HEADER MEMBRANE PROTEIN 23-JAN-18 6FKA TITLE CRYSTAL STRUCTURE OF N2C/D282C STABILIZED OPSIN BOUND TO RS11 CAVEAT 6FKA NED DENSITY ABOVE LIGAND IN THE CHANNEL COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 1-326; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: BOS TAURUS; SOURCE 3 ORGANISM_COMMON: BOVINE; SOURCE 4 ORGANISM_TAXID: 9913; SOURCE 5 GENE: RHO; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCMV-TET O KEYWDS RHODOPSIN, G PROTEIN-COUPLED RECEPTORS, RETINITIS PIGMENTOSA, KEYWDS 2 SIGNALING PROTEIN, SENSORY TRANSDUCTION, PHOTORECEPTOR PROTEIN, KEYWDS 3 KINTEGRAL MEMBRANE PROTEIN, VISION, MEMBRANE, RECEPTOR, TRANSDUCER KEYWDS 4 PHOTORECEPTOR, SMALL MOLECULE COMPLEX, MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR D.MATTLE,J.STANDFUSS,R.DAWSON REVDAT 3 29-JUL-20 6FKA 1 COMPND REMARK HETNAM LINK REVDAT 3 2 1 SITE ATOM REVDAT 2 11-APR-18 6FKA 1 JRNL REVDAT 1 04-APR-18 6FKA 0 JRNL AUTH D.MATTLE,B.KUHN,J.AEBI,M.BEDOUCHA,D.KEKILLI,N.GROZINGER, JRNL AUTH 2 A.ALKER,M.G.RUDOLPH,G.SCHMID,G.F.X.SCHERTLER,M.HENNIG, JRNL AUTH 3 J.STANDFUSS,R.J.P.DAWSON JRNL TITL LIGAND CHANNEL IN PHARMACOLOGICALLY STABILIZED RHODOPSIN. JRNL REF PROC. NATL. ACAD. SCI. V. 115 3640 2018 JRNL REF 2 U.S.A. JRNL REFN ESSN 1091-6490 JRNL PMID 29555765 JRNL DOI 10.1073/PNAS.1718084115 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.10_2155: ???) REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.74 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 34717 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.210 REMARK 3 R VALUE (WORKING SET) : 0.210 REMARK 3 FREE R VALUE : 0.222 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.100 REMARK 3 FREE R VALUE TEST SET COUNT : 1770 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 47.7440 - 6.3441 0.99 2610 135 0.2201 0.1958 REMARK 3 2 6.3441 - 5.0373 1.00 2560 148 0.2169 0.2309 REMARK 3 3 5.0373 - 4.4011 1.00 2537 139 0.1828 0.1706 REMARK 3 4 4.4011 - 3.9989 1.00 2552 135 0.1803 0.2064 REMARK 3 5 3.9989 - 3.7124 1.00 2527 141 0.1893 0.2380 REMARK 3 6 3.7124 - 3.4936 1.00 2543 133 0.2014 0.2154 REMARK 3 7 3.4936 - 3.3187 1.00 2526 122 0.2117 0.2306 REMARK 3 8 3.3187 - 3.1742 1.00 2532 123 0.2198 0.2439 REMARK 3 9 3.1742 - 3.0521 1.00 2534 141 0.2272 0.2537 REMARK 3 10 3.0521 - 2.9468 1.00 2516 123 0.2510 0.2922 REMARK 3 11 2.9468 - 2.8546 1.00 2515 139 0.2672 0.3334 REMARK 3 12 2.8546 - 2.7730 1.00 2497 147 0.2685 0.3056 REMARK 3 13 2.7730 - 2.7000 1.00 2498 144 0.2835 0.3183 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.320 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.910 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.003 2889 REMARK 3 ANGLE : 0.687 3932 REMARK 3 CHIRALITY : 0.039 458 REMARK 3 PLANARITY : 0.004 460 REMARK 3 DIHEDRAL : 14.189 1695 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: ALL REMARK 3 ORIGIN FOR THE GROUP (A):-353.6998-171.4414 150.6499 REMARK 3 T TENSOR REMARK 3 T11: 0.5351 T22: 0.4338 REMARK 3 T33: 0.5787 T12: 0.0153 REMARK 3 T13: -0.0719 T23: 0.0442 REMARK 3 L TENSOR REMARK 3 L11: 1.9272 L22: 3.2550 REMARK 3 L33: 1.1121 L12: 1.2121 REMARK 3 L13: -0.0566 L23: -0.0676 REMARK 3 S TENSOR REMARK 3 S11: -0.0936 S12: 0.1715 S13: 0.1219 REMARK 3 S21: -0.2907 S22: 0.0880 S23: 0.1410 REMARK 3 S31: 0.0228 S32: -0.0572 S33: 0.0107 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 6FKA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JAN-18. REMARK 100 THE DEPOSITION ID IS D_1200008392. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-DEC-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X10SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS (VERSION OCT 15 REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 45835 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.460 REMARK 200 RESOLUTION RANGE LOW (A) : 47.740 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 11.45 REMARK 200 R MERGE (I) : 0.09210 REMARK 200 R SYM (I) : 0.09210 REMARK 200 FOR THE DATA SET : 16.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.46 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.56 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.7 REMARK 200 DATA REDUNDANCY IN SHELL : 11.10 REMARK 200 R MERGE FOR SHELL (I) : 0.95650 REMARK 200 R SYM FOR SHELL (I) : 0.95650 REMARK 200 FOR SHELL : 0.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: 4J4Q REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: SEE PUBLICATION, VAPOR DIFFUSION, REMARK 280 SITTING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 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 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 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 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 122.06200 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.47253 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.06700 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 122.06200 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.47253 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.06700 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 122.06200 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.47253 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.06700 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 122.06200 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.47253 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.06700 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 122.06200 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.47253 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.06700 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 122.06200 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.47253 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.06700 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.94506 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 74.13400 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.94506 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 74.13400 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.94506 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 74.13400 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.94506 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 74.13400 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.94506 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 74.13400 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.94506 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 74.13400 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: 3610 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18040 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B 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 PRO A 327 REMARK 465 LEU A 328 REMARK 465 GLY A 329 REMARK 465 ASP A 330 REMARK 465 ASP A 331 REMARK 465 GLU A 332 REMARK 465 ALA A 333 REMARK 465 SER A 334 REMARK 465 THR A 335 REMARK 465 THR A 336 REMARK 465 VAL A 337 REMARK 465 SER A 338 REMARK 465 LYS A 339 REMARK 465 THR A 340 REMARK 465 GLU A 341 REMARK 465 THR A 342 REMARK 465 SER A 343 REMARK 465 GLN A 344 REMARK 465 VAL A 345 REMARK 465 ALA A 346 REMARK 465 PRO A 347 REMARK 465 ALA A 348 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 O HOH A 513 O HOH A 513 17437 2.11 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 ASN A 8 17.35 80.70 REMARK 500 GLN A 28 49.86 -102.77 REMARK 500 SER A 176 -163.91 61.56 REMARK 500 HIS A 195 93.67 -52.76 REMARK 500 PHE A 212 -54.34 -147.00 REMARK 500 GLN A 237 47.11 -140.43 REMARK 500 GLN A 279 24.40 -72.40 REMARK 500 ILE A 307 -55.30 -124.68 REMARK 500 CYS A 323 13.80 58.79 REMARK 500 REMARK 500 REMARK: NULL DBREF 6FKA A 1 348 UNP P02699 OPSD_BOVIN 1 348 SEQADV 6FKA ACE A 0 UNP P02699 ACETYLATION SEQADV 6FKA CYS A 2 UNP P02699 ASN 2 CONFLICT SEQADV 6FKA CYS A 282 UNP P02699 ASP 282 CONFLICT SEQRES 1 A 349 ACE MET CYS GLY THR GLU GLY PRO ASN PHE TYR VAL PRO SEQRES 2 A 349 PHE SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU SEQRES 3 A 349 ALA PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER SEQRES 4 A 349 MET LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY SEQRES 5 A 349 PHE PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN SEQRES 6 A 349 HIS LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU SEQRES 7 A 349 ASN LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY SEQRES 8 A 349 PHE THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE SEQRES 9 A 349 VAL PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE SEQRES 10 A 349 ALA THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL SEQRES 11 A 349 VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO SEQRES 12 A 349 MET SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET SEQRES 13 A 349 GLY VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA SEQRES 14 A 349 ALA PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU SEQRES 15 A 349 GLY MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO SEQRES 16 A 349 HIS GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET SEQRES 17 A 349 PHE VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE SEQRES 18 A 349 PHE CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA SEQRES 19 A 349 ALA ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA SEQRES 20 A 349 GLU LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE SEQRES 21 A 349 ALA PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA SEQRES 22 A 349 PHE TYR ILE PHE THR HIS GLN GLY SER CYS PHE GLY PRO SEQRES 23 A 349 ILE PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER SEQRES 24 A 349 ALA VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS SEQRES 25 A 349 GLN PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY SEQRES 26 A 349 LYS ASN PRO LEU GLY ASP ASP GLU ALA SER THR THR VAL SEQRES 27 A 349 SER LYS THR GLU THR SER GLN VAL ALA PRO ALA HET ACE A 0 3 HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET MAN B 4 11 HET MAN B 5 11 HET PLM A 401 17 HET BOG A 407 20 HET BOG A 408 20 HET BOG A 409 20 HET BOG A 410 20 HET BOG A 411 20 HET DN5 A 412 28 HETNAM ACE ACETYL GROUP HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM PLM PALMITIC ACID HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE HETNAM DN5 (2~{S})-2-(3,4-DICHLOROPHENYL)-3-METHYL-1-SPIRO[1,3- HETNAM 2 DN5 BENZODIOXOLE-2,4'-PIPERIDINE]-1'-YL-BUTAN-1-ONE FORMUL 1 ACE C2 H4 O FORMUL 2 NAG 2(C8 H15 N O6) FORMUL 2 BMA C6 H12 O6 FORMUL 2 MAN 2(C6 H12 O6) FORMUL 3 PLM C16 H32 O2 FORMUL 4 BOG 5(C14 H28 O6) FORMUL 9 DN5 C22 H23 CL2 N O3 FORMUL 10 HOH *19(H2 O) HELIX 1 AA1 GLU A 33 HIS A 65 1 33 HELIX 2 AA2 LYS A 66 ARG A 69 5 4 HELIX 3 AA3 THR A 70 GLY A 90 1 21 HELIX 4 AA4 GLY A 90 LEU A 99 1 10 HELIX 5 AA5 PHE A 105 LYS A 141 1 37 HELIX 6 AA6 GLY A 149 ALA A 169 1 21 HELIX 7 AA7 PRO A 170 VAL A 173 5 4 HELIX 8 AA8 HIS A 195 THR A 198 5 4 HELIX 9 AA9 ASN A 199 HIS A 211 1 13 HELIX 10 AB1 PHE A 212 GLN A 236 1 25 HELIX 11 AB2 SER A 240 THR A 277 1 38 HELIX 12 AB3 ILE A 286 MET A 288 5 3 HELIX 13 AB4 THR A 289 LYS A 296 1 8 HELIX 14 AB5 THR A 297 ILE A 307 1 11 HELIX 15 AB6 ASN A 310 CYS A 322 1 13 SHEET 1 AA1 2 THR A 4 GLY A 6 0 SHEET 2 AA1 2 PHE A 9 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 GLU A 181 0 SHEET 2 AA2 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181 SSBOND 1 CYS A 2 CYS A 282 1555 1555 2.03 SSBOND 2 CYS A 110 CYS A 187 1555 1555 2.04 LINK C ACE A 0 N MET A 1 1555 1555 1.35 LINK ND2 ASN A 15 C1 NAG B 1 1555 1555 1.44 LINK SG CYS A 322 C1 PLM A 401 1555 1555 1.73 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.44 LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.44 LINK O6 BMA B 3 C1 MAN B 5 1555 1555 1.44 CRYST1 244.124 244.124 111.201 90.00 90.00 120.00 H 3 2 18 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 0.004096 0.002365 0.000000 0.00000 SCALE2 0.000000 0.004730 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008993 0.00000 HETATM 1 C ACE A 0 -354.937-140.071 150.725 1.00103.03 C ANISOU 1 C ACE A 0 12793 8728 17626 595 -1136 1390 C HETATM 2 O ACE A 0 -355.988-140.062 150.081 1.00114.32 O ANISOU 2 O ACE A 0 14128 10075 19234 684 -1287 1549 O HETATM 3 CH3 ACE A 0 -354.981-139.915 152.221 1.00 93.54 C ANISOU 3 CH3 ACE A 0 11539 7475 16527 632 -909 1080 C ATOM 4 N MET A 1 -353.762-140.193 150.082 1.00 98.03 N ANISOU 4 N MET A 1 12311 8222 16713 455 -1175 1495 N ATOM 5 CA MET A 1 -352.374-140.254 150.569 1.00 98.98 C ANISOU 5 CA MET A 1 12542 8459 16607 327 -1043 1366 C ATOM 6 C MET A 1 -352.173-141.261 151.699 1.00 94.07 C ANISOU 6 C MET A 1 11895 8040 15806 328 -890 1114 C ATOM 7 O MET A 1 -351.645-140.928 152.761 1.00 98.38 O ANISOU 7 O MET A 1 12459 8553 16368 292 -749 909 O ATOM 8 CB MET A 1 -351.885-138.873 151.014 1.00 95.84 C ANISOU 8 CB MET A 1 12176 7813 16427 294 -975 1307 C ATOM 9 CG MET A 1 -351.646-137.911 149.866 1.00 97.88 C ANISOU 9 CG MET A 1 12507 7900 16784 240 -1117 1570 C ATOM 10 SD MET A 1 -350.896-138.702 148.428 1.00101.29 S ANISOU 10 SD MET A 1 13072 8574 16840 105 -1240 1819 S ATOM 11 CE MET A 1 -349.328-139.271 149.089 1.00101.42 C ANISOU 11 CE MET A 1 13158 8816 16561 -33 -1062 1625 C ATOM 12 N CYS A 2 -352.598-142.498 151.450 1.00 87.78 N ANISOU 12 N CYS A 2 11068 7451 14833 357 -930 1138 N ATOM 13 CA CYS A 2 -352.571-143.519 152.490 1.00 93.16 C ANISOU 13 CA CYS A 2 11722 8314 15360 366 -803 923 C ATOM 14 C CYS A 2 -351.192-144.153 152.636 1.00 93.32 C ANISOU 14 C CYS A 2 11841 8539 15077 242 -751 870 C ATOM 15 O CYS A 2 -350.756-144.437 153.757 1.00 99.53 O ANISOU 15 O CYS A 2 12636 9397 15785 211 -633 671 O ATOM 16 CB CYS A 2 -353.620-144.592 152.187 1.00 97.54 C ANISOU 16 CB CYS A 2 12196 8990 15874 447 -867 970 C ATOM 17 SG CYS A 2 -355.339-144.021 152.239 1.00102.03 S ANISOU 17 SG CYS A 2 12595 9331 16839 607 -913 995 S ATOM 18 N GLY A 3 -350.498-144.385 151.526 1.00 80.85 N ANISOU 18 N GLY A 3 10336 7053 13332 163 -836 1046 N ATOM 19 CA GLY A 3 -349.213-145.046 151.587 1.00 71.06 C ANISOU 19 CA GLY A 3 9160 6001 11839 54 -780 1002 C ATOM 20 C GLY A 3 -348.116-144.313 150.850 1.00 67.18 C ANISOU 20 C GLY A 3 8750 5460 11317 -62 -796 1122 C ATOM 21 O GLY A 3 -348.228-143.116 150.575 1.00 73.07 O ANISOU 21 O GLY A 3 9515 5999 12249 -70 -832 1203 O ATOM 22 N THR A 4 -347.041-145.029 150.531 1.00 67.00 N ANISOU 22 N THR A 4 8769 5616 11073 -156 -762 1134 N ATOM 23 CA THR A 4 -345.933-144.490 149.755 1.00 65.44 C ANISOU 23 CA THR A 4 8642 5398 10823 -282 -752 1249 C ATOM 24 C THR A 4 -345.746-145.366 148.527 1.00 62.48 C ANISOU 24 C THR A 4 8325 5182 10232 -329 -782 1393 C ATOM 25 O THR A 4 -345.502-146.568 148.654 1.00 64.92 O ANISOU 25 O THR A 4 8612 5680 10375 -323 -740 1321 O ATOM 26 CB THR A 4 -344.649-144.433 150.589 1.00 68.21 C ANISOU 26 CB THR A 4 8975 5800 11141 -371 -655 1104 C ATOM 27 OG1 THR A 4 -344.895-143.714 151.803 1.00 67.92 O ANISOU 27 OG1 THR A 4 8906 5628 11274 -338 -625 945 O ATOM 28 CG2 THR A 4 -343.535-143.721 149.827 1.00 64.42 C ANISOU 28 CG2 THR A 4 8550 5271 10656 -507 -631 1219 C ATOM 29 N GLU A 5 -345.876-144.770 147.348 1.00 70.93 N ANISOU 29 N GLU A 5 9480 6166 11303 -381 -855 1597 N ATOM 30 CA GLU A 5 -345.669-145.485 146.099 1.00 63.07 C ANISOU 30 CA GLU A 5 8576 5308 10081 -455 -874 1736 C ATOM 31 C GLU A 5 -344.198-145.472 145.710 1.00 73.54 C ANISOU 31 C GLU A 5 9949 6706 11286 -601 -751 1744 C ATOM 32 O GLU A 5 -343.430-144.585 146.092 1.00 74.82 O ANISOU 32 O GLU A 5 10097 6767 11565 -663 -696 1715 O ATOM 33 CB GLU A 5 -346.481-144.870 144.962 1.00 63.23 C ANISOU 33 CB GLU A 5 8688 5208 10128 -468 -1022 1968 C ATOM 34 CG GLU A 5 -347.977-144.954 145.122 1.00 66.57 C ANISOU 34 CG GLU A 5 9048 5561 10683 -330 -1161 1994 C ATOM 35 CD GLU A 5 -348.700-144.184 144.042 1.00 77.47 C ANISOU 35 CD GLU A 5 10510 6793 12133 -350 -1338 2244 C ATOM 36 OE1 GLU A 5 -348.428-142.976 143.891 1.00 84.37 O ANISOU 36 OE1 GLU A 5 11421 7480 13155 -393 -1360 2340 O ATOM 37 OE2 GLU A 5 -349.523-144.790 143.329 1.00 92.69 O ANISOU 37 OE2 GLU A 5 12468 8785 13965 -332 -1467 2353 O ATOM 38 N GLY A 6 -343.821-146.471 144.925 1.00 74.11 N ANISOU 38 N GLY A 6 10075 6950 11132 -660 -702 1778 N ATOM 39 CA GLY A 6 -342.518-146.535 144.319 1.00 75.52 C ANISOU 39 CA GLY A 6 10301 7200 11193 -804 -570 1804 C ATOM 40 C GLY A 6 -342.551-147.538 143.190 1.00 71.18 C ANISOU 40 C GLY A 6 9851 6801 10393 -861 -541 1876 C ATOM 41 O GLY A 6 -343.556-148.219 142.971 1.00 71.01 O ANISOU 41 O GLY A 6 9854 6833 10292 -787 -637 1895 O ATOM 42 N PRO A 7 -341.461-147.640 142.432 1.00 70.27 N ANISOU 42 N PRO A 7 9798 6749 10151 -1003 -400 1911 N ATOM 43 CA PRO A 7 -341.371-148.707 141.426 1.00 75.05 C ANISOU 43 CA PRO A 7 10502 7507 10506 -1068 -330 1936 C ATOM 44 C PRO A 7 -341.308-150.061 142.117 1.00 73.94 C ANISOU 44 C PRO A 7 10243 7514 10337 -968 -272 1752 C ATOM 45 O PRO A 7 -340.388-150.331 142.893 1.00 72.86 O ANISOU 45 O PRO A 7 9973 7418 10292 -954 -162 1616 O ATOM 46 CB PRO A 7 -340.072-148.384 140.676 1.00 66.65 C ANISOU 46 CB PRO A 7 9500 6457 9367 -1243 -147 1981 C ATOM 47 CG PRO A 7 -339.775-146.953 141.012 1.00 64.14 C ANISOU 47 CG PRO A 7 9163 5967 9242 -1283 -182 2051 C ATOM 48 CD PRO A 7 -340.285-146.759 142.402 1.00 64.22 C ANISOU 48 CD PRO A 7 9022 5911 9468 -1124 -287 1930 C ATOM 49 N ASN A 8 -342.327-150.889 141.868 1.00 68.57 N ANISOU 49 N ASN A 8 9608 6901 9545 -900 -366 1758 N ATOM 50 CA ASN A 8 -342.424-152.281 142.315 1.00 66.69 C ANISOU 50 CA ASN A 8 9292 6799 9249 -817 -323 1611 C ATOM 51 C ASN A 8 -342.883-152.436 143.759 1.00 68.61 C ANISOU 51 C ASN A 8 9379 7024 9665 -667 -394 1485 C ATOM 52 O ASN A 8 -342.701-153.515 144.333 1.00 74.40 O ANISOU 52 O ASN A 8 10029 7859 10380 -606 -342 1354 O ATOM 53 CB ASN A 8 -341.102-153.041 142.143 1.00 55.76 C ANISOU 53 CB ASN A 8 7868 5521 7799 -886 -113 1509 C ATOM 54 CG ASN A 8 -340.593-153.019 140.723 1.00 68.59 C ANISOU 54 CG ASN A 8 9655 7178 9230 -1049 6 1603 C ATOM 55 OD1 ASN A 8 -341.371-153.033 139.770 1.00 71.52 O ANISOU 55 OD1 ASN A 8 10193 7552 9429 -1103 -78 1720 O ATOM 56 ND2 ASN A 8 -339.277-152.984 140.572 1.00 75.72 N ANISOU 56 ND2 ASN A 8 10510 8103 10157 -1140 203 1554 N ATOM 57 N PHE A 9 -343.479-151.419 144.381 1.00 66.76 N ANISOU 57 N PHE A 9 9110 6657 9599 -609 -503 1515 N ATOM 58 CA PHE A 9 -343.963-151.614 145.743 1.00 68.09 C ANISOU 58 CA PHE A 9 9153 6815 9904 -482 -547 1381 C ATOM 59 C PHE A 9 -345.004-150.565 146.098 1.00 65.70 C ANISOU 59 C PHE A 9 8842 6354 9767 -415 -672 1435 C ATOM 60 O PHE A 9 -345.143-149.540 145.427 1.00 66.64 O ANISOU 60 O PHE A 9 9033 6351 9934 -467 -728 1575 O ATOM 61 CB PHE A 9 -342.819-151.588 146.769 1.00 65.00 C ANISOU 61 CB PHE A 9 8654 6442 9603 -494 -449 1246 C ATOM 62 CG PHE A 9 -342.042-150.298 146.801 1.00 68.42 C ANISOU 62 CG PHE A 9 9089 6755 10152 -578 -418 1287 C ATOM 63 CD1 PHE A 9 -340.832-150.192 146.133 1.00 58.88 C ANISOU 63 CD1 PHE A 9 7898 5577 8896 -700 -302 1325 C ATOM 64 CD2 PHE A 9 -342.506-149.202 147.518 1.00 72.35 C ANISOU 64 CD2 PHE A 9 9567 7103 10820 -540 -489 1276 C ATOM 65 CE1 PHE A 9 -340.103-149.015 146.169 1.00 67.54 C ANISOU 65 CE1 PHE A 9 8992 6561 10108 -788 -271 1364 C ATOM 66 CE2 PHE A 9 -341.785-148.021 147.555 1.00 65.32 C ANISOU 66 CE2 PHE A 9 8683 6091 10045 -625 -461 1308 C ATOM 67 CZ PHE A 9 -340.578-147.931 146.881 1.00 63.13 C ANISOU 67 CZ PHE A 9 8422 5850 9714 -752 -359 1357 C ATOM 68 N TYR A 10 -345.736-150.855 147.171 1.00 69.55 N ANISOU 68 N TYR A 10 9239 6836 10349 -302 -708 1321 N ATOM 69 CA TYR A 10 -346.636-149.905 147.816 1.00 66.53 C ANISOU 69 CA TYR A 10 8812 6295 10169 -224 -782 1314 C ATOM 70 C TYR A 10 -346.528-150.148 149.314 1.00 69.30 C ANISOU 70 C TYR A 10 9070 6667 10595 -165 -720 1121 C ATOM 71 O TYR A 10 -347.043-151.151 149.821 1.00 72.19 O ANISOU 71 O TYR A 10 9392 7131 10905 -100 -718 1036 O ATOM 72 CB TYR A 10 -348.078-150.068 147.335 1.00 63.87 C ANISOU 72 CB TYR A 10 8480 5925 9863 -148 -909 1405 C ATOM 73 CG TYR A 10 -349.087-149.259 148.128 1.00 68.62 C ANISOU 73 CG TYR A 10 8999 6364 10710 -45 -959 1366 C ATOM 74 CD1 TYR A 10 -349.225-147.884 147.928 1.00 72.25 C ANISOU 74 CD1 TYR A 10 9474 6626 11353 -51 -1009 1458 C ATOM 75 CD2 TYR A 10 -349.907-149.869 149.074 1.00 62.71 C ANISOU 75 CD2 TYR A 10 8159 5650 10020 54 -942 1233 C ATOM 76 CE1 TYR A 10 -350.147-147.141 148.650 1.00 73.13 C ANISOU 76 CE1 TYR A 10 9498 6568 11718 49 -1034 1408 C ATOM 77 CE2 TYR A 10 -350.828-149.138 149.798 1.00 67.51 C ANISOU 77 CE2 TYR A 10 8685 6103 10864 144 -954 1180 C ATOM 78 CZ TYR A 10 -350.948-147.776 149.583 1.00 77.60 C ANISOU 78 CZ TYR A 10 9968 7177 12339 146 -997 1261 C ATOM 79 OH TYR A 10 -351.869-147.056 150.311 1.00 86.40 O ANISOU 79 OH TYR A 10 10991 8121 13716 243 -988 1192 O ATOM 80 N VAL A 11 -345.834-149.256 150.012 1.00 65.31 N ANISOU 80 N VAL A 11 8546 6071 10199 -204 -674 1054 N ATOM 81 CA VAL A 11 -345.725-149.339 151.464 1.00 68.05 C ANISOU 81 CA VAL A 11 8832 6422 10602 -173 -627 873 C ATOM 82 C VAL A 11 -346.973-148.706 152.069 1.00 76.41 C ANISOU 82 C VAL A 11 9864 7340 11830 -81 -655 825 C ATOM 83 O VAL A 11 -347.239-147.520 151.835 1.00 71.78 O ANISOU 83 O VAL A 11 9291 6577 11405 -80 -681 884 O ATOM 84 CB VAL A 11 -344.447-148.656 151.973 1.00 63.83 C ANISOU 84 CB VAL A 11 8294 5848 10110 -269 -576 813 C ATOM 85 CG1 VAL A 11 -344.443-148.592 153.503 1.00 59.59 C ANISOU 85 CG1 VAL A 11 7723 5297 9623 -255 -550 628 C ATOM 86 CG2 VAL A 11 -343.217-149.384 151.451 1.00 55.61 C ANISOU 86 CG2 VAL A 11 7244 4948 8936 -350 -531 845 C ATOM 87 N PRO A 12 -347.767-149.450 152.843 1.00 73.83 N ANISOU 87 N PRO A 12 9491 7072 11487 -5 -640 718 N ATOM 88 CA PRO A 12 -348.991-148.872 153.416 1.00 62.21 C ANISOU 88 CA PRO A 12 7977 5462 10200 83 -636 659 C ATOM 89 C PRO A 12 -348.701-147.928 154.572 1.00 64.19 C ANISOU 89 C PRO A 12 8232 5588 10569 57 -559 507 C ATOM 90 O PRO A 12 -349.202-148.120 155.683 1.00 68.86 O ANISOU 90 O PRO A 12 8803 6178 11182 89 -490 349 O ATOM 91 CB PRO A 12 -349.771-150.108 153.877 1.00 57.57 C ANISOU 91 CB PRO A 12 7346 5003 9526 147 -620 587 C ATOM 92 CG PRO A 12 -348.702-151.092 154.214 1.00 65.00 C ANISOU 92 CG PRO A 12 8315 6119 10263 81 -589 531 C ATOM 93 CD PRO A 12 -347.587-150.862 153.224 1.00 63.40 C ANISOU 93 CD PRO A 12 8155 5939 9996 1 -615 649 C ATOM 94 N PHE A 13 -347.890-146.902 154.322 1.00 62.25 N ANISOU 94 N PHE A 13 8025 5233 10393 -15 -564 547 N ATOM 95 CA PHE A 13 -347.545-145.932 155.353 1.00 64.72 C ANISOU 95 CA PHE A 13 8358 5415 10819 -59 -497 401 C ATOM 96 C PHE A 13 -347.239-144.599 154.688 1.00 65.63 C ANISOU 96 C PHE A 13 8499 5337 11098 -97 -527 506 C ATOM 97 O PHE A 13 -346.506-144.554 153.696 1.00 66.56 O ANISOU 97 O PHE A 13 8647 5494 11150 -162 -575 656 O ATOM 98 CB PHE A 13 -346.347-146.409 156.179 1.00 66.72 C ANISOU 98 CB PHE A 13 8639 5802 10910 -161 -466 285 C ATOM 99 CG PHE A 13 -346.153-145.653 157.459 1.00 63.75 C ANISOU 99 CG PHE A 13 8299 5321 10603 -215 -402 98 C ATOM 100 CD1 PHE A 13 -346.827-146.031 158.609 1.00 61.98 C ANISOU 100 CD1 PHE A 13 8085 5120 10344 -186 -335 -71 C ATOM 101 CD2 PHE A 13 -345.293-144.572 157.517 1.00 61.59 C ANISOU 101 CD2 PHE A 13 8060 4925 10417 -311 -402 85 C ATOM 102 CE1 PHE A 13 -346.654-145.337 159.788 1.00 59.43 C ANISOU 102 CE1 PHE A 13 7822 4702 10056 -255 -267 -256 C ATOM 103 CE2 PHE A 13 -345.111-143.873 158.694 1.00 58.28 C ANISOU 103 CE2 PHE A 13 7690 4406 10049 -376 -347 -100 C ATOM 104 CZ PHE A 13 -345.792-144.255 159.831 1.00 59.88 C ANISOU 104 CZ PHE A 13 7918 4634 10198 -351 -278 -274 C ATOM 105 N SER A 14 -347.803-143.524 155.232 1.00 67.85 N ANISOU 105 N SER A 14 8775 5406 11599 -63 -486 423 N ATOM 106 CA SER A 14 -347.590-142.197 154.672 1.00 60.07 C ANISOU 106 CA SER A 14 7816 4205 10802 -94 -516 521 C ATOM 107 C SER A 14 -346.142-141.764 154.850 1.00 66.63 C ANISOU 107 C SER A 14 8705 5049 11564 -241 -495 491 C ATOM 108 O SER A 14 -345.521-142.017 155.884 1.00 59.80 O ANISOU 108 O SER A 14 7854 4263 10605 -307 -441 320 O ATOM 109 CB SER A 14 -348.517-141.182 155.336 1.00 62.83 C ANISOU 109 CB SER A 14 8137 4307 11427 -18 -457 409 C ATOM 110 OG SER A 14 -347.972-139.872 155.259 1.00 67.10 O ANISOU 110 OG SER A 14 8723 4637 12133 -85 -452 426 O ATOM 111 N ASN A 15 -345.604-141.087 153.838 1.00 70.88 N ANISOU 111 N ASN A 15 9276 5504 12152 -303 -546 665 N ATOM 112 CA ASN A 15 -344.237-140.590 153.890 1.00 69.14 C ANISOU 112 CA ASN A 15 9094 5277 11900 -450 -525 655 C ATOM 113 C ASN A 15 -344.173-139.099 154.202 1.00 71.43 C ANISOU 113 C ASN A 15 9417 5295 12426 -491 -503 614 C ATOM 114 O ASN A 15 -343.176-138.445 153.876 1.00 76.40 O ANISOU 114 O ASN A 15 10080 5866 13081 -614 -505 673 O ATOM 115 CB ASN A 15 -343.518-140.895 152.576 1.00 76.87 C ANISOU 115 CB ASN A 15 10094 6359 12754 -522 -565 864 C ATOM 116 CG ASN A 15 -342.014-140.906 152.728 1.00 73.62 C ANISOU 116 CG ASN A 15 9681 6032 12259 -671 -523 828 C ATOM 117 OD1 ASN A 15 -341.494-141.023 153.836 1.00 67.43 O ANISOU 117 OD1 ASN A 15 8872 5292 11458 -714 -493 651 O ATOM 118 ND2 ASN A 15 -341.304-140.787 151.618 1.00 72.71 N ANISOU 118 ND2 ASN A 15 9592 5941 12093 -759 -523 997 N ATOM 119 N LYS A 16 -345.214-138.542 154.829 1.00 78.47 N ANISOU 119 N LYS A 16 10296 6011 13509 -394 -471 507 N ATOM 120 CA LYS A 16 -345.198-137.111 155.126 1.00 78.03 C ANISOU 120 CA LYS A 16 10274 5671 13704 -426 -439 455 C ATOM 121 C LYS A 16 -344.118-136.766 156.143 1.00 76.59 C ANISOU 121 C LYS A 16 10136 5491 13473 -569 -378 264 C ATOM 122 O LYS A 16 -343.639-135.626 156.177 1.00 87.99 O ANISOU 122 O LYS A 16 11622 6735 15075 -654 -367 254 O ATOM 123 CB LYS A 16 -346.572-136.653 155.619 1.00 80.02 C ANISOU 123 CB LYS A 16 10485 5726 14192 -282 -393 359 C ATOM 124 CG LYS A 16 -347.005-137.234 156.954 1.00 85.83 C ANISOU 124 CG LYS A 16 11207 6548 14856 -248 -285 95 C ATOM 125 CD LYS A 16 -348.497-137.014 157.185 1.00 83.61 C ANISOU 125 CD LYS A 16 10854 6105 14807 -86 -230 39 C ATOM 126 CE LYS A 16 -348.955-137.626 158.500 1.00 91.83 C ANISOU 126 CE LYS A 16 11895 7239 15758 -66 -96 -225 C ATOM 127 NZ LYS A 16 -350.215-138.414 158.343 1.00102.34 N ANISOU 127 NZ LYS A 16 13124 8635 17124 83 -89 -193 N ATOM 128 N THR A 17 -343.719-137.731 156.969 1.00 72.23 N ANISOU 128 N THR A 17 9579 5158 12708 -608 -354 118 N ATOM 129 CA THR A 17 -342.609-137.549 157.894 1.00 70.50 C ANISOU 129 CA THR A 17 9400 4976 12411 -761 -335 -41 C ATOM 130 C THR A 17 -341.265-137.939 157.293 1.00 71.58 C ANISOU 130 C THR A 17 9511 5272 12415 -882 -395 84 C ATOM 131 O THR A 17 -340.231-137.697 157.923 1.00 78.87 O ANISOU 131 O THR A 17 10447 6212 13306 -1024 -404 -16 O ATOM 132 CB THR A 17 -342.841-138.352 159.177 1.00 76.51 C ANISOU 132 CB THR A 17 10179 5879 13013 -757 -293 -257 C ATOM 133 OG1 THR A 17 -343.001-139.743 158.854 1.00 82.62 O ANISOU 133 OG1 THR A 17 10900 6901 13593 -688 -330 -175 O ATOM 134 CG2 THR A 17 -344.082-137.852 159.904 1.00 67.58 C ANISOU 134 CG2 THR A 17 9077 4571 12030 -663 -192 -420 C ATOM 135 N GLY A 18 -341.248-138.536 156.104 1.00 73.27 N ANISOU 135 N GLY A 18 9686 5599 12555 -839 -432 291 N ATOM 136 CA GLY A 18 -340.001-138.824 155.427 1.00 77.64 C ANISOU 136 CA GLY A 18 10209 6278 13014 -954 -454 409 C ATOM 137 C GLY A 18 -339.273-140.071 155.880 1.00 71.35 C ANISOU 137 C GLY A 18 9353 5738 12019 -989 -468 343 C ATOM 138 O GLY A 18 -338.116-140.266 155.488 1.00 66.98 O ANISOU 138 O GLY A 18 8751 5275 11424 -1094 -473 408 O ATOM 139 N VAL A 19 -339.905-140.926 156.685 1.00 72.95 N ANISOU 139 N VAL A 19 9551 6052 12115 -906 -471 222 N ATOM 140 CA VAL A 19 -339.212-142.092 157.229 1.00 68.85 C ANISOU 140 CA VAL A 19 8980 5755 11423 -941 -502 161 C ATOM 141 C VAL A 19 -339.367-143.343 156.369 1.00 69.01 C ANISOU 141 C VAL A 19 8948 5961 11310 -858 -504 288 C ATOM 142 O VAL A 19 -338.605-144.303 156.551 1.00 71.99 O ANISOU 142 O VAL A 19 9264 6512 11578 -891 -528 277 O ATOM 143 CB VAL A 19 -339.693-142.401 158.660 1.00 59.95 C ANISOU 143 CB VAL A 19 7896 4659 10225 -926 -507 -41 C ATOM 144 CG1 VAL A 19 -339.602-141.156 159.530 1.00 61.84 C ANISOU 144 CG1 VAL A 19 8209 4704 10584 -1017 -488 -192 C ATOM 145 CG2 VAL A 19 -341.117-142.962 158.647 1.00 58.97 C ANISOU 145 CG2 VAL A 19 7789 4554 10064 -769 -468 -51 C ATOM 146 N VAL A 20 -340.324-143.361 155.437 1.00 71.31 N ANISOU 146 N VAL A 20 9262 6213 11619 -755 -489 408 N ATOM 147 CA VAL A 20 -340.587-144.562 154.654 1.00 67.46 C ANISOU 147 CA VAL A 20 8746 5895 10992 -682 -492 510 C ATOM 148 C VAL A 20 -339.391-144.890 153.768 1.00 69.79 C ANISOU 148 C VAL A 20 8998 6288 11231 -773 -470 620 C ATOM 149 O VAL A 20 -338.747-144.000 153.196 1.00 64.20 O ANISOU 149 O VAL A 20 8303 5480 10610 -867 -448 700 O ATOM 150 CB VAL A 20 -341.868-144.381 153.825 1.00 61.23 C ANISOU 150 CB VAL A 20 7996 5024 10244 -574 -505 623 C ATOM 151 CG1 VAL A 20 -342.106-145.589 152.925 1.00 55.48 C ANISOU 151 CG1 VAL A 20 7254 4465 9359 -521 -514 729 C ATOM 152 CG2 VAL A 20 -343.054-144.153 154.746 1.00 58.58 C ANISOU 152 CG2 VAL A 20 7671 4595 9991 -477 -502 497 C ATOM 153 N ARG A 21 -339.083-146.183 153.664 1.00 60.32 N ANISOU 153 N ARG A 21 7746 5277 9898 -748 -463 620 N ATOM 154 CA ARG A 21 -338.016-146.683 152.812 1.00 60.48 C ANISOU 154 CA ARG A 21 7711 5399 9869 -818 -412 