60 2823 3002 2644 -80 -242 121 C ATOM 458 C ILE A 60 -31.080 2.445 12.600 1.00 21.11 C ANISOU 458 C ILE A 60 2657 2868 2497 -49 -275 107 C ATOM 459 O ILE A 60 -30.687 3.577 12.284 1.00 20.80 O ANISOU 459 O ILE A 60 2632 2799 2472 -27 -293 111 O ATOM 460 CB ILE A 60 -30.055 0.390 11.488 1.00 24.28 C ANISOU 460 CB ILE A 60 3095 3248 2880 -112 -232 136 C ATOM 461 CG1 ILE A 60 -28.739 -0.396 11.438 1.00 23.87 C ANISOU 461 CG1 ILE A 60 3068 3169 2833 -134 -205 149 C ATOM 462 CG2 ILE A 60 -30.262 1.189 10.207 1.00 24.28 C ANISOU 462 CG2 ILE A 60 3112 3233 2878 -103 -254 145 C ATOM 463 CD1 ILE A 60 -28.622 -1.359 10.275 1.00 21.80 C ANISOU 463 CD1 ILE A 60 2826 2901 2558 -165 -193 162 C ATOM 464 N PRO A 61 -32.379 2.219 12.844 1.00 16.96 N ANISOU 464 N PRO A 61 2100 2388 1957 -45 -284 89 N ATOM 465 CA PRO A 61 -33.289 3.373 12.937 1.00 19.57 C ANISOU 465 CA PRO A 61 2410 2734 2292 -8 -317 70 C ATOM 466 C PRO A 61 -32.888 4.376 14.009 1.00 24.30 C ANISOU 466 C PRO A 61 2997 3322 2912 23 -327 57 C ATOM 467 O PRO A 61 -33.073 5.583 13.810 1.00 23.18 O ANISOU 467 O PRO A 61 2858 3165 2783 56 -356 50 O ATOM 468 CB PRO A 61 -34.645 2.722 13.240 1.00 17.53 C ANISOU 468 CB PRO A 61 2115 2533 2012 -16 -318 49 C ATOM 469 CG PRO A 61 -34.548 1.383 12.609 1.00 16.19 C ANISOU 469 CG PRO A 61 1960 2367 1826 -58 -292 64 C ATOM 470 CD PRO A 61 -33.130 0.948 12.849 1.00 15.00 C ANISOU 470 CD PRO A 61 1836 2176 1686 -75 -267 85 C ATOM 471 N PHE A 62 -32.303 3.923 15.118 1.00 24.40 N ANISOU 471 N PHE A 62 3001 3341 2930 14 -305 53 N ATOM 472 CA PHE A 62 -31.837 4.826 16.165 1.00 21.41 C ANISOU 472 CA PHE A 62 2610 2953 2572 41 -312 39 C ATOM 473 C PHE A 62 -30.662 5.649 15.645 1.00 21.35 C ANISOU 473 C PHE A 62 2638 2889 2585 50 -316 55 C ATOM 474 O PHE A 62 -30.598 6.823 15.904 1.00 21.45 O ANISOU 474 O PHE A 62 2648 2886 2616 80 -337 44 O ATOM 475 CB PHE A 62 -31.407 4.128 17.467 1.00 20.63 C ANISOU 475 CB PHE A 62 2495 2874 2470 30 -286 32 C ATOM 476 CG PHE A 62 -32.537 3.580 18.303 1.00 22.57 C ANISOU 476 CG PHE A 62 2701 3178 2697 25 -283 12 C ATOM 477 CD1 PHE A 62 -33.846 3.731 17.911 1.00 25.32 C ANISOU 477 CD1 PHE A 62 3027 3560 3032 32 -302 -4 C ATOM 478 CD2 PHE A 62 -32.276 2.839 19.432 1.00 23.25 C ANISOU 478 CD2 PHE A 62 2775 3285 2775 11 -260 9 C ATOM 479 CE1 PHE A 62 -34.870 3.199 18.648 1.00 25.66 C ANISOU 479 CE1 PHE A 62 3033 3659 3056 23 -296 -26 C ATOM 480 CE2 PHE A 62 -33.293 2.305 20.177 1.00 24.98 C ANISOU 480 CE2 PHE A 62 2960 3557 2973 1 -254 -9 C ATOM 481 CZ PHE A 62 -34.597 2.493 19.788 1.00 26.27 C ANISOU 481 CZ PHE A 62 3099 3757 3125 6 -272 -27 C ATOM 482 N ALA A 63 -29.746 5.012 14.920 1.00 19.42 N ANISOU 482 N ALA A 63 2425 2616 2337 21 -296 79 N ATOM 483 CA ALA A 63 -28.586 5.711 14.376 1.00 18.90 C ANISOU 483 CA ALA A 63 2393 2500 2289 22 -296 93 C ATOM 484 C ALA A 63 -28.997 6.724 13.315 1.00 21.53 C ANISOU 484 C ALA A 63 2744 2810 2625 38 -325 101 C ATOM 485 O ALA A 63 -28.409 7.808 13.221 1.00 23.31 O ANISOU 485 O ALA A 63 2988 2999 2869 53 -336 103 O ATOM 486 CB ALA A 63 -27.595 4.703 13.794 1.00 17.61 C ANISOU 486 CB ALA A 63 2255 2319 2118 -14 -268 113 C ATOM 487 N ILE A 64 -29.988 6.380 12.492 1.00 27.95 N ANISOU 487 N ILE A 64 3557 3644 3419 33 -336 105 N ATOM 488 CA ILE A 64 -30.504 7.329 11.512 1.00 27.19 C ANISOU 488 CA ILE A 64 3478 3530 3323 53 -367 112 C ATOM 489 C ILE A 64 -31.111 8.534 12.217 1.00 28.96 C ANISOU 489 C ILE A 64 3683 3757 3563 96 -398 89 C ATOM 490 O ILE A 64 -30.903 9.683 11.810 1.00 23.47 O ANISOU 490 O ILE A 64 3012 3025 2882 117 -421 95 O ATOM 491 CB ILE A 64 -31.523 6.634 10.590 1.00 27.41 C ANISOU 491 CB ILE A 64 3503 3588 3326 42 -374 116 C ATOM 492 CG1 ILE A 64 -30.818 5.606 9.700 1.00 24.52 C ANISOU 492 CG1 ILE A 64 3161 3209 2945 0 -347 139 C ATOM 493 CG2 ILE A 64 -32.286 7.655 9.754 1.00 28.63 C ANISOU 493 CG2 ILE A 64 3668 3734 3477 71 -412 117 C ATOM 494 CD1 ILE A 64 -31.764 4.787 8.845 1.00 28.04 C ANISOU 494 CD1 ILE A 64 3601 3688 3367 -15 -349 141 C ATOM 495 N THR A 65 -31.850 8.289 13.301 1.00 24.35 N ANISOU 495 N THR A 65 3057 3218 2977 109 -399 62 N ATOM 496 CA THR A 65 -32.498 9.374 14.028 1.00 23.64 C ANISOU 496 CA THR A 65 2942 3138 2902 152 -428 35 C ATOM 497 C THR A 65 -31.471 10.299 14.672 1.00 26.41 C ANISOU 497 C THR A 65 3304 3448 3280 166 -428 32 C ATOM 498 O THR A 65 -31.586 11.527 14.583 1.00 28.52 O ANISOU 498 O THR A 65 3582 3689 3565 198 -457 25 O ATOM 499 CB THR A 65 -33.443 8.799 15.085 1.00 25.51 C ANISOU 499 CB THR A 65 3129 3437 3128 156 -424 5 C ATOM 500 OG1 THR A 65 -34.326 7.851 14.474 1.00 26.95 O ANISOU 500 OG1 THR A 65 3301 3656 3284 136 -419 7 O ATOM 501 CG2 THR A 65 -34.269 9.902 15.718 1.00 31.44 C ANISOU 501 CG2 THR A 65 3851 4205 3891 202 -458 -28 C ATOM 502 N ILE A 66 -30.455 9.729 15.324 1.00 27.26 N ANISOU 502 N ILE A 66 3413 3552 3394 143 -396 36 N ATOM 503 CA ILE A 66 -29.480 10.549 16.034 1.00 27.80 C ANISOU 503 CA ILE A 66 3486 3590 3488 155 -394 28 C ATOM 504 C ILE A 66 -28.552 11.302 15.095 1.00 29.67 C ANISOU 504 C ILE A 66 3769 3765 3737 149 -397 50 C ATOM 505 O ILE A 66 -27.883 12.248 15.527 1.00 27.11 O ANISOU 505 O ILE A 66 3453 3411 3438 162 -403 42 O ATOM 506 CB ILE A 66 -28.669 9.687 17.024 1.00 27.19 C ANISOU 506 CB ILE A 66 3393 3528 3409 135 -359 24 C ATOM 507 CG1 ILE A 66 -28.151 10.551 18.178 1.00 30.74 C ANISOU 507 CG1 ILE A 66 3826 3971 3884 159 -363 0 C ATOM 508 CG2 ILE A 66 -27.518 8.987 16.320 1.00 27.48 C ANISOU 508 CG2 ILE A 66 3464 3536 3442 99 -332 51 C ATOM 509 CD1 ILE A 66 -27.549 9.756 19.314 1.00 31.45 C ANISOU 509 CD1 ILE A 66 3894 4087 3970 147 -334 -9 C ATOM 510 N SER A 67 -28.500 10.918 13.816 1.00 30.49 N ANISOU 510 N SER A 67 3905 3854 3827 126 -395 78 N ATOM 511 CA SER A 67 -27.713 11.669 12.845 1.00 26.75 C ANISOU 511 CA SER A 67 3477 3325 3360 117 -400 100 C ATOM 512 C SER A 67 -28.344 13.014 12.512 1.00 26.33 C ANISOU 512 C SER A 67 3438 3246 3319 153 -440 97 C ATOM 513 O SER A 67 -27.656 13.894 11.982 1.00 25.01 O ANISOU 513 O SER A 67 3309 3029 3164 150 -447 112 O ATOM 514 CB SER A 67 -27.530 10.852 11.563 1.00 23.12 C ANISOU 514 CB SER A 67 3045 2861 2878 83 -386 129 C ATOM 515 OG SER A 67 -28.755 10.715 10.860 1.00 24.92 O ANISOU 515 OG SER A 67 3269 3112 3087 94 -409 133 O ATOM 516 N THR A 68 -29.633 13.194 12.812 1.00 25.03 N ANISOU 516 N THR A 68 3245 3116 3151 185 -467 77 N ATOM 517 CA THR A 68 -30.321 14.437 12.488 1.00 24.35 C ANISOU 517 CA THR A 68 3171 3006 3074 225 -510 72 C ATOM 518 C THR A 68 -30.097 15.526 13.527 1.00 30.51 C ANISOU 518 C THR A 68 3940 3768 3885 256 -524 46 C ATOM 519 O THR A 68 -30.336 16.701 13.229 1.00 35.02 O ANISOU 519 O THR A 68 4533 4303 4471 286 -558 45 O ATOM 520 CB THR A 68 -31.826 14.194 12.342 1.00 25.36 C ANISOU 520 CB THR A 68 3270 3182 3184 250 -536 56 C ATOM 521 OG1 THR A 68 -32.388 13.875 13.622 1.00 24.24 O ANISOU 521 OG1 THR A 68 3074 3091 3045 265 -532 20 O ATOM 522 CG2 THR A 68 -32.093 13.047 11.381 1.00 21.01 C ANISOU 522 CG2 THR A 68 2726 2654 2602 218 -520 77 C ATOM 523 N GLY A 69 -29.654 15.171 14.730 1.00 25.07 N ANISOU 523 N GLY A 69 3217 3102 3206 251 -501 25 N ATOM 524 CA GLY A 69 -29.516 16.161 15.782 1.00 24.57 C ANISOU 524 CA GLY A 69 3136 3028 3170 282 -514 -5 C ATOM 525 C GLY A 69 -30.831 16.726 16.271 1.00 27.43 C ANISOU 525 C GLY A 69 3465 3422 3537 329 -551 -37 C ATOM 526 O GLY A 69 -30.870 17.862 16.751 1.00 29.10 O ANISOU 526 O GLY A 69 3674 3609 3774 362 -576 -58 O ATOM 527 N PHE A 70 -31.910 15.955 16.167 1.00 25.21 N ANISOU 527 N PHE A 70 3154 3193 3230 331 -556 -44 N ATOM 528 CA PHE A 70 -33.234 16.433 16.534 1.00 27.35 C ANISOU 528 CA PHE A 70 3390 3501 3502 375 -592 -78 C ATOM 529 C PHE A 70 -33.302 16.761 18.025 1.00 27.27 C ANISOU 529 C PHE A 70 3333 3520 3508 397 -591 -119 C ATOM 530 O PHE A 70 -32.529 16.252 18.841 1.00 27.40 O ANISOU 530 O PHE A 70 3335 3547 3527 374 -558 -122 O ATOM 531 CB PHE A 70 -34.292 15.386 16.182 1.00 27.68 C ANISOU 531 CB PHE A 70 3405 3600 3510 365 -589 -80 C ATOM 532 CG PHE A 70 -34.325 14.222 17.130 1.00 32.86 C ANISOU 532 CG PHE A 70 4020 4312 4152 338 -554 -93 C ATOM 533 CD1 PHE A 70 -33.276 13.318 17.178 1.00 32.87 C ANISOU 533 CD1 PHE A 70 4037 4304 4149 294 -513 -68 C ATOM 534 CD2 PHE A 70 -35.404 14.032 17.975 1.00 34.58 C ANISOU 534 CD2 PHE A 70 4184 4594 4360 356 -563 -131 C ATOM 535 CE1 PHE A 70 -33.301 12.252 18.055 1.00 30.95 C ANISOU 535 CE1 PHE A 70 3761 4109 3891 271 -482 -78 C ATOM 536 CE2 PHE A 70 -35.435 12.965 18.852 1.00 31.43 C ANISOU 536 CE2 PHE A 70 3750 4246 3945 329 -530 -141 C ATOM 537 CZ PHE A 70 -34.384 12.075 18.891 1.00 31.87 C ANISOU 537 CZ PHE A 70 3826 4286 3996 286 -490 -112 C ATOM 538 N CYS A 71 -34.251 17.627 18.373 1.00 27.47 N ANISOU 538 N CYS A 71 3334 3559 3544 445 -630 -154 N ATOM 539 CA CYS A 71 -34.440 18.027 19.761 1.00 30.65 C ANISOU 539 CA CYS A 71 3689 3994 3962 470 -635 -198 C ATOM 540 C CYS A 71 -35.086 16.897 20.554 1.00 30.39 C ANISOU 540 C CYS A 71 3601 4041 3903 454 -612 -218 C ATOM 541 O CYS A 71 -36.067 16.294 20.109 1.00 28.17 O ANISOU 541 O CYS A 71 3305 3801 3597 451 -618 -220 O ATOM 542 CB CYS A 71 -35.308 19.282 19.836 1.00 35.14 C ANISOU 542 CB CYS A 71 4247 4555 4549 528 -686 -231 C ATOM 543 SG CYS A 71 -34.575 20.751 19.085 1.00 43.39 S ANISOU 543 SG CYS A 71 5356 5501 5627 550 -715 -211 S ATOM 544 N ALA A 72 -34.546 16.622 21.738 1.00 27.23 N ANISOU 544 N ALA A 72 3173 3664 3508 442 -586 -233 N ATOM 545 CA ALA A 72 -35.047 15.528 22.557 1.00 26.89 C ANISOU 545 CA ALA A 72 3084 3694 3438 422 -561 -248 C ATOM 546 C ALA A 72 -34.611 15.739 23.996 1.00 29.72 C ANISOU 546 C ALA A 72 3408 4076 3810 430 -548 -277 C ATOM 547 O ALA A 72 -33.581 16.365 24.259 1.00 28.75 O ANISOU 547 O ALA A 72 3304 3908 3712 435 -544 -274 O ATOM 548 CB ALA A 72 -34.541 14.172 22.050 1.00 27.93 C ANISOU 548 CB ALA A 72 3238 3827 3546 370 -522 -208 C ATOM 549 N ALA A 73 -35.410 15.213 24.923 1.00 28.94 N ANISOU 549 N ALA A 73 3256 4049 3690 429 -542 -307 N ATOM 550 CA ALA A 73 -34.963 15.109 26.304 1.00 27.80 C ANISOU 550 CA ALA A 73 3078 3935 3547 427 -522 -329 C ATOM 551 C ALA A 73 -33.677 14.296 26.355 1.00 26.43 C ANISOU 551 C ALA A 73 2936 3736 3370 387 -482 -292 C ATOM 552 O ALA A 73 -33.547 13.272 25.679 1.00 27.07 O ANISOU 552 O ALA A 73 3041 3813 3430 351 -460 -257 O ATOM 553 CB ALA A 73 -36.043 14.463 27.172 1.00 29.96 C ANISOU 553 CB ALA A 73 3296 4295 3792 422 -515 -361 C ATOM 554 N CYS A 74 -32.716 14.767 27.154 1.00 27.04 N ANISOU 554 N CYS A 74 3011 3796 3468 395 -473 -301 N ATOM 555 CA CYS A 74 -31.361 14.228 27.077 1.00 29.97 C ANISOU 555 CA CYS A 74 3416 4132 3841 364 -441 -269 C ATOM 556 C CYS A 74 -31.323 12.740 27.405 1.00 30.04 C ANISOU 556 C CYS A 74 3417 4180 3815 326 -406 -249 C ATOM 557 O CYS A 74 -30.584 11.979 26.769 1.00 30.39 O ANISOU 557 O CYS A 74 3499 4196 3853 295 -384 -213 O ATOM 558 CB CYS A 74 -30.433 15.009 28.008 1.00 38.84 C ANISOU 558 CB CYS A 74 4529 5239 4990 382 -439 -291 C ATOM 559 SG CYS A 74 -28.679 14.594 27.824 1.00 43.02 S ANISOU 559 SG CYS A 74 5100 5719 5527 351 -405 -258 S ATOM 560 N HIS A 75 -32.111 12.300 28.389 1.00 29.26 N ANISOU 560 N HIS A 75 3274 4150 3696 326 -402 -274 N ATOM 561 CA HIS A 75 -32.075 10.889 28.763 1.00 31.16 C ANISOU 561 CA HIS A 75 3511 4426 3902 288 -368 -254 C ATOM 562 C HIS A 75 -32.767 10.012 27.727 1.00 30.12 C ANISOU 562 C HIS A 75 3398 4298 3749 260 -364 -229 C ATOM 563 O HIS A 75 -32.405 8.841 27.569 1.00 25.04 O ANISOU 563 O HIS A 75 2775 3655 3085 224 -336 -199 O ATOM 564 CB HIS A 75 -32.695 10.694 30.143 1.00 37.76 C ANISOU 564 CB HIS A 75 4295 5332 4719 293 -363 -287 C ATOM 565 CG HIS A 75 -31.827 11.181 31.260 1.00 46.00 C ANISOU 565 CG HIS A 75 5324 6379 5777 310 -357 -305 C ATOM 566 ND1 HIS A 75 -31.777 12.505 31.641 1.00 45.69 N ANISOU 566 ND1 HIS A 75 5264 6329 5767 350 -383 -341 N ATOM 567 CD2 HIS A 75 -30.957 10.526 32.064 1.00 50.31 C ANISOU 567 CD2 HIS A 75 5872 6934 6311 294 -330 -294 C ATOM 568 CE1 HIS A 75 -30.923 12.642 32.639 1.00 47.40 C ANISOU 568 CE1 HIS A 75 5469 6552 5990 356 -370 -352 C ATOM 569 NE2 HIS A 75 -30.411 11.456 32.915 1.00 51.32 N ANISOU 569 NE2 HIS A 75 5979 7061 6461 323 -339 -324 N ATOM 570 N GLY A 76 -33.692 10.578 26.980 1.00 29.07 N ANISOU 570 N GLY A 76 3260 4165 3620 278 -392 -241 N ATOM 571 CA GLY A 76 -34.337 9.866 25.900 1.00 31.07 C ANISOU 571 CA GLY A 76 3531 4420 3855 255 -391 -219 C ATOM 572 C GLY A 76 -33.315 9.711 24.787 1.00 32.30 C ANISOU 572 C GLY A 76 3742 4509 4022 239 -382 -178 C ATOM 573 O GLY A 76 -33.169 8.679 24.199 1.00 31.70 O ANISOU 573 O GLY A 76 3689 4427 3929 205 -361 -149 O ATOM 574 N CYS A 77 -32.557 10.760 24.551 1.00 28.64 N ANISOU 574 N CYS A 77 3300 3994 3589 262 -397 -178 N ATOM 575 CA CYS A 77 -31.515 10.749 23.576 1.00 25.65 C ANISOU 575 CA CYS A 77 2971 3554 3222 247 -388 -143 C ATOM 576 C CYS A 77 -30.439 9.712 23.939 1.00 26.13 C ANISOU 576 C CYS A 77 3046 3609 3273 214 -351 -121 C ATOM 577 O CYS A 77 -29.973 8.999 23.097 1.00 24.93 O ANISOU 577 O CYS A 77 2927 3432 3112 186 -335 -90 O ATOM 578 CB CYS A 77 -30.907 12.123 23.464 1.00 34.69 C ANISOU 578 CB CYS A 77 4132 4649 4400 276 -409 -152 C ATOM 579 SG CYS A 77 -29.574 12.134 22.290 1.00 37.29 S ANISOU 579 SG CYS A 77 4522 4906 4742 252 -396 -112 S ATOM 580 N LEU A 78 -30.116 9.610 25.215 1.00 23.77 N ANISOU 580 N LEU A 78 2721 3338 2973 219 -338 -139 N ATOM 581 CA LEU A 78 -29.146 8.670 25.685 1.00 26.81 C ANISOU 581 CA LEU A 78 3116 3721 3347 194 -307 -122 C ATOM 582 C LEU A 78 -29.548 7.255 25.367 1.00 27.35 C ANISOU 582 C LEU A 78 3193 3812 3385 159 -287 -99 C ATOM 583 O LEU A 78 -28.705 6.489 25.000 1.00 24.80 O ANISOU 583 O LEU A 78 2901 3465 3058 135 -266 -73 O ATOM 584 CB LEU A 78 -28.957 8.778 27.189 1.00 29.23 C ANISOU 584 CB LEU A 78 3389 4066 3653 208 -300 -147 C ATOM 585 CG LEU A 78 -27.839 9.609 27.770 1.00 30.34 C ANISOU 585 CG LEU A 78 3529 4179 3819 228 -300 -161 C ATOM 586 CD1 LEU A 78 -27.914 9.558 29.278 1.00 33.48 C ANISOU 586 CD1 LEU A 78 3886 4627 4207 240 -294 -188 C ATOM 587 CD2 LEU A 78 -26.478 9.167 27.261 1.00 24.49 C ANISOU 587 CD2 LEU A 78 2827 3394 3084 208 -280 -134 C ATOM 588 N PHE A 79 -30.821 6.907 25.527 1.00 18.92 N ANISOU 588 N PHE A 79 2099 2792 2296 154 -292 -110 N ATOM 589 CA PHE A 79 -31.264 5.560 25.225 1.00 19.00 C ANISOU 589 CA PHE A 79 2118 2823 2278 117 -272 -90 C ATOM 590 C PHE A 79 -31.078 5.236 23.763 1.00 19.99 C ANISOU 590 C PHE A 79 2282 2908 2405 99 -272 -62 C ATOM 591 O PHE A 79 -30.598 4.199 23.419 1.00 25.38 O ANISOU 591 O PHE A 79 2990 3578 3076 70 -250 -37 O ATOM 592 CB PHE A 79 -32.710 5.316 25.617 1.00 20.81 C ANISOU 592 CB PHE A 79 2308 3113 2484 114 -278 -112 C ATOM 593 CG PHE A 79 -33.147 3.912 25.388 1.00 24.19 C ANISOU 593 CG PHE A 79 2745 3564 2883 72 -255 -93 C ATOM 594 CD1 PHE A 79 -32.829 2.924 26.283 1.00 25.43 C ANISOU 594 CD1 PHE A 79 2903 3740 3020 48 -228 -83 C ATOM 595 CD2 PHE A 79 -33.847 3.574 24.272 1.00 22.78 C ANISOU 595 CD2 PHE A 79 2577 3383 2696 56 -260 -84 C ATOM 596 CE1 PHE A 79 -33.226 1.633 26.066 1.00 26.19 C ANISOU 596 CE1 PHE A 79 3011 3851 3090 8 -207 -65 C ATOM 597 CE2 PHE A 79 -34.246 2.289 24.051 1.00 21.93 C ANISOU 597 CE2 PHE A 79 2477 3293 2561 16 -239 -69 C ATOM 598 CZ PHE A 79 -33.936 1.316 24.946 1.00 26.83 C ANISOU 598 CZ PHE A 79 3100 3930 3164 -9 -212 -59 C ATOM 599 N ILE A 80 -31.409 6.201 22.929 1.00 19.82 N ANISOU 599 N ILE A 80 2266 2865 2400 120 -298 -68 N ATOM 600 CA ILE A 80 -31.277 6.164 21.491 1.00 25.27 C ANISOU 600 CA ILE A 80 2992 3517 3093 109 -303 -44 C ATOM 601 C ILE A 80 -29.800 5.993 21.117 1.00 20.07 C ANISOU 601 C ILE A 80 2372 2807 2447 96 -286 -19 C ATOM 602 O ILE A 80 -29.511 5.336 20.195 1.00 19.58 O ANISOU 602 O ILE A 80 2338 2724 2376 71 -275 5 O ATOM 603 CB ILE A 80 -31.836 7.460 20.886 1.00 35.02 C ANISOU 603 CB ILE A 80 4225 4737 4344 143 -339 -57 C ATOM 604 CG1 ILE A 80 -33.346 7.421 20.879 1.00 41.23 C ANISOU 604 CG1 ILE A 80 4978 5574 5114 151 -356 -79 C ATOM 605 CG2 ILE A 80 -31.373 7.680 19.485 1.00 38.11 C ANISOU 605 CG2 ILE A 80 4660 5078 4743 135 -345 -31 C ATOM 606 CD1 ILE A 80 -33.891 6.179 20.263 1.00 38.43 C ANISOU 606 CD1 ILE A 80 4628 5241 4731 115 -340 -64 C ATOM 607 N ALA A 81 -28.898 6.631 21.836 1.00 18.92 N ANISOU 607 N ALA A 81 2224 2644 2320 113 -284 -28 N ATOM 608 CA ALA A 81 -27.477 6.503 21.629 1.00 24.35 C ANISOU 608 CA ALA A 81 2942 3290 3019 101 -267 -12 C ATOM 609 C ALA A 81 -26.868 5.217 22.214 1.00 24.88 C ANISOU 609 C ALA A 81 3012 3371 3069 78 -238 -1 C ATOM 610 O ALA A 81 -25.967 4.687 21.679 1.00 22.37 O ANISOU 610 O ALA A 81 2723 3025 2752 59 -222 17 O ATOM 611 CB ALA A 81 -26.782 7.697 22.236 1.00 18.61 C ANISOU 611 CB ALA A 81 2209 2544 2319 128 -277 -31 C ATOM 612 N CYS A 82 -27.363 4.732 23.325 1.00 23.16 N ANISOU 612 N CYS A 82 2766 3196 2836 79 -231 -13 N ATOM 613 CA CYS A 82 -26.740 3.588 23.978 1.00 22.27 C ANISOU 613 CA CYS A 82 2660 3093 2708 61 -205 -2 C ATOM 614 C CYS A 82 -27.238 2.194 23.661 1.00 24.88 C ANISOU 614 C CYS A 82 3002 3439 3013 28 -189 17 C ATOM 615 O CYS A 82 -26.552 1.250 23.897 1.00 18.97 O ANISOU 615 O CYS A 82 2270 2682 2254 12 -170 32 O ATOM 616 CB CYS A 82 -26.690 3.836 25.494 1.00 23.39 C ANISOU 616 CB CYS A 82 2770 3270 2849 80 -204 -24 C ATOM 617 SG CYS A 82 -25.682 5.251 25.930 1.00 25.28 S ANISOU 617 SG CYS A 82 3002 3483 3121 113 -215 -46 S ATOM 618 N PHE A 83 -28.389 2.086 23.037 1.00 19.10 N ANISOU 618 N PHE A 83 2263 2725 2270 18 -198 18 N ATOM 619 CA PHE A 83 -28.979 0.764 22.855 1.00 22.98 C ANISOU 619 CA PHE A 83 2761 3235 2735 -16 -182 32 C ATOM 620 C PHE A 83 -28.114 -0.127 21.970 1.00 23.05 C ANISOU 620 C PHE A 83 2810 3205 2743 -40 -166 58 C ATOM 621 O PHE A 83 -28.043 -1.340 22.199 1.00 23.97 O ANISOU 621 O PHE A 83 2939 3327 2842 -64 -147 72 O ATOM 622 CB PHE A 83 -30.388 0.873 22.274 1.00 19.82 C ANISOU 622 CB PHE A 83 2343 2864 2324 -22 -195 23 C ATOM 623 CG PHE A 83 -31.051 -0.459 22.078 1.00 25.04 C ANISOU 623 CG PHE A 83 3009 3546 2958 -59 -178 34 C ATOM 624 CD1 PHE A 83 -31.440 -1.219 23.172 1.00 24.76 C ANISOU 624 CD1 PHE A 83 2958 3547 2901 -75 -162 31 C ATOM 625 CD2 PHE A 83 -31.266 -0.964 20.806 1.00 23.31 C ANISOU 625 CD2 PHE A 83 2812 3310 2735 -80 -176 49 C ATOM 626 CE1 PHE A 83 -32.041 -2.452 23.001 1.00 23.30 C ANISOU 626 CE1 PHE A 83 2781 3379 2692 -114 -144 42 C ATOM 627 CE2 PHE A 83 -31.869 -2.197 20.627 1.00 25.30 C ANISOU 627 CE2 PHE A 83 3069 3581 2965 -117 -159 58 C ATOM 628 CZ PHE A 83 -32.257 -2.942 21.727 1.00 23.02 C ANISOU 628 CZ PHE A 83 2766 3325 2655 -134 -143 54 C ATOM 629 N VAL A 84 -27.438 0.451 20.971 1.00 22.09 N ANISOU 629 N VAL A 84 2710 3044 2640 -33 -174 65 N ATOM 630 CA VAL A 84 -26.545 -0.345 20.132 1.00 20.81 C ANISOU 630 CA VAL A 84 2583 2846 2477 -54 -159 86 C ATOM 631 C VAL A 84 -25.401 -0.921 20.958 1.00 20.44 C ANISOU 631 C VAL A 84 2547 2790 2431 -53 -142 89 C ATOM 632 O VAL A 84 -24.859 -1.983 20.627 1.00 19.59 O ANISOU 632 O VAL A 84 2463 2665 2315 -73 -126 104 O ATOM 633 CB VAL A 84 -26.024 0.493 18.947 1.00 17.80 C ANISOU 633 CB VAL A 84 2221 2428 2113 -49 -170 91 C ATOM 634 CG1 VAL A 84 -25.081 1.590 19.430 1.00 16.02 C ANISOU 634 CG1 VAL A 84 1993 2183 1911 -23 -176 79 C ATOM 635 CG2 VAL A 84 -25.336 -0.403 17.919 1.00 13.36 C ANISOU 635 CG2 VAL A 84 1691 1838 1546 -75 -156 110 C ATOM 636 N LEU A 85 -25.024 -0.248 22.049 1.00 19.35 N ANISOU 636 N LEU A 85 2389 2661 2302 -29 -145 74 N ATOM 637 CA LEU A 85 -23.972 -0.770 22.915 1.00 19.50 C ANISOU 637 CA LEU A 85 2414 2675 2318 -24 -131 74 C ATOM 638 C LEU A 85 -24.443 -2.000 23.680 1.00 18.95 C ANISOU 638 C LEU A 85 2345 2632 2223 -40 -118 84 C ATOM 639 O LEU A 85 -23.635 -2.882 23.994 1.00 17.41 O ANISOU 639 O LEU A 85 2169 2424 2020 -45 -105 94 O ATOM 640 CB LEU A 85 -23.502 0.315 23.886 1.00 23.24 C ANISOU 640 CB LEU A 85 2866 3157 2808 8 -140 53 C ATOM 641 CG LEU A 85 -22.984 1.613 23.263 1.00 25.97 C ANISOU 641 CG LEU A 85 3213 3474 3180 23 -153 42 C ATOM 642 CD1 LEU A 85 -22.634 2.633 24.342 1.00 22.59 C ANISOU 642 CD1 LEU A 85 2759 3056 2767 53 -160 18 C ATOM 643 CD2 LEU A 85 -21.779 1.334 22.377 1.00 25.80 C ANISOU 643 CD2 LEU A 85 3222 3412 3167 11 -142 53 C ATOM 644 N VAL A 86 -25.733 -2.090 23.917 1.00 17.34 N ANISOU 644 N VAL A 86 2122 2463 2004 -49 -121 80 N ATOM 645 CA VAL A 86 -26.285 -3.247 24.558 1.00 21.24 C ANISOU 645 CA VAL A 86 2617 2981 2471 -72 -107 90 C ATOM 646 C VAL A 86 -26.157 -4.430 23.595 1.00 19.89 C ANISOU 646 C VAL A 86 2481 2785 2292 -102 -95 112 C ATOM 647 O VAL A 86 -25.714 -5.483 23.973 1.00 18.47 O ANISOU 647 O VAL A 86 2322 2596 2099 -115 -81 126 O ATOM 648 CB VAL A 86 -27.757 -3.067 24.947 1.00 19.54 C ANISOU 648 CB VAL A 86 2370 2814 2241 -80 -112 77 C ATOM 649 CG1 VAL A 86 -28.293 -4.320 25.586 1.00 20.36 C ANISOU 649 CG1 VAL A 86 2480 2942 2315 -109 -95 89 C ATOM 650 CG2 VAL A 86 -27.955 -1.884 25.847 1.00 13.78 C ANISOU 650 CG2 VAL A 86 1604 2112 1520 -48 -126 52 C ATOM 651 N LEU A 87 -26.483 -4.209 22.333 1.00 15.68 N ANISOU 651 N LEU A 87 1954 2237 1767 -112 -102 114 N ATOM 652 CA LEU A 87 -26.437 -5.287 21.354 1.00 19.08 C ANISOU 652 CA LEU A 87 2414 2645 2190 -141 -91 131 C ATOM 653 C LEU A 87 -25.004 -5.730 21.087 1.00 19.82 C ANISOU 653 C LEU A 87 2537 2698 2294 -137 -83 141 C ATOM 654 O LEU A 87 -24.733 -6.930 20.962 1.00 23.74 O ANISOU 654 O LEU A 87 3059 3180 2780 -156 -70 154 O ATOM 655 CB LEU A 87 -27.119 -4.846 20.061 1.00 16.95 C ANISOU 655 CB LEU A 87 2141 2373 1926 -149 -102 130 C ATOM 656 CG LEU A 87 -28.578 -4.402 20.196 1.00 22.80 C ANISOU 656 CG LEU A 87 2851 3157 2657 -151 -113 116 C ATOM 657 CD1 LEU A 87 -29.121 -3.950 18.848 1.00 20.31 C ANISOU 657 CD1 LEU A 87 2535 2834 2346 -154 -126 115 C ATOM 658 CD2 LEU A 87 -29.439 -5.515 20.785 1.00 20.63 C ANISOU 658 CD2 LEU A 87 2570 2912 2356 -180 -97 119 C ATOM 659 N ALA A 88 -24.073 -4.777 21.000 1.00 19.07 N ANISOU 659 N ALA A 88 2441 2586 2220 -112 -91 132 N ATOM 660 CA ALA A 88 -22.674 -5.135 20.798 1.00 22.48 C ANISOU 660 CA ALA A 88 2896 2985 2660 -107 -84 135 C ATOM 661 C ALA A 88 -22.134 -5.924 21.984 1.00 19.25 C ANISOU 661 C ALA A 88 2494 2581 2240 -99 -74 138 C ATOM 662 O ALA A 88 -21.369 -6.878 21.806 1.00 18.48 O ANISOU 662 O ALA A 88 2422 2460 2139 -105 -66 146 O ATOM 663 CB ALA A 88 -21.835 -3.879 20.559 1.00 20.86 C ANISOU 663 CB ALA A 88 2684 2764 2478 -84 -93 122 C ATOM 664 N GLN A 89 -22.524 -5.548 23.190 1.00 21.09 N ANISOU 664 N GLN A 89 2704 2844 2467 -85 -77 130 N ATOM 665 CA GLN A 89 -22.082 -6.256 24.385 1.00 22.07 C ANISOU 665 CA GLN A 89 2835 2976 2576 -76 -70 135 C ATOM 666 C GLN A 89 -22.583 -7.688 24.410 1.00 23.91 C ANISOU 666 C GLN A 89 3092 3207 2786 -105 -58 155 C ATOM 667 O GLN A 89 -21.855 -8.579 24.746 1.00 20.74 O ANISOU 667 O GLN A 89 2715 2788 2376 -103 -51 164 O ATOM 668 CB GLN A 89 -22.456 -5.541 25.666 1.00 22.01 C ANISOU 668 CB GLN A 89 2795 3004 2563 -57 -75 121 C ATOM 669 CG GLN A 89 -21.604 -5.984 26.837 1.00 30.83 C ANISOU 669 CG GLN A 89 3918 4125 3670 -39 -70 122 C ATOM 670 CD GLN A 89 -20.119 -5.786 26.596 1.00 32.95 C ANISOU 670 CD GLN A 89 4199 4363 3956 -17 -71 113 C ATOM 671 OE1 GLN A 89 -19.692 -4.745 26.193 1.00 24.34 O ANISOU 671 OE1 GLN A 89 3094 3265 2888 -3 -78 97 O ATOM 672 NE2 GLN A 89 -19.349 -6.802 26.860 1.00 32.10 N ANISOU 672 NE2 GLN A 89 4118 4241 3839 -14 -65 123 N ATOM 673 N SER A 90 -23.828 -7.868 24.002 1.00 21.18 N ANISOU 673 N SER A 90 2738 2878 2430 -131 -56 160 N ATOM 674 CA SER A 90 -24.446 -9.168 23.929 1.00 22.66 C ANISOU 674 CA SER A 90 2948 3065 2596 -165 -44 177 C ATOM 675 C SER A 90 -23.736 -10.041 22.930 1.00 22.89 C ANISOU 675 C SER A 90 3012 3052 2631 -176 -39 188 C ATOM 676 O SER A 90 -23.531 -11.193 23.176 1.00 20.74 O ANISOU 676 O SER A 90 2768 2764 2346 -189 -30 202 O ATOM 677 CB SER A 90 -25.926 -9.049 23.634 1.00 23.18 C ANISOU 677 CB SER A 90 2994 3163 2652 -190 -44 174 C ATOM 678 OG SER A 90 -26.473 -10.314 23.489 1.00 27.69 O ANISOU 678 OG SER A 90 3587 3730 3204 -226 -31 189 O ATOM 679 N SER A 91 -23.399 -9.465 21.794 1.00 18.41 N ANISOU 679 N SER A 91 2444 2468 2084 -172 -46 180 N ATOM 680 CA SER A 91 -22.640 -10.189 20.781 1.00 20.73 C ANISOU 680 CA SER A 91 2767 2725 2385 -182 -41 186 C ATOM 681 C SER A 91 -21.298 -10.653 21.331 1.00 20.25 C ANISOU 681 C SER A 91 2726 2641 2327 -160 -40 186 C ATOM 682 O SER A 91 -20.859 -11.776 21.057 1.00 22.58 O ANISOU 682 O SER A 91 3051 2910 2617 -170 -34 195 O ATOM 683 CB SER A 91 -22.436 -9.302 19.550 1.00 23.95 C ANISOU 683 CB SER A 91 3166 3122 2810 -179 -49 177 C ATOM 684 OG SER A 91 -23.676 -8.890 18.999 1.00 27.45 O ANISOU 684 OG SER A 91 3592 3587 3250 -195 -54 176 O ATOM 685 N ILE A 92 -20.638 -9.800 22.116 1.00 22.04 N ANISOU 685 N ILE A 92 2936 2877 2562 -129 -46 174 N ATOM 686 CA ILE A 92 -19.346 -10.149 22.696 1.00 22.78 C ANISOU 686 CA ILE A 92 3044 2954 2657 -104 -46 170 C ATOM 687 C ILE A 92 -19.486 -11.325 23.654 1.00 22.68 C ANISOU 687 C ILE A 92 3054 2942 2623 -108 -40 186 C ATOM 688 O ILE A 92 -18.675 -12.258 23.634 1.00 21.71 O ANISOU 688 O ILE A 92 2960 2792 2497 -102 -39 190 O ATOM 689 CB ILE A 92 -18.735 -8.916 23.387 1.00 25.78 C ANISOU 689 CB ILE A 92 3396 3349 3049 -72 -53 151 C ATOM 690 CG1 ILE A 92 -18.212 -7.934 22.337 1.00 28.86 C ANISOU 690 CG1 ILE A 92 3776 3726 3462 -68 -57 136 C ATOM 691 CG2 ILE A 92 -17.642 -9.326 24.361 1.00 22.24 C ANISOU 691 CG2 ILE A 92 2957 2896 2596 -44 -53 146 C ATOM 692 CD1 ILE A 92 -17.735 -6.631 22.914 1.00 36.24 C ANISOU 692 CD1 ILE A 92 4684 4674 4412 -41 -64 116 C ATOM 693 N PHE A 93 -20.509 -11.305 24.489 1.00 18.98 N ANISOU 693 N PHE A 93 2573 2502 2137 -118 -38 194 N ATOM 694 CA PHE A 93 -20.748 -12.395 25.402 1.00 24.99 C ANISOU 694 CA PHE A 93 3358 3264 2873 -127 -31 213 C ATOM 695 C PHE A 93 -21.007 -13.697 24.639 1.00 22.41 C ANISOU 695 C PHE A 93 3068 2908 2540 -159 -23 229 C ATOM 696 O PHE A 93 -20.494 -14.721 25.015 1.00 20.97 O ANISOU 696 O PHE A 93 2919 2703 2347 -156 -22 241 O ATOM 697 CB PHE A 93 -21.895 -12.126 26.374 1.00 30.26 C ANISOU 697 CB PHE A 93 4003 3974 3521 -139 -27 217 C ATOM 698 CG PHE A 93 -21.591 -11.103 27.428 1.00 32.77 C ANISOU 698 CG PHE A 93 4290 4321 3840 -107 -35 202 C ATOM 699 CD1 PHE A 93 -20.377 -11.081 28.075 1.00 39.33 C ANISOU 699 CD1 PHE A 93 5128 5142 4674 -73 -40 197 C ATOM 700 CD2 PHE A 93 -22.534 -10.185 27.795 1.00 27.65 C ANISOU 700 CD2 PHE A 93 3604 3713 3190 -110 -37 191 C ATOM 701 CE1 PHE A 93 -20.115 -10.146 29.045 1.00 37.71 C ANISOU 701 CE1 PHE A 93 4893 4966 4470 -44 -46 180 C ATOM 702 CE2 PHE A 93 -22.275 -9.245 28.751 1.00 25.92 C ANISOU 702 CE2 PHE A 93 3355 3521 2973 -80 -43 174 C ATOM 703 CZ PHE A 93 -21.066 -9.223 29.378 1.00 28.07 C ANISOU 703 CZ PHE A 93 3634 3783 3248 -48 -47 169 C ATOM 704 N SER A 94 -21.790 -13.636 23.573 1.00 21.45 N ANISOU 704 N SER A 94 2940 2787 2424 -187 -20 228 N ATOM 705 CA SER A 94 -22.073 -14.832 22.786 1.00 27.67 C ANISOU 705 CA SER A 94 3759 3548 3207 -218 -12 240 C ATOM 706 C SER A 94 -20.817 -15.356 22.100 1.00 23.96 C ANISOU 706 C SER A 94 3316 3037 2752 -203 -16 236 C ATOM 707 O SER A 94 -20.581 -16.569 22.069 1.00 21.11 O ANISOU 707 O SER A 94 2991 2647 2383 -213 -13 247 O ATOM 708 CB SER A 94 -23.163 -14.541 21.754 1.00 28.41 C ANISOU 708 CB SER A 94 3835 3657 3304 -249 -9 236 C ATOM 709 OG SER A 94 -24.413 -14.307 22.379 1.00 27.80 O ANISOU 709 OG SER A 94 3735 3618 3210 -267 -5 238 O ATOM 710 N LEU A 95 -20.001 -14.458 21.542 1.00 22.39 N ANISOU 710 N LEU A 95 3099 2836 2573 -179 -24 218 N ATOM 711 CA LEU A 95 -18.768 -14.881 20.884 1.00 23.37 C ANISOU 711 CA LEU A 95 3243 2927 2710 -164 -27 208 C ATOM 712 C LEU A 95 -17.806 -15.527 21.872 1.00 25.92 C ANISOU 712 C LEU A 95 3588 3234 3026 -136 -32 210 C ATOM 713 O LEU A 95 -17.143 -16.518 21.546 1.00 26.62 O ANISOU 713 O LEU A 95 3708 3292 3116 -132 -33 210 O ATOM 714 CB LEU A 95 -18.106 -13.688 20.193 1.00 18.97 C ANISOU 714 CB LEU A 95 2660 2374 2173 -148 -33 187 C ATOM 715 CG LEU A 95 -18.824 -13.159 18.951 1.00 20.22 C ANISOU 715 CG LEU A 95 2804 2540 2339 -173 -31 185 C ATOM 716 CD1 LEU A 95 -18.188 -11.862 18.460 1.00 20.46 C ANISOU 716 CD1 LEU A 95 2812 2576 2387 -157 -37 168 C ATOM 717 CD2 LEU A 95 -18.810 -14.209 17.862 1.00 18.06 C ANISOU 717 CD2 LEU A 95 2555 2241 2065 -197 -26 188 C ATOM 718 N LEU A 96 -17.713 -14.977 23.085 1.00 24.41 N ANISOU 718 N LEU A 96 3382 3066 2827 -113 -35 210 N ATOM 719 CA LEU A 96 -16.851 -15.576 24.098 1.00 26.41 C ANISOU 719 CA LEU A 96 3656 3308 3070 -84 -41 213 C ATOM 720 C LEU A 96 -17.398 -16.923 24.556 1.00 26.39 C ANISOU 720 C LEU A 96 3694 3288 3045 -104 -36 239 C ATOM 721 O LEU A 96 -16.631 -17.863 24.796 1.00 24.17 O ANISOU 721 O LEU A 96 3446 2977 2759 -87 -42 244 O ATOM 722 CB LEU A 96 -16.693 -14.621 25.283 1.00 27.65 C ANISOU 722 CB LEU A 96 3785 3498 3223 -56 -45 206 C ATOM 723 CG LEU A 96 -15.817 -15.095 26.448 1.00 29.09 C ANISOU 723 CG LEU A 96 3984 3677 3391 -21 -52 208 C ATOM 724 CD1 LEU A 96 -14.424 -15.472 25.964 1.00 27.11 C ANISOU 724 CD1 LEU A 96 3750 3398 3154 6 -61 190 C ATOM 725 CD2 LEU A 96 -15.738 -14.028 27.532 1.00 32.92 C ANISOU 725 CD2 LEU A 96 4436 4200 3873 3 -56 197 C ATOM 726 N ALA A 97 -18.724 -17.037 24.673 1.00 22.83 N ANISOU 726 N ALA A 97 3239 2854 2581 -140 -27 256 N ATOM 727 CA ALA A 97 -19.325 -18.304 25.074 1.00 25.45 C ANISOU 727 CA ALA A 97 3610 3169 2891 -167 -20 281 C ATOM 728 C ALA A 97 -19.085 -19.387 24.029 1.00 26.38 C ANISOU 728 C ALA A 97 3762 3243 3016 -183 -19 284 C ATOM 729 O ALA A 97 -18.810 -20.540 24.378 1.00 24.71 O ANISOU 729 O ALA A 97 3595 3000 2794 -183 -21 299 O ATOM 730 CB ALA A 97 -20.821 -18.118 25.320 1.00 19.09 C ANISOU 730 CB ALA A 97 2788 2398 2070 -206 -8 292 C ATOM 731 N ILE A 98 -19.190 -19.037 22.745 1.00 27.79 N ANISOU 731 N ILE A 98 3925 3420 3215 -196 -17 269 N ATOM 732 CA ILE A 98 -18.940 -20.010 21.684 1.00 26.98 C ANISOU 732 CA ILE A 98 3851 3279 3121 -211 -16 266 C ATOM 733 C ILE A 98 -17.500 -20.501 21.744 1.00 29.21 C ANISOU 733 C ILE A 98 4157 3530 3413 -172 -29 256 C ATOM 734 O ILE A 98 -17.229 -21.696 21.577 1.00 30.00 O ANISOU 734 O ILE A 98 4297 3591 3509 -176 -31 263 O ATOM 735 CB ILE A 98 -19.280 -19.404 20.308 1.00 21.53 C ANISOU 735 CB ILE A 98 3134 2599 2449 -230 -13 251 C ATOM 736 CG1 ILE A 98 -20.789 -19.193 20.175 1.00 19.38 C ANISOU 736 CG1 ILE A 98 2843 2354 2165 -270 -2 260 C ATOM 737 CG2 ILE A 98 -18.770 -20.299 19.183 1.00 20.91 C ANISOU 737 CG2 ILE A 98 3079 2483 2381 -238 -14 242 C ATOM 738 CD1 ILE A 98 -21.188 -18.359 18.972 1.00 18.94 C ANISOU 738 CD1 ILE A 98 2757 2317 2124 -283 -1 245 C ATOM 739 N ALA A 99 -16.555 -19.592 21.998 1.00 24.37 N ANISOU 739 N ALA A 99 3519 2931 2809 -134 -37 237 N ATOM 740 CA ALA A 99 -15.154 -19.991 22.088 1.00 24.47 C ANISOU 740 CA ALA A 99 3549 2920 2829 -94 -50 222 C ATOM 741 C ALA A 99 -14.922 -20.926 23.268 1.00 28.29 C ANISOU 741 C ALA A 99 4070 3384 3293 -76 -57 241 C ATOM 742 O ALA A 99 -14.224 -21.939 23.139 1.00 29.55 O ANISOU 742 O ALA A 99 4267 3508 3454 -60 -66 239 O ATOM 743 CB ALA A 99 -14.262 -18.754 22.193 1.00 18.53 C ANISOU 743 CB ALA A 99 2758 2192 2089 -61 -55 196 C ATOM 744 N ILE A 100 -15.504 -20.605 24.426 1.00 28.69 N ANISOU 744 N ILE A 100 4116 3461 3325 -77 -54 259 N ATOM 745 CA ILE A 100 -15.363 -21.469 25.594 1.00 28.77 C ANISOU 745 CA ILE A 100 4164 3455 3311 -62 -60 281 C ATOM 746 C ILE A 100 -16.018 -22.820 25.337 1.00 29.46 C ANISOU 746 C ILE A 100 4301 3505 3389 -97 -55 305 C ATOM 747 O ILE A 100 -15.485 -23.869 25.719 1.00 28.12 O ANISOU 747 O ILE A 100 4177 3298 3211 -80 -65 316 O ATOM 748 CB ILE A 100 -15.949 -20.777 26.839 1.00 26.37 C ANISOU 748 CB ILE A 100 3839 3192 2988 -61 -56 294 C ATOM 749 CG1 ILE A 100 -15.136 -19.525 27.180 1.00 27.50 C ANISOU 749 CG1 ILE A 100 3939 3368 3143 -21 -63 267 C ATOM 750 CG2 ILE A 100 -15.986 -21.730 28.023 1.00 21.57 C ANISOU 750 CG2 ILE A 100 3275 2570 2351 -55 -60 322 C ATOM 751 CD1 ILE A 100 -15.642 -18.779 28.392 1.00 26.09 C ANISOU 751 CD1 ILE A 100 3735 3232 2946 -17 -60 275 C ATOM 752 N ASP A 101 -17.175 -22.814 24.670 1.00 27.44 N ANISOU 752 N ASP A 101 4035 3257 3134 -146 -39 312 N ATOM 753 CA ASP A 101 -17.874 -24.059 24.369 1.00 28.75 C ANISOU 753 CA ASP A 101 4244 3389 3291 -186 -32 333 C ATOM 754 C ASP A 101 -17.030 -24.973 23.489 1.00 33.73 C ANISOU 754 C ASP A 101 4907 3970 3939 -173 -42 320 C ATOM 755 O ASP A 101 -17.010 -26.194 23.689 1.00 30.90 O ANISOU 755 O ASP A 101 4600 3570 3572 -179 -45 337 O ATOM 756 CB ASP A 101 -19.212 -23.749 23.698 1.00 30.10 C ANISOU 756 CB ASP A 101 4390 3584 3463 -238 -14 335 C ATOM 757 CG ASP A 101 -19.970 -24.998 23.306 1.00 35.43 C ANISOU 757 CG ASP A 101 5105 4226 4130 -284 -4 352 C ATOM 758 OD1 ASP A 101 -20.603 -25.608 24.191 1.00 40.34 O ANISOU 758 OD1 ASP A 101 5756 4845 4727 -307 4 378 O ATOM 759 OD2 ASP A 101 -19.940 -25.366 22.114 1.00 39.55 O ANISOU 759 OD2 ASP A 101 5631 4727 4670 -298 -2 338 O ATOM 760 N ARG A 102 -16.320 -24.405 22.512 1.00 32.15 N ANISOU 760 N ARG A 102 4678 3775 3763 -154 -47 290 N ATOM 761 CA ARG A 102 -15.508 -25.238 21.633 1.00 33.48 C ANISOU 761 CA ARG A 102 4871 3902 3947 -142 -57 273 C ATOM 762 C ARG A 102 -14.242 -25.719 22.331 1.00 32.23 C ANISOU 762 C ARG A 102 4740 3719 3786 -88 -77 267 C ATOM 763 O ARG A 102 -13.728 -26.795 22.005 1.00 33.42 O ANISOU 763 O ARG A 102 4930 3826 3943 -78 -87 263 O ATOM 764 CB ARG A 102 -15.159 -24.485 20.345 1.00 34.83 C ANISOU 764 CB ARG A 102 5003 4090 4142 -142 -55 242 C ATOM 765 CG ARG A 102 -16.358 -24.106 19.468 1.00 40.94 C ANISOU 765 CG ARG A 102 5753 4885 4919 -192 -38 245 C ATOM 766 CD ARG A 102 -17.527 -25.083 19.610 1.00 52.04 C ANISOU 766 CD ARG A 102 7190 6273 6310 -237 -27 271 C ATOM 767 NE ARG A 102 -17.199 -26.441 19.189 1.00 53.21 N ANISOU 767 NE ARG A 102 7385 6371 6463 -241 -32 271 N ATOM 768 CZ ARG A 102 -17.841 -27.526 19.611 1.00 55.65 C ANISOU 768 CZ ARG A 102 7737 6650 6758 -268 -27 295 C ATOM 769 NH1 ARG A 102 -18.842 -27.416 20.475 1.00 51.48 N ANISOU 769 NH1 ARG A 102 7211 6141 6209 -296 -15 321 N ATOM 770 NH2 ARG A 102 -17.477 -28.725 19.179 1.00 59.45 N ANISOU 770 NH2 ARG A 102 8261 7081 7246 -269 -34 292 N ATOM 771 N TYR A 103 -13.728 -24.944 23.290 1.00 27.89 N ANISOU 771 N TYR A 103 4171 3198 3230 -53 -84 264 N ATOM 772 CA TYR A 103 -12.584 -25.406 24.067 1.00 35.28 C ANISOU 772 CA TYR A 103 5132 4114 4159 0 -104 259 C ATOM 773 C TYR A 103 -12.962 -26.580 24.962 1.00 35.61 C ANISOU 773 C TYR A 103 5233 4121 4177 -5 -109 295 C ATOM 774 O TYR A 103 -12.203 -27.549 25.073 1.00 33.96 O ANISOU 774 O TYR A 103 5065 3869 3967 25 -127 293 O ATOM 775 CB TYR A 103 -12.006 -24.263 24.904 1.00 36.23 C ANISOU 775 CB TYR A 103 5213 4276 4275 37 -109 246 C ATOM 776 CG TYR A 103 -10.884 -24.709 25.816 1.00 42.20 C ANISOU 776 CG TYR A 103 5995 5019 5022 93 -131 241 C ATOM 777 CD1 TYR A 103 -9.606 -24.930 25.317 1.00 41.42 C ANISOU 777 CD1 TYR A 103 5896 4905 4939 134 -147 206 C ATOM 778 CD2 TYR A 103 -11.105 -24.926 27.171 1.00 43.91 C ANISOU 778 CD2 TYR A 103 6233 5240 5210 105 -135 269 C ATOM 779 CE1 TYR A 103 -8.578 -25.346 26.143 1.00 44.26 C ANISOU 779 CE1 TYR A 103 6276 5254 5288 189 -169 198 C ATOM 780 CE2 TYR A 103 -10.083 -25.343 28.005 1.00 44.72 C ANISOU 780 CE2 TYR A 103 6359 5330 5301 159 -157 265 C ATOM 781 CZ TYR A 103 -8.822 -25.550 27.486 1.00 45.86 C ANISOU 781 CZ TYR A 103 6503 5460 5463 202 -175 228 C ATOM 782 OH TYR A 103 -7.801 -25.965 28.311 1.00 48.66 O ANISOU 782 OH TYR A 103 6878 5804 5804 260 -199 221 O ATOM 783 N ILE A 104 -14.127 -26.512 25.612 1.00 34.19 N ANISOU 783 N ILE A 104 5057 3957 3976 -43 -94 327 N ATOM 784 CA ILE A 104 -14.565 -27.619 26.460 1.00 36.44 C ANISOU 784 CA ILE A 104 5400 4209 4235 -56 -96 364 C ATOM 785 C ILE A 104 -14.762 -28.879 25.628 1.00 30.69 C ANISOU 785 C ILE A 104 4719 3425 3516 -82 -96 369 C ATOM 786 O ILE A 104 -14.420 -29.987 26.059 1.00 36.24 O ANISOU 786 O ILE A 104 5480 4081 4208 -68 -109 386 O ATOM 787 CB ILE A 104 -15.849 -27.239 27.221 1.00 33.65 C ANISOU 787 CB ILE A 104 5036 3892 3858 -100 -76 392 C ATOM 788 CG1 ILE A 104 -15.595 -26.046 28.145 1.00 31.64 C ANISOU 788 CG1 ILE A 104 4738 3689 3594 -70 -78 385 C ATOM 789 CG2 ILE A 104 -16.368 -28.424 28.024 1.00 37.22 C ANISOU 789 CG2 ILE A 104 5552 4309 4281 -123 -75 432 C ATOM 790 CD1 ILE A 104 -16.837 -25.560 28.859 1.00 32.07 C ANISOU 790 CD1 ILE A 104 4774 3787 3626 -110 -60 407 C ATOM 791 N ALA A 105 -15.301 -28.729 24.417 1.00 29.81 N ANISOU 791 N ALA A 105 4583 3318 3423 -119 -82 354 N ATOM 792 CA ALA A 105 -15.575 -29.890 23.581 1.00 32.50 C ANISOU 792 CA ALA A 105 4965 3610 3774 -148 -80 356 C ATOM 793 C ALA A 105 -14.297 -30.566 23.104 1.00 44.64 C ANISOU 793 C ALA A 105 6527 5105 5329 -102 -104 332 C ATOM 794 O ALA A 105 -14.296 -31.775 22.852 1.00 50.04 O ANISOU 794 O ALA A 105 7262 5736 6015 -110 -110 340 O ATOM 795 CB ALA A 105 -16.433 -29.484 22.383 1.00 32.97 C ANISOU 795 CB ALA A 105 4987 3692 3849 -196 -61 343 C ATOM 796 N ILE A 106 -13.203 -29.817 22.981 1.00 42.83 N ANISOU 796 N ILE A 106 6262 4899 5113 -53 -117 300 N ATOM 797 CA ILE A 106 -11.981 -30.365 22.405 1.00 46.81 C ANISOU 797 CA ILE A 106 6779 5370 5634 -10 -138 269 C ATOM 798 C ILE A 106 -10.996 -30.751 23.504 1.00 46.40 C ANISOU 798 C ILE A 106 6760 5301 5570 49 -163 273 C ATOM 799 O ILE A 106 -10.171 -31.653 23.321 1.00 46.36 O ANISOU 799 O ILE A 106 6790 5252 5571 84 -185 258 O ATOM 800 CB ILE A 106 -11.353 -29.373 21.408 1.00 49.58 C ANISOU 800 CB ILE A 106 7071 5758 6008 3 -136 226 C ATOM 801 CG1 ILE A 106 -10.347 -30.084 20.507 1.00 51.28 C ANISOU 801 CG1 ILE A 106 7299 5941 6244 31 -152 190 C ATOM 802 CG2 ILE A 106 -10.691 -28.207 22.131 1.00 51.57 C ANISOU 802 CG2 ILE A 106 7282 6056 6256 41 -140 214 C ATOM 803 CD1 ILE A 106 -9.924 -29.255 19.322 1.00 54.83 C ANISOU 803 CD1 ILE A 106 7695 6424 6715 27 -145 151 C ATOM 804 N ALA A 107 -11.081 -30.086 24.657 1.00 41.67 N ANISOU 804 N ALA A 107 6148 4734 4950 63 -162 290 N ATOM 805 CA ALA A 107 -10.153 -30.354 25.749 1.00 43.63 C ANISOU 805 CA ALA A 107 6423 4973 5183 122 -186 293 C ATOM 806 C ALA A 107 -10.648 -31.459 26.673 1.00 50.65 C ANISOU 806 C ALA A 107 7382 5818 6045 112 -192 339 C ATOM 807 O ALA A 107 -9.850 -32.286 27.128 1.00 53.66 O ANISOU 807 O ALA A 107 7810 6161 6420 158 -218 340 O ATOM 808 CB ALA A 107 -9.896 -29.077 26.554 1.00 39.11 C ANISOU 808 CB ALA A 107 5801 4459 4601 145 -184 287 C ATOM 809 N ILE A 108 -11.945 -31.494 26.959 1.00 52.79 N ANISOU 809 N ILE A 108 7663 6096 6300 54 -169 375 N ATOM 810 CA ILE A 108 -12.516 -32.520 27.829 1.00 53.65 C ANISOU 810 CA ILE A 108 7839 6166 6380 35 -171 421 C ATOM 811 C ILE A 108 -13.779 -33.092 27.191 1.00 52.42 C ANISOU 811 C ILE A 108 7702 5988 6226 -38 -147 441 C ATOM 812 O ILE A 108 -14.877 -32.938 27.747 1.00 50.34 O ANISOU 812 O ILE A 108 7440 5747 5940 -86 -126 472 O ATOM 813 CB ILE A 108 -12.803 -31.959 29.231 1.00 59.87 C ANISOU 813 CB ILE A 108 8620 6992 7134 41 -167 449 C ATOM 814 CG1 ILE A 108 -13.476 -30.588 29.139 1.00 62.21 C ANISOU 814 CG1 ILE A 108 8845 7358 7435 12 -143 438 C ATOM 815 CG2 ILE A 108 -11.518 -31.857 30.039 1.00 62.36 C ANISOU 815 CG2 ILE A 108 8942 7310 7441 116 -196 437 C ATOM 816 CD1 ILE A 108 -13.936 -30.043 30.473 1.00 63.87 C ANISOU 816 CD1 ILE A 108 9045 7610 7611 8 -136 464 C ATOM 817 N PRO A 109 -13.676 -33.775 26.046 1.00 51.93 N ANISOU 817 N PRO A 109 7655 5886 6189 -50 -149 422 N ATOM 818 CA PRO A 109 -14.893 -34.265 25.377 1.00 53.49 C ANISOU 818 CA PRO A 109 7865 6069 6390 -122 -125 436 C ATOM 819 C PRO A 109 -15.633 -35.340 26.154 1.00 58.83 C ANISOU 819 C PRO A 109 8612 6702 7039 -158 -120 482 C ATOM 820 O PRO A 109 -16.824 -35.553 25.894 1.00 55.71 O ANISOU 820 O PRO A 109 8220 6310 6638 -225 -95 499 O ATOM 821 CB PRO A 109 -14.364 -34.809 24.043 1.00 52.61 C ANISOU 821 CB PRO A 109 7756 5922 6311 -113 -135 401 C ATOM 822 CG PRO A 109 -12.952 -35.185 24.334 1.00 53.77 C ANISOU 822 CG PRO A 109 7928 6039 6463 -40 -168 384 C ATOM 823 CD PRO A 109 -12.452 -34.175 25.330 1.00 52.50 C ANISOU 823 CD PRO A 109 7733 5927 6286 1 -174 385 C ATOM 824 N LEU A 110 -14.974 -36.019 27.097 1.00 67.42 N ANISOU 824 N LEU A 110 9757 7752 8109 -117 -143 504 N ATOM 825 CA LEU A 110 -15.640 -37.078 27.847 1.00 75.19 C ANISOU 825 CA LEU A 110 10786 8708 9074 -150 -136 537 C ATOM 826 C LEU A 110 -16.658 -36.523 28.835 1.00 75.55 C ANISOU 826 C LEU A 110 10807 8809 9090 -191 -111 564 C ATOM 827 O LEU A 110 -17.612 -37.221 29.197 1.00 75.80 O ANISOU 827 O LEU A 110 10855 8835 9110 -241 -93 585 O ATOM 828 CB LEU A 110 -14.606 -37.934 28.579 1.00 80.14 C ANISOU 828 CB LEU A 110 11464 9291 9694 -90 -168 543 C ATOM 829 CG LEU A 110 -13.645 -38.734 27.697 1.00 82.74 C ANISOU 829 CG LEU A 110 11825 9561 10051 -50 -195 515 C ATOM 830 CD1 LEU A 110 -12.671 -39.536 28.547 1.00 83.83 C ANISOU 830 CD1 LEU A 110 12011 9663 10180 12 -228 521 C ATOM 831 CD2 LEU A 110 -14.417 -39.645 26.756 1.00 82.98 C ANISOU 831 CD2 LEU A 110 11873 9556 10101 -107 -179 511 C ATOM 832 N ARG A 111 -16.479 -35.279 29.282 1.00 75.30 N ANISOU 832 N ARG A 111 10735 8831 9046 -169 -111 562 N ATOM 833 CA ARG A 111 -17.394 -34.660 30.234 1.00 75.81 C ANISOU 833 CA ARG A 111 10771 8952 9082 -203 -89 584 C ATOM 834 C ARG A 111 -18.077 -33.424 29.659 1.00 65.99 C ANISOU 834 C ARG A 111 9466 7764 7843 -236 -68 570 C ATOM 835 O ARG A 111 -18.610 -32.609 30.417 1.00 62.44 O ANISOU 835 O ARG A 111 8984 7370 7372 -249 -55 580 O ATOM 836 CB ARG A 111 -16.660 -34.309 31.530 1.00 83.48 C ANISOU 836 CB ARG A 111 11749 9942 10028 -150 -107 597 C ATOM 837 CG ARG A 111 -15.252 -33.783 31.322 1.00 91.09 C ANISOU 837 CG ARG A 111 12708 10898 11002 -74 -137 573 C ATOM 838 CD ARG A 111 -14.541 -33.577 32.648 1.00100.05 C ANISOU 838 CD ARG A 111 13851 12052 12111 -19 -156 585 C ATOM 839 NE ARG A 111 -13.091 -33.543 32.488 1.00107.34 N ANISOU 839 NE ARG A 111 14776 12959 13051 58 -189 555 N ATOM 840 CZ ARG A 111 -12.231 -33.381 33.488 1.00111.79 C ANISOU 840 CZ ARG A 111 15347 13534 13595 118 -212 557 C ATOM 841 NH1 ARG A 111 -12.675 -33.231 34.728 1.00112.59 N ANISOU 841 NH1 ARG A 111 15453 13665 13661 108 -205 588 N ATOM 842 NH2 ARG A 111 -10.927 -33.366 33.248 1.00113.31 N ANISOU 842 NH2 ARG A 111 15532 13715 13806 187 -240 522 N ATOM 843 N TYR A 112 -18.077 -33.270 28.334 1.00 60.52 N ANISOU 843 N TYR A 112 8747 7066 7183 -246 -63 539 N ATOM 844 CA TYR A 112 -18.722 -32.109 27.727 1.00 54.36 C ANISOU 844 CA TYR A 112 7892 6348 6416 -272 -44 516 C ATOM 845 C TYR A 112 -20.238 -32.187 27.864 1.00 55.56 C ANISOU 845 C TYR A 112 8040 6523 6548 -347 -15 536 C ATOM 846 O TYR A 112 -20.885 -31.219 28.280 1.00 46.54 O ANISOU 846 O TYR A 112 6848 5442 5393 -362 -1 535 O ATOM 847 CB TYR A 112 -18.316 -31.989 26.257 1.00 46.38 C ANISOU 847 CB TYR A 112 6854 5326 5444 -263 -48 478 C ATOM 848 CG TYR A 112 -19.058 -30.906 25.499 1.00 43.39 C ANISOU 848 CG TYR A 112 6406 5003 5079 -294 -29 456 C ATOM 849 CD1 TYR A 112 -18.632 -29.584 25.538 1.00 43.44 C ANISOU 849 CD1 TYR A 112 6352 5060 5094 -260 -33 434 C ATOM 850 CD2 TYR A 112 -20.181 -31.208 24.740 1.00 42.06 C ANISOU 850 CD2 TYR A 112 6233 4835 4913 -355 -8 457 C ATOM 851 CE1 TYR A 112 -19.308 -28.593 24.845 1.00 39.83 C ANISOU 851 CE1 TYR A 112 5836 4649 4648 -285 -18 415 C ATOM 852 CE2 TYR A 112 -20.863 -30.227 24.046 1.00 42.41 C ANISOU 852 CE2 TYR A 112 6216 4930 4968 -379 6 437 C ATOM 853 