707 C ATOM 155 C ARG A 21 -338.557-147.793 151.922 1.00 63.54 C ANISOU 155 C ARG A 21 8115 5910 10118 -739 -387 786 C ATOM 156 O ARG A 21 -339.630-148.352 152.169 1.00 64.81 O ANISOU 156 O ARG A 21 8303 6104 10216 -632 -425 757 O ATOM 157 CB ARG A 21 -336.833-147.207 153.636 1.00 59.10 C ANISOU 157 CB ARG A 21 7429 5322 9704 -884 -425 611 C ATOM 158 CG ARG A 21 -336.255-146.183 154.593 1.00 62.47 C ANISOU 158 CG ARG A 21 7845 5638 10250 -982 -470 520 C ATOM 159 CD ARG A 21 -335.457-145.134 153.844 1.00 58.20 C ANISOU 159 CD ARG A 21 7298 4990 9827 -1101 -418 607 C ATOM 160 NE ARG A 21 -334.927-144.111 154.736 1.00 69.48 N ANISOU 160 NE ARG A 21 8723 6299 11378 -1205 -465 516 N ATOM 161 CZ ARG A 21 -335.545-142.971 155.017 1.00 73.39 C ANISOU 161 CZ ARG A 21 9312 6614 11958 -1212 -478 482 C ATOM 162 NH1 ARG A 21 -334.983-142.096 155.835 1.00 72.15 N ANISOU 162 NH1 ARG A 21 9157 6351 11906 -1322 -516 384 N ATOM 163 NH2 ARG A 21 -336.726-142.704 154.477 1.00 78.01 N ANISOU 163 NH2 ARG A 21 9984 7116 12539 -1110 -458 547 N ATOM 164 N SER A 22 -337.792-148.110 150.884 1.00 61.40 N ANISOU 164 N SER A 22 7827 5704 9799 -803 -310 877 N ATOM 165 CA SER A 22 -338.162-149.190 149.983 1.00 66.60 C ANISOU 165 CA SER A 22 8513 6481 10312 -753 -271 938 C ATOM 166 C SER A 22 -338.174-150.519 150.734 1.00 64.58 C ANISOU 166 C SER A 22 8181 6362 9995 -675 -290 832 C ATOM 167 O SER A 22 -337.206-150.833 151.446 1.00 56.18 O ANISOU 167 O SER A 22 7013 5345 8987 -710 -286 755 O ATOM 168 CB SER A 22 -337.192-149.256 148.806 1.00 69.91 C ANISOU 168 CB SER A 22 8933 6939 10692 -858 -151 1029 C ATOM 169 OG SER A 22 -337.307-150.490 148.115 1.00 72.20 O ANISOU 169 OG SER A 22 9233 7359 10839 -823 -92 1042 O ATOM 170 N PRO A 23 -339.236-151.324 150.607 1.00 64.33 N ANISOU 170 N PRO A 23 8194 6388 9860 -576 -322 833 N ATOM 171 CA PRO A 23 -339.243-152.646 151.258 1.00 63.92 C ANISOU 171 CA PRO A 23 8079 6460 9749 -508 -336 746 C ATOM 172 C PRO A 23 -338.209-153.605 150.697 1.00 62.32 C ANISOU 172 C PRO A 23 7805 6362 9513 -542 -247 752 C ATOM 173 O PRO A 23 -338.047-154.701 151.247 1.00 64.56 O ANISOU 173 O PRO A 23 8022 6733 9776 -491 -262 687 O ATOM 174 CB PRO A 23 -340.668-153.156 151.005 1.00 56.47 C ANISOU 174 CB PRO A 23 7209 5537 8713 -411 -379 768 C ATOM 175 CG PRO A 23 -341.084-152.465 149.750 1.00 64.38 C ANISOU 175 CG PRO A 23 8303 6470 9688 -445 -368 898 C ATOM 176 CD PRO A 23 -340.446-151.095 149.801 1.00 59.83 C ANISOU 176 CD PRO A 23 7729 5771 9232 -529 -356 928 C ATOM 177 N PHE A 24 -337.509-153.232 149.628 1.00 65.90 N ANISOU 177 N PHE A 24 8271 6799 9968 -629 -147 828 N ATOM 178 CA PHE A 24 -336.390-154.007 149.111 1.00 64.53 C ANISOU 178 CA PHE A 24 8010 6704 9803 -674 -26 817 C ATOM 179 C PHE A 24 -335.041-153.559 149.664 1.00 62.03 C ANISOU 179 C PHE A 24 7553 6362 9653 -753 -3 780 C ATOM 180 O PHE A 24 -334.025-154.181 149.338 1.00 72.03 O ANISOU 180 O PHE A 24 8709 7682 10977 -786 101 763 O ATOM 181 CB PHE A 24 -336.357-153.935 147.575 1.00 52.86 C ANISOU 181 CB PHE A 24 6633 5232 8217 -744 102 911 C ATOM 182 CG PHE A 24 -337.622-154.415 146.910 1.00 58.44 C ANISOU 182 CG PHE A 24 7481 5969 8754 -687 64 958 C ATOM 183 CD1 PHE A 24 -338.038-155.734 147.041 1.00 58.08 C ANISOU 183 CD1 PHE A 24 7419 6015 8634 -602 58 896 C ATOM 184 CD2 PHE A 24 -338.395-153.549 146.146 1.00 55.71 C ANISOU 184 CD2 PHE A 24 7280 5553 8336 -725 21 1073 C ATOM 185 CE1 PHE A 24 -339.205-156.183 146.428 1.00 54.82 C ANISOU 185 CE1 PHE A 24 7129 5629 8071 -562 12 938 C ATOM 186 CE2 PHE A 24 -339.562-153.988 145.531 1.00 65.64 C ANISOU 186 CE2 PHE A 24 8654 6836 9449 -681 -41 1126 C ATOM 187 CZ PHE A 24 -339.966-155.311 145.674 1.00 67.98 C ANISOU 187 CZ PHE A 24 8930 7232 9668 -603 -44 1053 C ATOM 188 N GLU A 25 -334.996-152.523 150.505 1.00 67.98 N ANISOU 188 N GLU A 25 8299 7030 10500 -786 -96 760 N ATOM 189 CA GLU A 25 -333.708-151.926 150.845 1.00 64.59 C ANISOU 189 CA GLU A 25 7748 6563 10231 -890 -78 742 C ATOM 190 C GLU A 25 -333.490-151.706 152.337 1.00 64.95 C ANISOU 190 C GLU A 25 7726 6587 10364 -891 -224 653 C ATOM 191 O GLU A 25 -332.339-151.699 152.782 1.00 74.21 O ANISOU 191 O GLU A 25 8757 7769 11670 -960 -241 623 O ATOM 192 CB GLU A 25 -333.523-150.597 150.106 1.00 55.84 C ANISOU 192 CB GLU A 25 6710 5345 9162 -998 -15 825 C ATOM 193 CG GLU A 25 -333.149-150.742 148.634 1.00 76.44 C ANISOU 193 CG GLU A 25 9357 7980 11709 -1063 158 915 C ATOM 194 CD GLU A 25 -332.700-149.421 148.003 1.00113.70 C ANISOU 194 CD GLU A 25 14126 12586 16487 -1199 224 1004 C ATOM 195 OE1 GLU A 25 -332.974-148.347 148.585 1.00113.50 O ANISOU 195 OE1 GLU A 25 14139 12446 16538 -1220 123 1008 O ATOM 196 OE2 GLU A 25 -332.061-149.455 146.928 1.00131.83 O ANISOU 196 OE2 GLU A 25 16428 14902 18758 -1292 388 1066 O ATOM 197 N ALA A 26 -334.547-151.544 153.127 1.00 60.03 N ANISOU 197 N ALA A 26 7198 5937 9672 -826 -330 606 N ATOM 198 CA ALA A 26 -334.349-151.126 154.508 1.00 56.62 C ANISOU 198 CA ALA A 26 6744 5470 9299 -861 -455 515 C ATOM 199 C ALA A 26 -335.514-151.614 155.352 1.00 57.50 C ANISOU 199 C ALA A 26 6942 5610 9296 -765 -534 449 C ATOM 200 O ALA A 26 -336.622-151.783 154.832 1.00 59.31 O ANISOU 200 O ALA A 26 7261 5836 9438 -681 -497 480 O ATOM 201 CB ALA A 26 -334.210-149.597 154.603 1.00 54.96 C ANISOU 201 CB ALA A 26 6583 5117 9180 -957 -462 514 C ATOM 202 N PRO A 27 -335.299-151.847 156.648 1.00 60.99 N ANISOU 202 N PRO A 27 7363 6078 9734 -786 -646 362 N ATOM 203 CA PRO A 27 -336.363-152.409 157.490 1.00 64.29 C ANISOU 203 CA PRO A 27 7866 6532 10029 -709 -702 296 C ATOM 204 C PRO A 27 -337.553-151.469 157.643 1.00 59.68 C ANISOU 204 C PRO A 27 7412 5842 9423 -682 -675 254 C ATOM 205 O PRO A 27 -337.419-150.245 157.627 1.00 73.90 O ANISOU 205 O PRO A 27 9245 7523 11309 -747 -663 241 O ATOM 206 CB PRO A 27 -335.662-152.651 158.835 1.00 58.82 C ANISOU 206 CB PRO A 27 7136 5875 9336 -781 -833 222 C ATOM 207 CG PRO A 27 -334.440-151.792 158.800 1.00 59.72 C ANISOU 207 CG PRO A 27 7167 5933 9591 -903 -858 231 C ATOM 208 CD PRO A 27 -334.023-151.724 157.368 1.00 53.72 C ANISOU 208 CD PRO A 27 6332 5165 8913 -890 -732 330 C ATOM 209 N GLN A 28 -338.729-152.068 157.806 1.00 62.47 N ANISOU 209 N GLN A 28 7828 6228 9679 -585 -665 233 N ATOM 210 CA GLN A 28 -340.005-151.350 157.840 1.00 63.12 C ANISOU 210 CA GLN A 28 8004 6209 9768 -532 -626 201 C ATOM 211 C GLN A 28 -340.531-151.201 159.260 1.00 66.61 C ANISOU 211 C GLN A 28 8518 6628 10163 -550 -655 61 C ATOM 212 O GLN A 28 -341.698-151.483 159.532 1.00 70.51 O ANISOU 212 O GLN A 28 9061 7120 10608 -474 -621 20 O ATOM 213 CB GLN A 28 -341.024-152.065 156.964 1.00 55.63 C ANISOU 213 CB GLN A 28 7067 5306 8764 -420 -584 274 C ATOM 214 CG GLN A 28 -340.533-152.349 155.560 1.00 60.81 C ANISOU 214 CG GLN A 28 7682 6001 9422 -419 -545 401 C ATOM 215 CD GLN A 28 -340.548-151.116 154.688 1.00 64.64 C ANISOU 215 CD GLN A 28 8202 6361 9998 -455 -512 480 C ATOM 216 OE1 GLN A 28 -341.563-150.430 154.591 1.00 64.39 O ANISOU 216 OE1 GLN A 28 8227 6225 10011 -410 -515 490 O ATOM 217 NE2 GLN A 28 -339.418-150.817 154.057 1.00 68.96 N ANISOU 217 NE2 GLN A 28 8708 6907 10588 -539 -478 540 N ATOM 218 N TYR A 29 -339.691-150.730 160.180 1.00 66.71 N ANISOU 218 N TYR A 29 8541 6618 10186 -662 -713 -17 N ATOM 219 CA TYR A 29 -340.062-150.685 161.590 1.00 66.77 C ANISOU 219 CA TYR A 29 8641 6620 10107 -710 -743 -158 C ATOM 220 C TYR A 29 -341.020-149.549 161.926 1.00 67.75 C ANISOU 220 C TYR A 29 8859 6590 10292 -703 -658 -261 C ATOM 221 O TYR A 29 -341.393-149.404 163.096 1.00 70.73 O ANISOU 221 O TYR A 29 9332 6947 10594 -753 -648 -400 O ATOM 222 CB TYR A 29 -338.805-150.596 162.457 1.00 63.86 C ANISOU 222 CB TYR A 29 8262 6284 9718 -851 -858 -202 C ATOM 223 CG TYR A 29 -337.944-151.839 162.387 1.00 64.92 C ANISOU 223 CG TYR A 29 8294 6562 9809 -849 -952 -117 C ATOM 224 CD1 TYR A 29 -338.521-153.108 162.270 1.00 65.86 C ANISOU 224 CD1 TYR A 29 8404 6786 9835 -750 -942 -74 C ATOM 225 CD2 TYR A 29 -336.559-151.753 162.425 1.00 57.42 C ANISOU 225 CD2 TYR A 29 7246 5632 8940 -946 -1049 -79 C ATOM 226 CE1 TYR A 29 -337.734-154.252 162.204 1.00 57.00 C ANISOU 226 CE1 TYR A 29 7183 5773 8703 -741 -1024 2 C ATOM 227 CE2 TYR A 29 -335.766-152.881 162.356 1.00 53.49 C ANISOU 227 CE2 TYR A 29 6631 5245 8447 -934 -1131 0 C ATOM 228 CZ TYR A 29 -336.354-154.128 162.246 1.00 65.55 C ANISOU 228 CZ TYR A 29 8157 6864 9883 -828 -1117 39 C ATOM 229 OH TYR A 29 -335.551-155.244 162.179 1.00 68.70 O ANISOU 229 OH TYR A 29 8435 7352 10317 -810 -1196 115 O ATOM 230 N TYR A 30 -341.429-148.749 160.944 1.00 70.22 N ANISOU 230 N TYR A 30 9151 6786 10742 -646 -595 -196 N ATOM 231 CA TYR A 30 -342.533-147.819 161.131 1.00 67.93 C ANISOU 231 CA TYR A 30 8924 6338 10549 -601 -508 -275 C ATOM 232 C TYR A 30 -343.884-148.474 160.886 1.00 71.07 C ANISOU 232 C TYR A 30 9312 6765 10928 -466 -451 -257 C ATOM 233 O TYR A 30 -344.910-147.927 161.311 1.00 81.81 O ANISOU 233 O TYR A 30 10710 8010 12365 -422 -369 -352 O ATOM 234 CB TYR A 30 -342.365-146.600 160.213 1.00 64.81 C ANISOU 234 CB TYR A 30 8510 5780 10334 -606 -488 -197 C ATOM 235 CG TYR A 30 -341.940-146.961 158.809 1.00 63.13 C ANISOU 235 CG TYR A 30 8223 5629 10135 -573 -516 -7 C ATOM 236 CD1 TYR A 30 -342.868-147.405 157.874 1.00 62.42 C ANISOU 236 CD1 TYR A 30 8112 5558 10047 -456 -497 101 C ATOM 237 CD2 TYR A 30 -340.606-146.875 158.422 1.00 56.87 C ANISOU 237 CD2 TYR A 30 7383 4875 9349 -670 -555 59 C ATOM 238 CE1 TYR A 30 -342.485-147.747 156.592 1.00 59.68 C ANISOU 238 CE1 TYR A 30 7725 5270 9679 -446 -513 264 C ATOM 239 CE2 TYR A 30 -340.213-147.218 157.140 1.00 59.60 C ANISOU 239 CE2 TYR A 30 7675 5278 9694 -653 -548 217 C ATOM 240 CZ TYR A 30 -341.157-147.652 156.230 1.00 60.92 C ANISOU 240 CZ TYR A 30 7848 5465 9832 -546 -525 316 C ATOM 241 OH TYR A 30 -340.768-147.990 154.955 1.00 66.77 O ANISOU 241 OH TYR A 30 8564 6264 10543 -550 -510 462 O ATOM 242 N LEU A 31 -343.907-149.625 160.205 1.00 67.26 N ANISOU 242 N LEU A 31 8772 6424 10361 -404 -485 -144 N ATOM 243 CA LEU A 31 -345.134-150.407 160.069 1.00 62.51 C ANISOU 243 CA LEU A 31 8158 5870 9724 -293 -446 -133 C ATOM 244 C LEU A 31 -345.428-151.201 161.331 1.00 66.17 C ANISOU 244 C LEU A 31 8672 6423 10045 -318 -429 -256 C ATOM 245 O LEU A 31 -346.592-151.355 161.714 1.00 75.90 O ANISOU 245 O LEU A 31 9921 7630 11287 -258 -353 -323 O ATOM 246 CB LEU A 31 -345.033-151.376 158.887 1.00 61.73 C ANISOU 246 CB LEU A 31 7996 5884 9573 -234 -488 22 C ATOM 247 CG LEU A 31 -344.918-150.853 157.460 1.00 69.51 C ANISOU 247 CG LEU A 31 8951 6810 10649 -211 -502 170 C ATOM 248 CD1 LEU A 31 -344.798-152.030 156.506 1.00 59.36 C ANISOU 248 CD1 LEU A 31 7631 5663 9262 -175 -527 282 C ATOM 249 CD2 LEU A 31 -346.117-149.988 157.109 1.00 78.83 C ANISOU 249 CD2 LEU A 31 10136 7838 11978 -137 -475 189 C ATOM 250 N ALA A 32 -344.391-151.732 161.972 1.00 66.68 N ANISOU 250 N ALA A 32 8758 6590 9986 -409 -502 -277 N ATOM 251 CA ALA A 32 -344.565-152.578 163.142 1.00 57.21 C ANISOU 251 CA ALA A 32 7625 5487 8625 -451 -511 -365 C ATOM 252 C ALA A 32 -343.279-152.553 163.946 1.00 57.88 C ANISOU 252 C ALA A 32 7748 5619 8627 -587 -616 -399 C ATOM 253 O ALA A 32 -342.193-152.355 163.394 1.00 65.47 O ANISOU 253 O ALA A 32 8639 6586 9650 -623 -691 -320 O ATOM 254 CB ALA A 32 -344.928-154.016 162.753 1.00 49.63 C ANISOU 254 CB ALA A 32 6618 4661 7579 -372 -531 -276 C ATOM 255 N GLU A 33 -343.418-152.746 165.254 1.00 54.22 N ANISOU 255 N GLU A 33 7396 5184 8021 -673 -622 -516 N ATOM 256 CA GLU A 33 -342.257-152.827 166.125 1.00 61.49 C ANISOU 256 CA GLU A 33 8364 6158 8840 -817 -757 -541 C ATOM 257 C GLU A 33 -341.398-154.036 165.747 1.00 68.03 C ANISOU 257 C GLU A 33 9092 7120 9636 -796 -888 -397 C ATOM 258 O GLU A 33 -341.900-155.009 165.176 1.00 66.65 O ANISOU 258 O GLU A 33 8862 7013 9450 -688 -859 -318 O ATOM 259 CB GLU A 33 -342.701-152.929 167.582 1.00 69.47 C ANISOU 259 CB GLU A 33 9543 7186 9666 -923 -737 -685 C ATOM 260 CG GLU A 33 -343.304-151.651 168.126 1.00 78.25 C ANISOU 260 CG GLU A 33 10764 8152 10815 -976 -604 -859 C ATOM 261 CD GLU A 33 -342.251-150.606 168.409 1.00101.58 C ANISOU 261 CD GLU A 33 13751 11029 13814 -1109 -686 -912 C ATOM 262 OE1 GLU A 33 -341.485-150.788 169.381 1.00114.72 O ANISOU 262 OE1 GLU A 33 15509 12756 15324 -1263 -815 -953 O ATOM 263 OE2 GLU A 33 -342.175-149.615 167.651 1.00107.21 O ANISOU 263 OE2 GLU A 33 14399 11618 14718 -1068 -636 -903 O ATOM 264 N PRO A 34 -340.092-153.988 166.030 1.00 70.26 N ANISOU 264 N PRO A 34 9337 7431 9928 -899 -1033 -364 N ATOM 265 CA PRO A 34 -339.245-155.169 165.772 1.00 61.38 C ANISOU 265 CA PRO A 34 8100 6417 8804 -876 -1157 -235 C ATOM 266 C PRO A 34 -339.746-156.450 166.428 1.00 61.76 C ANISOU 266 C PRO A 34 8209 6562 8694 -856 -1197 -217 C ATOM 267 O PRO A 34 -339.644-157.521 165.815 1.00 63.93 O ANISOU 267 O PRO A 34 8387 6904 9000 -764 -1215 -111 O ATOM 268 CB PRO A 34 -337.881-154.740 166.327 1.00 53.86 C ANISOU 268 CB PRO A 34 7117 5459 7886 -1019 -1319 -234 C ATOM 269 CG PRO A 34 -337.874-153.257 166.193 1.00 54.70 C ANISOU 269 CG PRO A 34 7261 5443 8081 -1076 -1246 -320 C ATOM 270 CD PRO A 34 -339.296-152.796 166.375 1.00 54.44 C ANISOU 270 CD PRO A 34 7358 5341 7986 -1025 -1083 -430 C ATOM 271 N TRP A 35 -340.292-156.379 167.648 1.00 52.83 N ANISOU 271 N TRP A 35 7245 5436 7391 -947 -1198 -320 N ATOM 272 CA TRP A 35 -340.800-157.589 168.290 1.00 55.60 C ANISOU 272 CA TRP A 35 7670 5876 7581 -942 -1228 -295 C ATOM 273 C TRP A 35 -341.997-158.166 167.543 1.00 64.89 C ANISOU 273 C TRP A 35 8811 7061 8781 -792 -1073 -273 C ATOM 274 O TRP A 35 -342.266-159.370 167.636 1.00 63.76 O ANISOU 274 O TRP A 35 8666 6992 8566 -751 -1102 -206 O ATOM 275 CB TRP A 35 -341.164-157.317 169.753 1.00 59.93 C ANISOU 275 CB TRP A 35 8429 6425 7916 -1094 -1238 -419 C ATOM 276 CG TRP A 35 -342.419-156.508 169.980 1.00 72.51 C ANISOU 276 CG TRP A 35 10133 7938 9477 -1085 -1022 -576 C ATOM 277 CD1 TRP A 35 -342.496-155.161 170.192 1.00 71.12 C ANISOU 277 CD1 TRP A 35 10021 7653 9348 -1149 -940 -712 C ATOM 278 CD2 TRP A 35 -343.766-157.001 170.054 1.00 73.16 C ANISOU 278 CD2 TRP A 35 10266 8032 9499 -1013 -858 -619 C ATOM 279 NE1 TRP A 35 -343.802-154.785 170.378 1.00 71.19 N ANISOU 279 NE1 TRP A 35 10106 7598 9346 -1109 -729 -837 N ATOM 280 CE2 TRP A 35 -344.603-155.893 170.300 1.00 76.01 C ANISOU 280 CE2 TRP A 35 10703 8285 9892 -1027 -675 -782 C ATOM 281 CE3 TRP A 35 -344.346-158.269 169.930 1.00 75.96 C ANISOU 281 CE3 TRP A 35 10599 8468 9794 -938 -844 -536 C ATOM 282 CZ2 TRP A 35 -345.988-156.013 170.419 1.00 72.83 C ANISOU 282 CZ2 TRP A 35 10337 7856 9480 -966 -477 -863 C ATOM 283 CZ3 TRP A 35 -345.723-158.386 170.049 1.00 75.13 C ANISOU 283 CZ3 TRP A 35 10541 8344 9661 -888 -654 -615 C ATOM 284 CH2 TRP A 35 -346.527-157.262 170.290 1.00 71.80 C ANISOU 284 CH2 TRP A 35 10177 7817 9288 -900 -472 -776 C ATOM 285 N GLN A 36 -342.729-157.332 166.806 1.00 68.30 N ANISOU 285 N GLN A 36 9214 7411 9324 -715 -923 -322 N ATOM 286 CA GLN A 36 -343.836-157.834 166.006 1.00 64.43 C ANISOU 286 CA GLN A 36 8675 6926 8879 -578 -803 -289 C ATOM 287 C GLN A 36 -343.350-158.504 164.728 1.00 61.35 C ANISOU 287 C GLN A 36 8139 6577 8596 -477 -843 -151 C ATOM 288 O GLN A 36 -344.018-159.413 164.218 1.00 56.50 O ANISOU 288 O GLN A 36 7491 6005 7970 -388 -801 -99 O ATOM 289 CB GLN A 36 -344.806-156.696 165.697 1.00 58.90 C ANISOU 289 CB GLN A 36 7990 6113 8278 -534 -650 -379 C ATOM 290 CG GLN A 36 -345.530-156.219 166.941 1.00 65.74 C ANISOU 290 CG GLN A 36 9002 6936 9042 -618 -557 -538 C ATOM 291 CD GLN A 36 -346.185-154.869 166.773 1.00 71.08 C ANISOU 291 CD GLN A 36 9685 7465 9858 -593 -421 -644 C ATOM 292 OE1 GLN A 36 -345.780-154.058 165.937 1.00 68.70 O ANISOU 292 OE1 GLN A 36 9306 7085 9710 -558 -438 -600 O ATOM 293 NE2 GLN A 36 -347.209-154.619 167.574 1.00 73.51 N ANISOU 293 NE2 GLN A 36 10083 7724 10123 -616 -276 -784 N ATOM 294 N PHE A 37 -342.202-158.077 164.199 1.00 60.53 N ANISOU 294 N PHE A 37 7949 6456 8594 -500 -911 -98 N ATOM 295 CA PHE A 37 -341.562-158.844 163.136 1.00 59.29 C ANISOU 295 CA PHE A 37 7663 6346 8520 -429 -940 19 C ATOM 296 C PHE A 37 -341.039-160.169 163.672 1.00 57.21 C ANISOU 296 C PHE A 37 7379 6168 8192 -440 -1052 76 C ATOM 297 O PHE A 37 -341.093-161.192 162.980 1.00 55.20 O ANISOU 297 O PHE A 37 7056 5954 7963 -357 -1037 148 O ATOM 298 CB PHE A 37 -340.433-158.032 162.498 1.00 56.06 C ANISOU 298 CB PHE A 37 7163 5892 8246 -466 -964 54 C ATOM 299 CG PHE A 37 -340.902-157.049 161.468 1.00 57.28 C ANISOU 299 CG PHE A 37 7306 5965 8490 -421 -853 58 C ATOM 300 CD1 PHE A 37 -341.321-155.782 161.841 1.00 59.33 C ANISOU 300 CD1 PHE A 37 7640 6127 8776 -465 -811 -24 C ATOM 301 CD2 PHE A 37 -340.928-157.390 160.124 1.00 58.12 C ANISOU 301 CD2 PHE A 37 7340 6086 8656 -343 -793 146 C ATOM 302 CE1 PHE A 37 -341.760-154.873 160.893 1.00 59.58 C ANISOU 302 CE1 PHE A 37 7661 6069 8909 -422 -728 -1 C ATOM 303 CE2 PHE A 37 -341.362-156.483 159.172 1.00 61.16 C ANISOU 303 CE2 PHE A 37 7733 6394 9111 -316 -714 171 C ATOM 304 CZ PHE A 37 -341.779-155.225 159.557 1.00 57.43 C ANISOU 304 CZ PHE A 37 7322 5817 8682 -350 -690 107 C ATOM 305 N SER A 38 -340.541-160.169 164.913 1.00 54.67 N ANISOU 305 N SER A 38 7125 5864 7784 -550 -1172 46 N ATOM 306 CA SER A 38 -340.104-161.410 165.542 1.00 56.45 C ANISOU 306 CA SER A 38 7346 6157 7945 -569 -1303 115 C ATOM 307 C SER A 38 -341.271-162.373 165.712 1.00 62.57 C ANISOU 307 C SER A 38 8198 6970 8606 -511 -1236 116 C ATOM 308 O SER A 38 -341.131-163.579 165.470 1.00 61.14 O ANISOU 308 O SER A 38 7960 6828 8442 -453 -1279 201 O ATOM 309 CB SER A 38 -339.455-161.118 166.896 1.00 50.38 C ANISOU 309 CB SER A 38 6668 5397 7076 -722 -1463 87 C ATOM 310 OG SER A 38 -338.314-160.292 166.758 1.00 68.93 O ANISOU 310 OG SER A 38 8930 7711 9548 -785 -1543 92 O ATOM 311 N MET A 39 -342.431-161.856 166.131 1.00 59.03 N ANISOU 311 N MET A 39 7870 6500 8058 -528 -1121 18 N ATOM 312 CA MET A 39 -343.607-162.708 166.280 1.00 59.85 C ANISOU 312 CA MET A 39 8034 6636 8070 -481 -1039 13 C ATOM 313 C MET A 39 -344.075-163.242 164.934 1.00 55.57 C ANISOU 313 C MET A 39 7381 6095 7638 -343 -957 71 C ATOM 314 O MET A 39 -344.516-164.393 164.839 1.00 59.25 O ANISOU 314 O MET A 39 7844 6600 8067 -297 -953 120 O ATOM 315 CB MET A 39 -344.734-161.952 166.983 1.00 53.63 C ANISOU 315 CB MET A 39 7375 5813 7190 -529 -908 -117 C ATOM 316 CG MET A 39 -344.502-161.749 168.471 1.00 62.49 C ANISOU 316 CG MET A 39 8659 6950 8133 -687 -971 -186 C ATOM 317 SD MET A 39 -344.081-163.282 169.328 1.00 72.64 S ANISOU 317 SD MET A 39 10012 8325 9263 -753 -1136 -75 S ATOM 318 CE MET A 39 -345.466-164.332 168.876 1.00 72.95 C ANISOU 318 CE MET A 39 10037 8387 9294 -644 -989 -54 C ATOM 319 N LEU A 40 -343.981-162.427 163.879 1.00 53.91 N ANISOU 319 N LEU A 40 7092 5839 7554 -289 -895 70 N ATOM 320 CA LEU A 40 -344.236-162.938 162.537 1.00 59.26 C ANISOU 320 CA LEU A 40 7679 6523 8315 -183 -840 134 C ATOM 321 C LEU A 40 -343.280-164.077 162.203 1.00 63.59 C ANISOU 321 C LEU A 40 8147 7116 8900 -158 -920 221 C ATOM 322 O LEU A 40 -343.672-165.064 161.570 1.00 60.66 O ANISOU 322 O LEU A 40 7746 6768 8533 -89 -887 262 O ATOM 323 CB LEU A 40 -344.114-161.809 161.510 1.00 51.51 C ANISOU 323 CB LEU A 40 6645 5481 7444 -156 -781 135 C ATOM 324 CG LEU A 40 -344.128-162.217 160.034 1.00 58.89 C ANISOU 324 CG LEU A 40 7504 6425 8446 -77 -737 208 C ATOM 325 CD1 LEU A 40 -345.418-162.955 159.672 1.00 60.23 C ANISOU 325 CD1 LEU A 40 7698 6615 8571 -11 -684 214 C ATOM 326 CD2 LEU A 40 -343.930-161.006 159.137 1.00 67.07 C ANISOU 326 CD2 LEU A 40 8514 7397 9570 -79 -693 222 C ATOM 327 N ALA A 41 -342.021-163.959 162.633 1.00 60.55 N ANISOU 327 N ALA A 41 7717 6732 8557 -217 -1026 247 N ATOM 328 CA ALA A 41 -341.054-165.026 162.404 1.00 56.94 C ANISOU 328 CA ALA A 41 7159 6297 8177 -189 -1104 328 C ATOM 329 C ALA A 41 -341.385-166.260 163.235 1.00 56.96 C ANISOU 329 C ALA A 41 7219 6334 8089 -192 -1179 362 C ATOM 330 O ALA A 41 -341.234-167.391 162.763 1.00 53.71 O ANISOU 330 O ALA A 41 6745 5928 7735 -125 -1182 419 O ATOM 331 CB ALA A 41 -339.646-164.528 162.718 1.00 53.23 C ANISOU 331 CB ALA A 41 6607 5812 7806 -256 -1214 351 C ATOM 332 N ALA A 42 -341.831-166.062 164.478 1.00 48.42 N ANISOU 332 N ALA A 42 6267 5267 6864 -277 -1231 326 N ATOM 333 CA ALA A 42 -342.224-167.192 165.311 1.00 48.51 C ANISOU 333 CA ALA A 42 6358 5308 6765 -299 -1295 367 C ATOM 334 C ALA A 42 -343.419-167.920 164.711 1.00 58.34 C ANISOU 334 C ALA A 42 7620 6560 7985 -216 -1168 359 C ATOM 335 O ALA A 42 -343.511-169.151 164.779 1.00 66.27 O ANISOU 335 O ALA A 42 8622 7574 8982 -187 -1206 423 O ATOM 336 CB ALA A 42 -342.539-166.712 166.726 1.00 47.16 C ANISOU 336 CB ALA A 42 6352 5154 6415 -429 -1344 314 C ATOM 337 N TYR A 43 -344.344-167.170 164.117 1.00 56.84 N ANISOU 337 N TYR A 43 7443 6358 7797 -181 -1029 288 N ATOM 338 CA TYR A 43 -345.479-167.778 163.435 1.00 62.56 C ANISOU 338 CA TYR A 43 8164 7087 8518 -108 -924 284 C ATOM 339 C TYR A 43 -345.016-168.613 162.247 1.00 60.26 C ANISOU 339 C TYR A 43 7768 6792 8335 -23 -923 346 C ATOM 340 O TYR A 43 -345.498-169.730 162.034 1.00 57.32 O ANISOU 340 O TYR A 43 7400 6428 7951 15 -909 375 O ATOM 341 CB TYR A 43 -346.446-166.680 162.999 1.00 66.30 C ANISOU 341 CB TYR A 43 8649 7534 9008 -88 -804 208 C ATOM 342 CG TYR A 43 -347.705-167.146 162.307 1.00 66.64 C ANISOU 342 CG TYR A 43 8679 7578 9063 -23 -712 204 C ATOM 343 CD1 TYR A 43 -348.439-168.230 162.789 1.00 63.81 C ANISOU 343 CD1 TYR A 43 8365 7247 8634 -31 -700 214 C ATOM 344 CD2 TYR A 43 -348.181-166.472 161.195 1.00 69.07 C ANISOU 344 CD2 TYR A 43 8933 7856 9455 34 -650 196 C ATOM 345 CE1 TYR A 43 -349.604-168.637 162.156 1.00 66.81 C ANISOU 345 CE1 TYR A 43 8720 7624 9039 19 -626 208 C ATOM 346 CE2 TYR A 43 -349.335-166.866 160.561 1.00 71.58 C ANISOU 346 CE2 TYR A 43 9232 8173 9791 83 -595 199 C ATOM 347 CZ TYR A 43 -350.044-167.944 161.041 1.00 73.29 C ANISOU 347 CZ TYR A 43 9479 8418 9949 76 -581 201 C ATOM 348 OH TYR A 43 -351.191-168.310 160.386 1.00 71.90 O ANISOU 348 OH TYR A 43 9273 8240 9807 116 -536 204 O ATOM 349 N MET A 44 -344.075-168.083 161.461 1.00 61.72 N ANISOU 349 N MET A 44 7864 6959 8627 -1 -925 359 N ATOM 350 CA MET A 44 -343.521-168.850 160.349 1.00 61.80 C ANISOU 350 CA MET A 44 7782 6962 8738 65 -899 401 C ATOM 351 C MET A 44 -342.805-170.097 160.852 1.00 63.27 C ANISOU 351 C MET A 44 7930 7142 8968 74 -993 461 C ATOM 352 O MET A 44 -342.868-171.157 160.218 1.00 62.91 O ANISOU 352 O MET A 44 7850 7082 8970 132 -957 482 O ATOM 353 CB MET A 44 -342.573-167.985 159.521 1.00 64.50 C ANISOU 353 CB MET A 44 8040 7283 9183 66 -867 400 C ATOM 354 CG MET A 44 -343.220-166.800 158.836 1.00 79.71 C ANISOU 354 CG MET A 44 10001 9198 11089 64 -783 364 C ATOM 355 SD MET A 44 -344.486-167.273 157.653 1.00 96.71 S ANISOU 355 SD MET A 44 12191 11359 13197 124 -688 363 S ATOM 356 CE MET A 44 -345.938-166.788 158.569 1.00 74.44 C ANISOU 356 CE MET A 44 9454 8536 10294 108 -688 318 C ATOM 357 N PHE A 45 -342.122-169.989 161.995 1.00 61.24 N ANISOU 357 N PHE A 45 7683 6887 8700 11 -1122 491 N ATOM 358 CA PHE A 45 -341.433-171.142 162.562 1.00 60.17 C ANISOU 358 CA PHE A 45 7509 6733 8621 15 -1245 570 C ATOM 359 C PHE A 45 -342.424-172.229 162.966 1.00 61.33 C ANISOU 359 C PHE A 45 7750 6885 8668 23 -1241 592 C ATOM 360 O PHE A 45 -342.199-173.413 162.691 1.00 60.24 O ANISOU 360 O PHE A 45 7563 6711 8616 78 -1260 644 O ATOM 361 CB PHE A 45 -340.579-170.701 163.755 1.00 53.79 C ANISOU 361 CB PHE A 45 6711 5929 7798 -76 -1415 609 C ATOM 362 CG PHE A 45 -339.730-171.798 164.342 1.00 54.63 C ANISOU 362 CG PHE A 45 6760 6005 7994 -75 -1581 715 C ATOM 363 CD1 PHE A 45 -338.702-172.372 163.606 1.00 53.74 C ANISOU 363 CD1 PHE A 45 6469 5840 8110 3 -1591 760 C ATOM 364 CD2 PHE A 45 -339.947-172.242 165.638 1.00 59.67 C ANISOU 364 CD2 PHE A 45 7520 6655 8495 -158 -1724 774 C ATOM 365 CE1 PHE A 45 -337.914-173.380 164.150 1.00 55.43 C ANISOU 365 CE1 PHE A 45 6608 6005 8449 16 -1755 867 C ATOM 366 CE2 PHE A 45 -339.161-173.247 166.190 1.00 64.67 C ANISOU 366 CE2 PHE A 45 8102 7248 9223 -159 -1905 896 C ATOM 367 CZ PHE A 45 -338.141-173.813 165.445 1.00 49.99 C ANISOU 367 CZ PHE A 45 6044 5326 7626 -65 -1928 945 C ATOM 368 N LEU A 46 -343.535-171.840 163.596 1.00 62.71 N ANISOU 368 N LEU A 46 8055 7094 8679 -32 -1201 547 N ATOM 369 CA LEU A 46 -344.573-172.801 163.960 1.00 62.80 C ANISOU 369 CA LEU A 46 8155 7111 8596 -36 -1173 561 C ATOM 370 C LEU A 46 -345.112-173.521 162.729 1.00 65.77 C ANISOU 370 C LEU A 46 8475 7467 9046 54 -1067 548 C ATOM 371 O LEU A 46 -345.256-174.751 162.727 1.00 60.33 O ANISOU 371 O LEU A 46 7790 6751 8380 78 -1087 595 O ATOM 372 CB LEU A 46 -345.704-172.085 164.702 1.00 61.83 C ANISOU 372 CB LEU A 46 8158 7023 8312 -110 -1103 491 C ATOM 373 CG LEU A 46 -346.889-172.920 165.189 1.00 59.41 C ANISOU 373 CG LEU A 46 7946 6727 7899 -137 -1049 494 C ATOM 374 CD1 LEU A 46 -346.449-173.830 166.312 1.00 59.12 C ANISOU 374 CD1 LEU A 46 7991 6687 7785 -210 -1184 586 C ATOM 375 CD2 LEU A 46 -348.024-172.026 165.645 1.00 58.16 C ANISOU 375 CD2 LEU A 46 7869 6593 7636 -190 -927 397 C ATOM 376 N LEU A 47 -345.410-172.766 161.666 1.00 50.08 N ANISOU 376 N LEU A 47 6446 5489 7095 95 -961 488 N ATOM 377 CA LEU A 47 -345.948-173.366 160.449 1.00 49.39 C ANISOU 377 CA LEU A 47 6328 5389 7050 159 -870 471 C ATOM 378 C LEU A 47 -344.943-174.308 159.791 1.00 60.62 C ANISOU 378 C LEU A 47 7665 6767 8600 213 -884 505 C ATOM 379 O LEU A 47 -345.331-175.351 159.255 1.00 61.07 O ANISOU 379 O LEU A 47 7726 6798 8679 248 -844 505 O ATOM 380 CB LEU A 47 -346.376-172.270 159.475 1.00 59.24 C ANISOU 380 CB LEU A 47 7560 6651 8298 174 -782 418 C ATOM 381 CG LEU A 47 -347.518-171.364 159.943 1.00 61.58 C ANISOU 381 CG LEU A 47 7917 6968 8514 140 -745 374 C ATOM 382 CD1 LEU A 47 -347.653-170.164 159.019 1.00 57.27 C ANISOU 382 CD1 LEU A 47 7342 6414 8004 158 -692 346 C ATOM 383 CD2 LEU A 47 -348.820-172.138 160.006 1.00 54.88 C ANISOU 383 CD2 LEU A 47 7109 6126 7616 142 -705 364 C ATOM 384 N ILE A 48 -343.653-173.959 159.811 1.00 58.31 N ANISOU 384 N ILE A 48 7287 6457 8412 219 -932 528 N ATOM 385 CA ILE A 48 -342.641-174.844 159.236 1.00 55.67 C ANISOU 385 CA ILE A 48 6847 6065 8239 276 -927 552 C ATOM 386 C ILE A 48 -342.530-176.128 160.050 1.00 60.83 C ANISOU 386 C ILE A 48 7509 6672 8933 286 -1029 622 C ATOM 387 O ILE A 48 -342.501-177.231 159.492 1.00 57.95 O ANISOU 387 O ILE A 48 7114 6250 8655 339 -985 623 O ATOM 388 CB ILE A 48 -341.282-174.122 159.137 1.00 58.67 C ANISOU 388 CB ILE A 48 7110 6433 8748 274 -955 563 C ATOM 389 CG1 ILE A 48 -341.350-172.967 158.137 1.00 56.65 C ANISOU 389 CG1 ILE A 48 6849 6208 8466 264 -836 503 C ATOM 390 CG2 ILE A 48 -340.169-175.108 158.759 1.00 46.25 C ANISOU 390 CG2 ILE A 48 5403 4786 7385 335 -955 591 C ATOM 391 CD1 ILE A 48 -340.255-171.930 158.348 1.00 54.87 C ANISOU 391 CD1 ILE A 48 6539 5983 8325 228 -878 513 C ATOM 392 N MET A 49 -342.494-176.008 161.381 1.00 63.21 N ANISOU 392 N MET A 49 7865 6989 9161 224 -1166 682 N ATOM 393 CA MET A 49 -342.248-177.167 162.230 1.00 63.98 C ANISOU 393 CA MET A 49 7977 7035 9298 219 -1294 777 C ATOM 394 C MET A 49 -343.420-178.145 162.232 1.00 70.06 C ANISOU 394 C MET A 49 8845 7791 9982 221 -1241 776 C ATOM 395 O MET A 49 -343.210-179.353 162.383 1.00 70.26 O ANISOU 395 O MET A 49 8855 7742 10098 251 -1296 841 O ATOM 396 CB MET A 49 -341.940-176.704 163.655 1.00 64.47 C ANISOU 396 CB MET A 49 8104 7127 9263 125 -1463 845 C ATOM 397 CG MET A 49 -340.623-175.956 163.805 1.00 70.38 C ANISOU 397 CG MET A 49 8740 7871 10129 113 -1563 868 C ATOM 398 SD MET A 49 -339.167-176.999 163.578 1.00 77.75 S ANISOU 398 SD MET A 49 9477 8697 11369 195 -1673 965 S ATOM 399 CE MET A 49 -338.777-176.714 161.851 1.00 75.08 C ANISOU 399 CE MET A 49 8990 8338 11200 294 -1449 855 C ATOM 400 N LEU A 50 -344.651-177.654 162.081 1.00 63.89 N ANISOU 400 N LEU A 50 8156 7071 9049 188 -1140 708 N ATOM 401 CA LEU A 50 -345.798-178.540 161.946 1.00 60.99 C ANISOU 401 CA LEU A 50 7860 6691 8621 186 -1078 699 C ATOM 402 C LEU A 50 -346.104-178.888 160.493 1.00 67.71 C ANISOU 402 C LEU A 50 8663 7520 9545 252 -953 629 C ATOM 403 O LEU A 50 -346.588-179.989 160.217 1.00 84.97 O ANISOU 403 O LEU A 50 10872 9658 11755 267 -926 633 O ATOM 404 CB LEU A 50 -347.047-177.911 162.575 1.00 56.71 C ANISOU 404 CB LEU A 50 7428 6219 7902 111 -1031 661 C ATOM 405 CG LEU A 50 -346.989-177.506 164.049 1.00 59.66 C ANISOU 405 CG LEU A 50 7896 6625 8147 14 -1120 704 C ATOM 406 CD1 LEU A 50 -348.323-176.943 164.503 1.00 53.71 C ANISOU 406 CD1 LEU A 50 7237 5926 7245 -52 -1019 639 C ATOM 407 CD2 LEU A 50 -346.575-178.671 164.924 1.00 63.54 C ANISOU 407 CD2 LEU A 50 8436 7065 8640 -19 -1251 820 C ATOM 408 N GLY A 51 -345.824-177.979 159.566 1.00 67.46 N ANISOU 408 N GLY A 51 8577 7517 9537 278 -880 567 N ATOM 409 CA GLY A 51 -346.232-178.158 158.188 1.00 60.71 C ANISOU 409 CA GLY A 51 7712 6656 8698 312 -765 499 C ATOM 410 C GLY A 51 -345.341-179.062 157.368 1.00 60.84 C ANISOU 410 C GLY A 51 7659 6596 8861 369 -720 484 C ATOM 411 O GLY A 51 -345.836-179.800 156.513 1.00 67.07 O ANISOU 411 O GLY A 51 8477 7355 9650 381 -643 436 O ATOM 412 N PHE A 52 -344.021-179.010 157.594 1.00 59.97 N ANISOU 412 N PHE A 52 7451 6447 8889 401 -761 517 N ATOM 413 CA PHE A 52 -343.141-179.901 156.838 1.00 66.34 C ANISOU 413 CA PHE A 52 8171 7162 9873 463 -695 492 C ATOM 414 C PHE A 52 -343.326-181.364 157.221 1.00 66.85 C ANISOU 414 C PHE A 52 8252 7133 10014 490 -737 531 C ATOM 415 O PHE A 52 -343.538-182.190 156.316 1.00 66.75 O ANISOU 415 O PHE A 52 8254 7062 10046 516 -631 464 O ATOM 416 CB PHE A 52 -341.676-179.474 156.978 1.00 57.68 C ANISOU 416 CB PHE A 52 6934 6037 8945 494 -725 520 C ATOM 417 CG PHE A 52 -340.714-180.483 156.408 1.00 60.53 C ANISOU 417 CG PHE A 52 7178 6281 9537 566 -657 499 C ATOM 418 CD1 PHE A 52 -340.569-180.622 155.038 1.00 67.27 C ANISOU 418 CD1 PHE A 52 8021 7113 10427 585 -466 391 C ATOM 419 CD2 PHE A 52 -339.994-181.326 157.238 1.00 69.96 C ANISOU 419 CD2 PHE A 52 8283 7380 10916 609 -781 587 C ATOM 420 CE1 PHE A 52 -339.703-181.568 154.503 1.00 71.58 C ANISOU 420 CE1 PHE A 52 8460 7539 11200 651 -371 349 C ATOM 421 CE2 PHE A 52 -339.122-182.270 156.709 1.00 73.43 C ANISOU 421 CE2 PHE A 52 8597 7691 11611 687 -708 562 C ATOM 422 CZ PHE A 52 -338.979-182.390 155.340 1.00 72.00 C ANISOU 422 CZ PHE A 52 8399 7484 11473 710 -487 432 C ATOM 423 N PRO A 53 -343.249-181.766 158.498 1.00 65.10 N ANISOU 423 N PRO A 53 8042 6886 9806 475 -889 636 N ATOM 424 CA PRO A 53 -343.327-183.211 158.791 1.00 69.96 C ANISOU 424 CA PRO A 53 8669 7390 10521 503 -930 685 C ATOM 425 C PRO A 53 -344.636-183.844 158.349 1.00 67.61 C ANISOU 425 C PRO A 53 8486 7095 10109 473 -849 631 C ATOM 426 O PRO A 53 -344.621-184.899 157.708 1.00 68.92 O ANISOU 426 O PRO A 53 8642 7160 10382 512 -781 591 O ATOM 427 CB PRO A 53 -343.141-183.273 160.317 1.00 62.37 C ANISOU 427 CB PRO A 53 7736 6428 9532 460 -1125 823 C ATOM 428 CG PRO A 53 -342.547-181.970 160.700 1.00 62.50 C ANISOU 428 CG PRO A 53 7712 6530 9505 431 -1182 834 C ATOM 429 CD PRO A 53 -343.092-180.975 159.732 1.00 59.28 C ANISOU 429 CD PRO A 53 7326 6211 8986 421 -1030 716 C ATOM 430 N ILE A 54 -345.771-183.213 158.659 1.00 68.39 N ANISOU 430 N ILE A 54 8682 7295 10006 403 -850 622 N ATOM 431 CA ILE A 54 -347.072-183.768 158.290 1.00 69.15 C ANISOU 431 CA ILE A 54 8869 7398 10008 365 -788 578 C ATOM 432 C ILE A 54 -347.170-183.969 156.783 1.00 67.22 C ANISOU 432 C ILE A 54 8615 7133 9794 392 -656 465 C ATOM 433 O ILE A 54 -347.643-185.010 156.311 1.00 71.37 O ANISOU 433 O ILE A 54 9181 7589 10349 387 -612 428 O ATOM 434 CB ILE A 54 -348.199-182.861 158.817 1.00 77.27 C ANISOU 434 CB ILE A 54 9969 8540 10851 293 -795 578 C ATOM 435 CG1 ILE A 54 -348.158-182.798 160.343 1.00 82.26 C ANISOU 435 CG1 ILE A 54 10646 9186 11422 243 -906 678 C ATOM 436 CG2 ILE A 54 -349.561-183.354 158.341 1.00 86.32 C ANISOU 436 CG2 ILE A 54 11178 9694 11926 252 -733 530 C ATOM 437 CD1 ILE A 54 -349.258-181.950 160.949 1.00 87.74 C ANISOU 437 CD1 ILE A 54 11411 9978 11950 168 -883 661 C ATOM 438 N ASN A 55 -346.727-182.986 156.001 1.00 63.35 N ANISOU 438 N ASN A 55 8085 6699 9286 405 -592 407 N ATOM 439 CA ASN A 55 -346.865-183.104 154.553 1.00 62.15 C ANISOU 439 CA ASN A 55 7955 6539 9119 404 -467 301 C ATOM 440 C ASN A 55 -345.791-184.002 153.953 1.00 64.13 C ANISOU 440 C ASN A 55 8146 6673 9548 462 -383 252 C ATOM 441 O ASN A 55 -346.057-184.722 152.984 1.00 66.52 O ANISOU 441 O ASN A 55 8500 6923 9851 450 -284 162 O ATOM 442 CB ASN A 55 -346.839-181.720 153.906 1.00 61.66 C ANISOU 442 CB ASN A 55 7892 6576 8960 382 -425 267 C ATOM 443 CG ASN A 55 -348.102-180.930 154.182 1.00 68.57 C ANISOU 443 CG ASN A 55 8827 7545 9683 328 -477 288 C ATOM 444 OD1 ASN A 55 -349.141-181.172 153.571 1.00 76.43 O ANISOU 444 OD1 ASN A 55 9886 8557 10598 288 -459 251 O ATOM 445 ND2 ASN A 55 -348.018-179.979 155.105 1.00 66.46 N ANISOU 445 ND2 ASN A 55 8533 7331 9389 324 -542 342 N ATOM 446 N PHE A 56 -344.574-183.970 154.499 1.00 63.49 N ANISOU 446 N PHE A 56 7952 6540 9630 520 -420 304 N ATOM 447 CA PHE A 56 -343.557-184.903 154.031 1.00 63.48 C ANISOU 447 CA PHE A 56 7866 6403 9850 587 -337 260 C ATOM 448 C PHE A 56 -343.926-186.336 154.395 1.00 73.73 C ANISOU 448 C PHE A 56 9198 7578 11238 605 -373 283 C ATOM 449 O PHE A 56 -343.748-187.252 153.584 1.00 73.06 O ANISOU 449 O PHE A 56 9116 7384 11260 631 -253 191 O ATOM 450 CB PHE A 56 -342.186-184.547 154.604 1.00 58.43 C ANISOU 450 CB PHE A 56 7070 5729 9400 646 -392 326 C ATOM 451 CG PHE A 56 -341.105-185.497 154.186 1.00 66.88 C ANISOU 451 CG PHE A 56 8018 6642 10750 728 -304 285 C ATOM 452 CD1 PHE A 56 -340.458-185.338 152.972 1.00 69.00 C ANISOU 452 CD1 PHE A 56 8238 6888 11092 743 -102 157 C ATOM 453 CD2 PHE A 56 -340.754-186.568 154.993 1.00 70.59 C ANISOU 453 CD2 PHE A 56 8426 6978 11418 785 -413 372 C ATOM 454 CE1 PHE A 56 -339.470-186.221 152.576 1.00 74.70 C ANISOU 454 CE1 PHE A 56 8834 7452 12097 821 11 101 C ATOM 455 CE2 PHE A 56 -339.772-187.456 154.602 1.00 73.66 C ANISOU 455 CE2 PHE A 56 8683 7200 12105 871 -327 332 C ATOM 456 CZ PHE A 56 -339.126-187.281 153.392 1.00 76.41 C ANISOU 456 CZ PHE A 56 8968 7523 12542 893 -103 186 C ATOM 457 N LEU A 57 -344.449-186.546 155.607 1.00 73.49 N ANISOU 457 N LEU A 57 9204 7557 11159 582 -529 402 N ATOM 458 CA LEU A 57 -344.824-187.890 156.031 1.00 70.42 C ANISOU 458 CA LEU A 57 8858 7047 10853 588 -575 445 C ATOM 459 C LEU A 57 -345.949-188.452 155.174 1.00 72.77 C ANISOU 459 C LEU A 57 9270 7339 11041 535 -474 342 C ATOM 460 O LEU A 57 -346.012-189.666 154.948 1.00 70.07 O ANISOU 460 O LEU A 57 8948 6860 10816 551 -438 313 O ATOM 461 CB LEU A 57 -345.229-187.885 157.505 1.00 72.72 C ANISOU 461 CB LEU A 57 9193 7368 11069 546 -752 597 C ATOM 462 CG LEU A 57 -345.520-189.249 158.132 1.00 93.09 C ANISOU 462 CG LEU A 57 11818 9813 13738 542 -825 679 C ATOM 463 CD1 LEU A 57 -344.258-190.108 158.168 1.00 91.20 C ANISOU 463 CD1 LEU A 57 11459 9397 13798 640 -857 722 C ATOM 464 CD2 LEU A 57 -346.114-189.094 159.523 1.00101.53 C ANISOU 464 CD2 LEU A 57 12972 10945 14660 464 -974 819 C ATOM 465 N THR A 58 -346.850-187.592 154.693 1.00 72.47 N ANISOU 465 N THR A 58 9303 7439 10792 467 -440 288 N ATOM 466 CA THR A 58 -347.866-188.047 153.750 1.00 69.12 C ANISOU 466 CA THR A 58 8979 7017 10268 407 -361 188 C ATOM 467 C THR A 58 -347.224-188.650 152.508 1.00 68.93 C ANISOU 467 C THR A 58 8953 6894 10343 434 -210 54 C ATOM 468 O THR A 58 -347.657-189.699 152.021 1.00 78.86 O ANISOU 468 O THR A 58 10278 8056 11630 408 -157 -16 O ATOM 469 CB THR A 58 -348.788-186.885 153.372 1.00 64.21 C ANISOU 469 CB THR A 58 8409 6554 9434 339 -366 165 C ATOM 470 OG1 THR A 58 -349.572-186.509 154.508 1.00 63.07 O ANISOU 470 OG1 THR A 58 8277 6480 9209 304 -474 264 O ATOM 471 CG2 THR A 58 -349.713-187.274 152.223 1.00 58.04 C ANISOU 471 CG2 THR A 58 7723 5777 8555 268 -301 61 C ATOM 472 N LEU A 59 -346.183-188.004 151.986 1.00 74.02 N ANISOU 472 N LEU A 59 9526 7554 11043 477 -126 10 N ATOM 473 CA LEU A 59 -345.474-188.560 150.842 1.00 77.42 C ANISOU 473 CA LEU A 59 9953 7886 11578 498 51 -129 C ATOM 474 C LEU A 59 -344.682-189.803 151.228 1.00 82.36 C ANISOU 474 C LEU A 59 10493 8316 12484 584 72 -123 C ATOM 475 O LEU A 59 -344.516-190.714 150.408 1.00 83.00 O ANISOU 475 O LEU A 59 10608 8273 12657 589 215 -249 O ATOM 476 CB LEU A 59 -344.547-187.505 150.240 1.00 72.94 C ANISOU 476 CB LEU A 59 9321 7385 11006 513 150 -172 C ATOM 477 CG LEU A 59 -345.203-186.170 149.873 1.00 76.28 C ANISOU 477 CG LEU A 59 9817 7985 11180 436 119 -159 C ATOM 478 CD1 LEU A 59 -344.194-185.213 149.257 1.00 71.61 C ANISOU 478 CD1 LEU A 59 9166 7439 10603 445 229 -198 C ATOM 479 CD2 LEU A 59 -346.386-186.396 148.933 1.00 72.92 C ANISOU 479 CD2 LEU A 59 9553 7600 10553 336 149 -241 C ATOM 480 N TYR A 60 -344.193-189.864 152.467 1.00 78.63 N ANISOU 480 N TYR A 60 9917 7806 12152 648 -73 24 N ATOM 481 CA TYR A 60 -343.299-190.951 152.846 1.00 79.46 C ANISOU 481 CA TYR A 60 9916 7714 12563 742 -76 55 C ATOM 482 C TYR A 60 -344.064-192.251 153.063 1.00 87.39 C ANISOU 482 C TYR A 60 11009 8591 13604 722 -110 64 C ATOM 483 O TYR A 60 -343.635-193.316 152.605 1.00 86.95 O ANISOU 483 O TYR A 60 10927 8351 13759 772 -6 -16 O ATOM 484 CB TYR A 60 -342.506-190.575 154.096 1.00 74.79 C ANISOU 484 CB TYR A 60 9191 7123 12102 801 -253 227 C ATOM 485 CG TYR A 60 -341.474-191.618 154.451 1.00 86.73 C ANISOU 485 CG TYR A 60 10565 8422 13968 907 -278 277 C ATOM 486 CD1 TYR A 60 -340.356-191.809 153.651 1.00 92.23 C ANISOU 486 CD1 TYR A 60 11122 9006 14916 988 -110 167 C ATOM 487 CD2 TYR A 60 -341.624-192.424 155.569 1.00 89.93 C ANISOU 487 CD2 TYR A 60 10975 8726 14469 922 -464 435 C ATOM 488 CE1 TYR A 60 -339.413-192.766 153.958 1.00 96.51 C ANISOU 488 CE1 TYR A 60 11510 9332 15825 1096 -131 211 C ATOM 489 CE2 TYR A 60 -340.682-193.384 155.886 1.00 95.45 C ANISOU 489 CE2 TYR A 60 11538 9211 15517 1024 -508 497 C ATOM 490 CZ TYR A 60 -339.579-193.551 155.076 1.00 98.77 C ANISOU 490 CZ TYR A 60 11798 9514 16214 1118 -343 383 C ATOM 491 OH TYR A 60 -338.637-194.506 155.384 1.00104.94 O ANISOU 491 OH TYR A 60 12419 10064 17388 1231 -386 445 O ATOM 492 N VAL A 61 -345.198-192.190 153.766 1.00 81.92 N ANISOU 492 N VAL A 61 10418 7983 12723 646 -242 155 N ATOM 493 CA VAL A 61 -345.951-193.412 154.032 1.00 72.20 C ANISOU 493 CA VAL A 61 9273 6633 11529 614 -278 176 C ATOM 494 C VAL A 61 -346.547-193.972 152.748 1.00 79.50 C ANISOU 494 C VAL A 61 10301 7514 12393 558 -117 -9 C ATOM 495 O VAL A 61 -346.746-195.187 152.627 1.00 90.11 O ANISOU 495 O VAL A 61 11686 8690 13861 557 -85 -46 O ATOM 496 CB VAL A 61 -347.036-193.165 155.097 1.00 73.91 C ANISOU 496 CB VAL A 61 9569 6957 11556 532 -434 312 C ATOM 497 CG1 VAL A 61 -346.402-192.641 156.376 1.00 81.97 C ANISOU 497 CG1 VAL A 61 10515 8015 12613 567 -594 485 C ATOM 498 CG2 VAL A 61 -348.106-192.208 154.575 1.00 72.44 C ANISOU 498 CG2 VAL A 61 9466 6964 11096 439 -399 243 C ATOM 499 N THR A 62 -346.835-193.113 151.771 1.00 82.30 N ANISOU 499 N THR A 62 10707 8008 12554 501 -22 -123 N ATOM 500 CA THR A 62 -347.313-193.600 150.483 1.00 85.61 C ANISOU 500 CA THR A 62 11241 8391 12894 431 123 -302 C ATOM 501 C THR A 62 -346.257-194.454 149.791 1.00 88.16 C ANISOU 501 C THR A 62 11521 8521 13454 501 299 -434 C ATOM 502 O THR A 62 -346.594-195.353 149.011 1.00 97.42 O ANISOU 502 O THR A 62 12793 9583 14638 452 409 -574 O ATOM 503 CB THR A 62 -347.731-192.410 149.612 1.00 77.64 C ANISOU 503 CB THR A 62 10300 7574 11628 352 165 -371 C ATOM 504 OG1 THR A 62 -348.758-191.676 150.288 1.00 78.71 O ANISOU 504 OG1 THR A 62 10458 7862 11585 297 9 -254 O ATOM 505 CG2 THR A 62 -348.264-192.865 148.260 1.00 75.05 C ANISOU 505 CG2 THR A 62 10117 7222 11176 252 290 -549 C ATOM 506 N VAL A 63 -344.979-194.211 150.089 1.00 76.16 N ANISOU 506 N VAL A 63 9845 6947 12144 613 330 -396 N ATOM 507 CA VAL A 63 -343.911-195.019 149.508 1.00 78.10 C ANISOU 507 CA VAL A 63 10012 6991 12671 695 512 -520 C ATOM 508 C VAL A 63 -343.823-196.379 150.197 1.00 82.85 C ANISOU 508 C VAL A 63 10573 7363 13542 762 447 -457 C ATOM 509 O VAL A 63 -343.440-197.377 149.572 1.00 80.87 O ANISOU 509 O VAL A 63 10324 6913 13491 795 608 -596 O ATOM 510 CB VAL A 63 -342.577-194.246 149.580 1.00 74.19 C ANISOU 510 CB VAL A 63 9338 6516 12336 789 564 -496 C ATOM 511 CG1 VAL A 63 -341.408-195.123 149.167 1.00 67.93 C ANISOU 511 CG1 VAL A 63 8416 5490 11905 894 746 -604 C ATOM 512 CG2 VAL A 63 -342.640-193.006 148.708 1.00 72.10 C ANISOU 512 CG2 VAL A 63 9134 6447 11813 711 665 -580 C ATOM 513 N GLN A 64 -344.208-196.457 151.469 1.00 85.62 N ANISOU 513 N GLN A 64 10904 7731 13895 771 220 -252 N ATOM 514 CA GLN A 64 -344.022-197.661 152.268 1.00 95.15 C ANISOU 514 CA GLN A 64 12067 8720 15367 835 125 -146 C ATOM 515 C GLN A 64 -345.280-198.512 152.414 1.00 93.83 C ANISOU 515 C GLN A 64 12058 8505 15086 738 70 -138 C ATOM 516 O GLN A 64 -345.234-199.537 153.101 1.00100.29 O ANISOU 516 O GLN A 64 12861 9138 16106 775 -17 -36 O ATOM 517 CB GLN A 64 -343.497-197.285 153.656 1.00 99.76 C ANISOU 517 CB GLN A 64 12530 9329 16044 898 -101 94 C ATOM 518 CG GLN A 64 -342.018-196.945 153.679 1.00107.02 C ANISOU 518 CG GLN A 64 13244 10187 17233 1022 -72 110 C ATOM 519 CD GLN A 64 -341.444-196.937 155.084 1.00106.95 C ANISOU 519 CD GLN A 64 13120 10137 17378 1082 -326 357 C ATOM 520 OE1 GLN A 64 -340.245-196.731 155.273 1.00109.76 O ANISOU 520 OE1 GLN A 64 13289 10429 17986 1182 -352 405 O ATOM 521 NE2 GLN A 64 -342.298-197.165 156.077 1.00 99.18 N ANISOU 521 NE2 GLN A 64 12251 9190 16241 1010 -516 518 N ATOM 522 N HIS A 65 -346.396-198.127 151.795 1.00 77.39 N ANISOU 522 N HIS A 65 10123 6578 12704 611 109 -231 N ATOM 523 CA HIS A 65 -347.649-198.870 151.936 1.00 76.49 C ANISOU 523 CA HIS A 65 10146 6433 12484 505 51 -221 C ATOM 524 C HIS A 65 -348.348-198.925 150.585 1.00 90.87 C ANISOU 524 C HIS A 65 12102 8298 14125 396 198 -437 C ATOM 525 O HIS A 65 -348.836-197.901 150.098 1.00 91.37 O ANISOU 525 O HIS A 65 12214 8571 13933 324 201 -477 O ATOM 526 CB HIS A 65 -348.552-198.234 152.993 1.00 69.90 C ANISOU 526 CB HIS A 65 9340 5775 11443 436 -135 -42 C ATOM 527 CG HIS A 65 -347.945-198.198 154.362 1.00 76.53 C ANISOU 527 CG HIS A 65 10086 6579 12411 510 -295 175 C ATOM 528 ND1 HIS A 65 -348.312-199.071 155.364 1.00 80.22 N ANISOU 528 ND1 HIS A 65 10589 6930 12959 488 -421 327 N ATOM 529 CD2 HIS A 65 -346.994-197.394 154.893 1.00 78.72 C ANISOU 529 CD2 HIS A 65 10245 6922 12742 591 -361 269 C ATOM 530 CE1 HIS A 65 -347.614-198.805 156.454 1.00 83.06 C ANISOU 530 CE1 HIS A 65 10870 7289 13401 548 -566 511 C ATOM 531 NE2 HIS A 65 -346.807-197.792 156.195 1.00 85.09 N ANISOU 531 NE2 HIS A 65 11027 7655 13647 612 -537 476 N ATOM 532 N LYS A 66 -348.418-200.124 149.993 1.00 96.44 N ANISOU 532 N LYS A 66 12878 8801 14965 376 307 -570 N ATOM 533 CA LYS A 66 -348.971-200.257 148.648 1.00 94.89 C ANISOU 533 CA LYS A 66 12827 8627 14598 260 449 -791 C ATOM 534 C LYS A 66 -350.456-199.920 148.609 1.00 86.21 C ANISOU 534 C LYS A 66 11844 7700 13210 106 328 -761 C ATOM 535 O LYS A 66 -350.961-199.453 147.581 1.00 86.41 O ANISOU 535 O LYS A 66 11975 7848 13011 -1 382 -892 O ATOM 536 CB LYS A 66 -348.735-201.674 148.112 1.00100.93 C ANISOU 536 CB LYS A 66 13649 9116 15583 265 591 -946 C ATOM 537 CG LYS A 66 -349.070-201.837 146.627 1.00109.28 C ANISOU 537 CG LYS A 66 14872 10178 16472 140 768 -1207 C ATOM 538 CD LYS A 66 -348.635-203.190 146.084 1.00116.32 C ANISOU 538 CD LYS A 66 15811 10775 17609 159 947 -1387 C ATOM 539 CE LYS A 66 -348.684-203.219 144.557 1.00120.38 C ANISOU 539 CE LYS A 66 16494 11298 17946 38 1161 -1669 C ATOM 540 NZ LYS A 66 -347.678-202.305 143.931 1.00118.07 N ANISOU 540 NZ LYS A 66 16147 11103 17610 91 1325 -1753 N ATOM 541 N LYS A 67 -351.167-200.134 149.717 1.00 80.97 N ANISOU 541 N LYS A 67 11162 7049 12554 86 163 -586 N ATOM 542 CA LYS A 67 -352.606-199.902 149.748 1.00 85.56 C ANISOU 542 CA LYS A 67 11824 7772 12912 -57 58 -555 C ATOM 543 C LYS A 67 -352.976-198.436 149.543 1.00 90.33 C ANISOU 543 C LYS A 67 12411 8639 13271 -92 6 -528 C ATOM 544 O LYS A 67 -354.098-198.150 149.112 1.00 91.63 O ANISOU 544 O LYS A 67 12645 8921 13249 -216 -48 -560 O ATOM 545 CB LYS A 67 -353.176-200.406 151.072 1.00 88.14 C ANISOU 545 CB LYS A 67 12123 8050 13315 -68 -80 -366 C ATOM 546 CG LYS A 67 -353.155-201.914 151.225 1.00 92.13 C ANISOU 546 CG LYS A 67 12674 8294 14038 -73 -53 -383 C ATOM 547 CD LYS A 67 -354.111-202.574 150.251 1.00 95.43 C ANISOU 547 CD LYS A 67 13222 8665 14373 -218 -1 -550 C ATOM 548 CE LYS A 67 -354.185-204.074 150.486 1.00105.48 C ANISOU 548 CE LYS A 67 14544 9666 15867 -235 17 -558 C ATOM 549 NZ LYS A 67 -355.228-204.710 149.629 1.00111.77 N ANISOU 549 NZ LYS A 67 15472 10423 16571 -400 45 -712 N ATOM 550 N LEU A 68 -352.069-197.501 149.842 1.00 89.67 N ANISOU 550 N LEU A 68 12231 8641 13200 12 12 -465 N ATOM 551 CA LEU A 68 -352.381-196.083 149.698 1.00 81.52 C ANISOU 551 CA LEU A 68 11179 7840 11956 -15 -38 -431 C ATOM 552 C LEU A 68 -352.297-195.598 148.256 1.00 79.11 C ANISOU 552 C LEU A 68 10955 7605 11498 -74 66 -596 C ATOM 553 O LEU A 68 -352.906-194.575 147.929 1.00 85.22 O ANISOU 553 O LEU A 68 11749 8556 12073 -136 5 -578 O ATOM 554 CB LEU A 68 -351.447-195.238 150.567 1.00 76.87 C ANISOU 554 CB LEU A 68 10465 7312 11431 103 -77 -303 C ATOM 555 CG LEU A 68 -351.523-195.448 152.080 1.00 72.57 C ANISOU 555 CG LEU A 68 9858 6741 10977 142 -205 -115 C ATOM 556 CD1 LEU A 68 -350.468-194.614 152.786 1.00 62.48 C ANISOU 556 CD1 LEU A 68 8468 5516 9756 246 -244 -12 C ATOM 557 CD2 LEU A 68 -352.907-195.119 152.606 1.00 64.28 C ANISOU 557 CD2 LEU A 68 8845 5816 9763 39 -306 -39 C ATOM 558 N ARG A 69 -351.575-196.308 147.389 1.00 78.04 N ANISOU 558 N ARG A 69 10874 7327 11450 -63 225 -755 N ATOM 559 CA ARG A 69 -351.333-195.854 146.020 1.00 80.76 C ANISOU 559 CA ARG A 69 11316 7732 11636 -129 351 -917 C ATOM 560 C ARG A 69 -352.529-196.162 145.113 1.00 84.80 C ANISOU 560 C ARG A 69 11993 8282 11946 -302 314 -1019 C ATOM 561 O ARG A 69 -352.426-196.846 144.097 1.00 87.23 O ANISOU 561 O ARG A 69 12431 8493 12220 -379 440 -1200 O ATOM 562 CB ARG A 69 -350.050-196.477 145.485 1.00 79.85 C ANISOU 562 CB ARG A 69 11190 7445 11703 -53 564 -1060 C ATOM 563 CG ARG A 69 -348.816-196.126 146.306 1.00 74.71 C ANISOU 563 CG ARG A 69 10356 6757 11272 113 586 -957 C ATOM 564 CD ARG A 69 -347.529-196.515 145.603 1.00 79.24 C ANISOU 564 CD ARG A 69 10896 7184 12027 182 821 -1113 C ATOM 565 NE ARG A 69 -347.283-197.954 145.623 1.00 92.55 N ANISOU 565 NE ARG A 69 12587 8616 13962 221 910 -1201 N ATOM 566 CZ ARG A 69 -346.681-198.595 146.619 1.00 95.24 C ANISOU 566 CZ ARG A 69 12782 8794 14613 355 859 -1090 C ATOM 567 NH1 ARG A 69 -346.486-199.903 146.546 1.00 92.70 N ANISOU 567 NH1 ARG A 69 12472 8224 14527 387 946 -1175 N ATOM 568 NH2 ARG A 69 -346.274-197.930 147.692 1.00 91.49 N ANISOU 568 NH2 ARG A 69 12156 8396 14211 449 712 -890 N ATOM 569 N THR A 70 -353.692-195.624 145.504 1.00 89.23 N ANISOU 569 N THR A 70 12543 8984 12375 -370 135 -903 N ATOM 570 CA THR A 70 -354.912-195.696 144.716 1.00 91.80 C ANISOU 570 CA THR A 70 12992 9377 12511 -538 49 -964 C ATOM 571 C THR A 70 -355.143-194.385 143.969 1.00 95.67 C ANISOU 571 C THR A 70 13520 10060 12769 -599 -5 -951 C ATOM 572 O THR A 70 -354.771-193.311 144.455 1.00 92.79 O ANISOU 572 O THR A 70 13053 9805 12399 -512 -35 -840 O ATOM 573 CB THR A 70 -356.118-195.990 145.611 1.00 92.32 C ANISOU 573 CB THR A 70 13001 9460 12618 -580 -113 -841 C ATOM 574 OG1 THR A 70 -356.352-194.876 146.480 1.00101.69 O ANISOU 574 OG1 THR A 70 14060 10797 13782 -517 -217 -675 O ATOM 575 CG2 THR A 70 -355.853-197.219 146.450 1.00 90.19 C ANISOU 575 CG2 THR A 70 12695 8997 12575 -520 -72 -820 C ATOM 576 N PRO A 71 -355.741-194.447 142.775 1.00 96.00 N ANISOU 576 N PRO A 71 13720 10139 12615 -757 -27 -1061 N ATOM 577 CA PRO A 71 -355.967-193.208 142.005 1.00 89.08 C ANISOU 577 CA PRO A 71 12897 9436 11512 -827 -98 -1033 C ATOM 578 C PRO A 71 -356.748-192.147 142.763 1.00 80.83 C ANISOU 578 C PRO A 71 11713 8537 10460 -792 -283 -845 C ATOM 579 O PRO A 71 -356.460-190.952 142.616 1.00 97.55 O ANISOU 579 O PRO A 71 13801 10772 12491 -760 -305 -778 O ATOM 580 CB PRO A 71 -356.729-193.709 140.771 1.00 89.75 C ANISOU 580 CB PRO A 71 13180 9516 11404 -1027 -143 -1162 C ATOM 581 CG PRO A 71 -356.261-195.123 140.605 1.00 82.51 C ANISOU 581 CG PRO A 71 12345 8402 10603 -1036 22 -1327 C ATOM 582 CD PRO A 71 -356.085-195.653 142.001 1.00 80.74 C ANISOU 582 CD PRO A 71 11944 8078 10655 -884 25 -1226 C ATOM 583 N LEU A 72 -357.721-192.547 143.584 1.00 71.19 N ANISOU 583 N LEU A 72 10405 7303 9339 -801 -403 -764 N ATOM 584 CA LEU A 72 -358.480-191.589 144.380 1.00 70.28 C ANISOU 584 CA LEU A 72 10147 7310 9246 -765 -547 -602 C ATOM 585 C LEU A 72 -357.610-190.864 145.400 1.00 76.99 C ANISOU 585 C LEU A 72 10869 8189 10196 -604 -488 -504 C ATOM 586 O LEU A 72 -358.044-189.846 145.955 1.00 75.35 O ANISOU 586 O LEU A 72 10558 8088 9985 -568 -577 -389 O ATOM 587 CB LEU A 72 -359.639-192.308 145.076 1.00 74.57 C ANISOU 587 CB LEU A 72 10625 7815 9893 -817 -645 -553 C ATOM 588 CG LEU A 72 -360.935-191.532 145.330 1.00 82.72 C ANISOU 588 CG LEU A 72 11551 8966 10912 -868 -816 -442 C ATOM 589 CD1 LEU A 72 -361.235-190.553 144.198 1.00 81.41 C ANISOU 589 CD1 LEU A 72 11444 8914 10574 -945 -922 -442 C ATOM 590 CD2 LEU A 72 -362.092-192.507 145.507 1.00 80.00 C ANISOU 590 CD2 LEU A 72 11191 8563 10643 -978 -894 -451 C ATOM 591 N ASN A 73 -356.397-191.355 145.653 1.00 76.05 N ANISOU 591 N ASN A 73 10749 7968 10177 -509 -343 -551 N ATOM 592 CA ASN A 73 -355.463-190.722 146.570 1.00 69.51 C ANISOU 592 CA ASN A 73 9805 7159 9446 -367 -298 -464 C ATOM 593 C ASN A 73 -354.415-189.868 145.869 1.00 67.05 C ANISOU 593 C ASN A 73 9517 6897 9061 -330 -206 -504 C ATOM 594 O ASN A 73 -353.677-189.148 146.552 1.00 64.96 O ANISOU 594 O ASN A 73 9153 6668 8863 -227 -189 -427 O ATOM 595 CB ASN A 73 -354.753-191.781 147.425 1.00 74.28 C ANISOU 595 CB ASN A 73 10365 7611 10248 -279 -224 -459 C ATOM 596 CG ASN A 73 -355.637-192.335 148.522 1.00 75.19 C ANISOU 596 CG ASN A 73 10427 7697 10446 -293 -317 -362 C ATOM 597 OD1 ASN A 73 -356.625-191.717 148.909 1.00 82.65 O ANISOU 597 OD1 ASN A 73 11326 8749 11329 -335 -420 -283 O ATOM 598 ND2 ASN A 73 -355.275-193.501 149.041 1.00 80.94 N ANISOU 598 ND2 ASN A 73 11157 8269 11329 -258 -273 -366 N ATOM 599 N TYR A 74 -354.318-189.939 144.536 1.00 63.75 N ANISOU 599 N TYR A 74 9238 6481 8501 -425 -143 -625 N ATOM 600 CA TYR A 74 -353.356-189.104 143.818 1.00 69.01 C ANISOU 600 CA TYR A 74 9939 7199 9081 -410 -40 -662 C ATOM 601 C TYR A 74 -353.527-187.631 144.175 1.00 69.96 C ANISOU 601 C TYR A 74 9977 7461 9143 -376 -145 -526 C ATOM 602 O TYR A 74 -352.544-186.920 144.415 1.00 72.95 O ANISOU 602 O TYR A 74 10288 7863 9568 -293 -73 -495 O ATOM 603 CB TYR A 74 -353.506-189.283 142.304 1.00 67.35 C ANISOU 603 CB TYR A 74 9925 6998 8668 -560 16 -797 C ATOM 604 CG TYR A 74 -353.037-190.601 141.733 1.00 77.01 C ANISOU 604 CG TYR A 74 11255 8069 9937 -597 182 -974 C ATOM 605 CD1 TYR A 74 -352.781-191.696 142.550 1.00 86.95 C ANISOU 605 CD1 TYR A 74 12432 9180 11424 -508 233 -993 C ATOM 606 CD2 TYR A 74 -352.848-190.747 140.364 1.00 83.52 C ANISOU 606 CD2 TYR A 74 12274 8889 10572 -730 293 -1125 C ATOM 607 CE1 TYR A 74 -352.359-192.901 142.019 1.00 88.51 C ANISOU 607 CE1 TYR A 74 12721 9216 11691 -536 392 -1161 C ATOM 608 CE2 TYR A 74 -352.423-191.945 139.823 1.00 93.01 C ANISOU 608 CE2 TYR A 74 13581 9940 11820 -769 469 -1309 C ATOM 609 CZ TYR A 74 -352.179-193.019 140.653 1.00 96.14 C ANISOU 609 CZ TYR A 74 13877 10178 12475 -665 520 -1329 C ATOM 610 OH TYR A 74 -351.755-194.212 140.112 1.00104.22 O ANISOU 610 OH TYR A 74 14999 11029 13572 -698 703 -1519 O ATOM 611 N ILE A 75 -354.775-187.159 144.222 1.00 71.67 N ANISOU 611 N ILE A 75 10188 7765 9280 -440 -316 -447 N ATOM 612 CA ILE A 75 -355.032-185.750 144.491 1.00 70.80 C ANISOU 612 CA ILE A 75 10001 7770 9128 -412 -415 -326 C ATOM 613 C ILE A 75 -354.629-185.383 145.914 1.00 69.66 C ANISOU 613 C ILE A 75 9700 7626 9143 -279 -410 -235 C ATOM 614 O ILE A 75 -354.279-184.228 146.185 1.00 65.12 O ANISOU 614 O ILE A 75 9062 7118 8562 -227 -425 -164 O ATOM 615 CB ILE A 75 -356.509-185.414 144.211 1.00 66.78 C ANISOU 615 CB ILE A 75 9501 7332 8542 -507 -599 -265 C ATOM 616 CG1 ILE A 75 -356.684-183.909 143.993 1.00 62.53 C ANISOU 616 CG1 ILE A 75 8929 6897 7933 -502 -690 -165 C ATOM 617 CG2 ILE A 75 -357.401-185.909 145.340 1.00 48.45 C ANISOU 617 CG2 ILE A 75 7063 4986 6361 -477 -673 -210 C ATOM 618 CD1 ILE A 75 -355.914-183.380 142.796 1.00 65.67 C ANISOU 618 CD1 ILE A 75 9462 7323 8164 -561 -625 -206 C ATOM 619 N LEU A 76 -354.670-186.342 146.844 1.00 66.84 N ANISOU 619 N LEU A 76 9288 7188 8920 -233 -395 -231 N ATOM 620 CA LEU A 76 -354.237-186.060 148.208 1.00 65.90 C ANISOU 620 CA LEU A 76 9047 7066 8925 -127 -399 -142 C ATOM 621 C LEU A 76 -352.724-185.931 148.293 1.00 71.63 C ANISOU 621 C LEU A 76 9741 7750 9725 -40 -288 -162 C ATOM 622 O LEU A 76 -352.214-185.149 149.105 1.00 72.08 O ANISOU 622 O LEU A 76 9710 7846 9830 30 -306 -86 O ATOM 623 CB LEU A 76 -354.729-187.148 149.160 1.00 68.52 C ANISOU 623 CB LEU A 76 9350 7320 9364 -122 -425 -116 C ATOM 624 CG LEU A 76 -356.228-187.149 149.460 1.00 68.80 C ANISOU 624 CG LEU A 76 9365 7402 9373 -195 -531 -71 C ATOM 625 CD1 LEU A 76 -356.607-188.370 150.289 1.00 68.18 C ANISOU 625 CD1 LEU A 76 9279 7230 9395 -207 -531 -54 C ATOM 626 CD2 LEU A 76 -356.610-185.864 150.178 1.00 61.95 C ANISOU 626 CD2 LEU A 76 8406 6638 8495 -162 -590 22 C ATOM 627 N LEU A 77 -351.991-186.699 147.481 1.00 67.81 N ANISOU 627 N LEU A 77 9322 7181 9262 -49 -168 -271 N ATOM 628 CA LEU A 77 -350.551-186.492 147.380 1.00 70.64 C ANISOU 628 CA LEU A 77 9633 7501 9707 26 -46 -301 C ATOM 629 C LEU A 77 -350.248-185.144 146.745 1.00 75.03 C ANISOU 629 C LEU A 77 10202 8165 10140 4 -29 -288 C ATOM 630 O LEU A 77 -349.299-184.461 147.148 1.00 74.10 O ANISOU 630 O LEU A 77 9995 8063 10098 74 6 -247 O ATOM 631 CB LEU A 77 -349.909-187.619 146.574 1.00 73.67 C ANISOU 631 CB LEU A 77 10081 7757 10153 16 108 -441 C ATOM 632 CG LEU A 77 -350.004-189.024 147.167 1.00 73.83 C ANISOU 632 CG LEU A 77 10085 7634 10335 49 108 -456 C ATOM 633 CD1 LEU A 77 -349.629-190.058 146.125 1.00 79.09 C ANISOU 633 CD1 LEU A 77 10846 8174 11030 10 268 -624 C ATOM 634 CD2 LEU A 77 -349.109-189.141 148.386 1.00 71.10 C ANISOU 634 CD2 LEU A 77 9593 7223 10199 174 87 -361 C ATOM 635 N ASN A 78 -351.050-184.750 145.749 1.00 72.23 N ANISOU 635 N ASN A 78 9962 7881 9603 -102 -67 -314 N ATOM 636 CA ASN A 78 -350.919-183.424 145.157 1.00 71.59 C ANISOU 636 CA ASN A 78 9905 7899 9395 -136 -79 -275 C ATOM 637 C ASN A 78 -351.111-182.340 146.208 1.00 67.85 C ANISOU 637 C ASN A 78 9313 7493 8974 -70 -189 -147 C ATOM 638 O ASN A 78 -350.397-181.329 146.211 1.00 64.37 O ANISOU 638 O ASN A 78 8831 7092 8534 -40 -158 -111 O ATOM 639 CB ASN A 78 -351.934-183.260 144.027 1.00 73.67 C ANISOU 639 CB ASN A 78 10313 8219 9458 -270 -154 -295 C ATOM 640 CG ASN A 78 -351.603-182.106 143.107 1.00 71.72 C ANISOU 640 CG ASN A 78 10140 8048 9063 -329 -135 -273 C ATOM 641 OD1 ASN A 78 -350.485-181.998 142.607 1.00 70.19 O ANISOU 641 OD1 ASN A 78 9976 7833 8858 -328 25 -335 O ATOM 642 ND2 ASN A 78 -352.577-181.235 142.879 1.00 71.11 N ANISOU 642 ND2 ASN A 78 10085 8050 8885 -384 -297 -179 N ATOM 643 N LEU A 79 -352.070-182.541 147.115 1.00 59.59 N ANISOU 643 N LEU A 79 8212 6454 7975 -54 -304 -86 N ATOM 644 CA LEU A 79 -352.266-181.607 148.218 1.00 59.13 C ANISOU 644 CA LEU A 79 8049 6447 7971 4 -383 14 C ATOM 645 C LEU A 79 -351.016-181.495 149.084 1.00 64.14 C ANISOU 645 C LEU A 79 8596 7049 8725 94 -324 34 C ATOM 646 O LEU A 79 -350.615-180.389 149.463 1.00 69.05 O ANISOU 646 O LEU A 79 9163 7718 9354 126 -342 86 O ATOM 647 CB LEU A 79 -353.463-182.048 149.062 1.00 61.19 C ANISOU 647 CB LEU A 79 8274 6708 8268 -6 -476 55 C ATOM 648 CG LEU A 79 -353.729-181.222 150.320 1.00 59.15 C ANISOU 648 CG LEU A 79 7920 6490 8063 43 -531 138 C ATOM 649 CD1 LEU A 79 -354.120-179.797 149.953 1.00 58.15 C ANISOU 649 CD1 LEU A 79 7776 6436 7882 31 -583 179 C ATOM 650 CD2 LEU A 79 -354.804-181.879 151.181 1.00 49.84 C ANISOU 650 CD2 LEU A 79 6713 5297 6927 22 -579 163 C ATOM 651 N ALA A 80 -350.380-182.628 149.400 1.00 72.73 N ANISOU 651 N ALA A 80 9667 8047 9921 133 -265 -3 N ATOM 652 CA ALA A 80 -349.212-182.605 150.277 1.00 62.07 C ANISOU 652 CA ALA A 80 8219 6655 8708 216 -243 33 C ATOM 653 C ALA A 80 -348.034-181.888 149.633 1.00 68.40 C ANISOU 653 C ALA A 80 8992 7469 9530 235 -148 3 C ATOM 654 O ALA A 80 -347.246-181.241 150.333 1.00 69.39 O ANISOU 654 O ALA A 80 9026 7606 9733 285 -168 56 O ATOM 655 CB ALA A 80 -348.817-184.026 150.668 1.00 50.42 C ANISOU 655 CB ALA A 80 6726 5061 7371 256 -214 12 C ATOM 656 N VAL A 81 -347.890-181.996 148.311 1.00 67.02 N ANISOU 656 N VAL A 81 8899 7289 9278 183 -41 -85 N ATOM 657 CA VAL A 81 -346.818-181.284 147.626 1.00 63.94 C ANISOU 657 CA VAL A 81 8491 6912 8891 181 73 -117 C ATOM 658 C VAL A 81 -347.099-179.787 147.613 1.00 71.29 C ANISOU 658 C VAL A 81 9425 7944 9716 152 2 -42 C ATOM 659 O VAL A 81 -346.193-178.968 147.813 1.00 68.45 O ANISOU 659 O VAL A 81 8990 7600 9417 180 34 -13 O ATOM 660 CB VAL A 81 -346.631-181.845 146.205 1.00 61.72 C ANISOU 660 CB VAL A 81 8326 6597 8530 111 227 -241 C ATOM 661 CG1 VAL A 81 -345.784-180.904 145.367 1.00 66.35 C ANISOU 661 CG1 VAL A 81 8927 7223 9059 73 347 -265 C ATOM 662 CG2 VAL A 81 -345.984-183.219 146.265 1.00 58.10 C ANISOU 662 CG2 VAL A 81 7829 6007 8240 162 337 -328 C ATOM 663 N ALA A 82 -348.359-179.407 147.385 1.00 73.67 N ANISOU 663 N ALA A 82 9804 8307 9882 95 -102 -8 N ATOM 664 CA ALA A 82 -348.725-177.994 147.376 1.00 62.05 C ANISOU 664 CA ALA A 82 8330 6910 8336 74 -179 69 C ATOM 665 C ALA A 82 -348.404-177.334 148.708 1.00 67.12 C ANISOU 665 C ALA A 82 8854 7561 9087 146 -239 137 C ATOM 666 O ALA A 82 -347.895-176.206 148.745 1.00 70.67 O ANISOU 666 O ALA A 82 9270 8039 9542 149 -236 174 O ATOM 667 CB ALA A 82 -350.211-177.841 147.055 1.00 54.14 C ANISOU 667 CB ALA A 82 7397 5951 7223 16 -299 102 C ATOM 668 N ASP A 83 -348.703-178.018 149.816 1.00 64.14 N ANISOU 668 N ASP A 83 8426 7158 8787 189 -296 154 N ATOM 669 CA ASP A 83 -348.394-177.462 151.128 1.00 67.13 C ANISOU 669 CA ASP A 83 8718 7545 9242 237 -357 213 C ATOM 670 C ASP A 83 -346.889-177.305 151.317 1.00 68.31 C ANISOU 670 C ASP A 83 8790 7664 9500 276 -301 211 C ATOM 671 O ASP A 83 -346.433-176.356 151.967 1.00 70.96 O ANISOU 671 O ASP A 83 9071 8025 9867 288 -340 253 O ATOM 672 CB ASP A 83 -348.981-178.345 152.228 1.00 67.04 C ANISOU 672 CB ASP A 83 8694 7509 9269 254 -420 236 C ATOM 673 CG ASP A 83 -350.503-178.385 152.209 1.00 71.00 C ANISOU 673 CG ASP A 83 9242 8043 9694 213 -475 243 C ATOM 674 OD1 ASP A 83 -351.126-177.549 151.521 1.00 71.56 O ANISOU 674 OD1 ASP A 83 9337 8157 9696 181 -493 247 O ATOM 675 OD2 ASP A 83 -351.078-179.251 152.901 1.00 72.99 O ANISOU 675 OD2 ASP A 83 9498 8269 9966 209 -504 253 O ATOM 676 N LEU A 84 -346.102-178.228 150.754 1.00 61.67 N ANISOU 676 N LEU A 84 7936 6762 8733 293 -205 155 N ATOM 677 CA LEU A 84 -344.652-178.087 150.801 1.00 64.04 C ANISOU 677 CA LEU A 84 8136 7024 9171 331 -138 148 C ATOM 678 C LEU A 84 -344.174-176.899 149.971 1.00 68.89 C ANISOU 678 C LEU A 84 8758 7684 9732 290 -64 138 C ATOM 679 O LEU A 84 -343.182-176.256 150.330 1.00 59.69 O ANISOU 679 O LEU A 84 7497 6516 8666 308 -56 164 O ATOM 680 CB LEU A 84 -343.993-179.390 150.338 1.00 52.95 C ANISOU 680 CB LEU A 84 6705 5525 7889 364 -30 78 C ATOM 681 CG LEU A 84 -344.067-180.536 151.354 1.00 60.48 C ANISOU 681 CG LEU A 84 7615 6404 8959 417 -114 113 C ATOM 682 CD1 LEU A 84 -343.531-181.816 150.749 1.00 64.36 C ANISOU 682 CD1 LEU A 84 8090 6782 9583 450 6 33 C ATOM 683 CD2 LEU A 84 -343.299-180.190 152.635 1.00 57.36 C ANISOU 683 CD2 LEU A 84 7103 6001 8689 462 -228 205 C ATOM 684 N PHE A 85 -344.864-176.592 148.868 1.00 70.49 N ANISOU 684 N PHE A 85 9077 7926 9778 224 -21 111 N ATOM 685 CA PHE A 85 -344.598-175.350 148.150 1.00 69.48 C ANISOU 685 CA PHE A 85 8982 7844 9575 171 21 129 C ATOM 686 C PHE A 85 -344.859-174.140 149.039 1.00 70.49 C ANISOU 686 C PHE A 85 9065 8010 9708 184 -100 211 C ATOM 687 O PHE A 85 -344.074-173.185 149.047 1.00 69.16 O ANISOU 687 O PHE A 85 8847 7849 9582 173 -72 234 O ATOM 688 CB PHE A 85 -345.456-175.273 146.885 1.00 68.20 C ANISOU 688 CB PHE A 85 8973 7716 9225 87 43 109 C ATOM 689 CG PHE A 85 -344.824-175.907 145.680 1.00 74.91 C ANISOU 689 CG PHE A 85 9894 8537 10032 35 217 16 C ATOM 690 CD1 PHE A 85 -344.749-177.283 145.560 1.00 81.23 C ANISOU 690 CD1 PHE A 85 10703 9276 10883 55 289 -70 C ATOM 691 CD2 PHE A 85 -344.322-175.122 144.655 1.00 81.30 C ANISOU 691 CD2 PHE A 85 10772 9372 10747 -44 321 12 C ATOM 692 CE1 PHE A 85 -344.172-177.867 144.447 1.00 82.31 C ANISOU 692 CE1 PHE A 85 10913 9376 10983 1 476 -178 C ATOM 693 CE2 PHE A 85 -343.743-175.698 143.541 1.00 79.99 C ANISOU 693 CE2 PHE A 85 10688 9180 10525 -109 510 -88 C ATOM 694 CZ PHE A 85 -343.669-177.072 143.436 1.00 79.16 C ANISOU 694 CZ PHE A 85 10588 9012 10475 -85 595 -192 C ATOM 695 N MET A 86 -345.962-174.160 149.794 1.00 70.33 N ANISOU 695 N MET A 86 9061 8008 9652 199 -220 246 N ATOM 696 CA MET A 86 -346.242-173.069 150.724 1.00 70.31 C ANISOU 696 CA MET A 86 9021 8029 9663 210 -313 301 C ATOM 697 C MET A 86 -345.209-173.018 151.844 1.00 72.55 C ANISOU 697 C MET A 86 9204 8293 10070 247 -336 313 C ATOM 698 O MET A 86 -344.812-171.932 152.282 1.00 69.67 O ANISOU 698 O MET A 86 8802 7937 9732 237 -365 340 O ATOM 699 CB MET A 86 -347.649-173.222 151.304 1.00 62.75 C ANISOU 699 CB MET A 86 8096 7088 8657 214 -406 319 C ATOM 700 CG MET A 86 -348.772-173.027 150.295 1.00 73.23 C ANISOU 700 CG MET A 86 9503 8437 9884 172 -429 328 C ATOM 701 SD MET A 86 -350.399-173.389 150.992 1.00 77.79 S ANISOU 701 SD MET A 86 10079 9024 10453 179 -521 340 S ATOM 702 CE MET A 86 -350.427-172.267 152.388 1.00 84.88 C ANISOU 702 CE MET A 86 10910 9922 11418 210 -557 365 C ATOM 703 N VAL A 87 -344.766-174.184 152.320 1.00 67.95 N ANISOU 703 N VAL A 87 8576 7673 9568 284 -336 299 N ATOM 704 CA VAL A 87 -343.841-174.236 153.448 1.00 67.15 C ANISOU 704 CA VAL A 87 8380 7548 9585 313 -397 330 C ATOM 705 C VAL A 87 -342.468-173.705 153.048 1.00 69.40 C ANISOU 705 C VAL A 87 8573 7815 9981 311 -332 324 C ATOM 706 O VAL A 87 -341.849-172.930 153.787 1.00 63.94 O ANISOU 706 O VAL A 87 7817 7130 9346 301 -397 357 O ATOM 707 CB VAL A 87 -343.762-175.675 153.999 1.00 60.55 C ANISOU 707 CB VAL A 87 7522 6662 8823 353 -430 335 C ATOM 708 CG1 VAL A 87 -342.461-175.901 154.753 1.00 53.18 C ANISOU 708 CG1 VAL A 87 6469 5683 8056 385 -481 372 C ATOM 709 CG2 VAL A 87 -344.950-175.956 154.905 1.00 56.85 C ANISOU 709 CG2 VAL A 87 7123 6215 8262 340 -521 364 C ATOM 710 N PHE A 88 -341.973-174.101 151.876 1.00 63.59 N ANISOU 710 N PHE A 88 7830 7055 9277 310 -195 274 N ATOM 711 CA PHE A 88 -340.619-173.737 151.480 1.00 62.22 C ANISOU 711 CA PHE A 88 7550 6855 9235 306 -103 259 C ATOM 712 C PHE A 88 -340.581-172.484 150.620 1.00 71.09 C ANISOU 712 C PHE A 88 8723 8018 10268 240 -29 259 C ATOM 713 O PHE A 88 -339.681-171.653 150.782 1.00 80.28 O ANISOU 713 O PHE A 88 9803 9180 11522 220 -19 280 O ATOM 714 CB PHE A 88 -339.953-174.901 150.745 1.00 61.29 C ANISOU 714 CB PHE A 88 7383 6673 9232 337 38 193 C ATOM 715 CG PHE A 88 -339.631-176.064 151.631 1.00 69.50 C ANISOU 715 CG PHE A 88 8333 7644 10431 409 -37 210 C ATOM 716 CD1 PHE A 88 -338.566-175.997 152.513 1.00 71.81 C ANISOU 716 CD1 PHE A 88 8468 7899 10919 443 -119 262 C ATOM 717 CD2 PHE A 88 -340.385-177.225 151.584 1.00 75.13 C ANISOU 717 CD2 PHE A 88 9118 8323 11105 434 -42 185 C ATOM 718 CE1 PHE A 88 -338.256-177.066 153.332 1.00 76.80 C ANISOU 718 CE1 PHE A 88 9020 8458 11704 505 -215 300 C ATOM 719 CE2 PHE A 88 -340.079-178.301 152.406 1.00 78.02 C ANISOU 719 CE2 PHE A 88 9407 8611 11626 497 -120 217 C ATOM 720 CZ PHE A 88 -339.014-178.218 153.278 1.00 77.08 C ANISOU 720 CZ PHE A 88 9135 8452 11699 534 -212 281 C ATOM 721 N GLY A 89 -341.541-172.332 149.708 1.00 73.10 N ANISOU 721 N GLY A 89 9116 8305 10352 198 9 246 N ATOM 722 CA GLY A 89 -341.597-171.117 148.913 1.00 75.10 C ANISOU 722 CA GLY A 89 9436 8589 10511 129 52 270 C ATOM 723 C GLY A 89 -341.987-169.905 149.735 1.00 74.33 C ANISOU 723 C GLY A 89 9332 8510 10402 124 -76 333 C ATOM 724 O GLY A 89 -341.398-168.830 149.589 1.00 84.84 O ANISOU 724 O GLY A 89 10637 9837 11762 85 -53 360 O ATOM 725 N GLY A 90 -342.963-170.065 150.625 1.00 68.55 N ANISOU 725 N GLY A 90 8622 7789 9635 159 -199 350 N ATOM 726 CA GLY A 90 -343.476-168.952 151.395 1.00 64.50 C ANISOU 726 CA GLY A 90 8116 7283 9108 152 -298 388 C ATOM 727 C GLY A 90 -342.946-168.847 152.810 1.00 65.86 C ANISOU 727 C GLY A 90 8206 7445 9371 173 -379 391 C ATOM 728 O GLY A 90 -342.283-167.863 153.151 1.00 68.76 O ANISOU 728 O GLY A 90 8530 7801 9795 144 -397 405 O ATOM 729 N PHE A 91 -343.227-169.854 153.644 1.00 58.07 N ANISOU 729 N PHE A 91 7209 6460 8394 209 -438 383 N ATOM 730 CA PHE A 91 -342.973-169.718 155.077 1.00 56.59 C ANISOU 730 CA PHE A 91 6986 6270 8244 207 -542 396 C ATOM 731 C PHE A 91 -341.481-169.581 155.369 1.00 57.30 C ANISOU 731 C PHE A 91 6965 6339 8469 197 -559 410 C ATOM 732 O PHE A 91 -341.077-168.754 156.195 1.00 53.97 O ANISOU 732 O PHE A 91 6520 5916 8069 160 -633 421 O ATOM 733 CB PHE A 91 -343.548-170.911 155.848 1.00 55.14 C ANISOU 733 CB PHE A 91 6828 6089 8032 234 -599 400 C ATOM 734 CG PHE A 91 -345.012-171.170 155.599 1.00 64.53 C ANISOU 734 CG PHE A 91 8105 7297 9117 240 -583 386 C ATOM 735 CD1 PHE A 91 -345.848-170.187 155.088 1.00 63.07 C ANISOU 735 CD1 PHE A 91 7966 7124 8874 223 -560 379 C ATOM 736 CD2 PHE A 91 -345.557-172.414 155.894 1.00 65.03 C ANISOU 736 CD2 PHE A 91 8193 7355 9159 259 -600 387 C ATOM 737 CE1 PHE A 91 -347.192-170.443 154.865 1.00 58.02 C ANISOU 737 CE1 PHE A 91 7379 6496 8169 228 -560 373 C ATOM 738 CE2 PHE A 91 -346.900-172.673 155.677 1.00 62.15 C ANISOU 738 CE2 PHE A 91 7892 7006 8717 256 -589 374 C ATOM 739 CZ PHE A 91 -347.718-171.687 155.158 1.00 59.36 C ANISOU 739 CZ PHE A 91 7566 6668 8318 242 -571 367 C ATOM 740 N THR A 92 -340.650-170.393 154.711 1.00 57.91 N ANISOU 740 N THR A 92 6965 6391 8648 225 -487 403 N ATOM 741 CA THR A 92 -339.213-170.360 154.966 1.00 52.91 C ANISOU 741 CA THR A 92 6190 5727 8186 223 -502 419 C ATOM 742 C THR A 92 -338.610-169.023 154.547 1.00 59.58 C ANISOU 742 C THR A 92 7002 6575 9061 167 -454 417 C ATOM 743 O THR A 92 -337.850-168.406 155.304 1.00 56.38 O ANISOU 743 O THR A 92 6521 6161 8740 133 -541 439 O ATOM 744 CB THR A 92 -338.529-171.514 154.236 1.00 52.70 C ANISOU 744 CB THR A 92 6078 5657 8290 271 -400 396 C ATOM 745 OG1 THR A 92 -338.936-172.751 154.827 1.00 65.29 O ANISOU 745 OG1 THR A 92 7687 7228 9891 320 -472 410 O ATOM 746 CG2 THR A 92 -337.024-171.390 154.336 1.00 66.07 C ANISOU 746 CG2 THR A 92 7593 7309 10201 271 -392 409 C ATOM 747 N THR A 93 -338.951-168.553 153.346 1.00 63.77 N ANISOU 747 N THR A 93 7598 7116 9515 145 -327 398 N ATOM 748 CA THR A 93 -338.481-167.246 152.909 1.00 61.82 C ANISOU 748 CA THR A 93 7341 6864 9283 83 -280 409 C ATOM 749 C THR A 93 -338.941-166.149 153.861 1.00 60.38 C ANISOU 749 C THR A 93 7206 6685 9052 51 -401 427 C ATOM 750 O THR A 93 -338.156-165.268 154.233 1.00 53.87 O ANISOU 750 O THR A 93 6318 5840 8309 2 -433 436 O ATOM 751 CB THR A 93 -338.975-166.958 151.491 1.00 63.25 C ANISOU 751 CB THR A 93 7625 7055 9352 53 -148 404 C ATOM 752 OG1 THR A 93 -338.649-168.057 150.632 1.00 67.40 O ANISOU 752 OG1 THR A 93 8135 7577 9898 74 -21 365 O ATOM 753 CG2 THR A 93 -338.313-165.702 150.957 1.00 74.04 C ANISOU 753 CG2 THR A 93 8975 8405 10751 -20 -83 427 C ATOM 754 N THR A 94 -340.209-166.196 154.277 1.00 56.46 N ANISOU 754 N THR A 94 6815 6205 8432 72 -461 422 N ATOM 755 CA THR A 94 -340.755-165.135 155.115 1.00 54.46 C ANISOU 755 CA THR A 94 6616 5941 8135 42 -541 418 C ATOM 756 C THR A 94 -340.100-165.123 156.489 1.00 59.82 C ANISOU 756 C THR A 94 7243 6617 8866 15 -657 412 C ATOM 757 O THR A 94 -339.836-164.051 157.040 1.00 65.22 O ANISOU 757 O THR A 94 7933 7280 9568 -40 -702 400 O ATOM 758 CB THR A 94 -342.271-165.287 155.239 1.00 52.57 C ANISOU 758 CB THR A 94 6481 5715 7780 74 -557 407 C ATOM 759 OG1 THR A 94 -342.869-165.153 153.945 1.00 60.65 O ANISOU 759 OG1 THR A 94 7555 6736 8752 81 -482 427 O ATOM 760 CG2 THR A 94 -342.849-164.228 156.175 1.00 42.30 C ANISOU 760 CG2 THR A 94 5228 4389 6454 46 -612 383 C ATOM 761 N LEU A 95 -339.825-166.301 157.054 1.00 57.55 N ANISOU 761 N LEU A 95 6916 6347 8606 45 -716 423 N ATOM 762 CA LEU A 95 -339.069-166.360 158.302 1.00 60.56 C ANISOU 762 CA LEU A 95 7248 6725 9037 7 -854 438 C ATOM 763 C LEU A 95 -337.731-165.642 158.167 1.00 67.22 C ANISOU 763 C LEU A 95 7971 7543 10026 -42 -867 450 C ATOM 764 O LEU A 95 -337.285-164.954 159.095 1.00 66.46 O ANISOU 764 O LEU A 95 7870 7440 9943 -111 -978 448 O ATOM 765 CB LEU A 95 -338.854-167.817 158.717 1.00 54.23 C ANISOU 765 CB LEU A 95 6404 5927 8274 52 -918 472 C ATOM 766 CG LEU A 95 -337.843-168.118 159.830 1.00 58.86 C ANISOU 766 CG LEU A 95 6913 6503 8951 15 -1086 520 C ATOM 767 CD1 LEU A 95 -338.238-167.480 161.149 1.00 57.84 C ANISOU 767 CD1 LEU A 95 6898 6394 8685 -68 -1211 509 C ATOM 768 CD2 LEU A 95 -337.691-169.614 160.001 1.00 65.92 C ANISOU 768 CD2 LEU A 95 7760 7379 9909 75 -1135 568 C ATOM 769 N TYR A 96 -337.087-165.775 157.009 1.00 61.79 N ANISOU 769 N TYR A 96 7192 6841 9446 -19 -746 457 N ATOM 770 CA TYR A 96 -335.785-165.151 156.814 1.00 64.45 C ANISOU 770 CA TYR A 96 7392 7150 9945 -69 -736 469 C ATOM 771 C TYR A 96 -335.919-163.645 156.625 1.00 64.55 C ANISOU 771 C TYR A 96 7465 7146 9915 -141 -704 453 C ATOM 772 O TYR A 96 -335.240-162.863 157.301 1.00 59.26 O ANISOU 772 O TYR A 96 6748 6456 9313 -212 -794 454 O ATOM 773 CB TYR A 96 -335.087-165.794 155.619 1.00 60.56 C ANISOU 773 CB TYR A 96 6789 6642 9580 -30 -580 468 C ATOM 774 CG TYR A 96 -333.683-165.303 155.394 1.00 61.17 C ANISOU 774 CG TYR A 96 6694 6687 9860 -80 -546 478 C ATOM 775 CD1 TYR A 96 -332.638-165.737 156.202 1.00 62.71 C ANISOU 775 CD1 TYR A 96 6721 6860 10245 -81 -674 509 C ATOM 776 CD2 TYR A 96 -333.396-164.414 154.368 1.00 58.89 C ANISOU 776 CD2 TYR A 96 6406 6387 9583 -133 -392 467 C ATOM 777 CE1 TYR A 96 -331.344-165.295 155.995 1.00 59.41 C ANISOU 777 CE1 TYR A 96 6120 6409 10046 -129 -645 519 C ATOM 778 CE2 TYR A 96 -332.109-163.972 154.150 1.00 58.89 C ANISOU 778 CE2 TYR A 96 6238 6355 9781 -187 -343 475 C ATOM 779 CZ TYR A 96 -331.088-164.414 154.968 1.00 61.04 C ANISOU 779 CZ TYR A 96 6324 6606 10262 -183 -468 496 C ATOM 780 OH TYR A 96 -329.807-163.974 154.758 1.00 70.35 O ANISOU 780 OH TYR A 96 7312 7750 11667 -240 -422 504 O ATOM 781 N THR A 97 -336.793-163.221 155.708 1.00 63.52 N ANISOU 781 N THR A 97 7442 7016 9679 -128 -591 444 N ATOM 782 CA THR A 97 -337.003-161.793 155.487 1.00 55.83 C ANISOU 782 CA THR A 97 6530 6005 8677 -188 -566 442 C ATOM 783 C THR A 97 -337.532-161.112 156.743 1.00 52.34 C ANISOU 783 C THR A 97 6165 5547 8175 -221 -688 409 C ATOM 784 O THR A 97 -337.157-159.975 157.047 1.00 57.69 O ANISOU 784 O THR A 97 6843 6180 8896 -292 -716 395 O ATOM 785 CB THR A 97 -337.971-161.573 154.325 1.00 53.12 C ANISOU 785 CB THR A 97 6296 5659 8229 -163 -456 458 C ATOM 786 OG1 THR A 97 -339.201-162.255 154.593 1.00 55.61 O ANISOU 786 OG1 THR A 97 6699 6002 8427 -99 -492 444 O ATOM 787 CG2 THR A 97 -337.378-162.089 153.023 1.00 48.16 C ANISOU 787 CG2 THR A 97 5622 5044 7634 -163 -313 478 C ATOM 788 N SER A 98 -338.410-161.794 157.480 1.00 60.49 N ANISOU 788 N SER A 98 7270 6609 9104 -178 -749 387 N ATOM 789 CA SER A 98 -338.977-161.231 158.702 1.00 63.90 C ANISOU 789 CA SER A 98 7793 7028 9458 -219 -836 339 C ATOM 790 C SER A 98 -337.883-160.738 159.646 1.00 54.36 C ANISOU 790 C SER A 98 6533 5805 8316 -310 -951 326 C ATOM 791 O SER A 98 -337.977-159.641 160.203 1.00 50.96 O ANISOU 791 O SER A 98 6164 5330 7867 -380 -978 278 O ATOM 792 CB SER A 98 -339.870-162.271 159.388 1.00 61.29 C ANISOU 792 CB SER A 98 7531 6741 9014 -174 -875 325 C ATOM 793 OG SER A 98 -340.449-161.767 160.573 1.00 84.71 O ANISOU 793 OG SER A 98 10599 9697 11889 -225 -930 266 O ATOM 794 N LEU A 99 -336.823-161.530 159.820 1.00 55.04 N ANISOU 794 N LEU A 99 6498 5917 8496 -315 -1025 369 N ATOM 795 CA LEU A 99 -335.771-161.188 160.772 1.00 49.68 C ANISOU 795 CA LEU A 99 5759 5228 7889 -409 -1174 371 C ATOM 796 C LEU A 99 -334.857-160.073 160.274 1.00 57.93 C ANISOU 796 C LEU A 99 6716 6225 9071 -478 -1139 371 C ATOM 797 O LEU A 99 -334.012-159.594 161.044 1.00 53.43 O ANISOU 797 O LEU A 99 6098 5639 8565 -574 -1268 365 O ATOM 798 CB LEU A 99 -334.956-162.435 161.111 1.00 62.23 C ANISOU 798 CB LEU A 99 7226 6847 9570 -384 -1284 434 C ATOM 799 CG LEU A 99 -335.781-163.524 161.804 1.00 65.34 C ANISOU 799 CG LEU A 99 7719 7280 9826 -340 -1347 446 C ATOM 800 CD1 LEU A 99 -334.982-164.794 162.024 1.00 57.71 C ANISOU 800 CD1 LEU A 99 6626 6322 8981 -302 -1454 523 C ATOM 801 CD2 LEU A 99 -336.290-162.994 163.124 1.00 72.45 C ANISOU 801 CD2 LEU A 99 8779 8191 10560 -434 -1457 400 C ATOM 802 N HIS A 100 -334.995-159.662 159.012 1.00 53.62 N ANISOU 802 N HIS A 100 6154 5655 8565 -444 -977 382 N ATOM 803 CA HIS A 100 -334.393-158.427 158.529 1.00 59.19 C ANISOU 803 CA HIS A 100 6821 6302 9366 -520 -923 380 C ATOM 804 C HIS A 100 -335.356-157.250 158.563 1.00 65.80 C ANISOU 804 C HIS A 100 7811 7082 10110 -544 -883 336 C ATOM 805 O HIS A 100 -334.904-156.100 158.541 1.00 66.75 O ANISOU 805 O HIS A 100 7925 7136 10302 -627 -880 324 O ATOM 806 CB HIS A 100 -333.883-158.600 157.095 1.00 59.63 C ANISOU 806 CB HIS A 100 6781 6356 9522 -492 -762 428 C ATOM 807 CG HIS A 100 -332.791-159.614 156.955 1.00 63.20 C ANISOU 807 CG HIS A 100 7050 6837 10125 -471 -767 458 C ATOM 808 ND1 HIS A 100 -333.042-160.962 156.826 1.00 70.22 N ANISOU 808 ND1 HIS A 100 7918 7769 10993 -376 -752 469 N ATOM 809 CD2 HIS A 100 -331.445-159.475 156.920 1.00 59.02 C ANISOU 809 CD2 HIS A 100 6339 6289 9799 -529 -780 478 C ATOM 810 CE1 HIS A 100 -331.897-161.612 156.718 1.00 73.99 C ANISOU 810 CE1 HIS A 100 8207 8244 11663 -369 -753 493 C ATOM 811 NE2 HIS A 100 -330.912-160.733 156.773 1.00 71.23 N ANISOU 811 NE2 HIS A 100 7747 7860 11456 -461 -770 500 N ATOM 812 N GLY A 101 -336.661-157.509 158.614 1.00 57.43 N ANISOU 812 N GLY A 101 6873 6033 8915 -473 -851 314 N ATOM 813 CA GLY A 101 -337.636-156.442 158.623 1.00 52.77 C ANISOU 813 CA GLY A 101 6404 5371 8274 -479 -807 273 C ATOM 814 C GLY A 101 -337.962-155.879 157.262 1.00 63.31 C ANISOU 814 C GLY A 101 7753 6660 9643 -450 -688 330 C ATOM 815 O GLY A 101 -338.568-154.805 157.182 1.00 62.86 O ANISOU 815 O GLY A 101 7772 6516 9597 -463 -662 315 O ATOM 816 N TYR A 102 -337.565-156.563 156.188 1.00 59.89 N ANISOU 816 N TYR A 102 7254 6272 9229 -418 -615 396 N ATOM 817 CA TYR A 102 -337.906-156.164 154.826 1.00 60.58 C ANISOU 817 CA TYR A 102 7382 6329 9308 -406 -508 463 C ATOM 818 C TYR A 102 -337.527-157.300 153.885 1.00 63.48 C ANISOU 818 C TYR A 102 7694 6770 9654 -371 -426 503 C ATOM 819 O TYR A 102 -336.826-158.240 154.269 1.00 64.52 O ANISOU 819 O TYR A 102 7728 6957 9829 -357 -448 483 O ATOM 820 CB TYR A 102 -337.214-154.860 154.415 1.00 54.63 C ANISOU 820 CB TYR A 102 6615 5489 8651 -499 -471 493 C ATOM 821 CG TYR A 102 -335.709-154.939 154.252 1.00 56.55 C ANISOU 821 CG TYR A 102 6723 5751 9012 -574 -441 507 C ATOM 822 CD1 TYR A 102 -334.862-154.892 155.355 1.00 56.28 C ANISOU 822 CD1 TYR A 102 6598 5720 9065 -627 -543 456 C ATOM 823 CD2 TYR A 102 -335.134-155.028 152.991 1.00 55.61 C ANISOU 823 CD2 TYR A 102 6565 5642 8920 -603 -309 570 C ATOM 824 CE1 TYR A 102 -333.486-154.947 155.204 1.00 56.31 C ANISOU 824 CE1 TYR A 102 6449 5733 9213 -696 -524 474 C ATOM 825 CE2 TYR A 102 -333.764-155.084 152.833 1.00 57.14 C ANISOU 825 CE2 TYR A 102 6614 5845 9251 -673 -258 576 C ATOM 826 CZ TYR A 102 -332.943-155.040 153.940 1.00 58.53 C ANISOU 826 CZ TYR A 102 6673 6019 9546 -713 -371 530 C ATOM 827 OH TYR A 102 -331.578-155.097 153.773 1.00 63.25 O ANISOU 827 OH TYR A 102 7098 6619 10315 -781 -328 541 O ATOM 828 N PHE A 103 -337.989-157.194 152.638 1.00 58.02 N ANISOU 828 N PHE A 103 7071 6072 8902 -364 -336 562 N ATOM 829 CA PHE A 103 -337.792-158.256 151.651 1.00 60.83 C ANISOU 829 CA PHE A 103 7411 6492 9208 -340 -238 584 C ATOM 830 C PHE A 103 -336.411-158.093 151.021 1.00 60.28 C ANISOU 830 C PHE A 103 7246 6418 9241 -418 -126 602 C ATOM 831 O PHE A 103 -336.226-157.364 150.044 1.00 57.98 O ANISOU 831 O PHE A 103 7006 6092 8934 -487 -34 657 O ATOM 832 CB PHE A 103 -338.898-158.234 150.603 1.00 53.99 C ANISOU 832 CB PHE A 103 6678 5624 8210 -320 -204 638 C ATOM 833 CG PHE A 103 -338.933-159.465 149.760 1.00 59.94 C ANISOU 833 CG PHE A 103 7448 6448 8880 -295 -120 636 C ATOM 834 CD1 PHE A 103 -339.631-160.585 150.179 1.00 56.46 C ANISOU 834 CD1 PHE A 103 7012 6055 8383 -214 -169 595 C ATOM 835 CD2 PHE A 103 -338.239-159.521 148.564 1.00 64.20 C ANISOU 835 CD2 PHE A 103 8000 6997 9395 -362 22 666 C ATOM 836 CE1 PHE A 103 -339.651-161.739 149.411 1.00 59.46 C ANISOU 836 CE1 PHE A 103 7412 6487 8695 -195 -88 581 C ATOM 837 CE2 PHE A 103 -338.253-160.669 147.792 1.00 71.64 C ANISOU 837 CE2 PHE A 103 8969 7994 10255 -348 117 642 C ATOM 838 CZ PHE A 103 -338.961-161.783 148.217 1.00 65.31 C ANISOU 838 CZ PHE A 103 8172 7234 9409 -262 57 597 C ATOM 839 N VAL A 104 -335.433-158.807 151.584 1.00 55.86 N ANISOU 839 N VAL A 104 6539 5888 8796 -409 -134 561 N ATOM 840 CA VAL A 104 -334.021-158.584 151.280 1.00 62.97 C ANISOU 840 CA VAL A 104 7299 6773 9854 -483 -45 565 C ATOM 841 C VAL A 104 -333.623-159.176 149.935 1.00 66.41 C ANISOU 841 C VAL A 104 7727 7234 10272 -499 155 575 C ATOM 842 O VAL A 104 -332.485-159.003 149.491 1.00 78.86 O ANISOU 842 O VAL A 104 9188 8795 11981 -567 276 575 O ATOM 843 CB VAL A 104 -333.117-159.159 152.387 1.00 58.20 C ANISOU 843 CB VAL A 104 6521 6183 9410 -466 -147 528 C ATOM 844 CG1 VAL A 104 -333.327-158.412 153.679 1.00 56.34 C ANISOU 844 CG1 VAL A 104 6310 5919 9178 -493 -328 511 C ATOM 845 CG2 VAL A 104 -333.380-160.655 152.568 1.00 57.34 C ANISOU 845 CG2 VAL A 104 6384 6125 9278 -365 -163 502 C ATOM 846 N PHE A 105 -334.539-159.876 149.274 1.00 62.23 N ANISOU 846 N PHE A 105 7321 6741 9582 -449 199 576 N ATOM 847 CA PHE A 105 -334.213-160.558 148.027 1.00 61.44 C ANISOU 847 CA PHE A 105 7241 6668 9438 -473 395 564 C ATOM 848 C PHE A 105 -334.523-159.731 146.786 1.00 66.19 C ANISOU 848 C PHE A 105 8003 7254 9894 -569 501 628 C ATOM 849 O PHE A 105 -334.308-160.213 145.669 1.00 70.31 O ANISOU 849 O PHE A 105 8581 7799 10334 -615 676 617 O ATOM 850 CB PHE A 105 -334.945-161.904 147.959 1.00 62.24 C ANISOU 850 CB PHE A 105 7391 6815 9443 -380 385 521 C ATOM 851 CG PHE A 105 -334.540-162.864 149.044 1.00 63.57 C ANISOU 851 CG PHE A 105 7405 6990 9757 -294 298 472 C ATOM 852 CD1 PHE A 105 -333.212-163.240 149.192 1.00 59.81 C ANISOU 852 CD1 PHE A 105 6732 6495 9498 -299 371 442 C ATOM 853 CD2 PHE A 105 -335.484-163.393 149.912 1.00 58.07 C ANISOU 853 CD2 PHE A 105 6757 6314 8993 -213 140 465 C ATOM 854 CE1 PHE A 105 -332.830-164.122 150.190 1.00 60.77 C ANISOU 854 CE1 PHE A 105 6711 6612 9766 -221 262 419 C ATOM 855 CE2 PHE A 105 -335.111-164.281 150.909 1.00 62.00 C ANISOU 855 CE2 PHE A 105 7133 6814 9611 -146 47 439 C ATOM 856 CZ PHE A 105 -333.780-164.643 151.048 1.00 63.27 C ANISOU 856 CZ PHE A 105 7102 6951 9988 -149 95 423 C ATOM 857 N GLY A 106 -335.018-158.507 146.947 1.00 71.08 N ANISOU 857 N GLY A 106 8706 7825 10475 -608 402 696 N ATOM 858 CA GLY A 106 -335.230-157.623 145.825 1.00 71.57 C ANISOU 858 CA GLY A 106 8916 7855 10420 -709 478 782 C ATOM 859 C GLY A 106 -336.458-157.966 145.007 1.00 77.54 C ANISOU 859 C GLY A 106 9864 8640 10957 -694 451 826 C ATOM 860 O GLY A 106 -337.151-158.957 145.261 1.00 74.44 O ANISOU 860 O GLY A 106 9483 8295 10505 -605 392 779 O ATOM 861 N PRO A 107 -336.752-157.136 144.000 1.00 77.49 N ANISOU 861 N PRO A 107 10013 8601 10829 -793 481 928 N ATOM 862 CA PRO A 107 -337.953-157.369 143.177 1.00 70.98 C ANISOU 862 CA PRO A 107 9378 7798 9795 -795 419 992 C ATOM 863 C PRO A 107 -337.949-158.692 142.431 1.00 70.59 C ANISOU 863 C PRO A 107 9383 7830 9607 -803 540 926 C ATOM 864 O PRO A 107 -339.022-159.269 142.218 1.00 82.75 O ANISOU 864 O PRO A 107 11022 9402 11016 -759 444 934 O ATOM 865 CB PRO A 107 -337.949-156.175 142.207 1.00 64.71 C ANISOU 865 CB PRO A 107 8730 6943 8914 -928 441 1128 C ATOM 866 CG PRO A 107 -336.555-155.637 142.247 1.00 62.80 C ANISOU 866 CG PRO A 107 8381 6671 8807 -1014 595 1109 C ATOM 867 CD PRO A 107 -336.064-155.886 143.637 1.00 59.93 C ANISOU 867 CD PRO A 107 7803 6308 8661 -911 542 1004 C ATOM 868 N THR A 108 -336.782-159.188 142.013 1.00 72.20 N ANISOU 868 N THR A 108 9521 8061 9850 -861 756 855 N ATOM 869 CA THR A 108 -336.736-160.492 141.359 1.00 72.87 C ANISOU 869 CA THR A 108 9652 8208 9828 -863 893 766 C ATOM 870 C THR A 108 -337.108-161.604 142.331 1.00 73.62 C ANISOU 870 C THR A 108 9629 8329 10013 -712 797 675 C ATOM 871 O THR A 108 -337.924-162.477 142.009 1.00 80.20 O ANISOU 871 O THR A 108 10562 9200 10712 -682 764 646 O ATOM 872 CB THR A 108 -335.352-160.745 140.759 1.00 72.61 C ANISOU 872 CB THR A 108 9547 8180 9863 -951 1171 696 C ATOM 873 OG1 THR A 108 -335.174-159.921 139.602 1.00 74.41 O ANISOU 873 OG1 THR A 108 9946 8397 9930 -1118 1288 781 O ATOM 874 CG2 THR A 108 -335.210-162.207 140.356 1.00 69.68 C ANISOU 874 CG2 THR A 108 9173 7851 9450 -922 1321 568 C ATOM 875 N GLY A 109 -336.521-161.591 143.530 1.00 68.97 N ANISOU 875 N GLY A 109 8840 7719 9649 -629 742 633 N ATOM 876 CA GLY A 109 -336.941-162.536 144.549 1.00 70.76 C ANISOU 876 CA GLY A 109 8974 7963 9948 -498 623 571 C ATOM 877 C GLY A 109 -338.404-162.382 144.906 1.00 69.35 C ANISOU 877 C GLY A 109 8904 7791 9656 -442 423 621 C ATOM 878 O GLY A 109 -339.055-163.348 145.313 1.00 72.50 O ANISOU 878 O GLY A 109 9299 8217 10031 -360 355 576 O ATOM 879 N CYS A 110 -338.941-161.171 144.747 1.00 61.89 N ANISOU 879 N CYS A 110 8047 6810 8658 -487 333 716 N ATOM 880 CA CYS A 110 -340.357-160.938 144.999 1.00 66.40 C ANISOU 880 CA CYS A 110 8704 7372 9152 -435 155 768 C ATOM 881 C CYS A 110 -341.218-161.725 144.022 1.00 67.42 C ANISOU 881 C CYS A 110 8978 7545 9092 -455 157 778 C ATOM 882 O CYS A 110 -342.228-162.321 144.412 1.00 68.48 O ANISOU 882 O CYS A 110 9123 7699 9198 -382 44 762 O ATOM 883 CB CYS A 110 -340.649-159.439 144.904 1.00 60.41 C ANISOU 883 CB CYS A 110 8002 6543 8409 -483 75 872 C ATOM 884 SG CYS A 110 -342.224-158.888 145.570 1.00 74.40 S ANISOU 884 SG CYS A 110 9805 8265 10198 -397 -139 923 S ATOM 885 N ASN A 111 -340.828-161.740 142.745 1.00 60.45 N ANISOU 885 N ASN A 111 8215 6680 8072 -569 288 803 N ATOM 886 CA ASN A 111 -341.565-162.508 141.749 1.00 63.71 C ANISOU 886 CA ASN A 111 8789 7138 8280 -616 292 804 C ATOM 887 C ASN A 111 -341.423-164.007 141.982 1.00 68.43 C ANISOU 887 C ASN A 111 9328 7778 8895 -552 370 673 C ATOM 888 O ASN A 111 -342.381-164.761 141.785 1.00 72.48 O ANISOU 888 O ASN A 111 9918 8319 9303 -532 290 659 O ATOM 889 CB ASN A 111 -341.093-162.133 140.345 1.00 67.57 C ANISOU 889 CB ASN A 111 9444 7635 8595 -777 430 855 C ATOM 890 CG ASN A 111 -341.744-160.868 139.831 1.00 73.20 C ANISOU 890 CG ASN A 111 10288 8305 9219 -851 291 1019 C ATOM 891 OD1 ASN A 111 -342.796-160.457 140.318 1.00 76.65 O ANISOU 891 OD1 ASN A 111 10713 8710 9701 -779 84 1088 O ATOM 892 ND2 ASN A 111 -341.130-160.250 138.835 1.00 78.16 N ANISOU 892 ND2 ASN A 111 11040 8924 9733 -998 411 1084 N ATOM 893 N LEU A 112 -340.237-164.459 142.398 1.00 71.31 N ANISOU 893 N LEU A 112 9549 8138 9410 -522 518 582 N ATOM 894 CA LEU A 112 -340.042-165.875 142.693 1.00 70.37 C ANISOU 894 CA LEU A 112 9355 8035 9349 -451 585 466 C ATOM 895 C LEU A 112 -340.840-166.291 143.922 1.00 67.33 C ANISOU 895 C LEU A 112 8885 7648 9047 -325 399 461 C ATOM 896 O LEU A 112 -341.629-167.243 143.875 1.00 69.84 O ANISOU 896 O LEU A 112 9256 7985 9293 -291 352 425 O ATOM 897 CB LEU A 112 -338.556-166.170 142.896 1.00 73.90 C ANISOU 897 CB LEU A 112 9638 8458 9982 -441 769 387 C ATOM 898 CG LEU A 112 -337.697-166.294 141.639 1.00 80.64 C ANISOU 898 CG LEU A 112 10561 9314 10766 -559 1028 336 C ATOM 899 CD1 LEU A 112 -336.254-165.913 141.934 1.00 81.02 C ANISOU 899 CD1 LEU A 112 10419 9327 11039 -566 1171 310 C ATOM 900 CD2 LEU A 112 -337.773-167.714 141.112 1.00 79.41 C ANISOU 900 CD2 LEU A 112 10456 9164 10552 -548 1155 218 C ATOM 901 N GLU A 113 -340.641-165.586 145.038 1.00 58.25 N ANISOU 901 N GLU A 113 7613 6475 8045 -269 299 493 N ATOM 902 CA GLU A 113 -341.334-165.942 146.270 1.00 58.02 C ANISOU 902 CA GLU A 113 7514 6445 8084 -168 145 483 C ATOM 903 C GLU A 113 -342.842-165.811 146.104 1.00 64.49 C ANISOU 903 C GLU A 113 8450 7278 8776 -161 10 533 C ATOM 904 O GLU A 113 -343.607-166.636 146.617 1.00 65.92 O ANISOU 904 O GLU A 113 8622 7473 8950 -99 -63 503 O ATOM 905 CB GLU A 113 -340.829-165.071 147.421 1.00 56.43 C ANISOU 905 CB GLU A 113 7194 6216 8033 -139 70 504 C ATOM 906 CG GLU A 113 -341.274-165.524 148.803 1.00 63.50 C ANISOU 906 CG GLU A 113 8016 7113 8997 -52 -58 479 C ATOM 907 CD GLU A 113 -342.662-165.033 149.167 1.00 74.09 C ANISOU 907 CD GLU A 113 9432 8451 10267 -29 -187 515 C ATOM 908 OE1 GLU A 113 -343.019-163.902 148.772 1.00 73.69 O ANISOU 908 OE1 GLU A 113 9439 8373 10188 -68 -214 573 O ATOM 909 OE2 GLU A 113 -343.400-165.782 149.842 1.00 78.20 O ANISOU 909 OE2 GLU A 113 9948 8988 10777 27 -255 489 O ATOM 910 N GLY A 114 -343.289-164.789 145.373 1.00 59.53 N ANISOU 910 N GLY A 114 7924 6637 8059 -227 -27 618 N ATOM 911 CA GLY A 114 -344.715-164.615 145.164 1.00 59.66 C ANISOU 911 CA GLY A 114 8026 6653 7989 -219 -171 678 C ATOM 912 C GLY A 114 -345.304-165.685 144.268 1.00 63.35 C ANISOU 912 C GLY A 114 8603 7161 8304 -255 -158 654 C ATOM 913 O GLY A 114 -346.383-166.213 144.547 1.00 65.74 O ANISOU 913 O GLY A 114 8911 7475 8591 -212 -267 650 O ATOM 914 N PHE A 115 -344.605-166.022 143.182 1.00 60.66 N ANISOU 914 N PHE A 115 8355 6842 7852 -345 -16 628 N ATOM 915 CA PHE A 115 -345.084-167.070 142.285 1.00 68.65 C ANISOU 915 CA PHE A 115 9492 7888 8702 -399 12 584 C ATOM 916 C PHE A 115 -345.222-168.404 143.014 1.00 74.98 C ANISOU 916 C PHE A 115 10209 8697 9583 -310 23 481 C ATOM 917 O PHE A 115 -346.273-169.054 142.950 1.00 72.65 O ANISOU 917 O PHE A 115 9963 8416 9223 -302 -77 476 O ATOM 918 CB PHE A 115 -344.139-167.204 141.086 1.00 63.16 C ANISOU 918 CB PHE A 115 8911 7207 7881 -519 209 547 C ATOM 919 CG PHE A 115 -344.463-168.361 140.180 1.00 74.12 C ANISOU 919 CG PHE A 115 10439 8624 9099 -587 274 469 C ATOM 920 CD1 PHE A 115 -345.409-168.230 139.176 1.00 77.73 C ANISOU 920 CD1 PHE A 115 11090 9107 9336 -696 167 538 C ATOM 921 CD2 PHE A 115 -343.819-169.581 140.331 1.00 77.84 C ANISOU 921 CD2 PHE A 115 10849 9086 9639 -547 433 329 C ATOM 922 CE1 PHE A 115 -345.711-169.294 138.344 1.00 77.67 C ANISOU 922 CE1 PHE A 115 11227 9125 9157 -776 221 456 C ATOM 923 CE2 PHE A 115 -344.119-170.648 139.503 1.00 73.71 C ANISOU 923 CE2 PHE A 115 10464 8576 8965 -615 504 241 C ATOM 924 CZ PHE A 115 -345.065-170.503 138.508 1.00 69.38 C ANISOU 924 CZ PHE A 115 10124 8063 8175 -736 400 298 C ATOM 925 N PHE A 116 -344.167-168.832 143.713 1.00 69.87 N ANISOU 925 N PHE A 116 9428 8032 9088 -248 134 407 N ATOM 926 CA PHE A 116 -344.177-170.167 144.304 1.00 68.16 C ANISOU 926 CA PHE A 