CZ TYR A 112 -20.423 -28.922 24.101 1.00 39.98 C ANISOU 853 CZ TYR A 112 5853 4669 4669 -343 0 417 C ATOM 854 OH TYR A 112 -21.105 -27.947 23.407 1.00 39.10 O ANISOU 854 OH TYR A 112 5684 4604 4567 -364 12 399 O ATOM 855 N ASN A 113 -20.825 -33.337 27.519 1.00 62.48 N ANISOU 855 N ASN A 113 8955 7360 7427 -390 -5 546 N ATOM 856 CA ASN A 113 -22.280 -33.460 27.545 1.00 66.54 C ANISOU 856 CA ASN A 113 9446 7906 7931 -457 24 551 C ATOM 857 C ASN A 113 -22.838 -33.316 28.956 1.00 61.69 C ANISOU 857 C ASN A 113 8828 7329 7284 -469 34 575 C ATOM 858 O ASN A 113 -23.953 -32.812 29.132 1.00 60.50 O ANISOU 858 O ASN A 113 8637 7229 7119 -513 56 573 O ATOM 859 CB ASN A 113 -22.706 -34.795 26.933 1.00 72.09 C ANISOU 859 CB ASN A 113 10184 8560 8647 -493 30 549 C ATOM 860 CG ASN A 113 -22.524 -34.828 25.427 1.00 77.56 C ANISOU 860 CG ASN A 113 10867 9232 9371 -498 29 521 C ATOM 861 OD1 ASN A 113 -22.706 -33.818 24.747 1.00 79.73 O ANISOU 861 OD1 ASN A 113 11095 9545 9655 -504 35 503 O ATOM 862 ND2 ASN A 113 -22.160 -35.991 24.900 1.00 80.68 N ANISOU 862 ND2 ASN A 113 11306 9566 9782 -496 19 517 N ATOM 863 N GLY A 114 -22.082 -33.742 29.971 1.00 60.87 N ANISOU 863 N GLY A 114 8763 7201 7164 -430 17 596 N ATOM 864 CA GLY A 114 -22.544 -33.588 31.339 1.00 62.11 C ANISOU 864 CA GLY A 114 8917 7394 7287 -439 25 619 C ATOM 865 C GLY A 114 -22.337 -32.199 31.902 1.00 63.71 C ANISOU 865 C GLY A 114 9075 7657 7475 -412 23 615 C ATOM 866 O GLY A 114 -23.056 -31.788 32.818 1.00 64.15 O ANISOU 866 O GLY A 114 9108 7763 7505 -435 37 626 O ATOM 867 N LEU A 115 -21.364 -31.459 31.373 1.00 62.25 N ANISOU 867 N LEU A 115 8876 7470 7306 -364 4 597 N ATOM 868 CA LEU A 115 -21.055 -30.122 31.863 1.00 60.66 C ANISOU 868 CA LEU A 115 8627 7325 7096 -331 -1 587 C ATOM 869 C LEU A 115 -21.821 -29.038 31.115 1.00 54.74 C ANISOU 869 C LEU A 115 7803 6629 6365 -357 16 557 C ATOM 870 O LEU A 115 -22.324 -28.096 31.737 1.00 49.59 O ANISOU 870 O LEU A 115 7105 6038 5699 -362 25 553 O ATOM 871 CB LEU A 115 -19.548 -29.864 31.758 1.00 64.89 C ANISOU 871 CB LEU A 115 9160 7841 7653 -253 -30 566 C ATOM 872 CG LEU A 115 -19.041 -28.420 31.825 1.00 70.00 C ANISOU 872 CG LEU A 115 9735 8544 8315 -210 -36 534 C ATOM 873 CD1 LEU A 115 -19.361 -27.781 33.164 1.00 71.54 C ANISOU 873 CD1 LEU A 115 9910 8793 8478 -207 -31 548 C ATOM 874 CD2 LEU A 115 -17.545 -28.366 31.552 1.00 71.35 C ANISOU 874 CD2 LEU A 115 9910 8691 8510 -141 -63 511 C ATOM 875 N VAL A 116 -21.924 -29.155 29.796 1.00 50.69 N ANISOU 875 N VAL A 116 7279 6096 5883 -372 19 536 N ATOM 876 CA VAL A 116 -22.512 -28.127 28.947 1.00 44.72 C ANISOU 876 CA VAL A 116 6457 5388 5148 -388 30 506 C ATOM 877 C VAL A 116 -23.856 -28.656 28.460 1.00 46.48 C ANISOU 877 C VAL A 116 6684 5613 5363 -461 54 513 C ATOM 878 O VAL A 116 -23.915 -29.503 27.562 1.00 50.67 O ANISOU 878 O VAL A 116 7245 6099 5907 -483 57 512 O ATOM 879 CB VAL A 116 -21.592 -27.764 27.776 1.00 39.91 C ANISOU 879 CB VAL A 116 5826 4761 4579 -349 15 474 C ATOM 880 CG1 VAL A 116 -22.151 -26.589 27.014 1.00 34.58 C ANISOU 880 CG1 VAL A 116 5082 4135 3921 -361 24 447 C ATOM 881 CG2 VAL A 116 -20.191 -27.454 28.279 1.00 41.64 C ANISOU 881 CG2 VAL A 116 6048 4971 4804 -280 -8 466 C ATOM 882 N THR A 117 -24.941 -28.155 29.045 1.00 43.04 N ANISOU 882 N THR A 117 6217 5232 4903 -498 72 518 N ATOM 883 CA THR A 117 -26.291 -28.582 28.712 1.00 40.88 C ANISOU 883 CA THR A 117 5943 4973 4618 -569 97 521 C ATOM 884 C THR A 117 -27.090 -27.408 28.160 1.00 40.95 C ANISOU 884 C THR A 117 5876 5044 4637 -581 106 490 C ATOM 885 O THR A 117 -26.704 -26.244 28.287 1.00 38.16 O ANISOU 885 O THR A 117 5476 4727 4295 -539 95 472 O ATOM 886 CB THR A 117 -27.008 -29.172 29.933 1.00 46.74 C ANISOU 886 CB THR A 117 6700 5729 5328 -598 111 541 C ATOM 887 OG1 THR A 117 -27.206 -28.146 30.913 1.00 48.07 O ANISOU 887 OG1 THR A 117 6832 5958 5472 -589 113 544 O ATOM 888 CG2 THR A 117 -26.187 -30.302 30.544 1.00 47.05 C ANISOU 888 CG2 THR A 117 6805 5709 5364 -574 98 566 C ATOM 889 N GLY A 118 -28.229 -27.734 27.546 1.00 41.81 N ANISOU 889 N GLY A 118 5977 5166 4743 -640 125 484 N ATOM 890 CA GLY A 118 -29.063 -26.700 26.958 1.00 40.77 C ANISOU 890 CA GLY A 118 5777 5093 4620 -652 132 454 C ATOM 891 C GLY A 118 -29.720 -25.810 27.996 1.00 43.77 C ANISOU 891 C GLY A 118 6114 5542 4976 -656 138 451 C ATOM 892 O GLY A 118 -29.859 -24.601 27.789 1.00 44.31 O ANISOU 892 O GLY A 118 6124 5655 5057 -632 131 426 O ATOM 893 N THR A 119 -30.134 -26.392 29.124 1.00 44.72 N ANISOU 893 N THR A 119 6263 5669 5060 -687 151 476 N ATOM 894 CA THR A 119 -30.763 -25.602 30.178 1.00 44.89 C ANISOU 894 CA THR A 119 6244 5758 5054 -693 158 472 C ATOM 895 C THR A 119 -29.781 -24.607 30.785 1.00 41.61 C ANISOU 895 C THR A 119 5804 5357 4647 -625 137 466 C ATOM 896 O THR A 119 -30.136 -23.448 31.030 1.00 44.12 O ANISOU 896 O THR A 119 6064 5734 4967 -609 135 443 O ATOM 897 CB THR A 119 -31.328 -26.523 31.261 1.00 48.32 C ANISOU 897 CB THR A 119 6707 6192 5459 -727 173 491 C ATOM 898 OG1 THR A 119 -32.259 -27.439 30.673 1.00 51.96 O ANISOU 898 OG1 THR A 119 7177 6639 5926 -778 189 482 O ATOM 899 CG2 THR A 119 -32.038 -25.713 32.335 1.00 48.99 C ANISOU 899 CG2 THR A 119 6748 6353 5514 -738 182 484 C ATOM 900 N ARG A 120 -28.543 -25.040 31.036 1.00 38.89 N ANISOU 900 N ARG A 120 5505 4961 4310 -583 121 485 N ATOM 901 CA ARG A 120 -27.536 -24.125 31.564 1.00 40.52 C ANISOU 901 CA ARG A 120 5689 5181 4527 -517 101 477 C ATOM 902 C ARG A 120 -27.177 -23.054 30.543 1.00 41.41 C ANISOU 902 C ARG A 120 5752 5304 4680 -481 89 443 C ATOM 903 O ARG A 120 -26.917 -21.902 30.909 1.00 42.11 O ANISOU 903 O ARG A 120 5795 5430 4775 -444 79 425 O ATOM 904 CB ARG A 120 -26.288 -24.901 31.987 1.00 40.83 C ANISOU 904 CB ARG A 120 5787 5162 4564 -480 86 501 C ATOM 905 CG ARG A 120 -26.522 -25.889 33.121 1.00 44.51 C ANISOU 905 CG ARG A 120 6308 5617 4988 -508 95 538 C ATOM 906 CD ARG A 120 -25.306 -26.778 33.335 1.00 46.69 C ANISOU 906 CD ARG A 120 6649 5826 5265 -470 77 561 C ATOM 907 NE ARG A 120 -25.550 -27.803 34.344 1.00 52.42 N ANISOU 907 NE ARG A 120 7426 6533 5956 -494 84 595 N ATOM 908 CZ ARG A 120 -24.709 -28.795 34.618 1.00 55.90 C ANISOU 908 CZ ARG A 120 7926 6916 6399 -466 70 615 C ATOM 909 NH1 ARG A 120 -25.014 -29.685 35.552 1.00 58.87 N ANISOU 909 NH1 ARG A 120 8336 7281 6753 -483 76 639 N ATOM 910 NH2 ARG A 120 -23.565 -28.899 33.957 1.00 55.01 N ANISOU 910 NH2 ARG A 120 7837 6756 6310 -420 48 610 N ATOM 911 N ALA A 121 -27.158 -23.416 29.257 1.00 38.14 N ANISOU 911 N ALA A 121 5346 4855 4290 -493 88 434 N ATOM 912 CA ALA A 121 -26.865 -22.439 28.215 1.00 35.35 C ANISOU 912 CA ALA A 121 4950 4511 3972 -464 77 404 C ATOM 913 C ALA A 121 -27.920 -21.342 28.175 1.00 33.69 C ANISOU 913 C ALA A 121 4677 4365 3759 -478 83 381 C ATOM 914 O ALA A 121 -27.588 -20.155 28.070 1.00 31.16 O ANISOU 914 O ALA A 121 4314 4069 3457 -440 71 360 O ATOM 915 CB ALA A 121 -26.764 -23.135 26.858 1.00 34.24 C ANISOU 915 CB ALA A 121 4831 4325 3853 -481 78 400 C ATOM 916 N ALA A 122 -29.199 -21.719 28.259 1.00 34.18 N ANISOU 916 N ALA A 122 4733 4455 3800 -533 102 383 N ATOM 917 CA ALA A 122 -30.267 -20.724 28.268 1.00 33.82 C ANISOU 917 CA ALA A 122 4626 4474 3749 -546 106 359 C ATOM 918 C ALA A 122 -30.142 -19.794 29.469 1.00 36.08 C ANISOU 918 C ALA A 122 4880 4805 4023 -516 100 353 C ATOM 919 O ALA A 122 -30.426 -18.595 29.368 1.00 36.80 O ANISOU 919 O ALA A 122 4918 4937 4126 -494 92 327 O ATOM 920 CB ALA A 122 -31.630 -21.415 28.265 1.00 29.15 C ANISOU 920 CB ALA A 122 4036 3908 3132 -614 129 360 C ATOM 921 N GLY A 123 -29.719 -20.331 30.616 1.00 32.17 N ANISOU 921 N GLY A 123 4418 4301 3503 -512 103 378 N ATOM 922 CA GLY A 123 -29.502 -19.488 31.778 1.00 31.52 C ANISOU 922 CA GLY A 123 4307 4260 3408 -480 96 372 C ATOM 923 C GLY A 123 -28.333 -18.540 31.595 1.00 30.33 C ANISOU 923 C GLY A 123 4138 4097 3289 -416 74 357 C ATOM 924 O GLY A 123 -28.380 -17.389 32.037 1.00 32.63 O ANISOU 924 O GLY A 123 4381 4431 3585 -388 66 336 O ATOM 925 N ILE A 124 -27.268 -19.009 30.941 1.00 29.27 N ANISOU 925 N ILE A 124 4040 3905 3177 -392 65 366 N ATOM 926 CA ILE A 124 -26.135 -18.138 30.646 1.00 28.17 C ANISOU 926 CA ILE A 124 3884 3753 3068 -335 46 348 C ATOM 927 C ILE A 124 -26.546 -17.043 29.669 1.00 28.83 C ANISOU 927 C ILE A 124 3918 3857 3179 -330 41 319 C ATOM 928 O ILE A 124 -26.161 -15.878 29.826 1.00 30.06 O ANISOU 928 O ILE A 124 4037 4035 3351 -293 29 299 O ATOM 929 CB ILE A 124 -24.952 -18.966 30.111 1.00 27.22 C ANISOU 929 CB ILE A 124 3812 3568 2963 -315 37 361 C ATOM 930 CG1 ILE A 124 -24.426 -19.902 31.202 1.00 31.74 C ANISOU 930 CG1 ILE A 124 4433 4120 3508 -308 37 389 C ATOM 931 CG2 ILE A 124 -23.839 -18.058 29.608 1.00 24.21 C ANISOU 931 CG2 ILE A 124 3409 3175 2614 -264 20 339 C ATOM 932 CD1 ILE A 124 -23.314 -20.820 30.737 1.00 36.72 C ANISOU 932 CD1 ILE A 124 5114 4686 4151 -287 27 400 C ATOM 933 N ILE A 125 -27.341 -17.396 28.654 1.00 28.15 N ANISOU 933 N ILE A 125 3833 3766 3098 -368 49 317 N ATOM 934 CA ILE A 125 -27.781 -16.411 27.669 1.00 27.05 C ANISOU 934 CA ILE A 125 3651 3646 2982 -363 42 291 C ATOM 935 C ILE A 125 -28.614 -15.323 28.336 1.00 27.79 C ANISOU 935 C ILE A 125 3692 3801 3067 -359 41 271 C ATOM 936 O ILE A 125 -28.445 -14.130 28.055 1.00 24.62 O ANISOU 936 O ILE A 125 3254 3415 2687 -327 27 250 O ATOM 937 CB ILE A 125 -28.556 -17.105 26.531 1.00 27.29 C ANISOU 937 CB ILE A 125 3692 3663 3014 -407 52 292 C ATOM 938 CG1 ILE A 125 -27.621 -18.012 25.728 1.00 30.86 C ANISOU 938 CG1 ILE A 125 4191 4053 3481 -403 50 305 C ATOM 939 CG2 ILE A 125 -29.221 -16.078 25.622 1.00 21.03 C ANISOU 939 CG2 ILE A 125 2853 2899 2238 -405 45 266 C ATOM 940 CD1 ILE A 125 -28.322 -18.834 24.669 1.00 29.18 C ANISOU 940 CD1 ILE A 125 3993 3824 3268 -448 61 306 C ATOM 941 N ALA A 126 -29.519 -15.718 29.236 1.00 29.90 N ANISOU 941 N ALA A 126 3954 4104 3301 -392 54 278 N ATOM 942 CA ALA A 126 -30.349 -14.744 29.938 1.00 25.98 C ANISOU 942 CA ALA A 126 3406 3671 2794 -389 53 256 C ATOM 943 C ALA A 126 -29.504 -13.809 30.795 1.00 23.22 C ANISOU 943 C ALA A 126 3037 3333 2452 -338 39 247 C ATOM 944 O ALA A 126 -29.726 -12.592 30.804 1.00 21.87 O ANISOU 944 O ALA A 126 2820 3195 2296 -313 27 220 O ATOM 945 CB ALA A 126 -31.387 -15.469 30.797 1.00 22.62 C ANISOU 945 CB ALA A 126 2983 3283 2328 -437 72 265 C ATOM 946 N ILE A 127 -28.528 -14.361 31.518 1.00 24.97 N ANISOU 946 N ILE A 127 3294 3529 2666 -321 39 268 N ATOM 947 CA ILE A 127 -27.673 -13.538 32.367 1.00 25.56 C ANISOU 947 CA ILE A 127 3351 3616 2746 -273 27 258 C ATOM 948 C ILE A 127 -26.855 -12.566 31.526 1.00 25.09 C ANISOU 948 C ILE A 127 3274 3533 2726 -232 10 238 C ATOM 949 O ILE A 127 -26.701 -11.392 31.883 1.00 24.07 O ANISOU 949 O ILE A 127 3106 3431 2611 -200 -1 215 O ATOM 950 CB ILE A 127 -26.776 -14.436 33.240 1.00 24.50 C ANISOU 950 CB ILE A 127 3261 3456 2592 -263 29 285 C ATOM 951 CG1 ILE A 127 -27.631 -15.218 34.241 1.00 27.05 C ANISOU 951 CG1 ILE A 127 3598 3810 2872 -304 46 304 C ATOM 952 CG2 ILE A 127 -25.720 -13.609 33.961 1.00 26.09 C ANISOU 952 CG2 ILE A 127 3445 3664 2803 -209 15 272 C ATOM 953 CD1 ILE A 127 -26.867 -16.258 35.035 1.00 28.17 C ANISOU 953 CD1 ILE A 127 3794 3921 2989 -299 48 336 C ATOM 954 N CYS A 128 -26.327 -13.033 30.417 1.00 26.28 N ANISOU 954 N CYS A 128 3454 3635 2897 -234 8 246 N ATOM 955 CA CYS A 128 -25.529 -12.193 29.556 1.00 27.46 C ANISOU 955 CA CYS A 128 3591 3761 3081 -201 -5 230 C ATOM 956 C CYS A 128 -26.323 -11.025 28.954 1.00 27.51 C ANISOU 956 C CYS A 128 3553 3795 3104 -201 -13 205 C ATOM 957 O CYS A 128 -25.788 -9.987 28.745 1.00 23.38 O ANISOU 957 O CYS A 128 3008 3270 2604 -168 -25 188 O ATOM 958 CB CYS A 128 -24.809 -13.026 28.505 1.00 26.67 C ANISOU 958 CB CYS A 128 3533 3606 2995 -207 -4 243 C ATOM 959 SG CYS A 128 -23.496 -14.083 29.144 1.00 31.02 S ANISOU 959 SG CYS A 128 4133 4118 3537 -187 -5 263 S ATOM 960 N TRP A 129 -27.587 -11.244 28.648 1.00 23.18 N ANISOU 960 N TRP A 129 2993 3272 2543 -236 -5 204 N ATOM 961 CA TRP A 129 -28.446 -10.194 28.153 1.00 24.06 C ANISOU 961 CA TRP A 129 3062 3415 2667 -234 -14 180 C ATOM 962 C TRP A 129 -28.693 -9.127 29.219 1.00 24.15 C ANISOU 962 C TRP A 129 3030 3471 2675 -209 -22 158 C ATOM 963 O TRP A 129 -28.681 -7.974 28.924 1.00 22.20 O ANISOU 963 O TRP A 129 2754 3232 2449 -182 -37 137 O ATOM 964 CB TRP A 129 -29.732 -10.762 27.598 1.00 24.34 C ANISOU 964 CB TRP A 129 3094 3469 2687 -278 -4 181 C ATOM 965 CG TRP A 129 -29.642 -11.131 26.179 1.00 26.15 C ANISOU 965 CG TRP A 129 3344 3662 2932 -291 -5 186 C ATOM 966 CD1 TRP A 129 -29.519 -12.356 25.680 1.00 26.97 C ANISOU 966 CD1 TRP A 129 3486 3732 3028 -321 7 206 C ATOM 967 CD2 TRP A 129 -29.675 -10.248 25.068 1.00 21.32 C ANISOU 967 CD2 TRP A 129 2714 3041 2344 -275 -19 171 C ATOM 968 NE1 TRP A 129 -29.472 -12.320 24.337 1.00 26.48 N ANISOU 968 NE1 TRP A 129 3430 3646 2984 -325 2 203 N ATOM 969 CE2 TRP A 129 -29.577 -11.029 23.925 1.00 25.04 C ANISOU 969 CE2 TRP A 129 3214 3479 2820 -298 -14 183 C ATOM 970 CE3 TRP A 129 -29.784 -8.872 24.930 1.00 19.27 C ANISOU 970 CE3 TRP A 129 2420 2799 2102 -244 -37 150 C ATOM 971 CZ2 TRP A 129 -29.573 -10.488 22.654 1.00 26.01 C ANISOU 971 CZ2 TRP A 129 3331 3587 2962 -291 -25 175 C ATOM 972 CZ3 TRP A 129 -29.782 -8.337 23.674 1.00 22.16 C ANISOU 972 CZ3 TRP A 129 2784 3148 2489 -237 -49 144 C ATOM 973 CH2 TRP A 129 -29.678 -9.136 22.555 1.00 22.19 C ANISOU 973 CH2 TRP A 129 2816 3120 2494 -260 -42 156 C ATOM 974 N VAL A 130 -28.898 -9.545 30.461 1.00 25.33 N ANISOU 974 N VAL A 130 3179 3651 2796 -217 -13 164 N ATOM 975 CA VAL A 130 -29.089 -8.615 31.553 1.00 23.60 C ANISOU 975 CA VAL A 130 2918 3478 2571 -194 -20 143 C ATOM 976 C VAL A 130 -27.814 -7.796 31.756 1.00 22.50 C ANISOU 976 C VAL A 130 2776 3316 2457 -145 -33 134 C ATOM 977 O VAL A 130 -27.852 -6.617 31.918 1.00 22.91 O ANISOU 977 O VAL A 130 2792 3388 2527 -118 -46 109 O ATOM 978 CB VAL A 130 -29.508 -9.328 32.861 1.00 26.55 C ANISOU 978 CB VAL A 130 3295 3888 2905 -216 -5 154 C ATOM 979 CG1 VAL A 130 -29.379 -8.403 34.051 1.00 24.50 C ANISOU 979 CG1 VAL A 130 2997 3671 2642 -185 -12 133 C ATOM 980 CG2 VAL A 130 -30.913 -9.875 32.767 1.00 24.99 C ANISOU 980 CG2 VAL A 130 3087 3725 2682 -265 9 153 C ATOM 981 N LEU A 131 -26.679 -8.455 31.697 1.00 21.49 N ANISOU 981 N LEU A 131 2687 3145 2333 -136 -30 154 N ATOM 982 CA LEU A 131 -25.391 -7.804 31.832 1.00 23.90 C ANISOU 982 CA LEU A 131 2991 3428 2661 -94 -41 144 C ATOM 983 C LEU A 131 -25.146 -6.817 30.686 1.00 25.41 C ANISOU 983 C LEU A 131 3170 3596 2889 -78 -53 127 C ATOM 984 O LEU A 131 -24.576 -5.786 30.876 1.00 25.49 O ANISOU 984 O LEU A 131 3158 3607 2919 -45 -64 108 O ATOM 985 CB LEU A 131 -24.278 -8.815 31.948 1.00 21.48 C ANISOU 985 CB LEU A 131 2731 3083 2348 -88 -36 167 C ATOM 986 CG LEU A 131 -24.295 -9.616 33.233 1.00 31.21 C ANISOU 986 CG LEU A 131 3978 4336 3546 -94 -27 183 C ATOM 987 CD1 LEU A 131 -23.150 -10.597 33.271 1.00 31.95 C ANISOU 987 CD1 LEU A 131 4119 4386 3635 -83 -26 204 C ATOM 988 CD2 LEU A 131 -24.246 -8.697 34.419 1.00 33.15 C ANISOU 988 CD2 LEU A 131 4184 4626 3785 -67 -33 162 C ATOM 989 N SER A 132 -25.576 -7.176 29.493 1.00 20.54 N ANISOU 989 N SER A 132 2568 2958 2278 -102 -51 136 N ATOM 990 CA SER A 132 -25.438 -6.318 28.351 1.00 20.63 C ANISOU 990 CA SER A 132 2571 2947 2319 -91 -63 124 C ATOM 991 C SER A 132 -26.222 -5.026 28.514 1.00 21.64 C ANISOU 991 C SER A 132 2655 3109 2456 -76 -76 98 C ATOM 992 O SER A 132 -25.731 -3.990 28.167 1.00 20.76 O ANISOU 992 O SER A 132 2532 2984 2371 -51 -88 83 O ATOM 993 CB SER A 132 -25.828 -7.053 27.093 1.00 19.96 C ANISOU 993 CB SER A 132 2511 2838 2234 -122 -57 139 C ATOM 994 OG SER A 132 -24.953 -8.104 26.901 1.00 20.17 O ANISOU 994 OG SER A 132 2578 2829 2258 -129 -48 158 O ATOM 995 N PHE A 133 -27.436 -5.121 29.045 1.00 20.91 N ANISOU 995 N PHE A 133 2539 3062 2343 -93 -73 92 N ATOM 996 CA PHE A 133 -28.245 -3.960 29.288 1.00 22.84 C ANISOU 996 CA PHE A 133 2740 3344 2595 -77 -87 64 C ATOM 997 C PHE A 133 -27.568 -3.062 30.312 1.00 25.72 C ANISOU 997 C PHE A 133 3081 3721 2970 -40 -95 45 C ATOM 998 O PHE A 133 -27.490 -1.894 30.109 1.00 26.87 O ANISOU 998 O PHE A 133 3206 3864 3140 -14 -111 24 O ATOM 999 CB PHE A 133 -29.657 -4.336 29.715 1.00 21.43 C ANISOU 999 CB PHE A 133 2537 3217 2388 -105 -81 57 C ATOM 1000 CG PHE A 133 -30.608 -4.472 28.576 1.00 23.10 C ANISOU 1000 CG PHE A 133 2747 3428 2600 -128 -84 56 C ATOM 1001 CD1 PHE A 133 -31.252 -3.379 28.071 1.00 21.31 C ANISOU 1001 CD1 PHE A 133 2491 3217 2391 -109 -103 32 C ATOM 1002 CD2 PHE A 133 -30.834 -5.686 27.997 1.00 23.01 C ANISOU 1002 CD2 PHE A 133 2767 3402 2574 -166 -68 79 C ATOM 1003 CE1 PHE A 133 -32.124 -3.500 27.028 1.00 22.56 C ANISOU 1003 CE1 PHE A 133 2647 3378 2547 -127 -107 30 C ATOM 1004 CE2 PHE A 133 -31.690 -5.815 26.942 1.00 21.22 C ANISOU 1004 CE2 PHE A 133 2538 3179 2348 -186 -71 76 C ATOM 1005 CZ PHE A 133 -32.338 -4.719 26.456 1.00 23.41 C ANISOU 1005 CZ PHE A 133 2783 3473 2639 -167 -91 52 C ATOM 1006 N ALA A 134 -27.021 -3.645 31.368 1.00 22.66 N ANISOU 1006 N ALA A 134 2702 3342 2564 -38 -85 54 N ATOM 1007 CA ALA A 134 -26.344 -2.900 32.396 1.00 23.43 C ANISOU 1007 CA ALA A 134 2779 3456 2669 -4 -91 35 C ATOM 1008 C ALA A 134 -25.104 -2.195 31.895 1.00 23.95 C ANISOU 1008 C ALA A 134 2854 3479 2767 25 -100 29 C ATOM 1009 O ALA A 134 -24.911 -1.061 32.168 1.00 23.01 O ANISOU 1009 O ALA A 134 2708 3367 2668 52 -112 4 O ATOM 1010 CB ALA A 134 -25.983 -3.817 33.538 1.00 25.50 C ANISOU 1010 CB ALA A 134 3054 3735 2900 -10 -77 50 C ATOM 1011 N ILE A 135 -24.284 -2.892 31.140 1.00 23.92 N ANISOU 1011 N ILE A 135 2889 3430 2769 16 -93 50 N ATOM 1012 CA ILE A 135 -23.090 -2.308 30.595 1.00 24.27 C ANISOU 1012 CA ILE A 135 2943 3436 2842 38 -99 42 C ATOM 1013 C ILE A 135 -23.356 -1.224 29.559 1.00 23.30 C ANISOU 1013 C ILE A 135 2810 3295 2747 43 -112 30 C ATOM 1014 O ILE A 135 -22.875 -0.133 29.677 1.00 22.20 O ANISOU 1014 O ILE A 135 2654 3150 2631 68 -122 9 O ATOM 1015 CB ILE A 135 -22.199 -3.389 29.973 1.00 25.54 C ANISOU 1015 CB ILE A 135 3148 3557 3001 26 -89 66 C ATOM 1016 CG1 ILE A 135 -21.587 -4.235 31.069 1.00 29.58 C ANISOU 1016 CG1 ILE A 135 3672 4077 3489 34 -81 75 C ATOM 1017 CG2 ILE A 135 -21.100 -2.771 29.129 1.00 27.31 C ANISOU 1017 CG2 ILE A 135 3381 3741 3253 41 -94 57 C ATOM 1018 CD1 ILE A 135 -20.867 -5.461 30.604 1.00 28.72 C ANISOU 1018 CD1 ILE A 135 3607 3933 3373 23 -72 98 C ATOM 1019 N GLY A 136 -24.245 -1.521 28.631 1.00 22.80 N ANISOU 1019 N GLY A 136 2755 3228 2680 19 -113 41 N ATOM 1020 CA GLY A 136 -24.555 -0.636 27.542 1.00 22.55 C ANISOU 1020 CA GLY A 136 2720 3178 2671 22 -126 34 C ATOM 1021 C GLY A 136 -25.333 0.581 27.925 1.00 21.59 C ANISOU 1021 C GLY A 136 2560 3083 2559 42 -143 8 C ATOM 1022 O GLY A 136 -25.179 1.602 27.327 1.00 20.87 O ANISOU 1022 O GLY A 136 2467 2971 2493 58 -157 -3 O ATOM 1023 N LEU A 137 -26.164 0.450 28.934 1.00 16.97 N ANISOU 1023 N LEU A 137 1948 2546 1955 42 -142 -3 N ATOM 1024 CA LEU A 137 -26.954 1.579 29.405 1.00 21.01 C ANISOU 1024 CA LEU A 137 2419 3090 2475 64 -159 -33 C ATOM 1025 C LEU A 137 -26.368 2.218 30.659 1.00 21.08 C ANISOU 1025 C LEU A 137 2403 3117 2489 92 -162 -55 C ATOM 1026 O LEU A 137 -27.061 2.983 31.337 1.00 19.66 O ANISOU 1026 O LEU A 137 2184 2974 2310 109 -174 -82 O ATOM 1027 CB LEU A 137 -28.403 1.153 29.649 1.00 21.86 C ANISOU 1027 CB LEU A 137 2504 3246 2557 45 -159 -38 C ATOM 1028 CG LEU A 137 -29.140 0.545 28.449 1.00 22.22 C ANISOU 1028 CG LEU A 137 2567 3281 2595 16 -157 -21 C ATOM 1029 CD1 LEU A 137 -30.598 0.277 28.790 1.00 20.40 C ANISOU 1029 CD1 LEU A 137 2306 3105 2339 -1 -157 -34 C ATOM 1030 CD2 LEU A 137 -29.026 1.428 27.210 1.00 20.79 C ANISOU 1030 CD2 LEU A 137 2397 3062 2442 30 -175 -23 C ATOM 1031 N THR A 138 -25.109 1.921 30.978 1.00 23.45 N ANISOU 1031 N THR A 138 2721 3395 2793 99 -151 -47 N ATOM 1032 CA THR A 138 -24.436 2.596 32.086 1.00 24.20 C ANISOU 1032 CA THR A 138 2794 3506 2897 128 -154 -71 C ATOM 1033 C THR A 138 -24.496 4.120 31.998 1.00 25.81 C ANISOU 1033 C THR A 138 2971 3703 3131 156 -174 -101 C ATOM 1034 O THR A 138 -24.701 4.757 33.046 1.00 22.37 O ANISOU 1034 O THR A 138 2500 3304 2697 177 -181 -129 O ATOM 1035 CB THR A 138 -22.983 2.100 32.181 1.00 23.84 C ANISOU 1035 CB THR A 138 2774 3430 2853 132 -142 -59 C ATOM 1036 OG1 THR A 138 -22.963 0.808 32.799 1.00 24.99 O ANISOU 1036 OG1 THR A 138 2934 3594 2966 116 -127 -38 O ATOM 1037 CG2 THR A 138 -22.121 3.054 32.997 1.00 23.81 C ANISOU 1037 CG2 THR A 138 2747 3431 2867 164 -148 -88 C ATOM 1038 N PRO A 139 -24.350 4.764 30.829 1.00 21.65 N ANISOU 1038 N PRO A 139 2461 3133 2630 157 -185 -99 N ATOM 1039 CA PRO A 139 -24.555 6.223 30.780 1.00 22.70 C ANISOU 1039 CA PRO A 139 2573 3260 2793 183 -206 -127 C ATOM 1040 C PRO A 139 -25.898 6.681 31.332 1.00 23.72 C ANISOU 1040 C PRO A 139 2662 3435 2914 195 -221 -151 C ATOM 1041 O PRO A 139 -25.980 7.784 31.890 1.00 21.72 O ANISOU 1041 O PRO A 139 2381 3193 2680 223 -237 -183 O ATOM 1042 CB PRO A 139 -24.423 6.539 29.285 1.00 21.49 C ANISOU 1042 CB PRO A 139 2452 3055 2658 174 -214 -111 C ATOM 1043 CG PRO A 139 -23.502 5.493 28.774 1.00 21.18 C ANISOU 1043 CG PRO A 139 2449 2990 2610 150 -193 -83 C ATOM 1044 CD PRO A 139 -23.840 4.249 29.541 1.00 22.54 C ANISOU 1044 CD PRO A 139 2616 3200 2749 136 -178 -71 C ATOM 1045 N AMET A 140 -26.955 5.874 31.197 0.71 21.35 N ANISOU 1045 N AMET A 140 2358 3165 2587 173 -217 -139 N ATOM 1046 N BMET A 140 -26.947 5.861 31.203 0.29 21.56 N ANISOU 1046 N BMET A 140 2385 3192 2614 173 -217 -139 N ATOM 1047 CA AMET A 140 -28.257 6.251 31.738 0.71 20.84 C ANISOU 1047 CA AMET A 140 2253 3152 2512 182 -230 -165 C ATOM 1048 CA BMET A 140 -28.259 6.230 31.729 0.29 21.17 C ANISOU 1048 CA BMET A 140 2295 3194 2554 182 -230 -165 C ATOM 1049 C AMET A 140 -28.297 6.201 33.259 0.71 24.74 C ANISOU 1049 C AMET A 140 2712 3700 2990 192 -223 -187 C ATOM 1050 C BMET A 140 -28.240 6.368 33.245 0.29 23.43 C ANISOU 1050 C BMET A 140 2544 3530 2828 196 -226 -190 C ATOM 1051 O AMET A 140 -29.288 6.644 33.850 0.71 22.78 O ANISOU 1051 O AMET A 140 2423 3499 2735 203 -235 -216 O ATOM 1052 O BMET A 140 -29.069 7.090 33.812 0.29 22.05 O ANISOU 1052 O BMET A 140 2329 3395 2655 215 -241 -224 O ATOM 1053 CB AMET A 140 -29.358 5.351 31.164 0.71 18.56 C ANISOU 1053 CB AMET A 140 1969 2885 2198 152 -225 -149 C ATOM 1054 CB BMET A 140 -29.303 5.189 31.323 0.29 19.39 C ANISOU 1054 CB BMET A 140 2074 2995 2299 150 -221 -147 C ATOM 1055 CG AMET A 140 -29.430 5.338 29.640 0.71 20.04 C ANISOU 1055 CG AMET A 140 2190 3027 2398 142 -232 -128 C ATOM 1056 CG BMET A 140 -29.388 4.923 29.833 0.29 20.71 C ANISOU 1056 CG BMET A 140 2277 3119 2473 133 -224 -122 C ATOM 1057 SD AMET A 140 -30.918 4.531 29.003 0.71 24.34 S ANISOU 1057 SD AMET A 140 2729 3605 2915 112 -231 -121 S ATOM 1058 SD BMET A 140 -30.264 6.222 28.950 0.29 22.89 S ANISOU 1058 SD BMET A 140 2539 3385 2773 158 -257 -144 S ATOM 1059 CE AMET A 140 -32.176 5.732 29.435 0.71 23.31 C ANISOU 1059 CE AMET A 140 2545 3520 2791 145 -261 -167 C ATOM 1060 CE BMET A 140 -31.892 6.110 29.688 0.29 23.86 C ANISOU 1060 CE BMET A 140 2611 3585 2870 157 -264 -174 C ATOM 1061 N LEU A 141 -27.300 5.648 33.890 1.00 24.89 N ANISOU 1061 N LEU A 141 2742 3714 3000 189 -206 -175 N ATOM 1062 CA LEU A 141 -27.116 5.570 35.320 1.00 27.91 C ANISOU 1062 CA LEU A 141 3097 4143 3366 199 -199 -192 C ATOM 1063 C LEU A 141 -26.455 6.833 35.882 1.00 30.84 C ANISOU 1063 C LEU A 141 3443 4508 3766 236 -212 -227 C ATOM 1064 O LEU A 141 -26.361 6.988 37.065 1.00 32.55 O ANISOU 1064 O LEU A 141 3630 4765 3972 250 -210 -248 O ATOM 1065 CB LEU A 141 -26.422 4.295 35.763 1.00 31.57 C ANISOU 1065 CB LEU A 141 3586 4607 3801 179 -175 -163 C ATOM 1066 CG LEU A 141 -27.043 2.968 35.354 1.00 35.05 C ANISOU 1066 CG LEU A 141 4052 5053 4210 140 -160 -129 C ATOM 1067 CD1 LEU A 141 -26.434 1.807 36.099 1.00 34.18 C ANISOU 1067 CD1 LEU A 141 3964 4953 4071 125 -140 -105 C ATOM 1068 CD2 LEU A 141 -28.535 2.963 35.492 1.00 32.27 C ANISOU 1068 CD2 LEU A 141 3670 4750 3839 126 -164 -143 C ATOM 1069 N GLY A 142 -26.028 7.730 35.015 1.00 25.58 N ANISOU 1069 N GLY A 142 2792 3792 3136 250 -226 -232 N ATOM 1070 CA GLY A 142 -25.426 8.974 35.419 1.00 23.82 C ANISOU 1070 CA GLY A 142 2549 3556 2944 282 -239 -265 C ATOM 1071 C GLY A 142 -24.106 9.361 34.800 1.00 23.82 C ANISOU 1071 C GLY A 142 2580 3496 2972 286 -236 -257 C ATOM 1072 O GLY A 142 -23.699 10.491 34.886 1.00 24.88 O ANISOU 1072 O GLY A 142 2704 3611 3137 309 -249 -284 O ATOM 1073 N TRP A 143 -23.437 8.414 34.170 1.00 19.72 N ANISOU 1073 N TRP A 143 2100 2949 2444 263 -219 -223 N ATOM 1074 CA TRP A 143 -22.196 8.679 33.443 1.00 15.14 C ANISOU 1074 CA TRP A 143 1551 2314 1887 261 -214 -215 C ATOM 1075 C TRP A 143 -22.540 9.233 32.059 1.00 18.24 C ANISOU 1075 C TRP A 143 1969 2662 2301 253 -227 -203 C ATOM 1076 O TRP A 143 -22.419 8.567 31.031 1.00 21.67 O ANISOU 1076 O TRP A 143 2438 3067 2729 230 -220 -172 O ATOM 1077 CB TRP A 143 -21.352 7.415 33.352 1.00 20.31 C ANISOU 1077 CB TRP A 143 2235 2961 2521 241 -192 -186 C ATOM 1078 CG TRP A 143 -19.912 7.660 33.000 1.00 20.05 C ANISOU 1078 CG TRP A 143 2222 2887 2508 244 -185 -189 C ATOM 1079 CD1 TRP A 143 -19.344 8.848 32.634 1.00 17.99 C ANISOU 1079 CD1 TRP A 143 1962 2594 2281 255 -193 -209 C ATOM 1080 CD2 TRP A 143 -18.854 6.692 32.994 1.00 17.12 C ANISOU 1080 CD2 TRP A 143 1875 2507 2124 234 -167 -172 C ATOM 1081 NE1 TRP A 143 -18.002 8.676 32.394 1.00 19.63 N ANISOU 1081 NE1 TRP A 143 2188 2775 2497 250 -180 -208 N ATOM 1082 CE2 TRP A 143 -17.675 7.363 32.610 1.00 15.93 C ANISOU 1082 CE2 TRP A 143 1732 2320 1999 239 -165 -187 C ATOM 1083 CE3 TRP A 143 -18.791 5.322 33.273 1.00 17.56 C ANISOU 1083 CE3 TRP A 143 1946 2580 2148 222 -154 -148 C ATOM 1084 CZ2 TRP A 143 -16.447 6.711 32.498 1.00 17.82 C ANISOU 1084 CZ2 TRP A 143 1991 2546 2234 235 -150 -181 C ATOM 1085 CZ3 TRP A 143 -17.571 4.676 33.163 1.00 16.42 C ANISOU 1085 CZ3 TRP A 143 1823 2417 2000 220 -141 -141 C ATOM 1086 CH2 TRP A 143 -16.416 5.371 32.779 1.00 15.35 C ANISOU 1086 CH2 TRP A 143 1691 2250 1890 227 -140 -159 C ATOM 1087 N ASN A 144 -22.978 10.490 32.049 1.00 19.72 N ANISOU 1087 N ASN A 144 2138 2841 2513 275 -249 -229 N ATOM 1088 CA ASN A 144 -23.413 11.136 30.818 1.00 22.39 C ANISOU 1088 CA ASN A 144 2498 3138 2870 273 -266 -220 C ATOM 1089 C ASN A 144 -23.113 12.629 30.903 1.00 22.04 C ANISOU 1089 C ASN A 144 2446 3065 2862 298 -284 -250 C ATOM 1090 O ASN A 144 -22.669 13.139 31.935 1.00 22.61 O ANISOU 1090 O ASN A 144 2491 3155 2945 318 -284 -281 O ATOM 1091 CB ASN A 144 -24.902 10.884 30.559 1.00 19.99 C ANISOU 1091 CB ASN A 144 2183 2864 2550 271 -279 -216 C ATOM 1092 CG ASN A 144 -25.783 11.355 31.704 1.00 21.51 C ANISOU 1092 CG ASN A 144 2325 3109 2738 296 -293 -252 C ATOM 1093 OD1 ASN A 144 -25.856 12.544 31.992 1.00 23.32 O ANISOU 1093 OD1 ASN A 144 2536 3331 2993 324 -312 -283 O ATOM 1094 ND2 ASN A 144 -26.468 10.420 32.351 1.00 20.63 N ANISOU 1094 ND2 ASN A 144 2194 3052 2594 284 -282 -250 N ATOM 1095 N ASN A 145 -23.371 13.334 29.802 1.00 24.00 N ANISOU 1095 N ASN A 145 2720 3270 3130 299 -301 -242 N ATOM 1096 CA ASN A 145 -23.170 14.774 29.731 1.00 23.13 C ANISOU 1096 CA ASN A 145 2610 3124 3055 321 -322 -266 C ATOM 1097 C ASN A 145 -24.478 15.552 29.824 1.00 24.07 C ANISOU 1097 C ASN A 145 2706 3258 3182 349 -353 -288 C ATOM 1098 O ASN A 145 -24.515 16.734 29.464 1.00 25.40 O ANISOU 1098 O ASN A 145 2884 3386 3379 367 -375 -301 O ATOM 1099 CB ASN A 145 -22.431 15.143 28.443 1.00 25.71 C ANISOU 1099 CB ASN A 145 2985 3384 3398 302 -320 -242 C ATOM 1100 CG ASN A 145 -21.048 14.531 28.368 1.00 31.96 C ANISOU 1100 CG ASN A 145 3796 4161 4186 277 -291 -229 C ATOM 1101 OD1 ASN A 145 -20.355 14.404 29.378 1.00 34.32 O ANISOU 1101 OD1 ASN A 145 4072 4484 4485 284 -277 -249 O ATOM 1102 ND2 ASN A 145 -20.640 14.144 27.166 1.00 32.08 N ANISOU 1102 ND2 ASN A 145 3853 4140 4197 250 -282 -197 N ATOM 1103 N CYS A 146 -25.552 14.915 30.297 1.00 21.38 N ANISOU 1103 N CYS A 146 2335 2972 2815 352 -356 -293 N ATOM 1104 CA CYS A 146 -26.834 15.607 30.391 1.00 22.33 C ANISOU 1104 CA CYS A 146 2430 3114 2941 380 -386 -318 C ATOM 1105 C CYS A 146 -26.791 16.743 31.404 1.00 30.38 C ANISOU 1105 C CYS A 146 3414 4144 3986 415 -403 -365 C ATOM 1106 O CYS A 146 -27.555 17.707 31.282 1.00 30.28 O ANISOU 1106 O CYS A 146 3390 4123 3991 445 -434 -388 O ATOM 1107 CB CYS A 146 -27.940 14.616 30.747 1.00 26.65 C ANISOU 1107 CB CYS A 146 2948 3726 3452 372 -381 -317 C ATOM 1108 SG CYS A 146 -28.273 13.419 29.430 1.00 37.74 S ANISOU 1108 SG CYS A 146 4392 5118 4831 334 -369 -267 S ATOM 1109 N GLY A 147 -25.910 16.655 32.403 1.00 33.63 N ANISOU 1109 N GLY A 147 3807 4572 4398 415 -384 -380 N ATOM 1110 CA GLY A 147 -25.774 17.734 33.364 1.00 36.68 C ANISOU 1110 CA GLY A 147 4160 4968 4811 447 -398 -426 C ATOM 1111 C GLY A 147 -25.178 19.000 32.787 1.00 38.25 C ANISOU 1111 C GLY A 147 4387 5097 5051 460 -415 -435 C ATOM 1112 O GLY A 147 -25.377 20.079 33.353 1.00 39.99 O ANISOU 1112 O GLY A 147 4582 5316 5296 491 -436 -475 O ATOM 1113 N GLN A 148 -24.463 18.896 31.669 1.00 36.58 N ANISOU 1113 N GLN A 148 4226 4827 4845 435 -406 -399 N ATOM 1114 CA GLN A 148 -23.812 20.038 31.027 1.00 40.40 C ANISOU 1114 CA GLN A 148 4744 5241 5366 439 -417 -401 C ATOM 1115 C GLN A 148 -24.213 20.081 29.557 1.00 38.05 C ANISOU 1115 C GLN A 148 4495 4896 5068 426 -431 -364 C ATOM 1116 O GLN A 148 -23.404 19.788 28.668 1.00 39.88 O ANISOU 1116 O GLN A 148 4768 5087 5297 396 -413 -330 O ATOM 1117 CB GLN A 148 -22.292 19.954 31.174 1.00 51.63 C ANISOU 1117 CB GLN A 148 6181 6639 6796 416 -389 -398 C ATOM 1118 CG GLN A 148 -21.803 19.477 32.539 1.00 63.06 C ANISOU 1118 CG GLN A 148 7586 8143 8233 421 -369 -424 C ATOM 1119 CD GLN A 148 -21.707 17.962 32.635 1.00 69.39 C ANISOU 1119 CD GLN A 148 8386 8985 8994 398 -343 -394 C ATOM 1120 OE1 GLN A 148 -21.384 17.284 31.659 1.00 72.79 O ANISOU 1120 OE1 GLN A 148 8855 9390 9414 369 -330 -356 O ATOM 1121 NE2 GLN A 148 -21.993 17.425 33.816 1.00 69.59 N ANISOU 1121 NE2 GLN A 148 8369 9075 8999 408 -336 -413 N ATOM 1122 N PRO A 149 -25.459 20.443 29.264 1.00 34.80 N ANISOU 1122 N PRO A 149 4075 4491 4655 450 -461 -370 N ATOM 1123 CA PRO A 149 -25.915 20.444 27.873 1.00 33.22 C ANISOU 1123 CA PRO A 149 3919 4252 4450 441 -476 -335 C ATOM 1124 C PRO A 149 -25.362 21.623 27.089 1.00 33.00 C ANISOU 1124 C PRO A 149 3937 4146 4455 444 -492 -328 C ATOM 1125 O PRO A 149 -25.127 22.708 27.625 1.00 32.49 O ANISOU 1125 O PRO A 149 3865 4059 4421 467 -507 -360 O ATOM 1126 CB PRO A 149 -27.439 20.543 28.007 1.00 36.11 C ANISOU 1126 CB PRO A 149 4255 4659 4807 472 -506 -354 C ATOM 1127 CG PRO A 149 -27.643 21.284 29.275 1.00 34.58 C ANISOU 1127 CG PRO A 149 4014 4495 4631 507 -520 -405 C ATOM 1128 CD PRO A 149 -26.523 20.864 30.194 1.00 35.73 C ANISOU 1128 CD PRO A 149 4142 4657 4774 488 -486 -413 C ATOM 1129 N LYS A 150 -25.148 21.387 25.793 1.00 33.72 N ANISOU 1129 N LYS A 150 4079 4195 4538 418 -488 -286 N ATOM 1130 CA LYS A 150 -24.770 22.460 24.882 1.00 36.56 C ANISOU 1130 CA LYS A 150 4490 4480 4922 417 -505 -273 C ATOM 1131 C LYS A 150 -25.971 23.362 24.630 1.00 33.36 C ANISOU 1131 C LYS A 150 4085 4060 4529 460 -552 -286 C ATOM 1132 O LYS A 150 -26.775 23.102 23.730 1.00 31.17 O ANISOU 1132 O LYS A 150 3827 3782 4234 462 -568 -263 O ATOM 1133 CB LYS A 150 -24.231 21.896 23.566 1.00 40.28 C ANISOU 1133 CB LYS A 150 5013 4916 5377 376 -487 -223 C ATOM 1134 CG LYS A 150 -22.951 21.089 23.711 1.00 42.79 C ANISOU 1134 CG LYS A 150 5333 5241 5685 336 -444 -212 C ATOM 1135 CD LYS A 150 -22.293 20.859 22.363 1.00 45.39 C ANISOU 1135 CD LYS A 150 5717 5525 6005 297 -430 -169 C ATOM 1136 CE LYS A 150 -21.070 19.967 22.488 1.00 47.77 C ANISOU 1136 CE LYS A 150 6017 5838 6294 260 -388 -161 C ATOM 1137 NZ LYS A 150 -20.088 20.487 23.479 1.00 52.00 N ANISOU 1137 NZ LYS A 150 6532 6371 6853 262 -374 -195 N ATOM 1138 N GLU A 151 -26.098 24.426 25.425 1.00 41.68 N ANISOU 1138 N GLU A 151 5119 5106 5613 494 -574 -328 N ATOM 1139 CA GLU A 151 -27.297 25.256 25.368 1.00 49.51 C ANISOU 1139 CA GLU A 151 6103 6093 6616 542 -620 -350 C ATOM 1140 C GLU A 151 -27.357 26.066 24.079 1.00 46.69 C ANISOU 1140 C GLU A 151 5809 5659 6271 545 -647 -320 C ATOM 1141 O GLU A 151 -28.441 26.273 23.521 1.00 47.64 O ANISOU 1141 O GLU A 151 5938 5780 6385 573 -682 -317 O ATOM 1142 CB GLU A 151 -27.350 26.176 26.586 1.00 59.65 C ANISOU 1142 CB GLU A 151 7347 7387 7931 578 -637 -405 C ATOM 1143 CG GLU A 151 -28.707 26.233 27.269 1.00 67.81 C ANISOU 1143 CG GLU A 151 8326 8480 8958 623 -666 -444 C ATOM 1144 CD GLU A 151 -29.157 24.882 27.794 1.00 71.46 C ANISOU 1144 CD GLU A 151 8742 9027 9382 608 -641 -444 C ATOM 1145 OE1 GLU A 151 -29.775 24.116 27.025 1.00 74.57 O ANISOU 1145 OE1 GLU A 151 9147 9439 9748 595 -641 -415 O ATOM 1146 OE2 GLU A 151 -28.888 24.585 28.976 1.00 72.61 O ANISOU 1146 OE2 GLU A 151 8841 9222 9525 607 -621 -473 O ATOM 1147 N GLY A 152 -26.207 26.536 23.592 1.00 43.78 N ANISOU 1147 N GLY A 152 5489 5226 5918 515 -632 -299 N ATOM 1148 CA GLY A 152 -26.201 27.303 22.357 1.00 44.00 C ANISOU 1148 CA GLY A 152 5583 5179 5955 513 -655 -267 C ATOM 1149 C GLY A 152 -26.633 26.482 21.159 1.00 42.76 C ANISOU 1149 C GLY A 152 5455 5029 5764 493 -653 -221 C ATOM 1150 O GLY A 152 -27.333 26.977 20.273 1.00 42.50 O ANISOU 1150 O GLY A 152 5458 4963 5729 513 -688 -203 O ATOM 1151 N LYS A 153 -26.222 25.214 21.115 1.00 39.25 N ANISOU 1151 N LYS A 153 4995 4625 5291 455 -614 -202 N ATOM 1152 CA LYS A 153 -26.667 24.337 20.040 1.00 35.57 C ANISOU 1152 CA LYS A 153 4551 4173 4792 436 -611 -162 C ATOM 1153 C LYS A 153 -28.162 24.059 20.145 1.00 34.45 C ANISOU 1153 C LYS A 153 4374 4082 4634 475 -641 -178 C ATOM 1154 O LYS A 153 -28.864 24.010 19.128 1.00 34.11 O ANISOU 1154 O LYS A 153 4357 4028 4574 481 -663 -154 O ATOM 1155 CB LYS A 153 -25.866 23.037 20.067 1.00 35.96 C ANISOU 1155 CB LYS A 153 4590 4255 4817 389 -562 -143 C ATOM 1156 CG LYS A 153 -26.158 22.097 18.916 1.00 32.64 C ANISOU 1156 CG LYS A 153 4194 3845 4364 363 -554 -102 C ATOM 1157 CD LYS A 153 -25.275 20.863 18.989 1.00 35.66 C ANISOU 1157 CD LYS A 153 4568 4255 4728 318 -508 -87 C ATOM 1158 CE LYS A 153 -23.802 21.242 18.982 1.00 43.26 C ANISOU 1158 CE LYS A 153 5556 5174 5707 287 -481 -83 C ATOM 1159 NZ LYS A 153 -22.919 20.043 18.936 1.00 41.26 N ANISOU 1159 NZ LYS A 153 5298 4946 5434 246 -439 -68 N ATOM 1160 N ALA A 154 -28.668 23.891 21.370 1.00 33.42 N ANISOU 1160 N ALA A 154 4182 4009 4506 500 -643 -220 N ATOM 1161 CA ALA A 154 -30.089 23.615 21.554 1.00 35.05 C ANISOU 1161 CA ALA A 154 4350 4272 4697 534 -669 -241 C ATOM 1162 C ALA A 154 -30.942 24.827 21.201 1.00 37.18 C ANISOU 1162 C ALA A 154 4635 4507 4984 584 -722 -257 C ATOM 1163 O ALA A 154 -32.016 24.683 20.605 1.00 36.24 O ANISOU 1163 O ALA A 154 4515 4408 4848 605 -749 -254 O ATOM 1164 CB ALA A 154 -30.355 23.171 22.992 1.00 33.75 C ANISOU 1164 CB ALA A 154 4116 4178 4529 545 -655 -283 C ATOM 1165 N HIS A 155 -30.485 26.029 21.561 1.00 40.06 N ANISOU 1165 N HIS A 155 5016 4821 5386 605 -740 -276 N ATOM 1166 CA HIS A 155 -31.239 27.231 21.222 1.00 47.03 C ANISOU 1166 CA HIS A 155 5918 5662 6288 655 -793 -291 C ATOM 1167 C HIS A 155 -31.222 27.493 19.720 1.00 45.33 C ANISOU 1167 C HIS A 155 5774 5385 6064 646 -810 -242 C ATOM 1168 O HIS A 155 -32.232 27.918 19.149 1.00 48.38 O ANISOU 1168 O HIS A 155 6172 5764 6446 685 -853 -243 O ATOM 1169 CB HIS A 155 -30.687 28.437 21.984 1.00 52.39 C ANISOU 1169 CB HIS A 155 6600 6297 7010 677 -806 -324 C ATOM 1170 CG HIS A 155 -31.064 28.458 23.433 1.00 59.91 C ANISOU 1170 CG HIS A 155 7480 7312 7973 705 -807 -381 C ATOM 1171 ND1 HIS A 155 -32.365 28.612 23.861 1.00 66.48 N ANISOU 1171 ND1 HIS A 155 8265 8192 8801 755 -843 -422 N ATOM 1172 CD2 HIS A 155 -30.310 28.353 24.553 1.00 62.02 C ANISOU 1172 CD2 HIS A 155 7710 7601 8252 691 -776 -408 C ATOM 1173 CE1 HIS A 155 -32.397 28.596 25.181 1.00 68.42 C ANISOU 1173 CE1 HIS A 155 8450 8490 9056 768 -833 -469 C ATOM 1174 NE2 HIS A 155 -31.164 28.439 25.626 1.00 64.94 N ANISOU 1174 NE2 HIS A 155 8015 8034 8625 730 -794 -461 N ATOM 1175 N SER A 156 -30.087 27.240 19.063 1.00 42.41 N ANISOU 1175 N SER A 156 5452 4973 5690 594 -776 -199 N ATOM 1176 CA SER A 156 -29.997 27.484 17.627 1.00 45.74 C ANISOU 1176 CA SER A 156 5942 5337 6100 580 -789 -150 C ATOM 1177 C SER A 156 -30.918 26.562 16.838 1.00 42.65 C ANISOU 1177 C SER A 156 5545 4991 5671 580 -796 -130 C ATOM 1178 O SER A 156 -31.362 26.921 15.741 1.00 42.57 O ANISOU 1178 O SER A 156 5579 4945 5649 592 -825 -102 O ATOM 1179 CB SER A 156 -28.552 27.323 17.152 1.00 48.59 C ANISOU 1179 CB SER A 156 6348 5654 6462 520 -747 -114 C ATOM 1180 OG SER A 156 -28.097 25.995 17.341 1.00 57.46 O ANISOU 1180 OG SER A 156 7441 6831 7561 478 -701 -104 O ATOM 1181 N GLN A 157 -31.217 25.380 17.370 1.00 43.31 N ANISOU 1181 N GLN A 157 5573 5150 5731 566 -769 -142 N ATOM 1182 CA GLN A 157 -32.137 24.451 16.732 1.00 44.52 C ANISOU 1182 CA GLN A 157 5713 5353 5849 565 -773 -129 C ATOM 1183 C GLN A 157 -33.563 24.595 17.245 1.00 42.43 C ANISOU 1183 C GLN A 157 5398 5142 5582 619 -810 -172 C ATOM 1184 O GLN A 157 -34.429 23.801 16.862 1.00 44.03 O ANISOU 1184 O GLN A 157 5579 5396 5755 619 -813 -170 O ATOM 1185 CB GLN A 157 -31.658 23.013 16.929 1.00 50.79 C ANISOU 1185 CB GLN A 157 6481 6197 6619 515 -721 -116 C ATOM 1186 CG GLN A 157 -30.278 22.746 16.366 1.00 57.36 C ANISOU 1186 CG GLN A 157 7359 6985 7450 461 -683 -76 C ATOM 1187 CD GLN A 157 -29.907 21.283 16.429 1.00 65.06 C ANISOU 1187 CD GLN A 157 8313 8009 8400 417 -638 -62 C ATOM 1188 OE1 GLN A 157 -28.760 20.910 16.185 1.00 69.58 O ANISOU 1188 OE1 GLN A 157 8908 8558 8970 374 -603 -39 O ATOM 1189 NE2 GLN A 157 -30.882 20.441 16.755 1.00 65.76 N ANISOU 1189 NE2 GLN A 157 8355 8164 8466 426 -638 -79 N ATOM 1190 N GLY A 158 -33.824 25.580 18.099 1.00 42.92 N ANISOU 1190 N GLY A 158 5438 5196 5673 662 -839 -214 N ATOM 1191 CA GLY A 158 -35.168 25.802 18.594 1.00 45.03 C ANISOU 1191 CA GLY A 158 5656 5515 5938 716 -877 -261 C ATOM 1192 C GLY A 158 -35.675 24.734 19.534 1.00 44.71 C ANISOU 1192 C GLY A 158 5542 5567 5877 705 -851 -292 C ATOM 1193 O GLY A 158 -36.890 24.538 19.639 1.00 49.58 O ANISOU 1193 O GLY A 158 6118 6241 6478 736 -875 -321 O ATOM 1194 N CYS A 159 -34.777 24.034 20.221 1.00 38.84 N ANISOU 1194 N CYS A 159 4782 4843 5133 663 -803 -286 N ATOM 1195 CA CYS A 159 -35.194 23.007 21.163 1.00 39.00 C ANISOU 1195 CA CYS A 159 4738 4948 5132 649 -776 -312 C ATOM 1196 C CYS A 159 -35.946 23.625 22.335 1.00 43.29 C ANISOU 1196 C CYS A 159 5223 5535 5691 696 -802 -374 C ATOM 1197 O CYS A 159 -35.700 24.768 22.730 1.00 43.78 O ANISOU 1197 O CYS A 159 5292 5557 5787 729 -826 -396 O ATOM 1198 CB CYS A 159 -33.985 22.222 21.672 1.00 37.85 C ANISOU 1198 CB CYS A 159 4592 4805 4984 598 -722 -293 C ATOM 1199 SG CYS A 159 -33.115 21.289 20.393 1.00 40.08 S ANISOU 1199 SG CYS A 159 4931 5052 5244 539 -687 -227 S ATOM 1200 N GLY A 160 -36.881 22.859 22.883 1.00 47.03 N ANISOU 1200 N GLY A 160 5641 6090 6137 693 -791 -400 N ATOM 1201 CA GLY A 160 -37.617 23.305 24.045 1.00 48.56 C ANISOU 1201 CA GLY A 160 5790 6328 6331 708 -783 -452 C ATOM 1202 C GLY A 160 -36.777 23.248 25.306 1.00 55.94 C ANISOU 1202 C GLY A 160 6699 7276 7278 692 -752 -469 C ATOM 1203 O GLY A 160 -35.651 22.749 25.327 1.00 54.98 O ANISOU 1203 O GLY A 160 6588 7139 7164 669 -734 -443 O ATOM 1204 N GLU A 161 -37.346 23.778 26.385 1.00 62.90 N ANISOU 1204 N GLU A 161 7547 8191 8163 706 -747 -516 N ATOM 1205 CA GLU A 161 -36.662 23.764 27.670 1.00 69.52 C ANISOU 1205 CA GLU A 161 8358 9048 9008 692 -717 -536 C ATOM 1206 C GLU A 161 -36.475 22.332 28.155 1.00 63.74 C ANISOU 1206 C GLU A 161 7598 8376 8245 649 -674 -520 C ATOM 1207 O GLU A 161 -37.400 21.515 28.095 1.00 61.85 O ANISOU 1207 O GLU A 161 7338 8191 7973 634 -662 -521 O ATOM 1208 CB GLU A 161 -37.441 24.582 28.700 1.00 80.47 C ANISOU 1208 CB GLU A 161 9715 10463 10398 715 -722 -590 C ATOM 1209 CG GLU A 161 -37.197 26.084 28.608 1.00 89.10 C ANISOU 1209 CG GLU A 161 10834 11491 11530 753 -759 -611 C ATOM 1210 CD GLU A 161 -35.771 26.466 28.963 1.00 96.87 C ANISOU 1210 CD GLU A 161 11833 12429 12546 746 -751 -602 C ATOM 1211 OE1 GLU A 161 -35.107 25.694 29.687 1.00100.25 O ANISOU 1211 OE1 GLU A 161 12239 12889 12962 716 -713 -596 O ATOM 1212 OE2 GLU A 161 -35.312 27.538 28.515 1.00100.16 O ANISOU 1212 OE2 GLU A 161 12284 12774 12996 771 -782 -602 O ATOM 1213 N GLY A 162 -35.272 22.031 28.633 1.00 59.95 N ANISOU 1213 N GLY A 162 7119 7886 7774 629 -651 -507 N ATOM 1214 CA GLY A 162 -34.937 20.689 29.052 1.00 53.07 C ANISOU 1214 CA GLY A 162 6228 7062 6874 590 -613 -488 C ATOM 1215 C GLY A 162 -34.560 19.749 27.931 1.00 50.98 C ANISOU 1215 C GLY A 162 5988 6785 6598 569 -614 -443 C ATOM 1216 O GLY A 162 -34.321 18.565 28.196 1.00 52.90 O ANISOU 1216 O GLY A 162 6217 7068 6816 536 -584 -426 O ATOM 1217 N GLN A 163 -34.502 20.229 26.692 1.00 45.30 N ANISOU 1217 N GLN A 163 5311 6007 5893 583 -643 -419 N ATOM 1218 CA GLN A 163 -34.137 19.411 25.547 1.00 40.72 C ANISOU 1218 CA GLN A 163 4778 5399 5295 544 -623 -366 C ATOM 1219 C GLN A 163 -32.744 19.778 25.055 1.00 36.47 C ANISOU 1219 C GLN A 163 4295 4784 4780 525 -608 -332 C ATOM 1220 O GLN A 163 -32.217 20.856 25.343 1.00 37.76 O ANISOU 1220 O GLN A 163 4467 4905 4974 547 -623 -349 O ATOM 1221 CB GLN A 163 -35.144 19.573 24.403 1.00 38.77 C ANISOU 1221 CB GLN A 163 4548 5144 5038 561 -655 -358 C ATOM 1222 CG GLN A 163 -36.509 18.976 24.679 1.00 39.22 C ANISOU 1222 CG GLN A 163 4553 5281 5066 569 -663 -386 C ATOM 1223 CD GLN A 163 -37.436 19.094 23.487 1.00 44.36 C ANISOU 1223 CD GLN A 163 5223 5925 5706 585 -694 -377 C ATOM 1224 OE1 GLN A 163 -37.292 19.997 22.662 1.00 46.27 O ANISOU 1224 OE1 GLN A 163 5507 6105 5969 610 -724 -364 O ATOM 1225 NE2 GLN A 163 -38.389 18.176 23.385 1.00 49.61 N ANISOU 1225 NE2 GLN A 163 5858 6653 6339 570 -686 -383 N ATOM 1226 N VAL A 164 -32.149 18.855 24.303 1.00 26.73 N ANISOU 1226 N VAL A 164 3094 3534 3527 482 -579 -288 N ATOM 1227 CA VAL A 164 -30.851 19.062 23.682 1.00 29.61 C ANISOU 1227 CA VAL A 164 3512 3831 3907 457 -563 -254 C ATOM 1228 C VAL A 164 -30.936 18.606 22.233 1.00 25.86 C ANISOU 1228 C VAL A 164 3082 3328 3415 434 -562 -210 C ATOM 1229 O VAL A 164 -31.827 17.848 21.845 1.00 26.51 O ANISOU 1229 O VAL A 164 3153 3450 3472 428 -564 -204 O ATOM 1230 CB VAL A 164 -29.719 18.306 24.416 1.00 31.42 C ANISOU 1230 CB VAL A 164 3733 4073 4132 424 -519 -247 C ATOM 1231 CG1 VAL A 164 -29.658 18.722 25.877 1.00 33.22 C ANISOU 1231 CG1 VAL A 164 3914 4335 4374 447 -519 -291 C ATOM 1232 CG2 VAL A 164 -29.915 16.802 24.296 1.00 29.21 C ANISOU 1232 CG2 VAL A 164 3445 3838 3816 389 -490 -224 C ATOM 1233 N ALA A 165 -29.999 19.096 21.426 1.00 24.36 N ANISOU 1233 N ALA A 165 2945 3070 3240 419 -559 -182 N ATOM 1234 CA ALA A 165 -29.781 18.536 20.097 1.00 25.47 C ANISOU 1234 CA ALA A 165 3130 3184 3362 388 -550 -137 C ATOM 1235 C ALA A 165 -29.206 17.135 20.258 1.00 27.47 C ANISOU 1235 C ALA A 165 3375 3469 3593 345 -506 -120 C ATOM 1236 O ALA A 165 -28.092 16.969 20.764 1.00 28.83 O ANISOU 1236 O ALA A 165 3549 3630 3774 325 -478 -118 O ATOM 1237 CB ALA A 165 -28.845 19.428 19.288 1.00 28.44 C ANISOU 1237 CB ALA A 165 3563 3483 3759 379 -554 -114 C ATOM 1238 N CYS A 166 -29.964 16.125 19.844 1.00 27.06 N ANISOU 1238 N CYS A 166 3313 3457 3512 331 -500 -108 N ATOM 1239 CA CYS A 166 -29.611 14.733 20.118 1.00 25.29 C ANISOU 1239 CA CYS A 166 3076 3268 3265 294 -462 -95 C ATOM 1240 C CYS A 166 -28.493 14.295 19.179 1.00 24.86 C ANISOU 1240 C CYS A 166 3068 3170 3207 256 -438 -58 C ATOM 1241 O CYS A 166 -28.732 13.960 18.016 1.00 29.73 O ANISOU 1241 O CYS A 166 3713 3775 3809 240 -441 -31 O ATOM 1242 CB CYS A 166 -30.830 13.832 19.977 1.00 30.36 C ANISOU 1242 CB CYS A 166 3692 3965 3878 290 -465 -98 C ATOM 1243 SG CYS A 166 -30.499 12.124 20.424 1.00 36.42 S ANISOU 1243 SG CYS A 166 4445 4774 4617 247 -420 -84 S ATOM 1244 N LEU A 167 -27.265 14.290 19.694 1.00 22.68 N ANISOU 1244 N LEU A 167 2798 2876 2944 242 -414 -58 N ATOM 1245 CA LEU A 167 -26.086 13.838 18.971 1.00 23.58 C ANISOU 1245 CA LEU A 167 2948 2956 3054 205 -387 -29 C ATOM 1246 C LEU A 167 -25.286 12.918 19.881 1.00 24.05 C ANISOU 1246 C LEU A 167 2988 3042 3108 187 -354 -36 C ATOM 1247 O LEU A 167 -25.210 13.152 21.090 1.00 23.83 O ANISOU 1247 O LEU A 167 2927 3036 3090 205 -352 -63 O ATOM 1248 CB LEU A 167 -25.226 15.023 18.515 1.00 24.63 C ANISOU 1248 CB LEU A 167 3118 3029 3213 206 -395 -25 C ATOM 1249 CG LEU A 167 -25.900 15.952 17.502 1.00 25.87 C ANISOU 1249 CG LEU A 167 3305 3150 3374 223 -429 -12 C ATOM 1250 CD1 LEU A 167 -25.142 17.266 17.377 1.00 32.43 C ANISOU 1250 CD1 LEU A 167 4166 3922 4233 229 -440 -15 C ATOM 1251 CD2 LEU A 167 -26.010 15.260 16.152 1.00 19.24 C ANISOU 1251 CD2 LEU A 167 2498 2303 2510 194 -423 23 C ATOM 1252 N PHE A 168 -24.692 11.873 19.296 1.00 25.34 N ANISOU 1252 N PHE A 168 3171 3203 3255 153 -328 -11 N ATOM 1253 CA PHE A 168 -24.030 10.841 20.094 1.00 22.69 C ANISOU 1253 CA PHE A 168 2818 2893 2908 137 -298 -15 C ATOM 1254 C PHE A 168 -22.949 11.437 20.987 1.00 20.50 C ANISOU 1254 C PHE A 168 2532 2603 2652 147 -289 -36 C ATOM 1255 O PHE A 168 -22.958 11.248 22.209 1.00 26.88 O ANISOU 1255 O PHE A 168 3308 3446 3461 161 -284 -57 O ATOM 1256 CB PHE A 168 -23.435 9.761 19.183 1.00 22.06 C ANISOU 1256 CB PHE A 168 2767 2803 2811 101 -275 13 C ATOM 1257 CG PHE A 168 -22.858 8.581 19.932 1.00 20.51 C ANISOU 1257 CG PHE A 168 2558 2634 2603 88 -248 11 C ATOM 1258 CD1 PHE A 168 -21.567 8.623 20.442 1.00 20.16 C ANISOU 1258 CD1 PHE A 168 2515 2577 2570 85 -231 2 C ATOM 1259 CD2 PHE A 168 -23.607 7.431 20.121 1.00 20.31 C ANISOU 1259 CD2 PHE A 168 2518 2644 2553 78 -241 18 C ATOM 1260 CE1 PHE A 168 -21.036 7.541 21.133 1.00 20.76 C ANISOU 1260 CE1 PHE A 168 2581 2675 2632 76 -209 1 C ATOM 1261 CE2 PHE A 168 -23.083 6.344 20.809 1.00 23.73 C ANISOU 1261 CE2 PHE A 168 2944 3097 2973 67 -218 19 C ATOM 1262 CZ PHE A 168 -21.795 6.402 21.315 1.00 20.23 C ANISOU 1262 CZ PHE A 168 2505 2640 2541 68 -203 11 C ATOM 1263 N GLU A 169 -21.999 12.158 20.390 1.00 16.89 N ANISOU 1263 N GLU A 169 2105 2101 2213 137 -287 -30 N ATOM 1264 CA GLU A 169 -20.849 12.639 21.148 1.00 22.67 C ANISOU 1264 CA GLU A 169 2829 2820 2964 140 -274 -51 C ATOM 1265 C GLU A 169 -21.181 13.810 22.062 1.00 23.93 C ANISOU 1265 C GLU A 169 2965 2981 3147 174 -295 -82 C ATOM 1266 O GLU A 169 -20.325 14.208 22.859 1.00 28.72 O ANISOU 1266 O GLU A 169 3558 3586 3769 179 -285 -105 O ATOM 1267 CB GLU A 169 -19.716 13.022 20.194 1.00 23.35 C ANISOU 1267 CB GLU A 169 2954 2859 3059 113 -263 -38 C ATOM 1268 CG GLU A 169 -19.150 11.836 19.424 1.00 19.70 C ANISOU 1268 CG GLU A 169 2511 2398 2575 80 -239 -15 C ATOM 1269 CD GLU A 169 -17.870 12.169 18.684 1.00 28.42 C ANISOU 1269 CD GLU A 169 3646 3465 3688 53 -223 -10 C ATOM 1270 OE1 GLU A 169 -17.194 13.146 19.068 1.00 34.93 O ANISOU 1270 OE1 GLU A 169 4470 4268 4534 58 -223 -29 O ATOM 1271 OE2 GLU A 169 -17.541 11.453 17.716 1.00 30.66 O ANISOU 1271 OE2 GLU A 169 3952 3741 3955 25 -210 12 O ATOM 1272 N ASP A 170 -22.386 14.366 21.973 1.00 18.86 N ANISOU 1272 N ASP A 170 2315 2345 2508 197 -323 -87 N ATOM 1273 CA ASP A 170 -22.796 15.400 22.912 1.00 22.62 C ANISOU 1273 CA ASP A 170 2763 2828 3005 233 -344 -120 C ATOM 1274 C ASP A 170 -23.344 14.828 24.213 1.00 22.30 C ANISOU 1274 C ASP A 170 2673 2849 2953 250 -341 -144 C ATOM 1275 O ASP A 170 -23.251 15.489 25.254 1.00 29.43 O ANISOU 1275 O ASP A 170 3547 3763 3871 274 -347 -176 O ATOM 1276 CB ASP A 170 -23.848 16.319 22.281 1.00 24.90 C ANISOU 1276 CB ASP A 170 3063 3095 3303 255 -380 -119 C ATOM 1277 CG ASP A 170 -23.253 17.278 21.263 1.00 32.76 C ANISOU 1277 CG ASP A 170 4107 4025 4317 246 -389 -103 C ATOM 1278 OD1 ASP A 170 -22.014 17.294 21.109 1.00 35.20 O ANISOU 1278 OD1 ASP A 170 4435 4306 4632 220 -366 -97 O ATOM 1279 OD2 ASP A 170 -24.028 18.026 20.626 1.00 34.64 O ANISOU 1279 OD2 ASP A 170 4363 4237 4560 264 -420 -98 O ATOM 1280 N VAL A 171 -23.913 13.621 24.193 1.00 22.38 N ANISOU 1280 N VAL A 171 2673 2897 2933 237 -330 -129 N ATOM 1281 CA VAL A 171 -24.527 13.060 25.384 1.00 21.71 C ANISOU 1281 CA VAL A 171 2544 2872 2833 249 -326 -149 C ATOM 1282 C VAL A 171 -23.716 11.915 25.988 1.00 20.13 C ANISOU 1282 C VAL A 171 2339 2694 2614 229 -294 -141 C ATOM 1283 O VAL A 171 -23.715 11.759 27.215 1.00 21.68 O ANISOU 1283 O VAL A 171 2502 2930 2806 241 -289 -163 O ATOM 1284 CB VAL A 171 -25.981 12.614 25.108 1.00 22.63 C ANISOU 1284 CB VAL A 171 2647 3022 2928 252 -340 -144 C ATOM 1285 CG1 VAL A 171 -26.841 13.811 24.731 1.00 24.41 C ANISOU 1285 CG1 VAL A 171 2870 3233 3171 282 -376 -159 C ATOM 1286 CG2 VAL A 171 -26.035 11.542 24.028 1.00 20.12 C ANISOU 1286 CG2 VAL A 171 2360 2698 2589 219 -326 -108 C ATOM 1287 N VAL A 172 -23.025 11.122 25.178 1.00 17.32 N ANISOU 1287 N VAL A 172 2016 2317 2249 199 -275 -112 N ATOM 1288 CA VAL A 172 -22.257 9.979 25.665 1.00 18.85 C ANISOU 1288 CA VAL A 172 2210 2528 2426 182 -248 -104 C ATOM 1289 C VAL A 172 -20.827 10.447 25.919 1.00 23.65 C ANISOU 1289 C VAL A 172 2825 3110 3052 183 -236 -116 C ATOM 1290 O VAL A 172 -20.174 10.931 24.982 1.00 20.43 O ANISOU 1290 O VAL A 172 2446 2657 2659 171 -236 -107 O ATOM 1291 CB VAL A 172 -22.282 8.819 24.662 1.00 21.75 C ANISOU 1291 CB VAL A 172 2606 2887 2771 151 -234 -70 C ATOM 1292 CG1 VAL A 172 -21.526 7.618 25.220 1.00 18.80 C ANISOU 1292 CG1 VAL A 172 2233 2531 2380 138 -209 -63 C ATOM 1293 CG2 VAL A 172 -23.717 8.442 24.315 1.00 19.24 C ANISOU 1293 CG2 VAL A 172 2281 2595 2436 148 -247 -61 C ATOM 1294 N PRO A 173 -20.309 10.327 27.142 1.00 22.43 N ANISOU 1294 N PRO A 173 2643 2983 2896 196 -227 -137 N ATOM 1295 CA PRO A 173 -18.937 10.780 27.402 1.00 22.44 C ANISOU 1295 CA PRO A 173 2647 2962 2915 198 -215 -154 C ATOM 1296 C PRO A 173 -17.930 9.892 26.691 1.00 21.21 C ANISOU 1296 C PRO A 173 2521 2787 2749 171 -194 -133 C ATOM 1297 O PRO A 173 -18.116 8.679 26.574 1.00 21.52 O ANISOU 1297 O PRO A 173 2569 2844 2764 158 -184 -112 O ATOM 1298 CB PRO A 173 -18.801 10.669 28.926 1.00 19.30 C ANISOU 1298 CB PRO A 173 2212 2610 2512 220 -211 -180 C ATOM 1299 CG PRO A 173 -20.196 10.467 29.443 1.00 22.45 C ANISOU 1299 CG PRO A 173 2586 3050 2895 231 -224 -182 C ATOM 1300 CD PRO A 173 -20.945 9.781 28.350 1.00 17.88 C ANISOU 1300 CD PRO A 173 2033 2461 2301 209 -225 -149 C ATOM 1301 N AMET A 174 -16.848 10.507 26.217 0.62 17.36 N ANISOU 1301 N AMET A 174 2050 2264 2280 162 -188 -140 N ATOM 1302 N BMET A 174 -16.853 10.518 26.210 0.38 17.95 N ANISOU 1302 N BMET A 174 2126 2339 2356 162 -188 -140 N ATOM 1303 CA AMET A 174 -15.844 9.746 25.488 0.62 19.08 C ANISOU 1303 CA AMET A 174 2295 2465 2490 137 -168 -126 C ATOM 1304 CA BMET A 174 -15.822 9.774 25.495 0.38 19.25 C ANISOU 1304 CA BMET A 174 2316 2486 2512 137 -168 -126 C ATOM 1305 C AMET A 174 -14.933 8.945 26.411 0.62 19.18 C ANISOU 1305 C AMET A 174 2292 2505 2491 144 -151 -139 C ATOM 1306 C BMET A 174 -15.003 8.900 26.434 0.38 19.61 C ANISOU 1306 C BMET A 174 2345 2561 2544 145 -151 -138 C ATOM 1307 O AMET A 174 -14.327 7.967 25.960 0.62 22.03 O ANISOU 1307 O AMET A 174 2670 2862 2837 128 -137 -125 O ATOM 1308 O BMET A 174 -14.527 7.835 26.024 0.38 21.25 O ANISOU 1308 O BMET A 174 2571 2769 2736 129 -138 -122 O ATOM 1309 CB AMET A 174 -15.018 10.678 24.600 0.62 22.07 C ANISOU 1309 CB AMET A 174 2697 2798 2890 121 -165 -130 C ATOM 1310 CB BMET A 174 -14.909 10.736 24.735 0.38 22.04 C ANISOU 1310 CB BMET A 174 2690 2797 2888 123 -165 -134 C ATOM 1311 CG AMET A 174 -14.341 9.971 23.439 0.62 25.95 C ANISOU 1311 CG AMET A 174 3220 3268 3370 89 -150 -108 C ATOM 1312 CG BMET A 174 -15.608 11.500 23.628 0.38 23.74 C ANISOU 1312 CG BMET A 174 2932 2976 3114 112 -181 -116 C ATOM 1313 SD AMET A 174 -15.494 9.107 22.351 0.62 29.79 S ANISOU 1313 SD AMET A 174 3730 3753 3835 73 -156 -68 S ATOM 1314 SD BMET A 174 -16.286 10.409 22.366 0.38 32.20 S ANISOU 1314 SD BMET A 174 4031 4044 4159 88 -179 -75 S ATOM 1315 CE AMET A 174 -16.052 10.449 21.305 0.62 33.63 C ANISOU 1315 CE AMET A 174 4241 4199 4340 66 -176 -58 C ATOM 1316 CE BMET A 174 -14.786 9.692 21.712 0.38 30.97 C ANISOU 1316 CE BMET A 174 3897 3874 3996 58 -152 -71 C ATOM 1317 N ASN A 175 -14.826 9.323 27.689 1.00 20.10 N ANISOU 1317 N ASN A 175 2375 2649 2612 170 -154 -167 N ATOM 1318 CA ASN A 175 -14.083 8.490 28.629 1.00 23.74 C ANISOU 1318 CA ASN A 175 2822 3142 3058 180 -141 -178 C ATOM 1319 C ASN A 175 -14.832 7.197 28.930 1.00 19.92 C ANISOU 1319 C ASN A 175 2340 2686 2543 179 -139 -153 C ATOM 1320 O ASN A 175 -14.203 6.154 29.135 1.00 21.82 O ANISOU 1320 O ASN A 175 2588 2936 2765 177 -127 -146 O ATOM 1321 CB ASN A 175 -13.757 9.261 29.918 1.00 25.50 C ANISOU 1321 CB ASN A 175 3008 3388 3292 208 -144 -215 C ATOM 1322 CG ASN A 175 -14.977 9.916 30.561 1.00 26.75 C ANISOU 1322 CG ASN A 175 3141 3568 3455 227 -162 -224 C ATOM 1323 OD1 ASN A 175 -16.120 9.571 30.272 1.00 31.70 O ANISOU 1323 OD1 ASN A 175 3773 4203 4070 222 -171 -202 O ATOM 1324 ND2 ASN A 175 -14.723 10.864 31.457 1.00 22.54 N ANISOU 1324 ND2 ASN A 175 2577 3047 2938 249 -168 -260 N ATOM 1325 N TYR A 176 -16.167 7.233 28.924 1.00 19.90 N ANISOU 1325 N TYR A 176 2331 2696 2533 180 -151 -141 N ATOM 1326 CA TYR A 176 -16.935 5.992 28.983 1.00 21.08 C ANISOU 1326 CA TYR A 176 2488 2868 2654 170 -147 -114 C ATOM 1327 C TYR A 176 -16.678 5.136 27.748 1.00 17.79 C ANISOU 1327 C TYR A 176 2108 2421 2229 143 -138 -86 C ATOM 1328 O TYR A 176 -16.420 3.931 27.854 1.00 18.58 O ANISOU 1328 O TYR A 176 2221 2529 2308 135 -127 -71 O ATOM 1329 CB TYR A 176 -18.432 6.289 29.118 1.00 16.78 C ANISOU 1329 CB TYR A 176 1927 2343 2104 173 -162 -111 C ATOM 1330 CG TYR A 176 -19.293 5.081 28.801 1.00 19.75 C ANISOU 1330 CG TYR A 176 2317 2734 2453 153 -157 -82 C ATOM 1331 CD1 TYR A 176 -19.557 4.120 29.770 1.00 21.31 C ANISOU 1331 CD1 TYR A 176 2505 2968 2623 154 -149 -76 C ATOM 1332 CD2 TYR A 176 -19.818 4.887 27.525 1.00 18.94 C ANISOU 1332 CD2 TYR A 176 2239 2607 2351 132 -160 -60 C ATOM 1333 CE1 TYR A 176 -20.327 3.009 29.485 1.00 20.64 C ANISOU 1333 CE1 TYR A 176 2434 2893 2514 132 -143 -50 C ATOM 1334 CE2 TYR A 176 -20.585 3.775 27.230 1.00 22.24 C ANISOU 1334 CE2 TYR A 176 2669 3038 2745 112 -154 -36 C ATOM 1335 CZ TYR A 176 -20.837 2.840 28.216 1.00 22.79 C ANISOU 1335 CZ TYR A 176 2728 3141 2789 111 -145 -32 C ATOM 1336 OH TYR A 176 -21.602 1.732 27.932 1.00 25.02 O ANISOU 1336 OH TYR A 176 3024 3435 3047 87 -139 -9 O ATOM 1337 N MET A 177 -16.757 5.746 26.561 1.00 16.54 N ANISOU 1337 N MET A 177 1969 2230 2087 128 -143 -79 N ATOM 1338 CA MET A 177 -16.620 4.994 25.318 1.00 19.39 C ANISOU 1338 CA MET A 177 2362 2566 2440 101 -135 -53 C ATOM 1339 C MET A 177 -15.245 4.356 25.182 1.00 19.80 C ANISOU 1339 C MET A 177 2428 2605 2489 95 -119 -57 C ATOM 1340 O MET A 177 -15.128 3.249 24.643 1.00 20.24 O ANISOU 1340 O MET A 177 2504 2656 2529 79 -110 -38 O ATOM 1341 CB MET A 177 -16.892 5.902 24.118 1.00 19.29 C ANISOU 1341 CB MET A 177 2366 2520 2444 89 -145 -46 C ATOM 1342 CG MET A 177 -18.363 6.203 23.881 1.00 22.88 C ANISOU 1342 CG MET A 177 2815 2982 2895 91 -162 -36 C ATOM 1343 SD MET A 177 -19.359 4.707 23.722 1.00 22.38 S ANISOU 1343 SD MET A 177 2758 2945 2801 75 -157 -10 S ATOM 1344 CE MET A 177 -18.584 3.902 22.319 1.00 22.15 C ANISOU 1344 CE MET A 177 2768 2883 2767 44 -143 12 C ATOM 1345 N VAL A 178 -14.198 5.029 25.653 1.00 17.64 N ANISOU 1345 N VAL A 178 2142 2329 2231 107 -115 -84 N ATOM 1346 CA VAL A 178 -12.834 4.542 25.461 1.00 18.43 C ANISOU 1346 CA VAL A 178 2252 2420 2330 102 -101 -93 C ATOM 1347 C VAL A 178 -12.392 3.639 26.604 1.00 19.84 C ANISOU 1347 C VAL A 178 2419 2629 2492 123 -95 -102 C ATOM 1348 O VAL A 178 -11.933 2.517 26.378 1.00 20.65 O ANISOU 1348 O VAL A 178 2539 2730 2579 117 -87 -91 O ATOM 1349 CB VAL A 178 -11.863 5.727 25.283 1.00 18.89 C ANISOU 1349 CB VAL A 178 2306 2460 2413 101 -98 -121 C ATOM 1350 CG1 VAL A 178 -10.424 5.236 25.338 1.00 18.91 C ANISOU 1350 CG1 VAL A 178 2309 2464 2413 101 -83 -140 C ATOM 1351 CG2 VAL A 178 -12.136 6.443 23.971 1.00 18.25 C ANISOU 1351 CG2 VAL A 178 2247 2344 2345 76 -101 -107 C ATOM 1352 N TYR A 179 -12.504 4.111 27.847 1.00 18.35 N ANISOU 1352 N TYR A 179 2201 2467 2304 148 -101 -121 N ATOM 1353 CA TYR A 179 -11.991 3.336 28.972 1.00 24.66 C ANISOU 1353 CA TYR A 179 2989 3294 3085 170 -97 -130 C ATOM 1354 C TYR A 179 -12.932 2.200 29.349 1.00 22.59 C ANISOU 1354 C TYR A 179 2736 3052 2796 168 -98 -101 C ATOM 1355 O TYR A 179 -12.495 1.062 29.557 1.00 20.16 O ANISOU 1355 O TYR A 179 2443 2747 2468 171 -93 -91 O ATOM 1356 CB TYR A 179 -11.754 4.239 30.184 1.00 26.59 C ANISOU 1356 CB TYR A 179 3198 3566 3339 197 -102 -162 C ATOM 1357 CG TYR A 179 -10.567 5.168 30.065 1.00 26.74 C ANISOU 1357 CG TYR A 179 3206 3571 3381 200 -97 -196 C ATOM 1358 CD1 TYR A 179 -9.372 4.737 29.502 1.00 28.19 C ANISOU 1358 CD1 TYR A 179 3404 3740 3565 192 -86 -204 C ATOM 1359 CD2 TYR A 179 -10.635 6.472 30.536 1.00 25.38 C ANISOU 1359 CD2 TYR A 179 3008 3402 3231 211 -103 -223 C ATOM 1360 CE1 TYR A 179 -8.282 5.586 29.400 1.00 27.07 C ANISOU 1360 CE1 TYR A 179 3252 3591 3445 192 -79 -238 C ATOM 1361 CE2 TYR A 179 -9.552 7.328 30.437 1.00 28.11 C ANISOU 1361 CE2 TYR A 179 3346 3736 3599 211 -97 -255 C ATOM 1362 CZ TYR A 179 -8.378 6.878 29.867 1.00 28.77 C ANISOU 1362 CZ TYR A 179 3444 3808 3681 200 -84 -262 C ATOM 1363 OH TYR A 179 -7.295 7.723 29.765 1.00 31.61 O ANISOU 1363 OH TYR A 179 3793 4158 4061 195 -76 -297 O ATOM 1364 N PHE A 180 -14.226 2.494 29.459 1.00 21.16 N ANISOU 1364 N PHE A 180 2545 2881 2611 163 -106 -90 N ATOM 1365 CA PHE A 180 -15.165 1.506 29.976 1.00 23.42 C ANISOU 1365 CA PHE A 180 2836 3192 2870 159 -106 -67 C ATOM 1366 C PHE A 180 -15.655 0.580 28.868 1.00 25.16 C ANISOU 1366 C PHE A 180 3088 3390 3081 130 -102 -36 C ATOM 1367 O PHE A 180 -15.527 -0.645 28.963 1.00 29.13 O ANISOU 1367 O PHE A 180 3611 3893 3563 124 -95 -18 O ATOM 1368 CB PHE A 180 -16.336 2.223 30.655 1.00 20.77 C ANISOU 1368 CB PHE A 180 2471 2886 2535 167 -116 -74 C ATOM 1369 CG PHE A 180 -17.218 1.323 31.479 1.00 21.34 C ANISOU 1369 CG PHE A 180 2539 2992 2576 164 -115 -58 C ATOM 1370 CD1 PHE A 180 -18.310 0.693 30.906 1.00 20.69 C ANISOU 1370 CD1 PHE A 180 2471 2910 2480 139 -114 -33 C ATOM 1371 CD2 PHE A 180 -16.966 1.122 32.830 1.00 24.63 C ANISOU 1371 CD2 PHE A 180 2938 3444 2976 184 -113 -69 C ATOM 1372 CE1 PHE A 180 -19.130 -0.125 31.655 1.00 26.70 C ANISOU 1372 CE1 PHE A 180 3229 3703 3211 131 -110 -19 C ATOM 1373 CE2 PHE A 180 -17.786 0.304 33.586 1.00 26.66 C ANISOU 1373 CE2 PHE A 180 3194 3733 3202 177 -110 -53 C ATOM 1374 CZ PHE A 180 -18.869 -0.322 32.996 1.00 25.36 C ANISOU 1374 CZ PHE A 180 3045 3567 3024 149 -108 -27 C ATOM 1375 N ASN A 181 -16.200 1.153 27.797 1.00 22.47 N ANISOU 1375 N ASN A 181 2753 3029 2754 113 -107 -30 N ATOM 1376 CA ASN A 181 -16.782 0.325 26.750 1.00 24.84 C ANISOU 1376 CA ASN A 181 3080 3312 3044 86 -104 -2 C ATOM 1377 C ASN A 181 -15.709 -0.357 25.907 1.00 27.25 C ANISOU 1377 C ASN A 181 3413 3588 3351 75 -94 3 C ATOM 1378 O ASN A 181 -15.711 -1.585 25.768 1.00 29.71 O ANISOU 1378 O ASN A 181 3746 3897 3646 64 -87 21 O ATOM 1379 CB ASN A 181 -17.707 1.169 25.879 1.00 26.69 C ANISOU 1379 CB ASN A 181 3312 3538 3292 74 -114 1 C ATOM 1380 CG ASN A 181 -18.538 0.329 24.941 1.00 32.99 C ANISOU 1380 CG ASN A 181 4130 4328 4076 48 -112 27 C ATOM 1381 OD1 ASN A 181 -18.137 0.066 23.809 1.00 35.17 O ANISOU 1381 OD1 ASN A 181 4431 4576 4357 30 -107 37 O ATOM 1382 ND2 ASN A 181 -19.694 -0.118 25.415 1.00 25.76 N ANISOU 1382 ND2 ASN A 181 3205 3440 3143 42 -114 36 N ATOM 1383 N PHE A 182 -14.776 0.415 25.344 1.00 20.80 N ANISOU 1383 N PHE A 182 2598 2751 2555 76 -93 -13 N ATOM 1384 CA PHE A 182 -13.804 -0.168 24.422 1.00 20.39 C ANISOU 1384 CA PHE A 182 2569 2674 2504 63 -84 -11 C ATOM 1385 C PHE A 182 -12.760 -1.001 25.160 1.00 20.52 C ANISOU 1385 C PHE A 182 2588 2699 2510 80 -77 -22 C ATOM 1386 O PHE A 182 -12.633 -2.207 24.923 1.00 25.45 O ANISOU 1386 O PHE A 182 3234 3317 3120 73 -73 -8 O ATOM 1387 CB PHE A 182 -13.130 0.927 23.590 1.00 20.90 C ANISOU 1387 CB PHE A 182 2634 2716 2591 54 -83 -27 C ATOM 1388 CG PHE A 182 -12.140 0.402 22.583 1.00 25.21 C ANISOU 1388 CG PHE A 182 3201 3241 3137 37 -72 -28 C ATOM 1389 CD1 PHE A 182 -12.381 -0.784 21.904 1.00 21.96 C ANISOU 1389 CD1 PHE A 182 2812 2821 2710 21 -68 -7 C ATOM 1390 CD2 PHE A 182 -10.973 1.096 22.311 1.00 25.73 C ANISOU 1390 CD2 PHE A 182 3263 3297 3218 36 -66 -53 C ATOM 1391 CE1 PHE A 182 -11.473 -1.268 20.975 1.00 23.53 C ANISOU 1391 CE1 PHE A 182 3028 3004 2909 6 -59 -12 C ATOM 1392 CE2 PHE A 182 -10.063 0.619 21.383 1.00 27.57 C ANISOU 1392 CE2 PHE A 182 3512 3514 3449 19 -56 -58 C ATOM 1393 CZ PHE A 182 -10.312 -0.565 20.714 1.00 25.28 C ANISOU 1393 CZ PHE A 182 3243 3218 3144 6 -53 -38 C ATOM 1394 N PHE A 183 -11.991 -0.374 26.054 1.00 21.95 N ANISOU 1394 N PHE A 183 2746 2893 2699 104 -78 -49 N ATOM 1395 CA PHE A 183 -10.876 -1.077 26.685 1.00 23.60 C ANISOU 1395 CA PHE A 183 2957 3111 2899 125 -74 -64 C ATOM 1396 C PHE A 183 -11.367 -2.240 27.542 1.00 25.88 C ANISOU 1396 C PHE A 183 3255 3416 3162 135 -76 -44 C ATOM 1397 O PHE A 183 -10.925 -3.383 27.372 1.00 26.43 O ANISOU 1397 O PHE A 183 3347 3476 3218 136 -73 -35 O ATOM 1398 CB PHE A 183 -10.037 -0.109 27.524 1.00 17.55 C ANISOU 1398 CB PHE A 183 2162 2361 2146 149 -75 -99 C ATOM 1399 CG PHE A 183 -9.154 0.807 26.712 1.00 24.23 C ANISOU 1399 CG PHE A 183 3004 3189 3015 138 -69 -123 C ATOM 1400 CD1 PHE A 183 -9.164 0.764 25.327 1.00 27.17 C ANISOU 1400 CD1 PHE A 183 3397 3532 3393 108 -64 -110 C ATOM 1401 CD2 PHE A 183 -8.306 1.706 27.340 1.00 27.56 C ANISOU 1401 CD2 PHE A 183 3400 3622 3450 155 -67 -158 C ATOM 1402 CE1 PHE A 183 -8.352 1.603 24.584 1.00 23.65 C ANISOU 1402 CE1 PHE A 183 2950 3070 2965 93 -57 -130 C ATOM 1403 CE2 PHE A 183 -7.492 2.550 26.603 1.00 26.01 C ANISOU 1403 CE2 PHE A 183 3201 3408 3274 139 -60 -180 C ATOM 1404 CZ PHE A 183 -7.517 2.497 25.223 1.00 26.76 C ANISOU 1404 CZ PHE A 183 3320 3475 3373 108 -55 -165 C ATOM 1405 N ALA A 184 -12.296 -1.972 28.458 1.00 23.39 N ANISOU 1405 N ALA A 184 2923 3126 2838 143 -81 -38 N ATOM 1406 CA ALA A 184 -12.680 -2.978 29.442 1.00 22.26 C ANISOU 1406 CA ALA A 184 2787 3003 2668 153 -82 -22 C ATOM 1407 C ALA A 184 -13.679 -3.983 28.876 1.00 23.92 C ANISOU 1407 C ALA A 184 3025 3202 2863 125 -80 13 C ATOM 1408 O ALA A 184 -13.526 -5.194 29.068 1.00 26.36 O ANISOU 1408 O ALA A 184 3359 3504 3152 125 -77 29 O ATOM 1409 CB ALA A 184 -13.253 -2.298 30.686 1.00 20.77 C ANISOU 1409 CB ALA A 184 2567 2850 2473 170 -87 -31 C ATOM 1410 N CYS A 185 -14.706 -3.504 28.173 1.00 18.06 N ANISOU 1410 N CYS A 185 2279 2456 2129 102 -81 22 N ATOM 1411 CA CYS A 185 -15.836 -4.347 27.801 1.00 22.89 C ANISOU 1411 CA CYS A 185 2908 3066 2724 75 -78 51 C ATOM 1412 C CYS A 185 -15.746 -4.921 26.392 1.00 22.06 C ANISOU 1412 C CYS A 185 2830 2928 2624 51 -74 64 C ATOM 1413 O CYS A 185 -16.490 -5.854 26.075 1.00 23.86 O ANISOU 1413 O CYS A 185 3078 3151 2836 29 -70 86 O ATOM 1414 CB CYS A 185 -17.146 -3.564 27.956 1.00 27.17 C ANISOU 1414 CB CYS A 185 3426 3631 3266 67 -83 52 C ATOM 1415 SG CYS A 185 -17.519 -3.102 29.666 1.00 31.77 S ANISOU 1415 SG CYS A 185 3975 4259 3836 91 -87 38 S ATOM 1416 N VAL A 186 -14.864 -4.402 25.543 1.00 20.09 N ANISOU 1416 N VAL A 186 2582 2656 2393 52 -73 49 N ATOM 1417 CA VAL A 186 -14.688 -4.901 24.184 1.00 26.97 C ANISOU 1417 CA VAL A 186 3478 3500 3270 28 -69 58 C ATOM 1418 C VAL A 186 -13.302 -5.501 23.988 1.00 28.12 C ANISOU 1418 C VAL A 186 3638 3628 3417 39 -65 45 C ATOM 1419 O VAL A 186 -13.165 -6.666 23.600 1.00 25.67 O ANISOU 1419 O VAL A 186 3353 3303 3096 30 -61 57 O ATOM 1420 CB VAL A 186 -14.954 -3.795 23.134 1.00 25.47 C ANISOU 1420 CB VAL A 186 3280 3300 3099 14 -71 53 C ATOM 1421 CG1 VAL A 186 -14.639 -4.299 21.733 1.00 22.28 C ANISOU 1421 CG1 VAL A 186 2899 2870 2697 -10 -66 60 C ATOM 1422 CG2 VAL A 186 -16.392 -3.313 23.212 1.00 22.17 C ANISOU 1422 CG2 VAL A 186 2848 2897 2677 5 -78 65 C ATOM 1423 N LEU A 187 -12.259 -4.722 24.277 1.00 22.55 N ANISOU 1423 N LEU A 187 2762 2543 3262 361 -234 90 N ATOM 1424 CA LEU A 187 -10.893 -5.154 23.992 1.00 25.32 C ANISOU 1424 CA LEU A 187 3091 2860 3669 360 -188 78 C ATOM 1425 C LEU A 187 -10.496 -6.346 24.853 1.00 27.49 C ANISOU 1425 C LEU A 187 3337 3126 3983 375 -193 70 C ATOM 1426 O LEU A 187 -9.958 -7.337 24.346 1.00 28.33 O ANISOU 1426 O LEU A 187 3446 3214 4104 367 -152 57 O ATOM 1427 CB LEU A 187 -9.920 -3.993 24.208 1.00 31.80 C ANISOU 1427 CB LEU A 187 3883 3665 4537 368 -189 84 C ATOM 1428 CG LEU A 187 -8.732 -3.898 23.257 1.00 38.09 C ANISOU 1428 CG LEU A 187 4675 4428 5369 358 -131 81 C ATOM 1429 CD1 LEU A 187 -9.206 -4.023 21.818 1.00 37.66 C ANISOU 1429 CD1 LEU A 187 4667 4381 5263 335 -90 78 C ATOM 1430 CD2 LEU A 187 -8.011 -2.574 23.470 1.00 31.68 C ANISOU 1430 CD2 LEU A 187 3835 3604 4600 366 -143 94 C ATOM 1431 N VAL A 188 -10.740 -6.263 26.163 1.00 23.75 N ANISOU 1431 N VAL A 188 2833 2665 3524 399 -242 76 N ATOM 1432 CA VAL A 188 -10.364 -7.362 27.054 1.00 24.56 C ANISOU 1432 CA VAL A 188 2904 2762 3667 415 -247 69 C ATOM 1433 C VAL A 188 -11.081 -8.661 26.695 1.00 23.72 C ANISOU 1433 C VAL A 188 2816 2667 3530 406 -238 64 C ATOM 1434 O VAL A 188 -10.408 -9.696 26.579 1.00 24.69 O ANISOU 1434 O VAL A 188 2926 2772 3685 401 -206 50 O ATOM 1435 CB VAL A 188 -10.573 -6.951 28.525 1.00 28.19 C ANISOU 1435 CB VAL A 188 3351 3267 4093 415 -276 74 C ATOM 1436 CG1 VAL A 188 -10.487 -8.169 29.436 1.00 31.30 C ANISOU 1436 CG1 VAL A 188 3730 3682 4482 412 -268 68 C ATOM 1437 CG2 VAL A 188 -9.542 -5.910 28.934 1.00 23.92 C ANISOU 1437 CG2 VAL A 188 2796 2719 3575 411 -270 73 C ATOM 1438 N PRO A 189 -12.409 -8.685 26.500 1.00 23.41 N ANISOU 1438 N PRO A 189 2808 2654 3432 403 -265 75 N ATOM 1439 CA PRO A 189 -13.041 -9.951 26.084 1.00 26.86 C ANISOU 1439 CA PRO A 189 3263 3096 3845 395 -258 71 C ATOM 1440 C PRO A 189 -12.531 -10.475 24.752 1.00 24.73 C ANISOU 1440 C PRO A 189 3022 2803 3570 370 -202 55 C ATOM 1441 O PRO A 189 -12.411 -11.694 24.582 1.00 24.66 O ANISOU 1441 O PRO A 189 3011 2786 3572 368 -186 44 O ATOM 1442 CB PRO A 189 -14.533 -9.593 26.019 1.00 24.75 C ANISOU 1442 CB PRO A 189 3029 2857 3516 395 -297 92 C ATOM 1443 CG PRO A 189 -14.683 -8.417 26.913 1.00 24.23 C ANISOU 1443 CG PRO A 189 2946 2808 3452 414 -336 107 C ATOM 1444 CD PRO A 189 -13.418 -7.637 26.746 1.00 21.22 C ANISOU 1444 CD PRO A 189 2549 2403 3111 409 -308 94 C ATOM 1445 N LEU A 190 -12.228 -9.591 23.798 1.00 21.87 N ANISOU 1445 N LEU A 190 2687 2431 3192 354 -173 53 N ATOM 1446 CA LEU A 190 -11.702 -10.048 22.513 1.00 21.21 C ANISOU 1446 CA LEU A 190 2632 2325 3102 336 -117 38 C ATOM 1447 C LEU A 190 -10.317 -10.662 22.669 1.00 23.14 C ANISOU 1447 C LEU A 190 2843 2542 3407 340 -80 26 C ATOM 1448 O LEU A 190 -9.994 -11.653 22.004 1.00 23.59 O ANISOU 1448 O LEU A 190 2914 2584 3465 333 -45 13 O ATOM 1449 CB LEU A 190 -11.666 -8.893 21.515 1.00 20.24 C ANISOU 1449 CB LEU A 190 2540 2200 2951 323 -94 42 C ATOM 1450 CG LEU A 190 -13.008 -8.459 20.919 1.00 25.60 C ANISOU 1450 CG LEU A 190 3265 2901 3562 310 -115 51 C ATOM 1451 CD1 LEU A 190 -12.837 -7.193 20.093 1.00 31.30 C ANISOU 1451 CD1 LEU A 190 4004 3622 4266 297 -93 56 C ATOM 1452 CD2 LEU A 190 -13.604 -9.573 20.072 1.00 24.88 C ANISOU 1452 CD2 LEU A 190 3214 2806 3435 300 -102 42 C ATOM 1453 N LEU A 191 -9.482 -10.084 23.536 1.00 20.63 N ANISOU 1453 N LEU A 191 2483 2215 3140 353 -87 30 N ATOM 1454 CA LEU A 191 -8.183 -10.687 23.816 1.00 23.40 C ANISOU 1454 CA LEU A 191 2799 2537 3553 356 -54 21 C ATOM 1455 C LEU A 191 -8.338 -12.014 24.545 1.00 25.05 C ANISOU 1455 C LEU A 191 2985 2752 3779 363 -68 12 C ATOM 1456 O LEU A 191 -7.523 -12.924 24.356 1.00 28.77 O ANISOU 1456 O LEU A 191 3445 3203 4284 357 -31 1 O ATOM 1457 CB LEU A 191 -7.318 -9.722 24.628 1.00 20.76 C ANISOU 1457 CB LEU A 191 2426 2189 3272 369 -66 30 C ATOM 1458 CG LEU A 191 -6.918 -8.424 23.920 1.00 28.62 C ANISOU 1458 CG LEU A 191 3434 3174 4267 363 -49 40 C ATOM 1459 CD1 LEU A 191 -6.221 -7.471 24.883 1.00 31.98 C ANISOU 1459 CD1 LEU A 191 3818 3587 4746 380 -76 51 C ATOM 1460 CD2 LEU A 191 -6.030 -8.722 22.721 1.00 30.88 C ANISOU 1460 CD2 LEU A 191 3737 3432 4564 351 17 37 C ATOM 1461 N LEU A 192 -9.378 -12.143 25.373 1.00 25.52 N ANISOU 1461 N LEU A 192 3036 2841 3819 375 -120 19 N ATOM 1462 CA LEU A 192 -9.669 -13.425 26.003 1.00 27.33 C ANISOU 1462 CA LEU A 192 3242 3080 4062 383 -136 14 C ATOM 1463 C LEU A 192 -10.070 -14.471 24.968 1.00 26.24 C ANISOU 1463 C LEU A 192 3139 2939 3892 368 -112 4 C ATOM 1464 O LEU A 192 -9.632 -15.624 25.046 1.00 27.73 O ANISOU 1464 O LEU A 192 3309 3119 4109 366 -95 -8 O ATOM 1465 CB LEU A 192 -10.767 -13.257 27.054 1.00 33.03 C ANISOU 1465 CB LEU A 192 3949 3834 4765 405 -197 30 C ATOM 1466 CG LEU A 192 -10.370 -12.551 28.354 1.00 37.55 C ANISOU 1466 CG LEU A 192 4495 4430 5344 410 -215 37 C ATOM 1467 CD1 LEU A 192 -11.576 -12.382 29.264 1.00 39.34 C ANISOU 1467 CD1 LEU A 192 4733 4712 5502 410 -251 54 C ATOM 1468 CD2 LEU A 192 -9.267 -13.320 29.065 1.00 38.92 C ANISOU 1468 CD2 LEU A 192 4636 4602 5549 398 -189 24 C ATOM 1469 N MET A 193 -10.905 -14.090 23.993 1.00 26.81 N ANISOU 1469 N MET A 193 3262 3018 3906 357 -113 8 N ATOM 1470 CA MET A 193 -11.276 -15.025 22.932 1.00 28.63 C ANISOU 1470 CA MET A 193 3531 3243 4105 344 -93 -2 C ATOM 1471 C MET A 193 -10.051 -15.486 22.157 1.00 26.74 C ANISOU 1471 C MET A 193 3297 2973 3892 334 -33 -20 C ATOM 1472 O MET A 193 -9.917 -16.674 21.844 1.00 28.74 O ANISOU 1472 O MET A 193 3552 3217 4150 331 -18 -32 O ATOM 1473 CB MET A 193 -12.278 -14.384 21.972 1.00 31.06 C ANISOU 1473 CB MET A 193 3895 3558 4347 334 -101 6 C ATOM 1474 CG MET A 193 -13.566 -13.913 22.604 1.00 40.19 C ANISOU 1474 CG MET A 193 5055 4744 5472 341 -158 27 C ATOM 1475 SD MET A 193 -14.615 -13.102 21.381 1.00 42.66 S ANISOU 1475 SD MET A 193 5435 5062 5711 323 -159 36 S ATOM 1476 CE MET A 193 -15.647 -12.098 22.447 1.00 38.14 C ANISOU 1476 CE MET A 193 4850 4522 5120 335 -219 65 C ATOM 1477 N LEU A 194 -9.156 -14.551 21.824 1.00 24.72 N ANISOU 1477 N LEU A 194 3041 2700 3651 331 1 -18 N ATOM 1478 CA LEU A 194 -7.915 -14.913 21.149 1.00 28.65 C ANISOU 1478 CA LEU A 194 3539 3167 4177 325 60 -28 C ATOM 1479 C LEU A 194 -7.130 -15.937 21.957 1.00 29.51 C ANISOU 1479 C LEU A 194 3603 3266 4344 329 68 -37 C ATOM 1480 O LEU A 194 -6.612 -16.912 21.400 1.00 27.53 O ANISOU 1480 O LEU A 194 3360 2999 4101 323 104 -49 O ATOM 1481 CB LEU A 194 -7.073 -13.661 20.900 1.00 26.77 C ANISOU 1481 CB LEU A 194 3298 2915 3960 325 87 -17 C ATOM 1482 CG LEU A 194 -5.654 -13.863 20.365 1.00 33.59 C ANISOU 1482 CG LEU A 194 4154 3744 4864 324 147 -19 C ATOM 1483 CD1 LEU A 194 -5.679 -14.567 19.017 1.00 35.21 C ANISOU 1483 CD1 LEU A 194 4408 3940 5031 319 189 -29 C ATOM 1484 CD2 LEU A 194 -4.926 -12.530 20.265 1.00 37.27 C ANISOU 1484 CD2 LEU A 194 4609 4196 5357 327 163 -2 C ATOM 1485 N GLY A 195 -7.082 -15.740 23.264 1.00 32.76 N ANISOU 1485 N GLY A 195 3967 3688 4792 339 33 -30 N ATOM 1486 CA GLY A 195 -6.421 -16.653 24.167 1.00 31.57 C ANISOU 1486 CA GLY A 195 3767 3530 4696 343 36 -38 C ATOM 1487 C GLY A 195 -7.065 -18.027 24.154 1.00 33.92 C ANISOU 1487 C GLY A 195 4065 3841 4980 341 22 -49 C ATOM 1488 O GLY A 195 -6.391 -19.028 24.091 1.00 34.33 O ANISOU 1488 O GLY A 195 4101 3880 5063 335 51 -61 O ATOM 1489 N VAL A 196 -8.384 -18.059 24.215 1.00 28.98 N ANISOU 1489 N VAL A 196 3457 3243 4311 347 -23 -42 N ATOM 1490 CA VAL A 196 -9.099 -19.301 24.164 1.00 28.98 C ANISOU 1490 CA VAL A 196 3458 3255 4299 348 -42 -48 C ATOM 1491 C VAL A 196 -8.884 -19.996 22.826 1.00 32.51 C ANISOU 1491 C VAL A 196 3949 3682 4721 334 -2 -63 C ATOM 1492 O VAL A 196 -8.644 -21.173 22.790 1.00 35.73 O ANISOU 1492 O VAL A 196 4343 4084 5148 332 7 -76 O ATOM 1493 CB VAL A 196 -10.590 -19.113 24.440 1.00 25.99 C ANISOU 1493 CB VAL A 196 3092 2905 3878 358 -100 -31 C ATOM 1494 CG1 VAL A 196 -11.347 -20.388 24.174 1.00 21.75 C ANISOU 1494 CG1 VAL A 196 2562 2374 3326 359 -119 -34 C ATOM 1495 CG2 VAL A 196 -10.816 -18.648 25.863 1.00 23.18 C ANISOU 1495 CG2 VAL A 196 2690 2571 3548 378 -141 -15 C ATOM 1496 N TYR A 197 -8.931 -19.254 21.735 1.00 28.31 N ANISOU 1496 N TYR A 197 3469 3140 4149 328 21 -62 N ATOM 1497 CA TYR A 197 -8.721 -19.851 20.437 1.00 27.15 C ANISOU 1497 CA TYR A 197 3368 2974 3974 320 59 -76 C ATOM 1498 C TYR A 197 -7.312 -20.432 20.309 1.00 30.65 C ANISOU 1498 C TYR A 197 3791 3392 4464 316 113 -88 C ATOM 1499 O TYR A 197 -7.149 -21.491 19.793 1.00 28.92 O ANISOU 1499 O TYR A 197 3584 3163 4242 314 130 -102 O ATOM 1500 CB TYR A 197 -9.113 -18.927 19.277 1.00 26.36 C ANISOU 1500 CB TYR A 197 3328 2870 3819 316 73 -72 C ATOM 1501 CG TYR A 197 -10.599 -18.940 19.006 1.00 25.33 C ANISOU 1501 CG TYR A 197 3233 2758 3635 316 27 -66 C ATOM 1502 CD1 TYR A 197 -11.233 -20.099 18.617 1.00 25.22 C ANISOU 1502 CD1 TYR A 197 3238 2742 3602 318 8 -75 C ATOM 1503 CD2 TYR A 197 -11.369 -17.811 19.186 1.00 25.31 C ANISOU 1503 CD2 TYR A 197 3241 2772 3603 316 -2 -49 C ATOM 1504 CE1 TYR A 197 -12.578 -20.136 18.402 1.00 27.00 C ANISOU 1504 CE1 TYR A 197 3495 2980 3784 318 -37 -65 C ATOM 1505 CE2 TYR A 197 -12.722 -17.834 18.972 1.00 26.65 C ANISOU 1505 CE2 TYR A 197 3443 2957 3727 315 -44 -40 C ATOM 1506 CZ TYR A 197 -13.325 -19.000 18.593 1.00 29.62 C ANISOU 1506 CZ TYR A 197 3839 3328 4088 316 -62 -47 C ATOM 1507 OH TYR A 197 -14.660 -19.038 18.383 1.00 28.64 O ANISOU 1507 OH TYR A 197 3746 3214 3922 315 -106 -33 O ATOM 1508 N LEU A 198 -6.311 -19.755 20.843 1.00 30.47 N ANISOU 1508 N LEU A 198 3735 3357 4484 316 136 -81 N ATOM 1509 CA LEU A 198 -4.959 -20.266 20.787 1.00 31.51 C ANISOU 1509 CA LEU A 198 3847 3463 4664 311 187 -87 C ATOM 1510 C LEU A 198 -4.857 -21.596 21.531 1.00 32.99 C ANISOU 1510 C LEU A 198 3992 3655 4887 308 175 -100 C ATOM 1511 O LEU A 198 -4.220 -22.500 21.074 1.00 33.83 O ANISOU 1511 O LEU A 198 4102 3745 5006 303 211 -111 O ATOM 1512 CB LEU A 198 -3.969 -19.258 21.344 1.00 33.43 C ANISOU 1512 CB LEU A 198 4058 3691 4954 312 205 -73 C ATOM 1513 CG LEU A 198 -3.664 -18.063 20.462 1.00 42.06 C ANISOU 1513 CG LEU A 198 5185 4770 6027 314 234 -60 C ATOM 1514 CD1 LEU A 198 -2.615 -17.171 21.096 1.00 42.63 C ANISOU 1514 CD1 LEU A 198 5219 4823 6156 316 247 -44 C ATOM 1515 CD2 LEU A 198 -3.225 -18.516 19.091 1.00 44.30 C ANISOU 1515 CD2 LEU A 198 5513 5033 6284 313 287 -65 C ATOM 1516 N ARG A 199 -5.496 -21.688 22.678 1.00 33.23 N ANISOU 1516 N ARG A 199 3983 3711 4934 314 125 -96 N ATOM 1517 CA ARG A 199 -5.551 -22.908 23.438 1.00 34.73 C ANISOU 1517 CA ARG A 199 4128 3910 5156 314 107 -105 C ATOM 1518 C ARG A 199 -6.303 -24.005 22.681 1.00 33.21 C ANISOU 1518 C ARG A 199 3966 3725 4928 313 96 -117 C ATOM 1519 O ARG A 199 -5.932 -25.145 22.751 1.00 35.01 O ANISOU 1519 O ARG A 199 4172 3948 5182 308 107 -129 O ATOM 1520 CB ARG A 199 -6.163 -22.663 24.792 1.00 34.90 C ANISOU 1520 CB ARG A 199 4103 3960 5199 327 54 -94 C ATOM 1521 CG ARG A 199 -5.294 -21.831 25.687 1.00 42.10 C ANISOU 1521 CG ARG A 199 4977 4863 6158 331 63 -86 C ATOM 1522 CD ARG A 199 -5.983 -21.578 26.995 1.00 51.66 C ANISOU 1522 CD ARG A 199 6156 6112 7359 339 7 -73 C ATOM 1523 NE ARG A 199 -5.088 -20.876 27.887 1.00 61.61 N ANISOU 1523 NE ARG A 199 7399 7380 8628 324 12 -66 N ATOM 1524 CZ ARG A 199 -4.411 -21.474 28.853 1.00 66.79 C ANISOU 1524 CZ ARG A 199 8028 8055 9293 300 14 -67 C ATOM 1525 NH1 ARG A 199 -4.576 -22.772 29.044 1.00 66.19 N ANISOU 1525 NH1 ARG A 199 7937 7995 9216 289 12 -75 N ATOM 1526 NH2 ARG A 199 -3.585 -20.783 29.631 1.00 67.27 N ANISOU 1526 NH2 ARG A 199 8081 8117 9363 288 16 -61 N ATOM 1527 N ILE A 200 -7.375 -23.665 21.988 1.00 28.24 N ANISOU 1527 N ILE A 200 3385 3104 4241 318 70 -112 N ATOM 1528 CA ILE A 200 -8.108 -24.660 21.231 1.00 31.29 C ANISOU 1528 CA ILE A 200 3803 3491 4593 318 54 -122 C ATOM 1529 C ILE A 200 -7.270 -25.276 20.111 1.00 28.76 C ANISOU 1529 C ILE A 200 3518 3144 4266 312 107 -139 C ATOM 1530 O ILE A 200 -7.228 -26.465 19.965 1.00 28.77 O ANISOU 1530 O ILE A 200 3512 3142 4278 310 106 -153 O ATOM 1531 CB ILE A 200 -9.372 -24.079 20.582 1.00 28.84 C ANISOU 1531 CB ILE A 200 3546 3190 4220 323 20 -111 C ATOM 1532 CG1 ILE A 200 -10.466 -23.830 21.616 1.00 27.59 C ANISOU 1532 CG1 ILE A 200 3359 3062 4063 333 -43 -92 C ATOM 1533 CG2 ILE A 200 -9.884 -25.006 19.501 1.00 28.97 C ANISOU 1533 CG2 ILE A 200 3610 3196 4200 323 15 -124 C ATOM 1534 CD1 ILE A 200 -11.680 -23.125 21.063 1.00 23.92 C ANISOU 1534 CD1 ILE A 200 2944 2604 3538 335 -75 -77 C ATOM 1535 N PHE A 201 -6.592 -24.444 19.347 1.00 30.82 N ANISOU 1535 N PHE A 201 3814 3386 4511 309 154 -137 N ATOM 1536 CA PHE A 201 -5.767 -24.907 18.256 1.00 31.21 C ANISOU 1536 CA PHE A 201 3899 3409 4551 308 208 -150 C ATOM 1537 C PHE A 201 -4.547 -25.680 18.742 1.00 31.20 C ANISOU 1537 C PHE A 201 3852 3394 4608 301 245 -157 C ATOM 1538 O PHE A 201 -4.156 -26.643 18.152 1.00 32.39 O ANISOU 1538 O PHE A 201 4018 3531 4757 300 270 -170 O ATOM 1539 CB PHE A 201 -5.407 -23.761 17.330 1.00 32.82 C ANISOU 1539 CB PHE A 201 4148 3598 4723 312 247 -141 C ATOM 1540 CG PHE A 201 -6.585 -23.190 16.615 1.00 32.65 C ANISOU 1540 CG PHE A 201 4179 3587 4639 317 218 -138 C ATOM 1541 CD1 PHE A 201 -7.357 -23.981 15.801 1.00 35.62 C ANISOU 1541 CD1 PHE A 201 4600 3962 4971 323 199 -151 C ATOM 1542 CD2 PHE A 201 -6.930 -21.886 16.766 1.00 35.76 C ANISOU 1542 CD2 PHE A 201 4578 3992 5019 317 206 -122 C ATOM 1543 CE1 PHE A 201 -8.454 -23.478 15.157 1.00 36.33 C ANISOU 1543 CE1 PHE A 201 4740 4059 5005 326 171 -147 C ATOM 1544 CE2 PHE A 201 -8.023 -21.374 16.121 1.00 36.94 C ANISOU 1544 CE2 PHE A 201 4775 4151 5111 318 180 -119 C ATOM 1545 CZ PHE A 201 -8.790 -22.169 15.317 1.00 34.61 C ANISOU 1545 CZ PHE A 201 4525 3853 4773 322 163 -131 C ATOM 1546 N ALA A 202 -3.960 -25.239 19.829 1.00 33.63 N ANISOU 1546 N ALA A 202 4106 3704 4968 295 247 -147 N ATOM 1547 CA ALA A 202 -2.824 -25.938 20.420 1.00 34.98 C ANISOU 1547 CA ALA A 202 4229 3862 5199 286 280 -151 C ATOM 1548 C ALA A 202 -3.240 -27.297 20.966 1.00 33.18 C ANISOU 1548 C ALA A 202 3966 3651 4990 282 249 -166 C ATOM 1549 O ALA A 202 -2.479 -28.268 20.877 1.00 34.88 O ANISOU 1549 O ALA A 202 4166 3853 5234 273 280 -178 O ATOM 1550 CB ALA A 202 -2.189 -25.087 21.519 1.00 32.01 C ANISOU 1550 CB ALA A 202 3803 3483 4875 282 282 -137 C ATOM 1551 N ALA A 203 -4.434 -27.389 21.514 1.00 35.61 N ANISOU 1551 N ALA A 203 4260 3987 5285 289 188 -164 N ATOM 1552 CA ALA A 203 -4.916 -28.649 22.027 1.00 37.11 C ANISOU 1552 CA ALA A 203 4412 4194 5494 289 154 -174 C ATOM 1553 C ALA A 203 -5.160 -29.604 20.876 1.00 41.79 C ANISOU 1553 C ALA A 203 5051 4776 6052 290 160 -190 C ATOM 1554 O ALA A 203 -4.855 -30.757 20.969 1.00 38.56 O ANISOU 1554 O ALA A 203 4617 4366 5669 284 164 -203 O ATOM 1555 CB ALA A 203 -6.169 -28.458 22.829 1.00 34.69 C ANISOU 1555 CB ALA A 203 4083 3918 5181 301 87 -161 C ATOM 1556 N ALA A 204 -5.727 -29.104 19.796 1.00 40.89 N ANISOU 1556 N ALA A 204 5005 4654 5877 298 157 -189 N ATOM 1557 CA ALA A 204 -5.992 -29.915 18.643 1.00 41.48 C ANISOU 1557 CA ALA A 204 5131 4715 5913 303 160 -204 C ATOM 1558 C ALA A 204 -4.721 -30.436 18.003 1.00 44.39 C ANISOU 1558 C ALA A 204 5512 5058 6295 298 224 -217 C ATOM 1559 O ALA A 204 -4.652 -31.567 17.600 1.00 45.00 O ANISOU 1559 O ALA A 204 5597 5130 6372 299 224 -233 O ATOM 1560 CB ALA A 204 -6.785 -29.131 17.632 1.00 36.15 C ANISOU 1560 CB ALA A 204 4527 4036 5173 314 149 -199 C ATOM 1561 N ARG A 205 -3.729 -29.585 17.877 1.00 45.49 N ANISOU 1561 N ARG A 205 5658 5182 6445 295 277 -207 N ATOM 1562 CA ARG A 205 -2.488 -29.989 17.275 1.00 49.97 C ANISOU 1562 CA ARG A 205 6238 5723 7025 292 341 -213 C ATOM 1563 C ARG A 205 -1.804 -31.039 18.121 1.00 49.39 C ANISOU 1563 C ARG A 205 6102 5651 7012 277 350 -221 C ATOM 1564 O ARG A 205 -1.286 -32.013 17.618 1.00 50.19 O ANISOU 1564 O ARG A 205 6215 5740 7116 275 376 -234 O ATOM 1565 CB ARG A 205 -1.586 -28.786 17.070 1.00 53.57 C ANISOU 1565 CB ARG A 205 6706 6161 7488 292 392 -194 C ATOM 1566 CG ARG A 205 -0.484 -29.003 16.060 1.00 57.96 C ANISOU 1566 CG ARG A 205 7298 6686 8037 298 460 -192 C ATOM 1567 CD ARG A 205 0.545 -27.917 16.231 1.00 62.52 C ANISOU 1567 CD ARG A 205 7862 7246 8647 296 507 -168 C ATOM 1568 NE ARG A 205 0.841 -27.753 17.642 1.00 64.20 N ANISOU 1568 NE ARG A 205 8005 7467 8923 279 490 -161 N ATOM 1569 CZ ARG A 205 1.150 -26.603 18.211 1.00 66.15 C ANISOU 1569 CZ ARG A 205 8227 7709 9196 277 492 -141 C ATOM 1570 NH1 ARG A 205 1.196 -25.508 17.487 1.00 69.98 N ANISOU 1570 NH1 ARG A 205 8751 8185 9653 289 511 -125 N ATOM 1571 NH2 ARG A 205 1.387 -26.547 19.503 1.00 64.33 N ANISOU 1571 NH2 ARG A 205 7935 7486 9022 265 473 -138 N ATOM 1572 N ARG A 206 -1.823 -30.825 19.421 1.00 48.07 N ANISOU 1572 N ARG A 206 5870 5500 6892 267 327 -213 N ATOM 1573 CA ARG A 206 -1.208 -31.745 20.341 1.00 48.95 C ANISOU 1573 CA ARG A 206 5917 5617 7066 252 334 -221 C ATOM 1574 C ARG A 206 -1.892 -33.095 20.311 1.00 50.18 C ANISOU 1574 C ARG A 206 6059 5788 7218 253 295 -239 C ATOM 1575 O ARG A 206 -1.233 -34.111 20.298 1.00 45.39 O ANISOU 1575 O ARG A 206 5432 5175 6640 242 319 -251 O ATOM 1576 CB ARG A 206 -1.190 -31.173 21.728 1.00 54.34 C ANISOU 1576 CB ARG A 206 6535 6314 7795 246 312 -209 C ATOM 1577 CG ARG A 206 -0.719 -32.105 22.803 1.00 64.81 C ANISOU 1577 CG ARG A 206 7788 7651 9186 232 311 -216 C ATOM 1578 CD ARG A 206 -1.182 -31.557 24.135 1.00 78.47 C ANISOU 1578 CD ARG A 206 9476 9421 10917 222 259 -198 C ATOM 1579 NE ARG A 206 -0.644 -32.285 25.272 1.00 87.37 N ANISOU 1579 NE ARG A 206 10558 10579 12061 184 247 -191 N ATOM 1580 CZ ARG A 206 0.433 -31.910 25.946 1.00 92.52 C ANISOU 1580 CZ ARG A 206 11197 11226 12729 155 270 -178 C ATOM 1581 NH1 ARG A 206 1.093 -30.813 25.595 1.00 93.06 N ANISOU 1581 NH1 ARG A 206 11285 11267 12806 161 306 -168 N ATOM 1582 NH2 ARG A 206 0.852 -32.634 26.968 1.00 94.53 N ANISOU 1582 NH2 ARG A 206 11427 11500 12990 120 255 -174 N ATOM 1583 N GLN A 207 -3.201 -33.108 20.220 1.00 48.72 N ANISOU 1583 N GLN A 207 5891 5623 6999 266 235 -239 N ATOM 1584 CA GLN A 207 -3.904 -34.345 20.168 1.00 46.91 C ANISOU 1584 CA GLN A 207 5649 5406 6769 269 193 -252 C ATOM 1585 C GLN A 207 -3.588 -35.122 18.898 1.00 50.51 C ANISOU 1585 C GLN A 207 6160 5839 7192 274 219 -270 C ATOM 1586 O GLN A 207 -3.048 -36.158 18.976 1.00 55.90 O ANISOU 1586 O GLN A 207 6816 6519 7905 265 233 -283 O ATOM 1587 CB GLN A 207 -5.384 -34.118 20.360 1.00 45.01 C ANISOU 1587 CB GLN A 207 5414 5187 6501 284 122 -242 C ATOM 1588 CG GLN A 207 -5.725 -33.839 21.798 1.00 43.55 C ANISOU 1588 CG GLN A 207 5157 5030 6359 284 88 -226 C ATOM 1589 CD GLN A 207 -7.165 -33.478 21.990 1.00 47.29 C ANISOU 1589 CD GLN A 207 5640 5525 6805 300 22 -210 C ATOM 1590 OE1 GLN A 207 -8.011 -33.911 21.244 1.00 51.66 O ANISOU 1590 OE1 GLN A 207 6232 6074 7321 310 -12 -212 O ATOM 1591 NE2 GLN A 207 -7.446 -32.688 23.002 1.00 45.22 N ANISOU 1591 NE2 GLN A 207 5340 5281 6559 305 1 -191 N ATOM 1592 N LEU A 208 -3.770 -34.493 17.754 1.00 48.90 N ANISOU 1592 N LEU A 208 6032 5617 6929 287 234 -269 N ATOM 1593 CA LEU A 208 -3.463 -35.081 16.469 1.00 51.70 C ANISOU 1593 CA LEU A 208 6449 5949 7245 298 261 -284 C ATOM 1594 C LEU A 208 -2.049 -35.622 16.379 1.00 55.01 C ANISOU 1594 C LEU A 208 6854 6351 7697 287 326 -290 C ATOM 1595 O LEU A 208 -1.866 -36.760 16.004 1.00 58.11 O ANISOU 1595 O LEU A 208 7250 6737 8090 288 327 -307 O ATOM 1596 CB LEU A 208 -3.659 -34.062 15.369 1.00 53.94 C ANISOU 1596 CB LEU A 208 6811 6218 7466 314 280 -277 C ATOM 1597 CG LEU A 208 -5.114 -33.721 15.105 1.00 59.98 C ANISOU 1597 CG LEU A 208 7609 6994 8187 326 217 -274 C ATOM 1598 CD1 LEU A 208 -5.212 -32.521 14.194 1.00 62.69 C ANISOU 1598 CD1 LEU A 208 8018 7324 8475 338 241 -265 C ATOM 1599 CD2 LEU A 208 -5.843 -34.905 14.512 1.00 60.36 C ANISOU 1599 CD2 LEU A 208 7684 7038 8213 338 172 -292 C ATOM 1600 N ALA A1001 -0.059 -34.414 18.015 1.00 60.07 N ANISOU 1600 N ALA A1001 7402 6983 8438 253 410 -260 N ATOM 1601 CA ALA A1001 0.756 -35.453 17.511 1.00 61.35 C ANISOU 1601 CA ALA A1001 7572 7129 8608 248 450 -272 C ATOM 1602 C ALA A1001 0.495 -36.735 18.282 1.00 61.86 C ANISOU 1602 C ALA A1001 7576 7215 8714 234 414 -289 C ATOM 1603 O ALA A1001 1.040 -37.729 17.918 1.00 55.13 O ANISOU 1603 O ALA A1001 6725 6352 7869 229 437 -302 O ATOM 1604 CB ALA A1001 2.195 -35.024 17.601 1.00 61.25 C ANISOU 1604 CB ALA A1001 7549 7092 8632 236 523 -256 C ATOM 1605 N ASP A1002 -0.406 -36.742 19.268 1.00 68.46 N ANISOU 1605 N ASP A1002 8361 8079 9571 232 354 -288 N ATOM 1606 CA ASP A1002 -0.528 -37.940 20.095 1.00 65.22 C ANISOU 1606 CA ASP A1002 7881 7689 9209 219 326 -301 C ATOM 1607 C ASP A1002 -1.090 -39.118 19.307 1.00 63.02 C ANISOU 1607 C ASP A1002 7630 7412 8904 229 295 -320 C ATOM 1608 O ASP A1002 -0.643 -40.257 19.488 1.00 61.80 O ANISOU 1608 O ASP A1002 7439 7260 8784 217 302 -334 O ATOM 1609 CB ASP A1002 -1.396 -37.647 21.318 1.00 68.75 C ANISOU 1609 CB ASP A1002 8268 8168 9685 220 268 -291 C ATOM 1610 CG ASP A1002 -0.695 -36.763 22.329 1.00 76.71 C ANISOU 1610 CG ASP A1002 9239 9185 10720 200 291 -270 C ATOM 1611 OD1 ASP A1002 0.554 -36.773 22.363 1.00 78.37 O ANISOU 1611 OD1 ASP A1002 9448 9384 10946 175 344 -264 O ATOM 1612 OD2 ASP A1002 -1.391 -36.061 23.093 1.00 81.23 O ANISOU 1612 OD2 ASP A1002 9794 9782 11286 203 248 -255 O ATOM 1613 N LEU A1003 -2.074 -38.873 18.438 1.00 59.07 N ANISOU 1613 N LEU A1003 7193 6909 8344 252 258 -322 N ATOM 1614 CA LEU A1003 -2.633 -39.964 17.644 1.00 57.88 C ANISOU 1614 CA LEU A1003 7072 6753 8166 265 223 -340 C ATOM 1615 C LEU A1003 -1.585 -40.565 16.718 1.00 57.79 C ANISOU 1615 C LEU A1003 7100 6715 8140 265 280 -355 C ATOM 1616 O LEU A1003 -1.500 -41.791 16.577 1.00 52.08 O ANISOU 1616 O LEU A1003 6362 5993 7432 263 267 -372 O ATOM 1617 CB LEU A1003 -3.838 -39.475 16.840 1.00 57.28 C ANISOU 1617 CB LEU A1003 7063 6674 8027 290 175 -337 C ATOM 1618 CG LEU A1003 -5.159 -39.300 17.589 1.00 59.40 C ANISOU 1618 CG LEU A1003 7297 6968 8304 296 100 -324 C ATOM 1619 CD1 LEU A1003 -6.221 -38.754 16.650 1.00 62.62 C ANISOU 1619 CD1 LEU A1003 7781 7365 8646 317 64 -319 C ATOM 1620 CD2 LEU A1003 -5.611 -40.616 18.203 1.00 58.41 C ANISOU 1620 CD2 LEU A1003 7109 6861 8224 293 48 -331 C ATOM 1621 N GLU A1004 -0.814 -39.707 16.078 1.00 64.87 N ANISOU 1621 N GLU A1004 8048 7590 9009 270 342 -345 N ATOM 1622 CA GLU A1004 0.212 -40.144 15.156 1.00 71.61 C ANISOU 1622 CA GLU A1004 8945 8417 9846 275 402 -353 C