116 9143 7807 8948 -174 153 319 C ATOM 927 C PHE A 116 -345.097-170.251 145.515 1.00 69.23 C ANISOU 927 C PHE A 116 9204 7942 9159 -86 -16 350 C ATOM 928 O PHE A 116 -345.707-171.302 145.753 1.00 65.67 O ANISOU 928 O PHE A 116 8760 7491 8700 -53 -51 308 O ATOM 929 CB PHE A 116 -342.754-170.588 144.670 1.00 59.25 C ANISOU 929 CB PHE A 116 7882 6647 7984 -134 303 249 C ATOM 930 CG PHE A 116 -341.987-171.155 143.515 1.00 66.13 C ANISOU 930 CG PHE A 116 8818 7508 8800 -205 515 165 C ATOM 931 CD1 PHE A 116 -342.348-172.380 142.968 1.00 65.78 C ANISOU 931 CD1 PHE A 116 8859 7455 8680 -220 578 78 C ATOM 932 CD2 PHE A 116 -340.915-170.465 142.968 1.00 63.19 C ANISOU 932 CD2 PHE A 116 8427 7129 8453 -269 667 164 C ATOM 933 CE1 PHE A 116 -341.653-172.912 141.897 1.00 65.96 C ANISOU 933 CE1 PHE A 116 8956 7460 8647 -295 799 -21 C ATOM 934 CE2 PHE A 116 -340.217-170.988 141.895 1.00 64.79 C ANISOU 934 CE2 PHE A 116 8695 7319 8602 -345 896 72 C ATOM 935 CZ PHE A 116 -340.587-172.217 141.358 1.00 64.51 C ANISOU 935 CZ PHE A 116 8754 7273 8485 -358 968 -27 C ATOM 936 N ALA A 117 -345.212-169.172 146.290 1.00 64.40 N ANISOU 936 N ALA A 117 8528 7324 8619 -55 -108 414 N ATOM 937 CA ALA A 117 -346.165-169.172 147.393 1.00 63.42 C ANISOU 937 CA ALA A 117 8352 7198 8548 12 -243 433 C ATOM 938 C ALA A 117 -347.598-169.170 146.872 1.00 67.42 C ANISOU 938 C ALA A 117 8945 7718 8954 -13 -347 473 C ATOM 939 O ALA A 117 -348.456-169.892 147.393 1.00 67.77 O ANISOU 939 O ALA A 117 8971 7768 9012 24 -410 453 O ATOM 940 CB ALA A 117 -345.914-167.975 148.308 1.00 53.17 C ANISOU 940 CB ALA A 117 6977 5878 7347 38 -294 472 C ATOM 941 N THR A 118 -347.871-168.375 145.835 1.00 67.53 N ANISOU 941 N THR A 118 9052 7733 8872 -84 -373 540 N ATOM 942 CA THR A 118 -349.208-168.354 145.249 1.00 67.80 C ANISOU 942 CA THR A 118 9162 7776 8824 -116 -500 595 C ATOM 943 C THR A 118 -349.527-169.670 144.550 1.00 68.56 C ANISOU 943 C THR A 118 9344 7901 8806 -161 -477 537 C ATOM 944 O THR A 118 -350.651-170.176 144.654 1.00 63.94 O ANISOU 944 O THR A 118 8759 7323 8214 -153 -581 542 O ATOM 945 CB THR A 118 -349.335-167.185 144.271 1.00 64.44 C ANISOU 945 CB THR A 118 8828 7337 8321 -192 -553 700 C ATOM 946 OG1 THR A 118 -349.006-165.963 144.942 1.00 72.63 O ANISOU 946 OG1 THR A 118 9786 8330 9481 -151 -566 745 O ATOM 947 CG2 THR A 118 -350.753-167.090 143.724 1.00 61.53 C ANISOU 947 CG2 THR A 118 8515 6966 7898 -222 -724 778 C ATOM 948 N LEU A 119 -348.554-170.234 143.828 1.00 71.02 N ANISOU 948 N LEU A 119 9724 8222 9038 -215 -330 473 N ATOM 949 CA LEU A 119 -348.771-171.516 143.164 1.00 69.72 C ANISOU 949 CA LEU A 119 9651 8070 8768 -264 -284 394 C ATOM 950 C LEU A 119 -349.094-172.611 144.174 1.00 71.45 C ANISOU 950 C LEU A 119 9774 8274 9101 -177 -299 329 C ATOM 951 O LEU A 119 -349.960-173.457 143.927 1.00 69.79 O ANISOU 951 O LEU A 119 9615 8069 8834 -204 -358 303 O ATOM 952 CB LEU A 119 -347.539-171.896 142.343 1.00 65.63 C ANISOU 952 CB LEU A 119 9204 7548 8182 -326 -81 314 C ATOM 953 CG LEU A 119 -347.667-173.097 141.402 1.00 66.88 C ANISOU 953 CG LEU A 119 9499 7710 8203 -406 0 216 C ATOM 954 CD1 LEU A 119 -348.335-172.705 140.091 1.00 63.15 C ANISOU 954 CD1 LEU A 119 9227 7275 7493 -552 -72 271 C ATOM 955 CD2 LEU A 119 -346.305-173.713 141.151 1.00 69.73 C ANISOU 955 CD2 LEU A 119 9843 8039 8612 -407 242 98 C ATOM 956 N GLY A 120 -348.411-172.607 145.320 1.00 65.96 N ANISOU 956 N GLY A 120 8943 7557 8562 -86 -258 311 N ATOM 957 CA GLY A 120 -348.675-173.623 146.326 1.00 64.75 C ANISOU 957 CA GLY A 120 8712 7384 8506 -15 -279 268 C ATOM 958 C GLY A 120 -350.086-173.542 146.873 1.00 66.16 C ANISOU 958 C GLY A 120 8870 7575 8691 1 -425 315 C ATOM 959 O GLY A 120 -350.794-174.549 146.955 1.00 67.48 O ANISOU 959 O GLY A 120 9053 7736 8849 -3 -456 282 O ATOM 960 N GLY A 121 -350.513-172.337 147.254 1.00 66.54 N ANISOU 960 N GLY A 121 8877 7632 8774 18 -506 386 N ATOM 961 CA GLY A 121 -351.870-172.166 147.740 1.00 64.68 C ANISOU 961 CA GLY A 121 8602 7398 8575 35 -624 425 C ATOM 962 C GLY A 121 -352.918-172.443 146.681 1.00 65.70 C ANISOU 962 C GLY A 121 8810 7541 8611 -35 -714 451 C ATOM 963 O GLY A 121 -354.021-172.893 146.998 1.00 60.56 O ANISOU 963 O GLY A 121 8122 6889 7998 -30 -792 454 O ATOM 964 N GLU A 122 -352.586-172.189 145.413 1.00 69.15 N ANISOU 964 N GLU A 122 9362 7991 8920 -114 -706 471 N ATOM 965 CA GLU A 122 -353.526-172.440 144.325 1.00 69.94 C ANISOU 965 CA GLU A 122 9563 8107 8903 -205 -814 503 C ATOM 966 C GLU A 122 -353.697-173.936 144.071 1.00 74.00 C ANISOU 966 C GLU A 122 10134 8625 9356 -243 -776 411 C ATOM 967 O GLU A 122 -354.824-174.425 143.919 1.00 72.97 O ANISOU 967 O GLU A 122 10008 8499 9218 -278 -890 422 O ATOM 968 CB GLU A 122 -353.058-171.726 143.057 1.00 70.60 C ANISOU 968 CB GLU A 122 9784 8205 8837 -300 -812 555 C ATOM 969 CG GLU A 122 -353.564-170.303 142.910 1.00 74.07 C ANISOU 969 CG GLU A 122 10201 8629 9314 -300 -944 687 C ATOM 970 CD GLU A 122 -355.039-170.242 142.561 1.00 78.36 C ANISOU 970 CD GLU A 122 10737 9168 9867 -333 -1149 767 C ATOM 971 OE1 GLU A 122 -355.828-169.707 143.369 1.00 74.94 O ANISOU 971 OE1 GLU A 122 10161 8703 9610 -253 -1235 812 O ATOM 972 OE2 GLU A 122 -355.409-170.735 141.476 1.00 82.88 O ANISOU 972 OE2 GLU A 122 11446 9767 10278 -446 -1223 780 O ATOM 973 N ILE A 123 -352.586-174.680 144.012 1.00 67.01 N ANISOU 973 N ILE A 123 9285 7727 8448 -238 -614 318 N ATOM 974 CA ILE A 123 -352.668-176.126 143.821 1.00 63.69 C ANISOU 974 CA ILE A 123 8916 7287 7997 -266 -561 219 C ATOM 975 C ILE A 123 -353.464-176.768 144.950 1.00 69.08 C ANISOU 975 C ILE A 123 9488 7950 8810 -200 -624 217 C ATOM 976 O ILE A 123 -354.268-177.682 144.723 1.00 67.15 O ANISOU 976 O ILE A 123 9280 7695 8538 -248 -676 184 O ATOM 977 CB ILE A 123 -351.258-176.737 143.705 1.00 61.12 C ANISOU 977 CB ILE A 123 8611 6928 7686 -247 -363 121 C ATOM 978 CG1 ILE A 123 -350.550-176.229 142.451 1.00 57.45 C ANISOU 978 CG1 ILE A 123 8278 6482 7069 -341 -270 107 C ATOM 979 CG2 ILE A 123 -351.328-178.262 143.667 1.00 66.72 C ANISOU 979 CG2 ILE A 123 9354 7588 8408 -257 -301 15 C ATOM 980 CD1 ILE A 123 -349.070-176.568 142.403 1.00 53.17 C ANISOU 980 CD1 ILE A 123 7713 5902 6587 -311 -54 17 C ATOM 981 N ALA A 124 -353.263-176.294 146.182 1.00 64.17 N ANISOU 981 N ALA A 124 8737 7322 8323 -105 -619 251 N ATOM 982 CA ALA A 124 -354.013-176.831 147.312 1.00 59.63 C ANISOU 982 CA ALA A 124 8070 6732 7854 -58 -663 254 C ATOM 983 C ALA A 124 -355.506-176.563 147.157 1.00 69.19 C ANISOU 983 C ALA A 124 9257 7962 9070 -97 -802 306 C ATOM 984 O ALA A 124 -356.332-177.466 147.342 1.00 69.52 O ANISOU 984 O ALA A 124 9286 7992 9137 -122 -839 284 O ATOM 985 CB ALA A 124 -353.489-176.239 148.620 1.00 55.80 C ANISOU 985 CB ALA A 124 7481 6242 7478 28 -631 280 C ATOM 986 N LEU A 125 -355.867-175.322 146.811 1.00 72.06 N ANISOU 986 N LEU A 125 9604 8346 9431 -103 -883 381 N ATOM 987 CA LEU A 125 -357.274-174.959 146.654 1.00 64.06 C ANISOU 987 CA LEU A 125 8537 7337 8466 -130 -1028 444 C ATOM 988 C LEU A 125 -357.970-175.864 145.643 1.00 63.17 C ANISOU 988 C LEU A 125 8510 7232 8258 -232 -1113 427 C ATOM 989 O LEU A 125 -359.049-176.404 145.913 1.00 64.09 O ANISOU 989 O LEU A 125 8563 7342 8448 -250 -1187 428 O ATOM 990 CB LEU A 125 -357.395-173.494 146.228 1.00 59.34 C ANISOU 990 CB LEU A 125 7924 6739 7882 -125 -1109 536 C ATOM 991 CG LEU A 125 -358.779-173.081 145.719 1.00 56.85 C ANISOU 991 CG LEU A 125 7561 6417 7621 -164 -1289 620 C ATOM 992 CD1 LEU A 125 -359.828-173.209 146.819 1.00 50.84 C ANISOU 992 CD1 LEU A 125 6636 5635 7048 -107 -1303 611 C ATOM 993 CD2 LEU A 125 -358.754-171.673 145.151 1.00 65.70 C ANISOU 993 CD2 LEU A 125 8691 7522 8751 -165 -1378 725 C ATOM 994 N TRP A 126 -357.360-176.049 144.472 1.00 59.95 N ANISOU 994 N TRP A 126 8256 6838 7684 -311 -1096 404 N ATOM 995 CA TRP A 126 -357.978-176.850 143.431 1.00 73.47 C ANISOU 995 CA TRP A 126 10083 8559 9275 -431 -1182 380 C ATOM 996 C TRP A 126 -357.894-178.347 143.709 1.00 79.29 C ANISOU 996 C TRP A 126 10845 9266 10016 -443 -1092 268 C ATOM 997 O TRP A 126 -358.725-179.105 143.191 1.00 77.24 O ANISOU 997 O TRP A 126 10635 9002 9711 -533 -1183 245 O ATOM 998 CB TRP A 126 -357.346-176.505 142.076 1.00 71.13 C ANISOU 998 CB TRP A 126 9970 8286 8772 -532 -1176 385 C ATOM 999 CG TRP A 126 -357.701-175.120 141.658 1.00 81.18 C ANISOU 999 CG TRP A 126 11232 9576 10035 -546 -1315 520 C ATOM 1000 CD1 TRP A 126 -356.885-174.029 141.652 1.00 83.95 C ANISOU 1000 CD1 TRP A 126 11588 9929 10381 -507 -1256 571 C ATOM 1001 CD2 TRP A 126 -358.990-174.660 141.235 1.00 80.26 C ANISOU 1001 CD2 TRP A 126 11082 9464 9947 -599 -1547 631 C ATOM 1002 NE1 TRP A 126 -357.579-172.922 141.229 1.00 80.11 N ANISOU 1002 NE1 TRP A 126 11087 9440 9910 -533 -1434 709 N ATOM 1003 CE2 TRP A 126 -358.875-173.282 140.970 1.00 78.20 C ANISOU 1003 CE2 TRP A 126 10816 9199 9699 -584 -1620 751 C ATOM 1004 CE3 TRP A 126 -360.228-175.283 141.044 1.00 77.30 C ANISOU 1004 CE3 TRP A 126 10674 9089 9607 -661 -1708 644 C ATOM 1005 CZ2 TRP A 126 -359.949-172.515 140.524 1.00 82.38 C ANISOU 1005 CZ2 TRP A 126 11302 9715 10283 -620 -1855 892 C ATOM 1006 CZ3 TRP A 126 -361.295-174.520 140.599 1.00 73.50 C ANISOU 1006 CZ3 TRP A 126 10140 8605 9183 -700 -1944 781 C ATOM 1007 CH2 TRP A 126 -361.149-173.152 140.345 1.00 78.52 C ANISOU 1007 CH2 TRP A 126 10766 9227 9840 -674 -2019 906 C ATOM 1008 N SER A 127 -356.934-178.791 144.522 1.00 75.15 N ANISOU 1008 N SER A 127 10284 8711 9558 -358 -932 206 N ATOM 1009 CA SER A 127 -356.956-180.177 144.975 1.00 69.71 C ANISOU 1009 CA SER A 127 9594 7974 8918 -355 -865 122 C ATOM 1010 C SER A 127 -358.205-180.458 145.801 1.00 67.74 C ANISOU 1010 C SER A 127 9228 7720 8791 -345 -960 161 C ATOM 1011 O SER A 127 -358.845-181.502 145.632 1.00 70.99 O ANISOU 1011 O SER A 127 9668 8102 9201 -409 -992 117 O ATOM 1012 CB SER A 127 -355.692-180.490 145.777 1.00 62.79 C ANISOU 1012 CB SER A 127 8680 7058 8119 -258 -706 78 C ATOM 1013 OG SER A 127 -354.553-180.551 144.934 1.00 60.26 O ANISOU 1013 OG SER A 127 8461 6725 7710 -279 -588 14 O ATOM 1014 N LEU A 128 -358.572-179.533 146.693 1.00 59.90 N ANISOU 1014 N LEU A 128 8104 6748 7908 -273 -993 235 N ATOM 1015 CA LEU A 128 -359.807-179.690 147.455 1.00 62.95 C ANISOU 1015 CA LEU A 128 8368 7129 8419 -272 -1059 267 C ATOM 1016 C LEU A 128 -361.023-179.663 146.539 1.00 68.13 C ANISOU 1016 C LEU A 128 9024 7802 9062 -367 -1224 302 C ATOM 1017 O LEU A 128 -362.003-180.378 146.775 1.00 69.12 O ANISOU 1017 O LEU A 128 9091 7910 9262 -411 -1273 293 O ATOM 1018 CB LEU A 128 -359.920-178.596 148.517 1.00 60.10 C ANISOU 1018 CB LEU A 128 7880 6783 8175 -184 -1038 322 C ATOM 1019 CG LEU A 128 -358.815-178.508 149.572 1.00 62.75 C ANISOU 1019 CG LEU A 128 8206 7107 8529 -101 -908 302 C ATOM 1020 CD1 LEU A 128 -359.252-177.606 150.716 1.00 61.60 C ANISOU 1020 CD1 LEU A 128 7942 6969 8494 -44 -890 337 C ATOM 1021 CD2 LEU A 128 -358.442-179.889 150.090 1.00 66.72 C ANISOU 1021 CD2 LEU A 128 8747 7570 9032 -106 -832 249 C ATOM 1022 N VAL A 129 -360.980-178.840 145.489 1.00 68.36 N ANISOU 1022 N VAL A 129 9117 7859 8998 -408 -1320 351 N ATOM 1023 CA VAL A 129 -362.083-178.789 144.534 1.00 68.03 C ANISOU 1023 CA VAL A 129 9087 7832 8931 -513 -1513 402 C ATOM 1024 C VAL A 129 -362.127-180.065 143.702 1.00 71.37 C ANISOU 1024 C VAL A 129 9657 8244 9217 -634 -1529 319 C ATOM 1025 O VAL A 129 -363.198-180.651 143.495 1.00 72.21 O ANISOU 1025 O VAL A 129 9729 8342 9366 -714 -1651 322 O ATOM 1026 CB VAL A 129 -361.964-177.532 143.652 1.00 62.03 C ANISOU 1026 CB VAL A 129 8376 7098 8096 -533 -1625 496 C ATOM 1027 CG1 VAL A 129 -363.037-177.534 142.576 1.00 55.03 C ANISOU 1027 CG1 VAL A 129 7523 6224 7162 -658 -1857 563 C ATOM 1028 CG2 VAL A 129 -362.062-176.268 144.508 1.00 56.79 C ANISOU 1028 CG2 VAL A 129 7552 6423 7600 -415 -1615 571 C ATOM 1029 N VAL A 130 -360.968-180.520 143.217 1.00 70.12 N ANISOU 1029 N VAL A 130 9659 8077 8906 -652 -1399 236 N ATOM 1030 CA VAL A 130 -360.925-181.734 142.406 1.00 70.80 C ANISOU 1030 CA VAL A 130 9902 8137 8860 -769 -1384 133 C ATOM 1031 C VAL A 130 -361.328-182.948 143.234 1.00 71.63 C ANISOU 1031 C VAL A 130 9936 8187 9092 -754 -1330 70 C ATOM 1032 O VAL A 130 -362.065-183.821 142.759 1.00 64.34 O ANISOU 1032 O VAL A 130 9065 7241 8139 -865 -1412 26 O ATOM 1033 CB VAL A 130 -359.530-181.907 141.777 1.00 68.59 C ANISOU 1033 CB VAL A 130 9791 7847 8424 -780 -1215 44 C ATOM 1034 CG1 VAL A 130 -359.312-183.347 141.314 1.00 66.72 C ANISOU 1034 CG1 VAL A 130 9688 7550 8113 -862 -1126 -99 C ATOM 1035 CG2 VAL A 130 -359.362-180.949 140.610 1.00 65.12 C ANISOU 1035 CG2 VAL A 130 9480 7462 7802 -865 -1295 99 C ATOM 1036 N LEU A 131 -360.861-183.022 144.484 1.00 68.58 N ANISOU 1036 N LEU A 131 9441 7774 8841 -629 -1201 69 N ATOM 1037 CA LEU A 131 -361.252-184.135 145.342 1.00 68.12 C ANISOU 1037 CA LEU A 131 9323 7658 8902 -621 -1153 31 C ATOM 1038 C LEU A 131 -362.763-184.170 145.544 1.00 73.90 C ANISOU 1038 C LEU A 131 9937 8405 9738 -680 -1298 86 C ATOM 1039 O LEU A 131 -363.374-185.246 145.520 1.00 73.69 O ANISOU 1039 O LEU A 131 9923 8333 9743 -758 -1322 41 O ATOM 1040 CB LEU A 131 -360.533-184.047 146.689 1.00 60.68 C ANISOU 1040 CB LEU A 131 8291 6695 8070 -489 -1019 49 C ATOM 1041 CG LEU A 131 -360.854-185.177 147.670 1.00 68.80 C ANISOU 1041 CG LEU A 131 9273 7659 9211 -484 -965 29 C ATOM 1042 CD1 LEU A 131 -360.585-186.539 147.038 1.00 63.52 C ANISOU 1042 CD1 LEU A 131 8732 6908 8495 -554 -923 -71 C ATOM 1043 CD2 LEU A 131 -360.060-185.019 148.952 1.00 72.51 C ANISOU 1043 CD2 LEU A 131 9682 8112 9756 -371 -856 61 C ATOM 1044 N ALA A 132 -363.383-183.001 145.735 1.00 69.40 N ANISOU 1044 N ALA A 132 9240 7884 9242 -645 -1393 182 N ATOM 1045 CA ALA A 132 -364.834-182.950 145.877 1.00 67.10 C ANISOU 1045 CA ALA A 132 8807 7601 9089 -696 -1529 236 C ATOM 1046 C ALA A 132 -365.528-183.432 144.610 1.00 71.06 C ANISOU 1046 C ALA A 132 9394 8105 9500 -847 -1705 224 C ATOM 1047 O ALA A 132 -366.546-184.132 144.677 1.00 73.56 O ANISOU 1047 O ALA A 132 9640 8399 9909 -927 -1784 218 O ATOM 1048 CB ALA A 132 -365.282-181.530 146.226 1.00 59.80 C ANISOU 1048 CB ALA A 132 7728 6711 8283 -620 -1590 335 C ATOM 1049 N ILE A 133 -364.988-183.076 143.445 1.00 68.99 N ANISOU 1049 N ILE A 133 9294 7871 9048 -904 -1768 221 N ATOM 1050 CA ILE A 133 -365.589-183.504 142.185 1.00 69.26 C ANISOU 1050 CA ILE A 133 9449 7914 8954 -1072 -1947 208 C ATOM 1051 C ILE A 133 -365.458-185.012 142.019 1.00 73.43 C ANISOU 1051 C ILE A 133 10099 8384 9416 -1159 -1868 76 C ATOM 1052 O ILE A 133 -366.420-185.698 141.651 1.00 81.61 O ANISOU 1052 O ILE A 133 11131 9403 10475 -1284 -2002 61 O ATOM 1053 CB ILE A 133 -364.949-182.755 141.004 1.00 69.79 C ANISOU 1053 CB ILE A 133 9693 8025 8798 -1126 -2008 234 C ATOM 1054 CG1 ILE A 133 -365.286-181.266 141.072 1.00 70.08 C ANISOU 1054 CG1 ILE A 133 9603 8101 8923 -1058 -2132 383 C ATOM 1055 CG2 ILE A 133 -365.402-183.357 139.682 1.00 70.67 C ANISOU 1055 CG2 ILE A 133 9988 8145 8720 -1326 -2170 198 C ATOM 1056 CD1 ILE A 133 -364.626-180.442 139.990 1.00 63.08 C ANISOU 1056 CD1 ILE A 133 8892 7253 7822 -1111 -2186 431 C ATOM 1057 N GLU A 134 -364.264-185.548 142.284 1.00 67.65 N ANISOU 1057 N GLU A 134 9470 7610 8622 -1097 -1653 -20 N ATOM 1058 CA GLU A 134 -364.036-186.980 142.118 1.00 68.92 C ANISOU 1058 CA GLU A 134 9752 7693 8743 -1167 -1560 -152 C ATOM 1059 C GLU A 134 -364.946-187.791 143.030 1.00 74.73 C ANISOU 1059 C GLU A 134 10346 8377 9670 -1173 -1575 -144 C ATOM 1060 O GLU A 134 -365.563-188.773 142.597 1.00 69.02 O ANISOU 1060 O GLU A 134 9683 7607 8934 -1302 -1641 -208 O ATOM 1061 CB GLU A 134 -362.571-187.315 142.388 1.00 65.93 C ANISOU 1061 CB GLU A 134 9459 7262 8328 -1069 -1325 -237 C ATOM 1062 CG GLU A 134 -361.618-186.684 141.399 1.00 73.06 C ANISOU 1062 CG GLU A 134 10518 8204 9036 -1088 -1275 -269 C ATOM 1063 CD GLU A 134 -360.164-187.013 141.684 1.00 81.51 C ANISOU 1063 CD GLU A 134 11639 9216 10116 -986 -1036 -355 C ATOM 1064 OE1 GLU A 134 -359.853-187.435 142.819 1.00 89.84 O ANISOU 1064 OE1 GLU A 134 12579 10215 11340 -871 -938 -348 O ATOM 1065 OE2 GLU A 134 -359.333-186.848 140.765 1.00 79.23 O ANISOU 1065 OE2 GLU A 134 11503 8934 9667 -1029 -948 -425 O ATOM 1066 N ARG A 135 -365.039-187.396 144.301 1.00 65.12 N ANISOU 1066 N ARG A 135 8950 7166 8624 -1046 -1507 -71 N ATOM 1067 CA ARG A 135 -365.914-188.105 145.228 1.00 66.26 C ANISOU 1067 CA ARG A 135 8963 7268 8946 -1061 -1500 -56 C ATOM 1068 C ARG A 135 -367.372-188.003 144.800 1.00 72.61 C ANISOU 1068 C ARG A 135 9662 8101 9825 -1179 -1704 -7 C ATOM 1069 O ARG A 135 -368.123-188.981 144.888 1.00 73.50 O ANISOU 1069 O ARG A 135 9750 8162 10014 -1276 -1738 -41 O ATOM 1070 CB ARG A 135 -365.726-187.557 146.639 1.00 57.26 C ANISOU 1070 CB ARG A 135 7673 6140 7942 -920 -1383 13 C ATOM 1071 CG ARG A 135 -364.360-187.857 147.216 1.00 62.50 C ANISOU 1071 CG ARG A 135 8420 6760 8567 -816 -1204 -26 C ATOM 1072 CD ARG A 135 -364.150-187.129 148.519 1.00 65.60 C ANISOU 1072 CD ARG A 135 8689 7183 9055 -695 -1118 48 C ATOM 1073 NE ARG A 135 -363.008-187.660 149.251 1.00 66.34 N ANISOU 1073 NE ARG A 135 8843 7219 9145 -615 -976 27 N ATOM 1074 CZ ARG A 135 -362.537-187.119 150.366 1.00 65.14 C ANISOU 1074 CZ ARG A 135 8627 7085 9037 -519 -897 81 C ATOM 1075 NH1 ARG A 135 -363.110-186.033 150.855 1.00 63.77 N ANISOU 1075 NH1 ARG A 135 8336 6982 8912 -488 -922 141 N ATOM 1076 NH2 ARG A 135 -361.496-187.655 150.983 1.00 78.50 N ANISOU 1076 NH2 ARG A 135 10375 8719 10733 -456 -800 74 N ATOM 1077 N TYR A 136 -367.793-186.824 144.341 1.00 75.44 N ANISOU 1077 N TYR A 136 9948 8533 10183 -1173 -1850 80 N ATOM 1078 CA TYR A 136 -369.151-186.675 143.831 1.00 79.05 C ANISOU 1078 CA TYR A 136 10293 9012 10730 -1285 -2076 141 C ATOM 1079 C TYR A 136 -369.403-187.617 142.662 1.00 85.51 C ANISOU 1079 C TYR A 136 11284 9805 11399 -1468 -2206 65 C ATOM 1080 O TYR A 136 -370.464-188.245 142.578 1.00 89.19 O ANISOU 1080 O TYR A 136 11671 10247 11971 -1583 -2327 64 O ATOM 1081 CB TYR A 136 -369.397-185.225 143.417 1.00 72.69 C ANISOU 1081 CB TYR A 136 9404 8272 9941 -1243 -2224 256 C ATOM 1082 CG TYR A 136 -370.552-185.045 142.462 1.00 76.04 C ANISOU 1082 CG TYR A 136 9777 8717 10397 -1381 -2512 326 C ATOM 1083 CD1 TYR A 136 -371.856-184.967 142.926 1.00 83.11 C ANISOU 1083 CD1 TYR A 136 10420 9601 11558 -1398 -2619 392 C ATOM 1084 CD2 TYR A 136 -370.338-184.941 141.092 1.00 78.28 C ANISOU 1084 CD2 TYR A 136 10263 9031 10447 -1504 -2679 328 C ATOM 1085 CE1 TYR A 136 -372.916-184.804 142.057 1.00 89.08 C ANISOU 1085 CE1 TYR A 136 11106 10370 12371 -1525 -2909 468 C ATOM 1086 CE2 TYR A 136 -371.393-184.775 140.215 1.00 84.78 C ANISOU 1086 CE2 TYR A 136 11049 9874 11291 -1644 -2977 408 C ATOM 1087 CZ TYR A 136 -372.680-184.707 140.704 1.00 90.44 C ANISOU 1087 CZ TYR A 136 11492 10574 12298 -1650 -3103 482 C ATOM 1088 OH TYR A 136 -373.741-184.543 139.841 1.00 92.05 O ANISOU 1088 OH TYR A 136 11634 10791 12552 -1790 -3424 573 O ATOM 1089 N VAL A 137 -368.433-187.731 141.753 1.00 84.00 N ANISOU 1089 N VAL A 137 11334 9618 10965 -1507 -2171 -8 N ATOM 1090 CA VAL A 137 -368.602-188.593 140.587 1.00 83.41 C ANISOU 1090 CA VAL A 137 11461 9518 10714 -1697 -2277 -101 C ATOM 1091 C VAL A 137 -368.692-190.055 141.008 1.00 85.31 C ANISOU 1091 C VAL A 137 11734 9659 11022 -1747 -2163 -216 C ATOM 1092 O VAL A 137 -369.512-190.818 140.483 1.00 91.88 O ANISOU 1092 O VAL A 137 12601 10459 11849 -1912 -2301 -259 O ATOM 1093 CB VAL A 137 -367.454-188.356 139.588 1.00 74.69 C ANISOU 1093 CB VAL A 137 10615 8434 9329 -1725 -2212 -169 C ATOM 1094 CG1 VAL A 137 -367.426-189.444 138.527 1.00 71.02 C ANISOU 1094 CG1 VAL A 137 10394 7921 8667 -1917 -2241 -313 C ATOM 1095 CG2 VAL A 137 -367.595-186.992 138.942 1.00 67.30 C ANISOU 1095 CG2 VAL A 137 9675 7590 8307 -1731 -2386 -41 C ATOM 1096 N VAL A 138 -367.860-190.464 141.968 1.00 83.02 N ANISOU 1096 N VAL A 138 11430 9310 10804 -1613 -1924 -260 N ATOM 1097 CA VAL A 138 -367.804-191.866 142.367 1.00 75.65 C ANISOU 1097 CA VAL A 138 10547 8262 9936 -1652 -1805 -361 C ATOM 1098 C VAL A 138 -369.070-192.271 143.115 1.00 81.90 C ANISOU 1098 C VAL A 138 11141 9032 10945 -1700 -1883 -301 C ATOM 1099 O VAL A 138 -369.585-193.382 142.933 1.00 87.03 O ANISOU 1099 O VAL A 138 11837 9602 11628 -1829 -1914 -372 O ATOM 1100 CB VAL A 138 -366.536-192.120 143.201 1.00 67.99 C ANISOU 1100 CB VAL A 138 9607 7230 8996 -1491 -1555 -397 C ATOM 1101 CG1 VAL A 138 -366.610-193.465 143.887 1.00 70.43 C ANISOU 1101 CG1 VAL A 138 9916 7410 9432 -1508 -1449 -455 C ATOM 1102 CG2 VAL A 138 -365.301-192.039 142.322 1.00 59.04 C ANISOU 1102 CG2 VAL A 138 8679 6088 7666 -1478 -1456 -495 C ATOM 1103 N VAL A 139 -369.605-191.380 143.944 1.00 76.91 N ANISOU 1103 N VAL A 139 10286 8464 10471 -1607 -1906 -177 N ATOM 1104 CA VAL A 139 -370.762-191.714 144.773 1.00 75.08 C ANISOU 1104 CA VAL A 139 9849 8211 10466 -1644 -1933 -124 C ATOM 1105 C VAL A 139 -372.075-191.429 144.052 1.00 78.75 C ANISOU 1105 C VAL A 139 10199 8721 11002 -1781 -2189 -72 C ATOM 1106 O VAL A 139 -372.933-192.307 143.935 1.00 81.94 O ANISOU 1106 O VAL A 139 10565 9074 11494 -1921 -2269 -102 O ATOM 1107 CB VAL A 139 -370.683-190.959 146.114 1.00 71.59 C ANISOU 1107 CB VAL A 139 9227 7802 10170 -1483 -1793 -35 C ATOM 1108 CG1 VAL A 139 -371.934-191.219 146.945 1.00 73.33 C ANISOU 1108 CG1 VAL A 139 9229 8007 10626 -1533 -1798 16 C ATOM 1109 CG2 VAL A 139 -369.440-191.383 146.872 1.00 66.00 C ANISOU 1109 CG2 VAL A 139 8631 7041 9405 -1370 -1572 -74 C ATOM 1110 N CYS A 140 -372.262-190.201 143.573 1.00 83.07 N ANISOU 1110 N CYS A 140 10678 9355 11530 -1747 -2333 14 N ATOM 1111 CA CYS A 140 -373.527-189.837 142.948 1.00 84.88 C ANISOU 1111 CA CYS A 140 10764 9620 11864 -1864 -2603 90 C ATOM 1112 C CYS A 140 -373.704-190.448 141.567 1.00 91.73 C ANISOU 1112 C CYS A 140 11833 10480 12540 -2064 -2808 28 C ATOM 1113 O CYS A 140 -374.828-190.439 141.055 1.00100.58 O ANISOU 1113 O CYS A 140 12843 11614 13757 -2198 -3055 82 O ATOM 1114 CB CYS A 140 -373.647-188.317 142.852 1.00 85.90 C ANISOU 1114 CB CYS A 140 10763 9827 12048 -1761 -2707 215 C ATOM 1115 SG CYS A 140 -373.620-187.475 144.443 1.00 91.20 S ANISOU 1115 SG CYS A 140 11188 10506 12957 -1550 -2484 279 S ATOM 1116 N LYS A 141 -372.633-190.970 140.963 1.00 91.68 N ANISOU 1116 N LYS A 141 12113 10448 12275 -2094 -2710 -88 N ATOM 1117 CA LYS A 141 -372.641-191.590 139.640 1.00 94.40 C ANISOU 1117 CA LYS A 141 12701 10778 12389 -2294 -2859 -179 C ATOM 1118 C LYS A 141 -373.441-190.769 138.633 1.00 99.35 C ANISOU 1118 C LYS A 141 13302 11487 12962 -2414 -3190 -71 C ATOM 1119 O LYS A 141 -374.475-191.234 138.136 1.00101.39 O ANISOU 1119 O LYS A 141 13519 11733 13270 -2591 -3418 -62 O ATOM 1120 CB LYS A 141 -373.193-193.017 139.730 1.00 87.97 C ANISOU 1120 CB LYS A 141 11911 9866 11648 -2435 -2850 -283 C ATOM 1121 CG LYS A 141 -372.362-193.933 140.616 1.00 89.73 C ANISOU 1121 CG LYS A 141 12194 9988 11913 -2335 -2545 -384 C ATOM 1122 CD LYS A 141 -372.969-195.313 140.740 1.00 95.67 C ANISOU 1122 CD LYS A 141 12959 10628 12762 -2477 -2543 -472 C ATOM 1123 CE LYS A 141 -372.109-196.213 141.617 1.00103.15 C ANISOU 1123 CE LYS A 141 13972 11458 13762 -2373 -2257 -551 C ATOM 1124 NZ LYS A 141 -372.718-197.566 141.795 1.00114.32 N ANISOU 1124 NZ LYS A 141 15398 12748 15292 -2511 -2249 -626 N ATOM 1125 N PRO A 142 -373.004-189.549 138.304 1.00105.54 N ANISOU 1125 N PRO A 142 14105 12345 13649 -2330 -3241 24 N ATOM 1126 CA PRO A 142 -373.751-188.739 137.333 1.00107.20 C ANISOU 1126 CA PRO A 142 14297 12622 13811 -2446 -3581 152 C ATOM 1127 C PRO A 142 -373.566-189.179 135.891 1.00109.65 C ANISOU 1127 C PRO A 142 14934 12946 13780 -2674 -3742 77 C ATOM 1128 O PRO A 142 -374.282-188.677 135.014 1.00112.89 O ANISOU 1128 O PRO A 142 15355 13406 14131 -2813 -4067 187 O ATOM 1129 CB PRO A 142 -373.182-187.332 137.551 1.00 98.81 C ANISOU 1129 CB PRO A 142 13173 11617 12754 -2269 -3536 270 C ATOM 1130 CG PRO A 142 -371.780-187.579 137.982 1.00 95.62 C ANISOU 1130 CG PRO A 142 12928 11192 12212 -2145 -3200 151 C ATOM 1131 CD PRO A 142 -371.809-188.844 138.804 1.00 98.93 C ANISOU 1131 CD PRO A 142 13306 11530 12753 -2134 -3006 28 C ATOM 1132 N MET A 143 -372.634-190.087 135.617 1.00106.90 N ANISOU 1132 N MET A 143 14854 12551 13210 -2722 -3526 -106 N ATOM 1133 CA MET A 143 -372.396-190.604 134.277 1.00109.80 C ANISOU 1133 CA MET A 143 15563 12922 13235 -2952 -3626 -216 C ATOM 1134 C MET A 143 -372.779-192.077 134.241 1.00123.54 C ANISOU 1134 C MET A 143 17376 14568 14995 -3099 -3595 -377 C ATOM 1135 O MET A 143 -372.357-192.854 135.105 1.00126.30 O ANISOU 1135 O MET A 143 17677 14831 15480 -2990 -3327 -481 O ATOM 1136 CB MET A 143 -370.939-190.387 133.864 1.00 99.22 C ANISOU 1136 CB MET A 143 14490 11592 11616 -2898 -3379 -314 C ATOM 1137 CG MET A 143 -370.617-188.913 133.636 1.00106.07 C ANISOU 1137 CG MET A 143 15334 12554 12414 -2808 -3458 -150 C ATOM 1138 SD MET A 143 -368.874-188.508 133.396 1.00109.23 S ANISOU 1138 SD MET A 143 15972 12967 12564 -2706 -3130 -243 S ATOM 1139 CE MET A 143 -368.214-188.842 135.026 1.00100.46 C ANISOU 1139 CE MET A 143 14628 11783 11758 -2424 -2783 -297 C ATOM 1140 N SER A 144 -373.574-192.453 133.234 1.00130.05 N ANISOU 1140 N SER A 144 18326 15403 15683 -3356 -3882 -392 N ATOM 1141 CA SER A 144 -374.325-193.706 133.284 1.00137.07 C ANISOU 1141 CA SER A 144 19200 16206 16673 -3511 -3940 -498 C ATOM 1142 C SER A 144 -373.409-194.918 133.414 1.00139.66 C ANISOU 1142 C SER A 144 19742 16417 16905 -3510 -3611 -732 C ATOM 1143 O SER A 144 -373.606-195.765 134.294 1.00143.99 O ANISOU 1143 O SER A 144 20154 16869 17688 -3451 -3467 -788 O ATOM 1144 CB SER A 144 -375.209-193.824 132.044 1.00143.87 C ANISOU 1144 CB SER A 144 20205 17106 17354 -3809 -4324 -478 C ATOM 1145 OG SER A 144 -374.479-193.500 130.875 1.00148.70 O ANISOU 1145 OG SER A 144 21171 17770 17557 -3933 -4352 -533 O ATOM 1146 N ASN A 145 -372.411-195.031 132.539 1.00136.83 N ANISOU 1146 N ASN A 145 19720 16055 16214 -3581 -3483 -871 N ATOM 1147 CA ASN A 145 -371.459-196.144 132.572 1.00136.81 C ANISOU 1147 CA ASN A 145 19925 15924 16131 -3573 -3156 -1105 C ATOM 1148 C ASN A 145 -370.054-195.549 132.573 1.00133.20 C ANISOU 1148 C ASN A 145 19583 15491 15537 -3404 -2879 -1140 C ATOM 1149 O ASN A 145 -369.457-195.331 131.516 1.00132.39 O ANISOU 1149 O ASN A 145 19767 15425 15111 -3522 -2856 -1224 O ATOM 1150 CB ASN A 145 -371.677-197.102 131.402 1.00144.46 C ANISOU 1150 CB ASN A 145 21212 16835 16840 -3872 -3249 -1293 C ATOM 1151 CG ASN A 145 -372.874-198.016 131.612 1.00147.42 C ANISOU 1151 CG ASN A 145 21466 17138 17407 -4019 -3434 -1307 C ATOM 1152 OD1 ASN A 145 -373.288-198.266 132.744 1.00147.91 O ANISOU 1152 OD1 ASN A 145 21243 17151 17806 -3879 -3377 -1235 O ATOM 1153 ND2 ASN A 145 -373.433-198.521 130.519 1.00150.27 N ANISOU 1153 ND2 ASN A 145 22056 17493 17546 -4316 -3656 -1402 N ATOM 1154 N PHE A 146 -369.533-195.294 133.772 1.00129.54 N ANISOU 1154 N PHE A 146 18898 15006 15316 -3138 -2667 -1076 N ATOM 1155 CA PHE A 146 -368.247-194.639 133.958 1.00116.22 C ANISOU 1155 CA PHE A 146 17254 13344 13562 -2954 -2421 -1080 C ATOM 1156 C PHE A 146 -367.547-195.249 135.164 1.00109.45 C ANISOU 1156 C PHE A 146 16262 12374 12950 -2740 -2125 -1132 C ATOM 1157 O PHE A 146 -368.198-195.619 136.145 1.00101.36 O ANISOU 1157 O PHE A 146 15016 11306 12190 -2674 -2154 -1064 O ATOM 1158 CB PHE A 146 -368.428-193.125 134.146 1.00113.42 C ANISOU 1158 CB PHE A 146 16730 13129 13234 -2844 -2570 -858 C ATOM 1159 CG PHE A 146 -367.152-192.386 134.436 1.00110.71 C ANISOU 1159 CG PHE A 146 16400 12814 12852 -2652 -2329 -846 C ATOM 1160 CD1 PHE A 146 -366.336-191.957 133.405 1.00111.62 C ANISOU 1160 CD1 PHE A 146 16773 12974 12665 -2731 -2264 -908 C ATOM 1161 CD2 PHE A 146 -366.776-192.112 135.741 1.00102.82 C ANISOU 1161 CD2 PHE A 146 15159 11796 12112 -2407 -2168 -773 C ATOM 1162 CE1 PHE A 146 -365.165-191.278 133.668 1.00107.71 C ANISOU 1162 CE1 PHE A 146 16273 12500 12152 -2562 -2041 -897 C ATOM 1163 CE2 PHE A 146 -365.605-191.433 136.010 1.00101.43 C ANISOU 1163 CE2 PHE A 146 14988 11643 11909 -2242 -1964 -760 C ATOM 1164 CZ PHE A 146 -364.798-191.016 134.972 1.00103.25 C ANISOU 1164 CZ PHE A 146 15455 11914 11863 -2316 -1900 -822 C ATOM 1165 N ARG A 147 -366.221-195.356 135.082 1.00115.20 N ANISOU 1165 N ARG A 147 17124 13051 13597 -2642 -1844 -1248 N ATOM 1166 CA ARG A 147 -365.406-195.882 136.173 1.00119.51 C ANISOU 1166 CA ARG A 147 17555 13485 14370 -2435 -1575 -1286 C ATOM 1167 C ARG A 147 -364.181-194.997 136.338 1.00113.60 C ANISOU 1167 C ARG A 147 16796 12787 13581 -2259 -1392 -1253 C ATOM 1168 O ARG A 147 -363.403-194.833 135.394 1.00118.94 O ANISOU 1168 O ARG A 147 17686 13475 14032 -2323 -1284 -1362 O ATOM 1169 CB ARG A 147 -364.986-197.332 135.908 1.00131.93 C ANISOU 1169 CB ARG A 147 19302 14877 15947 -2510 -1391 -1508 C ATOM 1170 CG ARG A 147 -363.983-197.889 136.914 1.00143.57 C ANISOU 1170 CG ARG A 147 20681 16217 17651 -2297 -1115 -1546 C ATOM 1171 CD ARG A 147 -364.623-198.174 138.268 1.00151.98 C ANISOU 1171 CD ARG A 147 21494 17245 19006 -2190 -1170 -1408 C ATOM 1172 NE ARG A 147 -363.660-198.721 139.221 1.00155.67 N ANISOU 1172 NE ARG A 147 21888 17579 19679 -2001 -938 -1425 N ATOM 1173 CZ ARG A 147 -363.121-198.033 140.223 1.00156.52 C ANISOU 1173 CZ ARG A 147 21821 17736 19914 -1798 -873 -1287 C ATOM 1174 NH1 ARG A 147 -363.455-196.764 140.419 1.00154.32 N ANISOU 1174 NH1 ARG A 147 21419 17629 19586 -1751 -1000 -1134 N ATOM 1175 NH2 ARG A 147 -362.252-198.618 141.037 1.00157.43 N ANISOU 1175 NH2 ARG A 147 21884 17719 20212 -1647 -690 -1299 N ATOM 1176 N PHE A 148 -364.006-194.439 137.534 1.00102.03 N ANISOU 1176 N PHE A 148 15089 11349 12327 -2051 -1350 -1110 N ATOM 1177 CA PHE A 148 -362.890-193.540 137.808 1.00 97.69 C ANISOU 1177 CA PHE A 148 14500 10849 11767 -1881 -1198 -1062 C ATOM 1178 C PHE A 148 -361.597-194.339 137.933 1.00 93.05 C ANISOU 1178 C PHE A 148 13995 10124 11234 -1790 -903 -1216 C ATOM 1179 O PHE A 148 -361.464-195.180 138.828 1.00 90.69 O ANISOU 1179 O PHE A 148 13599 9707 11154 -1697 -807 -1234 O ATOM 1180 CB PHE A 148 -363.169-192.748 139.085 1.00 93.72 C ANISOU 1180 CB PHE A 148 13723 10410 11475 -1706 -1254 -872 C ATOM 1181 CG PHE A 148 -362.034-191.871 139.522 1.00 92.19 C ANISOU 1181 CG PHE A 148 13470 10257 11301 -1529 -1105 -820 C ATOM 1182 CD1 PHE A 148 -361.847-190.619 138.957 1.00 84.63 C ANISOU 1182 CD1 PHE A 148 12542 9420 10194 -1534 -1173 -744 C ATOM 1183 CD2 PHE A 148 -361.165-192.289 140.516 1.00 96.01 C ANISOU 1183 CD2 PHE A 148 13864 10653 11964 -1364 -913 -836 C ATOM 1184 CE1 PHE A 148 -360.805-189.807 139.366 1.00 85.97 C ANISOU 1184 CE1 PHE A 148 12652 9622 10392 -1381 -1037 -698 C ATOM 1185 CE2 PHE A 148 -360.122-191.484 140.930 1.00 95.67 C ANISOU 1185 CE2 PHE A 148 13756 10646 11949 -1212 -794 -786 C ATOM 1186 CZ PHE A 148 -359.942-190.239 140.355 1.00 90.02 C ANISOU 1186 CZ PHE A 148 13068 10051 11084 -1221 -849 -723 C ATOM 1187 N GLY A 149 -360.643-194.074 137.040 1.00 89.02 N ANISOU 1187 N GLY A 149 13660 9624 10540 -1821 -758 -1323 N ATOM 1188 CA GLY A 149 -359.406-194.832 137.008 1.00 79.55 C ANISOU 1188 CA GLY A 149 12536 8283 9406 -1746 -466 -1488 C ATOM 1189 C GLY A 149 -358.148-193.993 137.114 1.00 87.35 C ANISOU 1189 C GLY A 149 13479 9311 10398 -1600 -290 -1464 C ATOM 1190 O GLY A 149 -358.208-192.804 137.438 1.00 88.22 O ANISOU 1190 O GLY A 149 13475 9554 10490 -1528 -392 -1301 O ATOM 1191 N GLU A 150 -356.999-194.612 136.826 1.00 94.13 N ANISOU 1191 N GLU A 150 14422 10045 11298 -1559 -18 -1633 N ATOM 1192 CA GLU A 150 -355.715-193.935 136.990 1.00 92.16 C ANISOU 1192 CA GLU A 150 14103 9812 11102 -1413 172 -1621 C ATOM 1193 C GLU A 150 -355.590-192.731 136.063 1.00 98.21 C ANISOU 1193 C GLU A 150 14990 10736 11590 -1510 138 -1585 C ATOM 1194 O GLU A 150 -355.072-191.682 136.463 1.00 99.33 O ANISOU 1194 O GLU A 150 15008 10965 11768 -1395 145 -1461 O ATOM 1195 CB GLU A 150 -354.572-194.923 136.744 1.00 96.26 C ANISOU 1195 CB GLU A 150 14685 10147 11741 -1368 478 -1828 C ATOM 1196 CG GLU A 150 -353.180-194.319 136.860 1.00113.10 C ANISOU 1196 CG GLU A 150 16732 12280 13963 -1225 693 -1833 C ATOM 1197 CD GLU A 150 -352.081-195.313 136.531 1.00128.46 C ANISOU 1197 CD GLU A 150 18726 14029 16055 -1185 1007 -2051 C ATOM 1198 OE1 GLU A 150 -352.395-196.506 136.326 1.00136.61 O ANISOU 1198 OE1 GLU A 150 19852 14912 17141 -1251 1055 -2193 O ATOM 1199 OE2 GLU A 150 -350.903-194.900 136.477 1.00132.21 O ANISOU 1199 OE2 GLU A 150 19134 14489 16610 -1088 1210 -2084 O ATOM 1200 N ASN A 151 -356.054-192.863 134.818 1.00100.46 N ANISOU 1200 N ASN A 151 15527 11056 11587 -1734 94 -1690 N ATOM 1201 CA ASN A 151 -355.931-191.763 133.867 1.00104.15 C ANISOU 1201 CA ASN A 151 16141 11665 11765 -1851 57 -1648 C ATOM 1202 C ASN A 151 -356.803-190.579 134.267 1.00103.74 C ANISOU 1202 C ASN A 151 15957 11767 11693 -1826 -244 -1399 C ATOM 1203 O ASN A 151 -356.412-189.421 134.077 1.00104.77 O ANISOU 1203 O ASN A 151 16079 11999 11728 -1802 -253 -1295 O ATOM 1204 CB ASN A 151 -356.284-192.243 132.460 1.00113.57 C ANISOU 1204 CB ASN A 151 17661 12856 12635 -2120 57 -1812 C ATOM 1205 CG ASN A 151 -355.198-193.108 131.852 1.00125.25 C ANISOU 1205 CG ASN A 151 19303 14197 14089 -2155 417 -2077 C ATOM 1206 OD1 ASN A 151 -354.204-193.426 132.505 1.00126.10 O ANISOU 1206 OD1 ASN A 151 19258 14196 14459 -1967 653 -2133 O ATOM 1207 ND2 ASN A 151 -355.386-193.499 130.597 1.00133.98 N ANISOU 1207 ND2 ASN A 151 20722 15298 14885 -2403 458 -2245 N ATOM 1208 N HIS A 152 -357.987-190.846 134.822 1.00 95.53 N ANISOU 1208 N HIS A 152 14804 10735 10758 -1833 -481 -1304 N ATOM 1209 CA HIS A 152 -358.852-189.757 135.265 1.00 87.78 C ANISOU 1209 CA HIS A 152 13667 9879 9807 -1796 -749 -1077 C ATOM 1210 C HIS A 152 -358.232-189.000 136.433 1.00 87.62 C ANISOU 1210 C HIS A 152 13404 9878 10009 -1563 -675 -953 C ATOM 1211 O HIS A 152 -358.300-187.767 136.486 1.00 86.60 O ANISOU 1211 O HIS A 152 13208 9853 9842 -1525 -780 -805 O ATOM 1212 CB HIS A 152 -360.229-190.299 135.645 1.00 89.66 C ANISOU 1212 CB HIS A 152 13815 10105 10146 -1854 -983 -1021 C ATOM 1213 CG HIS A 152 -360.955-190.949 134.509 1.00 96.88 C ANISOU 1213 CG HIS A 152 14960 11011 10839 -2102 -1108 -1124 C ATOM 1214 ND1 HIS A 152 -360.830-192.290 134.216 1.00 99.30 N ANISOU 1214 ND1 HIS A 152 15403 11190 11136 -2188 -976 -1324 N ATOM 1215 CD2 HIS A 152 -361.807-190.440 133.588 1.00 94.06 C ANISOU 1215 CD2 HIS A 152 14726 10751 10261 -2290 -1365 -1053 C ATOM 1216 CE1 HIS A 152 -361.577-192.579 133.166 1.00101.73 C ANISOU 1216 CE1 HIS A 152 15918 11522 11212 -2428 -1141 -1383 C ATOM 1217 NE2 HIS A 152 -362.180-191.474 132.766 1.00100.37 N ANISOU 1217 NE2 HIS A 152 15742 11490 10905 -2497 -1389 -1213 N ATOM 1218 N ALA A 153 -357.623-189.721 137.378 1.00 87.08 N ANISOU 1218 N ALA A 153 13209 9703 10175 -1411 -506 -1008 N ATOM 1219 CA ALA A 153 -356.977-189.066 138.510 1.00 84.26 C ANISOU 1219 CA ALA A 153 12638 9359 10016 -1205 -441 -897 C ATOM 1220 C ALA A 153 -355.800-188.209 138.065 1.00 82.56 C ANISOU 1220 C ALA A 153 12471 9187 9711 -1167 -286 -908 C ATOM 1221 O ALA A 153 -355.506-187.182 138.689 1.00 77.09 O ANISOU 1221 O ALA A 153 11636 8560 9094 -1052 -314 -779 O ATOM 1222 CB ALA A 153 -356.516-190.108 139.528 1.00 81.57 C ANISOU 1222 CB ALA A 153 12181 8885 9928 -1074 -307 -950 C ATOM 1223 N ILE A 154 -355.115-188.613 136.995 1.00 78.91 N ANISOU 1223 N ILE A 154 12209 8683 9089 -1272 -109 -1070 N ATOM 1224 CA ILE A 154 -353.991-187.834 136.489 1.00 78.52 C ANISOU 1224 CA ILE A 154 12213 8672 8948 -1258 63 -1092 C ATOM 1225 C ILE A 154 -354.486-186.535 135.861 1.00 80.44 C ANISOU 1225 C ILE A 154 12534 9060 8970 -1358 -115 -953 C ATOM 1226 O ILE A 154 -353.911-185.463 136.084 1.00 83.25 O ANISOU 1226 O ILE A 154 12808 9476 9348 -1279 -88 -853 O ATOM 1227 CB ILE A 154 -353.165-188.677 135.500 1.00 80.71 C ANISOU 1227 CB ILE A 154 12691 8856 9118 -1357 331 -1321 C ATOM 1228 CG1 ILE A 154 -352.391-189.759 136.254 1.00 82.59 C ANISOU 1228 CG1 ILE A 154 12800 8932 9650 -1206 534 -1432 C ATOM 1229 CG2 ILE A 154 -352.215-187.806 134.699 1.00 77.31 C ANISOU 1229 CG2 ILE A 154 12367 8486 8521 -1407 497 -1345 C ATOM 1230 CD1 ILE A 154 -351.957-190.912 135.378 1.00 87.80 C ANISOU 1230 CD1 ILE A 154 13647 9460 10251 -1310 765 -1678 C ATOM 1231 N MET A 155 -355.562-186.614 135.071 1.00 78.77 N ANISOU 1231 N MET A 155 12479 8897 8553 -1538 -315 -939 N ATOM 1232 CA MET A 155 -356.222-185.406 134.583 1.00 86.54 C ANISOU 1232 CA MET A 155 13508 10004 9368 -1625 -547 -770 C ATOM 1233 C MET A 155 -356.534-184.453 135.730 1.00 86.23 C ANISOU 1233 C MET A 155 13204 10011 9549 -1450 -685 -578 C ATOM 1234 O MET A 155 -356.261-183.250 135.649 1.00 93.93 O ANISOU 1234 O MET A 155 14154 11054 10481 -1422 -723 -457 O ATOM 1235 CB MET A 155 -357.510-185.769 133.842 1.00 96.74 C ANISOU 1235 CB MET A 155 14943 11327 10488 -1820 -799 -758 C ATOM 1236 CG MET A 155 -357.333-186.219 132.407 1.00112.63 C ANISOU 1236 CG MET A 155 17286 13340 12169 -2058 -731 -905 C ATOM 1237 SD MET A 155 -358.928-186.629 131.667 1.00129.73 S ANISOU 1237 SD MET A 155 19592 15542 14158 -2291 -1084 -868 S ATOM 1238 CE MET A 155 -359.828-185.100 131.924 1.00125.70 C ANISOU 1238 CE MET A 155 18914 15147 13697 -2247 -1433 -565 C ATOM 1239 N GLY A 156 -357.107-184.984 136.813 1.00 75.50 N ANISOU 1239 N GLY A 156 11654 8609 8425 -1339 -751 -552 N ATOM 1240 CA GLY A 156 -357.468-184.139 137.940 1.00 72.29 C ANISOU 1240 CA GLY A 156 11008 8240 8219 -1188 -864 -390 C ATOM 1241 C GLY A 156 -356.280-183.408 138.534 1.00 79.38 C ANISOU 1241 C GLY A 156 11806 9140 9214 -1039 -697 -361 C ATOM 1242 O GLY A 156 -356.379-182.230 138.886 1.00 86.03 O ANISOU 1242 O GLY A 156 12548 10042 10099 -975 -787 -224 O ATOM 1243 N VAL A 157 -355.141-184.092 138.655 1.00 76.66 N ANISOU 1243 N VAL A 157 11480 8723 8926 -982 -455 -491 N ATOM 1244 CA VAL A 157 -353.938-183.442 139.165 1.00 71.78 C ANISOU 1244 CA VAL A 157 10761 8103 8410 -853 -300 -469 C ATOM 1245 C VAL A 157 -353.430-182.409 138.166 1.00 73.39 C ANISOU 1245 C VAL A 157 11095 8375 8417 -939 -262 -440 C ATOM 1246 O VAL A 157 -353.105-181.274 138.532 1.00 70.53 O ANISOU 1246 O VAL A 157 10637 8059 8100 -868 -287 -328 O ATOM 1247 CB VAL A 157 -352.858-184.488 139.497 1.00 70.69 C ANISOU 1247 CB VAL A 157 10592 7854 8414 -773 -63 -610 C ATOM 1248 CG1 VAL A 157 -351.543-183.802 139.836 1.00 67.66 C ANISOU 1248 CG1 VAL A 157 10111 7469 8127 -664 95 -594 C ATOM 1249 CG2 VAL A 157 -353.311-185.368 140.652 1.00 68.73 C ANISOU 1249 CG2 VAL A 157 10203 7536 8377 -675 -117 -599 C ATOM 1250 N ALA A 158 -353.361-182.786 136.887 1.00 77.23 N ANISOU 1250 N ALA A 158 11813 8863 8669 -1107 -198 -543 N ATOM 1251 CA ALA A 158 -352.956-181.838 135.854 1.00 72.80 C ANISOU 1251 CA ALA A 158 11412 8369 7882 -1223 -168 -507 C ATOM 1252 C ALA A 158 -353.877-180.624 135.831 1.00 78.82 C ANISOU 1252 C ALA A 158 12145 9217 8586 -1249 -443 -305 C ATOM 1253 O ALA A 158 -353.427-179.498 135.587 1.00 82.47 O ANISOU 1253 O ALA A 158 12622 9725 8988 -1254 -436 -210 O ATOM 1254 CB ALA A 158 -352.941-182.526 134.489 1.00 63.63 C ANISOU 1254 CB ALA A 158 10535 7198 6444 -1431 -80 -652 C ATOM 1255 N PHE A 159 -355.169-180.835 136.096 1.00 76.29 N ANISOU 1255 N PHE A 159 11770 8909 8309 -1265 -684 -234 N ATOM 1256 CA PHE A 159 -356.120-179.729 136.098 1.00 75.30 C ANISOU 1256 CA PHE A 159 11587 8845 8179 -1278 -953 -42 C ATOM 1257 C PHE A 159 -355.778-178.700 137.169 1.00 75.70 C ANISOU 1257 C PHE A 159 11419 8900 8443 -1100 -941 69 C ATOM 1258 O PHE A 159 -355.874-177.492 136.929 1.00 80.15 O ANISOU 1258 O PHE A 159 11983 9502 8969 -1111 -1048 205 O ATOM 1259 CB PHE A 159 -357.537-180.262 136.302 1.00 70.81 C ANISOU 1259 CB PHE A 159 10956 8274 7676 -1313 -1186 -4 C ATOM 1260 CG PHE A 159 -358.572-179.187 136.455 1.00 68.19 C ANISOU 1260 CG PHE A 159 10510 7983 7417 -1299 -1458 190 C ATOM 1261 CD1 PHE A 159 -359.047-178.504 135.349 1.00 65.90 C ANISOU 1261 CD1 PHE A 159 10373 7739 6926 -1451 -1656 300 C ATOM 1262 CD2 PHE A 159 -359.074-178.863 137.703 1.00 65.62 C ANISOU 1262 CD2 PHE A 159 9927 7641 7366 -1138 -1515 264 C ATOM 1263 CE1 PHE A 159 -360.003-177.516 135.486 1.00 67.31 C ANISOU 1263 CE1 PHE A 159 10426 7935 7212 -1428 -1916 487 C ATOM 1264 CE2 PHE A 159 -360.029-177.874 137.845 1.00 68.77 C ANISOU 1264 CE2 PHE A 159 10203 8059 7866 -1116 -1744 430 C ATOM 1265 CZ PHE A 159 -360.494-177.201 136.734 1.00 67.90 C ANISOU 1265 CZ PHE A 159 10225 7983 7591 -1253 -1950 545 C ATOM 1266 N THR A 160 -355.382-179.157 138.359 1.00 70.73 N ANISOU 1266 N THR A 160 10611 8224 8037 -943 -820 15 N ATOM 1267 CA THR A 160 -355.008-178.221 139.414 1.00 71.97 C ANISOU 1267 CA THR A 160 10580 8385 8380 -788 -803 103 C ATOM 1268 C THR A 160 -353.792-177.397 139.009 1.00 73.56 C ANISOU 1268 C THR A 160 10840 8601 8510 -790 -656 110 C ATOM 1269 O THR A 160 -353.706-176.206 139.329 1.00 70.00 O ANISOU 1269 O THR A 160 10309 8170 8119 -736 -713 224 O ATOM 1270 CB THR A 160 -354.731-178.971 140.717 1.00 67.90 C ANISOU 1270 CB THR A 160 9898 7818 8082 -647 -702 40 C ATOM 1271 OG1 THR A 160 -353.563-179.787 140.563 1.00 69.48 O ANISOU 1271 OG1 THR A 160 10154 7970 8276 -635 -479 -94 O ATOM 1272 CG2 THR A 160 -355.914-179.852 141.089 1.00 63.94 C ANISOU 1272 CG2 THR A 160 9350 7298 7647 -662 -825 29 C ATOM 1273 N TRP A 161 -352.841-178.015 138.304 1.00 68.67 N ANISOU 1273 N TRP A 161 10355 7962 7776 -856 -452 -19 N ATOM 1274 CA TRP A 161 -351.644-177.293 137.887 1.00 68.38 C ANISOU 1274 CA TRP A 161 10366 7935 7681 -870 -283 -24 C ATOM 1275 C TRP A 161 -351.977-176.231 136.850 1.00 79.04 C ANISOU 1275 C TRP A 161 11875 9342 8816 -1007 -403 94 C ATOM 1276 O TRP A 161 -351.414-175.130 136.877 1.00 78.37 O ANISOU 1276 O TRP A 161 11760 9272 8746 -985 -374 180 O ATOM 1277 CB TRP A 161 -350.608-178.268 137.331 1.00 66.43 C ANISOU 1277 CB TRP A 161 10220 7643 7378 -916 -15 -204 C ATOM 1278 CG TRP A 161 -350.132-179.284 138.320 1.00 76.15 C ANISOU 1278 CG TRP A 161 11292 8797 8844 -776 104 -304 C ATOM 1279 CD1 TRP A 161 -350.388-179.313 139.662 1.00 74.01 C ANISOU 1279 CD1 TRP A 161 10815 8508 8799 -625 11 -243 C ATOM 1280 CD2 TRP A 161 -349.315-180.426 138.043 1.00 89.84 C ANISOU 1280 CD2 TRP A 161 13068 10455 10614 -780 337 -480 C ATOM 1281 NE1 TRP A 161 -349.778-180.403 140.236 1.00 77.57 N ANISOU 1281 NE1 TRP A 161 11183 8877 9415 -540 150 -350 N ATOM 1282 CE2 TRP A 161 -349.114-181.103 139.262 1.00 90.17 C ANISOU 1282 CE2 TRP A 161 12915 10427 10918 -623 350 -498 C ATOM 1283 CE3 TRP A 161 -348.732-180.941 136.880 1.00 92.70 C ANISOU 1283 CE3 TRP A 161 13617 10790 10815 -907 545 -628 C ATOM 1284 CZ2 TRP A 161 -348.356-182.269 139.352 1.00 92.25 C ANISOU 1284 CZ2 TRP A 161 13150 10586 11315 -576 544 -644 C ATOM 1285 CZ3 TRP A 161 -347.979-182.098 136.971 1.00 90.83 C ANISOU 1285 CZ3 TRP A 161 13347 10449 10717 -857 765 -796 C ATOM 1286 CH2 TRP A 161 -347.798-182.749 138.198 1.00 91.24 C ANISOU 1286 CH2 TRP A 161 13186 10422 11058 -687 754 -796 C ATOM 1287 N VAL A 162 -352.885-176.545 135.925 1.00 83.97 N ANISOU 1287 N VAL A 162 12673 9992 9238 -1158 -550 106 N ATOM 1288 CA VAL A 162 -353.298-175.565 134.927 1.00 78.84 C ANISOU 1288 CA VAL A 162 12186 9393 8378 -1302 -709 244 C ATOM 1289 C VAL A 162 -354.006-174.393 135.598 1.00 79.15 C ANISOU 1289 C VAL A 162 12056 9437 8582 -1203 -934 434 C ATOM 1290 O VAL A 162 -353.718-173.226 135.310 1.00 80.62 O ANISOU 1290 O VAL A 162 12272 9634 8726 -1225 -968 556 O ATOM 1291 CB VAL A 162 -354.180-176.232 133.858 1.00 74.20 C ANISOU 1291 CB VAL A 162 11817 8830 7545 -1493 -853 220 C ATOM 1292 CG1 VAL A 162 -354.786-175.188 132.940 1.00 72.57 C ANISOU 1292 CG1 VAL A 162 11761 8670 7144 -1637 -1089 403 C ATOM 1293 CG2 VAL A 162 -353.363-177.237 133.059 1.00 70.16 C ANISOU 1293 CG2 VAL A 162 11511 8305 6842 -1613 -593 18 C ATOM 1294 N MET A 163 -354.930-174.687 136.515 1.00 78.28 N ANISOU 1294 N MET A 163 11762 9309 8673 -1095 -1075 458 N ATOM 1295 CA MET A 163 -355.624-173.620 137.230 1.00 80.47 C ANISOU 1295 CA MET A 163 11860 9575 9139 -991 -1257 614 C ATOM 1296 C MET A 163 -354.658-172.806 138.081 1.00 86.43 C ANISOU 1296 C MET A 163 12481 10309 10051 -856 -1109 626 C ATOM 1297 O MET A 163 -354.791-171.580 138.183 1.00 88.13 O ANISOU 1297 O MET A 163 12644 10513 10331 -825 -1207 759 O ATOM 1298 CB MET A 163 -356.739-174.205 138.097 1.00 77.05 C ANISOU 1298 CB MET A 163 11253 9124 8897 -909 -1385 608 C ATOM 1299 CG MET A 163 -357.929-174.731 137.321 1.00 81.66 C ANISOU 1299 CG MET A 163 11928 9725 9375 -1041 -1603 640 C ATOM 1300 SD MET A 163 -358.753-173.427 136.390 1.00 85.40 S ANISOU 1300 SD MET A 163 12469 10211 9767 -1143 -1903 862 S ATOM 1301 CE MET A 163 -358.233-173.845 134.730 1.00 93.58 C ANISOU 1301 CE MET A 163 13865 11296 10397 -1388 -1875 818 C ATOM 1302 N ALA A 164 -353.680-173.470 138.702 1.00 81.15 N ANISOU 1302 N ALA A 164 11752 9624 9458 -777 -884 492 N ATOM 1303 CA ALA A 164 -352.716-172.758 139.534 1.00 76.17 C ANISOU 1303 CA ALA A 164 10991 8973 8976 -661 -757 499 C ATOM 1304 C ALA A 164 -351.838-171.839 138.697 1.00 79.59 C ANISOU 1304 C ALA A 164 11544 9418 9277 -744 -673 548 C ATOM 1305 O ALA A 164 -351.592-170.691 139.080 1.00 76.00 O ANISOU 1305 O ALA A 164 11012 8948 8918 -691 -700 642 O ATOM 1306 CB ALA A 164 -351.858-173.752 140.312 1.00 76.30 C ANISOU 1306 CB ALA A 164 10918 8965 9107 -571 -561 357 C ATOM 1307 N LEU A 165 -351.350-172.329 137.555 1.00 77.59 N ANISOU 1307 N LEU A 165 11490 9186 8804 -883 -558 480 N ATOM 1308 CA LEU A 165 -350.577-171.476 136.658 1.00 75.84 C ANISOU 1308 CA LEU A 165 11410 8979 8427 -992 -469 532 C ATOM 1309 C LEU A 165 -351.434-170.342 136.111 1.00 82.32 C ANISOU 1309 C LEU A 165 12309 9809 9161 -1067 -713 724 C ATOM 1310 O LEU A 165 -350.943-169.226 135.904 1.00 80.06 O ANISOU 1310 O LEU A 165 12046 9511 8862 -1091 -698 825 O ATOM 1311 CB LEU A 165 -349.982-172.297 135.518 1.00 76.42 C ANISOU 1311 CB LEU A 165 11701 9072 8262 -1146 -282 405 C ATOM 1312 CG LEU A 165 -348.798-173.201 135.862 1.00 78.77 C ANISOU 1312 CG LEU A 165 11927 9338 8663 -1082 13 220 C ATOM 1313 CD1 LEU A 165 -348.398-174.033 134.653 1.00 83.08 C ANISOU 1313 CD1 LEU A 165 12705 9892 8969 -1247 199 80 C ATOM 1314 CD2 LEU A 165 -347.625-172.371 136.350 1.00 70.66 C ANISOU 1314 CD2 LEU A 165 10769 8292 7785 -1006 165 241 C ATOM 1315 N ALA A 166 -352.724-170.606 135.880 1.00 80.72 N ANISOU 1315 N ALA A 166 12137 9616 8916 -1106 -950 786 N ATOM 1316 CA ALA A 166 -353.621-169.573 135.373 1.00 75.15 C ANISOU 1316 CA ALA A 166 11484 8904 8165 -1169 -1216 985 C ATOM 1317 C ALA A 166 -353.747-168.398 136.335 1.00 81.08 C ANISOU 1317 C ALA A 166 12027 9602 9177 -1019 -1292 1097 C ATOM 1318 O ALA A 166 -354.110-167.295 135.911 1.00 81.52 O ANISOU 1318 O ALA A 166 12123 9629 9221 -1061 -1457 1267 O ATOM 1319 CB ALA A 166 -355.002-170.165 135.093 1.00 71.71 C ANISOU 1319 CB ALA A 166 11069 8482 7697 -1221 -1463 1022 C ATOM 1320 N CYS A 167 -353.458-168.610 137.617 1.00 81.03 N ANISOU 1320 N CYS A 167 11811 9574 9402 -853 -1180 1005 N ATOM 1321 CA CYS A 167 -353.462-167.542 138.604 1.00 80.25 C ANISOU 1321 CA CYS A 167 11530 9422 9541 -719 -1214 1077 C ATOM 1322 C CYS A 167 -352.069-166.987 138.883 1.00 77.28 C ANISOU 1322 C CYS A 167 11136 9033 9193 -692 -1004 1038 C ATOM 1323 O CYS A 167 -351.896-165.766 138.938 1.00 77.92 O ANISOU 1323 O CYS A 167 11194 9070 9344 -680 -1047 1146 O ATOM 1324 CB CYS A 167 -354.085-168.037 139.914 1.00 76.86 C ANISOU 1324 CB CYS A 167 10889 8976 9339 -570 -1235 1008 C ATOM 1325 SG CYS A 167 -353.656-167.035 141.356 1.00 79.32 S ANISOU 1325 SG CYS A 167 10994 9230 9914 -410 -1166 1010 S ATOM 1326 N ALA A 168 -351.067-167.856 139.035 1.00 68.32 N ANISOU 1326 N ALA A 168 10006 7927 8026 -685 -784 890 N ATOM 1327 CA ALA A 168 -349.750-167.434 139.496 1.00 68.91 C ANISOU 1327 CA ALA A 168 10011 7985 8185 -641 -591 843 C ATOM 1328 C ALA A 168 -348.867-166.877 138.386 1.00 74.73 C ANISOU 1328 C ALA A 168 10913 8732 8749 -779 -475 881 C ATOM 1329 O ALA A 168 -347.966-166.081 138.675 1.00 74.88 O ANISOU 1329 O ALA A 168 10871 8725 8855 -759 -373 900 O ATOM 1330 CB ALA A 168 -349.032-168.606 140.175 1.00 64.37 C ANISOU 1330 CB ALA A 168 9343 7422 7692 -567 -415 679 C ATOM 1331 N ALA A 169 -349.093-167.271 137.134 1.00 72.45 N ANISOU 1331 N ALA A 169 10838 8480 8210 -932 -482 890 N ATOM 1332 CA ALA A 169 -348.206-166.888 136.038 1.00 69.11 C ANISOU 1332 CA ALA A 169 10598 8072 7587 -1088 -330 906 C ATOM 1333 C ALA A 169 -348.492-165.511 135.431 1.00 77.64 C ANISOU 1333 C ALA A 169 11784 9128 8588 -1177 -480 1106 C ATOM 1334 O ALA A 169 -347.534-164.794 135.118 1.00 82.05 O ANISOU 1334 O ALA A 169 12388 9672 9115 -1240 -336 1136 O ATOM 1335 CB ALA A 169 -348.240-167.953 134.936 1.00 60.12 C ANISOU 1335 CB ALA A 169 9677 6983 6185 -1238 -243 810 C ATOM 1336 N PRO A 170 -349.749-165.101 135.222 1.00 80.17 N ANISOU 1336 N PRO A 170 12142 9432 8888 -1191 -763 1251 N ATOM 1337 CA PRO A 170 -350.012-163.784 134.584 1.00 81.91 C ANISOU 1337 CA PRO A 170 12469 9609 9044 -1280 -922 1461 C ATOM 1338 C PRO A 170 -349.292-162.626 135.262 1.00 84.29 C ANISOU 1338 C PRO A 170 12636 9843 9546 -1198 -850 1513 C ATOM 1339 O PRO A 170 -348.759-161.751 134.562 1.00 78.31 O ANISOU 1339 O PRO A 170 12011 9062 8680 -1315 -813 1622 O ATOM 1340 CB PRO A 170 -351.539-163.639 134.689 1.00 76.52 C ANISOU 1340 CB PRO A 170 11737 8898 8439 -1236 -1248 1586 C ATOM 1341 CG PRO A 170 -352.024-165.030 134.624 1.00 74.97 C ANISOU 1341 CG PRO A 170 11562 8765 8160 -1246 -1248 1454 C ATOM 1342 CD PRO A 170 -351.003-165.874 135.356 1.00 76.45 C ANISOU 1342 CD PRO A 170 11642 8978 8429 -1157 -958 1242 C ATOM 1343 N PRO A 171 -349.242-162.554 136.601 1.00 82.51 N ANISOU 1343 N PRO A 171 12166 9582 9601 -1014 -827 1442 N ATOM 1344 CA PRO A 171 -348.506-161.436 137.223 1.00 75.72 C ANISOU 1344 CA PRO A 171 11196 8655 8920 -956 -757 1480 C ATOM 1345 C PRO A 171 -347.035-161.378 136.851 1.00 80.63 C ANISOU 1345 C PRO A 171 11877 9300 9459 -1045 -492 1414 C ATOM 1346 O PRO A 171 -346.402-160.334 137.054 1.00 91.69 O ANISOU 1346 O PRO A 171 13236 10643 10959 -1049 -445 1476 O ATOM 1347 CB PRO A 171 -348.694-161.684 138.726 1.00 79.00 C ANISOU 1347 CB PRO A 171 11367 9050 9601 -766 -759 1375 C ATOM 1348 CG PRO A 171 -349.950-162.438 138.814 1.00 78.37 C ANISOU 1348 CG PRO A 171 11267 8993 9518 -721 -922 1368 C ATOM 1349 CD PRO A 171 -349.932-163.354 137.633 1.00 79.21 C ANISOU 1349 CD PRO A 171 11571 9173 9351 -864 -886 1342 C ATOM 1350 N LEU A 172 -346.465-162.459 136.320 1.00 75.61 N ANISOU 1350 N LEU A 172 11329 8737 8664 -1118 -307 1284 N ATOM 1351 CA LEU A 172 -345.088-162.422 135.847 1.00 71.43 C ANISOU 1351 CA LEU A 172 10852 8223 8063 -1215 -34 1218 C ATOM 1352 C LEU A 172 -344.961-161.868 134.434 1.00 83.04 C ANISOU 1352 C LEU A 172 12590 9704 9258 -1429 -10 1338 C ATOM 1353 O LEU A 172 -343.835-161.659 133.973 1.00 94.87 O ANISOU 1353 O LEU A 172 14143 11208 10694 -1531 227 1302 O ATOM 1354 CB LEU A 172 -344.469-163.825 135.884 1.00 67.28 C ANISOU 1354 CB LEU A 172 10294 7752 7516 -1198 186 1014 C ATOM 1355 CG LEU A 172 -344.423-164.629 137.183 1.00 66.98 C ANISOU 1355 CG LEU A 172 10020 7711 7718 -1011 197 883 C ATOM 1356 CD1 LEU A 172 -343.903-166.028 136.896 1.00 65.42 C ANISOU 1356 CD1 LEU A 172 9844 7551 7463 -1027 401 706 C ATOM 1357 CD2 LEU A 172 -343.549-163.951 138.215 1.00 70.04 C ANISOU 1357 CD2 LEU A 172 10200 8055 8358 -912 262 874 C ATOM 1358 N VAL A 173 -346.072-161.634 133.731 1.00 83.71 N ANISOU 1358 N VAL A 173 12843 9789 9175 -1510 -250 1483 N ATOM 1359 CA VAL A 173 -346.004-161.231 132.329 1.00 82.80 C ANISOU 1359 CA VAL A 173 13020 9691 8749 -1739 -247 1603 C ATOM 1360 C VAL A 173 -346.951-160.075 132.024 1.00 86.50 C ANISOU 1360 C VAL A 173 13567 10092 9208 -1775 -561 1857 C ATOM 1361 O VAL A 173 -347.293-159.836 130.861 1.00 91.71 O ANISOU 1361 O VAL A 173 14489 10767 9591 -1965 -665 1994 O ATOM 1362 CB VAL A 173 -346.293-162.420 131.392 1.00 82.62 C ANISOU 1362 CB VAL A 173 13210 9753 8430 -1874 -200 1508 C ATOM 1363 CG1 VAL A 173 -345.141-163.416 131.420 1.00 79.64 C ANISOU 1363 CG1 VAL A 173 12798 9419 8043 -1880 162 1270 C ATOM 1364 CG2 VAL A 173 -347.607-163.095 131.771 1.00 81.64 C ANISOU 1364 CG2 VAL A 173 13021 9641 8359 -1775 -459 1505 C ATOM 1365 N GLY A 174 -347.389-159.353 133.052 1.00 84.24 N ANISOU 1365 N GLY A 174 13062 9724 9223 -1601 -716 1922 N ATOM 1366 CA GLY A 174 -348.035-158.073 132.850 1.00 84.20 C ANISOU 1366 CA GLY A 174 13094 9619 9280 -1620 -965 2158 C ATOM 1367 C GLY A 174 -349.521-157.979 133.134 1.00 86.33 C ANISOU 1367 C GLY A 174 13282 9841 9678 -1519 -1297 2266 C ATOM 1368 O GLY A 174 -350.112-156.929 132.858 1.00 92.32 O ANISOU 1368 O GLY A 174 14077 10502 10497 -1539 -1521 2477 O ATOM 1369 N TRP A 175 -350.152-159.026 133.658 1.00 85.56 N ANISOU 1369 N TRP A 175 13071 9798 9641 -1414 -1336 2135 N ATOM 1370 CA TRP A 175 -351.528-158.938 134.141 1.00 79.90 C ANISOU 1370 CA TRP A 175 12214 9027 9116 -1292 -1617 2212 C ATOM 1371 C TRP A 175 -351.462-159.015 135.660 1.00 75.85 C ANISOU 1371 C TRP A 175 11414 8482 8923 -1074 -1524 2067 C ATOM 1372 O TRP A 175 -351.166-160.076 136.219 1.00 78.08 O ANISOU 1372 O TRP A 175 11616 8840 9212 -1012 -1369 1877 O ATOM 1373 CB TRP A 175 -352.411-160.040 133.555 1.00 82.09 C ANISOU 1373 CB TRP A 175 12589 9386 9217 -1360 -1754 2189 C ATOM 1374 CG TRP A 175 -353.889-159.751 133.686 1.00 87.52 C ANISOU 1374 CG TRP A 175 13174 10008 10073 -1290 -2089 2332 C ATOM 1375 CD1 TRP A 175 -354.469-158.538 133.925 1.00 86.43 C ANISOU 1375 CD1 TRP A 175 12932 9741 10168 -1216 -2287 2511 C ATOM 1376 CD2 TRP A 175 -354.965-160.697 133.596 1.00 90.93 C ANISOU 1376 CD2 TRP A 175 13579 10488 10484 -1286 -2257 2303 C ATOM 1377 NE1 TRP A 175 -355.837-158.669 133.986 1.00 85.11 N ANISOU 1377 NE1 TRP A 175 12660 9538 10142 -1160 -2564 2596 N ATOM 1378 CE2 TRP A 175 -356.167-159.983 133.785 1.00 86.11 C ANISOU 1378 CE2 TRP A 175 12831 9776 10110 -1207 -2555 2473 C ATOM 1379 CE3 TRP A 175 -355.028-162.077 133.372 1.00 88.71 C ANISOU 1379 CE3 TRP A 175 13368 10314 10023 -1343 -2181 2146 C ATOM 1380 CZ2 TRP A 175 -357.415-160.602 133.757 1.00 84.49 C ANISOU 1380 CZ2 TRP A 175 12547 9583 9971 -1187 -2781 2496 C ATOM 1381 CZ3 TRP A 175 -356.270-162.690 133.345 1.00 85.72 C ANISOU 1381 CZ3 TRP A 175 12929 9947 9693 -1331 -2409 2168 C ATOM 1382 CH2 TRP A 175 -357.446-161.953 133.538 1.00 87.17 C ANISOU 1382 CH2 TRP A 175 12965 10038 10117 -1255 -2707 2343 C ATOM 1383 N SER A 176 -351.731-157.884 136.317 1.00 78.18 N ANISOU 1383 N SER A 176 11568 8657 9478 -968 -1618 2157 N ATOM 1384 CA SER A 176 -351.419-157.670 137.727 1.00 78.70 C ANISOU 1384 CA SER A 176 11403 8680 9819 -796 -1499 2028 C ATOM 1385 C SER A 176 -349.911-157.769 137.942 1.00 76.73 C ANISOU 1385 C SER A 176 11167 8475 9511 -830 -1219 1904 C ATOM 1386 O SER A 176 -349.135-157.693 136.981 1.00 70.23 O ANISOU 1386 O SER A 176 10521 7688 8476 -982 -1118 1945 O ATOM 1387 CB SER A 176 -352.172-158.654 138.625 1.00 77.51 C ANISOU 1387 CB SER A 176 11089 8573 9790 -664 -1520 1891 C ATOM 1388 OG SER A 176 -352.078-158.266 139.985 1.00 84.09 O ANISOU 1388 OG SER A 176 11718 9347 10887 -512 -1449 1798 O ATOM 1389 N ARG A 177 -349.482-157.927 139.192 1.00 71.67 N ANISOU 1389 N ARG A 177 10340 7831 9059 -700 -1094 1754 N ATOM 1390 CA ARG A 177 -348.058-157.937 139.501 1.00 66.86 C ANISOU 1390 CA ARG A 177 9704 7250 8449 -721 -858 1648 C ATOM 1391 C ARG A 177 -347.861-158.463 140.914 1.00 63.42 C ANISOU 1391 C ARG A 177 9069 6832 8194 -576 -777 1480 C ATOM 1392 O ARG A 177 -348.775-158.418 141.743 1.00 73.16 O ANISOU 1392 O ARG A 177 10187 8028 9583 -461 -891 1464 O ATOM 1393 CB ARG A 177 -347.451-156.537 139.371 1.00 61.73 C ANISOU 1393 CB ARG A 177 9079 6500 7874 -773 -841 1757 C ATOM 1394 CG ARG A 177 -347.990-155.561 140.401 1.00 65.56 C ANISOU 1394 CG ARG A 177 9413 6864 8635 -646 -953 1784 C ATOM 1395 CD ARG A 177 -347.385-154.181 140.254 1.00 76.21 C ANISOU 1395 CD ARG A 177 10792 8098 10066 -703 -936 1890 C ATOM 1396 NE ARG A 177 -347.941-153.265 141.244 1.00 78.86 N ANISOU 1396 NE ARG A 177 10988 8301 10673 -581 -1032 1896 N ATOM 1397 CZ ARG A 177 -347.435-152.072 141.531 1.00 75.73 C ANISOU 1397 CZ ARG A 177 10568 7784 10422 -594 -1007 1939 C ATOM 1398 NH1 ARG A 177 -346.350-151.642 140.903 1.00 74.65 N ANISOU 1398 NH1 ARG A 177 10529 7647 10186 -725 -894 1991 N ATOM 1399 NH2 ARG A 177 -348.012-151.317 142.454 1.00 80.60 N ANISOU 1399 NH2 ARG A 177 11063 8274 11287 -481 -1081 1920 N ATOM 1400 N TYR A 178 -346.652-158.952 141.179 1.00 62.31 N ANISOU 1400 N TYR A 178 8891 6746 8039 -590 -577 1359 N ATOM 1401 CA TYR A 178 -346.235-159.312 142.527 1.00 61.70 C ANISOU 1401 CA TYR A 178 8638 6677 8130 -475 -506 1221 C ATOM 1402 C TYR A 178 -345.538-158.123 143.176 1.00 65.39 C ANISOU 1402 C TYR A 178 9025 7063 8758 -463 -474 1237 C ATOM 1403 O TYR A 178 -344.632-157.529 142.583 1.00 69.57 O ANISOU 1403 O TYR A 178 9611 7573 9250 -561 -380 1284 O ATOM 1404 CB TYR A 178 -345.300-160.522 142.514 1.00 64.05 C ANISOU 1404 CB TYR A 178 8914 7062 8361 -488 -331 1089 C ATOM 1405 CG TYR A 178 -345.983-161.818 142.159 1.00 67.44 C ANISOU 1405 CG TYR A 178 9396 7560 8667 -480 -355 1037 C ATOM 1406 CD1 TYR A 178 -346.898-162.402 143.030 1.00 70.43 C ANISOU 1406 CD1 TYR A 178 9685 7947 9130 -371 -457 989 C ATOM 1407 CD2 TYR A 178 -345.715-162.462 140.962 1.00 66.39 C ANISOU 1407 CD2 TYR A 178 9412 7481 8334 -591 -263 1028 C ATOM 1408 CE1 TYR A 178 -347.530-163.589 142.713 1.00 62.11 C ANISOU 1408 CE1 TYR A 178 8677 6947 7974 -372 -481 942 C ATOM 1409 CE2 TYR A 178 -346.341-163.650 140.636 1.00 76.05 C ANISOU 1409 CE2 TYR A 178 10692 8757 9445 -593 -286 970 C ATOM 1410 CZ TYR A 178 -347.247-164.209 141.517 1.00 71.86 C ANISOU 1410 CZ TYR A 178 10060 8229 9015 -481 -402 931 C ATOM 1411 OH TYR A 178 -347.867-165.391 141.192 1.00 75.25 O ANISOU 1411 OH TYR A 178 10544 8703 9343 -492 -426 874 O ATOM 1412 N ILE A 179 -345.978-157.770 144.379 1.00 59.77 N ANISOU 1412 N ILE A 179 8190 6299 8221 -357 -544 1192 N ATOM 1413 CA ILE A 179 -345.325-156.744 145.193 1.00 62.84 C ANISOU 1413 CA ILE A 179 8497 6610 8770 -344 -514 1173 C ATOM 1414 C ILE A 179 -345.287-157.224 146.635 1.00 60.71 C ANISOU 1414 C ILE A 179 8094 6361 8611 -247 -503 1037 C ATOM 1415 O ILE A 179 -346.038-158.128 147.025 1.00 67.94 O ANISOU 1415 O ILE A 179 8982 