ATOM 1623 C GLU A1004 1.376 -40.785 15.874 1.00 71.51 C ANISOU 1623 C GLU A1004 8871 8404 9896 247 447 -353 C ATOM 1624 O GLU A1004 1.998 -41.683 15.349 1.00 70.53 O ANISOU 1624 O GLU A1004 8761 8267 9769 247 475 -365 O ATOM 1625 CB GLU A1004 0.717 -38.993 14.308 1.00 77.62 C ANISOU 1625 CB GLU A1004 9772 9155 10564 290 456 -336 C ATOM 1626 CG GLU A1004 -0.241 -38.564 13.223 1.00 85.13 C ANISOU 1626 CG GLU A1004 10803 10101 11443 321 425 -341 C ATOM 1627 CD GLU A1004 -0.541 -39.658 12.231 1.00 91.72 C ANISOU 1627 CD GLU A1004 11687 10924 12238 342 404 -364 C ATOM 1628 OE1 GLU A1004 0.376 -40.422 11.875 1.00 93.66 O ANISOU 1628 OE1 GLU A1004 11940 11156 12492 343 446 -371 O ATOM 1629 OE2 GLU A1004 -1.705 -39.751 11.812 1.00 94.30 O ANISOU 1629 OE2 GLU A1004 12047 11255 12527 359 344 -373 O ATOM 1630 N ASP A1005 1.696 -40.296 17.062 1.00 70.04 N ANISOU 1630 N ASP A1005 8617 8230 9764 224 456 -339 N ATOM 1631 CA ASP A1005 2.772 -40.884 17.816 1.00 70.95 C ANISOU 1631 CA ASP A1005 8671 8345 9944 196 497 -339 C ATOM 1632 C ASP A1005 2.410 -42.296 18.175 1.00 69.68 C ANISOU 1632 C ASP A1005 8462 8203 9810 186 457 -361 C ATOM 1633 O ASP A1005 3.218 -43.182 18.039 1.00 68.67 O ANISOU 1633 O ASP A1005 8323 8069 9701 172 490 -369 O ATOM 1634 CB ASP A1005 3.067 -40.092 19.075 1.00 74.46 C ANISOU 1634 CB ASP A1005 9053 8802 10434 173 501 -319 C ATOM 1635 CG ASP A1005 3.914 -38.874 18.800 1.00 80.99 C ANISOU 1635 CG ASP A1005 9914 9604 11253 173 557 -294 C ATOM 1636 OD1 ASP A1005 4.378 -38.721 17.660 1.00 82.72 O ANISOU 1636 OD1 ASP A1005 10199 9792 11440 193 604 -293 O ATOM 1637 OD2 ASP A1005 4.104 -38.062 19.721 1.00 82.34 O ANISOU 1637 OD2 ASP A1005 10050 9790 11445 154 550 -273 O ATOM 1638 N ASN A1006 1.180 -42.512 18.614 1.00 66.41 N ANISOU 1638 N ASN A1006 8021 7816 9397 194 382 -367 N ATOM 1639 CA ASN A1006 0.771 -43.850 18.958 1.00 64.47 C ANISOU 1639 CA ASN A1006 7724 7589 9181 188 337 -385 C ATOM 1640 C ASN A1006 0.792 -44.761 17.738 1.00 56.24 C ANISOU 1640 C ASN A1006 6741 6530 8097 204 336 -405 C ATOM 1641 O ASN A1006 1.255 -45.844 17.829 1.00 52.34 O ANISOU 1641 O ASN A1006 6215 6039 7633 190 345 -419 O ATOM 1642 CB ASN A1006 -0.565 -43.859 19.679 1.00 70.38 C ANISOU 1642 CB ASN A1006 8431 8369 9942 198 256 -381 C ATOM 1643 CG ASN A1006 -0.461 -43.325 21.086 1.00 74.73 C ANISOU 1643 CG ASN A1006 8921 8958 10514 164 246 -353 C ATOM 1644 OD1 ASN A1006 0.545 -42.784 21.473 1.00 72.40 O ANISOU 1644 OD1 ASN A1006 8623 8661 10226 138 295 -338 O ATOM 1645 ND2 ASN A1006 -1.516 -43.457 21.842 1.00 80.23 N ANISOU 1645 ND2 ASN A1006 9584 9690 11210 163 177 -340 N ATOM 1646 N TRP A1007 0.357 -44.299 16.576 1.00 56.05 N ANISOU 1646 N TRP A1007 6806 6487 8004 233 330 -405 N ATOM 1647 CA TRP A1007 0.397 -45.157 15.399 1.00 53.17 C ANISOU 1647 CA TRP A1007 6501 6103 7597 252 328 -425 C ATOM 1648 C TRP A1007 1.843 -45.557 15.093 1.00 53.55 C ANISOU 1648 C TRP A1007 6556 6132 7657 239 408 -427 C ATOM 1649 O TRP A1007 2.113 -46.709 14.862 1.00 54.42 O ANISOU 1649 O TRP A1007 6658 6242 7778 237 405 -445 O ATOM 1650 CB TRP A1007 -0.202 -44.467 14.211 1.00 49.03 C ANISOU 1650 CB TRP A1007 6073 5560 6996 287 317 -423 C ATOM 1651 CG TRP A1007 -0.226 -45.278 13.012 1.00 46.14 C ANISOU 1651 CG TRP A1007 5773 5174 6584 312 310 -443 C ATOM 1652 CD1 TRP A1007 0.480 -45.076 11.896 1.00 45.74 C ANISOU 1652 CD1 TRP A1007 5800 5097 6484 333 365 -444 C ATOM 1653 CD2 TRP A1007 -1.035 -46.414 12.780 1.00 48.17 C ANISOU 1653 CD2 TRP A1007 6028 5436 6839 325 240 -464 C ATOM 1654 NE1 TRP A1007 0.169 -46.011 10.967 1.00 51.65 N ANISOU 1654 NE1 TRP A1007 6597 5832 7195 359 335 -466 N ATOM 1655 CE2 TRP A1007 -0.764 -46.853 11.494 1.00 51.84 C ANISOU 1655 CE2 TRP A1007 6574 5874 7250 354 255 -479 C ATOM 1656 CE3 TRP A1007 -1.976 -47.097 13.537 1.00 47.63 C ANISOU 1656 CE3 TRP A1007 5895 5390 6811 318 162 -468 C ATOM 1657 CZ2 TRP A1007 -1.385 -47.949 10.947 1.00 49.15 C ANISOU 1657 CZ2 TRP A1007 6253 5527 6893 374 194 -501 C ATOM 1658 CZ3 TRP A1007 -2.592 -48.170 12.993 1.00 47.35 C ANISOU 1658 CZ3 TRP A1007 5878 5349 6764 337 103 -488 C ATOM 1659 CH2 TRP A1007 -2.301 -48.589 11.711 1.00 45.99 C ANISOU 1659 CH2 TRP A1007 5788 5148 6537 364 117 -505 C ATOM 1660 N GLU A1008 2.770 -44.621 15.168 1.00 51.87 N ANISOU 1660 N GLU A1008 6353 5905 7449 230 476 -406 N ATOM 1661 CA GLU A1008 4.159 -44.937 14.890 1.00 55.51 C ANISOU 1661 CA GLU A1008 6822 6345 7924 218 554 -402 C ATOM 1662 C GLU A1008 4.734 -45.894 15.881 1.00 55.36 C ANISOU 1662 C GLU A1008 6717 6340 7975 182 563 -409 C ATOM 1663 O GLU A1008 5.391 -46.827 15.512 1.00 55.57 O ANISOU 1663 O GLU A1008 6749 6362 8002 174 588 -417 O ATOM 1664 CB GLU A1008 5.040 -43.713 14.954 1.00 58.24 C ANISOU 1664 CB GLU A1008 7182 6671 8274 213 622 -372 C ATOM 1665 CG GLU A1008 4.759 -42.602 13.976 1.00 68.54 C ANISOU 1665 CG GLU A1008 8568 7959 9514 246 633 -359 C ATOM 1666 CD GLU A1008 5.463 -41.317 14.391 1.00 77.46 C ANISOU 1666 CD GLU A1008 9687 9078 10668 236 683 -328 C ATOM 1667 OE1 GLU A1008 6.194 -41.328 15.405 1.00 81.11 O ANISOU 1667 OE1 GLU A1008 10083 9542 11194 203 709 -317 O ATOM 1668 OE2 GLU A1008 5.299 -40.291 13.709 1.00 80.46 O ANISOU 1668 OE2 GLU A1008 10123 9445 11003 260 695 -313 O ATOM 1669 N THR A1009 4.443 -45.661 17.143 1.00 52.76 N ANISOU 1669 N THR A1009 6314 6046 7689 153 530 -397 N ATOM 1670 CA THR A1009 4.960 -46.459 18.221 1.00 51.77 C ANISOU 1670 CA THR A1009 6110 5955 7606 102 522 -388 C ATOM 1671 C THR A1009 4.528 -47.910 18.167 1.00 54.17 C ANISOU 1671 C THR A1009 6385 6276 7922 100 477 -413 C ATOM 1672 O THR A1009 5.309 -48.802 18.438 1.00 54.25 O ANISOU 1672 O THR A1009 6365 6296 7950 64 495 -410 O ATOM 1673 CB THR A1009 4.558 -45.855 19.557 1.00 53.58 C ANISOU 1673 CB THR A1009 6281 6217 7862 74 482 -368 C ATOM 1674 OG1 THR A1009 5.346 -44.688 19.795 1.00 58.70 O ANISOU 1674 OG1 THR A1009 6943 6850 8510 61 529 -340 O ATOM 1675 CG2 THR A1009 4.777 -46.840 20.659 1.00 52.33 C ANISOU 1675 CG2 THR A1009 6065 6088 7731 23 448 -362 C ATOM 1676 N LEU A1010 3.279 -48.153 17.823 1.00 50.80 N ANISOU 1676 N LEU A1010 5968 5849 7484 136 415 -436 N ATOM 1677 CA LEU A1010 2.810 -49.511 17.712 1.00 48.05 C ANISOU 1677 CA LEU A1010 5593 5513 7149 139 365 -459 C ATOM 1678 C LEU A1010 3.590 -50.209 16.599 1.00 47.17 C ANISOU 1678 C LEU A1010 5539 5371 7013 152 411 -477 C ATOM 1679 O LEU A1010 4.059 -51.304 16.769 1.00 44.29 O ANISOU 1679 O LEU A1010 5139 5022 6668 127 411 -483 O ATOM 1680 CB LEU A1010 1.329 -49.502 17.394 1.00 50.17 C ANISOU 1680 CB LEU A1010 5879 5778 7405 181 287 -475 C ATOM 1681 CG LEU A1010 0.616 -50.781 16.996 1.00 54.49 C ANISOU 1681 CG LEU A1010 6420 6332 7951 196 219 -496 C ATOM 1682 CD1 LEU A1010 0.689 -51.770 18.133 1.00 56.97 C ANISOU 1682 CD1 LEU A1010 6635 6692 8318 153 190 -488 C ATOM 1683 CD2 LEU A1010 -0.826 -50.449 16.693 1.00 53.11 C ANISOU 1683 CD2 LEU A1010 6278 6160 7742 227 139 -492 C ATOM 1684 N ASN A1011 3.752 -49.533 15.477 1.00 44.57 N ANISOU 1684 N ASN A1011 5302 5004 6627 186 446 -477 N ATOM 1685 CA ASN A1011 4.484 -50.058 14.350 1.00 49.24 C ANISOU 1685 CA ASN A1011 5961 5569 7178 202 489 -486 C ATOM 1686 C ASN A1011 5.967 -50.289 14.617 1.00 49.13 C ANISOU 1686 C ASN A1011 5924 5553 7191 167 568 -469 C ATOM 1687 O ASN A1011 6.536 -51.250 14.150 1.00 45.36 O ANISOU 1687 O ASN A1011 5459 5071 6706 165 587 -479 O ATOM 1688 CB ASN A1011 4.241 -49.212 13.125 1.00 51.83 C ANISOU 1688 CB ASN A1011 6396 5872 7426 244 499 -479 C ATOM 1689 CG ASN A1011 2.850 -49.395 12.588 1.00 57.01 C ANISOU 1689 CG ASN A1011 7089 6532 8040 277 413 -495 C ATOM 1690 OD1 ASN A1011 2.233 -50.422 12.797 1.00 56.40 O ANISOU 1690 OD1 ASN A1011 6975 6469 7984 275 350 -515 O ATOM 1691 ND2 ASN A1011 2.352 -48.402 11.898 1.00 61.14 N ANISOU 1691 ND2 ASN A1011 7683 7042 8506 305 408 -486 N ATOM 1692 N ASP A1012 6.583 -49.392 15.362 1.00 49.61 N ANISOU 1692 N ASP A1012 5955 5624 7272 135 606 -436 N ATOM 1693 CA ASP A1012 7.977 -49.524 15.688 1.00 49.81 C ANISOU 1693 CA ASP A1012 5959 5651 7315 92 669 -408 C ATOM 1694 C ASP A1012 8.177 -50.674 16.628 1.00 47.82 C ANISOU 1694 C ASP A1012 5627 5433 7108 42 641 -412 C ATOM 1695 O ASP A1012 9.126 -51.404 16.496 1.00 45.66 O ANISOU 1695 O ASP A1012 5352 5156 6841 17 677 -406 O ATOM 1696 CB ASP A1012 8.517 -48.263 16.320 1.00 53.62 C ANISOU 1696 CB ASP A1012 6428 6132 7812 69 703 -372 C ATOM 1697 CG ASP A1012 8.586 -47.119 15.356 1.00 60.63 C ANISOU 1697 CG ASP A1012 7396 6985 8656 112 743 -360 C ATOM 1698 OD1 ASP A1012 8.531 -47.336 14.146 1.00 63.32 O ANISOU 1698 OD1 ASP A1012 7809 7299 8949 154 760 -374 O ATOM 1699 OD2 ASP A1012 8.672 -45.986 15.815 1.00 62.88 O ANISOU 1699 OD2 ASP A1012 7672 7268 8951 105 754 -337 O ATOM 1700 N ASN A1013 7.294 -50.822 17.594 1.00 44.72 N ANISOU 1700 N ASN A1013 5174 5073 6746 26 574 -419 N ATOM 1701 CA ASN A1013 7.426 -51.938 18.520 1.00 45.45 C ANISOU 1701 CA ASN A1013 5207 5191 6873 -25 536 -420 C ATOM 1702 C ASN A1013 7.122 -53.279 17.866 1.00 47.64 C ANISOU 1702 C ASN A1013 5479 5474 7147 -7 511 -451 C ATOM 1703 O ASN A1013 7.607 -54.310 18.344 1.00 47.91 O ANISOU 1703 O ASN A1013 5486 5516 7200 -49 500 -451 O ATOM 1704 CB ASN A1013 6.528 -51.717 19.735 1.00 46.40 C ANISOU 1704 CB ASN A1013 5289 5335 7006 -41 463 -413 C ATOM 1705 CG ASN A1013 7.145 -50.772 20.749 1.00 51.48 C ANISOU 1705 CG ASN A1013 5947 5965 7647 -69 475 -383 C ATOM 1706 OD1 ASN A1013 8.354 -50.793 20.974 1.00 52.59 O ANISOU 1706 OD1 ASN A1013 6115 6079 7788 -92 513 -368 O ATOM 1707 ND2 ASN A1013 6.316 -49.938 21.365 1.00 52.36 N ANISOU 1707 ND2 ASN A1013 6049 6091 7753 -57 436 -374 N ATOM 1708 N LEU A1014 6.335 -53.296 16.788 1.00 46.76 N ANISOU 1708 N LEU A1014 5415 5346 7007 55 493 -479 N ATOM 1709 CA LEU A1014 6.173 -54.533 16.032 1.00 46.84 C ANISOU 1709 CA LEU A1014 5440 5349 7008 77 469 -510 C ATOM 1710 C LEU A1014 7.449 -54.898 15.286 1.00 49.56 C ANISOU 1710 C LEU A1014 5832 5670 7327 72 543 -505 C ATOM 1711 O LEU A1014 7.760 -56.086 15.136 1.00 48.06 O ANISOU 1711 O LEU A1014 5624 5488 7147 60 536 -519 O ATOM 1712 CB LEU A1014 5.001 -54.413 15.058 1.00 47.09 C ANISOU 1712 CB LEU A1014 5534 5353 7003 142 417 -539 C ATOM 1713 CG LEU A1014 3.601 -54.477 15.672 1.00 49.68 C ANISOU 1713 CG LEU A1014 5812 5704 7358 151 325 -547 C ATOM 1714 CD1 LEU A1014 2.535 -54.182 14.626 1.00 46.86 C ANISOU 1714 CD1 LEU A1014 5538 5321 6947 206 272 -562 C ATOM 1715 CD2 LEU A1014 3.362 -55.836 16.313 1.00 52.24 C ANISOU 1715 CD2 LEU A1014 6055 6067 7726 122 270 -554 C ATOM 1716 N LYS A1015 8.203 -53.898 14.824 1.00 48.73 N ANISOU 1716 N LYS A1015 5786 5539 7193 81 613 -481 N ATOM 1717 CA LYS A1015 9.443 -54.178 14.108 1.00 51.36 C ANISOU 1717 CA LYS A1015 6166 5849 7500 79 684 -468 C ATOM 1718 C LYS A1015 10.525 -54.690 15.050 1.00 49.49 C ANISOU 1718 C LYS A1015 5863 5632 7308 8 714 -442 C ATOM 1719 O LYS A1015 11.287 -55.595 14.693 1.00 46.07 O ANISOU 1719 O LYS A1015 5439 5196 6872 -5 741 -443 O ATOM 1720 CB LYS A1015 9.923 -52.926 13.374 1.00 57.62 C ANISOU 1720 CB LYS A1015 7037 6607 8249 109 745 -443 C ATOM 1721 CG LYS A1015 9.010 -52.471 12.246 1.00 68.79 C ANISOU 1721 CG LYS A1015 8539 7993 9607 177 722 -466 C ATOM 1722 CD LYS A1015 9.477 -51.143 11.665 1.00 76.38 C ANISOU 1722 CD LYS A1015 9566 8926 10530 200 782 -435 C ATOM 1723 CE LYS A1015 8.599 -50.697 10.504 1.00 80.32 C ANISOU 1723 CE LYS A1015 10157 9395 10966 266 761 -456 C ATOM 1724 NZ LYS A1015 8.696 -51.624 9.341 1.00 83.34 N ANISOU 1724 NZ LYS A1015 10609 9759 11297 305 760 -477 N ATOM 1725 N AVAL A1016 10.611 -54.108 16.250 0.57 48.85 N ANISOU 1725 N AVAL A1016 5729 5567 7265 -39 703 -418 N ATOM 1726 N BVAL A1016 10.611 -54.133 16.260 0.43 48.86 N ANISOU 1726 N BVAL A1016 5729 5568 7267 -40 702 -419 N ATOM 1727 CA AVAL A1016 11.599 -54.540 17.235 0.57 48.28 C ANISOU 1727 CA AVAL A1016 5631 5487 7226 -106 707 -396 C ATOM 1728 CA BVAL A1016 11.655 -54.576 17.180 0.43 48.36 C ANISOU 1728 CA BVAL A1016 5643 5496 7235 -106 710 -396 C ATOM 1729 C AVAL A1016 11.369 -55.996 17.617 0.57 46.83 C ANISOU 1729 C AVAL A1016 5418 5317 7057 -126 651 -422 C ATOM 1730 C BVAL A1016 11.374 -55.990 17.682 0.43 46.80 C ANISOU 1730 C BVAL A1016 5414 5314 7055 -128 649 -422 C ATOM 1731 O AVAL A1016 12.320 -56.765 17.805 0.57 44.61 O ANISOU 1731 O AVAL A1016 5158 5016 6777 -149 662 -418 O ATOM 1732 O BVAL A1016 12.306 -56.735 18.012 0.43 44.47 O ANISOU 1732 O BVAL A1016 5141 5003 6753 -147 651 -416 O ATOM 1733 CB AVAL A1016 11.555 -53.616 18.468 0.57 48.12 C ANISOU 1733 CB AVAL A1016 5606 5456 7221 -128 675 -377 C ATOM 1734 CB BVAL A1016 11.814 -53.565 18.335 0.43 48.35 C ANISOU 1734 CB BVAL A1016 5643 5478 7248 -129 691 -372 C ATOM 1735 CG1AVAL A1016 12.502 -54.113 19.550 0.57 48.35 C ANISOU 1735 CG1AVAL A1016 5662 5497 7211 -131 637 -360 C ATOM 1736 CG1BVAL A1016 10.542 -53.452 19.127 0.43 50.03 C ANISOU 1736 CG1BVAL A1016 5822 5720 7468 -120 614 -389 C ATOM 1737 CG2AVAL A1016 11.892 -52.187 18.073 0.57 49.33 C ANISOU 1737 CG2AVAL A1016 5785 5593 7365 -114 733 -349 C ATOM 1738 CG2BVAL A1016 12.973 -53.949 19.244 0.43 50.71 C ANISOU 1738 CG2BVAL A1016 5973 5783 7510 -133 668 -351 C ATOM 1739 N ILE A1017 10.102 -56.399 17.727 1.00 47.10 N ANISOU 1739 N ILE A1017 5414 5382 7098 -107 585 -449 N ATOM 1740 CA ILE A1017 9.786 -57.776 18.095 1.00 51.16 C ANISOU 1740 CA ILE A1017 5907 5909 7622 -119 525 -473 C ATOM 1741 C ILE A1017 10.215 -58.737 16.993 1.00 51.66 C ANISOU 1741 C ILE A1017 5972 5975 7683 -109 559 -490 C ATOM 1742 O ILE A1017 10.728 -59.829 17.269 1.00 51.67 O ANISOU 1742 O ILE A1017 5974 5969 7688 -134 545 -497 O ATOM 1743 CB ILE A1017 8.286 -57.912 18.416 1.00 46.51 C ANISOU 1743 CB ILE A1017 5282 5349 7041 -96 443 -491 C ATOM 1744 CG1 ILE A1017 7.949 -57.162 19.704 1.00 47.53 C ANISOU 1744 CG1 ILE A1017 5425 5480 7154 -99 405 -468 C ATOM 1745 CG2 ILE A1017 7.887 -59.376 18.540 1.00 44.16 C ANISOU 1745 CG2 ILE A1017 4969 5064 6747 -96 384 -514 C ATOM 1746 CD1 ILE A1017 6.474 -57.115 20.016 1.00 46.58 C ANISOU 1746 CD1 ILE A1017 5278 5387 7034 -76 332 -475 C ATOM 1747 N GLU A1018 10.028 -58.343 15.730 1.00 53.42 N ANISOU 1747 N GLU A1018 6236 6188 7871 -48 596 -502 N ATOM 1748 CA GLU A1018 10.373 -59.223 14.617 1.00 60.02 C ANISOU 1748 CA GLU A1018 7117 7010 8677 -15 616 -523 C ATOM 1749 C GLU A1018 11.867 -59.515 14.575 1.00 63.34 C ANISOU 1749 C GLU A1018 7551 7419 9096 -57 689 -495 C ATOM 1750 O GLU A1018 12.276 -60.666 14.384 1.00 67.34 O ANISOU 1750 O GLU A1018 8048 7931 9608 -71 687 -507 O ATOM 1751 CB GLU A1018 9.921 -58.604 13.296 1.00 63.12 C ANISOU 1751 CB GLU A1018 7610 7365 9006 63 624 -540 C ATOM 1752 CG GLU A1018 8.422 -58.502 13.136 1.00 70.58 C ANISOU 1752 CG GLU A1018 8562 8309 9948 107 541 -571 C ATOM 1753 CD GLU A1018 8.032 -57.732 11.893 1.00 78.34 C ANISOU 1753 CD GLU A1018 9656 9246 10863 174 549 -582 C ATOM 1754 OE1 GLU A1018 8.897 -57.550 11.010 1.00 80.56 O ANISOU 1754 OE1 GLU A1018 10013 9500 11097 195 614 -570 O ATOM 1755 OE2 GLU A1018 6.865 -57.302 11.804 1.00 81.52 O ANISOU 1755 OE2 GLU A1018 10072 9642 11260 206 489 -598 O ATOM 1756 N LYS A1019 12.698 -58.489 14.744 1.00 64.42 N ANISOU 1756 N LYS A1019 7713 7535 9227 -75 749 -456 N ATOM 1757 CA LYS A1019 14.143 -58.651 14.682 1.00 67.38 C ANISOU 1757 CA LYS A1019 8114 7887 9602 -112 813 -423 C ATOM 1758 C LYS A1019 14.785 -58.809 16.057 1.00 63.91 C ANISOU 1758 C LYS A1019 7660 7424 9197 -171 779 -408 C ATOM 1759 O LYS A1019 16.009 -58.692 16.174 1.00 64.12 O ANISOU 1759 O LYS A1019 7730 7444 9191 -168 802 -376 O ATOM 1760 CB LYS A1019 14.778 -57.476 13.937 1.00 74.07 C ANISOU 1760 CB LYS A1019 9029 8704 10412 -81 887 -390 C ATOM 1761 CG LYS A1019 14.450 -56.111 14.506 1.00 79.46 C ANISOU 1761 CG LYS A1019 9704 9382 11106 -83 883 -371 C ATOM 1762 CD LYS A1019 15.084 -55.016 13.666 1.00 85.39 C ANISOU 1762 CD LYS A1019 10525 10101 11818 -48 953 -338 C ATOM 1763 CE LYS A1019 14.706 -55.165 12.200 1.00 90.38 C ANISOU 1763 CE LYS A1019 11240 10718 12383 29 965 -361 C ATOM 1764 NZ LYS A1019 15.384 -54.155 11.341 1.00 93.62 N ANISOU 1764 NZ LYS A1019 11726 11094 12750 63 1031 -324 N ATOM 1765 N ALA A1020 13.995 -59.072 17.095 1.00 60.95 N ANISOU 1765 N ALA A1020 7258 7088 8812 -162 690 -422 N ATOM 1766 CA ALA A1020 14.562 -59.425 18.387 1.00 60.37 C ANISOU 1766 CA ALA A1020 7205 7050 8682 -148 629 -402 C ATOM 1767 C ALA A1020 15.203 -60.808 18.319 1.00 65.37 C ANISOU 1767 C ALA A1020 7848 7699 9292 -149 617 -407 C ATOM 1768 O ALA A1020 14.766 -61.682 17.566 1.00 59.50 O ANISOU 1768 O ALA A1020 7082 6950 8576 -158 621 -436 O ATOM 1769 CB ALA A1020 13.486 -59.395 19.471 1.00 56.77 C ANISOU 1769 CB ALA A1020 6728 6627 8214 -134 552 -408 C ATOM 1770 N ASP A1021 16.259 -61.005 19.114 1.00 74.48 N ANISOU 1770 N ASP A1021 9032 8871 10395 -140 599 -381 N ATOM 1771 CA ASP A1021 16.974 -62.274 19.134 1.00 84.95 C ANISOU 1771 CA ASP A1021 10363 10202 11712 -142 598 -389 C ATOM 1772 C ASP A1021 16.844 -63.048 20.438 1.00 81.59 C ANISOU 1772 C ASP A1021 9924 9795 11282 -133 550 -401 C ATOM 1773 O ASP A1021 17.335 -64.180 20.509 1.00 83.97 O ANISOU 1773 O ASP A1021 10227 10102 11576 -134 546 -409 O ATOM 1774 CB ASP A1021 18.467 -62.061 18.836 1.00 97.27 C ANISOU 1774 CB ASP A1021 11958 11740 13261 -144 648 -366 C ATOM 1775 CG ASP A1021 19.180 -61.327 19.950 1.00107.86 C ANISOU 1775 CG ASP A1021 13309 13077 14597 -133 645 -350 C ATOM 1776 OD1 ASP A1021 18.564 -60.414 20.541 1.00111.26 O ANISOU 1776 OD1 ASP A1021 13729 13511 15033 -128 627 -346 O ATOM 1777 OD2 ASP A1021 20.343 -61.671 20.247 1.00114.20 O ANISOU 1777 OD2 ASP A1021 14127 13873 15391 -130 660 -342 O ATOM 1778 N ASN A1022 16.204 -62.488 21.463 1.00 74.27 N ANISOU 1778 N ASN A1022 8985 8875 10357 -124 518 -399 N ATOM 1779 CA ASN A1022 15.987 -63.194 22.718 1.00 68.01 C ANISOU 1779 CA ASN A1022 8184 8097 9560 -115 478 -406 C ATOM 1780 C ASN A1022 14.605 -62.845 23.255 1.00 63.25 C ANISOU 1780 C ASN A1022 7560 7505 8967 -107 437 -413 C ATOM 1781 O ASN A1022 13.937 -61.929 22.769 1.00 59.28 O ANISOU 1781 O ASN A1022 7050 6999 8475 -108 439 -411 O ATOM 1782 CB ASN A1022 17.069 -62.862 23.753 1.00 69.49 C ANISOU 1782 CB ASN A1022 8390 8278 9734 -110 488 -389 C ATOM 1783 CG ASN A1022 17.167 -61.378 24.034 1.00 67.82 C ANISOU 1783 CG ASN A1022 8186 8057 9526 -107 501 -371 C ATOM 1784 OD1 ASN A1022 16.356 -60.817 24.769 1.00 69.29 O ANISOU 1784 OD1 ASN A1022 8363 8250 9716 -101 474 -370 O ATOM 1785 ND2 ASN A1022 18.170 -60.734 23.453 1.00 67.15 N ANISOU 1785 ND2 ASN A1022 8121 7955 9439 -110 543 -355 N ATOM 1786 N ALA A1023 14.193 -63.578 24.267 1.00 61.78 N ANISOU 1786 N ALA A1023 7366 7330 8778 -99 401 -419 N ATOM 1787 CA ALA A1023 12.893 -63.386 24.846 1.00 60.22 C ANISOU 1787 CA ALA A1023 7151 7140 8589 -90 360 -423 C ATOM 1788 C ALA A1023 12.760 -62.101 25.622 1.00 60.68 C ANISOU 1788 C ALA A1023 7215 7194 8646 -86 360 -406 C ATOM 1789 O ALA A1023 11.690 -61.567 25.714 1.00 64.06 O ANISOU 1789 O ALA A1023 7630 7625 9085 -81 336 -407 O ATOM 1790 CB ALA A1023 12.537 -64.562 25.719 1.00 59.38 C ANISOU 1790 CB ALA A1023 7038 7043 8479 -82 327 -430 C ATOM 1791 N ALA A1024 13.848 -61.604 26.173 1.00 56.79 N ANISOU 1791 N ALA A1024 6741 6694 8141 -87 383 -391 N ATOM 1792 CA ALA A1024 13.797 -60.380 26.966 1.00 54.40 C ANISOU 1792 CA ALA A1024 6445 6388 7837 -83 381 -375 C ATOM 1793 C ALA A1024 13.504 -59.164 26.096 1.00 54.51 C ANISOU 1793 C ALA A1024 6457 6394 7862 -87 400 -369 C ATOM 1794 O ALA A1024 12.802 -58.241 26.527 1.00 53.49 O ANISOU 1794 O ALA A1024 6322 6265 7737 -82 385 -362 O ATOM 1795 CB ALA A1024 15.109 -60.194 27.728 1.00 55.40 C ANISOU 1795 CB ALA A1024 6591 6509 7949 -81 400 -361 C ATOM 1796 N GLN A1025 14.033 -59.140 24.870 1.00 55.98 N ANISOU 1796 N GLN A1025 6648 6570 8050 -95 435 -370 N ATOM 1797 CA GLN A1025 13.762 -58.020 23.974 1.00 56.07 C ANISOU 1797 CA GLN A1025 6659 6572 8071 -100 458 -363 C ATOM 1798 C GLN A1025 12.308 -58.017 23.522 1.00 56.04 C ANISOU 1798 C GLN A1025 6632 6578 8082 -99 428 -378 C ATOM 1799 O GLN A1025 11.695 -56.951 23.390 1.00 57.06 O ANISOU 1799 O GLN A1025 6757 6705 8219 -97 427 -371 O ATOM 1800 CB GLN A1025 14.696 -58.070 22.766 1.00 55.76 C ANISOU 1800 CB GLN A1025 6637 6519 8030 -109 507 -358 C ATOM 1801 CG GLN A1025 16.163 -57.884 23.108 1.00 62.84 C ANISOU 1801 CG GLN A1025 7557 7403 8916 -107 537 -340 C ATOM 1802 CD GLN A1025 17.062 -58.017 21.896 1.00 67.95 C ANISOU 1802 CD GLN A1025 8224 8034 9561 -115 586 -333 C ATOM 1803 OE1 GLN A1025 16.606 -58.353 20.804 1.00 70.79 O ANISOU 1803 OE1 GLN A1025 8580 8392 9926 -123 600 -341 O ATOM 1804 NE2 GLN A1025 18.350 -57.751 22.083 1.00 70.64 N ANISOU 1804 NE2 GLN A1025 8585 8360 9894 -111 614 -315 N ATOM 1805 N VAL A1026 11.741 -59.198 23.271 1.00 53.11 N ANISOU 1805 N VAL A1026 6247 6218 7716 -98 403 -397 N ATOM 1806 CA VAL A1026 10.328 -59.280 22.916 1.00 49.41 C ANISOU 1806 CA VAL A1026 5754 5759 7263 -92 365 -412 C ATOM 1807 C VAL A1026 9.467 -58.793 24.073 1.00 49.87 C ANISOU 1807 C VAL A1026 5805 5822 7323 -82 327 -406 C ATOM 1808 O VAL A1026 8.467 -58.093 23.872 1.00 50.45 O ANISOU 1808 O VAL A1026 5864 5897 7408 -77 308 -407 O ATOM 1809 CB VAL A1026 9.965 -60.717 22.497 1.00 44.26 C ANISOU 1809 CB VAL A1026 5086 5115 6614 -90 341 -433 C ATOM 1810 CG1 VAL A1026 8.498 -60.810 22.123 1.00 43.50 C ANISOU 1810 CG1 VAL A1026 4964 5028 6536 -81 295 -449 C ATOM 1811 CG2 VAL A1026 10.843 -61.169 21.340 1.00 44.83 C ANISOU 1811 CG2 VAL A1026 5167 5182 6683 -102 381 -439 C ATOM 1812 N LYS A1027 9.889 -59.119 25.278 1.00 50.16 N ANISOU 1812 N LYS A1027 5851 5860 7347 -77 319 -398 N ATOM 1813 CA LYS A1027 9.157 -58.717 26.450 1.00 55.61 C ANISOU 1813 CA LYS A1027 6538 6554 8037 -68 288 -390 C ATOM 1814 C LYS A1027 9.184 -57.222 26.664 1.00 54.62 C ANISOU 1814 C LYS A1027 6419 6423 7912 -69 300 -374 C ATOM 1815 O LYS A1027 8.188 -56.651 27.036 1.00 51.15 O ANISOU 1815 O LYS A1027 5969 5986 7479 -62 274 -371 O ATOM 1816 CB LYS A1027 9.665 -59.429 27.685 1.00 58.84 C ANISOU 1816 CB LYS A1027 6958 6966 8433 -64 280 -384 C ATOM 1817 CG LYS A1027 9.039 -58.922 28.952 1.00 61.61 C ANISOU 1817 CG LYS A1027 7309 7319 8782 -56 255 -373 C ATOM 1818 CD LYS A1027 9.807 -59.421 30.145 1.00 66.83 C ANISOU 1818 CD LYS A1027 7985 7981 9427 -55 257 -365 C ATOM 1819 CE LYS A1027 9.044 -59.181 31.426 1.00 70.30 C ANISOU 1819 CE LYS A1027 8424 8423 9865 -47 229 -356 C ATOM 1820 NZ LYS A1027 9.787 -59.723 32.587 1.00 71.09 N ANISOU 1820 NZ LYS A1027 8539 8525 9949 -45 231 -349 N ATOM 1821 N ASP A1028 10.323 -56.593 26.425 1.00 58.21 N ANISOU 1821 N ASP A1028 6889 6868 8358 -75 340 -362 N ATOM 1822 CA ASP A1028 10.456 -55.147 26.589 1.00 62.77 C ANISOU 1822 CA ASP A1028 7474 7439 8936 -75 355 -346 C ATOM 1823 C ASP A1028 9.553 -54.394 25.622 1.00 55.90 C ANISOU 1823 C ASP A1028 6591 6567 8080 -77 355 -349 C ATOM 1824 O ASP A1028 8.946 -53.380 25.987 1.00 54.54 O ANISOU 1824 O ASP A1028 6415 6396 7913 -73 342 -341 O ATOM 1825 CB ASP A1028 11.912 -54.723 26.397 1.00 72.88 C ANISOU 1825 CB ASP A1028 8777 8708 10208 -80 398 -332 C ATOM 1826 CG ASP A1028 12.710 -54.769 27.685 1.00 82.47 C ANISOU 1826 CG ASP A1028 10004 9923 11408 -74 392 -321 C ATOM 1827 OD1 ASP A1028 12.676 -53.773 28.439 1.00 86.56 O ANISOU 1827 OD1 ASP A1028 10526 10440 11924 -69 386 -308 O ATOM 1828 OD2 ASP A1028 13.375 -55.795 27.941 1.00 85.48 O ANISOU 1828 OD2 ASP A1028 10391 10306 11781 -74 394 -327 O ATOM 1829 N ALA A1029 9.442 -54.898 24.412 1.00 51.89 N ANISOU 1829 N ALA A1029 6076 6058 7580 -83 368 -363 N ATOM 1830 CA ALA A1029 8.609 -54.270 23.426 1.00 48.48 C ANISOU 1830 CA ALA A1029 5628 5623 7168 -84 371 -370 C ATOM 1831 C ALA A1029 7.140 -54.499 23.740 1.00 47.89 C ANISOU 1831 C ALA A1029 5532 5567 7099 -73 313 -380 C ATOM 1832 O ALA A1029 6.356 -53.589 23.677 1.00 47.46 O ANISOU 1832 O ALA A1029 5460 5516 7058 -68 303 -377 O ATOM 1833 CB ALA A1029 8.958 -54.782 22.065 1.00 44.85 C ANISOU 1833 CB ALA A1029 5154 5140 6748 -97 416 -394 C ATOM 1834 N LEU A1030 6.776 -55.718 24.091 1.00 42.99 N ANISOU 1834 N LEU A1030 4904 4950 6479 -68 280 -393 N ATOM 1835 CA LEU A1030 5.399 -56.038 24.425 1.00 44.55 C ANISOU 1835 CA LEU A1030 5084 5169 6675 -55 223 -395 C ATOM 1836 C LEU A1030 4.928 -55.298 25.658 1.00 44.87 C ANISOU 1836 C LEU A1030 5128 5200 6720 -49 204 -383 C ATOM 1837 O LEU A1030 3.806 -54.857 25.733 1.00 37.24 O ANISOU 1837 O LEU A1030 4150 4256 5743 -39 169 -373 O ATOM 1838 CB LEU A1030 5.194 -57.533 24.581 1.00 45.64 C ANISOU 1838 CB LEU A1030 5216 5303 6822 -50 197 -413 C ATOM 1839 CG LEU A1030 5.258 -58.336 23.290 1.00 43.54 C ANISOU 1839 CG LEU A1030 4939 5055 6549 -52 198 -424 C ATOM 1840 CD1 LEU A1030 5.380 -59.807 23.626 1.00 45.65 C ANISOU 1840 CD1 LEU A1030 5206 5309 6829 -49 182 -442 C ATOM 1841 CD2 LEU A1030 4.056 -58.067 22.408 1.00 40.19 C ANISOU 1841 CD2 LEU A1030 4484 4646 6138 -40 163 -433 C ATOM 1842 N THR A1031 5.816 -55.161 26.630 1.00 46.16 N ANISOU 1842 N THR A1031 5310 5357 6874 -52 224 -372 N ATOM 1843 CA THR A1031 5.490 -54.452 27.840 1.00 49.76 C ANISOU 1843 CA THR A1031 5770 5812 7324 -46 209 -356 C ATOM 1844 C THR A1031 5.176 -53.019 27.489 1.00 50.90 C ANISOU 1844 C THR A1031 5912 5954 7474 -47 216 -348 C ATOM 1845 O THR A1031 4.223 -52.467 27.994 1.00 49.59 O ANISOU 1845 O THR A1031 5739 5789 7313 -40 187 -342 O ATOM 1846 CB THR A1031 6.665 -54.454 28.825 1.00 51.38 C ANISOU 1846 CB THR A1031 5995 6016 7512 -49 231 -344 C ATOM 1847 OG1 THR A1031 6.997 -55.795 29.159 1.00 52.83 O ANISOU 1847 OG1 THR A1031 6181 6203 7690 -49 225 -352 O ATOM 1848 CG2 THR A1031 6.306 -53.730 30.086 1.00 46.85 C ANISOU 1848 CG2 THR A1031 5425 5442 6932 -44 213 -329 C ATOM 1849 N LYS A1032 5.990 -52.416 26.637 1.00 50.40 N ANISOU 1849 N LYS A1032 5856 5885 7411 -56 257 -345 N ATOM 1850 CA LYS A1032 5.723 -51.085 26.229 1.00 50.62 C ANISOU 1850 CA LYS A1032 5881 5914 7440 -56 268 -335 C ATOM 1851 C LYS A1032 4.440 -51.104 25.488 1.00 51.63 C ANISOU 1851 C LYS A1032 5987 6084 7546 -44 233 -332 C ATOM 1852 O LYS A1032 3.631 -50.398 25.863 1.00 52.83 O ANISOU 1852 O LYS A1032 6133 6251 7690 -35 208 -321 O ATOM 1853 CB LYS A1032 6.801 -50.518 25.323 1.00 54.70 C ANISOU 1853 CB LYS A1032 6410 6419 7955 -66 322 -328 C ATOM 1854 CG LYS A1032 7.962 -49.855 26.036 1.00 57.79 C ANISOU 1854 CG LYS A1032 6822 6797 8337 -68 350 -310 C ATOM 1855 CD LYS A1032 9.096 -49.600 25.059 1.00 61.72 C ANISOU 1855 CD LYS A1032 7335 7280 8835 -76 405 -303 C ATOM 1856 CE LYS A1032 10.234 -48.826 25.690 1.00 65.41 C ANISOU 1856 CE LYS A1032 7824 7740 9290 -75 426 -281 C ATOM 1857 NZ LYS A1032 11.141 -48.272 24.648 1.00 67.85 N ANISOU 1857 NZ LYS A1032 8144 8025 9609 -80 485 -270 N ATOM 1858 N MET A1033 4.192 -52.009 24.553 1.00 47.40 N ANISOU 1858 N MET A1033 5431 5546 7033 -44 230 -354 N ATOM 1859 CA MET A1033 2.932 -51.999 23.794 1.00 45.70 C ANISOU 1859 CA MET A1033 5183 5342 6841 -28 197 -369 C ATOM 1860 C MET A1033 1.670 -51.994 24.656 1.00 49.75 C ANISOU 1860 C MET A1033 5699 5886 7316 -12 135 -349 C ATOM 1861 O MET A1033 0.967 -51.069 24.692 1.00 60.37 O ANISOU 1861 O MET A1033 7036 7238 8664 -1 121 -341 O ATOM 1862 CB MET A1033 2.900 -53.134 22.778 1.00 50.90 C ANISOU 1862 CB MET A1033 5822 5994 7524 -25 195 -398 C ATOM 1863 CG MET A1033 3.894 -52.975 21.642 1.00 51.07 C ANISOU 1863 CG MET A1033 5836 5988 7580 -33 264 -418 C ATOM 1864 SD MET A1033 3.976 -54.361 20.506 1.00 51.23 S ANISOU 1864 SD MET A1033 5838 6005 7623 -26 265 -452 S ATOM 1865 CE MET A1033 2.475 -54.185 19.591 1.00 48.10 C ANISOU 1865 CE MET A1033 5424 5617 7236 32 211 -475 C ATOM 1866 N ARG A1034 1.595 -52.886 25.591 1.00 44.06 N ANISOU 1866 N ARG A1034 4995 5173 6575 -15 112 -340 N ATOM 1867 CA ARG A1034 0.438 -53.074 26.460 1.00 41.40 C ANISOU 1867 CA ARG A1034 4654 4839 6236 -4 65 -331 C ATOM 1868 C ARG A1034 0.050 -51.771 27.148 1.00 42.88 C ANISOU 1868 C ARG A1034 4846 5032 6415 0 61 -313 C ATOM 1869 O ARG A1034 -1.134 -51.420 27.206 1.00 47.64 O ANISOU 1869 O ARG A1034 5442 5655 7004 14 24 -300 O ATOM 1870 CB ARG A1034 0.725 -54.163 27.492 1.00 41.64 C ANISOU 1870 CB ARG A1034 4693 4843 6287 -10 61 -340 C ATOM 1871 CG ARG A1034 -0.521 -54.690 28.174 1.00 41.72 C ANISOU 1871 CG ARG A1034 4697 4858 6296 2 14 -330 C ATOM 1872 CD ARG A1034 -0.181 -55.640 29.306 1.00 48.65 C ANISOU 1872 CD ARG A1034 5583 5709 7192 -2 16 -335 C ATOM 1873 NE ARG A1034 -1.377 -56.300 29.822 1.00 56.01 N ANISOU 1873 NE ARG A1034 6510 6646 8127 7 -26 -324 N ATOM 1874 CZ ARG A1034 -2.204 -55.761 30.712 1.00 60.05 C ANISOU 1874 CZ ARG A1034 7022 7161 8633 12 -45 -304 C ATOM 1875 NH1 ARG A1034 -1.968 -54.546 31.188 1.00 62.87 N ANISOU 1875 NH1 ARG A1034 7385 7519 8982 10 -30 -294 N ATOM 1876 NH2 ARG A1034 -3.269 -56.434 31.124 1.00 59.08 N ANISOU 1876 NH2 ARG A1034 6894 7039 8513 20 -80 -292 N ATOM 1877 N ALA A1035 1.019 -51.050 27.679 1.00 45.32 N ANISOU 1877 N ALA A1035 5166 5320 6732 -11 97 -310 N ATOM 1878 CA ALA A1035 0.750 -49.771 28.288 1.00 46.81 C ANISOU 1878 CA ALA A1035 5359 5513 6913 -8 95 -294 C ATOM 1879 C ALA A1035 0.165 -48.803 27.273 1.00 47.31 C ANISOU 1879 C ALA A1035 5413 5609 6954 5 92 -284 C ATOM 1880 O ALA A1035 -0.779 -48.121 27.574 1.00 50.28 O ANISOU 1880 O ALA A1035 5787 6003 7316 18 64 -270 O ATOM 1881 CB ALA A1035 2.004 -49.207 28.921 1.00 45.05 C ANISOU 1881 CB ALA A1035 5152 5259 6707 -21 135 -294 C ATOM 1882 N ALA A1036 0.714 -48.753 26.070 1.00 48.13 N ANISOU 1882 N ALA A1036 5504 5700 7082 3 123 -301 N ATOM 1883 CA ALA A1036 0.196 -47.851 25.046 1.00 49.94 C ANISOU 1883 CA ALA A1036 5709 5919 7347 20 130 -315 C ATOM 1884 C ALA A1036 -1.200 -48.256 24.590 1.00 55.94 C ANISOU 1884 C ALA A1036 6454 6696 8106 46 74 -320 C ATOM 1885 O ALA A1036 -2.015 -47.389 24.254 1.00 56.69 O ANISOU 1885 O ALA A1036 6543 6793 8205 71 55 -317 O ATOM 1886 CB ALA A1036 1.149 -47.804 23.851 1.00 45.91 C ANISOU 1886 CB ALA A1036 5189 5378 6878 17 190 -339 C ATOM 1887 N ALA A1037 -1.494 -49.558 24.571 1.00 54.08 N ANISOU 1887 N ALA A1037 6218 6469 7861 44 44 -325 N ATOM 1888 CA ALA A1037 -2.819 -50.010 24.158 1.00 51.95 C ANISOU 1888 CA ALA A1037 5940 6211 7588 68 -14 -326 C ATOM 1889 C ALA A1037 -3.884 -49.564 25.154 1.00 55.28 C ANISOU 1889 C ALA A1037 6378 6661 7963 74 -51 -290 C ATOM 1890 O ALA A1037 -4.948 -49.073 24.761 1.00 55.18 O ANISOU 1890 O ALA A1037 6362 6652 7953 98 -88 -286 O ATOM 1891 CB ALA A1037 -2.831 -51.531 23.997 1.00 47.20 C ANISOU 1891 CB ALA A1037 5339 5611 6984 62 -34 -335 C ATOM 1892 N LEU A1038 -3.612 -49.728 26.451 1.00 58.68 N ANISOU 1892 N LEU A1038 6831 7109 8355 58 -42 -266 N ATOM 1893 CA LEU A1038 -4.546 -49.256 27.468 1.00 65.20 C ANISOU 1893 CA LEU A1038 7661 7937 9174 62 -70 -247 C ATOM 1894 C LEU A1038 -4.657 -47.738 27.466 1.00 73.32 C ANISOU 1894 C LEU A1038 8693 8981 10184 72 -60 -233 C ATOM 1895 O LEU A1038 -5.732 -47.196 27.747 1.00 75.88 O ANISOU 1895 O LEU A1038 9021 9319 10492 86 -90 -216 O ATOM 1896 CB LEU A1038 -4.112 -49.747 28.847 1.00 63.45 C ANISOU 1896 CB LEU A1038 7445 7691 8972 45 -60 -247 C ATOM 1897 CG LEU A1038 -3.938 -51.256 29.005 1.00 62.81 C ANISOU 1897 CG LEU A1038 7363 7592 8910 37 -66 -260 C ATOM 1898 CD1 LEU A1038 -3.516 -51.593 30.426 1.00 62.92 C ANISOU 1898 CD1 LEU A1038 7385 7582 8940 27 -55 -258 C ATOM 1899 CD2 LEU A1038 -5.219 -51.983 28.631 1.00 62.46 C ANISOU 1899 CD2 LEU A1038 7313 7559 8861 51 -112 -253 C ATOM 1900 N ASP A1039 -3.563 -47.039 27.157 1.00 78.66 N ANISOU 1900 N ASP A1039 9368 9647 10871 65 -17 -243 N ATOM 1901 CA ASP A1039 -3.601 -45.581 27.121 1.00 83.37 C ANISOU 1901 CA ASP A1039 9962 10238 11478 74 -6 -239 C ATOM 1902 C ASP A1039 -4.438 -45.080 25.950 1.00 85.96 C ANISOU 1902 C ASP A1039 10273 10553 11834 103 -27 -252 C ATOM 1903 O ASP A1039 -5.131 -44.062 26.066 1.00 88.81 O ANISOU 1903 O ASP A1039 10639 10922 12182 121 -43 -238 O ATOM 1904 CB ASP A1039 -2.179 -45.023 27.049 1.00 87.41 C ANISOU 1904 CB ASP A1039 10473 10722 12017 56 50 -250 C ATOM 1905 CG ASP A1039 -2.132 -43.519 27.226 1.00 92.97 C ANISOU 1905 CG ASP A1039 11179 11423 12724 63 63 -241 C ATOM 1906 OD1 ASP A1039 -2.177 -43.057 28.385 1.00 93.81 O ANISOU 1906 OD1 ASP A1039 11302 11547 12795 58 53 -219 O ATOM 1907 OD2 ASP A1039 -2.044 -42.799 26.208 1.00 95.92 O ANISOU 1907 OD2 ASP A1039 11539 11774 13130 79 87 -255 O ATOM 1908 N ALA A1040 -4.390 -45.782 24.816 1.00 85.67 N ANISOU 1908 N ALA A1040 10223 10497 11830 114 -28 -278 N ATOM 1909 CA ALA A1040 -5.218 -45.422 23.674 1.00 87.91 C ANISOU 1909 CA ALA A1040 10507 10764 12131 156 -56 -292 C ATOM 1910 C ALA A1040 -6.667 -45.855 23.844 1.00 90.68 C ANISOU 1910 C ALA A1040 10866 11135 12454 169 -125 -273 C ATOM 1911 O ALA A1040 -7.532 -45.377 23.103 1.00 92.19 O ANISOU 1911 O ALA A1040 11070 11312 12645 204 -160 -275 O ATOM 1912 CB ALA A1040 -4.650 -46.035 22.391 1.00 88.21 C ANISOU 1912 CB ALA A1040 10546 10768 12203 175 -32 -329 C ATOM 1913 N GLN A1041 -6.950 -46.748 24.794 1.00 91.11 N ANISOU 1913 N GLN A1041 10925 11217 12475 144 -142 -251 N ATOM 1914 CA GLN A1041 -8.319 -47.208 24.993 1.00 92.82 C ANISOU 1914 CA GLN A1041 11157 11453 12658 155 -194 -227 C ATOM 1915 C GLN A1041 -9.153 -46.187 25.755 1.00 95.45 C ANISOU 1915 C GLN A1041 11506 11810 12951 161 -205 -194 C ATOM 1916 O GLN A1041 -10.382 -46.172 25.623 1.00 97.52 O ANISOU 1916 O GLN A1041 11782 12081 13191 177 -246 -176 O ATOM 1917 CB GLN A1041 -8.315 -48.551 25.729 1.00 92.41 C ANISOU 1917 CB GLN A1041 11113 11422 12577 133 -194 -214 C ATOM 1918 CG GLN A1041 -9.652 -49.278 25.723 1.00 94.49 C ANISOU 1918 CG GLN A1041 11387 11693 12822 143 -242 -196 C ATOM 1919 CD GLN A1041 -9.573 -50.650 26.362 1.00 95.38 C ANISOU 1919 CD GLN A1041 11492 11786 12960 123 -249 -203 C ATOM 1920 OE1 GLN A1041 -8.614 -50.963 27.065 1.00 95.25 O ANISOU 1920 OE1 GLN A1041 11469 11759 12962 103 -216 -213 O ATOM 1921 NE2 GLN A1041 -10.581 -51.479 26.113 1.00 96.13 N ANISOU 1921 NE2 GLN A1041 11592 11874 13060 130 -290 -197 N ATOM 1922 N LYS A1042 -8.509 -45.329 26.542 1.00 93.47 N ANISOU 1922 N LYS A1042 11256 11569 12688 150 -170 -186 N ATOM 1923 CA LYS A1042 -9.211 -44.291 27.288 1.00 90.25 C ANISOU 1923 CA LYS A1042 10864 11184 12242 158 -178 -158 C ATOM 1924 C LYS A1042 -9.752 -43.213 26.356 1.00 87.88 C ANISOU 1924 C LYS A1042 10564 10864 11963 186 -198 -164 C ATOM 1925 O LYS A1042 -10.952 -43.157 26.084 1.00 86.71 O ANISOU 1925 O LYS A1042 10431 10722 11795 203 -238 -148 O ATOM 1926 CB LYS A1042 -8.285 -43.666 28.333 1.00 90.80 C ANISOU 1926 CB LYS A1042 10933 11257 12309 139 -141 -155 C ATOM 1927 CG LYS A1042 -7.763 -44.645 29.370 1.00 89.84 C ANISOU 1927 CG LYS A1042 10804 11116 12214 112 -132 -163 C ATOM 1928 CD LYS A1042 -6.868 -43.946 30.380 1.00 89.30 C ANISOU 1928 CD LYS A1042 10738 11037 12154 97 -103 -163 C ATOM 1929 CE LYS A1042 -6.341 -44.910 31.428 1.00 89.10 C ANISOU 1929 CE LYS A1042 10712 10989 12154 77 -94 -169 C ATOM 1930 NZ LYS A1042 -5.471 -44.221 32.420 1.00 88.21 N ANISOU 1930 NZ LYS A1042 10605 10861 12051 65 -69 -169 N ATOM 1931 N PRO A1056 -22.552 -48.997 17.893 1.00 89.28 N ANISOU 1931 N PRO A1056 11054 10860 12006 308 -760 -73 N ATOM 1932 CA PRO A1056 -22.209 -49.625 16.613 1.00 92.49 C ANISOU 1932 CA PRO A1056 11494 11221 12428 330 -812 -110 C ATOM 1933 C PRO A1056 -20.705 -49.627 16.357 1.00 96.48 C ANISOU 1933 C PRO A1056 11985 11713 12961 350 -804 -150 C ATOM 1934 O PRO A1056 -20.065 -50.674 16.469 1.00 93.97 O ANISOU 1934 O PRO A1056 11635 11398 12670 343 -799 -170 O ATOM 1935 CB PRO A1056 -22.939 -48.754 15.589 1.00 92.71 C ANISOU 1935 CB PRO A1056 11590 11215 12421 351 -852 -107 C ATOM 1936 CG PRO A1056 -24.096 -48.194 16.342 1.00 91.41 C ANISOU 1936 CG PRO A1056 11418 11082 12233 328 -828 -62 C ATOM 1937 CD PRO A1056 -23.593 -47.966 17.739 1.00 89.62 C ANISOU 1937 CD PRO A1056 11133 10902 12015 311 -767 -46 C ATOM 1938 N GLU A1057 -20.151 -48.462 16.012 1.00103.53 N ANISOU 1938 N GLU A1057 12903 12589 13844 377 -795 -161 N ATOM 1939 CA GLU A1057 -18.704 -48.355 15.858 1.00107.39 C ANISOU 1939 CA GLU A1057 13378 13065 14361 398 -768 -198 C ATOM 1940 C GLU A1057 -17.995 -48.523 17.196 1.00105.72 C ANISOU 1940 C GLU A1057 13088 12901 14179 365 -712 -190 C ATOM 1941 O GLU A1057 -16.903 -49.099 17.258 1.00106.91 O ANISOU 1941 O GLU A1057 13206 13051 14363 365 -688 -219 O ATOM 1942 CB GLU A1057 -18.334 -47.012 15.228 1.00112.09 C ANISOU 1942 CB GLU A1057 14030 13624 14934 435 -754 -209 C ATOM 1943 CG GLU A1057 -18.724 -46.864 13.768 1.00116.57 C ANISOU 1943 CG GLU A1057 14699 14132 15459 471 -792 -227 C ATOM 1944 CD GLU A1057 -18.182 -45.586 13.155 1.00120.86 C ANISOU 1944 CD GLU A1057 15316 14631 15972 500 -752 -246 C ATOM 1945 OE1 GLU A1057 -17.482 -44.834 13.867 1.00121.49 O ANISOU 1945 OE1 GLU A1057 15361 14734 16065 487 -693 -245 O ATOM 1946 OE2 GLU A1057 -18.453 -45.333 11.962 1.00123.10 O ANISOU 1946 OE2 GLU A1057 15698 14872 16203 520 -763 -261 O ATOM 1947 N MET A1058 -18.603 -48.026 18.277 1.00102.91 N ANISOU 1947 N MET A1058 12709 12585 13806 338 -684 -152 N ATOM 1948 CA MET A1058 -17.982 -48.133 19.593 1.00101.46 C ANISOU 1948 CA MET A1058 12471 12446 13634 308 -626 -142 C ATOM 1949 C MET A1058 -17.911 -49.576 20.072 1.00 99.43 C ANISOU 1949 C MET A1058 12186 12206 13387 283 -616 -141 C ATOM 1950 O MET A1058 -17.006 -49.928 20.839 1.00 98.91 O ANISOU 1950 O MET A1058 12083 12162 13335 265 -572 -148 O ATOM 1951 CB MET A1058 -18.744 -47.279 20.605 1.00102.66 C ANISOU 1951 CB MET A1058 12622 12635 13751 293 -598 -100 C ATOM 1952 CG MET A1058 -18.564 -45.785 20.416 1.00105.67 C ANISOU 1952 CG MET A1058 13020 13007 14124 312 -593 -100 C ATOM 1953 SD MET A1058 -16.862 -45.263 20.693 1.00106.44 S ANISOU 1953 SD MET A1058 13081 13102 14259 317 -544 -132 S ATOM 1954 CE MET A1058 -16.610 -45.824 22.376 1.00105.59 C ANISOU 1954 CE MET A1058 12928 13052 14140 275 -490 -109 C ATOM 1955 N LYS A1059 -18.849 -50.422 19.644 1.00 97.64 N ANISOU 1955 N LYS A1059 11980 11968 13150 281 -652 -132 N ATOM 1956 CA LYS A1059 -18.812 -51.820 20.055 1.00 95.85 C ANISOU 1956 CA LYS A1059 11733 11755 12932 261 -641 -131 C ATOM 1957 C LYS A1059 -17.706 -52.576 19.328 1.00 90.59 C ANISOU 1957 C LYS A1059 11054 11061 12304 270 -657 -175 C ATOM 1958 O LYS A1059 -17.041 -53.435 19.919 1.00 88.27 O ANISOU 1958 O LYS A1059 10731 10785 12023 250 -624 -181 O ATOM 1959 CB LYS A1059 -20.171 -52.472 19.808 1.00100.36 C ANISOU 1959 CB LYS A1059 12326 12306 13501 256 -685 -114 C ATOM 1960 CG LYS A1059 -21.344 -51.623 20.273 1.00104.53 C ANISOU 1960 CG LYS A1059 12867 12833 14015 250 -694 -83 C ATOM 1961 CD LYS A1059 -22.669 -52.339 20.081 1.00105.87 C ANISOU 1961 CD LYS A1059 13053 12971 14203 241 -743 -71 C ATOM 1962 CE LYS A1059 -23.838 -51.403 20.344 1.00107.68 C ANISOU 1962 CE LYS A1059 13300 13199 14414 238 -752 -40 C ATOM 1963 NZ LYS A1059 -23.713 -50.716 21.659 1.00109.63 N ANISOU 1963 NZ LYS A1059 13520 13473 14663 225 -712 -21 N ATOM 1964 N ASP A1060 -17.488 -52.263 18.048 1.00 88.33 N ANISOU 1964 N ASP A1060 10798 10734 12031 303 -703 -207 N ATOM 1965 CA ASP A1060 -16.410 -52.893 17.295 1.00 88.27 C ANISOU 1965 CA ASP A1060 10784 10701 12055 321 -714 -253 C ATOM 1966 C ASP A1060 -15.048 -52.319 17.663 1.00 81.60 C ANISOU 1966 C ASP A1060 9904 9865 11234 322 -659 -275 C ATOM 1967 O ASP A1060 -14.032 -53.010 17.528 1.00 82.14 O ANISOU 1967 O ASP A1060 9947 9929 11332 321 -640 -305 O ATOM 1968 CB ASP A1060 -16.658 -52.737 15.795 1.00 94.08 C ANISOU 1968 CB ASP A1060 11582 11386 12777 368 -774 -279 C ATOM 1969 CG ASP A1060 -18.044 -53.191 15.385 1.00100.88 C ANISOU 1969 CG ASP A1060 12481 12235 13612 363 -828 -257 C ATOM 1970 OD1 ASP A1060 -18.515 -54.222 15.908 1.00102.46 O ANISOU 1970 OD1 ASP A1060 12658 12454 13820 333 -825 -242 O ATOM 1971 OD2 ASP A1060 -18.666 -52.511 14.540 1.00104.25 O ANISOU 1971 OD2 ASP A1060 12969 12634 14008 390 -865 -255 O ATOM 1972 N PHE A1061 -15.005 -51.065 18.119 1.00 72.23 N ANISOU 1972 N PHE A1061 8716 8691 10038 324 -629 -259 N ATOM 1973 CA PHE A1061 -13.740 -50.480 18.553 1.00 67.76 C ANISOU 1973 CA PHE A1061 8117 8134 9496 320 -567 -276 C ATOM 1974 C PHE A1061 -13.310 -51.037 19.903 1.00 65.28 C ANISOU 1974 C PHE A1061 7756 7863 9184 272 -517 -259 C ATOM 1975 O PHE A1061 -12.123 -51.308 20.119 1.00 65.86 O ANISOU 1975 O PHE A1061 7799 7940 9283 259 -473 -281 O ATOM 1976 CB PHE A1061 -13.856 -48.958 18.612 1.00 71.16 C ANISOU 1976 CB PHE A1061 8567 8558 9911 338 -550 -264 C ATOM 1977 CG PHE A1061 -13.720 -48.289 17.277 1.00 75.85 C ANISOU 1977 CG PHE A1061 9230 9093 10496 392 -562 -292 C ATOM 1978 CD1 PHE A1061 -12.962 -48.869 16.272 1.00 74.97 C ANISOU 1978 CD1 PHE A1061 9154 8936 10394 419 -554 -336 C ATOM 1979 CD2 PHE A1061 -14.350 -47.083 17.024 1.00 78.21 C ANISOU 1979 CD2 PHE A1061 9579 9375 10764 412 -572 -276 C ATOM 1980 CE1 PHE A1061 -12.834 -48.257 15.040 1.00 76.07 C ANISOU 1980 CE1 PHE A1061 9400 9035 10467 437 -530 -356 C ATOM 1981 CE2 PHE A1061 -14.227 -46.465 15.794 1.00 79.15 C ANISOU 1981 CE2 PHE A1061 9794 9442 10836 440 -559 -299 C ATOM 1982 CZ PHE A1061 -13.467 -47.053 14.801 1.00 78.41 C ANISOU 1982 CZ PHE A1061 9752 9324 10716 442 -530 -336 C ATOM 1983 N ARG A1062 -14.259 -51.204 20.829 1.00 65.67 N ANISOU 1983 N ARG A1062 7811 7944 9197 248 -515 -216 N ATOM 1984 CA ARG A1062 -13.933 -51.828 22.106 1.00 67.21 C ANISOU 1984 CA ARG A1062 7986 8176 9374 214 -466 -196 C ATOM 1985 C ARG A1062 -13.530 -53.284 21.913 1.00 57.37 C ANISOU 1985 C ARG A1062 6731 6924 8145 204 -470 -213 C ATOM 1986 O ARG A1062 -12.619 -53.780 22.586 1.00 55.57 O ANISOU 1986 O ARG A1062 6486 6711 7916 183 -425 -216 O ATOM 1987 CB ARG A1062 -15.116 -51.715 23.068 1.00 78.72 C ANISOU 1987 CB ARG A1062 9455 9652 10803 203 -471 -156 C ATOM 1988 CG ARG A1062 -14.972 -52.553 24.331 1.00 90.32 C ANISOU 1988 CG ARG A1062 10903 11111 12304 176 -456 -154 C ATOM 1989 CD ARG A1062 -15.805 -51.996 25.473 1.00100.24 C ANISOU 1989 CD ARG A1062 12160 12371 13558 168 -455 -124 C ATOM 1990 NE ARG A1062 -15.338 -50.676 25.887 1.00107.87 N ANISOU 1990 NE ARG A1062 13125 13358 14502 170 -423 -118 N ATOM 1991 CZ ARG A1062 -14.335 -50.471 26.735 1.00111.25 C ANISOU 1991 CZ ARG A1062 13537 13793 14938 156 -382 -125 C ATOM 1992 NH1 ARG A1062 -13.688 -51.501 27.263 1.00111.98 N ANISOU 1992 NH1 ARG A1062 13617 13872 15058 140 -367 -138 N ATOM 1993 NH2 ARG A1062 -13.977 -49.234 27.055 1.00111.50 N ANISOU 1993 NH2 ARG A1062 13571 13843 14952 160 -358 -120 N ATOM 1994 N HIS A1063 -14.192 -53.982 20.986 1.00 49.96 N ANISOU 1994 N HIS A1063 5808 5959 7214 219 -523 -222 N ATOM 1995 CA HIS A1063 -13.786 -55.346 20.668 1.00 52.00 C ANISOU 1995 CA HIS A1063 6059 6207 7491 212 -531 -243 C ATOM 1996 C HIS A1063 -12.398 -55.370 20.043 1.00 52.39 C ANISOU 1996 C HIS A1063 6086 6236 7583 219 -518 -290 C ATOM 1997 O HIS A1063 -11.617 -56.296 20.291 1.00 52.27 O ANISOU 1997 O HIS A1063 6054 6227 7579 201 -491 -302 O ATOM 1998 CB HIS A1063 -14.809 -55.995 19.736 1.00 53.57 C ANISOU 1998 CB HIS A1063 6285 6379 7690 229 -596 -245 C ATOM 1999 CG HIS A1063 -14.547 -57.444 19.468 1.00 56.40 C ANISOU 1999 CG HIS A1063 6638 6728 8063 222 -607 -261 C ATOM 2000 ND1 HIS A1063 -14.475 -58.385 20.473 1.00 57.75 N ANISOU 2000 ND1 HIS A1063 6791 6900 8251 195 -585 -253 N ATOM 2001 CD2 HIS A1063 -14.339 -58.115 18.310 1.00 55.70 C ANISOU 2001 CD2 HIS A1063 6559 6604 8000 242 -656 -299 C ATOM 2002 CE1 HIS A1063 -14.235 -59.573 19.946 1.00 57.03 C ANISOU 2002 CE1 HIS A1063 6700 6793 8178 196 -605 -274 C ATOM 2003 NE2 HIS A1063 -14.148 -59.436 18.635 1.00 55.88 N ANISOU 2003 NE2 HIS A1063 6572 6635 8026 224 -642 -297 N ATOM 2004 N GLY A1064 -12.070 -54.357 19.238 1.00 50.85 N ANISOU 2004 N GLY A1064 5895 6019 7408 249 -530 -316 N ATOM 2005 CA GLY A1064 -10.746 -54.295 18.642 1.00 46.33 C ANISOU 2005 CA GLY A1064 5304 5429 6872 262 -501 -360 C ATOM 2006 C GLY A1064 -9.646 -54.119 19.672 1.00 41.83 C ANISOU 2006 C GLY A1064 4699 4884 6310 225 -424 -355 C ATOM 2007 O GLY A1064 -8.554 -54.676 19.528 1.00 40.09 O ANISOU 2007 O GLY A1064 4458 4660 6115 214 -389 -383 O ATOM 2008 N PHE A1065 -9.915 -53.344 20.725 1.00 44.28 N ANISOU 2008 N PHE A1065 5011 5222 6593 205 -396 -320 N ATOM 2009 CA PHE A1065 -8.931 -53.181 21.788 1.00 48.72 C ANISOU 2009 CA PHE A1065 5557 5807 7148 172 -329 -310 C ATOM 2010 C PHE A1065 -8.910 -54.374 22.736 1.00 52.06 C ANISOU 2010 C PHE A1065 5988 6255 7538 145 -314 -287 C ATOM 2011 O PHE A1065 -7.870 -54.654 23.341 1.00 51.27 O ANISOU 2011 O PHE A1065 5883 6164 7434 122 -266 -289 O ATOM 2012 CB PHE A1065 -9.196 -51.887 22.561 1.00 52.55 C ANISOU 2012 CB PHE A1065 6049 6310 7607 169 -308 -282 C ATOM 2013 CG PHE A1065 -8.638 -50.661 21.893 1.00 61.04 C ANISOU 2013 CG PHE A1065 7115 7364 8713 190 -289 -306 C ATOM 2014 CD1 PHE A1065 -7.310 -50.308 22.065 1.00 62.76 C ANISOU 2014 CD1 PHE A1065 7316 7577 8952 174 -225 -323 C ATOM 2015 CD2 PHE A1065 -9.439 -49.866 21.090 1.00 67.58 C ANISOU 2015 CD2 PHE A1065 7964 8172 9542 230 -328 -308 C ATOM 2016 CE1 PHE A1065 -6.790 -49.183 21.451 1.00 65.19 C ANISOU 2016 CE1 PHE A1065 7626 7862 9281 198 -191 -341 C ATOM 2017 CE2 PHE A1065 -8.926 -48.739 20.472 1.00 68.01 C ANISOU 2017 CE2 PHE A1065 8030 8199 9611 260 -297 -327 C ATOM 2018 CZ PHE A1065 -7.600 -48.398 20.653 1.00 66.92 C ANISOU 2018 CZ PHE A1065 7876 8057 9495 245 -223 -344 C ATOM 2019 N ASP A1066 -10.035 -55.081 22.880 1.00 52.06 N ANISOU 2019 N ASP A1066 6006 6264 7511 149 -350 -262 N ATOM 2020 CA ASP A1066 -10.026 -56.328 23.641 1.00 53.25 C ANISOU 2020 CA ASP A1066 6150 6394 7690 130 -354 -266 C ATOM 2021 C ASP A1066 -9.170 -57.381 22.951 1.00 49.64 C ANISOU 2021 C ASP A1066 5685 5929 7246 127 -347 -294 C ATOM 2022 O ASP A1066 -8.452 -58.139 23.614 1.00 54.58 O ANISOU 2022 O ASP A1066 6302 6542 7892 108 -321 -304 O ATOM 2023 CB ASP A1066 -11.451 -56.848 23.833 1.00 57.12 C ANISOU 2023 CB ASP A1066 6649 6868 8187 135 -404 -248 C ATOM 2024 CG ASP A1066 -12.242 -56.035 24.836 1.00 65.71 C ANISOU 2024 CG ASP A1066 7740 7958 9267 132 -404 -219 C ATOM 2025 OD1 ASP A1066 -11.619 -55.379 25.697 1.00 69.74 O ANISOU 2025 OD1 ASP A1066 8245 8479 9776 121 -365 -214 O ATOM 2026 OD2 ASP A1066 -13.489 -56.060 24.767 1.00 70.53 O ANISOU 2026 OD2 ASP A1066 8362 8561 9875 140 -443 -200 O ATOM 2027 N ILE A1067 -9.242 -57.448 21.621 1.00 43.06 N ANISOU 2027 N ILE A1067 4853 5091 6418 148 -377 -314 N ATOM 2028 CA ILE A1067 -8.379 -58.357 20.874 1.00 42.34 C ANISOU 2028 CA ILE A1067 4747 4979 6361 148 -378 -354 C ATOM 2029 C ILE A1067 -6.925 -57.918 20.985 1.00 43.26 C ANISOU 2029 C ILE A1067 4844 5094 6501 133 -317 -377 C ATOM 2030 O ILE A1067 -6.023 -58.747 21.157 1.00 40.43 O ANISOU 2030 O ILE A1067 4480 4737 6144 115 -285 -387 O ATOM 2031 CB ILE A1067 -8.833 -58.434 19.406 1.00 41.69 C ANISOU 2031 CB ILE A1067 4667 4862 6313 184 -445 -390 C ATOM 2032 CG1 ILE A1067 -10.268 -58.954 19.313 1.00 45.69 C ANISOU 2032 CG1 ILE A1067 5201 5366 6794 194 -502 -364 C ATOM 2033 CG2 ILE A1067 -7.888 -59.313 18.598 1.00 42.79 C ANISOU 2033 CG2 ILE A1067 4789 4981 6486 189 -445 -435 C ATOM 2034 CD1 ILE A1067 -10.870 -58.829 17.928 1.00 45.33 C ANISOU 2034 CD1 ILE A1067 5176 5285 6764 234 -578 -392 C ATOM 2035 N LEU A1068 -6.676 -56.610 20.903 1.00 41.62 N ANISOU 2035 N LEU A1068 4627 4883 6306 139 -297 -382 N ATOM 2036 CA LEU A1068 -5.306 -56.107 20.906 1.00 38.37 C ANISOU 2036 CA LEU A1068 4197 4464 5916 125 -232 -403 C ATOM 2037 C LEU A1068 -4.613 -56.402 22.230 1.00 36.98 C ANISOU 2037 C LEU A1068 4036 4312 5702 90 -182 -373 C ATOM 2038 O LEU A1068 -3.500 -56.941 22.256 1.00 37.55 O ANISOU 2038 O LEU A1068 4106 4379 5783 72 -141 -388 O ATOM 2039 CB LEU A1068 -5.302 -54.607 20.619 1.00 40.45 C ANISOU 2039 CB LEU A1068 4455 4720 6192 143 -215 -407 C ATOM 2040 CG LEU A1068 -3.928 -53.984 20.380 1.00 42.30 C ANISOU 2040 CG LEU A1068 4678 4942 6452 135 -138 -429 C ATOM 2041 CD1 LEU A1068 -3.351 -54.487 19.070 1.00 44.03 C ANISOU 2041 CD1 LEU A1068 4899 5130 6698 167 -123 -472 C ATOM 2042 CD2 LEU A1068 -4.015 -52.467 20.392 1.00 42.25 C ANISOU 2042 CD2 LEU A1068 4680 4930 6442 153 -113 -420 C ATOM 2043 N VAL A1069 -5.259 -56.054 23.345 1.00 36.13 N ANISOU 2043 N VAL A1069 3950 4231 5545 85 -185 -331 N ATOM 2044 CA VAL A1069 -4.662 -56.294 24.655 1.00 39.35 C ANISOU 2044 CA VAL A1069 4364 4626 5962 63 -154 -325 C ATOM 2045 C VAL A1069 -4.527 -57.789 24.915 1.00 40.48 C ANISOU 2045 C VAL A1069 4505 4748 6126 56 -164 -338 C ATOM 2046 O VAL A1069 -3.514 -58.249 25.457 1.00 37.73 O ANISOU 2046 O VAL A1069 4160 4385 5792 41 -129 -349 O ATOM 2047 CB VAL A1069 -5.489 -55.597 25.751 1.00 45.75 C ANISOU 2047 CB VAL A1069 5179 5435 6767 64 -168 -301 C ATOM 2048 CG1 VAL A1069 -4.915 -55.898 27.128 1.00 45.16 C ANISOU 2048 CG1 VAL A1069 5109 5339 6710 48 -143 -299 C ATOM 2049 CG2 VAL A1069 -5.531 -54.097 25.505 1.00 46.35 C ANISOU 2049 CG2 VAL A1069 5258 5532 6823 71 -155 -290 C ATOM 2050 N GLY A1070 -5.538 -58.570 24.530 1.00 37.68 N ANISOU 2050 N GLY A1070 4150 4392 5776 69 -212 -336 N ATOM 2051 CA GLY A1070 -5.453 -60.010 24.711 1.00 38.74 C ANISOU 2051 CA GLY A1070 4283 4506 5932 65 -223 -347 C ATOM 2052 C GLY A1070 -4.324 -60.632 23.912 1.00 40.10 C ANISOU 2052 C GLY A1070 4451 4679 6108 60 -198 -374 C ATOM 2053 O GLY A1070 -3.620 -61.520 24.401 1.00 41.54 O ANISOU 2053 O GLY A1070 4633 4844 6307 49 -177 -385 O ATOM 2054 N GLN A1071 -4.138 -60.178 22.670 1.00 39.34 N ANISOU 2054 N GLN A1071 4351 4603 5996 69 -199 -383 N ATOM 2055 CA GLN A1071 -3.052 -60.703 21.851 1.00 40.07 C ANISOU 2055 CA GLN A1071 4436 4697 6089 63 -171 -406 C ATOM 2056 C GLN A1071 -1.689 -60.287 22.388 1.00 39.98 C ANISOU 2056 C GLN A1071 4428 4681 6082 40 -106 -410 C ATOM 2057 O GLN A1071 -0.718 -61.042 22.259 1.00 40.78 O ANISOU 2057 O GLN A1071 4530 4772 6193 29 -77 -427 O ATOM 2058 CB GLN A1071 -3.217 -60.245 20.405 1.00 40.45 C ANISOU 2058 CB GLN A1071 4454 4715 6199 85 -201 -454 C ATOM 2059 CG GLN A1071 -4.325 -60.955 19.654 1.00 42.76 C ANISOU 2059 CG GLN A1071 4748 4997 6501 111 -277 -464 C ATOM 2060 CD GLN A1071 -4.534 -60.388 18.268 1.00 44.85 C ANISOU 2060 CD GLN A1071 4996 5237 6807 150 -317 -507 C ATOM 2061 OE1 GLN A1071 -4.334 -59.194 18.037 1.00 48.12 O ANISOU 2061 OE1 GLN A1071 5406 5646 7232 165 -292 -513 O ATOM 2062 NE2 GLN A1071 -4.930 -61.242 17.332 1.00 42.15 N ANISOU 2062 NE2 GLN A1071 4659 4877 6478 177 -378 -534 N ATOM 2063 N ILE A1072 -1.596 -59.098 22.987 1.00 39.05 N ANISOU 2063 N ILE A1072 4316 4566 5957 35 -82 -394 N ATOM 2064 CA ILE A1072 -0.353 -58.687 23.630 1.00 38.98 C ANISOU 2064 CA ILE A1072 4315 4542 5953 15 -26 -396 C ATOM 2065 C ILE A1072 -0.071 -59.561 24.846 1.00 39.53 C ANISOU 2065 C ILE A1072 4393 4584 6042 8 -22 -400 C ATOM 2066 O ILE A1072 1.069 -59.985 25.073 1.00 40.10 O ANISOU 2066 O ILE A1072 4472 4639 6123 -4 16 -412 O ATOM 2067 CB ILE A1072 -0.413 -57.193 24.000 1.00 40.14 C ANISOU 2067 CB ILE A1072 4466 4698 6089 14 -9 -379 C ATOM 2068 CG1 ILE A1072 -0.405 -56.329 22.737 1.00 40.90 C ANISOU 2068 CG1 ILE A1072 4537 4784 6220 22 1 -402 C ATOM 2069 CG2 ILE A1072 0.742 -56.813 24.916 1.00 37.78 C ANISOU 2069 CG2 ILE A1072 4181 4375 5800 -4 39 -378 C ATOM 2070 CD1 ILE A1072 -0.538 -54.848 23.009 1.00 44.41 C ANISOU 2070 CD1 ILE A1072 4980 5228 6665 24 17 -390 C ATOM 2071 N ASP A1073 -1.107 -59.856 25.638 1.00 39.40 N ANISOU 2071 N ASP A1073 4377 4563 6031 17 -60 -387 N ATOM 2072 CA ASP A1073 -0.934 -60.727 26.797 1.00 40.77 C ANISOU 2072 CA ASP A1073 4556 4712 6222 14 -57 -388 C ATOM 2073 C ASP A1073 -0.537 -62.141 26.389 1.00 41.15 C ANISOU 2073 C ASP A1073 4601 4750 6283 14 -59 -408 C ATOM 2074 O ASP A1073 0.217 -62.801 27.114 1.00 41.94 O ANISOU 2074 O ASP A1073 4709 4830 6397 8 -36 -417 O ATOM 2075 CB ASP A1073 -2.215 -60.759 27.632 1.00 45.40 C ANISOU 2075 CB ASP A1073 5141 5296 6812 23 -96 -367 C ATOM 2076 CG ASP A1073 -2.536 -59.417 28.270 1.00 55.27 C ANISOU 2076 CG ASP A1073 6396 6555 8051 22 -91 -347 C ATOM 2077 OD1 ASP A1073 -1.595 -58.637 28.537 1.00 58.33 O ANISOU 2077 OD1 ASP A1073 6791 6938 8434 13 -54 -350 O ATOM 2078 OD2 ASP A1073 -3.733 -59.145 28.508 1.00 56.63 O ANISOU 2078 OD2 ASP A1073 6565 6734 8216 31 -126 -327 O ATOM 2079 N ASP A1074 -1.033 -62.626 25.246 1.00 41.52 N ANISOU 2079 N ASP A1074 4639 4811 6327 22 -88 -416 N ATOM 2080 CA ASP A1074 -0.657 -63.961 24.786 1.00 42.68 C ANISOU 2080 CA ASP A1074 4783 4949 6485 23 -92 -436 C ATOM 2081 C ASP A1074 0.830 -64.027 24.465 1.00 43.12 C ANISOU 2081 C ASP A1074 4843 5002 6540 10 -40 -453 C ATOM 2082 O ASP A1074 1.528 -64.958 24.882 1.00 43.97 O ANISOU 2082 O ASP A1074 4955 5092 6659 6 -22 -466 O ATOM 2083 CB ASP A1074 -1.480 -64.358 23.559 1.00 48.12 C ANISOU 2083 CB ASP A1074 5461 5652 7169 36 -138 -441 C ATOM 2084 CG ASP A1074 -2.955 -64.529 23.867 1.00 50.73 C ANISOU 2084 CG ASP A1074 5791 5978 7505 50 -192 -424 C ATOM 2085 OD1 ASP A1074 -3.323 -64.548 25.061 1.00 57.09 O ANISOU 2085 OD1 ASP A1074 6601 6770 8321 47 -192 -408 O ATOM 2086 OD2 ASP A1074 -3.748 -64.657 22.909 1.00 45.33 O ANISOU 2086 OD2 ASP A1074 5105 5303 6816 64 -236 -425 O ATOM 2087 N ALA A1075 1.333 -63.043 23.715 1.00 43.04 N ANISOU 2087 N ALA A1075 4833 5007 6515 2 -14 -453 N ATOM 2088 CA ALA A1075 2.746 -63.036 23.358 1.00 49.64 C ANISOU 2088 CA ALA A1075 5675 5837 7349 -12 40 -466 C ATOM 2089 C ALA A1075 3.630 -62.752 24.566 1.00 42.90 C ANISOU 2089 C ALA A1075 4839 4961 6500 -22 79 -461 C ATOM 2090 O ALA A1075 4.750 -63.270 24.646 1.00 43.61 O ANISOU 2090 O ALA A1075 4939 5053 6577 -31 113 -462 O ATOM 2091 CB ALA A1075 3.000 -62.011 22.253 1.00 44.05 C ANISOU 2091 CB ALA A1075 4963 5151 6624 -18 62 -462 C ATOM 2092 N LEU A1076 3.146 -61.942 25.511 1.00 42.60 N ANISOU 2092 N LEU A1076 4805 4919 6462 -19 71 -444 N ATOM 2093 CA LEU A1076 3.918 -61.658 26.717 1.00 47.61 C ANISOU 2093 CA LEU A1076 5456 5553 7080 -25 98 -427 C ATOM 2094 C LEU A1076 4.116 -62.912 27.556 1.00 45.29 C ANISOU 2094 C LEU A1076 5167 5259 6782 -23 91 -426 C ATOM 2095 O LEU A1076 5.204 -63.143 28.096 1.00 45.40 O ANISOU 2095 O LEU A1076 5195 5275 6780 -29 121 -422 O ATOM 2096 CB LEU A1076 3.226 -60.572 27.543 1.00 50.84 C ANISOU 2096 CB LEU A1076 5867 5958 7491 -21 85 -411 C ATOM 2097 CG LEU A1076 3.781 -59.153 27.435 1.00 55.12 C ANISOU 2097 CG LEU A1076 6417 6501 8026 -28 116 -402 C ATOM 2098 CD1 LEU A1076 2.907 -58.173 28.204 1.00 56.93 C ANISOU 2098 CD1 LEU A1076 6645 6727 8258 -22 95 -386 C ATOM 2099 CD2 LEU A1076 5.216 -59.105 27.937 1.00 53.92 C ANISOU 2099 CD2 LEU A1076 6284 6350 7855 -38 158 -394 C ATOM 2100 N LYS A1077 3.071 -63.732 27.686 1.00 49.30 N ANISOU 2100 N LYS A1077 5664 5762 7305 -12 51 -429 N ATOM 2101 CA LYS A1077 3.200 -64.973 28.441 1.00 47.58 C ANISOU 2101 CA LYS A1077 5449 5543 7086 -10 44 -428 C ATOM 2102 C LYS A1077 4.188 -65.922 27.775 1.00 48.30 C ANISOU 2102 C LYS A1077 5543 5640 7170 -16 65 -444 C ATOM 2103 O LYS A1077 4.938 -66.629 28.458 1.00 47.92 O ANISOU 2103 O LYS A1077 5504 5593 7109 -19 82 -441 O ATOM 2104 CB LYS A1077 1.833 -65.640 28.593 1.00 46.66 C ANISOU 2104 CB LYS A1077 5320 5417 6991 2 -4 -426 C ATOM 2105 CG LYS A1077 1.885 -66.980 29.296 1.00 49.81 C ANISOU 2105 CG LYS A1077 5721 5812 7393 4 -11 -425 C ATOM 2106 CD LYS A1077 0.501 -67.566 29.481 1.00 52.04 C ANISOU 2106 CD LYS A1077 5992 6080 7699 15 -57 -419 C ATOM 2107 CE LYS A1077 0.588 -68.957 30.076 1.00 57.04 C ANISOU 2107 CE LYS A1077 6626 6709 8339 16 -62 -419 C ATOM 2108 NZ LYS A1077 1.244 -69.920 29.149 1.00 58.34 N ANISOU 2108 NZ LYS A1077 6787 6879 8500 16 -55 -439 N ATOM 2109 N LEU A1078 4.205 -65.949 26.441 1.00 46.65 N ANISOU 2109 N LEU A1078 5324 5434 6967 -16 65 -459 N ATOM 2110 CA LEU A1078 5.165 -66.790 25.734 1.00 46.28 C ANISOU 2110 CA LEU A1078 5279 5393 6912 -23 87 -473 C ATOM 2111 C LEU A1078 6.584 -66.262 25.901 1.00 47.78 C ANISOU 2111 C LEU A1078 5487 5586 7081 -37 138 -466 C ATOM 2112 O LEU A1078 7.532 -67.045 26.040 1.00 47.17 O ANISOU 2112 O LEU A1078 5420 5512 6992 -42 159 -469 O ATOM 2113 CB LEU A1078 4.794 -66.881 24.255 1.00 46.44 C ANISOU 2113 CB LEU A1078 5285 5415 6944 -20 72 -492 C ATOM 2114 CG LEU A1078 3.467 -67.571 23.939 1.00 51.37 C ANISOU 2114 CG LEU A1078 5894 6035 7590 -4 15 -500 C ATOM 2115 CD1 LEU A1078 3.068 -67.314 22.497 1.00 47.41 C ANISOU 2115 CD1 LEU A1078 5381 5537 7098 1 -5 -518 C ATOM 2116 CD2 LEU A1078 3.564 -69.065 24.214 1.00 47.83 C ANISOU 2116 CD2 LEU A1078 5445 5585 7145 0 3 -506 C ATOM 2117 N ALA A1079 6.749 -64.936 25.892 1.00 48.41 N ANISOU 2117 N ALA A1079 5573 5664 7157 -42 157 -456 N ATOM 2118 CA ALA A1079 8.071 -64.352 26.096 1.00 50.75 C ANISOU 2118 CA ALA A1079 5889 5960 7435 -53 202 -446 C ATOM 2119 C ALA A1079 8.578 -64.599 27.512 1.00 53.09 C ANISOU 2119 C ALA A1079 6200 6256 7717 -51 206 -433 C ATOM 2120 O ALA A1079 9.779 -64.820 27.716 1.00 55.00 O ANISOU 2120 O ALA A1079 6457 6498 7943 -58 234 -429 O ATOM 2121 CB ALA A1079 8.038 -62.855 25.793 1.00 47.39 C ANISOU 2121 CB ALA A1079 5465 5530 7011 -57 219 -437 C ATOM 2122 N ASN A1080 7.686 -64.556 28.508 1.00 55.29 N ANISOU 2122 N ASN A1080 6474 6533 8000 -43 176 -425 N ATOM 2123 CA ASN A1080 8.116 -64.814 29.878 1.00 57.69 C ANISOU 2123 CA ASN A1080 6791 6837 8291 -41 178 -413 C ATOM 2124 C ASN A1080 8.543 -66.263 30.067 1.00 56.11 C ANISOU 2124 C ASN A1080 6593 6640 8085 -41 177 -421 C ATOM 2125 O ASN A1080 9.334 -66.565 30.968 1.00 56.17 O ANISOU 2125 O ASN A1080 6616 6649 8077 -42 189 -414 O ATOM 2126 CB ASN A1080 6.995 -64.459 30.853 1.00 58.09 C ANISOU 2126 CB ASN A1080 6837 6885 8350 -33 149 -402 C ATOM 2127 CG ASN A1080 6.804 -62.967 31.000 1.00 62.78 C ANISOU 2127 CG ASN A1080 7434 7477 8943 -34 154 -391 C ATOM 2128 OD1 ASN A1080 7.768 -62.202 30.949 1.00 67.72 O ANISOU 2128 OD1 ASN A1080 8072 8103 9557 -40 183 -385 O ATOM 2129 ND2 ASN A1080 5.564 -62.541 31.173 1.00 61.40 N ANISOU 2129 ND2 ASN A1080 7248 7299 8783 -27 125 -386 N ATOM 2130 N GLU A1081 8.040 -67.166 29.230 1.00 53.42 N ANISOU 2130 N GLU A1081 6239 6301 7758 -38 161 -436 N ATOM 2131 CA GLU A1081 8.428 -68.569 29.253 1.00 55.72 C ANISOU 2131 CA GLU A1081 6531 6595 8046 -38 160 -445 C ATOM 2132 C GLU A1081 9.694 -68.848 28.451 1.00 54.19 C ANISOU 2132 C GLU A1081 6346 6405 7839 -47 193 -453 C ATOM 2133 O GLU A1081 10.104 -70.010 28.352 1.00 53.74 O ANISOU 2133 O GLU A1081 6290 6351 7777 -48 194 -461 O ATOM 2134 CB GLU A1081 7.283 -69.435 28.722 1.00 58.89 C ANISOU 2134 CB GLU A1081 6913 6994 8470 -29 124 -457 C ATOM 2135 CG GLU A1081 6.042 -69.431 29.600 1.00 64.55 C ANISOU 2135 CG GLU A1081 7622 7703 9202 -19 89 -447 C ATOM 2136 CD GLU A1081 4.877 -70.147 28.947 1.00 72.76 C ANISOU 2136 CD GLU A1081 8644 8737 10267 -10 51 -456 C ATOM 2137 OE1 GLU A1081 4.991 -70.481 27.752 1.00 75.25 O ANISOU 2137 OE1 GLU A1081 8951 9055 10587 -10 49 -472 O ATOM 2138 OE2 GLU A1081 3.851 -70.376 29.624 1.00 76.26 O ANISOU 2138 OE2 GLU A1081 9080 9170 10724 -2 21 -447 O ATOM 2139 N GLY A1082 10.255 -67.818 27.854 1.00 51.88 N ANISOU 2139 N GLY A1082 6059 6110 7541 -55 219 -449 N ATOM 2140 CA GLY A1082 11.447 -67.969 27.070 1.00 52.40 C ANISOU 2140 CA GLY A1082 6136 6178 7597 -65 253 -454 C ATOM 2141 C GLY A1082 11.212 -68.496 25.681 1.00 53.21 C ANISOU 2141 C GLY A1082 6225 6283 7711 -68 252 -471 C ATOM 2142 O GLY A1082 12.157 -68.803 25.000 1.00 58.22 O ANISOU 2142 O GLY A1082 6867 6916 8337 -76 280 -475 O ATOM 2143 N LYS A1083 9.967 -68.617 25.259 1.00 49.33 N ANISOU 2143 N LYS A1083 5713 5792 7238 -60 218 -481 N ATOM 2144 CA LYS A1083 9.703 -69.095 23.924 1.00 49.78 C ANISOU 2144 CA LYS A1083 5756 5852 7306 -60 211 -499 C ATOM 2145 C LYS A1083 9.688 -67.934 22.944 1.00 50.64 C ANISOU 2145 C LYS A1083 5863 5959 7421 -67 230 -500 C ATOM 2146 O LYS A1083 8.639 -67.434 22.597 1.00 49.04 O ANISOU 2146 O LYS A1083 5645 5756 7233 -60 203 -504 O ATOM 2147 CB LYS A1083 8.392 -69.853 23.888 1.00 52.86 C ANISOU 2147 CB LYS A1083 6126 6243 7715 -46 161 -510 C ATOM 2148 CG LYS A1083 8.179 -70.769 25.076 1.00 55.52 C ANISOU 2148 CG LYS A1083 6465 6578 8050 -39 142 -504 C ATOM 2149 CD LYS A1083 6.848 -71.483 24.982 1.00 58.42 C ANISOU 2149 CD LYS A1083 6815 6941 8441 -24 92 -512 C ATOM 2150 CE LYS A1083 6.732 -72.562 26.034 1.00 57.61 C ANISOU 2150 CE LYS A1083 6716 6835 8339 -19 79 -507 C ATOM 2151 NZ LYS A1083 5.408 -73.215 26.012 1.00 56.56 N ANISOU 2151 NZ LYS A1083 6567 6692 8231 -5 30 -510 N ATOM 2152 N VAL A1084 10.856 -67.528 22.471 1.00 49.29 N ANISOU 2152 N VAL A1084 5708 5784 7237 -81 277 -494 N ATOM 2153 CA VAL A1084 10.942 -66.405 21.568 1.00 49.50 C ANISOU 2153 CA VAL A1084 5736 5805 7268 -89 303 -491 C ATOM 2154 C VAL A1084 10.245 -66.558 20.231 1.00 48.80 C ANISOU 2154 C VAL A1084 5626 5720 7194 -89 289 -510 C ATOM 2155 O VAL A1084 9.517 -65.681 19.820 1.00 47.80 O ANISOU 2155 O VAL A1084 5490 5592 7080 -86 280 -511 O ATOM 2156 CB VAL A1084 12.389 -66.106 21.235 1.00 54.50 C ANISOU 2156 CB VAL A1084 6393 6428 7886 -104 359 -479 C ATOM 2157 CG1 VAL A1084 12.503 -64.718 20.655 1.00 53.32 C ANISOU 2157 CG1 VAL A1084 6251 6267 7740 -111 392 -467 C ATOM 2158 CG2 VAL A1084 13.232 -66.242 22.475 1.00 61.74 C ANISOU 2158 CG2 VAL A1084 7328 7343 8787 -102 367 -464 C ATOM 2159 N LYS A1085 10.431 -67.687 19.571 1.00 49.74 N ANISOU 2159 N LYS A1085 5739 5845 7315 -89 283 -526 N ATOM 2160 CA LYS A1085 9.803 -67.890 18.281 1.00 52.75 C ANISOU 2160 CA LYS A1085 6089 6221 7734 -88 270 -559 C ATOM 2161 C LYS A1085 8.297 -67.896 18.380 1.00 49.63 C ANISOU 2161 C LYS A1085 5669 5829 7361 -67 203 -573 C ATOM 2162 O LYS A1085 7.619 -67.372 17.533 1.00 49.58 O ANISOU 2162 O LYS A1085 5624 5804 7410 -64 190 -609 O ATOM 2163 CB LYS A1085 10.297 -69.168 17.626 1.00 55.60 C ANISOU 2163 CB LYS A1085 6443 6584 8097 -92 272 -578 C ATOM 2164 CG LYS A1085 11.758 -69.122 17.273 1.00 59.90 C ANISOU 2164 CG LYS A1085 7013 7118 8630 -114 342 -568 C ATOM 2165 CD LYS A1085 12.007 -68.361 15.995 1.00 63.40 C ANISOU 2165 CD LYS A1085 7430 7524 9133 -136 405 -598 C ATOM 2166 CE LYS A1085 13.502 -68.185 15.795 1.00 67.09 C ANISOU 2166 CE LYS A1085 7940 7976 9577 -157 482 -571 C ATOM 2167 NZ LYS A1085 13.877 -68.038 14.374 1.00 69.55 N ANISOU 2167 NZ LYS A1085 8232 8252 9943 -180 562 -598 N ATOM 2168 N GLU A1086 7.786 -68.536 19.407 1.00 49.47 N ANISOU 2168 N GLU A1086 5660 5822 7315 -53 163 -555 N ATOM 2169 CA GLU A1086 6.364 -68.570 19.612 1.00 51.05 C ANISOU 2169 CA GLU A1086 5845 6022 7531 -33 101 -560 C ATOM 2170 C GLU A1086 5.825 -67.162 19.916 1.00 47.69 C ANISOU 2170 C GLU A1086 5420 5595 7106 -33 101 -545 C ATOM 2171 O GLU A1086 4.776 -66.795 19.441 1.00 47.28 O ANISOU 2171 O GLU A1086 5348 5549 7065 -20 59 -550 O ATOM 2172 CB GLU A1086 5.993 -69.566 20.702 1.00 53.47 C ANISOU 2172 CB GLU A1086 6153 6324 7839 -23 74 -554 C ATOM 2173 CG GLU A1086 5.025 -70.607 20.202 1.00 65.60 C ANISOU 2173 CG GLU A1086 7674 7858 9391 -5 15 -570 C ATOM 2174 CD GLU A1086 4.209 -71.265 21.290 1.00 72.73 C ANISOU 2174 CD GLU A1086 8578 8752 10305 7 -19 -560 C ATOM 2175 OE1 GLU A1086 4.809 -71.898 22.171 1.00 72.45 O ANISOU 2175 OE1 GLU A1086 8551 8715 10261 1 3 -551 O ATOM 2176 OE2 GLU A1086 2.961 -71.158 21.243 1.00 72.88 O ANISOU 2176 OE2 GLU A1086 8589 8761 10340 22 -69 -559 O ATOM 2177 N ALA A1087 6.555 -66.401 20.720 1.00 47.18 N ANISOU 2177 N ALA A1087 5372 5523 7031 -45 145 -527 N ATOM 2178 CA ALA A1087 6.143 -65.054 21.068 1.00 46.03 C ANISOU 2178 CA ALA A1087 5229 5373 6888 -45 148 -514 C ATOM 2179 C ALA A1087 6.108 -64.169 19.834 1.00 47.08 C ANISOU 2179 C ALA A1087 5339 5500 7049 -52 168 -532 C ATOM 2180 O ALA A1087 5.162 -63.449 19.615 1.00 45.11 O ANISOU 2180 O ALA A1087 5068 5250 6822 -42 140 -538 O ATOM 2181 CB ALA A1087 7.053 -64.472 22.120 1.00 45.61 C ANISOU 2181 CB ALA A1087 5196 5314 6818 -56 189 -492 C ATOM 2182 N GLN A1088 7.124 -64.282 19.003 1.00 46.63 N ANISOU 2182 N GLN A1088 5276 5421 7019 -69 221 -555 N ATOM 2183 CA GLN A1088 7.179 -63.512 17.794 1.00 48.79 C ANISOU 2183 CA GLN A1088 5516 5675 7348 -79 259 -584 C ATOM 2184 C GLN A1088 6.005 -63.885 16.893 1.00 51.11 C ANISOU 2184 C GLN A1088 5766 5982 7672 -46 197 -618 C ATOM 2185 O GLN A1088 5.279 -63.039 16.444 1.00 57.73 O ANISOU 2185 O GLN A1088 6596 6825 8514 -8 184 -623 O ATOM 2186 CB GLN A1088 8.511 -63.718 17.105 1.00 47.79 C ANISOU 2186 CB GLN A1088 5399 5532 7227 -102 337 -589 C ATOM 2187 CG GLN A1088 9.629 -62.926 17.729 1.00 47.41 C ANISOU 2187 CG GLN A1088 5397 5472 7144 -119 397 -549 C ATOM 2188 CD GLN A1088 11.001 -63.410 17.325 1.00 52.79 C ANISOU 2188 CD GLN A1088 6106 6144 7809 -136 457 -538 C ATOM 2189 OE1 GLN A1088 11.268 -64.591 17.351 1.00 49.18 O ANISOU 2189 OE1 GLN A1088 5652 5702 7331 -133 435 -543 O ATOM 2190 NE2 GLN A1088 11.876 -62.492 16.980 1.00 48.23 N ANISOU 2190 NE2 GLN A1088 5552 5540 7233 -151 532 -518 N ATOM 2191 N ALA A1089 5.772 -65.164 16.693 1.00 48.05 N ANISOU 2191 N ALA A1089 5370 5598 7290 -39 149 -639 N ATOM 2192 CA ALA A1089 4.662 -65.579 15.841 1.00 48.47 C ANISOU 2192 CA ALA A1089 5394 5659 7362 8 72 -670 C ATOM 2193 C ALA A1089 3.329 -65.095 16.397 1.00 51.91 C ANISOU 2193 C ALA A1089 5831 6100 7793 24 2 -654 C ATOM 2194 O ALA A1089 2.425 -64.735 15.634 1.00 51.00 O ANISOU 2194 O ALA A1089 5712 5981 7683 78 -49 -670 O ATOM 2195 CB ALA A1089 4.659 -67.098 15.680 1.00 49.54 C ANISOU 2195 CB ALA A1089 5525 5793 7504 4 27 -691 C ATOM 2196 N ALA A1090 3.187 -65.080 17.725 1.00 46.61 N ANISOU 2196 N ALA A1090 5194 5437 7081 6 2 -610 N ATOM 2197 CA ALA A1090 1.961 -64.571 18.331 1.00 45.60 C ANISOU 2197 CA ALA A1090 5074 5320 6931 24 -48 -582 C ATOM 2198 C ALA A1090 1.847 -63.062 18.154 1.00 47.59 C ANISOU 2198 C ALA A1090 5312 5568 7201 26 -26 -583 C ATOM 2199 O ALA A1090 0.747 -62.536 17.949 1.00 44.19 O ANISOU 2199 O ALA A1090 4874 5140 6776 53 -79 -582 O ATOM 2200 CB ALA A1090 1.910 -64.944 19.812 1.00 45.01 C ANISOU 2200 CB ALA A1090 5041 5274 6787 15 -41 -524 C ATOM 2201 N ALA A1091 2.974 -62.351 18.232 1.00 44.57 N ANISOU 2201 N ALA A1091 4934 5179 6822 2 54 -579 N ATOM 2202 CA ALA A1091 2.963 -60.911 18.013 1.00 47.16 C ANISOU 2202 CA ALA A1091 5256 5503 7158 11 89 -574 C ATOM 2203 C ALA A1091 2.654 -60.554 16.567 1.00 51.80 C ANISOU 2203 C ALA A1091 5861 6073 7748 79 92 -605 C ATOM 2204 O ALA A1091 2.206 -59.434 16.300 1.00 52.50 O ANISOU 2204 O ALA A1091 5986 6144 7817 115 98 -601 O ATOM 2205 CB ALA A1091 4.303 -60.302 18.428 1.00 43.63 C ANISOU 2205 CB ALA A1091 4831 5046 6700 -25 177 -554 C ATOM 2206 N GLU A1092 2.881 -61.479 15.630 1.00 50.07 N ANISOU 2206 N GLU A1092 5667 5836 7522 107 85 -635 N ATOM 2207 CA GLU A1092 2.546 -61.214 14.236 1.00 56.53 C ANISOU 2207 CA GLU A1092 6587 6603 8289 178 76 -662 C ATOM 2208 C GLU A1092 1.039 -61.125 14.031 1.00 49.97 C ANISOU 2208 C GLU A1092 5768 5765 7455 221 -26 -668 C ATOM 2209 O GLU A1092 0.579 -60.450 13.103 1.00 48.45 O ANISOU 2209 O GLU A1092 5671 5536 7204 266 -38 -674 O ATOM 2210 CB GLU A1092 3.144 -62.297 13.337 1.00 67.60 C ANISOU 2210 CB GLU A1092 8029 7986 9670 193 84 -689 C ATOM 2211 CG GLU A1092 3.373 -61.854 11.901 1.00 78.91 C ANISOU 2211 CG GLU A1092 9595 9365 11024 247 114 -706 C ATOM 2212 CD GLU A1092 4.529 -60.880 11.772 1.00 88.23 C ANISOU 2212 CD GLU A1092 10819 10529 12175 234 228 -685 C ATOM 2213 OE1 GLU A1092 5.504 -61.007 12.543 1.00 93.20 O ANISOU 2213 OE1 GLU A1092 11388 11186 12839 180 289 -665 O ATOM 2214 OE2 GLU A1092 4.463 -59.985 10.903 1.00 89.60 O ANISOU 2214 OE2 GLU A1092 11091 10675 12277 270 250 -676 O ATOM 2215 N GLN A1093 0.259 -61.792 14.885 1.00 45.26 N ANISOU 2215 N GLN A1093 5084 5210 6904 196 -102 -655 N ATOM 2216 CA GLN A1093 -1.194 -61.709 14.800 1.00 48.49 C ANISOU 2216 CA GLN A1093 5497 5616 7310 229 -200 -649 C ATOM 2217 C GLN A1093 -1.705 -60.306 15.092 1.00 45.69 C ANISOU 2217 C GLN A1093 5162 5256 6940 241 -189 -627 C ATOM 2218 O GLN A1093 -2.829 -59.973 14.701 1.00 43.75 O ANISOU 2218 O GLN A1093 4953 4993 6676 280 -257 -624 O ATOM 2219 CB GLN A1093 -1.833 -62.705 15.769 1.00 53.03 C ANISOU 2219 CB GLN A1093 6005 6232 7911 180 -268 -628 C ATOM 2220 CG GLN A1093 -1.264 -64.108 15.675 1.00 57.90 C ANISOU 2220 CG GLN A1093 6607 6853 8541 157 -272 -645 C ATOM 2221 CD GLN A1093 -1.521 -64.750 14.329 1.00 60.36 C ANISOU 2221 CD GLN A1093 6951 7136 8847 220 -327 -682 C ATOM 2222 OE1 GLN A1093 -2.668 -64.919 13.918 1.00 62.62 O ANISOU 2222 OE1 GLN A1093 7261 7410 9121 255 -415 -681 O ATOM 2223 NE2 GLN A1093 -0.450 -65.107 13.630 1.00 64.07 N ANISOU 2223 NE2 GLN A1093 7453 7587 9304 233 -269 -710 N ATOM 2224 N LEU A1094 -0.905 -59.481 15.772 1.00 43.14 N ANISOU 2224 N LEU A1094 4819 4948 6623 205 -108 -610 N ATOM 2225 CA LEU A1094 -1.317 -58.114 16.068 1.00 45.47 C ANISOU 2225 CA LEU A1094 5133 5240 6905 214 -94 -589 C ATOM 2226 C LEU A1094 -1.526 -57.300 14.799 1.00 50.03 C ANISOU 2226 C LEU A1094 5828 5766 7417 266 -83 -603 C ATOM 2227 O LEU A1094 -2.353 -56.380 14.784 1.00 51.07 O ANISOU 2227 O LEU A1094 5989 5893 7521 283 -111 -586 O ATOM 2228 CB LEU A1094 -0.279 -57.443 16.966 1.00 42.57 C ANISOU 2228 CB LEU A1094 4732 4895 6548 162 -8 -566 C ATOM 2229 CG LEU A1094 -0.157 -58.015 18.379 1.00 43.91 C ANISOU 2229 CG LEU A1094 4850 5105 6728 92 -22 -536 C ATOM 2230 CD1 LEU A1094 1.196 -57.682 18.980 1.00 42.60 C ANISOU 2230 CD1 LEU A1094 4689 4939 6558 46 63 -522 C ATOM 2231 CD2 LEU A1094 -1.275 -57.480 19.255 1.00 44.75 C ANISOU 2231 CD2 LEU A1094 4962 5229 6813 89 -72 -502 C ATOM 2232 N LYS A1095 -0.793 -57.618 13.728 1.00 53.42 N ANISOU 2232 N LYS A1095 6335 6167 7796 280 -44 -621 N ATOM 2233 CA LYS A1095 -0.957 -56.883 12.479 1.00 56.81 C ANISOU 2233 CA LYS A1095 6888 6560 8137 319 -33 -623 C ATOM 2234 C LYS A1095 -2.345 -57.084 11.887 1.00 54.52 C ANISOU 2234 C LYS A1095 6639 6257 7819 359 -134 -627 C ATOM 2235 O LYS A1095 -2.893 -56.167 11.267 1.00 53.16 O ANISOU 2235 O LYS A1095 6544 6066 7590 385 -142 -619 O ATOM 2236 CB LYS A1095 0.116 -57.302 11.476 1.00 59.91 C ANISOU 2236 CB LYS A1095 7351 6928 8485 330 28 -640 C ATOM 2237 CG LYS A1095 1.508 -56.840 11.850 1.00 66.14 C ANISOU 2237 CG LYS A1095 8124 7720 9286 297 137 -628 C ATOM 2238 CD LYS A1095 2.531 -57.302 10.835 1.00 74.30 C ANISOU 2238 CD LYS A1095 9228 8728 10275 312 195 -640 C ATOM 2239 CE LYS A1095 3.887 -56.691 11.121 1.00 80.35 C ANISOU 2239 CE LYS A1095 9988 9490 11050 283 306 -621 C ATOM 2240 NZ LYS A1095 4.940 -57.233 10.219 1.00 84.36 N ANISOU 2240 NZ LYS A1095 10557 9976 11522 297 365 -628 N ATOM 2241 N THR A1096 -2.926 -58.272 12.065 1.00 53.13 N ANISOU 2241 N THR A1096 6412 6090 7686 364 -214 -640 N ATOM 2242 CA THR A1096 -4.300 -58.490 11.624 1.00 52.33 C ANISOU 2242 CA THR A1096 6339 5974 7570 400 -318 -639 C ATOM 2243 C THR A1096 -5.265 -57.591 12.387 1.00 48.24 C ANISOU 2243 C THR A1096 5785 5472 7072 395 -352 -609 C ATOM 2244 O THR A1096 -6.175 -56.999 11.795 1.00 45.82 O ANISOU 2244 O THR A1096 5546 5144 6719 424 -394 -600 O ATOM 2245 CB THR A1096 -4.680 -59.961 11.796 1.00 54.24 C ANISOU 2245 CB THR A1096 6519 6224 7867 403 -398 -654 C ATOM 2246 OG1 THR A1096 -3.808 -60.778 11.003 1.00 55.72 O ANISOU 2246 OG1 THR A1096 6749 6394 8028 412 -369 -683 O ATOM 2247 CG2 THR A1096 -6.120 -60.197 11.363 1.00 53.97 C ANISOU 2247 CG2 THR A1096 6511 6170 7824 442 -511 -649 C ATOM 2248 N THR A1097 -5.073 -57.469 13.703 1.00 48.97 N ANISOU 2248 N THR A1097 5773 5601 7232 359 -331 -592 N ATOM 2249 CA THR A1097 -5.916 -56.582 14.498 1.00 48.06 C ANISOU 2249 CA THR A1097 5621 5504 7135 355 -357 -561 C ATOM 2250 C THR A1097 -5.682 -55.121 14.135 1.00 46.27 C ANISOU 2250 C THR A1097 5471 5263 6846 358 -294 -550 C ATOM 2251 O THR A1097 -6.622 -54.318 14.152 1.00 43.64 O ANISOU 2251 O THR A1097 5163 4927 6492 373 -331 -530 O ATOM 2252 CB THR A1097 -5.655 -56.806 15.988 1.00 47.33 C ANISOU 2252 CB THR A1097 5414 5470 7099 301 -340 -535 C ATOM 2253 OG1 THR A1097 -5.745 -58.207 16.289 1.00 50.67 O ANISOU 2253 OG1 THR A1097 5792 5920 7541 270 -381 -535 O ATOM 2254 CG2 THR A1097 -6.667 -56.049 16.832 1.00 45.58 C ANISOU 2254 CG2 THR A1097 5172 5278 6869 285 -373 -493 C ATOM 2255 N ARG A1098 -4.441 -54.766 13.798 1.00 47.72 N ANISOU 2255 N ARG A1098 5692 5437 7001 344 -201 -561 N ATOM 2256 CA ARG A1098 -4.127 -53.381 13.460 1.00 49.77 C ANISOU 2256 CA ARG A1098 6019 5684 7206 347 -138 -548 C ATOM 2257 C ARG A1098 -4.832 -52.946 12.181 1.00 49.21 C ANISOU 2257 C ARG A1098 6062 5580 7057 388 -169 -553 C ATOM 2258 O ARG A1098 -5.368 -51.833 12.107 1.00 49.30 O ANISOU 2258 O ARG A1098 6109 5587 7036 396 -170 -535 O ATOM 2259 CB ARG A1098 -2.616 -53.210 13.320 1.00 48.84 C ANISOU 2259 CB ARG A1098 5916 5560 7080 327 -34 -556 C ATOM 2260 CG ARG A1098 -2.177 -51.832 12.865 1.00 47.82 C ANISOU 2260 CG ARG A1098 5857 5414 6897 332 34 -542 C ATOM 2261 CD ARG A1098 -0.758 -51.876 12.334 1.00 50.15 C ANISOU 2261 CD ARG A1098 6190 5693 7173 326 125 -549 C ATOM 2262 NE ARG A1098 -0.640 -52.811 11.219 1.00 51.85 N ANISOU 2262 NE ARG A1098 6467 5885 7348 355 111 -573 N ATOM 2263 CZ ARG A1098 0.513 -53.190 10.678 1.00 52.25 C ANISOU 2263 CZ ARG A1098 6549 5920 7382 355 178 -581 C ATOM 2264 NH1 ARG A1098 1.657 -52.717 11.152 1.00 50.00 N ANISOU 2264 NH1 ARG A1098 6238 5639 7121 326 264 -566 N ATOM 2265 NH2 ARG A1098 0.521 -54.047 9.666 1.00 54.33 N ANISOU 2265 NH2 ARG A1098 6871 6163 7606 386 156 -603 N ATOM 2266 N ASN A1099 -4.846 -53.810 11.165 1.00 48.78 N ANISOU 2266 N ASN A1099 6064 5501 6971 415 -196 -576 N ATOM 2267 CA ASN A1099 -5.453 -53.447 9.890 1.00 53.07 C ANISOU 2267 CA ASN A1099 6718 6009 7437 457 -224 -583 C ATOM 2268 C ASN A1099 -6.971 -53.381 9.994 1.00 56.49 C ANISOU 2268 C ASN A1099 7148 6440 7875 473 -323 -570 C ATOM 2269 O ASN A1099 -7.598 -52.466 9.450 1.00 66.64 O ANISOU 2269 O ASN A1099 8502 7709 9110 492 -332 -560 O ATOM 2270 CB ASN A1099 -5.036 -54.444 8.808 1.00 53.68 C ANISOU 2270 CB ASN A1099 6857 6060 7480 485 -230 -613 C ATOM 2271 CG ASN A1099 -3.532 -54.556 8.669 1.00 56.66 C ANISOU 2271 CG ASN A1099 7240 6438 7851 470 -131 -622 C ATOM 2272 OD1 ASN A1099 -2.794 -53.640 9.028 1.00 57.57 O ANISOU 2272 OD1 ASN A1099 7347 6562 7965 448 -52 -606 O ATOM 2273 ND2 ASN A1099 -3.069 -55.686 8.145 1.00 58.00 N ANISOU 2273 ND2 ASN A1099 7423 6596 8017 483 -138 -646 N ATOM 2274 N ALA A1100 -7.579 -54.337 10.693 1.00 50.27 N ANISOU 2274 N ALA A1100 6279 5668 7152 467 -396 -567 N ATOM 2275 CA ALA A1100 -9.029 -54.456 10.732 1.00 48.75 C ANISOU 2275 CA ALA A1100 6083 5469 6971 487 -498 -551 C ATOM 2276 C ALA A1100 -9.686 -53.597 11.803 1.00 51.31 C ANISOU 2276 C ALA A1100 6348 5820 7329 468 -509 -515 C ATOM 2277 O ALA A1100 -10.905 -53.399 11.749 1.00 55.52 O ANISOU 2277 O ALA A1100 6893 6343 7858 486 -582 -496 O ATOM 2278 CB ALA A1100 -9.431 -55.919 10.947 1.00 50.35 C ANISOU 2278 CB ALA A1100 6224 5673 7231 493 -579 -560 C ATOM 2279 N TYR A1101 -8.923 -53.082 12.767 1.00 48.20 N ANISOU 2279 N TYR A1101 5890 5457 6965 435 -441 -506 N ATOM 2280 CA TYR A1101 -9.524 -52.337 13.868 1.00 48.39 C ANISOU 2280 CA TYR A1101 5852 5510 7025 421 -454 -472 C ATOM 2281 C TYR A1101 -8.775 -51.048 14.182 1.00 49.00 C ANISOU 2281 C TYR A1101 5941 5597 7079 400 -365 -464 C ATOM 2282 O TYR A1101 -9.365 -49.963 14.162 1.00 45.97 O ANISOU 2282 O TYR A1101 5592 5211 6664 406 -369 -444 O ATOM 2283 CB TYR A1101 -9.590 -53.203 15.129 1.00 49.14 C ANISOU 2283 CB TYR A1101 5821 5641 7210 402 -487 -462 C ATOM 2284 CG TYR A1101 -10.551 -54.367 15.042 1.00 52.72 C ANISOU 2284 CG TYR A1101 6255 6108 7669 401 -576 -450 C ATOM 2285 CD1 TYR A1101 -11.903 -54.201 15.324 1.00 53.96 C ANISOU 2285 CD1 TYR A1101 6414 6282 7806 392 -637 -411 C ATOM 2286 CD2 TYR A1101 -10.106 -55.636 14.693 1.00 47.64 C ANISOU 2286 CD2 TYR A1101 5597 5460 7042 398 -589 -474 C ATOM 2287 CE1 TYR A1101 -12.784 -55.266 15.252 1.00 52.40 C ANISOU 2287 CE1 TYR A1101 6215 6094 7603 377 -700 -399 C ATOM 2288 CE2 TYR A1101 -10.978 -56.704 14.618 1.00 49.06 C ANISOU 2288 CE2 TYR A1101 5769 5653 7221 387 -664 -463 C ATOM 2289 CZ TYR A1101 -12.316 -56.514 14.899 1.00 53.88 C ANISOU 2289 CZ TYR A1101 6390 6275 7808 374 -714 -425 C ATOM 2290 OH TYR A1101 -13.186 -57.578 14.825 1.00 57.79 O ANISOU 2290 OH TYR A1101 6891 6771 8296 358 -768 -414 O ATOM 2291 N ILE A1102 -7.478 -51.159 14.481 1.00 50.83 N ANISOU 2291 N ILE A1102 6144 5840 7330 375 -288 -478 N ATOM 2292 CA ILE A1102 -6.738 -50.029 15.036 1.00 51.16 C ANISOU 2292 CA ILE A1102 6175 5894 7370 353 -210 -465 C ATOM 2293 C ILE A1102 -6.626 -48.898 14.022 1.00 53.84 C ANISOU 2293 C ILE A1102 6620 6206 7631 368 -168 -465 C ATOM 2294 O ILE A1102 -6.764 -47.719 14.372 1.00 56.38 O ANISOU 2294 O ILE A1102 6947 6535 7940 362 -146 -445 O ATOM 2295 CB ILE A1102 -5.353 -50.487 15.527 1.00 52.06 C ANISOU 2295 CB ILE A1102 6237 6020 7525 323 -138 -478 C ATOM 2296 CG1 ILE A1102 -5.494 -51.663 16.497 1.00 54.47 C ANISOU 2296 CG1 ILE A1102 6435 6354 7909 308 -181 -480 C ATOM 2297 CG2 ILE A1102 -4.612 -49.332 16.182 1.00 52.15 C ANISOU 2297 CG2 ILE A1102 6230 6041 7542 300 -64 -463 C ATOM 2298 CD1 ILE A1102 -6.389 -51.379 17.685 1.00 56.30 C ANISOU 2298 CD1 ILE A1102 6588 6618 8188 304 -231 -452 C ATOM 2299 N GLN A1103 -6.369 -49.228 12.754 1.00 54.41 N ANISOU 2299 N GLN A1103 6777 6248 7650 390 -157 -486 N ATOM 2300 CA GLN A1103 -6.235 -48.184 11.745 1.00 57.31 C ANISOU 2300 CA GLN A1103 7243 6590 7942 408 -115 -486 C ATOM 2301 C GLN A1103 -7.553 -47.454 11.513 1.00 51.36 C ANISOU 2301 C GLN A1103 6529 5831 7155 426 -174 -469 C ATOM 2302 O GLN A1103 -7.551 -46.250 11.234 1.00 43.83 O ANISOU 2302 O GLN A1103 5622 4872 6160 429 -138 -458 O ATOM 2303 CB GLN A1103 -5.714 -48.775 10.435 1.00 62.73 C ANISOU 2303 CB GLN A1103 8011 7245 8577 434 -95 -511 C ATOM 2304 CG GLN A1103 -5.458 -47.740 9.351 1.00 67.87 C ANISOU 2304 CG GLN A1103 8763 7873 9153 457 -44 -510 C ATOM 2305 CD GLN A1103 -4.892 -48.345 8.083 1.00 72.61 C ANISOU 2305 CD GLN A1103 9442 8443 9703 487 -20 -534 C ATOM 2306 OE1 GLN A1103 -4.178 -49.346 8.124 1.00 74.96 O ANISOU 2306 OE1 GLN A1103 9715 8741 10026 483 -5 -549 O ATOM 2307 NE2 GLN A1103 -5.212 -47.740 6.945 1.00 75.05 N ANISOU 2307 NE2 GLN A1103 9849 8727 9940 521 -17 -536 N ATOM 2308 N LYS A1104 -8.682 -48.155 11.631 1.00 51.79 N ANISOU 2308 N LYS A1104 6564 5886 7229 439 -265 -466 N ATOM 2309 CA LYS A1104 -9.972 -47.493 11.479 1.00 56.60 C ANISOU 2309 CA LYS A1104 7206 6488 7812 453 -323 -446 C ATOM 2310 C LYS A1104 -10.263 -46.556 12.645 1.00 53.32 C ANISOU 2310 C LYS A1104 6729 6102 7427 432 -317 -416 C ATOM 2311 O LYS A1104 -10.959 -45.549 12.469 1.00 52.11 O ANISOU 2311 O LYS A1104 6616 5945 7238 438 -328 -398 O ATOM 2312 CB LYS A1104 -11.086 -48.530 11.340 1.00 60.23 C ANISOU 2312 CB LYS A1104 7657 6937 8292 473 -425 -445 C ATOM 2313 CG LYS A1104 -10.952 -49.419 10.117 1.00 68.12 C ANISOU 2313 CG LYS A1104 8726 7902 9255 501 -444 -476 C ATOM 2314 CD LYS A1104 -12.103 -50.405 10.030 1.00 76.02 C ANISOU 2314 CD LYS A1104 9714 8889 10282 521 -552 -471 C ATOM 2315 CE LYS A1104 -11.946 -51.333 8.836 1.00 80.28 C ANISOU 2315 CE LYS A1104 10323 9393 10788 551 -576 -504 C ATOM 2316 NZ LYS A1104 -10.704 -52.149 8.925 1.00 81.82 N ANISOU 2316 NZ LYS A1104 10485 9598 11005 540 -525 -529 N ATOM 2317 N TYR A1105 -9.744 -46.864 13.834 1.00 47.00 N ANISOU 2317 N TYR A1105 5833 5333 6693 407 -299 -409 N ATOM 2318 CA TYR A1105 -9.955 -45.991 14.983 1.00 48.33 C ANISOU 2318 CA TYR A1105 5942 5531 6891 391 -292 -382 C ATOM 2319 C TYR A1105 -9.075 -44.748 14.913 1.00 45.34 C ANISOU 2319 C TYR A1105 5595 5151 6482 377 -207 -380 C ATOM 2320 O TYR A1105 -9.526 -43.651 15.259 1.00 47.80 O ANISOU 2320 O TYR A1105 5911 5471 6779 376 -207 -359 O ATOM 2321 CB TYR A1105 -9.693 -46.751 16.284 1.00 49.14 C ANISOU 2321 CB TYR A1105 5929 5666 7075 372 -302 -376 C ATOM 2322 CG TYR A1105 -9.649 -45.857 17.503 1.00 58.96 C ANISOU 2322 CG TYR A1105 7112 6940 8350 356 -282 -351 C ATOM 2323 CD1 TYR A1105 -10.818 -45.378 18.079 1.00 66.42 C ANISOU 2323 CD1 TYR A1105 8035 7900 9302 367 -339 -320 C ATOM 2324 CD2 TYR A1105 -8.437 -45.489 18.077 1.00 60.00 C ANISOU 2324 CD2 TYR A1105 7209 7083 8504 332 -206 -357 C ATOM 2325 CE1 TYR A1105 -10.784 -44.557 19.191 1.00 69.40 C ANISOU 2325 CE1 TYR A1105 8359 8304 9704 357 -322 -297 C ATOM 2326 CE2 TYR A1105 -8.392 -44.669 19.190 1.00 64.65 C ANISOU 2326 CE2 TYR A1105 7745 7698 9122 321 -191 -336 C ATOM 2327 CZ TYR A1105 -9.569 -44.206 19.743 1.00 70.01 C ANISOU 2327 CZ TYR A1105 8404 8393 9804 335 -249 -307 C ATOM 2328 OH TYR A1105 -9.533 -43.389 20.850 1.00 74.80 O ANISOU 2328 OH TYR A1105 8969 9031 10419 318 -234 -282 O ATOM 2329 N LEU A1106 -7.827 -44.904 14.478 1.00 43.63 N ANISOU 2329 N LEU A1106 5398 4923 6256 369 -136 -401 N ATOM 2330 CA LEU A1106 -6.862 -43.806 14.401 1.00 47.59 C ANISOU 2330 CA LEU A1106 5925 5420 6737 358 -54 -397 C ATOM 2331 C LEU A1106 -7.411 -42.588 13.666 1.00 51.95 C ANISOU 2331 C LEU A1106 6556 5958 7224 373 -51 -386 C ATOM 2332 O LEU A1106 -7.279 -41.457 14.132 1.00 56.42 O ANISOU 2332 O LEU A1106 7113 6535 7790 363 -22 -369 O ATOM 2333 CB LEU A1106 -5.576 -44.282 13.717 1.00 50.35 C ANISOU 2333 CB LEU A1106 6305 5752 7076 356 14 -418 C ATOM 2334 CG LEU A1106 -4.671 -43.223 13.074 1.00 55.53 C ANISOU 2334 CG LEU A1106 7020 6390 7690 358 95 -414 C ATOM 2335 CD1 LEU A1106 -3.987 -42.354 14.122 1.00 53.61 C ANISOU 2335 CD1 LEU A1106 6718 6162 7487 331 143 -395 C ATOM 2336 CD2 LEU A1106 -3.642 -43.872 12.152 1.00 56.66 C ANISOU 2336 CD2 LEU A1106 7207 6509 7812 367 148 -433 C ATOM 2337 N GLU A 219 -8.796 -43.956 11.289 1.00 73.91 N ANISOU 2337 N GLU A 219 9482 8685 9914 431 -149 -419 N ATOM 2338 CA GLU A 219 -8.811 -42.638 10.677 1.00 70.17 C ANISOU 2338 CA GLU A 219 9076 8202 9385 438 -110 -410 C ATOM 2339 C GLU A 219 -9.978 -41.807 11.199 1.00 64.30 C ANISOU 2339 C GLU A 219 8320 7471 8639 434 -158 -384 C ATOM 2340 O GLU A 219 -10.161 -40.657 10.802 1.00 65.20 O ANISOU 2340 O GLU A 219 8483 7581 8710 437 -135 -374 O ATOM 2341 CB GLU A 219 -8.884 -42.751 9.152 1.00 74.78 C ANISOU 2341 CB GLU A 219 9764 8752 9899 470 -106 -429 C ATOM 2342 CG GLU A 219 -7.664 -43.398 8.514 1.00 78.99 C ANISOU 2342 CG GLU A 219 10321 9270 10422 479 -48 -451 C ATOM 2343 CD GLU A 219 -7.934 -44.811 8.041 1.00 81.60 C ANISOU 2343 CD GLU A 219 10664 9584 10755 499 -102 -474 C ATOM 2344 OE1 GLU A 219 -9.096 -45.257 8.136 1.00 83.82 O ANISOU 2344 OE1 GLU A 219 10939 9863 11045 506 -187 -472 O ATOM 2345 OE2 GLU A 219 -6.987 -45.474 7.572 1.00 84.27 O ANISOU 2345 OE2 GLU A 219 11019 9912 11088 507 -62 -493 O ATOM 2346 N ARG A 220 -10.764 -42.394 12.104 1.00 58.82 N ANISOU 2346 N ARG A 220 7559 6795 7994 428 -225 -371 N ATOM 2347 CA ARG A 220 -11.978 -41.754 12.596 1.00 58.96 C ANISOU 2347 CA ARG A 220 7565 6825 8013 428 -280 -342 C ATOM 2348 C ARG A 220 -11.708 -40.787 13.742 1.00 56.46 C ANISOU 2348 C ARG A 220 7190 6539 7725 406 -247 -320 C ATOM 2349 O ARG A 220 -12.367 -39.747 13.838 1.00 53.58 O ANISOU 2349 O ARG A 220 6845 6179 7335 406 -258 -299 O ATOM 2350 CB ARG A 220 -12.995 -42.817 13.012 1.00 63.89 C ANISOU 2350 CB ARG A 220 8145 7452 8677 437 -369 -332 C ATOM 2351 CG ARG A 220 -13.617 -43.535 11.823 1.00 77.33 C ANISOU 2351 CG ARG A 220 9919 9118 10343 463 -420 -347 C ATOM 2352 CD ARG A 220 -14.385 -44.776 12.234 1.00 88.70 C ANISOU 2352 CD ARG A 220 11307 10559 11834 472 -505 -339 C ATOM 2353 NE ARG A 220 -14.896 -45.492 11.069 1.00 96.25 N ANISOU 2353 NE ARG A 220 12334 11478 12758 498 -555 -356 N ATOM 2354 CZ ARG A 220 -15.467 -46.690 11.118 1.00100.12 C ANISOU 2354 CZ ARG A 220 12795 11958 13286 512 -631 -355 C ATOM 2355 NH1 ARG A 220 -15.600 -47.315 12.279 1.00101.00 N ANISOU 2355 NH1 ARG A 220 12805 12099 13473 502 -662 -338 N ATOM 2356 NH2 ARG A 220 -15.901 -47.265 10.005 1.00101.98 N ANISOU 2356 NH2 ARG A 220 13103 12155 13489 538 -676 -372 N ATOM 2357 N ALA A 221 -10.750 -41.098 14.616 1.00 55.05 N ANISOU 2357 N ALA A 221 6938 6379 7598 389 -209 -325 N ATOM 2358 CA ALA A 221 -10.364 -40.127 15.636 1.00 52.55 C ANISOU 2358 CA ALA A 221 6574 6087 7307 371 -173 -307 C ATOM 2359 C ALA A 221 -9.719 -38.902 15.001 1.00 52.52 C ANISOU 2359 C ALA A 221 6630 6070 7255 368 -106 -309 C ATOM 2360 O ALA A 221 -9.953 -37.768 15.440 1.00 49.25 O ANISOU 2360 O ALA A 221 6212 5668 6833 363 -100 -289 O ATOM 2361 CB ALA A 221 -9.419 -40.766 16.652 1.00 57.02 C ANISOU 2361 CB ALA A 221 7053 6673 7940 353 -145 -313 C ATOM 2362 N ARG A 222 -8.943 -39.107 13.955 1.00 48.77 N ANISOU 2362 N ARG A 222 6211 5570 6748 375 -59 -330 N ATOM 2363 CA ARG A 222 -8.288 -38.026 13.272 1.00 50.14 C ANISOU 2363 CA ARG A 222 6441 5730 6879 376 5 -330 C ATOM 2364 C ARG A 222 -9.324 -37.202 12.548 1.00 53.48 C ANISOU 2364 C ARG A 222 6932 6144 7243 390 -25 -321 C ATOM 2365 O ARG A 222 -9.271 -36.001 12.556 1.00 50.64 O ANISOU 2365 O ARG A 222 6589 5789 6863 386 3 -307 O ATOM 2366 CB ARG A 222 -7.279 -38.563 12.289 1.00 55.16 C ANISOU 2366 CB ARG A 222 7122 6342 7494 386 58 -352 C ATOM 2367 CG ARG A 222 -6.613 -37.528 11.419 1.00 61.78 C ANISOU 2367 CG ARG A 222 8023 7163 8286 394 125 -349 C ATOM 2368 CD ARG A 222 -6.004 -38.204 10.211 1.00 71.30 C ANISOU 2368 CD ARG A 222 9291 8343 9456 416 158 -370 C ATOM 2369 NE ARG A 222 -4.896 -39.088 10.559 1.00 80.33 N ANISOU 2369 NE ARG A 222 10392 9486 10643 405 196 -379 N ATOM 2370 CZ ARG A 222 -4.473 -40.091 9.795 1.00 85.05 C ANISOU 2370 CZ ARG A 222 11023 10066 11226 421 206 -399 C ATOM 2371 NH1 ARG A 222 -5.082 -40.357 8.648 1.00 86.21 N ANISOU 2371 NH1 ARG A 222 11247 10193 11315 452 178 -413 N ATOM 2372 NH2 ARG A 222 -3.453 -40.839 10.181 1.00 83.86 N ANISOU 2372 NH2 ARG A 222 10830 9916 11117 408 243 -405 N ATOM 2373 N SER A 223 -10.280 -37.868 11.935 1.00 52.99 N ANISOU 2373 N SER A 223 6908 6070 7157 407 -84 -327 N ATOM 2374 CA SER A 223 -11.335 -37.196 11.228 1.00 51.26 C ANISOU 2374 CA SER A 223 6754 5839 6883 419 -117 -318 C ATOM 2375 C SER A 223 -12.165 -36.345 12.167 1.00 48.66 C ANISOU 2375 C SER A 223 6386 5533 6568 407 -150 -289 C ATOM 2376 O SER A 223 -12.560 -35.263 11.817 1.00 51.40 O ANISOU 2376 O SER A 223 6776 5879 6876 407 -142 -278 O ATOM 2377 CB SER A 223 -12.196 -38.196 10.484 1.00 56.52 C ANISOU 2377 CB SER A 223 7462 6484 7530 440 -181 -330 C ATOM 2378 OG SER A 223 -13.454 -37.680 10.172 1.00 57.83 O ANISOU 2378 OG SER A 223 7668 6642 7661 447 -233 -314 O ATOM 2379 N THR A 224 -12.449 -36.835 13.356 1.00 48.76 N ANISOU 2379 N THR A 224 6320 5569 6638 398 -189 -276 N ATOM 2380 CA THR A 224 -13.224 -36.063 14.307 1.00 47.14 C ANISOU 2380 CA THR A 224 6077 5388 6448 391 -221 -245 C ATOM 2381 C THR A 224 -12.482 -34.791 14.722 1.00 42.71 C ANISOU 2381 C THR A 224 5505 4840 5884 377 -161 -238 C ATOM 2382 O THR A 224 -13.064 -33.738 14.790 1.00 36.90 O ANISOU 2382 O THR A 224 4788 4111 5122 375 -169 -219 O ATOM 2383 CB THR A 224 -13.615 -36.904 15.522 1.00 46.90 C ANISOU 2383 CB THR A 224 5959 5380 6481 389 -271 -231 C ATOM 2384 OG1 THR A 224 -14.592 -37.857 15.135 1.00 48.99 O ANISOU 2384 OG1 THR A 224 6238 5632 6745 404 -341 -228 O ATOM 2385 CG2 THR A 224 -14.204 -36.061 16.581 1.00 46.22 C ANISOU 2385 CG2 THR A 224 5830 5321 6411 385 -293 -199 C ATOM 2386 N LEU A 225 -11.188 -34.900 14.958 1.00 39.68 N ANISOU 2386 N LEU A 225 5091 4457 5528 367 -101 -252 N ATOM 2387 CA LEU A 225 -10.388 -33.759 15.336 1.00 44.14 C ANISOU 2387 CA LEU A 225 5643 5030 6098 356 -45 -244 C ATOM 2388 C LEU A 225 -10.362 -32.714 14.242 1.00 46.64 C ANISOU 2388 C LEU A 225 6038 5330 6354 361 -11 -245 C ATOM 2389 O LEU A 225 -10.428 -31.540 14.528 1.00 48.42 O ANISOU 2389 O LEU A 225 6263 5565 6570 355 1 -229 O ATOM 2390 CB LEU A 225 -8.973 -34.151 15.707 1.00 45.94 C ANISOU 2390 CB LEU A 225 5830 5257 6371 345 13 -257 C ATOM 2391 CG LEU A 225 -8.759 -34.443 17.178 1.00 47.77 C ANISOU 2391 CG LEU A 225 5969 5513 6669 333 -1 -248 C ATOM 2392 CD1 LEU A 225 -7.547 -35.319 17.419 1.00 48.73 C ANISOU 2392 CD1 LEU A 225 6049 5629 6835 322 43 -265 C ATOM 2393 CD2 LEU A 225 -8.657 -33.158 17.965 1.00 50.17 C ANISOU 2393 CD2 LEU A 225 6248 5832 6982 326 12 -228 C ATOM 2394 N GLN A 226 -10.280 -33.144 12.989 1.00 47.79 N ANISOU 2394 N GLN A 226 6250 5451 6459 375 2 -263 N ATOM 2395 CA GLN A 226 -10.252 -32.231 11.861 1.00 50.72 C ANISOU 2395 CA GLN A 226 6696 5805 6770 384 35 -265 C ATOM 2396 C GLN A 226 -11.523 -31.425 11.788 1.00 47.89 C ANISOU 2396 C GLN A 226 6366 5455 6377 384 -11 -247 C ATOM 2397 O GLN A 226 -11.495 -30.261 11.503 1.00 45.60 O ANISOU 2397 O GLN A 226 6102 5166 6058 381 16 -238 O ATOM 2398 CB GLN A 226 -10.103 -32.973 10.541 1.00 54.07 C ANISOU 2398 CB GLN A 226 7189 6202 7154 404 47 -287 C ATOM 2399 CG GLN A 226 -8.798 -33.686 10.373 1.00 62.62 C ANISOU 2399 CG GLN A 226 8259 7275 8260 407 101 -304 C ATOM 2400 CD GLN A 226 -7.691 -32.987 11.099 1.00 71.40 C ANISOU 2400 CD GLN A 226 9322 8397 9411 391 159 -292 C ATOM 2401 OE1 GLN A 226 -7.674 -31.777 11.193 1.00 75.50 O ANISOU 2401 OE1 GLN A 226 9845 8922 9919 386 179 -276 O ATOM 2402 NE2 GLN A 226 -6.760 -33.750 11.619 1.00 74.10 N ANISOU 2402 NE2 GLN A 226 9615 8739 9800 382 185 -299 N ATOM 2403 N LYS A 227 -12.641 -32.076 12.033 1.00 46.73 N ANISOU 2403 N LYS A 227 6212 5311 6234 387 -81 -241 N ATOM 2404 CA LYS A 227 -13.919 -31.424 12.046 1.00 45.51 C ANISOU 2404 CA LYS A 227 6080 5161 6051 386 -130 -221 C ATOM 2405 C LYS A 227 -13.970 -30.396 13.165 1.00 43.15 C ANISOU 2405 C LYS A 227 5730 4891 5775 372 -127 -196 C ATOM 2406 O LYS A 227 -14.576 -29.368 13.009 1.00 42.40 O ANISOU 2406 O LYS A 227 5663 4801 5647 368 -134 -181 O ATOM 2407 CB LYS A 227 -15.044 -32.440 12.092 1.00 45.64 C ANISOU 2407 CB LYS A 227 6096 5171 6073 395 -207 -215 C ATOM 2408 CG LYS A 227 -15.091 -33.231 10.806 1.00 53.13 C ANISOU 2408 CG LYS A 227 7112 6087 6987 413 -212 -239 C ATOM 2409 CD LYS A 227 -16.235 -34.208 10.723 1.00 62.22 C ANISOU 2409 CD LYS A 227 8271 7226 8145 424 -293 -233 C ATOM 2410 CE LYS A 227 -16.036 -35.100 9.508 1.00 66.47 C ANISOU 2410 CE LYS A 227 8871 7731 8654 444 -294 -262 C ATOM 2411 NZ LYS A 227 -17.054 -36.176 9.392 1.00 69.17 N ANISOU 2411 NZ LYS A 227 9217 8055 9008 458 -377 -258 N ATOM 2412 N GLU A 228 -13.403 -30.704 14.316 1.00 39.09 N ANISOU 2412 N GLU A 228 5140 4396 5319 365 -122 -192 N ATOM 2413 CA GLU A 228 -13.314 -29.722 15.367 1.00 42.89 C ANISOU 2413 CA GLU A 228 5573 4900 5821 355 -116 -172 C ATOM 2414 C GLU A 228 -12.408 -28.561 15.012 1.00 43.63 C ANISOU 2414 C GLU A 228 5688 4990 5898 348 -52 -176 C ATOM 2415 O GLU A 228 -12.737 -27.443 15.270 1.00 45.06 O ANISOU 2415 O GLU A 228 5873 5184 6065 343 -55 -159 O ATOM 2416 CB GLU A 228 -12.920 -30.341 16.659 1.00 44.36 C ANISOU 2416 CB GLU A 228 5675 5106 6072 352 -127 -168 C ATOM 2417 CG GLU A 228 -14.087 -31.006 17.290 1.00 52.05 C ANISOU 2417 CG GLU A 228 6618 6094 7064 360 -200 -149 C ATOM 2418 CD GLU A 228 -13.681 -31.704 18.526 1.00 59.73 C ANISOU 2418 CD GLU A 228 7505 7087 8103 360 -209 -146 C ATOM 2419 OE1 GLU A 228 -13.061 -32.757 18.377 1.00 62.21 O ANISOU 2419 OE1 GLU A 228 7801 7392 8443 359 -195 -167 O ATOM 2420 OE2 GLU A 228 -13.969 -31.183 19.608 1.00 61.68 O ANISOU 2420 OE2 GLU A 228 7705 7359 8373 362 -228 -124 O ATOM 2421 N VAL A 229 -11.281 -28.812 14.364 1.00 39.03 N ANISOU 2421 N VAL A 229 5123 4389 5317 350 6 -195 N ATOM 2422 CA VAL A 229 -10.419 -27.723 13.962 1.00 37.70 C ANISOU 2422 CA VAL A 229 4975 4215 5136 346 66 -194 C ATOM 2423 C VAL A 229 -11.178 -26.819 12.992 1.00 37.58 C ANISOU 2423 C VAL A 229 5027 4194 5057 351 62 -189 C ATOM 2424 O VAL A 229 -11.180 -25.637 13.156 1.00 33.78 O ANISOU 2424 O VAL A 229 4545 3723 4568 344 74 -175 O ATOM 2425 CB VAL A 229 -9.150 -28.211 13.307 1.00 40.62 C ANISOU 2425 CB VAL A 229 5357 4563 5513 351 128 -212 C ATOM 2426 CG1 VAL A 229 -8.418 -27.048 12.702 1.00 38.61 C ANISOU 2426 CG1 VAL A 229 5131 4299 5239 353 186 -205 C ATOM 2427 CG2 VAL A 229 -8.287 -28.905 14.332 1.00 42.45 C ANISOU 2427 CG2 VAL A 229 5519 4801 5811 342 141 -215 C ATOM 2428 N HIS A 230 -11.883 -27.414 12.043 1.00 37.54 N ANISOU 2428 N HIS A 230 5078 4174 5011 361 38 -199 N ATOM 2429 CA HIS A 230 -12.680 -26.703 11.086 1.00 40.06 C ANISOU 2429 CA HIS A 230 5465 4486 5271 365 29 -196 C ATOM 2430 C HIS A 230 -13.777 -25.887 11.738 1.00 33.33 C ANISOU 2430 C HIS A 230 4599 3654 4411 353 -18 -171 C ATOM 2431 O HIS A 230 -13.983 -24.765 11.369 1.00 30.95 O ANISOU 2431 O HIS A 230 4326 3357 4078 348 -2 -162 O ATOM 2432 CB HIS A 230 -13.306 -27.671 10.100 1.00 49.12 C ANISOU 2432 CB HIS A 230 6669 5612 6383 380 0 -212 C ATOM 2433 CG HIS A 230 -13.750 -27.027 8.832 1.00 61.48 C ANISOU 2433 CG HIS A 230 8314 7162 7885 388 13 -215 C ATOM 2434 ND1 HIS A 230 -15.057 -26.664 8.597 1.00 66.46 N ANISOU 2434 ND1 HIS A 230 8980 7793 8481 384 -37 -203 N ATOM 2435 CD2 HIS A 230 -13.055 -26.663 7.732 1.00 65.68 C ANISOU 2435 CD2 HIS A 230 8895 7679 8382 401 70 -228 C ATOM 2436 CE1 HIS A 230 -15.148 -26.117 7.402 1.00 68.45 C ANISOU 2436 CE1 HIS A 230 9299 8031 8679 392 -10 -211 C ATOM 2437 NE2 HIS A 230 -13.948 -26.106 6.857 1.00 68.82 N ANISOU 2437 NE2 HIS A 230 9355 8069 8725 405 54 -226 N ATOM 2438 N ALA A 231 -14.496 -26.472 12.675 1.00 31.85 N ANISOU 2438 N ALA A 231 4370 3480 4253 351 -74 -159 N ATOM 2439 CA ALA A 231 -15.563 -25.739 13.346 1.00 32.76 C ANISOU 2439 CA ALA A 231 4472 3614 4360 344 -120 -132 C ATOM 2440 C ALA A 231 -15.011 -24.617 14.214 1.00 33.31 C ANISOU 2440 C ALA A 231 4497 3705 4452 334 -95 -119 C ATOM 2441 O ALA A 231 -15.647 -23.564 14.341 1.00 30.26 O ANISOU 2441 O ALA A 231 4123 3333 4042 328 -109 -100 O ATOM 2442 CB ALA A 231 -16.413 -26.694 14.185 1.00 30.60 C ANISOU 2442 CB ALA A 231 4159 3349 4117 349 -187 -117 C ATOM 2443 N ALA A 232 -13.837 -24.820 14.817 1.00 31.42 N ANISOU 2443 N ALA A 232 4209 3470 4261 334 -59 -128 N ATOM 2444 CA ALA A 232 -13.231 -23.768 15.625 1.00 32.48 C ANISOU 2444 CA ALA A 232 4301 3619 4420 327 -36 -116 C ATOM 2445 C ALA A 232 -12.725 -22.622 14.760 1.00 35.40 C ANISOU 2445 C ALA A 232 4712 3980 4758 323 14 -119 C ATOM 2446 O ALA A 232 -12.740 -21.465 15.198 1.00 32.82 O ANISOU 2446 O ALA A 232 4371 3668 4432 318 15 -104 O ATOM 2447 CB ALA A 232 -12.093 -24.339 16.471 1.00 30.00 C ANISOU 2447 CB ALA A 232 3925 3307 4168 328 -11 -125 C ATOM 2448 N LYS A 233 -12.273 -22.919 13.538 1.00 32.45 N ANISOU 2448 N LYS A 233 4388 3584 4357 329 53 -136 N ATOM 2449 CA LYS A 233 -11.828 -21.860 12.639 1.00 35.24 C ANISOU 2449 CA LYS A 233 4779 3930 4679 329 101 -136 C ATOM 2450 C LYS A 233 -13.003 -21.021 12.154 1.00 31.75 C ANISOU 2450 C LYS A 233 4382 3496 4185 324 73 -125 C ATOM 2451 O LYS A 233 -12.889 -19.796 12.033 1.00 30.61 O ANISOU 2451 O LYS A 233 4242 3360 4028 318 93 -114 O ATOM 2452 CB LYS A 233 -11.068 -22.454 11.454 1.00 44.20 C ANISOU 2452 CB LYS A 233 5957 5039 5798 342 150 -155 C ATOM 2453 CG LYS A 233 -9.697 -23.001 11.808 1.00 52.39 C ANISOU 2453 CG LYS A 233 6954 6067 6886 346 194 -162 C ATOM 2454 CD LYS A 233 -8.967 -23.504 10.577 1.00 59.37 C ANISOU 2454 CD LYS A 233 7884 6926 7747 363 245 -177 C ATOM 2455 CE LYS A 233 -7.580 -24.022 10.928 1.00 60.63 C ANISOU 2455 CE LYS A 233 8005 7074 7958 365 291 -180 C ATOM 2456 NZ LYS A 233 -6.859 -24.523 9.724 1.00 60.90 N ANISOU 2456 NZ LYS A 233 8087 7085 7969 385 342 -191 N ATOM 2457 N SER A 234 -14.138 -21.664 11.868 1.00 29.43 N ANISOU 2457 N SER A 234 4121 3200 3862 325 25 -126 N ATOM 2458 CA SER A 234 -15.323 -20.921 11.454 1.00 31.99 C ANISOU 2458 CA SER A 234 4487 3530 4137 317 -4 -112 C ATOM 2459 C SER A 234 -15.794 -19.979 12.553 1.00 31.92 C ANISOU 2459 C SER A 234 4438 3548 4143 305 -34 -87 C ATOM 2460 O SER A 234 -16.153 -18.827 12.283 1.00 37.64 O ANISOU 2460 O SER A 234 5182 4281 4837 296 -28 -76 O ATOM 2461 CB SER A 234 -16.437 -21.892 11.063 1.00 29.51 C ANISOU 2461 CB SER A 234 4210 3203 3799 321 -56 -114 C ATOM 2462 OG SER A 234 -16.034 -22.706 9.978 1.00 32.44 O ANISOU 2462 OG SER A 234 4626 3548 4151 335 -32 -139 O ATOM 2463 N ALA A 235 -15.791 -20.447 13.802 1.00 28.02 N ANISOU 2463 N ALA A 235 3884 3067 3694 307 -65 -78 N ATOM 2464 CA ALA A 235 -16.196 -19.594 14.913 1.00 25.51 C ANISOU 2464 CA ALA A 235 3526 2775 3390 302 -94 -54 C ATOM 2465 C ALA A 235 -15.193 -18.469 15.143 1.00 28.26 C ANISOU 2465 C ALA A 235 3850 3130 3757 298 -50 -54 C ATOM 2466 O ALA A 235 -15.579 -17.343 15.481 1.00 24.87 O ANISOU 2466 O ALA A 235 3417 2718 3315 292 -63 -37 O ATOM 2467 CB ALA A 235 -16.373 -20.433 16.177 1.00 24.50 C ANISOU 2467 CB ALA A 235 3340 2660 3309 311 -135 -44 C ATOM 2468 N ALA A 236 -13.900 -18.751 14.960 1.00 29.55 N ANISOU 2468 N ALA A 236 3997 3279 3951 303 -1 -71 N ATOM 2469 CA ALA A 236 -12.887 -17.712 15.112 1.00 29.63 C ANISOU 2469 CA ALA A 236 3984 3290 3984 301 40 -68 C ATOM 2470 C ALA A 236 -13.010 -16.650 14.026 1.00 26.64 C ANISOU 2470 C ALA A 236 3653 2908 3560 295 68 -66 C ATOM 2471 O ALA A 236 -12.754 -15.468 14.285 1.00 24.70 O ANISOU 2471 O ALA A 236 3391 2673 3322 291 77 -54 O ATOM 2472 CB ALA A 236 -11.489 -18.330 15.097 1.00 28.26 C ANISOU 2472 CB ALA A 236 3785 3097 3854 308 88 -82 C ATOM 2473 N ILE A 237 -13.398 -17.050 12.812 1.00 23.29 N ANISOU 2473 N ILE A 237 3288 2470 3090 297 80 -77 N ATOM 2474 CA ILE A 237 -13.614 -16.080 11.741 1.00 22.87 C ANISOU 2474 CA ILE A 237 3282 2416 2992 292 106 -75 C ATOM 2475 C ILE A 237 -14.727 -15.112 12.121 1.00 23.33 C ANISOU 2475 C ILE A 237 3343 2496 3023 278 64 -56 C ATOM 2476 O ILE A 237 -14.627 -13.902 11.884 1.00 24.32 O ANISOU 2476 O ILE A 237 3471 2632 3137 271 82 -48 O ATOM 2477 CB ILE A 237 -13.913 -16.807 10.414 1.00 27.11 C ANISOU 2477 CB ILE A 237 3884 2933 3484 300 120 -92 C ATOM 2478 CG1 ILE A 237 -12.656 -17.499 9.887 1.00 34.16 C ANISOU 2478 CG1 ILE A 237 4777 3805 4398 317 173 -108 C ATOM 2479 CG2 ILE A 237 -14.463 -15.841 9.373 1.00 25.29 C ANISOU 2479 CG2 ILE A 237 3704 2705 3199 294 134 -89 C ATOM 2480 CD1 ILE A 237 -12.909 -18.391 8.680 1.00 34.93 C ANISOU 2480 CD1 ILE A 237 4937 3881 4454 331 182 -127 C ATOM 2481 N ILE A 238 -15.796 -15.628 12.735 1.00 20.27 N ANISOU 2481 N ILE A 238 2955 2119 2629 274 7 -47 N ATOM 2482 CA ILE A 238 -16.897 -14.778 13.184 1.00 22.21 C ANISOU 2482 CA ILE A 238 3203 2386 2851 262 -35 -25 C ATOM 2483 C ILE A 238 -16.411 -13.770 14.218 1.00 21.44 C ANISOU 2483 C ILE A 238 3052 2308 2787 261 -37 -12 C ATOM 2484 O ILE A 238 -16.748 -12.582 14.156 1.00 23.35 O ANISOU 2484 O ILE A 238 3301 2565 3008 250 -39 1 O ATOM 2485 CB ILE A 238 -18.044 -15.645 13.740 1.00 29.71 C ANISOU 2485 CB ILE A 238 4154 3339 3795 263 -96 -12 C ATOM 2486 CG1 ILE A 238 -18.606 -16.556 12.648 1.00 38.76 C ANISOU 2486 CG1 ILE A 238 5359 4463 4907 265 -101 -24 C ATOM 2487 CG2 ILE A 238 -19.149 -14.771 14.306 1.00 30.62 C ANISOU 2487 CG2 ILE A 238 4270 3477 3889 253 -139 16 C ATOM 2488 CD1 ILE A 238 -19.452 -15.826 11.637 1.00 43.09 C ANISOU 2488 CD1 ILE A 238 5968 5008 5398 251 -101 -19 C ATOM 2489 N ALA A 239 -15.614 -14.226 15.189 1.00 19.88 N ANISOU 2489 N ALA A 239 2800 2110 2643 272 -37 -14 N ATOM 2490 CA ALA A 239 -15.096 -13.312 16.202 1.00 22.87 C ANISOU 2490 CA ALA A 239 3128 2503 3057 275 -41 -3 C ATOM 2491 C ALA A 239 -14.132 -12.300 15.592 1.00 23.28 C ANISOU 2491 C ALA A 239 3181 2548 3116 271 9 -7 C ATOM 2492 O ALA A 239 -14.128 -11.126 15.979 1.00 23.84 O ANISOU 2492 O ALA A 239 3235 2633 3191 268 0 6 O ATOM 2493 CB ALA A 239 -14.417 -14.099 17.323 1.00 21.09 C ANISOU 2493 CB ALA A 239 2847 2277 2890 288 -50 -6 C ATOM 2494 N GLY A 240 -13.328 -12.717 14.633 1.00 21.45 N ANISOU 2494 N GLY A 240 2970 2295 2886 275 59 -23 N ATOM 2495 CA GLY A 240 -12.393 -11.832 13.982 1.00 20.78 C ANISOU 2495 CA GLY A 240 2885 2201 2811 276 109 -22 C ATOM 2496 C GLY A 240 -13.063 -10.723 13.203 1.00 23.38 C ANISOU 2496 C GLY A 240 3249 2543 3093 264 112 -14 C ATOM 2497 O GLY A 240 -12.628 -9.604 13.222 1.00 26.26 O ANISOU 2497 O GLY A 240 3595 2913 3471 262 126 -4 O ATOM 2498 N LEU A 241 -14.120 -11.081 12.502 1.00 25.04 N ANISOU 2498 N LEU A 241 3511 2755 3249 257 97 -19 N ATOM 2499 CA LEU A 241 -14.930 -10.171 11.724 1.00 26.31 C ANISOU 2499 CA LEU A 241 3711 2927 3359 242 96 -12 C ATOM 2500 C LEU A 241 -15.608 -9.146 12.606 1.00 20.93 C ANISOU 2500 C LEU A 241 3006 2271 2675 230 54 8 C ATOM 2501 O LEU A 241 -15.740 -8.029 12.226 1.00 26.07 O ANISOU 2501 O LEU A 241 3664 2934 3309 219 64 15 O ATOM 2502 CB LEU A 241 -15.921 -10.908 10.850 1.00 29.54 C ANISOU 2502 CB LEU A 241 4182 3328 3715 238 85 -21 C ATOM 2503 CG LEU A 241 -15.330 -11.547 9.593 1.00 31.48 C ANISOU 2503 CG LEU A 241 4466 3549 3946 251 134 -40 C ATOM 2504 CD1 LEU A 241 -16.363 -12.397 8.923 1.00 30.53 C ANISOU 2504 CD1 LEU A 241 4404 3418 3779 249 110 -49 C ATOM 2505 CD2 LEU A 241 -14.777 -10.533 8.616 1.00 35.78 C ANISOU 2505 CD2 LEU A 241 5024 4094 4476 252 186 -39 C ATOM 2506 N PHE A 242 -16.030 -9.544 13.790 1.00 21.49 N ANISOU 2506 N PHE A 242 3049 2353 2765 233 6 16 N ATOM 2507 CA PHE A 242 -16.610 -8.599 14.717 1.00 21.37 C ANISOU 2507 CA PHE A 242 3009 2361 2749 227 -35 36 C ATOM 2508 C PHE A 242 -15.560 -7.553 15.081 1.00 19.90 C ANISOU 2508 C PHE A 242 2779 2178 2603 232 -15 39 C ATOM 2509 O PHE A 242 -15.831 -6.384 15.081 1.00 21.32 O ANISOU 2509 O PHE A 242 2957 2374 2769 222 -23 51 O ATOM 2510 CB PHE A 242 -17.113 -9.298 15.981 1.00 22.93 C ANISOU 2510 CB PHE A 242 3178 2568 2965 237 -87 46 C ATOM 2511 CG PHE A 242 -17.721 -8.370 16.998 1.00 25.98 C ANISOU 2511 CG PHE A 242 3542 2980 3349 237 -131 69 C ATOM 2512 CD1 PHE A 242 -16.937 -7.670 17.876 1.00 28.87 C ANISOU 2512 CD1 PHE A 242 3859 3354 3758 248 -135 72 C ATOM 2513 CD2 PHE A 242 -19.072 -8.208 17.069 1.00 22.99 C ANISOU 2513 CD2 PHE A 242 3191 2617 2926 228 -171 88 C ATOM 2514 CE1 PHE A 242 -17.500 -6.826 18.803 1.00 28.86 C ANISOU 2514 CE1 PHE A 242 3839 3375 3751 252 -178 92 C ATOM 2515 CE2 PHE A 242 -19.642 -7.369 17.983 1.00 26.13 C ANISOU 2515 CE2 PHE A 242 3570 3039 3318 230 -211 111 C ATOM 2516 CZ PHE A 242 -18.858 -6.680 18.857 1.00 27.97 C ANISOU 2516 CZ PHE A 242 3756 3280 3591 243 -215 112 C ATOM 2517 N ALA A 243 -14.349 -7.996 15.353 1.00 18.65 N ANISOU 2517 N ALA A 243 2587 2003 2497 247 12 30 N ATOM 2518 CA ALA A 243 -13.277 -7.089 15.672 1.00 23.54 C ANISOU 2518 CA ALA A 243 3164 2618 3161 254 31 35 C ATOM 2519 C ALA A 243 -12.952 -6.168 14.506 1.00 21.28 C ANISOU 2519 C ALA A 243 2898 2329 2858 246 73 37 C ATOM 2520 O ALA A 243 -12.848 -5.001 14.675 1.00 25.36 O ANISOU 2520 O ALA A 243 3394 2856 3383 243 67 49 O ATOM 2521 CB ALA A 243 -12.046 -7.857 16.096 1.00 21.33 C ANISOU 2521 CB ALA A 243 2848 2315 2940 269 55 27 C ATOM 2522 N LEU A 244 -12.863 -6.714 13.312 1.00 23.06 N ANISOU 2522 N LEU A 244 3163 2541 3057 245 115 25 N ATOM 2523 CA LEU A 244 -12.543 -5.925 12.153 1.00 23.22 C ANISOU 2523 CA LEU A 244 3202 2559 3061 243 159 28 C ATOM 2524 C LEU A 244 -13.620 -4.884 11.883 1.00 23.61 C ANISOU 2524 C LEU A 244 3273 2634 3064 223 136 37 C ATOM 2525 O LEU A 244 -13.335 -3.781 11.525 1.00 20.31 O ANISOU 2525 O LEU A 244 2842 2224 2651 219 153 46 O ATOM 2526 CB LEU A 244 -12.378 -6.823 10.948 1.00 30.23 C ANISOU 2526 CB LEU A 244 4136 3429 3923 250 203 13 C ATOM 2527 CG LEU A 244 -11.794 -6.180 9.698 1.00 45.56 C ANISOU 2527 CG LEU A 244 6092 5364 5854 256 259 16 C ATOM 2528 CD1 LEU A 244 -10.310 -5.938 9.893 1.00 52.88 C ANISOU 2528 CD1 LEU A 244 6972 6274 6847 275 295 26 C ATOM 2529 CD2 LEU A 244 -12.045 -7.053 8.480 1.00 51.11 C ANISOU 2529 CD2 LEU A 244 6855 6053 6511 263 290 0 C ATOM 2530 N CYS A 245 -14.858 -5.299 12.023 1.00 20.92 N ANISOU 2530 N CYS A 245 2965 2304 2679 210 98 35 N ATOM 2531 CA CYS A 245 -15.985 -4.440 11.839 1.00 20.02 C ANISOU 2531 CA CYS A 245 2875 2213 2519 189 73 46 C ATOM 2532 C CYS A 245 -16.138 -3.332 12.842 1.00 27.04 C ANISOU 2532 C CYS A 245 3724 3125 3425 183 36 63 C ATOM 2533 O CYS A 245 -16.573 -2.337 12.463 1.00 24.61 O ANISOU 2533 O CYS A 245 3425 2833 3093 168 35 71 O ATOM 2534 CB CYS A 245 -17.294 -5.199 11.693 1.00 25.86 C ANISOU 2534 CB CYS A 245 3662 2954 3208 177 41 45 C ATOM 2535 SG CYS A 245 -17.482 -6.041 10.136 1.00 32.75 S ANISOU 2535 SG CYS A 245 4601 3806 4038 177 80 26 S ATOM 2536 N TRP A 246 -15.828 -3.541 14.114 1.00 23.07 N ANISOU 2536 N TRP A 246 3179 2623 2964 197 3 68 N ATOM 2537 CA TRP A 246 -16.011 -2.529 15.144 1.00 19.90 C ANISOU 2537 CA TRP A 246 2742 2241 2577 197 -39 83 C ATOM 2538 C TRP A 246 -14.798 -1.696 15.519 1.00 20.29 C ANISOU 2538 C TRP A 246 2740 2285 2684 210 -26 87 C ATOM 2539 O TRP A 246 -14.952 -0.642 16.060 1.00 16.51 O ANISOU 2539 O TRP A 246 2238 1822 2212 208 -55 99 O ATOM 2540 CB TRP A 246 -16.551 -3.162 16.433 1.00 19.96 C ANISOU 2540 CB TRP A 246 2735 2257 2592 209 -91 90 C ATOM 2541 CG TRP A 246 -18.001 -3.434 16.430 1.00 21.74 C ANISOU 2541 CG TRP A 246 3000 2498 2762 196 -126 101 C ATOM 2542 CD1 TRP A 246 -18.601 -4.567 16.052 1.00 25.73 C ANISOU 2542 CD1 TRP A 246 3541 2993 3242 193 -127 97 C ATOM 2543 CD2 TRP A 246 -19.036 -2.543 16.816 1.00 20.16 C ANISOU 2543 CD2 TRP A 246 2809 2323 2528 184 -165 121 C ATOM 2544 NE1 TRP A 246 -19.947 -4.454 16.173 1.00 26.63 N ANISOU 2544 NE1 TRP A 246 3684 3123 3311 180 -165 115 N ATOM 2545 CE2 TRP A 246 -20.240 -3.214 16.653 1.00 24.46 C ANISOU 2545 CE2 TRP A 246 3395 2872 3028 174 -188 131 C ATOM 2546 CE3 TRP A 246 -19.059 -1.247 17.307 1.00 22.14 C ANISOU 2546 CE3 TRP A 246 3036 2594 2782 182 -186 134 C ATOM 2547 CZ2 TRP A 246 -21.452 -2.629 16.930 1.00 24.78 C ANISOU 2547 CZ2 TRP A 246 3454 2933 3027 162 -226 154 C ATOM 2548 CZ3 TRP A 246 -20.257 -0.671 17.576 1.00 23.78 C ANISOU 2548 CZ3 TRP A 246 3263 2825 2946 169 -224 154 C ATOM 2549 CH2 TRP A 246 -21.438 -1.361 17.398 1.00 23.30 C ANISOU 2549 CH2 TRP A 246 3245 2767 2841 159 -242 165 C ATOM 2550 N LEU A 247 -13.605 -2.201 15.254 1.00 20.46 N ANISOU 2550 N LEU A 247 2744 2280 2750 225 14 78 N ATOM 2551 CA LEU A 247 -12.385 -1.501 15.652 1.00 20.32 C ANISOU 2551 CA LEU A 247 2675 2250 2795 239 24 85 C ATOM 2552 C LEU A 247 -12.236 -0.112 15.040 1.00 20.22 C ANISOU 2552 C LEU A 247 2653 2248 2783 231 38 97 C ATOM 2553 O LEU A 247 -11.806 0.799 15.769 1.00 25.95 O ANISOU 2553 O LEU A 247 3336 2976 3548 239 11 108 O ATOM 2554 CB LEU A 247 -11.155 -2.361 15.330 1.00 20.23 C ANISOU 2554 CB LEU A 247 2652 2207 2828 255 71 77 C ATOM 2555 CG LEU A 247 -10.730 -3.313 16.451 1.00 26.57 C ANISOU 2555 CG LEU A 247 3428 2997 3672 269 51 72 C ATOM 2556 CD1 LEU A 247 -9.646 -4.277 15.975 1.00 32.98 C ANISOU 2556 CD1 LEU A 247 4237 3777 4517 280 102 63 C ATOM 2557 CD2 LEU A 247 -10.258 -2.522 17.659 1.00 25.55 C ANISOU 2557 CD2 LEU A 247 3246 2867 3593 282 13 83 C ATOM 2558 N PRO A 248 -12.545 0.105 13.771 1.00 20.53 N ANISOU 2558 N PRO A 248 2727 2293 2781 217 75 95 N ATOM 2559 CA PRO A 248 -12.406 1.444 13.204 1.00 21.30 C ANISOU 2559 CA PRO A 248 2810 2403 2882 210 87 107 C ATOM 2560 C PRO A 248 -13.161 2.511 13.980 1.00 21.93 C ANISOU 2560 C PRO A 248 2873 2509 2949 198 32 117 C ATOM 2561 O PRO A 248 -12.559 3.498 14.268 1.00 23.15 O ANISOU 2561 O PRO A 248 2986 2664 3144 205 24 129 O ATOM 2562 CB PRO A 248 -12.930 1.279 11.797 1.00 21.46 C ANISOU 2562 CB PRO A 248 2880 2428 2846 196 129 99 C ATOM 2563 CG PRO A 248 -12.631 -0.112 11.483 1.00 19.60 C ANISOU 2563 CG PRO A 248 2671 2170 2608 208 157 85 C ATOM 2564 CD PRO A 248 -12.976 -0.828 12.740 1.00 22.28 C ANISOU 2564 CD PRO A 248 3002 2508 2956 211 108 81 C ATOM 2565 N LEU A 249 -14.403 2.267 14.359 1.00 21.05 N ANISOU 2565 N LEU A 249 2793 2417 2786 183 -5 115 N ATOM 2566 CA LEU A 249 -15.170 3.222 15.152 1.00 22.51 C ANISOU 2566 CA LEU A 249 2967 2630 2956 174 -59 128 C ATOM 2567 C LEU A 249 -14.545 3.425 16.529 1.00 23.86 C ANISOU 2567 C LEU A 249 3088 2794 3182 199 -101 133 C ATOM 2568 O LEU A 249 -14.474 4.554 17.027 1.00 23.12 O ANISOU 2568 O LEU A 249 2965 2713 3106 201 -132 144 O ATOM 2569 CB LEU A 249 -16.620 2.750 15.277 1.00 23.16 C ANISOU 2569 CB LEU A 249 3097 2731 2974 157 -88 129 C ATOM 2570 CG LEU A 249 -17.621 3.659 15.996 1.00 23.52 C ANISOU 2570 CG LEU A 249 3141 2805 2989 147 -142 145 C ATOM 2571 CD1 LEU A 249 -17.582 5.077 15.445 1.00 23.91 C ANISOU 2571 CD1 LEU A 249 3177 2872 3035 129 -133 152 C ATOM 2572 CD2 LEU A 249 -19.031 3.086 15.885 1.00 23.77 C ANISOU 2572 CD2 LEU A 249 3224 2850 2957 129 -160 150 C ATOM 2573 N HIS A 250 -14.073 2.345 17.154 1.00 19.21 N ANISOU 2573 N HIS A 250 2491 2185 2622 218 -103 126 N ATOM 2574 CA HIS A 250 -13.433 2.467 18.460 1.00 17.83 C ANISOU 2574 CA HIS A 250 2271 2002 2503 243 -141 130 C ATOM 2575 C HIS A 250 -12.112 3.220 18.366 1.00 19.41 C ANISOU 2575 C HIS A 250 2425 2181 2769 256 -122 135 C ATOM 2576 O HIS A 250 -11.776 4.007 19.259 1.00 19.05 O ANISOU 2576 O HIS A 250 2342 2135 2761 270 -163 144 O ATOM 2577 CB HIS A 250 -13.210 1.085 19.068 1.00 17.10 C ANISOU 2577 CB HIS A 250 2177 1893 2428 259 -142 120 C ATOM 2578 CG HIS A 250 -14.456 0.450 19.596 1.00 22.13 C ANISOU 2578 CG HIS A 250 2842 2550 3015 256 -179 122 C ATOM 2579 ND1 HIS A 250 -15.161 0.968 20.661 1.00 20.80 N ANISOU 2579 ND1 HIS A 250 2664 2404 2834 266 -237 134 N ATOM 2580 CD2 HIS A 250 -15.118 -0.668 19.215 1.00 25.00 C ANISOU 2580 CD2 HIS A 250 3243 2914 3342 248 -168 115 C ATOM 2581 CE1 HIS A 250 -16.208 0.201 20.909 1.00 22.80 C ANISOU 2581 CE1 HIS A 250 2946 2670 3046 264 -258 138 C ATOM 2582 NE2 HIS A 250 -16.205 -0.799 20.046 1.00 26.27 N ANISOU 2582 NE2 HIS A 250 3413 3096 3471 252 -219 127 N ATOM 2583 N ILE A 251 -11.346 2.983 17.300 1.00 18.05 N ANISOU 2583 N ILE A 251 2256 1989 2614 253 -64 133 N ATOM 2584 CA ILE A 251 -10.070 3.672 17.132 1.00 20.49 C ANISOU 2584 CA ILE A 251 2521 2275 2989 267 -43 144 C ATOM 2585 C ILE A 251 -10.291 5.162 16.899 1.00 19.73 C ANISOU 2585 C ILE A 251 2407 2199 2891 258 -61 158 C ATOM 2586 O ILE A 251 -9.544 6.002 17.419 1.00 18.94 O ANISOU 2586 O ILE A 251 2261 2088 2849 273 -84 171 O ATOM 2587 CB ILE A 251 -9.265 3.029 15.986 1.00 22.62 C ANISOU 2587 CB ILE A 251 2801 2521 3271 269 27 142 C ATOM 2588 CG1 ILE A 251 -8.843 1.601 16.356 1.00 21.73 C ANISOU 2588 CG1 ILE A 251 2696 2385 3175 280 42 130 C ATOM 2589 CG2 ILE A 251 -8.043 3.871 15.649 1.00 24.74 C ANISOU 2589 CG2 ILE A 251 3026 2769 3607 283 52 162 C ATOM 2590 CD1 ILE A 251 -8.195 0.835 15.209 1.00 23.69 C ANISOU 2590 CD1 ILE A 251 2965 2612 3425 283 110 127 C ATOM 2591 N ILE A 252 -11.314 5.516 16.116 1.00 16.78 N ANISOU 2591 N ILE A 252 2069 1854 2452 233 -53 156 N ATOM 2592 CA ILE A 252 -11.641 6.926 15.916 1.00 20.79 C ANISOU 2592 CA ILE A 252 2561 2386 2954 221 -72 168 C ATOM 2593 C ILE A 252 -11.978 7.588 17.246 1.00 21.42 C ANISOU 2593 C ILE A 252 2616 2477 3044 230 -143 174 C ATOM 2594 O ILE A 252 -11.540 8.711 17.527 1.00 21.92 O ANISOU 2594 O ILE A 252 2638 2541 3148 238 -168 186 O ATOM 2595 CB ILE A 252 -12.791 7.074 14.901 1.00 20.82 C ANISOU 2595 CB ILE A 252 2611 2417 2881 191 -51 164 C ATOM 2596 CG1 ILE A 252 -12.317 6.698 13.495 1.00 24.98 C ANISOU 2596 CG1 ILE A 252 3156 2932 3403 188 20 160 C ATOM 2597 CG2 ILE A 252 -13.336 8.496 14.915 1.00 15.47 C ANISOU 2597 CG2 ILE A 252 1918 1770 2190 174 -82 175 C ATOM 2598 CD1 ILE A 252 -13.431 6.642 12.474 1.00 24.07 C ANISOU 2598 CD1 ILE A 252 3093 2839 3212 159 42 153 C ATOM 2599 N ASN A 253 -12.751 6.899 18.091 1.00 18.78 N ANISOU 2599 N ASN A 253 2306 2153 2677 233 -179 166 N ATOM 2600 CA ASN A 253 -13.070 7.436 19.411 1.00 22.02 C ANISOU 2600 CA ASN A 253 2696 2575 3096 248 -247 172 C ATOM 2601 C ASN A 253 -11.809 7.662 20.233 1.00 20.08 C ANISOU 2601 C ASN A 253 2398 2299 2932 279 -267 176 C ATOM 2602 O ASN A 253 -11.723 8.633 20.995 1.00 20.74 O ANISOU 2602 O ASN A 253 2452 2388 3040 292 -317 185 O ATOM 2603 CB ASN A 253 -14.029 6.499 20.148 1.00 22.57 C ANISOU 2603 CB ASN A 253 2798 2657 3120 251 -275 167 C ATOM 2604 CG ASN A 253 -15.425 6.508 19.555 1.00 19.60 C ANISOU 2604 CG ASN A 253 2472 2312 2665 221 -273 170 C ATOM 2605 OD1 ASN A 253 -15.796 7.429 18.830 1.00 22.44 O ANISOU 2605 OD1 ASN A 253 2838 2688 2998 199 -264 176 O ATOM 2606 ND2 ASN A 253 -16.209 5.483 19.867 1.00 18.48 N ANISOU 2606 ND2 ASN A 253 2362 2174 2485 222 -283 168 N ATOM 2607 N CYS A 254 -10.819 6.777 20.090 1.00 18.80 N ANISOU 2607 N CYS A 254 2225 2104 2814 291 -229 171 N ATOM 2608 CA CYS A 254 -9.551 6.965 20.788 1.00 21.74 C ANISOU 2608 CA CYS A 254 2548 2442 3269 318 -243 177 C ATOM 2609 C CYS A 254 -8.841 8.230 20.314 1.00 17.78 C ANISOU 2609 C CYS A 254 2009 1932 2814 320 -240 194 C ATOM 2610 O CYS A 254 -8.258 8.960 21.123 1.00 22.36 O ANISOU 2610 O CYS A 254 2549 2497 3449 341 -284 203 O ATOM 2611 CB CYS A 254 -8.654 5.740 20.593 1.00 20.25 C ANISOU 2611 CB CYS A 254 2359 2220 3116 326 -196 170 C ATOM 2612 SG CYS A 254 -9.187 4.260 21.493 1.00 21.49 S ANISOU 2612 SG CYS A 254 2539 2379 3246 334 -212 153 S ATOM 2613 N PHE A 255 -8.872 8.503 19.006 1.00 17.49 N ANISOU 2613 N PHE A 255 1984 1903 2759 300 -190 199 N ATOM 2614 CA PHE A 255 -8.265 9.731 18.497 1.00 18.55 C ANISOU 2614 CA PHE A 255 2080 2033 2937 302 -186 217 C ATOM 2615 C PHE A 255 -9.015 10.962 18.989 1.00 21.84 C ANISOU 2615 C PHE A 255 2485 2480 3333 296 -246 222 C ATOM 2616 O PHE A 255 -8.393 11.950 19.396 1.00 24.12 O ANISOU 2616 O PHE A 255 2728 2757 3680 312 -281 236 O ATOM 2617 CB PHE A 255 -8.215 9.709 16.967 1.00 16.55 C ANISOU 2617 CB PHE A 255 1842 1785 2661 284 -117 222 C ATOM 2618 CG PHE A 255 -6.999 9.022 16.409 1.00 18.69 C ANISOU 2618 CG PHE A 255 2100 2019 2984 300 -60 230 C ATOM 2619 CD1 PHE A 255 -5.813 9.718 16.233 1.00 21.71 C ANISOU 2619 CD1 PHE A 255 2430 2373 3446 319 -50 255 C ATOM 2620 CD2 PHE A 255 -7.040 7.678 16.070 1.00 18.63 C ANISOU 2620 CD2 PHE A 255 2130 2001 2946 298 -17 215 C ATOM 2621 CE1 PHE A 255 -4.692 9.088 15.725 1.00 27.04 C ANISOU 2621 CE1 PHE A 255 3094 3011 4168 335 4 267 C ATOM 2622 CE2 PHE A 255 -5.923 7.044 15.559 1.00 22.81 C ANISOU 2622 CE2 PHE A 255 2650 2495 3521 313 36 224 C ATOM 2623 CZ PHE A 255 -4.746 7.749 15.387 1.00 25.78 C ANISOU 2623 CZ PHE A 255 2976 2845 3975 332 48 251 C ATOM 2624 N THR A 256 -10.350 10.922 18.955 1.00 20.33 N ANISOU 2624 N THR A 256 2335 2326 3061 274 -260 212 N ATOM 2625 CA THR A 256 -11.145 12.021 19.496 1.00 21.78 C ANISOU 2625 CA THR A 256 2514 2541 3220 268 -318 217 C ATOM 2626 C THR A 256 -10.800 12.282 20.957 1.00 25.28 C ANISOU 2626 C THR A 256 2928 2971 3706 301 -387 219 C ATOM 2627 O THR A 256 -10.663 13.437 21.376 1.00 28.05 O ANISOU 2627 O THR A 256 3265 3341 4050 293 -407 214 O ATOM 2628 CB THR A 256 -12.636 11.706 19.355 1.00 22.34 C ANISOU 2628 CB THR A 256 2640 2650 3199 242 -322 208 C ATOM 2629 OG1 THR A 256 -12.956 11.480 17.977 1.00 24.81 O ANISOU 2629 OG1 THR A 256 2981 2972 3471 213 -260 205 O ATOM 2630 CG2 THR A 256 -13.483 12.854 19.894 1.00 20.21 C ANISOU 2630 CG2 THR A 256 2367 2414 2900 236 -380 216 C ATOM 2631 N PHE A 257 -10.636 11.214 21.741 1.00 25.34 N ANISOU 2631 N PHE A 257 2947 2962 3719 319 -393 208 N ATOM 2632 CA PHE A 257 -10.440 11.338 23.181 1.00 27.83 C ANISOU 2632 CA PHE A 257 3271 3295 4008 319 -411 188 C ATOM 2633 C PHE A 257 -8.997 11.680 23.529 1.00 25.34 C ANISOU 2633 C PHE A 257 2924 2953 3749 326 -398 185 C ATOM 2634 O PHE A 257 -8.742 12.610 24.301 1.00 27.61 O ANISOU 2634 O PHE A 257 3210 3258 4024 319 -414 177 O ATOM 2635 CB PHE A 257 -10.862 10.036 23.868 1.00 22.29 C ANISOU 2635 CB PHE A 257 2594 2593 3280 330 -413 178 C ATOM 2636 CG PHE A 257 -10.711 10.056 25.364 1.00 21.30 C ANISOU 2636 CG PHE A 257 2476 2487 3129 332 -423 162 C ATOM 2637 CD1 PHE A 257 -11.459 10.929 26.141 1.00 18.88 C ANISOU 2637 CD1 PHE A 257 2186 2221 2766 320 -437 157 C ATOM 2638 CD2 PHE A 257 -9.827 9.192 25.996 1.00 20.53 C ANISOU 2638 CD2 PHE A 257 2369 2366 3066 345 -412 154 C ATOM 2639 CE1 PHE A 257 -11.324 10.945 27.519 1.00 21.58 C ANISOU 2639 CE1 PHE A 257 2534 2577 3088 324 -438 146 C ATOM 2640 CE2 PHE A 257 -9.691 9.201 27.374 1.00 25.65 C ANISOU 2640 CE2 PHE A 257 3023 3030 3691 346 -418 142 C ATOM 2641 CZ PHE A 257 -10.439 10.081 28.138 1.00 25.81 C ANISOU 2641 CZ PHE A 257 3059 3089 3657 337 -431 140 C ATOM 2642 N PHE A 258 -8.040 10.939 22.969 1.00 20.63 N ANISOU 2642 N PHE A 258 2308 2316 3215 338 -367 194 N ATOM 2643 CA PHE A 258 -6.650 11.064 23.395 1.00 23.13 C ANISOU 2643 CA PHE A 258 2601 2607 3581 341 -355 192 C ATOM 2644 C PHE A 258 -5.906 12.215 22.729 1.00 26.44 C ANISOU 2644 C PHE A 258 2990 3018 4037 334 -345 207 C ATOM 2645 O PHE A 258 -4.872 12.644 23.255 1.00 25.27 O ANISOU 2645 O PHE A 258 2828 2857 3916 331 -348 206 O ATOM 2646 CB PHE A 258 -5.902 9.755 23.130 1.00 19.05 C ANISOU 2646 CB PHE A 258 2077 2051 3111 354 -319 195 C ATOM 2647 CG PHE A 258 -6.230 8.663 24.106 1.00 24.54 C ANISOU 2647 CG PHE A 258 2795 2752 3778 361 -329 178 C ATOM 2648 CD1 PHE A 258 -6.127 8.883 25.472 1.00 24.78 C ANISOU 2648 CD1 PHE A 258 2833 2802 3780 357 -357 163 C ATOM 2649 CD2 PHE A 258 -6.631 7.414 23.660 1.00 24.98 C ANISOU 2649 CD2 PHE A 258 2863 2792 3837 370 -308 177 C ATOM 2650 CE1 PHE A 258 -6.423 7.877 26.375 1.00 24.68 C ANISOU 2650 CE1 PHE A 258 2837 2798 3741 363 -362 149 C ATOM 2651 CE2 PHE A 258 -6.934 6.405 24.559 1.00 24.54 C ANISOU 2651 CE2 PHE A 258 2824 2745 3755 375 -318 162 C ATOM 2652 CZ PHE A 258 -6.828 6.637 25.919 1.00 23.46 C ANISOU 2652 CZ PHE A 258 2691 2632 3589 371 -344 149 C ATOM 2653 N CYS A 259 -6.386 12.727 21.592 1.00 31.08 N ANISOU 2653 N CYS A 259 3568 3613 4627 329 -334 223 N ATOM 2654 CA CYS A 259 -5.715 13.813 20.877 1.00 33.95 C ANISOU 2654 CA CYS A 259 3901 3973 5027 321 -320 239 C ATOM 2655 C CYS A 259 -6.665 14.995 20.709 1.00 33.07 C ANISOU 2655 C CYS A 259 3794 3901 4871 305 -347 237 C ATOM 2656 O CYS A 259 -7.257 15.177 19.634 1.00 32.31 O ANISOU 2656 O CYS A 259 3689 3814 4773 300 -331 253 O ATOM 2657 CB CYS A 259 -5.192 13.355 19.515 1.00 42.55 C ANISOU 2657 CB CYS A 259 4967 5032 6169 332 -264 264 C ATOM 2658 SG CYS A 259 -4.165 14.616 18.701 1.00 54.58 S ANISOU 2658 SG CYS A 259 6449 6549 7739 324 -243 287 S ATOM 2659 N PRO A 260 -6.822 15.832 21.740 1.00 35.65 N ANISOU 2659 N PRO A 260 4134 4251 5159 294 -381 220 N ATOM 2660 CA PRO A 260 -7.607 17.063 21.560 1.00 39.07 C ANISOU 2660 CA PRO A 260 4572 4721 5552 276 -399 218 C ATOM 2661 C PRO A 260 -6.959 18.061 20.611 1.00 41.56 C ANISOU 2661 C PRO A 260 4852 5030 5909 268 -382 235 C ATOM 2662 O PRO A 260 -7.637 19.001 20.178 1.00 40.84 O ANISOU 2662 O PRO A 260 4759 4968 5789 252 -389 236 O ATOM 2663 CB PRO A 260 -7.706 17.632 22.982 1.00 40.23 C ANISOU 2663 CB PRO A 260 4742 4885 5657 273 -426 197 C ATOM 2664 CG PRO A 260 -6.517 17.085 23.685 1.00 38.01 C ANISOU 2664 CG PRO A 260 4454 4571 5418 286 -423 194 C ATOM 2665 CD PRO A 260 -6.309 15.706 23.116 1.00 35.32 C ANISOU 2665 CD PRO A 260 4107 4205 5110 299 -400 203 C ATOM 2666 N ASP A 261 -5.675 17.895 20.277 1.00 37.52 N ANISOU 2666 N ASP A 261 4312 4483 5461 277 -358 249 N ATOM 2667 CA ASP A 261 -5.034 18.773 19.306 1.00 40.19 C ANISOU 2667 CA ASP A 261 4617 4816 5839 270 -337 269 C ATOM 2668 C ASP A 261 -5.240 18.311 17.870 1.00 37.64 C ANISOU 2668 C ASP A 261 4273 4489 5542 276 -292 294 C ATOM 2669 O ASP A 261 -4.975 19.082 16.941 1.00 38.11 O ANISOU 2669 O ASP A 261 4304 4553 5622 270 -270 312 O ATOM 2670 CB ASP A 261 -3.537 18.883 19.593 1.00 49.20 C ANISOU 2670 CB ASP A 261 5739 5922 7033 276 -329 277 C ATOM 2671 CG ASP A 261 -3.246 19.586 20.899 1.00 57.81 C ANISOU 2671 CG ASP A 261 6846 7016 8103 269 -367 257 C ATOM 2672 OD1 ASP A 261 -4.075 20.420 21.321 1.00 57.92 O ANISOU 2672 OD1 ASP A 261 6878 7062 8068 259 -392 242 O ATOM 2673 OD2 ASP A 261 -2.192 19.304 21.504 1.00 62.82 O ANISOU 2673 OD2 ASP A 261 7477 7622 8771 275 -369 258 O ATOM 2674 N CYS A 262 -5.687 17.075 17.667 1.00 37.84 N ANISOU 2674 N CYS A 262 4311 4503 5564 290 -274 296 N ATOM 2675 CA CYS A 262 -6.023 16.592 16.336 1.00 35.95 C ANISOU 2675 CA CYS A 262 4058 4261 5342 300 -224 319 C ATOM 2676 C CYS A 262 -7.418 17.062 15.952 1.00 33.55 C ANISOU 2676 C CYS A 262 3765 3999 4983 281 -240 318 C ATOM 2677 O CYS A 262 -8.330 17.089 16.784 1.00 35.17 O ANISOU 2677 O CYS A 262 3999 4226 5137 271 -289 299 O ATOM 2678 CB CYS A 262 -5.970 15.063 16.282 1.00 39.07 C ANISOU 2678 CB CYS A 262 4479 4627 5740 317 -189 316 C ATOM 2679 SG CYS A 262 -4.390 14.278 16.708 1.00 50.34 S ANISOU 2679 SG CYS A 262 5893 6002 7232 338 -165 321 S ATOM 2680 N SER A 263 -7.584 17.436 14.687 1.00 33.72 N ANISOU 2680 N SER A 263 3784 4042 4985 263 -188 326 N ATOM 2681 CA SER A 263 -8.919 17.724 14.184 1.00 36.93 C ANISOU 2681 CA SER A 263 4230 4499 5304 225 -182 311 C ATOM 2682 C SER A 263 -9.781 16.472 14.269 1.00 33.37 C ANISOU 2682 C SER A 263 3851 4056 4773 209 -163 284 C ATOM 2683 O SER A 263 -9.306 15.357 14.043 1.00 31.60 O ANISOU 2683 O SER A 263 3648 3805 4553 221 -121 279 O ATOM 2684 CB SER A 263 -8.855 18.229 12.742 1.00 42.27 C ANISOU 2684 CB SER A 263 4891 5193 5976 211 -122 324 C ATOM 2685 OG SER A 263 -8.299 19.530 12.683 1.00 46.75 O ANISOU 2685 OG SER A 263 5390 5763 6611 221 -148 349 O ATOM 2686 N HIS A 264 -11.049 16.660 14.623 1.00 30.53 N ANISOU 2686 N HIS A 264 3526 3731 4342 184 -197 271 N ATOM 2687 CA HIS A 264 -11.969 15.536 14.720 1.00 28.46 C ANISOU 2687 CA HIS A 264 3330 3477 4004 168 -185 250 C ATOM 2688 C HIS A 264 -12.089 14.844 13.368 1.00 30.11 C ANISOU 2688 C HIS A 264 3576 3689 4177 152 -108 244 C ATOM 2689 O HIS A 264 -12.049 15.492 12.318 1.00 29.46 O ANISOU 2689 O HIS A 264 3479 3621 4092 139 -71 253 O ATOM 2690 CB HIS A 264 -13.340 16.023 15.194 1.00 27.87 C ANISOU 2690 CB HIS A 264 3286 3442 3862 143 -231 244 C ATOM 2691 CG HIS A 264 -14.247 14.930 15.667 1.00 27.39 C ANISOU 2691 CG HIS A 264 3284 3385 3737 136 -240 229 C ATOM 2692 ND1 HIS A 264 -14.775 13.978 14.821 1.00 31.69 N ANISOU 2692 ND1 HIS A 264 3880 3932 4227 116 -188 219 N ATOM 2693 CD2 HIS A 264 -14.730 14.645 16.900 1.00 25.97 C ANISOU 2693 CD2 HIS A 264 3118 3208 3541 148 -295 226 C ATOM 2694 CE1 HIS A 264 -15.536 13.149 15.513 1.00 33.00 C ANISOU 2694 CE1 HIS A 264 4087 4100 4350 116 -213 211 C ATOM 2695 NE2 HIS A 264 -15.529 13.534 16.777 1.00 32.19 N ANISOU 2695 NE2 HIS A 264 3963 4000 4269 136 -276 216 N ATOM 2696 N ALA A 265 -12.212 13.521 13.398 1.00 24.78 N ANISOU 2696 N ALA A 265 2945 2997 3472 156 -85 230 N ATOM 2697 CA ALA A 265 -12.426 12.769 12.172 1.00 21.31 C ANISOU 2697 CA ALA A 265 2549 2559 2991 143 -18 221 C ATOM 2698 C ALA A 265 -13.607 13.362 11.405 1.00 25.16 C ANISOU 2698 C ALA A 265 3066 3084 3408 106 -9 218 C ATOM 2699 O ALA A 265 -14.616 13.736 12.019 1.00 22.85 O ANISOU 2699 O ALA A 265 2790 2816 3074 86 -56 215 O ATOM 2700 CB ALA A 265 -12.685 11.293 12.485 1.00 19.55 C ANISOU 2700 CB ALA A 265 2374 2318 2736 148 -11 204 C ATOM 2701 N PRO A 266 -13.513 13.486 10.084 1.00 29.47 N ANISOU 2701 N PRO A 266 3619 3637 3941 97 50 219 N ATOM 2702 CA PRO A 266 -14.576 14.154 9.326 1.00 30.44 C ANISOU 2702 CA PRO A 266 3765 3797 4004 60 60 217 C ATOM 2703 C PRO A 266 -15.871 13.358 9.356 1.00 29.45 C ANISOU 2703 C PRO A 266 3711 3681 3796 34 52 201 C ATOM 2704 O PRO A 266 -15.896 12.161 9.651 1.00 26.05 O ANISOU 2704 O PRO A 266 3317 3229 3353 45 54 190 O ATOM 2705 CB PRO A 266 -14.005 14.242 7.906 1.00 28.84 C ANISOU 2705 CB PRO A 266 3555 3592 3812 66 131 222 C ATOM 2706 CG PRO A 266 -12.978 13.160 7.839 1.00 31.45 C ANISOU 2706 CG PRO A 266 3889 3883 4179 102 164 221 C ATOM 2707 CD PRO A 266 -12.406 13.037 9.222 1.00 29.29 C ANISOU 2707 CD PRO A 266 3582 3587 3958 123 111 225 C ATOM 2708 N LEU A 267 -16.965 14.057 9.046 1.00 28.00 N ANISOU 2708 N LEU A 267 3548 3532 3560 -3 42 201 N ATOM 2709 CA LEU A 267 -18.290 13.456 9.170 1.00 31.11 C ANISOU 2709 CA LEU A 267 4007 3935 3878 -30 26 192 C ATOM 2710 C LEU A 267 -18.440 12.238 8.265 1.00 32.27 C ANISOU 2710 C LEU A 267 4210 4063 3989 -29 75 178 C ATOM 2711 O LEU A 267 -19.062 11.242 8.656 1.00 28.15 O ANISOU 2711 O LEU A 267 3734 3529 3431 -31 58 171 O ATOM 2712 CB LEU A 267 -19.368 14.494 8.861 1.00 33.33 C ANISOU 2712 CB LEU A 267 4298 4254 4112 -72 13 199 C ATOM 2713 CG LEU A 267 -20.821 14.032 8.991 1.00 37.94 C ANISOU 2713 CG LEU A 267 4947 4849 4619 -103 -7 197 C ATOM 2714 CD1 LEU A 267 -21.107 13.535 10.398 1.00 37.17 C ANISOU 2714 CD1 LEU A 267 4857 4744 4522 -87 -66 201 C ATOM 2715 CD2 LEU A 267 -21.779 15.155 8.610 1.00 37.06 C ANISOU 2715 CD2 LEU A 267 4840 4774 4467 -146 -14 205 C ATOM 2716 N TRP A 268 -17.873 12.291 7.055 1.00 30.43 N ANISOU 2716 N TRP A 268 3972 3825 3765 -23 135 176 N ATOM 2717 CA TRP A 268 -17.995 11.151 6.151 1.00 29.62 C ANISOU 2717 CA TRP A 268 3925 3703 3626 -18 181 161 C ATOM 2718 C TRP A 268 -17.284 9.920 6.700 1.00 25.87 C ANISOU 2718 C TRP A 268 3456 3193 3181 15 179 154 C ATOM 2719 O TRP A 268 -17.746 8.793 6.486 1.00 25.40 O ANISOU 2719 O TRP A 268 3451 3118 3083 15 187 140 O ATOM 2720 CB TRP A 268 -17.462 11.508 4.760 1.00 27.58 C ANISOU 2720 CB TRP A 268 3658 3447 3374 -12 246 162 C ATOM 2721 CG TRP A 268 -15.980 11.752 4.691 1.00 26.06 C ANISOU 2721 CG TRP A 268 3405 3239 3258 27 272 174 C ATOM 2722 CD1 TRP A 268 -15.344 12.957 4.767 1.00 27.05 C ANISOU 2722 CD1 TRP A 268 3462 3379 3437 33 268 193 C ATOM 2723 CD2 TRP A 268 -14.953 10.768 4.513 1.00 24.74 C ANISOU 2723 CD2 TRP A 268 3239 3038 3124 66 305 171 C ATOM 2724 NE1 TRP A 268 -13.987 12.784 4.657 1.00 25.58 N ANISOU 2724 NE1 TRP A 268 3235 3167 3317 73 296 205 N ATOM 2725 CE2 TRP A 268 -13.720 11.449 4.501 1.00 25.47 C ANISOU 2725 CE2 TRP A 268 3264 3124 3291 93 321 192 C ATOM 2726 CE3 TRP A 268 -14.956 9.375 4.371 1.00 28.76 C ANISOU 2726 CE3 TRP A 268 3800 3520 3609 80 322 155 C ATOM 2727 CZ2 TRP A 268 -12.503 10.787 4.350 1.00 27.51 C ANISOU 2727 CZ2 TRP A 268 3505 3349 3597 134 356 199 C ATOM 2728 CZ3 TRP A 268 -13.746 8.720 4.221 1.00 29.18 C ANISOU 2728 CZ3 TRP A 268 3836 3543 3708 119 356 159 C ATOM 2729 CH2 TRP A 268 -12.537 9.426 4.211 1.00 31.33 C ANISOU 2729 CH2 TRP A 268 4043 3809 4053 145 374 182 C ATOM 2730 N LEU A 269 -16.172 10.112 7.416 1.00 24.22 N ANISOU 2730 N LEU A 269 3191 2970 3041 44 167 163 N ATOM 2731 CA LEU A 269 -15.468 8.981 8.011 1.00 25.45 C ANISOU 2731 CA LEU A 269 3348 3094 3230 74 164 156 C ATOM 2732 C LEU A 269 -16.224 8.421 9.211 1.00 25.15 C ANISOU 2732 C LEU A 269 3330 3056 3169 67 106 151 C ATOM 2733 O LEU A 269 -16.194 7.208 9.451 1.00 24.14 O ANISOU 2733 O LEU A 269 3230 2907 3036 79 107 141 O ATOM 2734 CB LEU A 269 -14.053 9.398 8.413 1.00 23.84 C ANISOU 2734 CB LEU A 269 3076 2872 3108 105 168 170 C ATOM 2735 CG LEU A 269 -13.121 8.285 8.896 1.00 24.67 C ANISOU 2735 CG LEU A 269 3177 2941 3256 137 176 166 C ATOM 2736 CD1 LEU A 269 -12.999 7.198 7.842 1.00 24.18 C ANISOU 2736 CD1 LEU A 269 3161 2862 3164 146 233 154 C ATOM 2737 CD2 LEU A 269 -11.750 8.848 9.253 1.00 26.72 C ANISOU 2737 CD2 LEU A 269 3369 3182 3601 165 179 185 C ATOM 2738 N MET A 270 -16.900 9.285 9.974 1.00 23.40 N ANISOU 2738 N MET A 270 3094 2859 2938 49 56 161 N ATOM 2739 CA MET A 270 -17.768 8.810 11.045 1.00 24.37 C ANISOU 2739 CA MET A 270 3240 2987 3032 44 2 160 C ATOM 2740 C MET A 270 -18.888 7.944 10.486 1.00 23.84 C ANISOU 2740 C MET A 270 3241 2920 2896 22 12 152 C ATOM 2741 O MET A 270 -19.162 6.854 11.001 1.00 26.48 O ANISOU 2741 O MET A 270 3601 3240 3221 32 -6 147 O ATOM 2742 CB MET A 270 -18.350 9.994 11.821 1.00 21.94 C ANISOU 2742 CB MET A 270 2909 2708 2719 29 -51 174 C ATOM 2743 CG MET A 270 -17.319 10.930 12.429 1.00 24.62 C ANISOU 2743 CG MET A 270 3181 3046 3128 50 -71 183 C ATOM 2744 SD MET A 270 -16.220 10.110 13.600 1.00 30.12 S ANISOU 2744 SD MET A 270 3845 3708 3890 94 -93 181 S ATOM 2745 CE MET A 270 -17.394 9.280 14.671 1.00 34.93 C ANISOU 2745 CE MET A 270 4497 4325 4450 92 -145 179 C ATOM 2746 N TYR A 271 -19.504 8.394 9.410 1.00 24.38 N ANISOU 2746 N TYR A 271 3339 3004 2922 -5 40 151 N ATOM 2747 CA TYR A 271 -20.558 7.637 8.782 1.00 26.79 C ANISOU 2747 CA TYR A 271 3711 3306 3164 -26 50 145 C ATOM 2748 C TYR A 271 -20.014 6.299 8.290 1.00 26.74 C ANISOU 2748 C TYR A 271 3729 3266 3163 -2 84 129 C ATOM 2749 O TYR A 271 -20.629 5.290 8.466 1.00 24.60 O ANISOU 2749 O TYR A 271 3499 2982 2865 -3 68 124 O ATOM 2750 CB TYR A 271 -21.176 8.399 7.609 1.00 26.47 C ANISOU 2750 CB TYR A 271 3693 3284 3080 -58 81 145 C ATOM 2751 CG TYR A 271 -22.086 9.532 7.980 1.00 29.46 C ANISOU 2751 CG TYR A 271 4066 3696 3433 -91 45 161 C ATOM 2752 CD1 TYR A 271 -22.732 9.544 9.190 1.00 33.97 C ANISOU 2752 CD1 TYR A 271 4636 4275 3995 -94 -13 174 C ATOM 2753 CD2 TYR A 271 -22.326 10.576 7.107 1.00 32.91 C ANISOU 2753 CD2 TYR A 271 4497 4156 3852 -118 72 163 C ATOM 2754 CE1 TYR A 271 -23.569 10.564 9.546 1.00 35.81 C ANISOU 2754 CE1 TYR A 271 4866 4538 4202 -122 -46 189 C ATOM 2755 CE2 TYR A 271 -23.173 11.603 7.449 1.00 32.43 C ANISOU 2755 CE2 TYR A 271 4430 4126 3766 -150 40 177 C ATOM 2756 CZ TYR A 271 -23.789 11.586 8.674 1.00 38.66 C ANISOU 2756 CZ TYR A 271 5222 4922 4546 -152 -19 191 C ATOM 2757 OH TYR A 271 -24.617 12.587 9.053 1.00 43.93 O ANISOU 2757 OH TYR A 271 5884 5618 5187 -181 -52 207 O ATOM 2758 N LEU A 272 -18.842 6.313 7.687 1.00 19.84 N ANISOU 2758 N LEU A 272 2830 2380 2330 20 130 123 N ATOM 2759 CA LEU A 272 -18.263 5.102 7.187 1.00 24.23 C ANISOU 2759 CA LEU A 272 3409 2905 2892 45 165 108 C ATOM 2760 C LEU A 272 -17.970 4.122 8.331 1.00 23.61 C ANISOU 2760 C LEU A 272 3321 2809 2843 65 131 106 C ATOM 2761 O LEU A 272 -18.282 2.965 8.243 1.00 24.18 O ANISOU 2761 O LEU A 272 3432 2864 2894 70 131 95 O ATOM 2762 CB LEU A 272 -17.021 5.405 6.380 1.00 26.33 C ANISOU 2762 CB LEU A 272 3645 3162 3198 68 221 108 C ATOM 2763 CG LEU A 272 -16.324 4.239 5.707 1.00 34.71 C ANISOU 2763 CG LEU A 272 4731 4194 4265 96 265 95 C ATOM 2764 CD1 LEU A 272 -17.285 3.441 4.864 1.00 36.80 C ANISOU 2764 CD1 LEU A 272 5068 4452 4463 83 276 80 C ATOM 2765 CD2 LEU A 272 -15.163 4.739 4.881 1.00 36.00 C ANISOU 2765 CD2 LEU A 272 4861 4351 4466 120 321 103 C ATOM 2766 N ALA A 273 -17.433 4.627 9.423 1.00 23.08 N ANISOU 2766 N ALA A 273 3200 2745 2824 76 100 116 N ATOM 2767 CA ALA A 273 -17.137 3.791 10.561 1.00 20.62 C ANISOU 2767 CA ALA A 273 2874 2419 2543 97 68 114 C ATOM 2768 C ALA A 273 -18.414 3.204 11.146 1.00 16.55 C ANISOU 2768 C ALA A 273 2396 1912 1982 82 22 116 C ATOM 2769 O ALA A 273 -18.445 2.073 11.521 1.00 18.30 O ANISOU 2769 O ALA A 273 2631 2116 2205 95 12 110 O ATOM 2770 CB ALA A 273 -16.363 4.546 11.606 1.00 18.71 C ANISOU 2770 CB ALA A 273 2570 2181 2361 112 40 125 C ATOM 2771 N ILE A 274 -19.455 4.009 11.218 1.00 20.72 N ANISOU 2771 N ILE A 274 2938 2466 2470 56 -5 128 N ATOM 2772 CA ILE A 274 -20.722 3.541 11.741 1.00 24.22 C ANISOU 2772 CA ILE A 274 3417 2916 2869 43 -49 137 C ATOM 2773 C ILE A 274 -21.332 2.440 