7327 9504 -179 -543 983 O ATOM 1416 CB ILE A 179 -346.056-155.384 145.112 1.00 66.38 C ANISOU 1416 CB ILE A 179 8971 6926 9326 -337 -635 1287 C ATOM 1417 CG1 ILE A 179 -347.478-155.507 145.657 1.00 68.03 C ANISOU 1417 CG1 ILE A 179 9126 7101 9622 -229 -765 1279 C ATOM 1418 CG2 ILE A 179 -346.062-154.832 143.686 1.00 53.41 C ANISOU 1418 CG2 ILE A 179 7479 5252 7564 -450 -669 1451 C ATOM 1419 CD1 ILE A 179 -348.189-154.190 145.774 1.00 69.57 C ANISOU 1419 CD1 ILE A 179 9307 7142 9985 -197 -871 1368 C ATOM 1420 N PRO A 180 -344.411-156.641 147.453 1.00 59.05 N ANISOU 1420 N PRO A 180 7809 6114 8513 -253 -454 982 N ATOM 1421 CA PRO A 180 -344.477-156.919 148.892 1.00 54.61 C ANISOU 1421 CA PRO A 180 7148 5559 8042 -179 -471 866 C ATOM 1422 C PRO A 180 -345.827-156.502 149.457 1.00 57.90 C ANISOU 1422 C PRO A 180 7557 5908 8532 -103 -566 864 C ATOM 1423 O PRO A 180 -346.424-155.511 149.031 1.00 64.19 O ANISOU 1423 O PRO A 180 8390 6607 9392 -106 -624 948 O ATOM 1424 CB PRO A 180 -343.332-156.080 149.470 1.00 50.95 C ANISOU 1424 CB PRO A 180 6631 5046 7682 -229 -426 834 C ATOM 1425 CG PRO A 180 -342.366-155.959 148.341 1.00 53.77 C ANISOU 1425 CG PRO A 180 7025 5420 7985 -323 -336 901 C ATOM 1426 CD PRO A 180 -343.215-155.853 147.103 1.00 58.30 C ANISOU 1426 CD PRO A 180 7719 5982 8451 -345 -372 1015 C ATOM 1427 N GLU A 181 -346.315-157.281 150.415 1.00 53.90 N ANISOU 1427 N GLU A 181 7001 5449 8031 -37 -578 771 N ATOM 1428 CA GLU A 181 -347.631-157.059 150.992 1.00 58.90 C ANISOU 1428 CA GLU A 181 7612 6028 8741 34 -637 750 C ATOM 1429 C GLU A 181 -347.529-157.051 152.508 1.00 58.39 C ANISOU 1429 C GLU A 181 7495 5957 8733 59 -607 623 C ATOM 1430 O GLU A 181 -346.577-157.577 153.088 1.00 59.36 O ANISOU 1430 O GLU A 181 7600 6145 8811 31 -572 562 O ATOM 1431 CB GLU A 181 -348.628-158.135 150.530 1.00 55.52 C ANISOU 1431 CB GLU A 181 7192 5667 8235 74 -678 771 C ATOM 1432 CG GLU A 181 -348.186-159.559 150.837 1.00 65.58 C ANISOU 1432 CG GLU A 181 8455 7058 9406 77 -632 700 C ATOM 1433 CD GLU A 181 -349.008-160.613 150.109 1.00 78.85 C ANISOU 1433 CD GLU A 181 10165 8799 10995 91 -669 731 C ATOM 1434 OE1 GLU A 181 -349.927-160.240 149.338 1.00 85.67 O ANISOU 1434 OE1 GLU A 181 11057 9623 11869 92 -746 815 O ATOM 1435 OE2 GLU A 181 -348.725-161.818 150.316 1.00 77.89 O ANISOU 1435 OE2 GLU A 181 10037 8757 10802 97 -631 675 O ATOM 1436 N GLY A 182 -348.524-156.442 153.141 1.00 64.50 N ANISOU 1436 N GLY A 182 8248 6647 9613 107 -622 584 N ATOM 1437 CA GLY A 182 -348.593-156.441 154.593 1.00 62.77 C ANISOU 1437 CA GLY A 182 8007 6421 9422 117 -581 453 C ATOM 1438 C GLY A 182 -347.386-155.759 155.196 1.00 61.09 C ANISOU 1438 C GLY A 182 7806 6180 9225 49 -558 403 C ATOM 1439 O GLY A 182 -347.114-154.578 154.941 1.00 60.60 O ANISOU 1439 O GLY A 182 7755 6012 9257 21 -558 430 O ATOM 1440 N MET A 183 -346.637-156.508 156.004 1.00 58.59 N ANISOU 1440 N MET A 183 7486 5951 8824 15 -551 336 N ATOM 1441 CA MET A 183 -345.426-155.995 156.631 1.00 58.75 C ANISOU 1441 CA MET A 183 7506 5958 8856 -62 -554 291 C ATOM 1442 C MET A 183 -344.227-156.014 155.691 1.00 57.15 C ANISOU 1442 C MET A 183 7275 5785 8653 -108 -557 374 C ATOM 1443 O MET A 183 -343.099-155.810 156.151 1.00 59.20 O ANISOU 1443 O MET A 183 7509 6053 8932 -174 -569 346 O ATOM 1444 CB MET A 183 -345.125-156.777 157.908 1.00 60.29 C ANISOU 1444 CB MET A 183 7709 6229 8968 -88 -572 202 C ATOM 1445 CG MET A 183 -346.065-156.435 159.059 1.00 61.47 C ANISOU 1445 CG MET A 183 7908 6331 9117 -85 -540 91 C ATOM 1446 SD MET A 183 -346.066-157.628 160.417 1.00 75.46 S ANISOU 1446 SD MET A 183 9721 8207 10741 -117 -561 15 S ATOM 1447 CE MET A 183 -344.369-157.571 160.982 1.00 72.42 C ANISOU 1447 CE MET A 183 9332 7859 10325 -221 -652 14 C ATOM 1448 N GLN A 184 -344.459-156.254 154.398 1.00 53.67 N ANISOU 1448 N GLN A 184 6842 5361 8190 -84 -544 471 N ATOM 1449 CA GLN A 184 -343.480-156.066 153.332 1.00 60.36 C ANISOU 1449 CA GLN A 184 7681 6215 9037 -140 -512 552 C ATOM 1450 C GLN A 184 -342.384-157.127 153.335 1.00 60.00 C ANISOU 1450 C GLN A 184 7579 6271 8948 -162 -484 536 C ATOM 1451 O GLN A 184 -341.356-156.958 152.675 1.00 65.46 O ANISOU 1451 O GLN A 184 8241 6966 9665 -220 -434 576 O ATOM 1452 CB GLN A 184 -342.857-154.664 153.392 1.00 63.44 C ANISOU 1452 CB GLN A 184 8075 6498 9530 -208 -506 563 C ATOM 1453 CG GLN A 184 -343.875-153.514 153.401 1.00 60.59 C ANISOU 1453 CG GLN A 184 7760 6004 9256 -181 -530 579 C ATOM 1454 CD GLN A 184 -344.773-153.497 152.173 1.00 62.23 C ANISOU 1454 CD GLN A 184 8012 6190 9442 -143 -551 697 C ATOM 1455 OE1 GLN A 184 -344.338-153.155 151.070 1.00 58.96 O ANISOU 1455 OE1 GLN A 184 7636 5760 9007 -197 -539 804 O ATOM 1456 NE2 GLN A 184 -346.034-153.868 152.360 1.00 57.34 N ANISOU 1456 NE2 GLN A 184 7392 5570 8824 -62 -586 683 N ATOM 1457 N CYS A 185 -342.582-158.231 154.053 1.00 58.79 N ANISOU 1457 N CYS A 185 7403 6190 8745 -119 -509 481 N ATOM 1458 CA CYS A 185 -341.586-159.290 154.111 1.00 63.49 C ANISOU 1458 CA CYS A 185 7930 6862 9333 -127 -495 471 C ATOM 1459 C CYS A 185 -341.892-160.450 153.178 1.00 65.73 C ANISOU 1459 C CYS A 185 8227 7207 9542 -84 -447 501 C ATOM 1460 O CYS A 185 -341.058-161.350 153.048 1.00 68.60 O ANISOU 1460 O CYS A 185 8528 7616 9923 -84 -413 492 O ATOM 1461 CB CYS A 185 -341.450-159.813 155.544 1.00 59.59 C ANISOU 1461 CB CYS A 185 7408 6397 8836 -120 -569 404 C ATOM 1462 SG CYS A 185 -340.762-158.596 156.662 1.00 72.39 S ANISOU 1462 SG CYS A 185 9019 7957 10529 -203 -629 353 S ATOM 1463 N SER A 186 -343.057-160.453 152.535 1.00 63.48 N ANISOU 1463 N SER A 186 8016 6915 9190 -52 -449 534 N ATOM 1464 CA SER A 186 -343.402-161.486 151.571 1.00 61.03 C ANISOU 1464 CA SER A 186 7739 6658 8792 -32 -411 558 C ATOM 1465 C SER A 186 -344.241-160.861 150.471 1.00 64.65 C ANISOU 1465 C SER A 186 8285 7084 9198 -48 -418 633 C ATOM 1466 O SER A 186 -344.798-159.770 150.630 1.00 70.74 O ANISOU 1466 O SER A 186 9076 7785 10018 -48 -467 663 O ATOM 1467 CB SER A 186 -344.137-162.658 152.227 1.00 64.70 C ANISOU 1467 CB SER A 186 8199 7169 9216 29 -450 513 C ATOM 1468 OG SER A 186 -345.087-162.197 153.162 1.00 70.50 O ANISOU 1468 OG SER A 186 8946 7873 9967 58 -511 487 O ATOM 1469 N CYS A 187 -344.321-161.567 149.349 1.00 62.55 N ANISOU 1469 N CYS A 187 8073 6859 8833 -68 -375 663 N ATOM 1470 CA CYS A 187 -344.868-161.017 148.119 1.00 65.82 C ANISOU 1470 CA CYS A 187 8589 7250 9170 -115 -390 754 C ATOM 1471 C CYS A 187 -346.102-161.790 147.671 1.00 70.43 C ANISOU 1471 C CYS A 187 9230 7866 9663 -86 -455 770 C ATOM 1472 O CYS A 187 -346.248-162.985 147.953 1.00 74.08 O ANISOU 1472 O CYS A 187 9670 8383 10093 -51 -439 706 O ATOM 1473 CB CYS A 187 -343.805-161.028 147.013 1.00 61.88 C ANISOU 1473 CB CYS A 187 8136 6771 8605 -203 -272 781 C ATOM 1474 SG CYS A 187 -342.417-159.896 147.330 1.00 71.96 S ANISOU 1474 SG CYS A 187 9341 7995 10006 -260 -202 787 S ATOM 1475 N GLY A 188 -346.986-161.092 146.963 1.00 58.83 N ANISOU 1475 N GLY A 188 7831 6355 8165 -108 -540 864 N ATOM 1476 CA GLY A 188 -348.193-161.704 146.441 1.00 50.71 C ANISOU 1476 CA GLY A 188 6852 5351 7063 -97 -628 896 C ATOM 1477 C GLY A 188 -348.853-160.817 145.407 1.00 60.03 C ANISOU 1477 C GLY A 188 8122 6479 8207 -149 -731 1031 C ATOM 1478 O GLY A 188 -348.320-159.778 145.010 1.00 62.32 O ANISOU 1478 O GLY A 188 8451 6714 8512 -200 -718 1103 O ATOM 1479 N ILE A 189 -350.038-161.255 144.970 1.00 74.95 N ANISOU 1479 N ILE A 189 10042 8381 10055 -142 -847 1074 N ATOM 1480 CA ILE A 189 -350.814-160.496 144.000 1.00 66.21 C ANISOU 1480 CA ILE A 189 9013 7220 8923 -191 -990 1222 C ATOM 1481 C ILE A 189 -351.124-159.117 144.564 1.00 72.04 C ANISOU 1481 C ILE A 189 9674 7838 9860 -135 -1053 1282 C ATOM 1482 O ILE A 189 -351.322-158.942 145.773 1.00 83.13 O ANISOU 1482 O ILE A 189 10955 9206 11424 -43 -1024 1197 O ATOM 1483 CB ILE A 189 -352.115-161.235 143.639 1.00 72.71 C ANISOU 1483 CB ILE A 189 9844 8071 9712 -183 -1127 1251 C ATOM 1484 CG1 ILE A 189 -351.843-162.708 143.333 1.00 80.10 C ANISOU 1484 CG1 ILE A 189 10839 9113 10481 -223 -1048 1155 C ATOM 1485 CG2 ILE A 189 -352.828-160.558 142.467 1.00 67.01 C ANISOU 1485 CG2 ILE A 189 9222 7302 8938 -257 -1304 1424 C ATOM 1486 CD1 ILE A 189 -351.105-162.933 142.055 1.00 82.81 C ANISOU 1486 CD1 ILE A 189 11356 9503 10603 -355 -987 1187 C ATOM 1487 N ASP A 190 -351.177-158.128 143.676 1.00 67.91 N ANISOU 1487 N ASP A 190 9235 7244 9323 -199 -1138 1428 N ATOM 1488 CA ASP A 190 -351.422-156.743 144.065 1.00 71.62 C ANISOU 1488 CA ASP A 190 9644 7574 9993 -154 -1199 1498 C ATOM 1489 C ASP A 190 -352.926-156.500 144.084 1.00 72.94 C ANISOU 1489 C ASP A 190 9737 7665 10311 -83 -1376 1573 C ATOM 1490 O ASP A 190 -353.542-156.178 143.068 1.00 72.55 O ANISOU 1490 O ASP A 190 9761 7576 10229 -135 -1538 1733 O ATOM 1491 CB ASP A 190 -350.703-155.796 143.114 1.00 76.74 C ANISOU 1491 CB ASP A 190 10419 8170 10569 -261 -1202 1630 C ATOM 1492 CG ASP A 190 -350.885-154.341 143.488 1.00 68.39 C ANISOU 1492 CG ASP A 190 9306 6947 9731 -219 -1261 1704 C ATOM 1493 OD1 ASP A 190 -351.374-154.057 144.601 1.00 65.87 O ANISOU 1493 OD1 ASP A 190 8848 6560 9620 -107 -1256 1617 O ATOM 1494 OD2 ASP A 190 -350.521-153.477 142.668 1.00 73.69 O ANISOU 1494 OD2 ASP A 190 10082 7550 10366 -307 -1299 1844 O ATOM 1495 N TYR A 191 -353.527-156.667 145.263 1.00 72.78 N ANISOU 1495 N TYR A 191 9568 7621 10463 29 -1346 1460 N ATOM 1496 CA TYR A 191 -354.899-156.250 145.515 1.00 69.72 C ANISOU 1496 CA TYR A 191 9062 7131 10296 114 -1475 1507 C ATOM 1497 C TYR A 191 -354.959-154.897 146.211 1.00 74.35 C ANISOU 1497 C TYR A 191 9564 7554 11131 182 -1454 1505 C ATOM 1498 O TYR A 191 -355.997-154.540 146.774 1.00 85.94 O ANISOU 1498 O TYR A 191 10898 8923 12833 275 -1497 1489 O ATOM 1499 CB TYR A 191 -355.635-157.290 146.359 1.00 68.08 C ANISOU 1499 CB TYR A 191 8744 6991 10133 184 -1434 1377 C ATOM 1500 CG TYR A 191 -355.498-158.712 145.870 1.00 72.66 C ANISOU 1500 CG TYR A 191 9400 7723 10484 123 -1426 1344 C ATOM 1501 CD1 TYR A 191 -356.202-159.153 144.758 1.00 83.28 C ANISOU 1501 CD1 TYR A 191 10805 9099 11737 64 -1585 1457 C ATOM 1502 CD2 TYR A 191 -354.683-159.616 146.533 1.00 66.98 C ANISOU 1502 CD2 TYR A 191 8693 7105 9651 121 -1268 1201 C ATOM 1503 CE1 TYR A 191 -356.086-160.452 144.307 1.00 86.23 C ANISOU 1503 CE1 TYR A 191 11260 9600 11905 1 -1568 1411 C ATOM 1504 CE2 TYR A 191 -354.559-160.917 146.090 1.00 75.59 C ANISOU 1504 CE2 TYR A 191 9850 8313 10560 71 -1252 1164 C ATOM 1505 CZ TYR A 191 -355.261-161.329 144.973 1.00 86.97 C ANISOU 1505 CZ TYR A 191 11359 9779 11905 10 -1392 1261 C ATOM 1506 OH TYR A 191 -355.147-162.628 144.530 1.00 92.99 O ANISOU 1506 OH TYR A 191 12198 10647 12488 -46 -1367 1209 O ATOM 1507 N TYR A 192 -353.860-154.147 146.193 1.00 69.56 N ANISOU 1507 N TYR A 192 9028 6909 10492 133 -1376 1512 N ATOM 1508 CA TYR A 192 -353.699-152.973 147.039 1.00 75.44 C ANISOU 1508 CA TYR A 192 9704 7507 11451 186 -1315 1463 C ATOM 1509 C TYR A 192 -353.614-151.670 146.267 1.00 77.49 C ANISOU 1509 C TYR A 192 10020 7613 11808 150 -1414 1633 C ATOM 1510 O TYR A 192 -353.953-150.620 146.815 1.00 85.55 O ANISOU 1510 O TYR A 192 10962 8466 13076 215 -1416 1624 O ATOM 1511 CB TYR A 192 -352.446-153.128 147.906 1.00 79.53 C ANISOU 1511 CB TYR A 192 10240 8092 11885 158 -1139 1309 C ATOM 1512 CG TYR A 192 -352.320-154.514 148.499 1.00 80.40 C ANISOU 1512 CG TYR A 192 10328 8363 11859 170 -1056 1174 C ATOM 1513 CD1 TYR A 192 -353.015-154.860 149.649 1.00 82.84 C ANISOU 1513 CD1 TYR A 192 10534 8670 12272 250 -1006 1043 C ATOM 1514 CD2 TYR A 192 -351.528-155.484 147.894 1.00 81.39 C ANISOU 1514 CD2 TYR A 192 10536 8631 11757 97 -1019 1178 C ATOM 1515 CE1 TYR A 192 -352.918-156.126 150.193 1.00 85.53 C ANISOU 1515 CE1 TYR A 192 10863 9147 12488 254 -940 937 C ATOM 1516 CE2 TYR A 192 -351.423-156.754 148.432 1.00 84.50 C ANISOU 1516 CE2 TYR A 192 10905 9150 12051 114 -952 1064 C ATOM 1517 CZ TYR A 192 -352.121-157.068 149.583 1.00 84.71 C ANISOU 1517 CZ TYR A 192 10837 9172 12178 191 -923 953 C ATOM 1518 OH TYR A 192 -352.028-158.328 150.129 1.00 79.07 O ANISOU 1518 OH TYR A 192 10107 8572 11363 200 -866 855 O ATOM 1519 N THR A 193 -353.155-151.713 145.016 1.00 71.95 N ANISOU 1519 N THR A 193 9461 6959 10916 40 -1487 1784 N ATOM 1520 CA THR A 193 -353.072-150.549 144.153 1.00 78.92 C ANISOU 1520 CA THR A 193 10427 7704 11856 -18 -1597 1976 C ATOM 1521 C THR A 193 -353.729-150.863 142.816 1.00 79.84 C ANISOU 1521 C THR A 193 10643 7852 11839 -87 -1794 2172 C ATOM 1522 O THR A 193 -353.610-151.990 142.318 1.00 86.70 O ANISOU 1522 O THR A 193 11590 8887 12463 -151 -1783 2149 O ATOM 1523 CB THR A 193 -351.613-150.125 143.920 1.00 79.79 C ANISOU 1523 CB THR A 193 10652 7833 11831 -130 -1469 1977 C ATOM 1524 OG1 THR A 193 -351.041-150.922 142.875 1.00 70.61 O ANISOU 1524 OG1 THR A 193 9637 6822 10368 -254 -1454 2036 O ATOM 1525 CG2 THR A 193 -350.796-150.318 145.181 1.00 74.48 C ANISOU 1525 CG2 THR A 193 9899 7206 11193 -93 -1277 1760 C ATOM 1526 N PRO A 194 -354.437-149.890 142.209 1.00 84.64 N ANISOU 1526 N PRO A 194 11257 8297 12606 -82 -1988 2371 N ATOM 1527 CA PRO A 194 -355.048-150.090 140.890 1.00 84.90 C ANISOU 1527 CA PRO A 194 11406 8351 12500 -170 -2213 2585 C ATOM 1528 C PRO A 194 -354.072-149.829 139.744 1.00 85.10 C ANISOU 1528 C PRO A 194 11669 8417 12246 -351 -2209 2726 C ATOM 1529 O PRO A 194 -354.350-149.042 138.835 1.00101.22 O ANISOU 1529 O PRO A 194 13813 10349 14296 -423 -2395 2958 O ATOM 1530 CB PRO A 194 -356.195-149.077 140.896 1.00 89.45 C ANISOU 1530 CB PRO A 194 11859 8708 13419 -73 -2422 2736 C ATOM 1531 CG PRO A 194 -355.641-147.937 141.697 1.00 76.39 C ANISOU 1531 CG PRO A 194 10142 6892 11990 -13 -2290 2672 C ATOM 1532 CD PRO A 194 -354.733-148.549 142.747 1.00 82.12 C ANISOU 1532 CD PRO A 194 10835 7748 12617 6 -2016 2407 C ATOM 1533 N HIS A 195 -352.912-150.490 139.787 1.00 85.70 N ANISOU 1533 N HIS A 195 11832 8646 12083 -430 -1993 2591 N ATOM 1534 CA HIS A 195 -351.855-150.292 138.797 1.00 87.44 C ANISOU 1534 CA HIS A 195 12266 8915 12043 -607 -1923 2686 C ATOM 1535 C HIS A 195 -352.410-150.463 137.388 1.00 95.33 C ANISOU 1535 C HIS A 195 13456 9945 12822 -742 -2131 2899 C ATOM 1536 O HIS A 195 -352.483-151.581 136.872 1.00100.30 O ANISOU 1536 O HIS A 195 14176 10731 13202 -813 -2122 2853 O ATOM 1537 CB HIS A 195 -350.699-151.265 139.050 1.00 84.40 C ANISOU 1537 CB HIS A 195 11909 8705 11454 -656 -1663 2487 C ATOM 1538 CG HIS A 195 -349.359-150.753 138.615 1.00 92.69 C ANISOU 1538 CG HIS A 195 13081 9758 12380 -790 -1499 2512 C ATOM 1539 ND1 HIS A 195 -348.648-151.315 137.576 1.00 95.46 N ANISOU 1539 ND1 HIS A 195 13620 10231 12418 -957 -1401 2539 N ATOM 1540 CD2 HIS A 195 -348.593-149.741 139.090 1.00 97.06 C ANISOU 1540 CD2 HIS A 195 13590 10203 13085 -790 -1403 2505 C ATOM 1541 CE1 HIS A 195 -347.505-150.668 137.425 1.00 94.32 C ANISOU 1541 CE1 HIS A 195 13532 10056 12250 -1052 -1244 2552 C ATOM 1542 NE2 HIS A 195 -347.447-149.709 138.332 1.00 99.17 N ANISOU 1542 NE2 HIS A 195 14006 10531 13144 -954 -1253 2537 N ATOM 1543 N GLU A 196 -352.814-149.351 136.767 1.00105.06 N ANISOU 1543 N GLU A 196 14757 11017 14146 -786 -2329 3138 N ATOM 1544 CA GLU A 196 -353.497-149.403 135.478 1.00104.40 C ANISOU 1544 CA GLU A 196 14850 10938 13878 -914 -2585 3372 C ATOM 1545 C GLU A 196 -352.614-149.959 134.368 1.00105.51 C ANISOU 1545 C GLU A 196 15269 11234 13585 -1138 -2478 3400 C ATOM 1546 O GLU A 196 -353.138-150.419 133.349 1.00110.31 O ANISOU 1546 O GLU A 196 16047 11910 13956 -1264 -2653 3529 O ATOM 1547 CB GLU A 196 -353.998-148.008 135.101 1.00106.37 C ANISOU 1547 CB GLU A 196 15115 10962 14340 -914 -2818 3636 C ATOM 1548 CG GLU A 196 -354.920-147.379 136.137 1.00111.36 C ANISOU 1548 CG GLU A 196 15469 11410 15432 -693 -2914 3609 C ATOM 1549 CD GLU A 196 -355.312-145.953 135.792 1.00143.76 C ANISOU 1549 CD GLU A 196 19578 15262 19782 -686 -3123 3863 C ATOM 1550 OE1 GLU A 196 -355.045-145.514 134.652 1.00151.62 O ANISOU 1550 OE1 GLU A 196 20806 16233 20572 -860 -3252 4099 O ATOM 1551 OE2 GLU A 196 -355.886-145.270 136.666 1.00155.08 O ANISOU 1551 OE2 GLU A 196 20791 16514 21619 -509 -3152 3827 O ATOM 1552 N GLU A 197 -351.290-149.927 134.543 1.00107.78 N ANISOU 1552 N GLU A 197 15605 11577 13769 -1199 -2192 3277 N ATOM 1553 CA GLU A 197 -350.393-150.440 133.515 1.00113.53 C ANISOU 1553 CA GLU A 197 16584 12444 14107 -1413 -2042 3281 C ATOM 1554 C GLU A 197 -350.516-151.950 133.372 1.00115.17 C ANISOU 1554 C GLU A 197 16822 12841 14096 -1431 -1966 3113 C ATOM 1555 O GLU A 197 -350.324-152.485 132.274 1.00120.58 O ANISOU 1555 O GLU A 197 17747 13631 14438 -1617 -1951 3159 O ATOM 1556 CB GLU A 197 -348.948-150.051 133.835 1.00117.14 C ANISOU 1556 CB GLU A 197 17037 12903 14567 -1457 -1740 3175 C ATOM 1557 CG GLU A 197 -348.691-148.545 133.953 1.00127.04 C ANISOU 1557 CG GLU A 197 18278 13963 16026 -1463 -1788 3332 C ATOM 1558 CD GLU A 197 -349.103-147.959 135.300 1.00133.47 C ANISOU 1558 CD GLU A 197 18821 14639 17253 -1240 -1829 3247 C ATOM 1559 OE1 GLU A 197 -350.156-148.359 135.839 1.00139.66 O ANISOU 1559 OE1 GLU A 197 19458 15414 18191 -1089 -1971 3199 O ATOM 1560 OE2 GLU A 197 -348.369-147.094 135.823 1.00135.47 O ANISOU 1560 OE2 GLU A 197 19011 14789 17674 -1226 -1709 3221 O ATOM 1561 N THR A 198 -350.839-152.647 134.461 1.00111.46 N ANISOU 1561 N THR A 198 16125 12412 13814 -1249 -1912 2915 N ATOM 1562 CA THR A 198 -351.006-154.094 134.451 1.00107.04 C ANISOU 1562 CA THR A 198 15568 12011 13092 -1246 -1844 2749 C ATOM 1563 C THR A 198 -352.465-154.520 134.588 1.00108.36 C ANISOU 1563 C THR A 198 15640 12166 13366 -1155 -2107 2792 C ATOM 1564 O THR A 198 -352.735-155.714 134.756 1.00107.26 O ANISOU 1564 O THR A 198 15467 12140 13147 -1128 -2065 2646 O ATOM 1565 CB THR A 198 -350.162-154.735 135.560 1.00 91.66 C ANISOU 1565 CB THR A 198 13448 10131 11249 -1131 -1566 2488 C ATOM 1566 OG1 THR A 198 -350.472-154.130 136.822 1.00 88.83 O ANISOU 1566 OG1 THR A 198 12850 9665 11236 -944 -1597 2441 O ATOM 1567 CG2 THR A 198 -348.680-154.554 135.272 1.00 80.70 C ANISOU 1567 CG2 THR A 198 12154 8779 9729 -1246 -1297 2433 C ATOM 1568 N ASN A 199 -353.406-153.578 134.507 1.00107.33 N ANISOU 1568 N ASN A 199 15457 11891 13431 -1108 -2375 2990 N ATOM 1569 CA ASN A 199 -354.840-153.857 134.594 1.00105.08 C ANISOU 1569 CA ASN A 199 15056 11574 13296 -1024 -2643 3055 C ATOM 1570 C ASN A 199 -355.169-154.682 135.841 1.00100.89 C ANISOU 1570 C ASN A 199 14280 11092 12960 -843 -2527 2822 C ATOM 1571 O ASN A 199 -355.705-155.790 135.769 1.00103.09 O ANISOU 1571 O ASN A 199 14549 11476 13144 -848 -2565 2740 O ATOM 1572 CB ASN A 199 -355.338-154.553 133.325 1.00105.17 C ANISOU 1572 CB ASN A 199 15291 11684 12986 -1204 -2828 3168 C ATOM 1573 CG ASN A 199 -355.145-153.708 132.086 1.00109.03 C ANISOU 1573 CG ASN A 199 16040 12118 13269 -1399 -2979 3425 C ATOM 1574 OD1 ASN A 199 -355.921-152.792 131.818 1.00121.11 O ANISOU 1574 OD1 ASN A 199 17545 13505 14968 -1384 -3261 3657 O ATOM 1575 ND2 ASN A 199 -354.109-154.016 131.315 1.00105.18 N ANISOU 1575 ND2 ASN A 199 15807 11738 12421 -1587 -2786 3389 N ATOM 1576 N ASN A 200 -354.835-154.111 137.000 1.00 96.80 N ANISOU 1576 N ASN A 200 13576 10492 12712 -695 -2384 2717 N ATOM 1577 CA ASN A 200 -355.067-154.803 138.264 1.00 89.87 C ANISOU 1577 CA ASN A 200 12484 9654 12008 -536 -2258 2500 C ATOM 1578 C ASN A 200 -356.548-155.050 138.521 1.00 93.04 C ANISOU 1578 C ASN A 200 12725 10011 12614 -437 -2467 2536 C ATOM 1579 O ASN A 200 -356.911-156.079 139.101 1.00105.50 O ANISOU 1579 O ASN A 200 14203 11678 14204 -375 -2404 2383 O ATOM 1580 CB ASN A 200 -354.460-154.001 139.419 1.00 82.12 C ANISOU 1580 CB ASN A 200 11359 8578 11263 -421 -2089 2398 C ATOM 1581 CG ASN A 200 -352.948-154.074 139.453 1.00 82.81 C ANISOU 1581 CG ASN A 200 11545 8739 11180 -497 -1843 2298 C ATOM 1582 OD1 ASN A 200 -352.312-154.438 138.465 1.00 86.17 O ANISOU 1582 OD1 ASN A 200 12160 9254 11326 -647 -1795 2341 O ATOM 1583 ND2 ASN A 200 -352.364-153.731 140.592 1.00 79.46 N ANISOU 1583 ND2 ASN A 200 10989 8275 10925 -404 -1681 2159 N ATOM 1584 N GLU A 201 -357.414-154.134 138.089 1.00 95.55 N ANISOU 1584 N GLU A 201 13011 10186 13109 -424 -2717 2743 N ATOM 1585 CA GLU A 201 -358.833-154.241 138.410 1.00 97.10 C ANISOU 1585 CA GLU A 201 13007 10314 13572 -314 -2910 2780 C ATOM 1586 C GLU A 201 -359.452-155.488 137.788 1.00 89.87 C ANISOU 1586 C GLU A 201 12153 9537 12454 -398 -3032 2776 C ATOM 1587 O GLU A 201 -360.183-156.229 138.455 1.00 94.86 O ANISOU 1587 O GLU A 201 12615 10206 13222 -307 -3020 2657 O ATOM 1588 CB GLU A 201 -359.564-152.980 137.947 1.00110.04 C ANISOU 1588 CB GLU A 201 14602 11756 15453 -293 -3172 3027 C ATOM 1589 CG GLU A 201 -360.993-152.861 138.438 1.00123.22 C ANISOU 1589 CG GLU A 201 16007 13311 17501 -148 -3345 3058 C ATOM 1590 CD GLU A 201 -361.551-151.466 138.236 1.00137.27 C ANISOU 1590 CD GLU A 201 17698 14854 19604 -87 -3550 3272 C ATOM 1591 OE1 GLU A 201 -360.756-150.501 138.243 1.00141.21 O ANISOU 1591 OE1 GLU A 201 18281 15257 20117 -100 -3466 3318 O ATOM 1592 OE2 GLU A 201 -362.781-151.335 138.065 1.00143.17 O ANISOU 1592 OE2 GLU A 201 18285 15502 20610 -27 -3798 3398 O ATOM 1593 N SER A 202 -359.158-155.742 136.510 1.00 81.86 N ANISOU 1593 N SER A 202 11394 8602 11106 -586 -3141 2900 N ATOM 1594 CA SER A 202 -359.738-156.901 135.839 1.00 86.47 C ANISOU 1594 CA SER A 202 12065 9312 11478 -689 -3269 2896 C ATOM 1595 C SER A 202 -359.196-158.212 136.397 1.00 85.92 C ANISOU 1595 C SER A 202 11994 9395 11257 -676 -3006 2635 C ATOM 1596 O SER A 202 -359.888-159.236 136.346 1.00 87.76 O ANISOU 1596 O SER A 202 12192 9704 11448 -691 -3077 2573 O ATOM 1597 CB SER A 202 -359.486-156.821 134.334 1.00 90.54 C ANISOU 1597 CB SER A 202 12889 9873 11639 -916 -3430 3080 C ATOM 1598 OG SER A 202 -358.105-156.907 134.037 1.00 97.01 O ANISOU 1598 OG SER A 202 13916 10774 12170 -1021 -3171 2996 O ATOM 1599 N PHE A 203 -357.973-158.208 136.930 1.00 76.68 N ANISOU 1599 N PHE A 203 10854 8263 10018 -651 -2712 2487 N ATOM 1600 CA PHE A 203 -357.434-159.429 137.522 1.00 74.17 C ANISOU 1600 CA PHE A 203 10517 8071 9595 -625 -2474 2252 C ATOM 1601 C PHE A 203 -358.088-159.722 138.866 1.00 74.75 C ANISOU 1601 C PHE A 203 10324 8115 9964 -446 -2423 2121 C ATOM 1602 O PHE A 203 -358.304-160.888 139.215 1.00 78.40 O ANISOU 1602 O PHE A 203 10744 8665 10378 -431 -2355 1983 O ATOM 1603 CB PHE A 203 -355.917-159.323 137.669 1.00 70.82 C ANISOU 1603 CB PHE A 203 10187 7688 9033 -656 -2196 2148 C ATOM 1604 CG PHE A 203 -355.245-160.640 137.948 1.00 69.94 C ANISOU 1604 CG PHE A 203 10104 7703 8766 -667 -1975 1939 C ATOM 1605 CD1 PHE A 203 -354.995-161.533 136.920 1.00 73.39 C ANISOU 1605 CD1 PHE A 203 10747 8241 8896 -821 -1953 1916 C ATOM 1606 CD2 PHE A 203 -354.869-160.985 139.236 1.00 65.03 C ANISOU 1606 CD2 PHE A 203 9310 7090 8306 -531 -1792 1767 C ATOM 1607 CE1 PHE A 203 -354.378-162.748 137.170 1.00 74.34 C ANISOU 1607 CE1 PHE A 203 10883 8454 8906 -823 -1745 1722 C ATOM 1608 CE2 PHE A 203 -354.251-162.198 139.494 1.00 65.44 C ANISOU 1608 CE2 PHE A 203 9382 7242 8241 -536 -1608 1593 C ATOM 1609 CZ PHE A 203 -354.007-163.081 138.459 1.00 69.18 C ANISOU 1609 CZ PHE A 203 10043 7801 8441 -674 -1580 1569 C ATOM 1610 N VAL A 204 -358.411-158.678 139.635 1.00 79.89 N ANISOU 1610 N VAL A 204 10801 8634 10919 -318 -2443 2158 N ATOM 1611 CA VAL A 204 -359.116-158.874 140.900 1.00 82.99 C ANISOU 1611 CA VAL A 204 10951 8989 11593 -162 -2386 2036 C ATOM 1612 C VAL A 204 -360.490-159.481 140.649 1.00 85.25 C ANISOU 1612 C VAL A 204 11140 9281 11969 -159 -2590 2087 C ATOM 1613 O VAL A 204 -360.918-160.404 141.354 1.00 80.73 O ANISOU 1613 O VAL A 204 10455 8767 11453 -105 -2512 1948 O ATOM 1614 CB VAL A 204 -359.216-157.543 141.669 1.00 75.12 C ANISOU 1614 CB VAL A 204 9807 7832 10904 -42 -2364 2064 C ATOM 1615 CG1 VAL A 204 -360.069-157.711 142.922 1.00 72.88 C ANISOU 1615 CG1 VAL A 204 9281 7501 10908 104 -2300 1937 C ATOM 1616 CG2 VAL A 204 -357.829-157.040 142.031 1.00 68.46 C ANISOU 1616 CG2 VAL A 204 9046 6990 9976 -52 -2153 1990 C ATOM 1617 N ILE A 205 -361.204-158.969 139.642 1.00 81.45 N ANISOU 1617 N ILE A 205 10700 8737 11509 -225 -2867 2296 N ATOM 1618 CA ILE A 205 -362.497-159.534 139.270 1.00 78.00 C ANISOU 1618 CA ILE A 205 10175 8307 11155 -244 -3099 2366 C ATOM 1619 C ILE A 205 -362.333-160.982 138.828 1.00 83.06 C ANISOU 1619 C ILE A 205 10958 9111 11490 -361 -3060 2264 C ATOM 1620 O ILE A 205 -363.103-161.865 139.226 1.00 84.09 O ANISOU 1620 O ILE A 205 10962 9281 11706 -331 -3078 2179 O ATOM 1621 CB ILE A 205 -363.152-158.681 138.169 1.00 74.34 C ANISOU 1621 CB ILE A 205 9760 7745 10741 -316 -3432 2635 C ATOM 1622 CG1 ILE A 205 -363.313-157.237 138.638 1.00 79.68 C ANISOU 1622 CG1 ILE A 205 10284 8232 11757 -189 -3460 2731 C ATOM 1623 CG2 ILE A 205 -364.499-159.265 137.757 1.00 68.30 C ANISOU 1623 CG2 ILE A 205 8890 6986 10076 -347 -3703 2718 C ATOM 1624 CD1 ILE A 205 -363.804-156.307 137.546 1.00 79.68 C ANISOU 1624 CD1 ILE A 205 10350 8117 11808 -260 -3790 3019 C ATOM 1625 N TYR A 206 -361.322-161.244 137.997 1.00 77.53 N ANISOU 1625 N TYR A 206 10521 8499 10437 -502 -2992 2265 N ATOM 1626 CA TYR A 206 -361.059-162.606 137.545 1.00 74.19 C ANISOU 1626 CA TYR A 206 10251 8215 9721 -617 -2925 2149 C ATOM 1627 C TYR A 206 -360.721-163.519 138.718 1.00 78.46 C ANISOU 1627 C TYR A 206 10673 8813 10327 -512 -2663 1918 C ATOM 1628 O TYR A 206 -361.229-164.642 138.812 1.00 79.58 O ANISOU 1628 O TYR A 206 10786 9018 10434 -533 -2673 1828 O ATOM 1629 CB TYR A 206 -359.931-162.601 136.513 1.00 68.16 C ANISOU 1629 CB TYR A 206 9784 7518 8595 -779 -2846 2173 C ATOM 1630 CG TYR A 206 -359.207-163.921 136.394 1.00 78.22 C ANISOU 1630 CG TYR A 206 11194 8918 9610 -853 -2635 1982 C ATOM 1631 CD1 TYR A 206 -359.790-165.002 135.749 1.00 79.44 C ANISOU 1631 CD1 TYR A 206 11446 9144 9594 -968 -2745 1952 C ATOM 1632 CD2 TYR A 206 -357.935-164.086 136.931 1.00 80.92 C ANISOU 1632 CD2 TYR A 206 11556 9293 9897 -809 -2332 1831 C ATOM 1633 CE1 TYR A 206 -359.128-166.213 135.643 1.00 83.58 C ANISOU 1633 CE1 TYR A 206 12092 9761 9905 -1031 -2541 1768 C ATOM 1634 CE2 TYR A 206 -357.265-165.291 136.828 1.00 78.11 C ANISOU 1634 CE2 TYR A 206 11303 9030 9345 -864 -2138 1659 C ATOM 1635 CZ TYR A 206 -357.866-166.349 136.181 1.00 82.52 C ANISOU 1635 CZ TYR A 206 11964 9649 9742 -972 -2236 1624 C ATOM 1636 OH TYR A 206 -357.206-167.551 136.075 1.00 83.70 O ANISOU 1636 OH TYR A 206 12215 9869 9719 -1023 -2034 1445 O ATOM 1637 N MET A 207 -359.863-163.052 139.628 1.00 77.11 N ANISOU 1637 N MET A 207 10436 8615 10248 -409 -2440 1827 N ATOM 1638 CA MET A 207 -359.570-163.831 140.827 1.00 76.28 C ANISOU 1638 CA MET A 207 10215 8552 10217 -310 -2219 1630 C ATOM 1639 C MET A 207 -360.825-164.053 141.655 1.00 77.65 C ANISOU 1639 C MET A 207 10160 8683 10660 -209 -2291 1603 C ATOM 1640 O MET A 207 -361.044-165.147 142.189 1.00 80.88 O ANISOU 1640 O MET A 207 10518 9152 11061 -193 -2205 1477 O ATOM 1641 CB MET A 207 -358.502-163.130 141.670 1.00 64.13 C ANISOU 1641 CB MET A 207 8641 6980 8748 -226 -2011 1560 C ATOM 1642 CG MET A 207 -357.097-163.282 141.138 1.00 68.25 C ANISOU 1642 CG MET A 207 9349 7564 9018 -314 -1857 1520 C ATOM 1643 SD MET A 207 -356.585-165.007 141.085 1.00 79.38 S ANISOU 1643 SD MET A 207 10846 9097 10219 -367 -1702 1348 S ATOM 1644 CE MET A 207 -356.645-165.431 142.826 1.00 72.75 C ANISOU 1644 CE MET A 207 9792 8248 9602 -209 -1557 1197 C ATOM 1645 N PHE A 208 -361.666-163.024 141.768 1.00 74.14 N ANISOU 1645 N PHE A 208 9572 8127 10473 -142 -2439 1722 N ATOM 1646 CA PHE A 208 -362.834-163.125 142.632 1.00 76.27 C ANISOU 1646 CA PHE A 208 9598 8342 11041 -38 -2469 1685 C ATOM 1647 C PHE A 208 -363.839-164.128 142.089 1.00 82.80 C ANISOU 1647 C PHE A 208 10403 9221 11838 -112 -2638 1711 C ATOM 1648 O PHE A 208 -364.451-164.880 142.856 1.00 80.24 O ANISOU 1648 O PHE A 208 9936 8916 11635 -65 -2568 1604 O ATOM 1649 CB PHE A 208 -363.484-161.757 142.797 1.00 73.67 C ANISOU 1649 CB PHE A 208 9111 7859 11022 52 -2583 1806 C ATOM 1650 CG PHE A 208 -364.792-161.798 143.521 1.00 74.45 C ANISOU 1650 CG PHE A 208 8946 7886 11456 149 -2624 1781 C ATOM 1651 CD1 PHE A 208 -364.833-162.035 144.884 1.00 78.00 C ANISOU 1651 CD1 PHE A 208 9258 8332 12047 248 -2389 1605 C ATOM 1652 CD2 PHE A 208 -365.979-161.596 142.842 1.00 72.71 C ANISOU 1652 CD2 PHE A 208 8613 7599 11414 133 -2898 1936 C ATOM 1653 CE1 PHE A 208 -366.036-162.073 145.560 1.00 82.39 C ANISOU 1653 CE1 PHE A 208 9571 8822 12914 327 -2392 1571 C ATOM 1654 CE2 PHE A 208 -367.186-161.632 143.512 1.00 79.76 C ANISOU 1654 CE2 PHE A 208 9237 8420 12650 223 -2918 1908 C ATOM 1655 CZ PHE A 208 -367.214-161.873 144.873 1.00 83.04 C ANISOU 1655 CZ PHE A 208 9517 8833 13200 320 -2648 1718 C ATOM 1656 N VAL A 209 -364.020-164.160 140.772 1.00 81.34 N ANISOU 1656 N VAL A 209 10367 9058 11481 -243 -2864 1852 N ATOM 1657 CA VAL A 209 -365.018-165.046 140.188 1.00 73.33 C ANISOU 1657 CA VAL A 209 9336 8086 10439 -332 -3061 1887 C ATOM 1658 C VAL A 209 -364.473-166.463 140.050 1.00 82.26 C ANISOU 1658 C VAL A 209 10627 9344 11285 -424 -2924 1736 C ATOM 1659 O VAL A 209 -365.092-167.430 140.506 1.00 85.20 O ANISOU 1659 O VAL A 209 10897 9747 