10.868 1.00 22.67 C ANISOU 2773 C ILE A 274 3280 2702 2632 35 -29 127 C ATOM 2774 O ILE A 274 -21.734 1.421 11.364 1.00 19.36 O ANISOU 2774 O ILE A 274 2878 2271 2207 44 -55 128 O ATOM 2775 CB ILE A 274 -21.712 4.699 11.944 1.00 23.40 C ANISOU 2775 CB ILE A 274 3317 2842 2730 16 -79 155 C ATOM 2776 CG1 ILE A 274 -21.263 5.581 13.099 1.00 24.60 C ANISOU 2776 CG1 ILE A 274 3414 3010 2922 30 -117 166 C ATOM 2777 CG2 ILE A 274 -23.101 4.166 12.207 1.00 22.03 C ANISOU 2777 CG2 ILE A 274 3191 2673 2505 0 -115 169 C ATOM 2778 CD1 ILE A 274 -21.874 6.942 13.124 1.00 23.01 C ANISOU 2778 CD1 ILE A 274 3206 2840 2698 5 -136 180 C ATOM 2779 N VAL A 275 -21.330 2.635 9.559 1.00 20.80 N ANISOU 2779 N VAL A 275 3072 2462 2370 22 16 117 N ATOM 2780 CA VAL A 275 -21.887 1.629 8.665 1.00 24.68 C ANISOU 2780 CA VAL A 275 3623 2934 2821 16 33 106 C ATOM 2781 C VAL A 275 -21.115 0.324 8.699 1.00 21.73 C ANISOU 2781 C VAL A 275 3249 2530 2475 47 48 91 C ATOM 2782 O VAL A 275 -21.685 -0.715 8.608 1.00 21.61 O ANISOU 2782 O VAL A 275 3273 2500 2439 48 34 87 O ATOM 2783 CB VAL A 275 -22.206 2.088 7.228 1.00 30.45 C ANISOU 2783 CB VAL A 275 4393 3667 3511 -4 75 99 C ATOM 2784 CG1 VAL A 275 -23.269 3.163 7.229 1.00 32.29 C ANISOU 2784 CG1 VAL A 275 4636 3928 3707 -41 54 116 C ATOM 2785 CG2 VAL A 275 -20.975 2.506 6.483 1.00 33.68 C ANISOU 2785 CG2 VAL A 275 4773 4073 3951 13 131 88 C ATOM 2786 N LEU A 276 -19.807 0.422 8.831 1.00 22.62 N ANISOU 2786 N LEU A 276 3318 2637 2640 70 75 84 N ATOM 2787 CA LEU A 276 -18.961 -0.743 8.914 1.00 21.89 C ANISOU 2787 CA LEU A 276 3221 2518 2580 98 92 70 C ATOM 2788 C LEU A 276 -19.303 -1.571 10.155 1.00 19.31 C ANISOU 2788 C LEU A 276 2882 2187 2267 107 42 75 C ATOM 2789 O LEU A 276 -19.360 -2.760 10.094 1.00 15.41 O ANISOU 2789 O LEU A 276 2411 1674 1771 118 40 66 O ATOM 2790 CB LEU A 276 -17.503 -0.339 8.935 1.00 22.51 C ANISOU 2790 CB LEU A 276 3249 2590 2715 120 128 68 C ATOM 2791 CG LEU A 276 -16.530 -1.495 8.988 1.00 31.59 C ANISOU 2791 CG LEU A 276 4391 3712 3901 148 151 56 C ATOM 2792 CD1 LEU A 276 -16.689 -2.418 7.802 1.00 32.91 C ANISOU 2792 CD1 LEU A 276 4613 3860 4030 153 185 40 C ATOM 2793 CD2 LEU A 276 -15.104 -1.014 9.125 1.00 33.03 C ANISOU 2793 CD2 LEU A 276 4519 3886 4143 169 182 61 C ATOM 2794 N ALA A 277 -19.552 -0.891 11.260 1.00 21.72 N ANISOU 2794 N ALA A 277 3153 2512 2587 103 0 91 N ATOM 2795 CA ALA A 277 -19.929 -1.538 12.478 1.00 19.27 C ANISOU 2795 CA ALA A 277 2829 2203 2290 114 -49 100 C ATOM 2796 C ALA A 277 -21.250 -2.266 12.261 1.00 20.74 C ANISOU 2796 C ALA A 277 3067 2387 2426 100 -76 107 C ATOM 2797 O ALA A 277 -21.385 -3.379 12.654 1.00 22.00 O ANISOU 2797 O ALA A 277 3232 2534 2595 114 -94 105 O ATOM 2798 CB ALA A 277 -20.051 -0.539 13.592 1.00 16.75 C ANISOU 2798 CB ALA A 277 2469 1907 1986 114 -89 118 C ATOM 2799 N HIS A 278 -22.178 -1.650 11.562 1.00 16.96 N ANISOU 2799 N HIS A 278 2627 1919 1898 73 -76 115 N ATOM 2800 CA HIS A 278 -23.476 -2.269 11.327 1.00 20.65 C ANISOU 2800 CA HIS A 278 3146 2380 2320 59 -103 126 C ATOM 2801 C HIS A 278 -23.388 -3.432 10.343 1.00 20.66 C ANISOU 2801 C HIS A 278 3189 2352 2309 65 -78 106 C ATOM 2802 O HIS A 278 -24.177 -4.378 10.440 1.00 21.86 O ANISOU 2802 O HIS A 278 3371 2490 2446 66 -108 114 O ATOM 2803 CB HIS A 278 -24.473 -1.221 10.831 1.00 20.23 C ANISOU 2803 CB HIS A 278 3122 2345 2218 25 -108 141 C ATOM 2804 CG HIS A 278 -24.821 -0.186 11.856 1.00 22.31 C ANISOU 2804 CG HIS A 278 3354 2638 2485 19 -145 165 C ATOM 2805 ND1 HIS A 278 -25.343 1.046 11.525 1.00 23.34 N ANISOU 2805 ND1 HIS A 278 3492 2791 2586 -10 -142 176 N ATOM 2806 CD2 HIS A 278 -24.726 -0.203 13.207 1.00 22.11 C ANISOU 2806 CD2 HIS A 278 3288 2623 2488 39 -185 179 C ATOM 2807 CE1 HIS A 278 -25.551 1.745 12.628 1.00 22.77 C ANISOU 2807 CE1 HIS A 278 3386 2741 2522 -6 -181 196 C ATOM 2808 NE2 HIS A 278 -25.184 1.010 13.662 1.00 23.32 N ANISOU 2808 NE2 HIS A 278 3429 2805 2628 25 -207 198 N ATOM 2809 N ATHR A 279 -22.448 -3.377 9.395 0.56 21.94 N ANISOU 2809 N ATHR A 279 3354 2502 2480 72 -24 84 N ATOM 2810 N BTHR A 279 -22.445 -3.384 9.393 0.44 21.94 N ANISOU 2810 N BTHR A 279 3354 2502 2480 72 -24 84 N ATOM 2811 CA ATHR A 279 -22.289 -4.454 8.423 0.56 22.68 C ANISOU 2811 CA ATHR A 279 3490 2568 2561 83 2 64 C ATOM 2812 CA BTHR A 279 -22.311 -4.471 8.425 0.44 22.66 C ANISOU 2812 CA BTHR A 279 3488 2565 2558 83 2 64 C ATOM 2813 C ATHR A 279 -21.968 -5.786 9.093 0.56 23.52 C ANISOU 2813 C ATHR A 279 3581 2655 2698 107 -18 58 C ATOM 2814 C BTHR A 279 -21.949 -5.792 9.085 0.44 23.53 C ANISOU 2814 C BTHR A 279 3583 2657 2701 108 -17 57 C ATOM 2815 O ATHR A 279 -22.242 -6.843 8.513 0.56 22.28 O ANISOU 2815 O ATHR A 279 3464 2475 2525 114 -19 47 O ATOM 2816 O BTHR A 279 -22.147 -6.849 8.477 0.44 22.35 O ANISOU 2816 O BTHR A 279 3472 2484 2536 115 -15 45 O ATOM 2817 CB ATHR A 279 -21.194 -4.087 7.413 0.56 22.47 C ANISOU 2817 CB ATHR A 279 3460 2536 2543 94 66 44 C ATOM 2818 CB BTHR A 279 -21.254 -4.144 7.363 0.44 22.46 C ANISOU 2818 CB BTHR A 279 3463 2533 2539 93 65 44 C ATOM 2819 OG1ATHR A 279 -21.474 -2.799 6.851 0.56 18.97 O ANISOU 2819 OG1ATHR A 279 3021 2112 2074 71 84 51 O ATOM 2820 OG1BTHR A 279 -20.040 -3.723 7.999 0.44 27.38 O ANISOU 2820 OG1BTHR A 279 4025 3164 3216 110 83 44 O ATOM 2821 CG2ATHR A 279 -21.119 -5.109 6.285 0.56 20.19 C ANISOU 2821 CG2ATHR A 279 3222 2217 2230 107 94 24 C ATOM 2822 CG2BTHR A 279 -21.748 -3.062 6.414 0.44 18.59 C ANISOU 2822 CG2BTHR A 279 2999 2057 2007 69 88 47 C ATOM 2823 N ASN A 280 -21.414 -5.759 10.308 1.00 20.26 N ANISOU 2823 N ASN A 280 3113 2253 2331 121 -36 65 N ATOM 2824 CA ASN A 280 -21.112 -7.001 11.010 1.00 24.78 C ANISOU 2824 CA ASN A 280 3666 2812 2938 142 -56 60 C ATOM 2825 C ASN A 280 -22.371 -7.809 11.290 1.00 23.24 C ANISOU 2825 C ASN A 280 3500 2611 2719 138 -107 75 C ATOM 2826 O ASN A 280 -22.312 -9.040 11.377 1.00 25.14 O ANISOU 2826 O ASN A 280 3745 2833 2974 153 -118 67 O ATOM 2827 CB ASN A 280 -20.376 -6.704 12.315 1.00 27.93 C ANISOU 2827 CB ASN A 280 3999 3224 3389 157 -69 67 C ATOM 2828 CG ASN A 280 -20.016 -7.966 13.074 1.00 35.30 C ANISOU 2828 CG ASN A 280 4907 4145 4360 178 -87 62 C ATOM 2829 OD1 ASN A 280 -19.149 -8.729 12.650 1.00 42.30 O ANISOU 2829 OD1 ASN A 280 5793 5012 5268 191 -53 41 O ATOM 2830 ND2 ASN A 280 -20.684 -8.194 14.198 1.00 30.34 N ANISOU 2830 ND2 ASN A 280 4258 3530 3740 183 -138 81 N ATOM 2831 N SER A 281 -23.515 -7.141 11.430 1.00 23.02 N ANISOU 2831 N SER A 281 3492 2599 2656 117 -139 99 N ATOM 2832 CA SER A 281 -24.780 -7.835 11.622 1.00 30.92 C ANISOU 2832 CA SER A 281 4523 3591 3633 113 -187 120 C ATOM 2833 C SER A 281 -25.276 -8.512 10.350 1.00 33.88 C ANISOU 2833 C SER A 281 4962 3938 3974 105 -177 108 C ATOM 2834 O SER A 281 -26.328 -9.158 10.379 1.00 30.64 O ANISOU 2834 O SER A 281 4581 3514 3545 102 -219 126 O ATOM 2835 CB SER A 281 -25.827 -6.852 12.153 1.00 25.39 C ANISOU 2835 CB SER A 281 3825 2915 2907 94 -222 154 C ATOM 2836 OG SER A 281 -25.457 -6.365 13.433 1.00 28.27 O ANISOU 2836 OG SER A 281 4133 3304 3304 107 -242 166 O ATOM 2837 N VAL A 282 -24.544 -8.382 9.244 1.00 34.03 N ANISOU 2837 N VAL A 282 5003 3946 3983 105 -125 80 N ATOM 2838 CA VAL A 282 -24.900 -9.031 7.995 1.00 29.89 C ANISOU 2838 CA VAL A 282 4540 3393 3424 104 -113 65 C ATOM 2839 C VAL A 282 -24.026 -10.249 7.706 1.00 29.83 C ANISOU 2839 C VAL A 282 4531 3361 3441 132 -94 38 C ATOM 2840 O VAL A 282 -24.500 -11.200 7.073 1.00 29.13 O ANISOU 2840 O VAL A 282 4488 3245 3334 138 -109 30 O ATOM 2841 CB VAL A 282 -24.836 -8.024 6.821 1.00 27.97 C ANISOU 2841 CB VAL A 282 4330 3154 3142 87 -67 53 C ATOM 2842 CG1 VAL A 282 -25.247 -8.676 5.507 1.00 29.54 C ANISOU 2842 CG1 VAL A 282 4598 3322 3303 88 -56 37 C ATOM 2843 CG2 VAL A 282 -25.702 -6.805 7.098 1.00 21.71 C ANISOU 2843 CG2 VAL A 282 3536 2386 2325 56 -85 79 C ATOM 2844 N VAL A 283 -22.780 -10.270 8.185 1.00 24.44 N ANISOU 2844 N VAL A 283 3799 2686 2802 149 -65 25 N ATOM 2845 CA VAL A 283 -21.801 -11.208 7.638 1.00 27.17 C ANISOU 2845 CA VAL A 283 4150 3009 3165 173 -30 -2 C ATOM 2846 C VAL A 283 -21.953 -12.622 8.198 1.00 32.13 C ANISOU 2846 C VAL A 283 4769 3621 3818 189 -68 -3 C ATOM 2847 O VAL A 283 -21.595 -13.590 7.518 1.00 35.98 O ANISOU 2847 O VAL A 283 5283 4084 4303 206 -54 -25 O ATOM 2848 CB VAL A 283 -20.373 -10.685 7.866 1.00 30.44 C ANISOU 2848 CB VAL A 283 4515 3434 3618 185 18 -12 C ATOM 2849 CG1 VAL A 283 -20.170 -9.371 7.137 1.00 30.00 C ANISOU 2849 CG1 VAL A 283 4467 3391 3539 173 59 -11 C ATOM 2850 CG2 VAL A 283 -20.090 -10.526 9.355 1.00 29.46 C ANISOU 2850 CG2 VAL A 283 4325 3329 3541 187 -9 3 C ATOM 2851 N ASN A 284 -22.464 -12.781 9.424 1.00 29.22 N ANISOU 2851 N ASN A 284 4363 3267 3474 187 -117 19 N ATOM 2852 CA ASN A 284 -22.504 -14.109 10.040 1.00 38.35 C ANISOU 2852 CA ASN A 284 5500 4411 4662 204 -151 19 C ATOM 2853 C ASN A 284 -23.324 -15.127 9.250 1.00 37.81 C ANISOU 2853 C ASN A 284 5487 4313 4567 207 -179 16 C ATOM 2854 O ASN A 284 -22.831 -16.251 9.046 1.00 33.06 O ANISOU 2854 O ASN A 284 4885 3691 3984 226 -175 -4 O ATOM 2855 CB ASN A 284 -22.999 -13.992 11.488 1.00 42.02 C ANISOU 2855 CB ASN A 284 5914 4898 5154 204 -199 49 C ATOM 2856 CG ASN A 284 -22.057 -13.179 12.364 1.00 47.21 C ANISOU 2856 CG ASN A 284 6512 5579 5846 207 -177 49 C ATOM 2857 OD1 ASN A 284 -21.149 -12.510 11.869 1.00 41.47 O ANISOU 2857 OD1 ASN A 284 5783 4854 5120 205 -127 33 O ATOM 2858 ND2 ASN A 284 -22.272 -13.235 13.673 1.00 53.69 N ANISOU 2858 ND2 ASN A 284 7285 6419 6697 215 -215 71 N ATOM 2859 N PRO A 285 -24.547 -14.831 8.785 1.00 35.95 N ANISOU 2859 N PRO A 285 5299 4070 4290 191 -209 34 N ATOM 2860 CA PRO A 285 -25.277 -15.840 7.997 1.00 37.48 C ANISOU 2860 CA PRO A 285 5548 4230 4463 197 -238 29 C ATOM 2861 C PRO A 285 -24.515 -16.327 6.777 1.00 45.23 C ANISOU 2861 C PRO A 285 6569 5187 5428 212 -194 -8 C ATOM 2862 O PRO A 285 -24.677 -17.487 6.380 1.00 44.93 O ANISOU 2862 O PRO A 285 6557 5121 5392 228 -217 -20 O ATOM 2863 CB PRO A 285 -26.566 -15.107 7.600 1.00 32.80 C ANISOU 2863 CB PRO A 285 5001 3636 3826 172 -264 55 C ATOM 2864 CG PRO A 285 -26.753 -14.097 8.666 1.00 34.81 C ANISOU 2864 CG PRO A 285 5209 3925 4090 158 -273 83 C ATOM 2865 CD PRO A 285 -25.373 -13.635 9.025 1.00 35.56 C ANISOU 2865 CD PRO A 285 5255 4041 4214 167 -223 61 C ATOM 2866 N PHE A 286 -23.673 -15.481 6.177 1.00 46.70 N ANISOU 2866 N PHE A 286 6760 5383 5600 210 -133 -27 N ATOM 2867 CA PHE A 286 -22.888 -15.914 5.025 1.00 46.64 C ANISOU 2867 CA PHE A 286 6790 5355 5578 230 -88 -59 C ATOM 2868 C PHE A 286 -21.744 -16.831 5.433 1.00 46.21 C ANISOU 2868 C PHE A 286 6695 5295 5567 254 -70 -77 C ATOM 2869 O PHE A 286 -21.391 -17.747 4.682 1.00 49.29 O ANISOU 2869 O PHE A 286 7118 5660 5950 275 -58 -100 O ATOM 2870 CB PHE A 286 -22.356 -14.699 4.268 1.00 50.06 C ANISOU 2870 CB PHE A 286 7235 5801 5984 223 -28 -68 C ATOM 2871 CG PHE A 286 -23.425 -13.914 3.578 1.00 53.60 C ANISOU 2871 CG PHE A 286 7734 6249 6383 201 -38 -57 C ATOM 2872 CD1 PHE A 286 -24.156 -12.959 4.264 1.00 54.31 C ANISOU 2872 CD1 PHE A 286 7803 6363 6470 173 -62 -29 C ATOM 2873 CD2 PHE A 286 -23.715 -14.146 2.246 1.00 55.96 C ANISOU 2873 CD2 PHE A 286 8102 6522 6637 209 -24 -74 C ATOM 2874 CE1 PHE A 286 -25.150 -12.244 3.631 1.00 52.00 C ANISOU 2874 CE1 PHE A 286 7556 6070 6132 149 -70 -18 C ATOM 2875 CE2 PHE A 286 -24.704 -13.434 1.609 1.00 56.56 C ANISOU 2875 CE2 PHE A 286 8225 6597 6670 187 -33 -64 C ATOM 2876 CZ PHE A 286 -25.426 -12.485 2.302 1.00 53.96 C ANISOU 2876 CZ PHE A 286 7873 6293 6339 155 -55 -36 C ATOM 2877 N ILE A 287 -21.158 -16.609 6.609 1.00 45.26 N ANISOU 2877 N ILE A 287 6505 5198 5492 251 -67 -67 N ATOM 2878 CA ILE A 287 -20.086 -17.485 7.069 1.00 47.32 C ANISOU 2878 CA ILE A 287 6725 5454 5799 271 -51 -82 C ATOM 2879 C ILE A 287 -20.630 -18.874 7.383 1.00 43.49 C ANISOU 2879 C ILE A 287 6242 4952 5330 281 -104 -82 C ATOM 2880 O ILE A 287 -19.986 -19.888 7.088 1.00 44.32 O ANISOU 2880 O ILE A 287 6350 5039 5450 300 -91 -103 O ATOM 2881 CB ILE A 287 -19.375 -16.865 8.283 1.00 46.28 C ANISOU 2881 CB ILE A 287 6520 5350 5713 265 -39 -70 C ATOM 2882 CG1 ILE A 287 -18.951 -15.427 7.976 1.00 43.11 C ANISOU 2882 CG1 ILE A 287 6117 4966 5298 254 5 -66 C ATOM 2883 CG2 ILE A 287 -18.171 -17.707 8.682 1.00 44.80 C ANISOU 2883 CG2 ILE A 287 6293 5157 5574 283 -14 -86 C ATOM 2884 CD1 ILE A 287 -17.992 -15.307 6.818 1.00 42.79 C ANISOU 2884 CD1 ILE A 287 6104 4911 5243 269 69 -87 C ATOM 2885 N TYR A 288 -21.823 -18.945 7.980 1.00 41.01 N ANISOU 2885 N TYR A 288 5924 4643 5015 269 -164 -56 N ATOM 2886 CA TYR A 288 -22.426 -20.242 8.271 1.00 43.18 C ANISOU 2886 CA TYR A 288 6197 4900 5308 280 -220 -51 C ATOM 2887 C TYR A 288 -22.756 -20.993 6.989 1.00 41.42 C ANISOU 2887 C TYR A 288 6045 4641 5051 292 -227 -70 C ATOM 2888 O TYR A 288 -22.588 -22.215 6.913 1.00 47.03 O ANISOU 2888 O TYR A 288 6756 5333 5782 310 -247 -84 O ATOM 2889 CB TYR A 288 -23.687 -20.063 9.115 1.00 42.40 C ANISOU 2889 CB TYR A 288 6084 4813 5215 268 -282 -12 C ATOM 2890 CG TYR A 288 -23.478 -19.285 10.390 1.00 41.51 C ANISOU 2890 CG TYR A 288 5905 4735 5130 260 -281 10 C ATOM 2891 CD1 TYR A 288 -22.324 -19.445 11.147 1.00 42.65 C ANISOU 2891 CD1 TYR A 288 5989 4895 5319 270 -253 -3 C ATOM 2892 CD2 TYR A 288 -24.436 -18.385 10.835 1.00 39.30 C ANISOU 2892 CD2 TYR A 288 5626 4472 4832 244 -310 43 C ATOM 2893 CE1 TYR A 288 -22.135 -18.729 12.317 1.00 43.26 C ANISOU 2893 CE1 TYR A 288 6010 5003 5424 266 -256 15 C ATOM 2894 CE2 TYR A 288 -24.255 -17.666 11.998 1.00 37.32 C ANISOU 2894 CE2 TYR A 288 5320 4254 4606 242 -312 62 C ATOM 2895 CZ TYR A 288 -23.106 -17.842 12.737 1.00 40.64 C ANISOU 2895 CZ TYR A 288 5682 4689 5072 254 -286 47 C ATOM 2896 OH TYR A 288 -22.932 -17.122 13.897 1.00 43.74 O ANISOU 2896 OH TYR A 288 6021 5110 5487 254 -292 65 O ATOM 2897 N ALA A 289 -23.227 -20.274 5.967 1.00 42.94 N ANISOU 2897 N ALA A 289 6299 4823 5192 283 -213 -73 N ATOM 2898 CA ALA A 289 -23.603 -20.920 4.715 1.00 47.93 C ANISOU 2898 CA ALA A 289 7004 5419 5787 297 -222 -92 C ATOM 2899 C ALA A 289 -22.379 -21.426 3.962 1.00 56.27 C ANISOU 2899 C ALA A 289 8075 6463 6842 322 -169 -128 C ATOM 2900 O ALA A 289 -22.423 -22.493 3.340 1.00 55.33 O ANISOU 2900 O ALA A 289 7993 6315 6716 343 -187 -146 O ATOM 2901 CB ALA A 289 -24.403 -19.950 3.847 1.00 39.90 C ANISOU 2901 CB ALA A 289 6047 4397 4715 280 -217 -84 C ATOM 2902 N TYR A 290 -21.276 -20.679 4.005 1.00 59.68 N ANISOU 2902 N TYR A 290 8479 6917 7281 322 -104 -137 N ATOM 2903 CA TYR A 290 -20.086 -21.049 3.253 1.00 62.19 C ANISOU 2903 CA TYR A 290 8812 7223 7595 348 -48 -166 C ATOM 2904 C TYR A 290 -19.179 -22.022 3.996 1.00 60.68 C ANISOU 2904 C TYR A 290 8567 7032 7455 361 -44 -175 C ATOM 2905 O TYR A 290 -18.318 -22.643 3.363 1.00 61.07 O ANISOU 2905 O TYR A 290 8635 7067 7503 385 -9 -198 O ATOM 2906 CB TYR A 290 -19.281 -19.798 2.880 1.00 69.63 C ANISOU 2906 CB TYR A 290 9748 8183 8523 345 22 -167 C ATOM 2907 CG TYR A 290 -19.785 -19.076 1.647 1.00 81.15 C ANISOU 2907 CG TYR A 290 11274 9634 9924 345 40 -171 C ATOM 2908 CD1 TYR A 290 -19.520 -19.568 0.374 1.00 84.97 C ANISOU 2908 CD1 TYR A 290 11820 10092 10371 374 66 -195 C ATOM 2909 CD2 TYR A 290 -20.512 -17.897 1.754 1.00 87.23 C ANISOU 2909 CD2 TYR A 290 12045 10423 10674 317 34 -152 C ATOM 2910 CE1 TYR A 290 -19.973 -18.911 -0.756 1.00 88.38 C ANISOU 2910 CE1 TYR A 290 12313 10517 10750 376 84 -200 C ATOM 2911 CE2 TYR A 290 -20.969 -17.232 0.630 1.00 90.19 C ANISOU 2911 CE2 TYR A 290 12480 10792 10998 315 53 -156 C ATOM 2912 CZ TYR A 290 -20.697 -17.744 -0.622 1.00 91.24 C ANISOU 2912 CZ TYR A 290 12673 10899 11097 345 78 -181 C ATOM 2913 OH TYR A 290 -21.150 -17.087 -1.744 1.00 93.14 O ANISOU 2913 OH TYR A 290 12971 11133 11285 346 98 -186 O ATOM 2914 N ARG A 291 -19.348 -22.182 5.312 1.00 56.58 N ANISOU 2914 N ARG A 291 7984 6532 6982 347 -78 -156 N ATOM 2915 CA ARG A 291 -18.434 -22.996 6.100 1.00 51.28 C ANISOU 2915 CA ARG A 291 7255 5866 6364 355 -70 -164 C ATOM 2916 C ARG A 291 -19.085 -24.144 6.860 1.00 46.76 C ANISOU 2916 C ARG A 291 6654 5288 5824 357 -137 -156 C ATOM 2917 O ARG A 291 -18.365 -25.053 7.286 1.00 47.24 O ANISOU 2917 O ARG A 291 6678 5348 5925 367 -132 -168 O ATOM 2918 CB ARG A 291 -17.669 -22.120 7.105 1.00 50.28 C ANISOU 2918 CB ARG A 291 7060 5768 6273 342 -37 -151 C ATOM 2919 CG ARG A 291 -16.740 -21.102 6.461 1.00 49.92 C ANISOU 2919 CG ARG A 291 7028 5728 6212 345 33 -157 C ATOM 2920 CD ARG A 291 -15.741 -20.565 7.470 1.00 50.72 C ANISOU 2920 CD ARG A 291 7058 5850 6362 337 64 -148 C ATOM 2921 NE ARG A 291 -14.990 -21.647 8.097 1.00 54.20 N ANISOU 2921 NE ARG A 291 7457 6286 6852 347 66 -158 N ATOM 2922 CZ ARG A 291 -13.848 -22.138 7.625 1.00 54.46 C ANISOU 2922 CZ ARG A 291 7491 6304 6895 363 115 -174 C ATOM 2923 NH1 ARG A 291 -13.319 -21.638 6.518 1.00 52.12 N ANISOU 2923 NH1 ARG A 291 7238 5997 6567 376 168 -182 N ATOM 2924 NH2 ARG A 291 -13.235 -23.128 8.262 1.00 56.07 N ANISOU 2924 NH2 ARG A 291 7654 6505 7144 367 114 -182 N ATOM 2925 N ILE A 292 -20.402 -24.138 7.046 1.00 43.31 N ANISOU 2925 N ILE A 292 6232 4848 5376 348 -198 -134 N ATOM 2926 CA ILE A 292 -21.098 -25.185 7.788 1.00 44.81 C ANISOU 2926 CA ILE A 292 6391 5034 5601 351 -265 -119 C ATOM 2927 C ILE A 292 -22.140 -25.805 6.870 1.00 44.30 C ANISOU 2927 C ILE A 292 6393 4934 5503 360 -315 -120 C ATOM 2928 O ILE A 292 -23.105 -25.137 6.480 1.00 37.95 O ANISOU 2928 O ILE A 292 5631 4125 4663 349 -336 -103 O ATOM 2929 CB ILE A 292 -21.747 -24.646 9.072 1.00 48.04 C ANISOU 2929 CB ILE A 292 6745 5472 6037 336 -301 -83 C ATOM 2930 CG1 ILE A 292 -20.722 -23.862 9.895 1.00 48.05 C ANISOU 2930 CG1 ILE A 292 6688 5504 6065 328 -252 -83 C ATOM 2931 CG2 ILE A 292 -22.327 -25.792 9.889 1.00 45.55 C ANISOU 2931 CG2 ILE A 292 6387 5153 5765 345 -366 -65 C ATOM 2932 CD1 ILE A 292 -21.288 -23.241 11.150 1.00 45.75 C ANISOU 2932 CD1 ILE A 292 6345 5242 5796 317 -283 -49 C ATOM 2933 N ARG A 293 -21.951 -27.087 6.541 1.00 50.35 N ANISOU 2933 N ARG A 293 7169 5678 6285 380 -336 -139 N ATOM 2934 CA ARG A 293 -22.842 -27.757 5.596 1.00 55.73 C ANISOU 2934 CA ARG A 293 7917 6321 6937 393 -384 -144 C ATOM 2935 C ARG A 293 -24.269 -27.834 6.124 1.00 47.03 C ANISOU 2935 C ARG A 293 6809 5213 5847 383 -461 -104 C ATOM 2936 O ARG A 293 -25.226 -27.593 5.378 1.00 45.50 O ANISOU 2936 O ARG A 293 6678 4995 5615 381 -491 -95 O ATOM 2937 CB ARG A 293 -22.326 -29.163 5.286 1.00 67.86 C ANISOU 2937 CB ARG A 293 9454 7834 8494 419 -397 -170 C ATOM 2938 CG ARG A 293 -20.924 -29.223 4.704 1.00 79.16 C ANISOU 2938 CG ARG A 293 10896 9266 9914 433 -323 -207 C ATOM 2939 CD ARG A 293 -20.607 -30.634 4.225 1.00 86.31 C ANISOU 2939 CD ARG A 293 11819 10145 10831 459 -344 -233 C ATOM 2940 NE ARG A 293 -19.202 -30.798 3.864 1.00 93.75 N ANISOU 2940 NE ARG A 293 12760 11091 11771 473 -274 -262 N ATOM 2941 CZ ARG A 293 -18.689 -31.913 3.354 1.00101.60 C ANISOU 2941 CZ ARG A 293 13772 12064 12769 498 -276 -288 C ATOM 2942 NH1 ARG A 293 -19.466 -32.965 3.139 1.00103.61 N ANISOU 2942 NH1 ARG A 293 14047 12291 13030 512 -347 -291 N ATOM 2943 NH2 ARG A 293 -17.398 -31.976 3.057 1.00105.05 N ANISOU 2943 NH2 ARG A 293 14207 12505 13203 510 -207 -309 N ATOM 2944 N GLU A 294 -24.435 -28.177 7.404 1.00 46.39 N ANISOU 2944 N GLU A 294 6653 5154 5819 380 -494 -78 N ATOM 2945 CA GLU A 294 -25.777 -28.364 7.949 1.00 46.56 C ANISOU 2945 CA GLU A 294 6664 5170 5857 376 -570 -35 C ATOM 2946 C GLU A 294 -26.591 -27.077 7.878 1.00 44.23 C ANISOU 2946 C GLU A 294 6399 4884 5524 354 -568 -7 C ATOM 2947 O GLU A 294 -27.808 -27.116 7.664 1.00 44.04 O ANISOU 2947 O GLU A 294 6409 4838 5487 351 -624 22 O ATOM 2948 CB GLU A 294 -25.697 -28.872 9.387 1.00 52.91 C ANISOU 2948 CB GLU A 294 7376 6002 6726 379 -597 -11 C ATOM 2949 CG GLU A 294 -26.992 -29.489 9.889 1.00 59.06 C ANISOU 2949 CG GLU A 294 8138 6768 7533 386 -682 33 C ATOM 2950 CD GLU A 294 -27.321 -30.795 9.193 1.00 62.78 C ANISOU 2950 CD GLU A 294 8629 7212 8012 398 -723 19 C ATOM 2951 OE1 GLU A 294 -26.379 -31.488 8.752 1.00 64.89 O ANISOU 2951 OE1 GLU A 294 8910 7458 8289 418 -705 -19 O ATOM 2952 OE2 GLU A 294 -28.520 -31.127 9.082 1.00 64.47 O ANISOU 2952 OE2 GLU A 294 8830 7447 8221 374 -755 39 O ATOM 2953 N PHE A 295 -25.938 -25.926 8.056 1.00 40.74 N ANISOU 2953 N PHE A 295 5944 4471 5063 339 -507 -14 N ATOM 2954 CA PHE A 295 -26.629 -24.655 7.860 1.00 38.35 C ANISOU 2954 CA PHE A 295 5674 4176 4720 317 -500 7 C ATOM 2955 C PHE A 295 -26.929 -24.422 6.386 1.00 38.70 C ANISOU 2955 C PHE A 295 5808 4189 4707 316 -487 -13 C ATOM 2956 O PHE A 295 -28.046 -24.035 6.022 1.00 38.13 O ANISOU 2956 O PHE A 295 5780 4101 4607 303 -521 11 O ATOM 2957 CB PHE A 295 -25.795 -23.502 8.421 1.00 37.30 C ANISOU 2957 CB PHE A 295 5502 4084 4588 304 -440 3 C ATOM 2958 CG PHE A 295 -26.129 -23.141 9.839 1.00 37.85 C ANISOU 2958 CG PHE A 295 5504 4186 4692 297 -466 40 C ATOM 2959 CD1 PHE A 295 -27.323 -22.506 10.143 1.00 33.39 C ANISOU 2959 CD1 PHE A 295 4951 3626 4110 283 -505 82 C ATOM 2960 CD2 PHE A 295 -25.244 -23.421 10.868 1.00 38.49 C ANISOU 2960 CD2 PHE A 295 5511 4292 4821 306 -450 35 C ATOM 2961 CE1 PHE A 295 -27.632 -22.166 11.448 1.00 31.73 C ANISOU 2961 CE1 PHE A 295 4681 3447 3929 283 -528 118 C ATOM 2962 CE2 PHE A 295 -25.547 -23.082 12.175 1.00 36.65 C ANISOU 2962 CE2 PHE A 295 5219 4090 4619 305 -474 69 C ATOM 2963 CZ PHE A 295 -26.742 -22.453 12.465 1.00 31.11 C ANISOU 2963 CZ PHE A 295 4530 3394 3898 295 -514 110 C ATOM 2964 N ARG A 296 -25.932 -24.614 5.548 1.00 39.93 N ANISOU 2964 N ARG A 296 5990 4335 4846 329 -436 -55 N ATOM 2965 CA ARG A 296 -26.094 -24.415 4.133 1.00 40.89 C ANISOU 2965 CA ARG A 296 6195 4428 4913 333 -419 -77 C ATOM 2966 C ARG A 296 -27.259 -25.223 3.558 1.00 42.13 C ANISOU 2966 C ARG A 296 6406 4541 5059 342 -490 -66 C ATOM 2967 O ARG A 296 -28.078 -24.690 2.839 1.00 42.14 O ANISOU 2967 O ARG A 296 6467 4525 5020 331 -501 -57 O ATOM 2968 CB ARG A 296 -24.799 -24.715 3.409 1.00 45.30 C ANISOU 2968 CB ARG A 296 6769 4982 5462 355 -358 -121 C ATOM 2969 CG ARG A 296 -24.839 -24.327 1.955 1.00 52.31 C ANISOU 2969 CG ARG A 296 7739 5847 6290 363 -328 -143 C ATOM 2970 CD ARG A 296 -23.714 -24.961 1.181 1.00 59.45 C ANISOU 2970 CD ARG A 296 8665 6737 7186 395 -283 -183 C ATOM 2971 NE ARG A 296 -22.429 -24.797 1.829 1.00 63.70 N ANISOU 2971 NE ARG A 296 9141 7306 7757 396 -227 -191 N ATOM 2972 CZ ARG A 296 -21.728 -25.796 2.319 1.00 64.80 C ANISOU 2972 CZ ARG A 296 9240 7445 7937 411 -230 -203 C ATOM 2973 NH1 ARG A 296 -20.571 -25.588 2.895 1.00 66.67 N ANISOU 2973 NH1 ARG A 296 9421 7707 8204 410 -178 -208 N ATOM 2974 NH2 ARG A 296 -22.198 -27.005 2.229 1.00 66.94 N ANISOU 2974 NH2 ARG A 296 9524 7689 8221 426 -288 -208 N ATOM 2975 N GLN A 297 -27.325 -26.502 3.897 1.00 43.65 N ANISOU 2975 N GLN A 297 6575 4716 5292 361 -538 -66 N ATOM 2976 CA GLN A 297 -28.396 -27.362 3.417 1.00 48.15 C ANISOU 2976 CA GLN A 297 7191 5243 5862 372 -613 -53 C ATOM 2977 C GLN A 297 -29.751 -26.928 3.922 1.00 46.97 C ANISOU 2977 C GLN A 297 7016 5115 5714 342 -657 -6 C ATOM 2978 O GLN A 297 -30.724 -26.952 3.206 1.00 49.42 O ANISOU 2978 O GLN A 297 7357 5426 5996 325 -680 -2 O ATOM 2979 CB GLN A 297 -28.133 -28.811 3.782 1.00 53.05 C ANISOU 2979 CB GLN A 297 7775 5848 6531 397 -655 -61 C ATOM 2980 CG GLN A 297 -26.837 -29.351 3.215 1.00 60.71 C ANISOU 2980 CG GLN A 297 8753 6817 7496 419 -604 -111 C ATOM 2981 CD GLN A 297 -26.602 -30.796 3.582 1.00 70.86 C ANISOU 2981 CD GLN A 297 10002 8090 8832 442 -647 -119 C ATOM 2982 OE1 GLN A 297 -27.049 -31.256 4.618 1.00 72.77 O ANISOU 2982 OE1 GLN A 297 10182 8343 9125 438 -696 -88 O ATOM 2983 NE2 GLN A 297 -25.899 -31.522 2.723 1.00 74.72 N ANISOU 2983 NE2 GLN A 297 10528 8557 9306 467 -630 -160 N ATOM 2984 N THR A 298 -29.807 -26.546 5.177 1.00 45.43 N ANISOU 2984 N THR A 298 6750 4959 5554 327 -658 24 N ATOM 2985 CA THR A 298 -31.042 -26.077 5.761 1.00 43.12 C ANISOU 2985 CA THR A 298 6407 4713 5266 289 -677 60 C ATOM 2986 C THR A 298 -31.490 -24.787 5.119 1.00 40.35 C ANISOU 2986 C THR A 298 6108 4363 4861 265 -649 63 C ATOM 2987 O THR A 298 -32.650 -24.581 4.920 1.00 39.00 O ANISOU 2987 O THR A 298 5929 4211 4679 236 -663 75 O ATOM 2988 CB THR A 298 -30.953 -25.967 7.268 1.00 40.33 C ANISOU 2988 CB THR A 298 5959 4405 4960 282 -676 86 C ATOM 2989 OG1 THR A 298 -30.330 -27.138 7.768 1.00 37.85 O ANISOU 2989 OG1 THR A 298 5603 4085 4694 307 -695 78 O ATOM 2990 CG2 THR A 298 -32.319 -25.858 7.849 1.00 40.01 C ANISOU 2990 CG2 THR A 298 5857 4409 4936 246 -688 114 C ATOM 2991 N PHE A 299 -30.548 -23.909 4.810 1.00 43.89 N ANISOU 2991 N PHE A 299 6606 4790 5279 277 -602 50 N ATOM 2992 CA PHE A 299 -30.887 -22.675 4.130 1.00 44.91 C ANISOU 2992 CA PHE A 299 6788 4921 5356 254 -571 51 C ATOM 2993 C PHE A 299 -31.480 -23.000 2.760 1.00 44.10 C ANISOU 2993 C PHE A 299 6753 4791 5213 253 -582 31 C ATOM 2994 O PHE A 299 -32.464 -22.417 2.373 1.00 44.64 O ANISOU 2994 O PHE A 299 6831 4876 5253 223 -586 41 O ATOM 2995 CB PHE A 299 -29.681 -21.747 3.946 1.00 44.86 C ANISOU 2995 CB PHE A 299 6788 4928 5329 256 -495 25 C ATOM 2996 CG PHE A 299 -29.148 -21.144 5.217 1.00 43.73 C ANISOU 2996 CG PHE A 299 6566 4833 5218 247 -473 40 C ATOM 2997 CD1 PHE A 299 -29.905 -21.086 6.346 1.00 40.51 C ANISOU 2997 CD1 PHE A 299 6114 4439 4838 238 -520 85 C ATOM 2998 CD2 PHE A 299 -27.861 -20.674 5.270 1.00 43.78 C ANISOU 2998 CD2 PHE A 299 6541 4865 5227 250 -406 10 C ATOM 2999 CE1 PHE A 299 -29.407 -20.545 7.499 1.00 42.75 C ANISOU 2999 CE1 PHE A 299 6328 4766 5150 234 -501 97 C ATOM 3000 CE2 PHE A 299 -27.354 -20.132 6.417 1.00 42.32 C ANISOU 3000 CE2 PHE A 299 6287 4720 5074 243 -388 23 C ATOM 3001 CZ PHE A 299 -28.126 -20.074 7.537 1.00 42.08 C ANISOU 3001 CZ PHE A 299 6214 4704 5068 236 -437 65 C ATOM 3002 N ARG A 300 -30.910 -23.960 2.042 1.00 49.50 N ANISOU 3002 N ARG A 300 7477 5435 5895 286 -587 0 N ATOM 3003 CA ARG A 300 -31.439 -24.294 0.725 1.00 54.83 C ANISOU 3003 CA ARG A 300 8216 6087 6529 289 -599 -19 C ATOM 3004 C ARG A 300 -32.877 -24.775 0.796 1.00 52.02 C ANISOU 3004 C ARG A 300 7825 5754 6185 262 -656 1 C ATOM 3005 O ARG A 300 -33.699 -24.375 0.010 1.00 52.18 O ANISOU 3005 O ARG A 300 7882 5776 6170 243 -660 0 O ATOM 3006 CB ARG A 300 -30.579 -25.350 0.037 1.00 59.86 C ANISOU 3006 CB ARG A 300 8890 6687 7168 331 -596 -58 C ATOM 3007 CG ARG A 300 -29.198 -24.873 -0.348 1.00 64.99 C ANISOU 3007 CG ARG A 300 9571 7324 7800 354 -520 -98 C ATOM 3008 CD ARG A 300 -28.494 -25.843 -1.277 1.00 70.79 C ANISOU 3008 CD ARG A 300 10346 8028 8522 393 -511 -142 C ATOM 3009 NE ARG A 300 -27.210 -25.319 -1.727 1.00 77.19 N ANISOU 3009 NE ARG A 300 11155 8864 9310 404 -424 -175 N ATOM 3010 CZ ARG A 300 -26.027 -25.795 -1.348 1.00 77.82 C ANISOU 3010 CZ ARG A 300 11188 8962 9417 421 -388 -195 C ATOM 3011 NH1 ARG A 300 -24.919 -25.251 -1.819 1.00 77.97 N ANISOU 3011 NH1 ARG A 300 11210 9000 9415 432 -309 -219 N ATOM 3012 NH2 ARG A 300 -25.949 -26.818 -0.505 1.00 74.42 N ANISOU 3012 NH2 ARG A 300 10708 8531 9039 428 -430 -188 N ATOM 3013 N LYS A 301 -33.176 -25.613 1.769 1.00 52.61 N ANISOU 3013 N LYS A 301 7824 5849 6316 260 -694 17 N ATOM 3014 CA LYS A 301 -34.515 -26.132 1.940 1.00 55.44 C ANISOU 3014 CA LYS A 301 8136 6228 6700 233 -735 32 C ATOM 3015 C LYS A 301 -35.535 -25.085 2.296 1.00 55.59 C ANISOU 3015 C LYS A 301 8122 6283 6717 190 -719 53 C ATOM 3016 O LYS A 301 -36.636 -25.119 1.820 1.00 56.77 O ANISOU 3016 O LYS A 301 8273 6435 6861 168 -734 53 O ATOM 3017 CB LYS A 301 -34.515 -27.257 2.965 1.00 63.39 C ANISOU 3017 CB LYS A 301 9062 7251 7772 240 -766 43 C ATOM 3018 CG LYS A 301 -33.663 -28.427 2.529 1.00 70.26 C ANISOU 3018 CG LYS A 301 9959 8086 8649 280 -788 19 C ATOM 3019 CD LYS A 301 -33.877 -29.643 3.397 1.00 75.50 C ANISOU 3019 CD LYS A 301 10544 8767 9377 282 -823 29 C ATOM 3020 CE LYS A 301 -32.938 -30.755 2.978 1.00 78.59 C ANISOU 3020 CE LYS A 301 10959 9124 9776 321 -842 1 C ATOM 3021 NZ LYS A 301 -32.749 -31.734 4.079 1.00 80.16 N ANISOU 3021 NZ LYS A 301 11071 9345 10040 325 -862 12 N ATOM 3022 N ILE A 302 -35.176 -24.172 3.176 1.00 54.66 N ANISOU 3022 N ILE A 302 7968 6193 6607 180 -686 70 N ATOM 3023 CA ILE A 302 -36.078 -23.116 3.551 1.00 54.29 C ANISOU 3023 CA ILE A 302 7885 6182 6560 142 -665 88 C ATOM 3024 C ILE A 302 -36.380 -22.221 2.361 1.00 58.44 C ANISOU 3024 C ILE A 302 8484 6692 7028 127 -645 72 C ATOM 3025 O ILE A 302 -37.505 -21.827 2.145 1.00 58.09 O ANISOU 3025 O ILE A 302 8425 6663 6984 97 -645 75 O ATOM 3026 CB ILE A 302 -35.468 -22.236 4.660 1.00 49.52 C ANISOU 3026 CB ILE A 302 7235 5610 5969 139 -633 106 C ATOM 3027 CG1 ILE A 302 -35.283 -23.039 5.939 1.00 47.91 C ANISOU 3027 CG1 ILE A 302 6950 5431 5825 151 -648 124 C ATOM 3028 CG2 ILE A 302 -36.345 -21.035 4.908 1.00 45.40 C ANISOU 3028 CG2 ILE A 302 6684 5123 5442 102 -606 120 C ATOM 3029 CD1 ILE A 302 -34.365 -22.406 6.941 1.00 42.66 C ANISOU 3029 CD1 ILE A 302 6251 4788 5171 160 -623 137 C ATOM 3030 N ILE A 303 -35.349 -21.873 1.614 1.00 64.94 N ANISOU 3030 N ILE A 303 9385 7486 7805 149 -621 53 N ATOM 3031 CA ILE A 303 -35.506 -21.025 0.445 1.00 70.07 C ANISOU 3031 CA ILE A 303 10108 8121 8395 137 -595 37 C ATOM 3032 C ILE A 303 -36.311 -21.707 -0.663 1.00 75.05 C ANISOU 3032 C ILE A 303 10780 8729 9006 138 -627 20 C ATOM 3033 O ILE A 303 -37.157 -21.087 -1.291 1.00 73.48 O ANISOU 3033 O ILE A 303 10601 8537 8783 111 -620 15 O ATOM 3034 CB ILE A 303 -34.150 -20.555 -0.086 1.00 66.65 C ANISOU 3034 CB ILE A 303 9743 7660 7920 166 -550 23 C ATOM 3035 CG1 ILE A 303 -33.445 -19.700 0.958 1.00 62.72 C ANISOU 3035 CG1 ILE A 303 9205 7186 7439 160 -516 40 C ATOM 3036 CG2 ILE A 303 -34.319 -19.757 -1.363 1.00 66.21 C ANISOU 3036 CG2 ILE A 303 9763 7591 7803 157 -518 6 C ATOM 3037 CD1 ILE A 303 -31.952 -19.670 0.774 1.00 61.11 C ANISOU 3037 CD1 ILE A 303 9044 6947 7226 197 -474 23 C ATOM 3038 N ARG A 304 -36.049 -22.987 -0.892 1.00 79.60 N ANISOU 3038 N ARG A 304 11368 9281 9595 169 -662 11 N ATOM 3039 CA ARG A 304 -36.776 -23.713 -1.915 1.00 83.32 C ANISOU 3039 CA ARG A 304 11878 9732 10049 172 -698 -4 C ATOM 3040 C ARG A 304 -38.219 -23.780 -1.515 1.00 85.04 C ANISOU 3040 C ARG A 304 12032 9975 10305 134 -723 10 C ATOM 3041 O ARG A 304 -39.087 -23.253 -2.176 1.00 84.54 O ANISOU 3041 O ARG A 304 11988 9915 10218 109 -719 4 O ATOM 3042 CB ARG A 304 -36.234 -25.126 -2.093 1.00 85.29 C ANISOU 3042 CB ARG A 304 12138 9954 10315 212 -734 -17 C ATOM 3043 CG ARG A 304 -34.955 -25.183 -2.898 1.00 88.79 C ANISOU 3043 CG ARG A 304 12656 10364 10718 255 -704 -39 C ATOM 3044 CD ARG A 304 -34.554 -26.598 -3.273 1.00 90.78 C ANISOU 3044 CD ARG A 304 12921 10588 10985 294 -739 -57 C ATOM 3045 NE ARG A 304 -34.297 -27.446 -2.124 1.00 94.21 N ANISOU 3045 NE ARG A 304 13281 11031 11482 300 -766 -48 N ATOM 3046 CZ ARG A 304 -35.184 -28.291 -1.613 1.00 96.38 C ANISOU 3046 CZ ARG A 304 13497 11320 11802 283 -817 -36 C ATOM 3047 NH1 ARG A 304 -34.873 -29.038 -0.575 1.00 94.38 N ANISOU 3047 NH1 ARG A 304 13175 11078 11606 290 -834 -27 N ATOM 3048 NH2 ARG A 304 -36.384 -28.396 -2.156 1.00 98.23 N ANISOU 3048 NH2 ARG A 304 13738 11557 12028 260 -846 -34 N ATOM 3049 N SER A 305 -38.467 -24.413 -0.391 1.00 88.25 N ANISOU 3049 N SER A 305 12356 10402 10773 129 -742 29 N ATOM 3050 CA SER A 305 -39.832 -24.576 0.095 1.00 91.91 C ANISOU 3050 CA SER A 305 12750 10891 11282 97 -756 46 C ATOM 3051 C SER A 305 -40.456 -23.227 0.435 1.00 92.73 C ANISOU 3051 C SER A 305 12824 11028 11383 62 -716 59 C ATOM 3052 O SER A 305 -40.619 -22.886 1.607 1.00 94.84 O ANISOU 3052 O SER A 305 13015 11330 11688 51 -697 83 O ATOM 3053 CB SER A 305 -39.860 -25.494 1.320 1.00 95.54 C ANISOU 3053 CB SER A 305 13125 11371 11807 104 -772 67 C ATOM 3054 OG SER A 305 -39.334 -26.773 1.012 1.00 98.19 O ANISOU 3054 OG SER A 305 13480 11676 12150 134 -810 53 O TER 3055 SER A 305 HETATM 3056 NA NA A2400 -23.617 -8.562 16.523 1.00 48.60 NA HETATM 3057 N1 ACFF A2401 -21.085 4.674 18.403 0.55 20.85 N HETATM 3058 N1 BCFF A2401 -21.414 4.596 18.273 0.45 20.70 N HETATM 3059 C2 ACFF A2401 -19.998 5.581 18.516 0.55 21.13 C HETATM 3060 C2 BCFF A2401 -22.617 4.782 17.541 0.45 21.10 C HETATM 3061 C10ACFF A2401 -20.999 3.383 19.000 0.55 17.12 C HETATM 3062 C10BCFF A2401 -21.183 3.374 18.967 0.45 17.26 C HETATM 3063 C6 ACFF A2401 -22.240 5.048 17.705 0.55 20.74 C HETATM 3064 C6 BCFF A2401 -20.454 5.613 18.313 0.45 20.97 C HETATM 3065 N3 ACFF A2401 -20.083 6.883 17.917 0.55 20.50 N HETATM 3066 N3 BCFF A2401 -22.852 6.015 16.842 0.45 22.36 N HETATM 3067 O11ACFF A2401 -18.996 5.259 19.121 0.55 19.79 O HETATM 3068 O11BCFF A2401 -23.450 3.899 17.507 0.45 22.99 O HETATM 3069 C12ACFF A2401 -18.989 7.788 18.034 0.55 19.76 C HETATM 3070 C12BCFF A2401 -24.058 6.204 16.108 0.45 22.92 C HETATM 3071 C4 ACFF A2401 -21.283 7.279 17.191 0.55 22.40 C HETATM 3072 C4 BCFF A2401 -21.858 7.078 16.881 0.45 22.39 C HETATM 3073 C5 ACFF A2401 -22.331 6.418 17.075 0.55 22.20 C HETATM 3074 C5 BCFF A2401 -20.702 6.909 17.578 0.45 21.26 C HETATM 3075 N9 ACFF A2401 -21.609 8.439 16.541 0.55 22.77 N HETATM 3076 N9 BCFF A2401 -21.840 8.321 16.312 0.45 22.71 N HETATM 3077 O13ACFF A2401 -23.163 4.263 17.615 0.55 22.49 O HETATM 3078 O13BCFF A2401 -19.428 5.442 18.943 0.45 20.82 O HETATM 3079 N7 ACFF A2401 -23.310 7.052 16.349 0.55 22.34 N HETATM 3080 N7 BCFF A2401 -19.965 8.057 17.439 0.45 22.22 N HETATM 3081 C8 ACFF A2401 -22.857 8.294 16.027 0.55 23.24 C HETATM 3082 C8 BCFF A2401 -20.671 8.920 16.658 0.45 23.81 C HETATM 3083 C14ACFF A2401 -24.583 6.526 15.984 0.55 21.81 C HETATM 3084 C14BCFF A2401 -18.685 8.320 18.002 0.45 18.02 C HETATM 3085 C1 CLR A2402 -38.180 9.224 31.032 1.00 97.83 C HETATM 3086 C2 CLR A2402 -37.980 10.757 30.993 1.00 97.03 C HETATM 3087 C3 CLR A2402 -36.644 11.161 30.421 1.00 95.45 C HETATM 3088 C4 CLR A2402 -36.381 10.480 29.066 1.00 95.25 C HETATM 3089 C5 CLR A2402 -36.613 8.992 29.125 1.00 96.16 C HETATM 3090 C6 CLR A2402 -35.648 8.169 28.673 1.00 95.23 C HETATM 3091 C7 CLR A2402 -35.824 6.681 28.426 1.00 94.54 C HETATM 3092 C8 CLR A2402 -37.261 6.246 28.682 1.00 95.41 C HETATM 3093 C9 CLR A2402 -37.836 6.976 29.905 1.00 96.81 C HETATM 3094 C10 CLR A2402 -37.921 8.498 29.704 1.00 97.50 C HETATM 3095 C11 CLR A2402 -39.153 6.334 30.351 1.00 97.10 C HETATM 3096 C12 CLR A2402 -39.133 4.799 30.411 1.00 97.99 C HETATM 3097 C13 CLR A2402 -38.632 4.129 29.161 1.00 98.35 C HETATM 3098 C14 CLR A2402 -37.264 4.750 28.917 1.00 96.34 C HETATM 3099 C15 CLR A2402 -36.639 3.892 27.821 1.00 96.04 C HETATM 3100 C16 CLR A2402 -37.253 2.515 28.057 1.00 96.38 C HETATM 3101 C17 CLR A2402 -38.280 2.632 29.183 1.00 98.48 C HETATM 3102 C18 CLR A2402 -39.641 4.369 28.002 1.00 99.31 C HETATM 3103 C19 CLR A2402 -39.050 8.865 28.699 1.00 97.21 C HETATM 3104 C20 CLR A2402 -39.389 1.576 29.045 1.00 98.19 C HETATM 3105 C21 CLR A2402 -39.982 1.200 30.405 1.00 98.07 C HETATM 3106 C22 CLR A2402 -38.881 0.309 28.313 1.00 97.25 C HETATM 3107 C23 CLR A2402 -39.351 -1.042 28.877 1.00 96.14 C HETATM 3108 C24 CLR A2402 -40.267 -1.758 27.880 1.00 94.49 C HETATM 3109 C25 CLR A2402 -41.003 -2.976 28.460 1.00 94.22 C HETATM 3110 C26 CLR A2402 -40.195 -4.260 28.287 1.00 94.31 C HETATM 3111 C27 CLR A2402 -41.368 -2.794 29.932 1.00 93.93 C HETATM 3112 O1 CLR A2402 -36.599 12.584 30.223 1.00 94.20 O HETATM 3113 C1 CLR A2403 -38.208 10.768 21.755 1.00 24.83 C HETATM 3114 C2 CLR A2403 -37.983 12.230 22.079 1.00 29.09 C HETATM 3115 C3 CLR A2403 -38.208 12.565 23.546 1.00 29.87 C HETATM 3116 C4 CLR A2403 -37.319 11.714 24.415 1.00 26.81 C HETATM 3117 C5 CLR A2403 -37.517 10.274 24.085 1.00 28.74 C HETATM 3118 C6 CLR A2403 -37.706 9.461 25.106 1.00 28.74 C HETATM 3119 C7 CLR A2403 -38.094 8.026 24.971 1.00 28.94 C HETATM 3120 C8 CLR A2403 -37.720 7.469 23.617 1.00 28.69 C HETATM 3121 C9 CLR A2403 -38.131 8.432 22.522 1.00 27.42 C HETATM 3122 C10 CLR A2403 -37.465 9.797 22.661 1.00 28.57 C HETATM 3123 C11 CLR A2403 -37.972 7.795 21.148 1.00 27.32 C HETATM 3124 C12 CLR A2403 -38.722 6.475 21.018 1.00 25.45 C HETATM 3125 C13 CLR A2403 -38.217 5.526 22.068 1.00 23.99 C HETATM 3126 C14 CLR A2403 -38.447 6.156 23.418 1.00 25.65 C HETATM 3127 C15 CLR A2403 -38.164 5.049 24.407 1.00 31.27 C HETATM 3128 C16 CLR A2403 -38.711 3.828 23.701 1.00 27.56 C HETATM 3129 C17 CLR A2403 -38.963 4.227 22.251 1.00 27.33 C HETATM 3130 C18 CLR A2403 -36.745 5.248 21.845 1.00 19.78 C HETATM 3131 C19 CLR A2403 -35.998 9.712 22.296 1.00 30.95 C HETATM 3132 C20 CLR A2403 -38.661 3.074 21.313 1.00 27.53 C HETATM 3133 C21 CLR A2403 -38.796 3.439 19.854 1.00 28.26 C HETATM 3134 C22 CLR A2403 -39.578 1.930 21.677 1.00 32.48 C HETATM 3135 C23 CLR A2403 -39.406 0.673 20.860 1.00 37.85 C HETATM 3136 C24 CLR A2403 -40.343 -0.388 21.393 1.00 45.33 C HETATM 3137 C25 CLR A2403 -40.093 -1.750 20.773 1.00 54.68 C HETATM 3138 C26 CLR A2403 -40.787 -2.819 21.587 1.00 57.58 C HETATM 3139 C27 CLR A2403 -40.569 -1.828 19.330 1.00 55.58 C HETATM 3140 O1 CLR A2403 -37.885 13.916 23.779 1.00 32.56 O HETATM 3141 C1 CLR A2404 -8.326 10.916 13.240 1.00 28.09 C HETATM 3142 C2 CLR A2404 -8.316 12.455 13.341 1.00 29.64 C HETATM 3143 C3 CLR A2404 -6.954 13.040 13.080 1.00 34.98 C HETATM 3144 C4 CLR A2404 -6.372 12.542 11.743 1.00 31.00 C HETATM 3145 C5 CLR A2404 -6.441 11.040 11.609 1.00 31.17 C HETATM 3146 C6 CLR A2404 -5.342 10.371 11.204 1.00 28.41 C HETATM 3147 C7 CLR A2404 -5.292 8.877 10.915 1.00 30.28 C HETATM 3148 C8 CLR A2404 -6.680 8.244 10.942 1.00 28.82 C HETATM 3149 C9 CLR A2404 -7.518 8.845 12.078 1.00 24.77 C HETATM 3150 C10 CLR A2404 -7.752 10.353 11.935 1.00 31.42 C HETATM 3151 C11 CLR A2404 -8.817 8.064 12.262 1.00 23.01 C HETATM 3152 C12 CLR A2404 -8.620 6.545 12.327 1.00 24.82 C HETATM 3153 C13 CLR A2404 -7.848 5.963 11.176 1.00 29.38 C HETATM 3154 C14 CLR A2404 -6.542 6.746 11.144 1.00 33.77 C HETATM 3155 C15 CLR A2404 -5.686 5.986 10.134 1.00 34.88 C HETATM 3156 C16 CLR A2404 -6.104 4.534 10.351 1.00 31.85 C HETATM 3157 C17 CLR A2404 -7.328 4.515 11.268 1.00 31.57 C HETATM 3158 C18 CLR A2404 -8.673 6.116 9.868 1.00 28.80 C HETATM 3159 C19 CLR A2404 -8.744 10.646 10.773 1.00 30.78 C HETATM 3160 C20 CLR A2404 -8.244 3.323 10.939 1.00 32.71 C HETATM 3161 C21 CLR A2404 -9.400 3.179 11.928 1.00 32.15 C HETATM 3162 C22 CLR A2404 -7.453 1.996 10.925 1.00 32.43 C HETATM 3163 C23 CLR A2404 -8.317 0.729 11.017 1.00 33.94 C HETATM 3164 C24 CLR A2404 -7.434 -0.517 11.125 1.00 41.71 C HETATM 3165 C25 CLR A2404 -8.210 -1.842 11.066 1.00 44.85 C HETATM 3166 C26 CLR A2404 -8.933 -2.117 12.382 1.00 38.65 C HETATM 3167 C27 CLR A2404 -9.210 -1.873 9.912 1.00 49.32 C HETATM 3168 O1 CLR A2404 -7.044 14.474 13.039 1.00 37.04 O HETATM 3169 C1 CLR A2405 -3.116 8.324 21.134 1.00 24.82 C HETATM 3170 C2 CLR A2405 -2.840 9.842 21.083 1.00 22.56 C HETATM 3171 C3 CLR A2405 -1.858 10.205 20.005 1.00 22.54 C HETATM 3172 C4 CLR A2405 -2.272 9.628 18.636 1.00 23.56 C HETATM 3173 C5 CLR A2405 -2.594 8.153 18.705 1.00 23.73 C HETATM 3174 C6 CLR A2405 -2.042 7.319 17.798 1.00 24.32 C HETATM 3175 C7 CLR A2405 -2.322 5.826 17.709 1.00 26.83 C HETATM 3176 C8 CLR A2405 -3.509 5.424 18.580 1.00 27.12 C HETATM 3177 C9 CLR A2405 -3.476 6.161 19.925 1.00 24.88 C HETATM 3178 C10 CLR A2405 -3.529 7.690 19.800 1.00 24.91 C HETATM 3179 C11 CLR A2405 -4.550 5.609 20.865 1.00 23.55 C HETATM 3180 C12 CLR A2405 -4.596 4.079 20.944 1.00 23.86 C HETATM 3181 C13 CLR A2405 -4.648 3.374 19.613 1.00 31.93 C HETATM 3182 C14 CLR A2405 -3.463 3.931 18.835 1.00 24.92 C HETATM 3183 C15 CLR A2405 -3.360 3.031 17.606 1.00 25.95 C HETATM 3184 C16 CLR A2405 -3.891 1.689 18.102 1.00 26.47 C HETATM 3185 C17 CLR A2405 -4.379 1.860 19.538 1.00 32.86 C HETATM 3186 C18 CLR A2405 -6.015 3.656 18.922 1.00 29.02 C HETATM 3187 C19 CLR A2405 -4.962 8.172 19.434 1.00 26.11 C HETATM 3188 C20 CLR A2405 -5.490 0.842 19.846 1.00 37.30 C HETATM 3189 C21 CLR A2405 -5.949 0.869 21.304 1.00 34.82 C HETATM 3190 C22 CLR A2405 -5.029 -0.592 19.501 1.00 41.13 C HETATM 3191 C23 CLR A2405 -6.063 -1.684 19.810 1.00 47.15 C HETATM 3192 C24 CLR A2405 -5.372 -2.948 20.328 1.00 52.37 C HETATM 3193 C25 CLR A2405 -5.016 -3.957 19.228 1.00 53.83 C HETATM 3194 C26 CLR A2405 -4.688 -5.326 19.820 1.00 54.92 C HETATM 3195 C27 CLR A2405 -6.130 -4.089 18.192 1.00 54.79 C HETATM 3196 O1 CLR A2405 -1.778 11.635 19.906 1.00 25.01 O HETATM 3197 C1 OLA A2406 -20.213 -22.298 28.167 1.00 60.90 C HETATM 3198 O1 OLA A2406 -20.626 -21.972 27.021 1.00 60.24 O HETATM 3199 O2 OLA A2406 -20.230 -23.504 28.466 1.00 67.43 O HETATM 3200 C2 OLA A2406 -19.710 -21.272 29.162 1.00 54.52 C HETATM 3201 C3 OLA A2406 -20.269 -19.876 28.879 1.00 50.33 C HETATM 3202 C4 OLA A2406 -19.378 -18.752 29.394 1.00 42.81 C HETATM 3203 C5 OLA A2406 -20.005 -17.378 29.261 1.00 43.27 C HETATM 3204 C6 OLA A2406 -19.048 -16.272 28.837 1.00 40.76 C HETATM 3205 C7 OLA A2406 -19.685 -14.893 28.986 1.00 42.24 C HETATM 3206 C1 OLA A2407 -20.900 12.937 3.674 1.00 76.12 C HETATM 3207 O1 OLA A2407 -20.249 13.452 2.749 1.00 80.34 O HETATM 3208 O2 OLA A2407 -21.152 13.652 4.684 1.00 75.36 O HETATM 3209 C2 OLA A2407 -21.365 11.497 3.573 1.00 71.11 C HETATM 3210 C3 OLA A2407 -20.906 10.842 2.267 1.00 67.42 C HETATM 3211 C4 OLA A2407 -21.318 9.380 2.141 1.00 63.48 C HETATM 3212 C5 OLA A2407 -21.364 8.643 3.465 1.00 58.03 C HETATM 3213 C6 OLA A2407 -20.625 7.310 3.484 1.00 53.99 C HETATM 3214 C7 OLA A2407 -21.541 6.156 3.887 1.00 49.12 C HETATM 3215 C8 OLA A2407 -21.061 4.780 3.463 1.00 50.67 C HETATM 3216 C9 OLA A2407 -21.013 4.724 1.942 1.00 52.65 C HETATM 3217 C10 OLA A2407 -20.470 3.729 1.207 1.00 52.78 C HETATM 3218 C11 OLA A2407 -19.820 2.504 1.812 1.00 54.50 C HETATM 3219 C12 OLA A2407 -20.790 1.308 1.866 1.00 58.61 C HETATM 3220 C13 OLA A2407 -20.094 -0.036 2.160 1.00 61.47 C HETATM 3221 C14 OLA A2407 -20.198 -0.465 3.632 1.00 62.61 C HETATM 3222 C15 OLA A2407 -18.855 -0.902 4.249 1.00 64.04 C HETATM 3223 C16 OLA A2407 -18.220 -2.107 3.532 1.00 65.54 C HETATM 3224 C1 OLA A2408 -31.279 -17.392 41.010 1.00 76.06 C HETATM 3225 O1 OLA A2408 -31.828 -18.527 40.945 1.00 77.79 O HETATM 3226 O2 OLA A2408 -31.555 -16.675 41.985 1.00 72.31 O HETATM 3227 C2 OLA A2408 -30.318 -16.902 39.943 1.00 76.75 C HETATM 3228 C3 OLA A2408 -28.860 -17.231 40.278 1.00 74.28 C HETATM 3229 C4 OLA A2408 -27.903 -17.035 39.107 1.00 71.45 C HETATM 3230 C5 OLA A2408 -26.571 -16.430 39.505 1.00 68.04 C HETATM 3231 C6 OLA A2408 -25.660 -16.054 38.343 1.00 66.60 C HETATM 3232 C7 OLA A2408 -24.691 -14.934 38.718 1.00 67.20 C HETATM 3233 C8 OLA A2408 -24.912 -13.624 37.982 1.00 67.86 C HETATM 3234 C9 OLA A2408 -24.129 -12.520 38.679 1.00 65.69 C HETATM 3235 C10 OLA A2408 -24.506 -11.224 38.782 1.00 60.93 C HETATM 3236 C11 OLA A2408 -23.679 -10.172 39.492 1.00 60.05 C HETATM 3237 C12 OLA A2408 -24.081 -8.739 39.086 1.00 59.14 C HETATM 3238 C13 OLA A2408 -23.208 -7.649 39.741 1.00 54.77 C HETATM 3239 C14 OLA A2408 -22.358 -6.861 38.732 1.00 53.30 C HETATM 3240 C15 OLA A2408 -23.159 -6.302 37.541 1.00 51.76 C HETATM 3241 C16 OLA A2408 -22.286 -5.551 36.519 1.00 49.88 C HETATM 3242 C17 OLA A2408 -22.665 -4.070 36.366 1.00 48.45 C HETATM 3243 C18 OLA A2408 -21.944 -3.390 35.194 1.00 47.69 C HETATM 3244 C1 OLA A2409 -8.549 14.810 8.518 1.00 77.84 C HETATM 3245 O1 OLA A2409 -8.707 15.776 7.721 1.00 80.66 O HETATM 3246 O2 OLA A2409 -8.767 15.013 9.725 1.00 77.47 O HETATM 3247 C2 OLA A2409 -8.109 13.442 8.037 1.00 73.25 C HETATM 3248 C3 OLA A2409 -8.906 12.992 6.810 1.00 69.83 C HETATM 3249 C4 OLA A2409 -9.384 11.548 6.895 1.00 67.51 C HETATM 3250 C5 OLA A2409 -8.473 10.568 6.183 1.00 65.39 C HETATM 3251 C6 OLA A2409 -8.911 9.112 6.261 1.00 63.53 C HETATM 3252 C7 OLA A2409 -7.718 8.171 6.406 1.00 62.78 C HETATM 3253 C8 OLA A2409 -7.986 6.739 5.984 1.00 63.59 C HETATM 3254 C9 OLA A2409 -9.419 6.641 5.482 1.00 64.48 C HETATM 3255 C10 OLA A2409 -9.914 5.662 4.692 1.00 65.46 C HETATM 3256 C11 OLA A2409 -11.352 5.617 4.221 1.00 65.71 C HETATM 3257 C12 OLA A2409 -11.502 4.852 2.892 1.00 66.22 C HETATM 3258 C13 OLA A2409 -11.434 3.319 3.051 1.00 69.31 C HETATM 3259 C14 OLA A2409 -11.857 2.557 1.785 1.00 72.06 C HETATM 3260 C15 OLA A2409 -10.992 1.316 1.484 1.00 75.09 C HETATM 3261 C16 OLA A2409 -10.117 0.876 2.671 1.00 75.94 C HETATM 3262 C17 OLA A2409 -9.056 -0.171 2.298 1.00 74.48 C HETATM 3263 C18 OLA A2409 -9.673 -1.534 1.948 1.00 75.40 C HETATM 3264 C1 OLA A2410 -36.124 -15.707 5.163 1.00 80.58 C HETATM 3265 O1 OLA A2410 -36.123 -16.791 5.769 1.00 81.51 O HETATM 3266 O2 OLA A2410 -36.466 -14.675 5.803 1.00 82.08 O HETATM 3267 C2 OLA A2410 -35.723 -15.645 3.703 1.00 78.14 C HETATM 3268 C3 OLA A2410 -34.396 -14.908 3.511 1.00 76.91 C HETATM 3269 C4 OLA A2410 -33.480 -15.570 2.489 1.00 74.17 C HETATM 3270 C5 OLA A2410 -32.828 -14.586 1.539 1.00 68.11 C HETATM 3271 C6 OLA A2410 -31.323 -14.439 1.711 1.00 61.07 C HETATM 3272 C7 OLA A2410 -30.972 -13.313 2.680 1.00 54.87 C HETATM 3273 C8 OLA A2410 -29.611 -13.451 3.338 1.00 56.53 C HETATM 3274 C9 OLA A2410 -28.747 -12.267 2.930 1.00 54.46 C HETATM 3275 C10 OLA A2410 -28.371 -11.252 3.740 1.00 54.12 C HETATM 3276 C1 OLA A2411 -15.219 12.850 0.687 1.00 63.36 C HETATM 3277 O1 OLA A2411 -14.042 13.288 0.564 1.00 65.74 O HETATM 3278 O2 OLA A2411 -16.109 13.662 0.992 1.00 63.55 O HETATM 3279 C2 OLA A2411 -15.554 11.387 0.474 1.00 62.82 C HETATM 3280 C3 OLA A2411 -16.969 11.048 0.952 1.00 62.06 C HETATM 3281 C4 OLA A2411 -17.312 9.569 0.821 1.00 60.76 C HETATM 3282 C5 OLA A2411 -16.100 8.683 0.607 1.00 59.96 C HETATM 3283 C6 OLA A2411 -16.235 7.271 1.163 1.00 58.54 C HETATM 3284 C1 OLA A2412 -39.672 12.524 9.181 1.00 80.42 C HETATM 3285 O1 OLA A2412 -40.880 12.878 9.289 1.00 82.80 O HETATM 3286 O2 OLA A2412 -38.800 13.402 9.290 1.00 83.40 O HETATM 3287 C2 OLA A2412 -39.281 11.082 8.926 1.00 72.98 C HETATM 3288 C3 OLA A2412 -40.461 10.129 9.129 1.00 67.81 C HETATM 3289 C4 OLA A2412 -40.135 8.677 8.803 1.00 66.15 C HETATM 3290 C5 OLA A2412 -41.306 7.911 8.223 1.00 65.78 C HETATM 3291 C6 OLA A2412 -41.210 6.397 8.359 1.00 64.52 C HETATM 3292 C7 OLA A2412 -42.094 5.677 7.344 1.00 61.39 C HETATM 3293 C8 OLA A2412 -41.944 4.167 7.331 1.00 63.46 C HETATM 3294 C9 OLA A2412 -43.278 3.539 7.708 1.00 65.58 C HETATM 3295 C10 OLA A2412 -43.442 2.331 8.290 1.00 66.00 C HETATM 3296 C11 OLA A2412 -42.292 1.417 8.653 1.00 62.96 C HETATM 3297 C12 OLA A2412 -42.722 -0.063 8.672 1.00 64.08 C HETATM 3298 C13 OLA A2412 -43.114 -0.572 10.074 1.00 65.22 C HETATM 3299 C1 OLA A2413 -33.594 9.550 2.620 1.00 77.22 C HETATM 3300 O1 OLA A2413 -34.769 9.941 2.715 1.00 78.81 O HETATM 3301 O2 OLA A2413 -32.678 10.363 2.926 1.00 79.53 O HETATM 3302 C2 OLA A2413 -33.291 8.141 2.151 1.00 73.21 C HETATM 3303 C3 OLA A2413 -34.192 7.720 0.986 1.00 69.81 C HETATM 3304 C4 OLA A2413 -35.214 6.656 1.365 1.00 67.38 C HETATM 3305 C5 OLA A2413 -35.138 5.408 0.507 1.00 65.35 C HETATM 3306 C6 OLA A2413 -34.675 4.154 1.237 1.00 64.99 C HETATM 3307 C7 OLA A2413 -34.617 2.944 0.306 1.00 63.35 C HETATM 3308 C8 OLA A2413 -33.641 1.858 0.723 1.00 63.50 C HETATM 3309 C9 OLA A2413 -32.757 1.511 -0.466 1.00 62.79 C HETATM 3310 C1 OLA A2414 -43.610 -24.525 12.842 1.00 78.57 C HETATM 3311 O1 OLA A2414 -43.881 -25.071 11.737 1.00 80.35 O HETATM 3312 O2 OLA A2414 -42.849 -25.131 13.616 1.00 78.94 O HETATM 3313 C2 OLA A2414 -44.181 -23.175 13.230 1.00 74.32 C HETATM 3314 C3 OLA A2414 -43.217 -22.385 14.119 1.00 72.66 C HETATM 3315 C4 OLA A2414 -43.747 -21.016 14.528 1.00 74.97 C HETATM 3316 C5 OLA A2414 -42.727 -20.170 15.265 1.00 76.25 C HETATM 3317 C6 OLA A2414 -41.281 -20.399 14.843 1.00 74.13 C HETATM 3318 C7 OLA A2414 -40.293 -19.868 15.879 1.00 72.82 C HETATM 3319 C8 OLA A2414 -39.580 -18.587 15.486 1.00 71.08 C HETATM 3320 C9 OLA A2414 -38.187 -18.926 14.974 1.00 68.15 C HETATM 3321 C10 OLA A2414 -37.458 -18.174 14.119 1.00 68.71 C HETATM 3322 C11 OLA A2414 -37.941 -16.861 13.538 1.00 69.27 C HETATM 3323 C12 OLA A2414 -37.300 -15.641 14.230 1.00 65.53 C HETATM 3324 C13 OLA A2414 -37.894 -14.294 13.769 1.00 65.05 C HETATM 3325 C14 OLA A2414 -37.533 -13.115 14.687 1.00 66.61 C HETATM 3326 C15 OLA A2414 -37.458 -11.759 13.956 1.00 68.42 C HETATM 3327 C16 OLA A2414 -38.427 -10.699 14.512 1.00 66.86 C HETATM 3328 C17 OLA A2414 -38.580 -9.468 13.605 1.00 63.65 C HETATM 3329 C1 OLA A2415 -28.251 -21.090 34.876 1.00 74.36 C HETATM 3330 O1 OLA A2415 -27.072 -21.134 34.485 1.00 72.49 O HETATM 3331 O2 OLA A2415 -29.001 -22.067 34.595 1.00 74.49 O HETATM 3332 C2 OLA A2415 -28.751 -19.894 35.665 1.00 74.67 C HETATM 3333 C3 OLA A2415 -30.193 -19.526 35.304 1.00 73.24 C HETATM 3334 C4 OLA A2415 -30.791 -18.448 36.201 1.00 70.99 C HETATM 3335 C5 OLA A2415 -30.545 -17.038 35.700 1.00 70.25 C HETATM 3336 C6 OLA A2415 -31.773 -16.321 35.154 1.00 68.94 C HETATM 3337 C7 OLA A2415 -31.583 -14.805 35.139 1.00 65.51 C HETATM 3338 C8 OLA A2415 -30.991 -14.219 36.409 1.00 61.80 C HETATM 3339 C9 OLA A2415 -30.294 -12.904 36.081 1.00 60.17 C HETATM 3340 C10 OLA A2415 -29.232 -12.386 36.741 1.00 56.74 C HETATM 3341 C11 OLA A2415 -28.572 -11.072 36.375 1.00 53.29 C HETATM 3342 C12 OLA A2415 -27.095 -11.019 36.816 1.00 49.03 C HETATM 3343 C3 OLA A2416 -16.904 -16.059 3.087 1.00 70.93 C HETATM 3344 C4 OLA A2416 -17.679 -14.832 2.620 1.00 70.07 C HETATM 3345 C5 OLA A2416 -17.795 -13.750 3.676 1.00 70.21 C HETATM 3346 C6 OLA A2416 -17.983 -12.339 3.136 1.00 70.01 C HETATM 3347 C7 OLA A2416 -17.548 -11.278 4.146 1.00 69.23 C HETATM 3348 C8 OLA A2416 -16.087 -11.340 4.559 1.00 68.96 C HETATM 3349 C9 OLA A2416 -15.374 -10.084 4.074 1.00 66.61 C HETATM 3350 C10 OLA A2416 -15.632 -8.818 4.475 1.00 64.53 C HETATM 3351 C11 OLA A2416 -16.696 -8.459 5.491 1.00 62.67 C HETATM 3352 C12 OLA A2416 -16.609 -6.984 5.932 1.00 60.29 C HETATM 3353 C6 OLA A2417 -21.158 -12.443 0.578 1.00 68.51 C HETATM 3354 C7 OLA A2417 -21.187 -11.000 1.077 1.00 66.80 C HETATM 3355 C8 OLA A2417 -20.798 -10.819 2.533 1.00 66.58 C HETATM 3356 C9 OLA A2417 -21.906 -10.064 3.253 1.00 66.98 C HETATM 3357 C10 OLA A2417 -21.905 -8.740 3.528 1.00 63.97 C HETATM 3358 C11 OLA A2417 -20.770 -7.815 3.145 1.00 62.48 C HETATM 3359 C12 OLA A2417 -21.289 -6.454 2.644 1.00 65.13 C HETATM 3360 C13 OLA A2417 -22.709 -6.120 3.144 1.00 65.74 C HETATM 3361 C14 OLA A2417 -23.003 -4.612 3.159 1.00 65.77 C HETATM 3362 C15 OLA A2417 -24.448 -4.255 2.764 1.00 66.34 C HETATM 3363 C16 OLA A2417 -24.562 -2.881 2.083 1.00 70.22 C HETATM 3364 C17 OLA A2417 -23.201 -2.262 1.729 1.00 72.35 C HETATM 3365 C18 OLA A2417 -23.291 -0.750 1.473 1.00 72.78 C HETATM 3366 C1 OLA A2418 -8.131 -18.931 11.986 1.00 71.85 C HETATM 3367 C2 OLA A2418 -9.017 -17.850 11.398 1.00 71.30 C HETATM 3368 C3 OLA A2418 -8.631 -16.456 11.901 1.00 70.51 C HETATM 3369 C4 OLA A2418 -9.811 -15.497 12.011 1.00 70.74 C HETATM 3370 C5 OLA A2418 -9.469 -14.062 11.659 1.00 69.56 C HETATM 3371 C6 OLA A2418 -10.296 -13.461 10.529 1.00 67.18 C HETATM 3372 C7 OLA A2418 -10.131 -11.944 10.450 1.00 66.59 C HETATM 3373 C8 OLA A2418 -9.678 -11.284 11.740 1.00 65.99 C HETATM 3374 C9 OLA A2418 -8.765 -10.115 11.402 1.00 65.61 C HETATM 3375 C10 OLA A2418 -8.297 -9.196 12.277 1.00 64.10 C HETATM 3376 C11 OLA A2418 -8.623 -9.203 13.755 1.00 61.31 C HETATM 3377 C12 OLA A2418 -8.030 -7.977 14.477 1.00 60.55 C HETATM 3378 C6 OLA A2419 -5.657 -17.979 15.592 1.00 61.55 C HETATM 3379 C7 OLA A2419 -7.106 -17.838 16.052 1.00 61.53 C HETATM 3380 C8 OLA A2419 -7.480 -16.469 16.590 1.00 60.39 C HETATM 3381 C9 OLA A2419 -8.465 -15.814 15.633 1.00 58.82 C HETATM 3382 C10 OLA A2419 -9.491 -15.007 15.983 1.00 57.81 C HETATM 3383 C11 OLA A2419 -9.812 -14.633 17.414 1.00 54.96 C HETATM 3384 C12 OLA A2419 -11.012 -13.671 17.495 1.00 53.12 C HETATM 3385 C13 OLA A2419 -10.754 -12.426 18.368 1.00 54.14 C HETATM 3386 C14 OLA A2419 -10.025 -11.298 17.622 1.00 51.90 C HETATM 3387 C15 OLA A2419 -8.758 -10.807 18.347 1.00 53.94 C HETATM 3388 C16 OLA A2419 -8.319 -9.395 17.922 1.00 55.31 C HETATM 3389 C17 OLA A2419 -8.187 -8.419 19.102 1.00 54.86 C HETATM 3390 C18 OLA A2419 -8.131 -6.955 18.643 1.00 54.54 C HETATM 3391 C1 OLA A2420 -34.954 10.076 33.680 1.00 81.14 C HETATM 3392 O1 OLA A2420 -35.801 10.983 33.629 1.00 82.35 O HETATM 3393 O2 OLA A2420 -33.738 10.413 33.731 1.00 83.18 O HETATM 3394 C2 OLA A2420 -35.388 8.623 33.681 1.00 77.29 C HETATM 3395 C3 OLA A2420 -34.313 7.698 33.105 1.00 73.45 C HETATM 3396 C4 OLA A2420 -34.667 6.218 33.200 1.00 69.60 C HETATM 3397 C5 OLA A2420 -33.652 5.313 32.528 1.00 66.15 C HETATM 3398 C6 OLA A2420 -33.762 3.833 32.872 1.00 65.80 C HETATM 3399 C7 OLA A2420 -32.384 3.194 33.037 1.00 65.66 C HETATM 3400 C8 OLA A2420 -32.310 1.716 32.698 1.00 63.71 C HETATM 3401 C9 OLA A2420 -30.847 1.313 32.580 1.00 58.99 C HETATM 3402 C10 OLA A2420 -30.306 0.144 32.993 1.00 54.48 C HETATM 3403 C11 OLA A2420 -31.101 -0.962 33.651 1.00 55.49 C HETATM 3404 C1 OLA A2421 -3.836 9.349 29.998 1.00 79.89 C HETATM 3405 O1 OLA A2421 -4.284 9.545 28.856 1.00 82.36 O HETATM 3406 O2 OLA A2421 -3.139 10.264 30.519 1.00 80.48 O HETATM 3407 C2 OLA A2421 -4.129 8.051 30.723 1.00 74.68 C HETATM 3408 C3 OLA A2421 -3.098 6.968 30.394 1.00 70.47 C HETATM 3409 C4 OLA A2421 -3.588 5.950 29.372 1.00 68.47 C HETATM 3410 C5 OLA A2421 -4.554 4.931 29.944 1.00 68.88 C HETATM 3411 C6 OLA A2421 -3.927 3.604 30.350 1.00 68.39 C HETATM 3412 C7 OLA A2421 -3.986 2.577 29.221 1.00 67.74 C HETATM 3413 C8 OLA A2421 -4.980 1.448 29.428 1.00 66.11 C HETATM 3414 C9 OLA A2421 -4.236 0.121 29.396 1.00 69.26 C HETATM 3415 C10 OLA A2421 -4.697 -1.038 28.869 1.00 70.26 C HETATM 3416 C11 OLA A2421 -6.056 -1.191 28.218 1.00 68.27 C HETATM 3417 C12 OLA A2421 -6.069 -2.314 27.161 1.00 66.41 C HETATM 3418 C13 OLA A2421 -6.429 -3.700 27.733 1.00 65.07 C HETATM 3419 C1 OLA A2422 -28.492 10.617 35.646 1.00 68.05 C HETATM 3420 O1 OLA A2422 -28.136 11.328 34.664 1.00 66.98 O HETATM 3421 O2 OLA A2422 -27.975 10.852 36.752 1.00 72.41 O HETATM 3422 C2 OLA A2422 -29.515 9.508 35.501 1.00 60.08 C HETATM 3423 C3 OLA A2422 -30.605 9.594 36.571 1.00 55.51 C HETATM 3424 C4 OLA A2422 -31.795 8.684 36.293 1.00 53.60 C HETATM 3425 C5 OLA A2422 -31.467 7.210 36.415 1.00 48.40 C HETATM 3426 C6 OLA A2422 -32.677 6.292 36.474 1.00 48.30 C HETATM 3427 C7 OLA A2422 -32.339 4.895 35.959 1.00 51.66 C HETATM 3428 C8 OLA A2422 -31.548 4.034 36.925 1.00 52.84 C HETATM 3429 C9 OLA A2422 -32.512 3.105 37.645 1.00 52.62 C HETATM 3430 C10 OLA A2422 -32.247 1.846 38.060 1.00 52.80 C HETATM 3431 C11 OLA A2422 -30.920 1.143 37.867 1.00 47.40 C HETATM 3432 C12 OLA A2422 -31.110 -0.385 37.789 1.00 43.76 C HETATM 3433 C13 OLA A2422 -29.981 -1.195 38.454 1.00 42.43 C HETATM 3434 C14 OLA A2422 -30.479 -2.511 39.071 1.00 44.35 C HETATM 3435 C2 OLA A2423 -34.136 -18.117 27.233 1.00 51.38 C HETATM 3436 C3 OLA A2423 -33.557 -17.048 26.301 1.00 50.97 C HETATM 3437 C4 OLA A2423 -33.114 -15.783 27.026 1.00 49.73 C HETATM 3438 C5 OLA A2423 -33.941 -14.563 26.672 1.00 52.16 C HETATM 3439 C6 OLA A2423 -33.231 -13.229 26.856 1.00 51.72 C HETATM 3440 C7 OLA A2423 -33.239 -12.783 28.315 1.00 52.62 C HETATM 3441 C8 OLA A2423 -34.256 -11.705 28.639 1.00 54.77 C HETATM 3442 C9 OLA A2423 -33.717 -10.367 28.155 1.00 52.99 C HETATM 3443 C10 OLA A2423 -33.585 -9.257 28.914 1.00 53.39 C HETATM 3444 C11 OLA A2423 -33.966 -9.207 30.378 1.00 55.34 C HETATM 3445 C12 OLA A2423 -34.236 -7.766 30.852 1.00 56.35 C HETATM 3446 C13 OLA A2423 -33.485 -6.698 30.033 1.00 57.24 C HETATM 3447 C14 OLA A2423 -32.861 -5.595 30.904 1.00 59.91 C HETATM 3448 C15 OLA A2423 -33.594 -5.370 32.240 1.00 61.18 C HETATM 3449 C16 OLA A2423 -33.001 -4.216 33.066 1.00 65.36 C HETATM 3450 C17 OLA A2423 -31.481 -4.061 32.896 1.00 67.91 C HETATM 3451 C9 OLC A2424 -3.816 -1.985 24.525 1.00 56.42 C HETATM 3452 C8 OLC A2424 -4.353 -0.595 24.712 1.00 51.61 C HETATM 3453 C24 OLC A2424 -2.387 12.830 25.246 1.00 60.35 C HETATM 3454 C7 OLC A2424 -3.341 0.509 25.132 1.00 46.84 C HETATM 3455 C6 OLC A2424 -3.480 1.849 24.368 1.00 44.93 C HETATM 3456 C5 OLC A2424 -3.197 3.114 25.218 1.00 45.63 C HETATM 3457 C4 OLC A2424 -3.141 4.437 24.418 1.00 42.50 C HETATM 3458 C3 OLC A2424 -3.180 5.698 25.301 1.00 37.95 C HETATM 3459 C2 OLC A2424 -2.891 7.019 24.566 1.00 40.76 C HETATM 3460 C21 OLC A2424 -2.590 10.394 25.831 1.00 52.20 C HETATM 3461 C1 OLC A2424 -2.483 8.058 25.577 1.00 49.65 C HETATM 3462 C22 OLC A2424 -1.589 11.551 25.614 1.00 57.31 C HETATM 3463 O19 OLC A2424 -2.429 7.894 26.783 1.00 62.33 O HETATM 3464 O25 OLC A2424 -1.574 13.879 25.695 1.00 60.39 O HETATM 3465 O23 OLC A2424 -0.944 11.763 26.829 1.00 58.27 O HETATM 3466 O20 OLC A2424 -2.148 9.280 25.061 1.00 48.28 O HETATM 3467 C9 OLC A2425 -38.326 4.656 4.984 1.00 59.88 C HETATM 3468 C8 OLC A2425 -37.144 5.301 5.646 1.00 60.35 C HETATM 3469 C24 OLC A2425 -30.159 15.963 7.779 1.00 91.55 C HETATM 3470 C7 OLC A2425 -37.075 6.855 5.625 1.00 60.87 C HETATM 3471 C6 OLC A2425 -36.209 7.491 6.740 1.00 61.01 C HETATM 3472 C5 OLC A2425 -36.376 9.023 6.899 1.00 63.26 C HETATM 3473 C4 OLC A2425 -35.213 9.732 7.632 1.00 66.47 C HETATM 3474 C3 OLC A2425 -35.343 11.268 7.677 1.00 72.91 C HETATM 3475 C2 OLC A2425 -34.198 12.028 6.974 1.00 80.04 C HETATM 3476 C21 OLC A2425 -31.784 14.039 7.787 1.00 92.09 C HETATM 3477 C1 OLC A2425 -34.039 13.393 7.596 1.00 87.02 C HETATM 3478 C22 OLC A2425 -31.475 15.420 8.410 1.00 92.82 C HETATM 3479 O19 OLC A2425 -34.729 13.861 8.486 1.00 87.04 O HETATM 3480 O25 OLC A2425 -29.310 16.163 8.878 1.00 90.62 O HETATM 3481 O23 OLC A2425 -32.531 16.262 8.068 1.00 95.03 O HETATM 3482 O20 OLC A2425 -33.017 14.149 7.087 1.00 91.42 O HETATM 3483 C10 OLC A2426 -42.302 4.249 12.287 1.00 54.20 C HETATM 3484 C9 OLC A2426 -41.382 5.222 12.305 1.00 56.52 C HETATM 3485 C11 OLC A2426 -43.242 3.856 13.376 1.00 47.11 C HETATM 3486 C8 OLC A2426 -41.059 6.147 13.431 1.00 55.10 C HETATM 3487 C24 OLC A2426 -41.102 19.188 15.386 1.00 96.29 C HETATM 3488 C16 OLC A2426 -44.362 -2.356 14.573 1.00 58.24 C HETATM 3489 C12 OLC A2426 -43.039 2.445 13.956 1.00 52.45 C HETATM 3490 C7 OLC A2426 -40.315 7.448 13.065 1.00 54.88 C HETATM 3491 C15 OLC A2426 -44.219 -0.853 14.892 1.00 60.22 C HETATM 3492 C13 OLC A2426 -44.259 1.515 13.832 1.00 56.97 C HETATM 3493 C6 OLC A2426 -40.774 8.686 13.851 1.00 53.79 C HETATM 3494 C14 OLC A2426 -43.891 0.025 13.664 1.00 59.00 C HETATM 3495 C5 OLC A2426 -41.232 9.875 12.980 1.00 51.02 C HETATM 3496 C4 OLC A2426 -40.691 11.233 13.445 1.00 51.87 C HETATM 3497 C3 OLC A2426 -41.686 12.389 13.313 1.00 56.65 C HETATM 3498 C2 OLC A2426 -41.345 13.597 14.195 1.00 64.32 C HETATM 3499 C21 OLC A2426 -41.206 16.784 14.686 1.00 88.53 C HETATM 3500 C1 OLC A2426 -41.912 14.844 13.572 1.00 75.40 C HETATM 3501 C22 OLC A2426 -41.022 18.225 14.169 1.00 93.64 C HETATM 3502 O19 OLC A2426 -43.017 14.959 13.071 1.00 76.25 O HETATM 3503 O25 OLC A2426 -42.185 20.024 15.080 1.00 97.43 O HETATM 3504 O23 OLC A2426 -39.748 18.297 13.606 1.00 95.18 O HETATM 3505 O20 OLC A2426 -41.073 15.920 13.572 1.00 83.48 O HETATM 3506 C10 OLC A2427 -38.155 3.246 14.519 1.00 50.77 C HETATM 3507 C9 OLC A2427 -37.574 4.445 14.664 1.00 47.16 C HETATM 3508 C11 OLC A2427 -38.606 2.306 15.593 1.00 50.38 C HETATM 3509 C8 OLC A2427 -37.219 5.135 15.937 1.00 44.00 C HETATM 3510 C24 OLC A2427 -39.615 16.673 19.935 1.00 68.68 C HETATM 3511 C16 OLC A2427 -41.251 -3.659 15.981 1.00 61.67 C HETATM 3512 C12 OLC A2427 -39.504 1.126 15.144 1.00 55.26 C HETATM 3513 C7 OLC A2427 -37.468 6.663 16.003 1.00 46.86 C HETATM 3514 C15 OLC A2427 -40.152 -2.586 16.136 1.00 61.59 C HETATM 3515 C13 OLC A2427 -39.585 -0.042 16.159 1.00 60.21 C HETATM 3516 C6 OLC A2427 -36.847 7.357 17.227 1.00 46.65 C HETATM 3517 C14 OLC A2427 -40.608 -1.147 15.790 1.00 61.85 C HETATM 3518 C5 OLC A2427 -37.584 8.622 17.722 1.00 44.63 C HETATM 3519 C4 OLC A2427 -37.946 9.673 16.651 1.00 43.09 C HETATM 3520 C3 OLC A2427 -37.907 11.109 17.210 1.00 45.63 C HETATM 3521 C2 OLC A2427 -38.802 12.144 16.502 1.00 51.36 C HETATM 3522 C21 OLC A2427 -40.142 15.290 17.906 1.00 55.72 C HETATM 3523 C1 OLC A2427 -39.268 13.146 17.530 1.00 55.60 C HETATM 3524 C22 OLC A2427 -39.252 16.434 18.438 1.00 65.11 C HETATM 3525 O19 OLC A2427 -39.571 12.893 18.684 1.00 61.71 O HETATM 3526 O25 OLC A2427 -39.364 18.039 20.132 1.00 69.45 O HETATM 3527 O23 OLC A2427 -37.933 15.996 18.358 1.00 65.74 O HETATM 3528 O20 OLC A2427 -39.331 14.443 17.104 1.00 52.70 O HETATM 3529 C10 OLC A2428 -34.420 -10.049 23.986 1.00 55.07 C HETATM 3530 C9 OLC A2428 -34.267 -11.198 23.313 1.00 54.91 C HETATM 3531 C11 OLC A2428 -33.358 -9.177 24.575 1.00 53.58 C HETATM 3532 C8 OLC A2428 -32.993 -11.894 22.970 1.00 52.42 C HETATM 3533 C24 OLC A2428 -31.995 -24.371 25.334 1.00 80.73 C HETATM 3534 C16 OLC A2428 -36.145 -3.539 22.999 1.00 59.60 C HETATM 3535 C12 OLC A2428 -33.514 -7.658 24.336 1.00 53.62 C HETATM 3536 C7 OLC A2428 -32.867 -13.365 23.426 1.00 52.33 C HETATM 3537 C15 OLC A2428 -35.981 -5.068 22.843 1.00 58.91 C HETATM 3538 C13 OLC A2428 -34.914 -7.237 23.820 1.00 57.23 C HETATM 3539 C6 OLC A2428 -33.011 -14.415 22.308 1.00 52.21 C HETATM 3540 C14 OLC A2428 -35.246 -5.740 24.025 1.00 58.88 C HETATM 3541 C5 OLC A2428 -31.881 -15.463 22.292 1.00 54.65 C HETATM 3542 C4 OLC A2428 -32.331 -16.915 22.044 1.00 55.25 C HETATM 3543 C3 OLC A2428 -31.235 -17.947 22.355 1.00 61.71 C HETATM 3544 C2 OLC A2428 -31.578 -19.390 21.961 1.00 68.67 C HETATM 3545 C21 OLC A2428 -31.965 -22.102 24.265 1.00 81.72 C HETATM 3546 C1 OLC A2428 -32.240 -20.065 23.131 1.00 77.50 C HETATM 3547 C22 OLC A2428 -32.655 -23.482 24.239 1.00 81.21 C HETATM 3548 O19 OLC A2428 -32.708 -19.506 24.107 1.00 81.93 O HETATM 3549 O25 OLC A2428 -32.950 -25.366 25.593 1.00 81.89 O HETATM 3550 O23 OLC A2428 -33.992 -23.272 24.568 1.00 81.60 O HETATM 3551 O20 OLC A2428 -32.300 -21.427 23.060 1.00 80.74 O HETATM 3552 C10 OLC A2429 -35.938 -10.221 19.453 1.00 60.20 C HETATM 3553 C9 OLC A2429 -36.260 -11.189 18.578 1.00 60.41 C HETATM 3554 C11 OLC A2429 -36.857 -9.239 20.118 1.00 59.15 C HETATM 3555 C8 OLC A2429 -35.340 -12.168 17.920 1.00 56.76 C HETATM 3556 C24 OLC A2429 -33.813 -25.048 19.995 1.00 91.77 C HETATM 3557 C7 OLC A2429 -35.094 -13.495 18.685 1.00 56.77 C HETATM 3558 C6 OLC A2429 -35.619 -14.770 17.998 1.00 55.79 C HETATM 3559 C5 OLC A2429 -35.160 -16.087 18.664 1.00 57.73 C HETATM 3560 C4 OLC A2429 -36.061 -17.307 18.377 1.00 62.43 C HETATM 3561 C3 OLC A2429 -35.306 -18.485 17.740 1.00 65.29 C HETATM 3562 C2 OLC A2429 -35.676 -19.869 18.296 1.00 70.00 C HETATM 3563 C21 OLC A2429 -34.249 -23.118 18.450 1.00 85.59 C HETATM 3564 C1 OLC A2429 -34.542 -20.828 18.025 1.00 76.62 C HETATM 3565 C22 OLC A2429 -34.906 -24.078 19.465 1.00 89.34 C HETATM 3566 O19 OLC A2429 -33.788 -20.797 17.067 1.00 78.13 O HETATM 3567 O25 OLC A2429 -34.515 -25.941 20.817 1.00 93.66 O HETATM 3568 O23 OLC A2429 -35.372 -23.296 20.518 1.00 90.88 O HETATM 3569 O20 OLC A2429 -34.373 -21.802 18.966 1.00 81.31 O HETATM 3570 C18 OLC A2430 -39.688 -3.974 12.084 1.00 58.84 C HETATM 3571 C10 OLC A2430 -36.070 4.608 9.789 1.00 51.14 C HETATM 3572 C9 OLC A2430 -35.644 5.609 10.570 1.00 44.56 C HETATM 3573 C17 OLC A2430 -39.537 -2.734 11.209 1.00 58.08 C HETATM 3574 C11 OLC A2430 -37.482 4.178 9.562 1.00 53.59 C HETATM 3575 C8 OLC A2430 -36.482 6.517 11.405 1.00 40.79 C HETATM 3576 C24 OLC A2430 -33.834 18.574 11.669 1.00 93.31 C HETATM 3577 C16 OLC A2430 -38.871 -1.554 11.931 1.00 57.23 C HETATM 3578 C12 OLC A2430 -37.713 2.667 9.406 1.00 56.82 C HETATM 3579 C7 OLC A2430 -35.907 7.916 11.703 1.00 44.25 C HETATM 3580 C15 OLC A2430 -39.393 -0.185 11.457 1.00 56.78 C HETATM 3581 C13 OLC A2430 -38.755 2.089 10.384 1.00 57.30 C HETATM 3582 C6 OLC A2430 -36.944 9.053 11.708 1.00 47.90 C HETATM 3583 C14 OLC A2430 -38.279 0.826 11.134 1.00 56.71 C HETATM 3584 C5 OLC A2430 -36.338 10.468 11.638 1.00 50.06 C HETATM 3585 C4 OLC A2430 -36.407 11.265 12.953 1.00 55.33 C HETATM 3586 C3 OLC A2430 -35.999 12.736 12.800 1.00 60.64 C HETATM 3587 C2 OLC A2430 -37.181 13.717 12.726 1.00 68.23 C HETATM 3588 C21 OLC A2430 -35.584 16.773 11.782 1.00 88.20 C HETATM 3589 C1 OLC A2430 -36.686 15.109 13.019 1.00 76.73 C HETATM 3590 C22 OLC A2430 -34.651 17.662 12.630 1.00 92.64 C HETATM 3591 O19 OLC A2430 -37.190 15.902 13.795 1.00 78.66 O HETATM 3592 O25 OLC A2430 -32.724 18.962 12.434 1.00 92.96 O HETATM 3593 O23 OLC A2430 -35.471 18.456 13.430 1.00 93.88 O HETATM 3594 O20 OLC A2430 -35.554 15.472 12.346 1.00 82.71 O HETATM 3595 O1 TAR A2431 -19.402 12.837 32.556 0.48 68.66 O HETATM 3596 O11 TAR A2431 -17.469 11.903 32.930 0.48 67.85 O1- HETATM 3597 C1 TAR A2431 -18.590 12.292 33.350 0.48 68.33 C HETATM 3598 C2 TAR A2431 -18.963 12.103 34.805 0.48 67.60 C HETATM 3599 O2 TAR A2431 -18.416 13.178 35.533 0.48 66.83 O HETATM 3600 C3 TAR A2431 -20.459 12.106 35.035 0.48 67.61 C HETATM 3601 O3 TAR A2431 -21.006 13.187 34.315 0.48 66.83 O HETATM 3602 C4 TAR A2431 -20.832 12.282 36.492 0.48 68.34 C HETATM 3603 O4 TAR A2431 -21.945 11.870 36.912 0.48 67.80 O HETATM 3604 O41 TAR A2431 -20.032 12.846 37.285 0.48 68.57 O1- HETATM 3605 O HOH A2501 -32.971 16.925 28.528 1.00 45.42 O HETATM 3606 O HOH A2502 22.506 -61.808 20.680 1.00 62.77 O HETATM 3607 O HOH A2503 14.694 -61.881 15.319 1.00 55.20 O HETATM 3608 O HOH A2504 -13.659 -32.658 36.832 1.00 61.78 O HETATM 3609 O HOH A2505 -25.473 -13.313 13.486 1.00 29.51 O HETATM 3610 O HOH A2506 -18.459 12.950 23.948 1.00 45.37 O HETATM 3611 O HOH A2507 -22.142 -6.617 15.502 1.00 34.87 O HETATM 3612 O HOH A2508 -4.429 -63.652 27.148 1.00 41.57 O HETATM 3613 O HOH A2509 -22.500 17.853 25.735 1.00 42.91 O HETATM 3614 O HOH A2510 -13.172 17.433 11.124 1.00 49.25 O HETATM 3615 O HOH A2511 -1.169 -44.908 23.919 1.00 65.67 O HETATM 3616 O HOH A2512 0.569 -61.970 29.513 1.00 34.63 O HETATM 3617 O HOH A2513 -27.313 19.527 14.547 1.00 55.79 O HETATM 3618 O HOH A2514 -23.731 15.145 33.180 1.00 38.15 O HETATM 3619 O HOH A2515 -23.189 15.238 4.954 1.00 58.07 O HETATM 3620 O HOH A2516 -24.944 13.472 11.473 1.00 50.47 O HETATM 3621 O HOH A2517 -24.818 23.723 30.029 1.00 42.46 O HETATM 3622 O HOH A2518 -13.967 -28.147 19.763 1.00 46.40 O HETATM 3623 O HOH A2519 -25.146 -15.830 14.528 1.00 39.94 O HETATM 3624 O HOH A2520 -13.060 -33.527 21.293 1.00 40.17 O HETATM 3625 O HOH A2521 -15.258 10.103 17.770 1.00 21.21 O HETATM 3626 O HOH A2522 -19.286 -35.576 26.885 1.00 52.71 O HETATM 3627 O HOH A2523 -24.016 -11.076 11.364 1.00 32.12 O HETATM 3628 O HOH A2524 -20.767 -11.494 15.001 1.00 47.48 O HETATM 3629 O HOH A2525 -7.366 10.224 30.666 1.00 54.57 O HETATM 3630 O HOH A2526 -11.240 15.294 23.212 1.00 46.95 O HETATM 3631 O HOH A2527 -25.247 2.655 15.964 1.00 20.18 O HETATM 3632 O HOH A2528 -17.208 -25.197 9.699 1.00 56.03 O HETATM 3633 O HOH A2529 -25.738 7.994 13.106 1.00 23.94 O HETATM 3634 O HOH A2530 -18.871 -11.429 12.978 1.00 29.07 O HETATM 3635 O HOH A2531 -23.983 21.081 5.052 1.00 69.62 O HETATM 3636 O HOH A2532 -17.889 -17.445 16.859 1.00 30.52 O HETATM 3637 O HOH A2533 14.986 -70.148 13.119 1.00 73.11 O HETATM 3638 O HOH A2534 -27.673 3.045 17.075 1.00 23.29 O HETATM 3639 O HOH A2535 -1.090 -63.060 19.857 1.00 36.45 O HETATM 3640 O HOH A2536 -16.230 -16.925 19.033 1.00 28.60 O HETATM 3641 O HOH A2537 -23.387 -4.784 14.169 1.00 19.93 O HETATM 3642 O HOH A2538 -17.514 -54.874 22.166 1.00 57.27 O HETATM 3643 O HOH A2539 -24.366 16.723 2.124 1.00 57.48 O HETATM 3644 O HOH A2540 -20.965 -2.652 24.418 1.00 26.52 O HETATM 3645 O HOH A2541 -2.994 -64.624 20.291 1.00 53.97 O HETATM 3646 O HOH A2542 -26.323 18.545 22.124 1.00 31.17 O HETATM 3647 O HOH A2543 -10.255 14.740 25.113 1.00 42.52 O HETATM 3648 O HOH A2544 -40.165 15.191 22.953 1.00 50.08 O HETATM 3649 O HOH A2545 -16.340 15.221 20.659 1.00 40.55 O HETATM 3650 O HOH A2546 -24.736 -6.679 17.752 1.00 44.72 O HETATM 3651 O HOH A2547 3.235 -73.253 23.995 1.00 52.07 O HETATM 3652 O HOH A2548 -15.169 3.513 21.890 1.00 21.77 O HETATM 3653 O HOH A2549 -25.611 16.973 26.931 1.00 41.75 O HETATM 3654 O HOH A2550 -23.288 -28.654 0.285 1.00 51.67 O HETATM 3655 O HOH A2551 -28.689 2.497 19.571 1.00 25.67 O HETATM 3656 O HOH A2552 -26.246 -12.009 25.683 1.00 37.36 O HETATM 3657 O HOH A2553 -27.257 -11.427 6.768 1.00 43.42 O HETATM 3658 O HOH A2554 -22.135 -28.983 8.767 1.00 44.18 O HETATM 3659 O HOH A2555 -16.555 -38.007 13.149 1.00 65.04 O HETATM 3660 O HOH A2556 -25.883 -14.601 24.742 1.00 35.72 O HETATM 3661 O HOH A2557 6.076 -75.881 26.550 1.00 43.10 O HETATM 3662 O HOH A2558 -33.954 13.774 30.417 1.00 52.89 O HETATM 3663 O HOH A2559 -19.917 11.754 16.260 1.00 41.43 O HETATM 3664 O HOH A2560 -19.521 -1.797 22.228 1.00 26.58 O HETATM 3665 O HOH A2561 9.315 -70.552 20.634 1.00 32.66 O HETATM 3666 O HOH A2562 -11.392 12.128 15.731 1.00 25.77 O HETATM 3667 O HOH A2563 -25.987 -12.154 21.414 1.00 27.80 O HETATM 3668 O HOH A2564 -16.289 0.614 12.612 1.00 21.32 O HETATM 3669 O HOH A2565 0.184 -50.815 21.992 1.00 51.52 O HETATM 3670 O HOH A2566 -18.929 9.948 22.645 1.00 39.95 O HETATM 3671 O HOH A2567 -4.858 -64.020 17.850 1.00 45.17 O HETATM 3672 O HOH A2568 17.701 -57.362 18.011 1.00 65.86 O HETATM 3673 O HOH A2569 -2.253 13.448 22.032 1.00 34.41 O HETATM 3674 O HOH A2570 -44.673 15.847 10.943 1.00 59.14 O HETATM 3675 O HOH A2571 -16.706 16.853 8.615 1.00 47.02 O HETATM 3676 O HOH A2572 -9.991 15.167 18.836 1.00 45.98 O HETATM 3677 O HOH A2573 -22.604 -10.131 15.021 1.00 54.55 O HETATM 3678 O HOH A2574 -14.354 -58.397 23.380 1.00 64.22 O HETATM 3679 O HOH A2575 -29.766 17.960 29.491 1.00 54.77 O HETATM 3680 O HOH A2576 -24.709 11.718 16.440 1.00 32.57 O HETATM 3681 O HOH A2577 -24.941 14.556 6.956 1.00 57.42 O HETATM 3682 O HOH A2578 -22.049 12.771 17.561 1.00 27.61 O HETATM 3683 O HOH A2579 5.692 -73.572 19.980 1.00 58.96 O HETATM 3684 O HOH A2580 3.564 -42.917 21.256 1.00 64.55 O HETATM 3685 O HOH A2581 -27.776 20.666 22.498 1.00 27.30 O HETATM 3686 O HOH A2582 -18.177 -2.938 20.135 1.00 25.52 O HETATM 3687 O HOH A2583 15.657 -65.967 25.083 1.00 76.53 O HETATM 3688 O HOH A2584 -22.334 -24.203 30.380 1.00 48.80 O HETATM 3689 O HOH A2585 3.914 -47.525 26.444 1.00 50.35 O HETATM 3690 O HOH A2586 -5.189 17.489 12.970 1.00 49.27 O HETATM 3691 O HOH A2587 -5.658 -61.379 28.521 1.00 49.18 O HETATM 3692 O HOH A2588 -7.453 -60.057 14.749 1.00 48.71 O HETATM 3693 O HOH A2589 -25.762 5.353 18.807 1.00 32.97 O HETATM 3694 O HOH A2590 -17.335 14.891 12.253 1.00 52.07 O HETATM 3695 O HOH A2591 -4.861 -37.792 20.658 1.00 49.34 O HETATM 3696 O HOH A2592 1.483 -46.896 20.593 1.00 40.45 O HETATM 3697 O HOH A2593 -15.548 -39.919 17.042 1.00 61.09 O HETATM 3698 O HOH A2594 -5.356 -31.436 24.723 1.00 46.09 O HETATM 3699 O HOH A2595 -36.213 18.670 16.318 1.00 52.00 O HETATM 3700 O HOH A2596 -14.696 -27.165 17.511 1.00 37.50 O HETATM 3701 O HOH A2597 -25.789 18.659 24.745 1.00 25.33 O HETATM 3702 O HOH A2598 -32.722 23.799 25.532 1.00 55.10 O HETATM 3703 O HOH A2599 6.987 -60.865 15.274 1.00 46.13 O HETATM 3704 O HOH A2600 15.203 -55.957 18.250 1.00 47.23 O HETATM 3705 O HOH A2601 -29.152 12.934 8.789 1.00 61.60 O HETATM 3706 O HOH A2602 -17.580 13.931 28.302 1.00 58.74 O HETATM 3707 O HOH A2603 -3.114 -46.838 30.137 1.00 67.17 O HETATM 3708 O HOH A2604 11.161 -65.244 14.396 1.00 55.89 O HETATM 3709 O HOH A2605 -4.557 -26.207 25.232 1.00 53.90 O HETATM 3710 O HOH A2606 -9.263 13.455 16.914 1.00 33.34 O HETATM 3711 O HOH A2607 -17.022 -29.465 11.221 1.00 63.21 O HETATM 3712 O HOH A2608 -35.004 -31.937 12.118 1.00 53.39 O HETATM 3713 O HOH A2609 -27.980 5.606 17.588 1.00 25.93 O HETATM 3714 O HOH A2610 -7.912 -29.040 9.896 1.00 62.14 O HETATM 3715 O HOH A2611 2.425 -68.579 18.714 1.00 49.32 O HETATM 3716 O HOH A2612 -10.742 -29.111 8.792 1.00 67.13 O HETATM 3717 O HOH A2613 18.574 -59.154 26.067 1.00 61.32 O HETATM 3718 O HOH A2614 -39.850 25.303 25.502 1.00 57.38 O HETATM 3719 O HOH A2615 5.724 -58.378 15.173 1.00 53.53 O HETATM 3720 O HOH A2616 -17.101 13.583 26.135 1.00 34.62 O HETATM 3721 O HOH A2617 -16.323 13.852 30.842 1.00 57.81 O HETATM 3722 O HOH A2618 -31.225 -32.219 19.043 1.00 60.97 O HETATM 3723 O HOH A2619 -20.956 -33.724 22.203 1.00 56.94 O HETATM 3724 O HOH A2620 -18.639 -28.115 6.970 1.00 43.08 O HETATM 3725 O HOH A2621 -35.577 21.072 15.974 1.00 75.68 O HETATM 3726 O HOH A2622 -11.210 16.970 17.938 1.00 50.32 O HETATM 3727 O HOH A2623 -3.444 16.326 21.789 1.00 41.80 O HETATM 3728 O HOH A2624 0.124 -52.331 30.513 1.00 61.35 O HETATM 3729 O HOH A2625 -12.018 19.587 15.118 1.00 51.54 O HETATM 3730 O HOH A2626 -12.078 -35.836 28.301 1.00 50.18 O HETATM 3731 O HOH A2627 -17.840 16.229 19.057 1.00 63.59 O HETATM 3732 O HOH A2628 -24.121 -30.115 24.470 1.00 63.09 O HETATM 3733 O HOH A2629 -15.013 12.364 28.541 1.00 29.07 O HETATM 3734 O HOH A2630 -36.768 -30.788 17.355 1.00 51.42 O HETATM 3735 O HOH A2631 -34.635 27.628 21.826 1.00 49.82 O HETATM 3736 O HOH A2632 -1.109 -48.124 30.743 1.00 49.34 O HETATM 3737 O HOH A2633 -17.704 15.298 5.926 1.00 47.18 O HETATM 3738 O HOH A2634 -25.618 -29.878 22.647 1.00 55.38 O HETATM 3739 O HOH A2635 -27.397 17.996 12.867 1.00 77.42 O HETATM 3740 O HOH A2636 2.595 -44.927 22.787 1.00 55.90 O HETATM 3741 O HOH A2637 -16.127 -29.436 7.282 1.00 76.94 O HETATM 3742 O HOH A2638 -43.510 14.790 8.929 1.00 58.99 O HETATM 3743 O HOH A2639 2.594 -53.334 30.704 1.00 56.36 O HETATM 3744 O HOH A2640 -30.546 20.122 3.496 1.00 61.45 O HETATM 3745 O HOH A2641 -16.658 -30.803 15.222 1.00 53.66 O HETATM 3746 O HOH A2642 -38.223 26.422 17.165 1.00 66.05 O HETATM 3747 O HOH A2643 -19.838 -28.590 8.731 1.00 58.48 O HETATM 3748 O HOH A2644 -5.516 13.475 26.484 1.00 75.98 O HETATM 3749 O HOH A2645 -31.542 20.347 29.023 1.00 57.54 O HETATM 3750 O HOH A2646 -1.319 -48.585 21.141 1.00 61.15 O HETATM 3751 O HOH A2647 8.125 -72.781 21.852 1.00 62.88 O HETATM 3752 O HOH A2648 0.951 -44.324 25.337 1.00 70.84 O HETATM 3753 O HOH A2649 -20.910 -55.276 18.197 1.00 60.51 O HETATM 3754 O HOH A2650 -17.265 -33.310 21.877 1.00 60.25 O HETATM 3755 O HOH A2651 4.996 -75.372 22.792 1.00 51.54 O HETATM 3756 O HOH A2652 1.965 -45.877 27.954 1.00 65.12 O HETATM 3757 O HOH A2653 -37.695 17.408 28.309 1.00 50.98 O HETATM 3758 O HOH A2654 -10.980 -37.566 18.864 1.00 58.94 O HETATM 3759 O HOH A2655 -1.634 -28.329 24.359 1.00 60.73 O HETATM 3760 O HOH A2656 2.389 -49.449 21.046 1.00 60.44 O HETATM 3761 O HOH A2657 -23.877 19.812 15.460 1.00 71.73 O HETATM 3762 O HOH A2658 6.200 -71.158 17.462 1.00 51.71 O HETATM 3763 O HOH A2659 -16.697 -33.456 15.374 1.00 73.98 O HETATM 3764 O HOH A2660 8.755 -62.323 13.712 1.00 63.06 O HETATM 3765 O HOH A2661 -20.937 -24.690 32.173 1.00 53.30 O HETATM 3766 O HOH A2662 -18.517 15.700 16.391 1.00 50.32 O HETATM 3767 O HOH A2663 -19.641 -31.107 21.032 1.00 57.75 O HETATM 3768 O HOH A2664 -16.430 16.962 12.325 1.00 64.11 O HETATM 3769 O HOH A2665 -13.093 13.697 24.185 1.00 36.22 O HETATM 3770 O HOH A2666 -18.767 -34.916 22.763 1.00 63.09 O HETATM 3771 O HOH A2667 -25.444 16.912 12.235 1.00 67.25 O HETATM 3772 O HOH A2668 -24.457 9.942 14.079 1.00 41.31 O HETATM 3773 O HOH A2669 -18.501 14.925 14.217 1.00 62.45 O HETATM 3774 O HOH A2670 -20.687 -24.034 15.120 1.00 66.10 O HETATM 3775 O HOH A2671 -7.259 12.166 28.031 1.00 49.15 O HETATM 3776 O HOH A2672 -18.363 -27.169 10.951 1.00 50.61 O HETATM 3777 O HOH A2673 -21.543 15.384 17.323 1.00 46.22 O HETATM 3778 O HOH A2674 -1.915 -24.304 25.694 1.00 62.83 O HETATM 3779 O HOH A2675 3.679 -71.127 16.715 1.00 69.05 O HETATM 3780 O HOH A2676 -20.396 -21.352 14.040 1.00 56.98 O HETATM 3781 O HOH A2677 -3.050 -48.356 19.670 1.00 63.71 O CONECT 407 3056 CONECT 543 1199 CONECT 559 1108 CONECT 579 1243 CONECT 684 3056 CONECT 1108 559 CONECT 1199 543 CONECT 1243 579 CONECT 2658 2679 CONECT 2679 2658 CONECT 3056 407 684 3611 3650 CONECT 3056 3677 CONECT 3057 3059 3061 3063 CONECT 3058 3060 3062 3064 CONECT 3059 3057 3065 3067 CONECT 3060 3058 3066 3068 CONECT 3061 3057 CONECT 3062 3058 CONECT 3063 3057 3073 3077 CONECT 3064 3058 3074 3078 CONECT 3065 3059 3069 3071 CONECT 3066 3060 3070 3072 CONECT 3067 3059 CONECT 3068 3060 CONECT 3069 3065 CONECT 3070 3066 CONECT 3071 3065 3073 3075 CONECT 3072 3066 3074 3076 CONECT 3073 3063 3071 3079 CONECT 3074 3064 3072 3080 CONECT 3075 3071 3081 CONECT 3076 3072 3082 CONECT 3077 3063 CONECT 3078 3064 CONECT 3079 3073 3081 3083 CONECT 3080 3074 3082 3084 CONECT 3081 3075 3079 CONECT 3082 3076 3080 CONECT 3083 3079 CONECT 3084 3080 CONECT 3085 3086 3094 CONECT 3086 3085 3087 CONECT 3087 3086 3088 3112 CONECT 3088 3087 3089 CONECT 3089 3088 3090 3094 CONECT 3090 3089 3091 CONECT 3091 3090 3092 CONECT 3092 3091 3093 3098 CONECT 3093 3092 3094 3095 CONECT 3094 3085 3089 3093 3103 CONECT 3095 3093 3096 CONECT 3096 3095 3097 CONECT 3097 3096 3098 3101 3102 CONECT 3098 3092 3097 3099 CONECT 3099 3098 3100 CONECT 3100 3099 3101 CONECT 3101 3097 3100 3104 CONECT 3102 3097 CONECT 3103 3094 CONECT 3104 3101 3105 3106 CONECT 3105 3104 CONECT 3106 3104 3107 CONECT 3107 3106 3108 CONECT 3108 3107 3109 CONECT 3109 3108 3110 3111 CONECT 3110 3109 CONECT 3111 3109 CONECT 3112 3087 CONECT 3113 3114 3122 CONECT 3114 3113 3115 CONECT 3115 3114 3116 3140 CONECT 3116 3115 3117 CONECT 3117 3116 3118 3122 CONECT 3118 3117 3119 CONECT 3119 3118 3120 CONECT 3120 3119 3121 3126 CONECT 3121 3120 3122 3123 CONECT 3122 3113 3117 3121 3131 CONECT 3123 3121 3124 CONECT 3124 3123 3125 CONECT 3125 3124 3126 3129 3130 CONECT 3126 3120 3125 3127 CONECT 3127 3126 3128 CONECT 3128 3127 3129 CONECT 3129 3125 3128 3132 CONECT 3130 3125 CONECT 3131 3122 CONECT 3132 3129 3133 3134 CONECT 3133 3132 CONECT 3134 3132 3135 CONECT 3135 3134 3136 CONECT 3136 3135 3137 CONECT 3137 3136 3138 3139 CONECT 3138 3137 CONECT 3139 3137 CONECT 3140 3115 CONECT 3141 3142 3150 CONECT 3142 3141 3143 CONECT 3143 3142 3144 3168 CONECT 3144 3143 3145 CONECT 3145 3144 3146 3150 CONECT 3146 3145 3147 CONECT 3147 3146 3148 CONECT 3148 3147 3149 3154 CONECT 3149 3148 3150 3151 CONECT 3150 3141 3145 3149 3159 CONECT 3151 3149 3152 CONECT 3152 3151 3153 CONECT 3153 3152 3154 3157 3158 CONECT 3154 3148 3153 3155 CONECT 3155 3154 3156 CONECT 3156 3155 3157 CONECT 3157 3153 3156 3160 CONECT 3158 3153 CONECT 3159 3150 CONECT 3160 3157 3161 3162 CONECT 3161 3160 CONECT 3162 3160 3163 CONECT 3163 3162 3164 CONECT 3164 3163 3165 CONECT 3165 3164 3166 3167 CONECT 3166 3165 CONECT 3167 3165 CONECT 3168 3143 CONECT 3169 3170 3178 CONECT 3170 3169 3171 CONECT 3171 3170 3172 3196 CONECT 3172 3171 3173 CONECT 3173 3172 3174 3178 CONECT 3174 3173 3175 CONECT 3175 3174 3176 CONECT 3176 3175 3177 3182 CONECT 3177 3176 3178 3179 CONECT 3178 3169 3173 3177 3187 CONECT 3179 3177 3180 CONECT 3180 3179 3181 CONECT 3181 3180 3182 3185 3186 CONECT 3182 3176 3181 3183 CONECT 3183 3182 3184 CONECT 3184 3183 3185 CONECT 3185 3181 3184 3188 CONECT 3186 3181 CONECT 3187 3178 CONECT 3188 3185 3189 3190 CONECT 3189 3188 CONECT 3190 3188 3191 CONECT 3191 3190 3192 CONECT 3192 3191 3193 CONECT 3193 3192 3194 3195 CONECT 3194 3193 CONECT 3195 3193 CONECT 3196 3171 CONECT 3197 3198 3199 3200 CONECT 3198 3197 CONECT 3199 3197 CONECT 3200 3197 3201 CONECT 3201 3200 3202 CONECT 3202 3201 3203 CONECT 3203 3202 3204 CONECT 3204 3203 3205 CONECT 3205 3204 CONECT 3206 3207 3208 3209 CONECT 3207 3206 CONECT 3208 3206 CONECT 3209 3206 3210 CONECT 3210 3209 3211 CONECT 3211 3210 3212 CONECT 3212 3211 3213 CONECT 3213 3212 3214 CONECT 3214 3213 3215 CONECT 3215 3214 3216 CONECT 3216 3215 3217 CONECT 3217 3216 3218 CONECT 3218 3217 3219 CONECT 3219 3218 3220 CONECT 3220 3219 3221 CONECT 3221 3220 3222 CONECT 3222 3221 3223 CONECT 3223 3222 CONECT 3224 3225 3226 3227 CONECT 3225 3224 CONECT 3226 3224 CONECT 3227 3224 3228 CONECT 3228 3227 3229 CONECT 3229 3228 3230 CONECT 3230 3229 3231 CONECT 3231 3230 3232 CONECT 3232 3231 3233 CONECT 3233 3232 3234 CONECT 3234 3233 3235 CONECT 3235 3234 3236 CONECT 3236 3235 3237 CONECT 3237 3236 3238 CONECT 3238 3237 3239 CONECT 3239 3238 3240 CONECT 3240 3239 3241 CONECT 3241 3240 3242 CONECT 3242 3241 3243 CONECT 3243 3242 CONECT 3244 3245 3246 3247 CONECT 3245 3244 CONECT 3246 3244 CONECT 3247 3244 3248 CONECT 3248 3247 3249 CONECT 3249 3248 3250 CONECT 3250 3249 3251 CONECT 3251 3250 3252 CONECT 3252 3251 3253 CONECT 3253 3252 3254 CONECT 3254 3253 3255 CONECT 3255 3254 3256 CONECT 3256 3255 3257 CONECT 3257 3256 3258 CONECT 3258 3257 3259 CONECT 3259 3258 3260 CONECT 3260 3259 3261 CONECT 3261 3260 3262 CONECT 3262 3261 3263 CONECT 3263 3262 CONECT 3264 3265 3266 3267 CONECT 3265 3264 CONECT 3266 3264 CONECT 3267 3264 3268 CONECT 3268 3267 3269 CONECT 3269 3268 3270 CONECT 3270 3269 3271 CONECT 3271 3270 3272 CONECT 3272 3271 3273 CONECT 3273 3272 3274 CONECT 3274 3273 3275 CONECT 3275 3274 CONECT 3276 3277 3278 3279 CONECT 3277 3276 CONECT 3278 3276 CONECT 3279 3276 3280 CONECT 3280 3279 3281 CONECT 3281 3280 3282 CONECT 3282 3281 3283 CONECT 3283 3282 CONECT 3284 3285 3286 3287 CONECT 3285 3284 CONECT 3286 3284 CONECT 3287 3284 3288 CONECT 3288 3287 3289 CONECT 3289 3288 3290 CONECT 3290 3289 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 CONECT 3310 3311 3312 3313 CONECT 3311 3310 CONECT 3312 3310 CONECT 3313 3310 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 3326 CONECT 3326 3325 3327 CONECT 3327 3326 3328 CONECT 3328 3327 CONECT 3329 3330 3331 3332 CONECT 3330 3329 CONECT 3331 3329 CONECT 3332 3329 3333 CONECT 3333 3332 3334 CONECT 3334 3333 3335 CONECT 3335 3334 3336 CONECT 3336 3335 3337 CONECT 3337 3336 3338 CONECT 3338 3337 3339 CONECT 3339 3338 3340 CONECT 3340 3339 3341 CONECT 3341 3340 3342 CONECT 3342 3341 CONECT 3343 3344 CONECT 3344 3343 3345 CONECT 3345 3344 3346 CONECT 3346 3345 3347 CONECT 3347 3346 3348 CONECT 3348 3347 3349 CONECT 3349 3348 3350 CONECT 3350 3349 3351 CONECT 3351 3350 3352 CONECT 3352 3351 CONECT 3353 3354 CONECT 3354 3353 3355 CONECT 3355 3354 3356 CONECT 3356 3355 3357 CONECT 3357 3356 3358 CONECT 3358 3357 3359 CONECT 3359 3358 3360 CONECT 3360 3359 3361 CONECT 3361 3360 3362 CONECT 3362 3361 3363 CONECT 3363 3362 3364 CONECT 3364 3363 3365 CONECT 3365 3364 CONECT 3366 3367 CONECT 3367 3366 3368 CONECT 3368 3367 3369 CONECT 3369 3368 3370 CONECT 3370 3369 3371 CONECT 3371 3370 3372 CONECT 3372 3371 3373 CONECT 3373 3372 3374 CONECT 3374 3373 3375 CONECT 3375 3374 3376 CONECT 3376 3375 3377 CONECT 3377 3376 CONECT 3378 3379 CONECT 3379 3378 3380 CONECT 3380 3379 3381 CONECT 3381 3380 3382 CONECT 3382 3381 3383 CONECT 3383 3382 3384 CONECT 3384 3383 3385 CONECT 3385 3384 3386 CONECT 3386 3385 3387 CONECT 3387 3386 3388 CONECT 3388 3387 3389 CONECT 3389 3388 3390 CONECT 3390 3389 CONECT 3391 3392 3393 3394 CONECT 3392 3391 CONECT 3393 3391 CONECT 3394 3391 3395 CONECT 3395 3394 3396 CONECT 3396 3395 3397 CONECT 3397 3396 3398 CONECT 3398 3397 3399 CONECT 3399 3398 3400 CONECT 3400 3399 3401 CONECT 3401 3400 3402 CONECT 3402 3401 3403 CONECT 3403 3402 CONECT 3404 3405 3406 3407 CONECT 3405 3404 CONECT 3406 3404 CONECT 3407 3404 3408 CONECT 3408 3407 3409 CONECT 3409 3408 3410 CONECT 3410 3409 3411 CONECT 3411 3410 3412 CONECT 3412 3411 3413 CONECT 3413 3412 3414 CONECT 3414 3413 3415 CONECT 3415 3414 3416 CONECT 3416 3415 3417 CONECT 3417 3416 3418 CONECT 3418 3417 CONECT 3419 3420 3421 3422 CONECT 3420 3419 CONECT 3421 3419 CONECT 3422 3419 3423 CONECT 3423 3422 3424 CONECT 3424 3423 3425 CONECT 3425 3424 3426 CONECT 3426 3425 3427 CONECT 3427 3426 3428 CONECT 3428 3427 3429 CONECT 3429 3428 3430 CONECT 3430 3429 3431 CONECT 3431 3430 3432 CONECT 3432 3431 3433 CONECT 3433 3432 3434 CONECT 3434 3433 CONECT 3435 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 3449 CONECT 3449 3448 3450 CONECT 3450 3449 CONECT 3451 3452 CONECT 3452 3451 3454 CONECT 3453 3462 3464 CONECT 3454 3452 3455 CONECT 3455 3454 3456 CONECT 3456 3455 3457 CONECT 3457 3456 3458 CONECT 3458 3457 3459 CONECT 3459 3458 3461 CONECT 3460 3462 3466 CONECT 3461 3459 3463 3466 CONECT 3462 3453 3460 3465 CONECT 3463 3461 CONECT 3464 3453 CONECT 3465 3462 CONECT 3466 3460 3461 CONECT 3467 3468 CONECT 3468 3467 3470 CONECT 3469 3478 3480 CONECT 3470 3468 3471 CONECT 3471 3470 3472 CONECT 3472 3471 3473 CONECT 3473 3472 3474 CONECT 3474 3473 3475 CONECT 3475 3474 3477 CONECT 3476 3478 3482 CONECT 3477 3475 3479 3482 CONECT 3478 3469 3476 3481 CONECT 3479 3477 CONECT 3480 3469 CONECT 3481 3478 CONECT 3482 3476 3477 CONECT 3483 3484 3485 CONECT 3484 3483 3486 CONECT 3485 3483 3489 CONECT 3486 3484 3490 CONECT 3487 3501 3503 CONECT 3488 3491 CONECT 3489 3485 3492 CONECT 3490 3486 3493 CONECT 3491 3488 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 3487 3499 3504 CONECT 3502 3500 CONECT 3503 3487 CONECT 3504 3501 CONECT 3505 3499 3500 CONECT 3506 3507 3508 CONECT 3507 3506 3509 CONECT 3508 3506 3512 CONECT 3509 3507 3513 CONECT 3510 3524 3526 CONECT 3511 3514 CONECT 3512 3508 3515 CONECT 3513 3509 3516 CONECT 3514 3511 3517 CONECT 3515 3512 3517 CONECT 3516 3513 3518 CONECT 3517 3514 3515 CONECT 3518 3516 3519 CONECT 3519 3518 3520 CONECT 3520 3519 3521 CONECT 3521 3520 3523 CONECT 3522 3524 3528 CONECT 3523 3521 3525 3528 CONECT 3524 3510 3522 3527 CONECT 3525 3523 CONECT 3526 3510 CONECT 3527 3524 CONECT 3528 3522 3523 CONECT 3529 3530 3531 CONECT 3530 3529 3532 CONECT 3531 3529 3535 CONECT 3532 3530 3536 CONECT 3533 3547 3549 CONECT 3534 3537 CONECT 3535 3531 3538 CONECT 3536 3532 3539 CONECT 3537 3534 3540 CONECT 3538 3535 3540 CONECT 3539 3536 3541 CONECT 3540 3537 3538 CONECT 3541 3539 3542 CONECT 3542 3541 3543 CONECT 3543 3542 3544 CONECT 3544 3543 3546 CONECT 3545 3547 3551 CONECT 3546 3544 3548 3551 CONECT 3547 3533 3545 3550 CONECT 3548 3546 CONECT 3549 3533 CONECT 3550 3547 CONECT 3551 3545 3546 CONECT 3552 3553 3554 CONECT 3553 3552 3555 CONECT 3554 3552 CONECT 3555 3553 3557 CONECT 3556 3565 3567 CONECT 3557 3555 3558 CONECT 3558 3557 3559 CONECT 3559 3558 3560 CONECT 3560 3559 3561 CONECT 3561 3560 3562 CONECT 3562 3561 3564 CONECT 3563 3565 3569 CONECT 3564 3562 3566 3569 CONECT 3565 3556 3563 3568 CONECT 3566 3564 CONECT 3567 3556 CONECT 3568 3565 CONECT 3569 3563 3564 CONECT 3570 3573 CONECT 3571 3572 3574 CONECT 3572 3571 3575 CONECT 3573 3570 3577 CONECT 3574 3571 3578 CONECT 3575 3572 3579 CONECT 3576 3590 3592 CONECT 3577 3573 3580 CONECT 3578 3574 3581 CONECT 3579 3575 3582 CONECT 3580 3577 3583 CONECT 3581 3578 3583 CONECT 3582 3579 3584 CONECT 3583 3580 3581 CONECT 3584 3582 3585 CONECT 3585 3584 3586 CONECT 3586 3585 3587 CONECT 3587 3586 3589 CONECT 3588 3590 3594 CONECT 3589 3587 3591 3594 CONECT 3590 3576 3588 3593 CONECT 3591 3589 CONECT 3592 3576 CONECT 3593 3590 CONECT 3594 3588 3589 CONECT 3595 3597 CONECT 3596 3597 CONECT 3597 3595 3596 3598 CONECT 3598 3597 3599 3600 CONECT 3599 3598 CONECT 3600 3598 3601 3602 CONECT 3601 3600 CONECT 3602 3600 3603 3604 CONECT 3603 3602 CONECT 3604 3602 CONECT 3611 3056 CONECT 3650 3056 CONECT 3677 3056 MASTER 493 0 32 21 2 0 54 6 3722 1 563 34 END