11728 -416 -2900 1642 O ATOM 1660 CB VAL A 209 -365.488-164.494 138.832 1.00 69.80 C ANISOU 1660 CB VAL A 209 8997 7607 9917 -452 -3388 2110 C ATOM 1661 CG1 VAL A 209 -366.510-165.429 138.222 1.00 71.34 C ANISOU 1661 CG1 VAL A 209 9181 7850 10076 -561 -3611 2144 C ATOM 1662 CG2 VAL A 209 -366.069-163.092 138.999 1.00 70.36 C ANISOU 1662 CG2 VAL A 209 8889 7527 10320 -346 -3533 2270 C ATOM 1663 N VAL A 210 -363.304-166.606 139.425 1.00 80.96 N ANISOU 1663 N VAL A 210 10708 9241 10811 -513 -2822 1707 N ATOM 1664 CA VAL A 210 -362.821-167.926 139.038 1.00 70.88 C ANISOU 1664 CA VAL A 210 9605 8067 9261 -620 -2721 1579 C ATOM 1665 C VAL A 210 -362.102-168.614 140.194 1.00 74.07 C ANISOU 1665 C VAL A 210 9944 8499 9699 -520 -2426 1386 C ATOM 1666 O VAL A 210 -362.251-169.825 140.399 1.00 78.68 O ANISOU 1666 O VAL A 210 10535 9130 10232 -546 -2360 1270 O ATOM 1667 CB VAL A 210 -361.924-167.808 137.794 1.00 71.66 C ANISOU 1667 CB VAL A 210 9995 8212 9020 -774 -2728 1626 C ATOM 1668 CG1 VAL A 210 -361.119-169.083 137.590 1.00 73.42 C ANISOU 1668 CG1 VAL A 210 10386 8521 8991 -852 -2527 1450 C ATOM 1669 CG2 VAL A 210 -362.769-167.498 136.564 1.00 61.47 C ANISOU 1669 CG2 VAL A 210 8809 6913 7635 -918 -3056 1811 C ATOM 1670 N HIS A 211 -361.310-167.869 140.965 1.00 67.35 N ANISOU 1670 N HIS A 211 9037 7615 8936 -412 -2256 1356 N ATOM 1671 CA HIS A 211 -360.506-168.452 142.031 1.00 62.02 C ANISOU 1671 CA HIS A 211 8322 6967 8275 -330 -1999 1193 C ATOM 1672 C HIS A 211 -361.052-168.137 143.419 1.00 63.73 C ANISOU 1672 C HIS A 211 8309 7132 8775 -190 -1936 1152 C ATOM 1673 O HIS A 211 -360.306-168.194 144.402 1.00 73.47 O ANISOU 1673 O HIS A 211 9508 8370 10038 -115 -1742 1051 O ATOM 1674 CB HIS A 211 -359.056-167.981 141.909 1.00 64.27 C ANISOU 1674 CB HIS A 211 8731 7265 8424 -335 -1836 1168 C ATOM 1675 CG HIS A 211 -358.418-168.339 140.604 1.00 68.26 C ANISOU 1675 CG HIS A 211 9471 7823 8641 -481 -1840 1181 C ATOM 1676 ND1 HIS A 211 -357.638-169.462 140.442 1.00 61.14 N ANISOU 1676 ND1 HIS A 211 8681 6978 7572 -530 -1675 1047 N ATOM 1677 CD2 HIS A 211 -358.447-167.725 139.398 1.00 71.54 C ANISOU 1677 CD2 HIS A 211 10040 8236 8905 -597 -1979 1311 C ATOM 1678 CE1 HIS A 211 -357.214-169.525 139.192 1.00 64.44 C ANISOU 1678 CE1 HIS A 211 9311 7428 7743 -671 -1691 1075 C ATOM 1679 NE2 HIS A 211 -357.689-168.482 138.537 1.00 64.86 N ANISOU 1679 NE2 HIS A 211 9405 7454 7785 -723 -1878 1240 N ATOM 1680 N PHE A 212 -362.338-167.808 143.524 1.00 67.60 N ANISOU 1680 N PHE A 212 8641 7568 9475 -160 -2093 1226 N ATOM 1681 CA PHE A 212 -362.935-167.570 144.832 1.00 71.19 C ANISOU 1681 CA PHE A 212 8881 7971 10198 -40 -2004 1169 C ATOM 1682 C PHE A 212 -364.399-168.002 144.860 1.00 73.73 C ANISOU 1682 C PHE A 212 9041 8270 10702 -47 -2142 1197 C ATOM 1683 O PHE A 212 -364.791-168.802 145.715 1.00 73.60 O ANISOU 1683 O PHE A 212 8930 8274 10762 -21 -2032 1094 O ATOM 1684 CB PHE A 212 -362.793-166.097 145.226 1.00 68.82 C ANISOU 1684 CB PHE A 212 8499 7578 10072 49 -1987 1226 C ATOM 1685 CG PHE A 212 -363.113-165.823 146.668 1.00 67.85 C ANISOU 1685 CG PHE A 212 8199 7404 10177 162 -1830 1127 C ATOM 1686 CD1 PHE A 212 -362.312-166.338 147.676 1.00 62.16 C ANISOU 1686 CD1 PHE A 212 7514 6732 9373 189 -1614 988 C ATOM 1687 CD2 PHE A 212 -364.210-165.048 147.016 1.00 66.34 C ANISOU 1687 CD2 PHE A 212 7808 7110 10287 235 -1896 1173 C ATOM 1688 CE1 PHE A 212 -362.601-166.094 149.004 1.00 60.36 C ANISOU 1688 CE1 PHE A 212 7155 6463 9317 269 -1467 895 C ATOM 1689 CE2 PHE A 212 -364.504-164.793 148.342 1.00 63.88 C ANISOU 1689 CE2 PHE A 212 7350 6749 10171 324 -1721 1064 C ATOM 1690 CZ PHE A 212 -363.699-165.316 149.338 1.00 65.07 C ANISOU 1690 CZ PHE A 212 7568 6961 10195 333 -1505 924 C ATOM 1691 N ILE A 213 -365.211-167.493 143.930 1.00 71.45 N ANISOU 1691 N ILE A 213 8719 7939 10490 -90 -2390 1345 N ATOM 1692 CA ILE A 213 -366.625-167.861 143.891 1.00 75.01 C ANISOU 1692 CA ILE A 213 8992 8363 11147 -103 -2547 1386 C ATOM 1693 C ILE A 213 -366.789-169.301 143.414 1.00 80.07 C ANISOU 1693 C ILE A 213 9736 9092 11594 -222 -2588 1329 C ATOM 1694 O ILE A 213 -367.406-170.132 144.092 1.00 75.37 O ANISOU 1694 O ILE A 213 9020 8509 11107 -211 -2517 1242 O ATOM 1695 CB ILE A 213 -367.417-166.890 142.998 1.00 78.18 C ANISOU 1695 CB ILE A 213 9322 8682 11699 -119 -2835 1580 C ATOM 1696 CG1 ILE A 213 -367.416-165.477 143.590 1.00 81.62 C ANISOU 1696 CG1 ILE A 213 9618 8998 12395 15 -2784 1625 C ATOM 1697 CG2 ILE A 213 -368.843-167.395 142.794 1.00 68.45 C ANISOU 1697 CG2 ILE A 213 7910 7430 10666 -155 -3032 1631 C ATOM 1698 CD1 ILE A 213 -367.969-165.399 144.995 1.00 80.66 C ANISOU 1698 CD1 ILE A 213 9256 8820 12569 141 -2589 1503 C ATOM 1699 N ILE A 214 -366.240-169.609 142.233 1.00 81.68 N ANISOU 1699 N ILE A 214 10174 9353 11507 -348 -2692 1373 N ATOM 1700 CA ILE A 214 -366.400-170.946 141.654 1.00 75.91 C ANISOU 1700 CA ILE A 214 9565 8695 10584 -478 -2741 1313 C ATOM 1701 C ILE A 214 -365.945-172.056 142.600 1.00 79.41 C ANISOU 1701 C ILE A 214 10008 9176 10987 -443 -2488 1135 C ATOM 1702 O ILE A 214 -366.695-173.026 142.777 1.00 84.18 O ANISOU 1702 O ILE A 214 10542 9792 11648 -486 -2517 1084 O ATOM 1703 CB ILE A 214 -365.710-171.017 140.282 1.00 72.72 C ANISOU 1703 CB ILE A 214 9444 8341 9845 -624 -2841 1364 C ATOM 1704 CG1 ILE A 214 -366.405-170.099 139.272 1.00 70.58 C ANISOU 1704 CG1 ILE A 214 9179 8030 9607 -692 -3153 1566 C ATOM 1705 CG2 ILE A 214 -365.665-172.452 139.778 1.00 67.86 C ANISOU 1705 CG2 ILE A 214 8982 7791 9009 -755 -2828 1258 C ATOM 1706 CD1 ILE A 214 -367.907-170.082 139.393 1.00 84.92 C ANISOU 1706 CD1 ILE A 214 10755 9795 11715 -679 -3378 1651 C ATOM 1707 N PRO A 215 -364.757-171.992 143.225 1.00 75.47 N ANISOU 1707 N PRO A 215 9581 8693 10400 -374 -2253 1046 N ATOM 1708 CA PRO A 215 -364.380-173.068 144.161 1.00 71.65 C ANISOU 1708 CA PRO A 215 9091 8235 9899 -342 -2044 899 C ATOM 1709 C PRO A 215 -365.416-173.325 145.243 1.00 72.88 C ANISOU 1709 C PRO A 215 9025 8358 10307 -281 -2008 867 C ATOM 1710 O PRO A 215 -365.682-174.488 145.567 1.00 77.56 O ANISOU 1710 O PRO A 215 9614 8970 10885 -320 -1952 788 O ATOM 1711 CB PRO A 215 -363.054-172.566 144.751 1.00 68.45 C ANISOU 1711 CB PRO A 215 8745 7832 9431 -259 -1844 849 C ATOM 1712 CG PRO A 215 -362.490-171.687 143.700 1.00 67.99 C ANISOU 1712 CG PRO A 215 8818 7776 9240 -303 -1932 940 C ATOM 1713 CD PRO A 215 -363.672-171.002 143.079 1.00 72.74 C ANISOU 1713 CD PRO A 215 9333 8339 9965 -334 -2179 1079 C ATOM 1714 N LEU A 216 -366.020-172.274 145.803 1.00 68.93 N ANISOU 1714 N LEU A 216 8341 7802 10047 -192 -2028 923 N ATOM 1715 CA LEU A 216 -367.039-172.478 146.828 1.00 70.04 C ANISOU 1715 CA LEU A 216 8266 7908 10437 -143 -1965 883 C ATOM 1716 C LEU A 216 -368.271-173.169 146.256 1.00 80.65 C ANISOU 1716 C LEU A 216 9520 9252 11872 -232 -2148 924 C ATOM 1717 O LEU A 216 -368.822-174.085 146.880 1.00 81.97 O ANISOU 1717 O LEU A 216 9606 9426 12115 -254 -2069 852 O ATOM 1718 CB LEU A 216 -367.428-171.142 147.461 1.00 74.72 C ANISOU 1718 CB LEU A 216 8681 8424 11283 -32 -1936 923 C ATOM 1719 CG LEU A 216 -368.365-171.257 148.663 1.00 79.82 C ANISOU 1719 CG LEU A 216 9109 9031 12189 22 -1805 855 C ATOM 1720 CD1 LEU A 216 -367.602-171.802 149.851 1.00 81.44 C ANISOU 1720 CD1 LEU A 216 9388 9272 12283 47 -1548 726 C ATOM 1721 CD2 LEU A 216 -368.977-169.921 149.006 1.00 82.74 C ANISOU 1721 CD2 LEU A 216 9285 9303 12849 119 -1814 901 C ATOM 1722 N ILE A 217 -368.716-172.745 145.069 1.00 74.08 N ANISOU 1722 N ILE A 217 8707 8409 11033 -296 -2403 1047 N ATOM 1723 CA ILE A 217 -369.911-173.331 144.463 1.00 75.08 C ANISOU 1723 CA ILE A 217 8741 8532 11255 -394 -2618 1100 C ATOM 1724 C ILE A 217 -369.700-174.818 144.196 1.00 78.25 C ANISOU 1724 C ILE A 217 9297 8995 11441 -511 -2583 1005 C ATOM 1725 O ILE A 217 -370.565-175.651 144.495 1.00 71.65 O ANISOU 1725 O ILE A 217 8344 8154 10727 -557 -2598 967 O ATOM 1726 CB ILE A 217 -370.285-172.581 143.171 1.00 76.47 C ANISOU 1726 CB ILE A 217 8949 8688 11418 -459 -2927 1267 C ATOM 1727 CG1 ILE A 217 -370.473-171.085 143.435 1.00 76.69 C ANISOU 1727 CG1 ILE A 217 8820 8630 11687 -335 -2962 1368 C ATOM 1728 CG2 ILE A 217 -371.554-173.169 142.561 1.00 71.01 C ANISOU 1728 CG2 ILE A 217 8149 7991 10842 -570 -3180 1330 C ATOM 1729 CD1 ILE A 217 -371.524-170.785 144.476 1.00 77.38 C ANISOU 1729 CD1 ILE A 217 8589 8641 12171 -230 -2890 1346 C ATOM 1730 N VAL A 218 -368.546-175.171 143.626 1.00 77.98 N ANISOU 1730 N VAL A 218 9522 9009 11099 -562 -2526 960 N ATOM 1731 CA VAL A 218 -368.288-176.559 143.250 1.00 76.70 C ANISOU 1731 CA VAL A 218 9523 8885 10733 -674 -2494 863 C ATOM 1732 C VAL A 218 -368.202-177.444 144.487 1.00 74.04 C ANISOU 1732 C VAL A 218 9115 8540 10477 -620 -2264 743 C ATOM 1733 O VAL A 218 -368.764-178.546 144.523 1.00 79.15 O ANISOU 1733 O VAL A 218 9749 9185 11141 -700 -2279 690 O ATOM 1734 CB VAL A 218 -367.010-176.655 142.399 1.00 73.48 C ANISOU 1734 CB VAL A 218 9396 8517 10006 -730 -2447 830 C ATOM 1735 CG1 VAL A 218 -366.653-178.109 142.142 1.00 74.89 C ANISOU 1735 CG1 VAL A 218 9736 8715 10005 -827 -2363 703 C ATOM 1736 CG2 VAL A 218 -367.200-175.913 141.089 1.00 68.04 C ANISOU 1736 CG2 VAL A 218 8810 7840 9201 -824 -2692 958 C ATOM 1737 N ILE A 219 -367.497-176.977 145.517 1.00 68.41 N ANISOU 1737 N ILE A 219 8367 7819 9808 -495 -2057 704 N ATOM 1738 CA ILE A 219 -367.351-177.768 146.736 1.00 70.70 C ANISOU 1738 CA ILE A 219 8612 8100 10151 -453 -1847 607 C ATOM 1739 C ILE A 219 -368.708-177.996 147.390 1.00 76.07 C ANISOU 1739 C ILE A 219 9070 8752 11083 -462 -1866 615 C ATOM 1740 O ILE A 219 -369.036-179.115 147.805 1.00 81.69 O ANISOU 1740 O ILE A 219 9773 9458 11808 -516 -1800 554 O ATOM 1741 CB ILE A 219 -366.362-177.088 147.699 1.00 65.84 C ANISOU 1741 CB ILE A 219 8006 7484 9528 -332 -1654 578 C ATOM 1742 CG1 ILE A 219 -364.926-177.344 147.235 1.00 71.93 C ANISOU 1742 CG1 ILE A 219 8991 8280 10058 -338 -1584 537 C ATOM 1743 CG2 ILE A 219 -366.586-177.574 149.125 1.00 61.85 C ANISOU 1743 CG2 ILE A 219 7401 6962 9136 -290 -1474 514 C ATOM 1744 CD1 ILE A 219 -363.872-176.785 148.164 1.00 73.16 C ANISOU 1744 CD1 ILE A 219 9159 8436 10203 -234 -1411 508 C ATOM 1745 N PHE A 220 -369.524-176.942 147.480 1.00 73.59 N ANISOU 1745 N PHE A 220 8565 8407 10989 -411 -1950 691 N ATOM 1746 CA PHE A 220 -370.834-177.072 148.110 1.00 72.61 C ANISOU 1746 CA PHE A 220 8198 8247 11143 -414 -1946 694 C ATOM 1747 C PHE A 220 -371.761-177.964 147.292 1.00 76.53 C ANISOU 1747 C PHE A 220 8663 8746 11668 -547 -2142 720 C ATOM 1748 O PHE A 220 -372.480-178.800 147.854 1.00 77.63 O ANISOU 1748 O PHE A 220 8697 8873 11927 -595 -2077 673 O ATOM 1749 CB PHE A 220 -371.462-175.696 148.312 1.00 71.53 C ANISOU 1749 CB PHE A 220 7852 8058 11267 -321 -1991 766 C ATOM 1750 CG PHE A 220 -371.248-175.128 149.683 1.00 86.20 C ANISOU 1750 CG PHE A 220 9624 9890 13238 -211 -1735 698 C ATOM 1751 CD1 PHE A 220 -370.072-174.470 150.002 1.00 94.26 C ANISOU 1751 CD1 PHE A 220 10781 10922 14113 -135 -1619 675 C ATOM 1752 CD2 PHE A 220 -372.230-175.242 150.652 1.00 97.16 C ANISOU 1752 CD2 PHE A 220 10799 11240 14876 -197 -1605 653 C ATOM 1753 CE1 PHE A 220 -369.878-173.938 151.268 1.00 97.62 C ANISOU 1753 CE1 PHE A 220 11146 11323 14624 -53 -1395 606 C ATOM 1754 CE2 PHE A 220 -372.041-174.715 151.919 1.00104.79 C ANISOU 1754 CE2 PHE A 220 11713 12183 15919 -116 -1357 578 C ATOM 1755 CZ PHE A 220 -370.865-174.058 152.224 1.00102.97 C ANISOU 1755 CZ PHE A 220 11634 11965 15526 -46 -1261 554 C ATOM 1756 N PHE A 221 -371.759-177.805 145.967 1.00 72.88 N ANISOU 1756 N PHE A 221 8302 8301 11087 -624 -2385 795 N ATOM 1757 CA PHE A 221 -372.625-178.622 145.122 1.00 75.17 C ANISOU 1757 CA PHE A 221 8582 8595 11383 -771 -2600 820 C ATOM 1758 C PHE A 221 -372.263-180.098 145.232 1.00 83.08 C ANISOU 1758 C PHE A 221 9741 9615 12210 -860 -2488 704 C ATOM 1759 O PHE A 221 -373.113-180.941 145.541 1.00 88.68 O ANISOU 1759 O PHE A 221 10338 10304 13052 -931 -2491 672 O ATOM 1760 CB PHE A 221 -372.536-178.154 143.668 1.00 75.65 C ANISOU 1760 CB PHE A 221 8779 8677 11288 -854 -2879 922 C ATOM 1761 CG PHE A 221 -373.252-179.052 142.697 1.00 78.47 C ANISOU 1761 CG PHE A 221 9189 9047 11580 -1033 -3114 936 C ATOM 1762 CD1 PHE A 221 -374.591-178.848 142.402 1.00 78.31 C ANISOU 1762 CD1 PHE A 221 8941 8995 11816 -1087 -3359 1036 C ATOM 1763 CD2 PHE A 221 -372.588-180.101 142.076 1.00 80.32 C ANISOU 1763 CD2 PHE A 221 9694 9315 11509 -1152 -3090 844 C ATOM 1764 CE1 PHE A 221 -375.254-179.675 141.510 1.00 74.77 C ANISOU 1764 CE1 PHE A 221 8545 8560 11304 -1268 -3595 1050 C ATOM 1765 CE2 PHE A 221 -373.247-180.931 141.186 1.00 81.91 C ANISOU 1765 CE2 PHE A 221 9961 9523 11637 -1332 -3304 843 C ATOM 1766 CZ PHE A 221 -374.581-180.716 140.902 1.00 79.04 C ANISOU 1766 CZ PHE A 221 9380 9138 11513 -1396 -3567 949 C ATOM 1767 N CYS A 222 -370.998-180.427 144.971 1.00 80.84 N ANISOU 1767 N CYS A 222 9710 9358 11647 -860 -2384 640 N ATOM 1768 CA CYS A 222 -370.577-181.822 144.947 1.00 78.09 C ANISOU 1768 CA CYS A 222 9524 9006 11140 -942 -2289 531 C ATOM 1769 C CYS A 222 -370.850-182.510 146.279 1.00 80.13 C ANISOU 1769 C CYS A 222 9663 9233 11550 -902 -2087 471 C ATOM 1770 O CYS A 222 -371.374-183.629 146.320 1.00 84.80 O ANISOU 1770 O CYS A 222 10251 9798 12170 -1000 -2094 423 O ATOM 1771 CB CYS A 222 -369.095-181.903 144.589 1.00 72.98 C ANISOU 1771 CB CYS A 222 9130 8378 10222 -916 -2173 472 C ATOM 1772 SG CYS A 222 -368.732-181.504 142.863 1.00 77.63 S ANISOU 1772 SG CYS A 222 9936 9005 10555 -1028 -2384 515 S ATOM 1773 N TYR A 223 -370.504-181.850 147.383 1.00 76.60 N ANISOU 1773 N TYR A 223 9128 8784 11192 -770 -1908 472 N ATOM 1774 CA TYR A 223 -370.682-182.479 148.685 1.00 72.43 C ANISOU 1774 CA TYR A 223 8522 8230 10769 -747 -1706 420 C ATOM 1775 C TYR A 223 -372.146-182.514 149.104 1.00 74.37 C ANISOU 1775 C TYR A 223 8518 8452 11285 -789 -1741 448 C ATOM 1776 O TYR A 223 -372.566-183.462 149.776 1.00 76.68 O ANISOU 1776 O TYR A 223 8773 8719 11643 -846 -1636 405 O ATOM 1777 CB TYR A 223 -369.828-181.759 149.728 1.00 67.05 C ANISOU 1777 CB TYR A 223 7850 7557 10068 -615 -1509 408 C ATOM 1778 CG TYR A 223 -368.383-182.183 149.665 1.00 73.78 C ANISOU 1778 CG TYR A 223 8926 8416 10689 -586 -1419 361 C ATOM 1779 CD1 TYR A 223 -368.047-183.516 149.458 1.00 67.95 C ANISOU 1779 CD1 TYR A 223 8326 7652 9841 -660 -1394 303 C ATOM 1780 CD2 TYR A 223 -367.357-181.257 149.783 1.00 68.42 C ANISOU 1780 CD2 TYR A 223 8312 7761 9925 -487 -1360 372 C ATOM 1781 CE1 TYR A 223 -366.731-183.916 149.386 1.00 71.28 C ANISOU 1781 CE1 TYR A 223 8926 8063 10093 -626 -1307 258 C ATOM 1782 CE2 TYR A 223 -366.033-181.646 149.714 1.00 62.56 C ANISOU 1782 CE2 TYR A 223 7747 7019 9004 -461 -1278 330 C ATOM 1783 CZ TYR A 223 -365.725-182.978 149.514 1.00 70.27 C ANISOU 1783 CZ TYR A 223 8842 7964 9894 -526 -1250 273 C ATOM 1784 OH TYR A 223 -364.408-183.376 149.444 1.00 77.85 O ANISOU 1784 OH TYR A 223 9953 8908 10718 -490 -1162 229 O ATOM 1785 N GLY A 224 -372.937-181.511 148.717 1.00 68.81 N ANISOU 1785 N GLY A 224 7637 7747 10761 -766 -1887 524 N ATOM 1786 CA GLY A 224 -374.360-181.567 149.006 1.00 72.63 C ANISOU 1786 CA GLY A 224 7857 8200 11540 -811 -1933 550 C ATOM 1787 C GLY A 224 -375.041-182.712 148.282 1.00 81.35 C ANISOU 1787 C GLY A 224 8974 9296 12640 -970 -2095 544 C ATOM 1788 O GLY A 224 -375.816-183.468 148.873 1.00 86.26 O ANISOU 1788 O GLY A 224 9471 9889 13413 -1036 -2017 512 O ATOM 1789 N GLN A 225 -374.755-182.854 146.985 1.00 79.02 N ANISOU 1789 N GLN A 225 8842 9022 12161 -1047 -2317 570 N ATOM 1790 CA GLN A 225 -375.280-183.985 146.228 1.00 78.39 C ANISOU 1790 CA GLN A 225 8822 8932 12031 -1216 -2475 546 C ATOM 1791 C GLN A 225 -374.819-185.305 146.826 1.00 79.89 C ANISOU 1791 C GLN A 225 9150 9096 12108 -1262 -2276 440 C ATOM 1792 O GLN A 225 -375.595-186.264 146.912 1.00 89.16 O ANISOU 1792 O GLN A 225 10257 10237 13384 -1378 -2301 412 O ATOM 1793 CB GLN A 225 -374.844-183.881 144.767 1.00 76.37 C ANISOU 1793 CB GLN A 225 8779 8707 11532 -1299 -2711 575 C ATOM 1794 CG GLN A 225 -375.532-182.778 143.981 1.00 87.00 C ANISOU 1794 CG GLN A 225 9992 10066 12999 -1304 -2987 707 C ATOM 1795 CD GLN A 225 -377.021-183.012 143.828 1.00 99.14 C ANISOU 1795 CD GLN A 225 11274 11574 14820 -1404 -3188 765 C ATOM 1796 OE1 GLN A 225 -377.820-182.564 144.649 1.00101.52 O ANISOU 1796 OE1 GLN A 225 11284 11843 15447 -1327 -3120 799 O ATOM 1797 NE2 GLN A 225 -377.402-183.719 142.771 1.00109.15 N ANISOU 1797 NE2 GLN A 225 12649 12850 15973 -1584 -3431 770 N ATOM 1798 N LEU A 226 -373.555-185.371 147.246 1.00 78.45 N ANISOU 1798 N LEU A 226 9154 8920 11732 -1175 -2087 387 N ATOM 1799 CA LEU A 226 -373.025-186.594 147.837 1.00 76.84 C ANISOU 1799 CA LEU A 226 9084 8676 11436 -1204 -1908 303 C ATOM 1800 C LEU A 226 -373.782-186.959 149.109 1.00 81.04 C ANISOU 1800 C LEU A 226 9434 9176 12180 -1205 -1748 302 C ATOM 1801 O LEU A 226 -374.238-188.097 149.269 1.00 84.57 O ANISOU 1801 O LEU A 226 9886 9575 12669 -1314 -1725 265 O ATOM 1802 CB LEU A 226 -371.530-186.423 148.111 1.00 66.85 C ANISOU 1802 CB LEU A 226 8011 7420 9968 -1092 -1751 267 C ATOM 1803 CG LEU A 226 -370.708-187.647 148.515 1.00 70.75 C ANISOU 1803 CG LEU A 226 8680 7859 10344 -1108 -1597 190 C ATOM 1804 CD1 LEU A 226 -369.281-187.494 148.013 1.00 71.03 C ANISOU 1804 CD1 LEU A 226 8924 7903 10162 -1041 -1554 151 C ATOM 1805 CD2 LEU A 226 -370.722-187.829 150.024 1.00 66.65 C ANISOU 1805 CD2 LEU A 226 8076 7316 9931 -1048 -1393 200 C ATOM 1806 N VAL A 227 -373.926-185.998 150.026 1.00 74.28 N ANISOU 1806 N VAL A 227 8425 8341 11459 -1096 -1624 337 N ATOM 1807 CA VAL A 227 -374.644-186.260 151.270 1.00 72.86 C ANISOU 1807 CA VAL A 227 8082 8135 11466 -1107 -1441 329 C ATOM 1808 C VAL A 227 -376.093-186.624 150.981 1.00 84.01 C ANISOU 1808 C VAL A 227 9278 9522 13118 -1227 -1559 349 C ATOM 1809 O VAL A 227 -376.677-187.489 151.646 1.00 90.57 O ANISOU 1809 O VAL A 227 10046 10316 14052 -1312 -1446 325 O ATOM 1810 CB VAL A 227 -374.535-185.050 152.213 1.00 72.69 C ANISOU 1810 CB VAL A 227 7946 8137 11534 -975 -1284 346 C ATOM 1811 CG1 VAL A 227 -375.445-185.229 153.411 1.00 73.98 C ANISOU 1811 CG1 VAL A 227 7927 8276 11904 -1008 -1089 330 C ATOM 1812 CG2 VAL A 227 -373.096-184.868 152.664 1.00 71.07 C ANISOU 1812 CG2 VAL A 227 7954 7951 11097 -879 -1156 323 C ATOM 1813 N PHE A 228 -376.691-185.985 149.975 1.00 83.97 N ANISOU 1813 N PHE A 228 9158 9534 13212 -1244 -1800 402 N ATOM 1814 CA PHE A 228 -378.052-186.336 149.588 1.00 82.60 C ANISOU 1814 CA PHE A 228 8769 9335 13279 -1367 -1957 431 C ATOM 1815 C PHE A 228 -378.126-187.775 149.091 1.00 83.83 C ANISOU 1815 C PHE A 228 9070 9460 13323 -1529 -2033 382 C ATOM 1816 O PHE A 228 -378.978-188.554 149.536 1.00 87.59 O ANISOU 1816 O PHE A 228 9416 9895 13968 -1633 -1980 366 O ATOM 1817 CB PHE A 228 -378.563-185.373 148.517 1.00 81.53 C ANISOU 1817 CB PHE A 228 8511 9220 13247 -1359 -2245 516 C ATOM 1818 CG PHE A 228 -379.919-185.726 147.992 1.00 87.43 C ANISOU 1818 CG PHE A 228 9036 9940 14244 -1494 -2460 559 C ATOM 1819 CD1 PHE A 228 -381.060-185.313 148.658 1.00 87.96 C ANISOU 1819 CD1 PHE A 228 8759 9975 14687 -1474 -2399 590 C ATOM 1820 CD2 PHE A 228 -380.058-186.481 146.837 1.00 97.79 C ANISOU 1820 CD2 PHE A 228 10480 11254 15422 -1650 -2717 561 C ATOM 1821 CE1 PHE A 228 -382.312-185.639 148.183 1.00 86.37 C ANISOU 1821 CE1 PHE A 228 8326 9745 14747 -1600 -2605 634 C ATOM 1822 CE2 PHE A 228 -381.309-186.814 146.357 1.00 95.91 C ANISOU 1822 CE2 PHE A 228 10033 10992 15417 -1788 -2937 604 C ATOM 1823 CZ PHE A 228 -382.436-186.392 147.030 1.00 91.08 C ANISOU 1823 CZ PHE A 228 9056 10348 15202 -1760 -2888 647 C ATOM 1824 N THR A 229 -377.241-188.143 148.159 1.00 79.67 N ANISOU 1824 N THR A 229 8812 8944 12517 -1560 -2146 352 N ATOM 1825 CA THR A 229 -377.234-189.502 147.625 1.00 78.80 C ANISOU 1825 CA THR A 229 8864 8788 12289 -1714 -2210 287 C ATOM 1826 C THR A 229 -377.024-190.533 148.728 1.00 79.70 C ANISOU 1826 C THR A 229 9028 8842 12412 -1729 -1957 232 C ATOM 1827 O THR A 229 -377.709-191.562 148.767 1.00 87.87 O ANISOU 1827 O THR A 229 10026 9821 13540 -1868 -1973 205 O ATOM 1828 CB THR A 229 -376.149-189.633 146.551 1.00 75.75 C ANISOU 1828 CB THR A 229 8776 8415 11588 -1725 -2308 242 C ATOM 1829 OG1 THR A 229 -376.555-188.931 145.371 1.00 83.80 O ANISOU 1829 OG1 THR A 229 9772 9481 12587 -1778 -2590 301 O ATOM 1830 CG2 THR A 229 -375.892-191.094 146.210 1.00 67.14 C ANISOU 1830 CG2 THR A 229 7889 7256 10365 -1858 -2292 145 C ATOM 1831 N VAL A 230 -376.099-190.263 149.648 1.00 77.42 N ANISOU 1831 N VAL A 230 8822 8561 12032 -1595 -1732 224 N ATOM 1832 CA VAL A 230 -375.800-191.218 150.711 1.00 74.49 C ANISOU 1832 CA VAL A 230 8527 8130 11645 -1610 -1509 193 C ATOM 1833 C VAL A 230 -376.982-191.348 151.668 1.00 76.80 C ANISOU 1833 C VAL A 230 8580 8406 12195 -1671 -1397 222 C ATOM 1834 O VAL A 230 -377.344-192.457 152.076 1.00 86.69 O ANISOU 1834 O VAL A 230 9851 9592 13497 -1784 -1322 203 O ATOM 1835 CB VAL A 230 -374.507-190.808 151.439 1.00 69.04 C ANISOU 1835 CB VAL A 230 7982 7458 10793 -1459 -1331 193 C ATOM 1836 CG1 VAL A 230 -374.362-191.567 152.747 1.00 65.95 C ANISOU 1836 CG1 VAL A 230 7627 7013 10419 -1472 -1109 196 C ATOM 1837 CG2 VAL A 230 -373.305-191.063 150.542 1.00 58.20 C ANISOU 1837 CG2 VAL A 230 6857 6073 9182 -1428 -1402 147 C ATOM 1838 N LYS A 231 -377.608-190.225 152.034 1.00 75.26 N ANISOU 1838 N LYS A 231 8156 8261 12180 -1603 -1372 264 N ATOM 1839 CA LYS A 231 -378.767-190.290 152.918 1.00 73.79 C ANISOU 1839 CA LYS A 231 7721 8056 12260 -1663 -1238 279 C ATOM 1840 C LYS A 231 -379.958-190.947 152.233 1.00 78.62 C ANISOU 1840 C LYS A 231 8175 8632 13066 -1826 -1416 283 C ATOM 1841 O LYS A 231 -380.798-191.566 152.901 1.00 70.23 O ANISOU 1841 O LYS A 231 6973 7527 12183 -1930 -1294 279 O ATOM 1842 CB LYS A 231 -379.140-188.890 153.406 1.00 69.09 C ANISOU 1842 CB LYS A 231 6909 7506 11835 -1544 -1161 307 C ATOM 1843 CG LYS A 231 -378.157-188.304 154.403 1.00 73.27 C ANISOU 1843 CG LYS A 231 7565 8063 12212 -1413 -934 293 C ATOM 1844 CD LYS A 231 -378.605-186.937 154.889 1.00 78.50 C ANISOU 1844 CD LYS A 231 8010 8753 13065 -1307 -843 303 C ATOM 1845 CE LYS A 231 -377.672-186.402 155.967 1.00 80.75 C ANISOU 1845 CE LYS A 231 8431 9062 13189 -1203 -610 278 C ATOM 1846 NZ LYS A 231 -377.674-187.259 157.186 1.00 77.48 N ANISOU 1846 NZ LYS A 231 8098 8625 12717 -1285 -363 255 N ATOM 1847 N GLU A 232 -380.049-190.818 150.909 1.00 82.20 N ANISOU 1847 N GLU A 232 8652 9101 13480 -1864 -1705 294 N ATOM 1848 CA GLU A 232 -381.095-191.499 150.158 1.00 79.25 C ANISOU 1848 CA GLU A 232 8160 8693 13258 -2039 -1914 297 C ATOM 1849 C GLU A 232 -380.905-193.010 150.215 1.00 89.16 C ANISOU 1849 C GLU A 232 9602 9874 14399 -2177 -1859 236 C ATOM 1850 O GLU A 232 -381.848-193.758 150.501 1.00 92.17 O ANISOU 1850 O GLU A 232 9841 10204 14973 -2316 -1837 232 O ATOM 1851 CB GLU A 232 -381.083-191.009 148.711 1.00 83.61 C ANISOU 1851 CB GLU A 232 8755 9283 13731 -2059 -2247 326 C ATOM 1852 CG GLU A 232 -382.445-190.845 148.071 1.00101.49 C ANISOU 1852 CG GLU A 232 10742 11544 16275 -2175 -2505 383 C ATOM 1853 CD GLU A 232 -382.339-190.389 146.629 1.00117.24 C ANISOU 1853 CD GLU A 232 12831 13578 18138 -2212 -2853 425 C ATOM 1854 OE1 GLU A 232 -381.250-190.554 146.037 1.00127.86 O ANISOU 1854 OE1 GLU A 232 14492 14940 19148 -2197 -2879 381 O ATOM 1855 OE2 GLU A 232 -383.337-189.860 146.091 1.00113.86 O ANISOU 1855 OE2 GLU A 232 12161 13158 17943 -2261 -3099 506 O ATOM 1856 N ALA A 233 -379.679-193.474 149.956 1.00 86.15 N ANISOU 1856 N ALA A 233 9533 9475 13725 -2139 -1829 187 N ATOM 1857 CA ALA A 233 -379.415-194.908 149.937 1.00 78.99 C ANISOU 1857 CA ALA A 233 8819 8475 12719 -2259 -1784 126 C ATOM 1858 C ALA A 233 -379.591-195.523 151.320 1.00 77.10 C ANISOU 1858 C ALA A 233 8534 8179 12581 -2277 -1515 140 C ATOM 1859 O ALA A 233 -380.144-196.622 151.452 1.00 74.73 O ANISOU 1859 O ALA A 233 8229 7796 12369 -2428 -1496 120 O ATOM 1860 CB ALA A 233 -378.010-195.172 149.401 1.00 66.85 C ANISOU 1860 CB ALA A 233 7601 6920 10880 -2191 -1785 68 C ATOM 1861 N ALA A 234 -379.131-194.829 152.363 1.00 78.22 N ANISOU 1861 N ALA A 234 8655 8362 12702 -2137 -1306 176 N ATOM 1862 CA ALA A 234 -379.274-195.361 153.715 1.00 80.73 C ANISOU 1862 CA ALA A 234 8957 8635 13081 -2168 -1047 198 C ATOM 1863 C ALA A 234 -380.740-195.444 154.124 1.00 87.43 C ANISOU 1863 C ALA A 234 9517 9476 14227 -2294 -1000 219 C ATOM 1864 O ALA A 234 -381.140-196.365 154.847 1.00 84.52 O ANISOU 1864 O ALA A 234 9148 9038 13929 -2412 -854 227 O ATOM 1865 CB ALA A 234 -378.484-194.504 154.705 1.00 72.94 C ANISOU 1865 CB ALA A 234 8020 7704 11989 -2007 -852 227 C ATOM 1866 N ALA A 235 -381.561-194.496 153.660 1.00 90.46 N ANISOU 1866 N ALA A 235 9644 9921 14805 -2273 -1124 235 N ATOM 1867 CA ALA A 235 -382.981-194.512 154.000 1.00 88.38 C ANISOU 1867 CA ALA A 235 9064 9645 14871 -2384 -1082 252 C ATOM 1868 C ALA A 235 -383.676-195.760 153.469 1.00 91.84 C ANISOU 1868 C ALA A 235 9488 10005 15402 -2589 -1212 234 C ATOM 1869 O ALA A 235 -384.685-196.195 154.035 1.00 98.20 O ANISOU 1869 O ALA A 235 10093 10772 16446 -2715 -1100 244 O ATOM 1870 CB ALA A 235 -383.667-193.257 153.463 1.00 79.36 C ANISOU 1870 CB ALA A 235 7643 8566 13944 -2311 -1235 281 C ATOM 1871 N GLN A 236 -383.160-196.345 152.392 1.00 86.91 N ANISOU 1871 N GLN A 236 9075 9352 14596 -2636 -1434 200 N ATOM 1872 CA GLN A 236 -383.713-197.563 151.819 1.00 83.45 C ANISOU 1872 CA GLN A 236 8666 8828 14215 -2838 -1569 166 C ATOM 1873 C GLN A 236 -383.131-198.832 152.434 1.00 82.08 C ANISOU 1873 C GLN A 236 8735 8548 13905 -2904 -1390 139 C ATOM 1874 O GLN A 236 -383.497-199.933 152.009 1.00 78.55 O ANISOU 1874 O GLN A 236 8344 8008 13493 -3075 -1480 102 O ATOM 1875 CB GLN A 236 -383.487-197.578 150.305 1.00 87.83 C ANISOU 1875 CB GLN A 236 9344 9394 14631 -2879 -1897 128 C ATOM 1876 CG GLN A 236 -384.560-196.871 149.494 1.00 95.97 C ANISOU 1876 CG GLN A 236 10099 10483 15881 -2936 -2168 169 C ATOM 1877 CD GLN A 236 -385.827-197.700 149.338 1.00107.31 C ANISOU 1877 CD GLN A 236 11336 11856 17580 -3157 -2272 166 C ATOM 1878 OE1 GLN A 236 -386.252-198.392 150.262 1.00102.48 O ANISOU 1878 OE1 GLN A 236 10646 11181 17110 -3235 -2055 163 O ATOM 1879 NE2 GLN A 236 -386.434-197.633 148.159 1.00121.56 N ANISOU 1879 NE2 GLN A 236 13065 13676 19446 -3273 -2613 172 N ATOM 1880 N GLN A 237 -382.236-198.706 153.412 1.00 77.21 N ANISOU 1880 N GLN A 237 8265 7933 13139 -2780 -1155 162 N ATOM 1881 CA GLN A 237 -381.603-199.852 154.058 1.00 81.76 C ANISOU 1881 CA GLN A 237 9076 8399 13591 -2826 -997 161 C ATOM 1882 C GLN A 237 -381.470-199.610 155.555 1.00 83.32 C ANISOU 1882 C GLN A 237 9254 8613 13791 -2770 -703 225 C ATOM 1883 O GLN A 237 -380.419-199.842 156.153 1.00 84.50 O ANISOU 1883 O GLN A 237 9629 8730 13746 -2688 -583 249 O ATOM 1884 CB GLN A 237 -380.228-200.145 153.462 1.00 93.58 C ANISOU 1884 CB GLN A 237 10883 9857 14816 -2729 -1071 116 C ATOM 1885 CG GLN A 237 -380.231-200.697 152.054 1.00105.73 C ANISOU 1885 CG GLN A 237 12523 11347 16301 -2822 -1318 32 C ATOM 1886 CD GLN A 237 -378.871-201.238 151.664 1.00113.27 C ANISOU 1886 CD GLN A 237 13794 12226 17017 -2746 -1314 -26 C ATOM 1887 OE1 GLN A 237 -378.231-201.946 152.442 1.00112.48 O ANISOU 1887 OE1 GLN A 237 13841 12030 16868 -2721 -1150 -3 O ATOM 1888 NE2 GLN A 237 -378.416-200.898 150.464 1.00116.86 N ANISOU 1888 NE2 GLN A 237 14352 12720 17331 -2713 -1493 -96 N ATOM 1889 N GLN A 238 -382.548-199.149 156.190 1.00 88.87 N ANISOU 1889 N GLN A 238 9686 9362 14720 -2824 -580 254 N ATOM 1890 CA GLN A 238 -382.471-198.842 157.613 1.00 87.80 C ANISOU 1890 CA GLN A 238 9543 9250 14566 -2790 -283 302 C ATOM 1891 C GLN A 238 -382.336-200.086 158.481 1.00 91.22 C ANISOU 1891 C GLN A 238 10150 9572 14939 -2919 -115 346 C ATOM 1892 O GLN A 238 -382.075-199.953 159.682 1.00 96.00 O ANISOU 1892 O GLN A 238 10825 10189 15460 -2903 122 396 O ATOM 1893 CB GLN A 238 -383.689-198.028 158.042 1.00 85.71 C ANISOU 1893 CB GLN A 238 8935 9052 14578 -2821 -168 303 C ATOM 1894 CG GLN A 238 -383.806-196.690 157.338 1.00 94.77 C ANISOU 1894 CG GLN A 238 9902 10298 15807 -2676 -318 280 C ATOM 1895 CD GLN A 238 -384.901-195.827 157.917 1.00111.52 C ANISOU 1895 CD GLN A 238 11684 12467 18222 -2679 -161 278 C ATOM 1896 OE1 GLN A 238 -385.419-196.106 158.994 1.00119.07 O ANISOU 1896 OE1 GLN A 238 12569 13400 19271 -2772 113 285 O ATOM 1897 NE2 GLN A 238 -385.263-194.771 157.202 1.00120.27 N ANISOU 1897 NE2 GLN A 238 12579 13632 19485 -2582 -326 270 N ATOM 1898 N GLU A 239 -382.499-201.282 157.911 1.00 93.03 N ANISOU 1898 N GLU A 239 10461 9685 15200 -3055 -234 330 N ATOM 1899 CA GLU A 239 -382.250-202.512 158.653 1.00 95.76 C ANISOU 1899 CA GLU A 239 11001 9900 15482 -3169 -101 383 C ATOM 1900 C GLU A 239 -380.766-202.757 158.894 1.00 93.95 C ANISOU 1900 C GLU A 239 11088 9623 14984 -3038 -93 414 C ATOM 1901 O GLU A 239 -380.422-203.631 159.695 1.00102.12 O ANISOU 1901 O GLU A 239 12297 10553 15951 -3104 29 485 O ATOM 1902 CB GLU A 239 -382.858-203.712 157.914 1.00 88.83 C ANISOU 1902 CB GLU A 239 10119 8896 14738 -3353 -240 347 C ATOM 1903 CG GLU A 239 -382.203-204.027 156.571 1.00 83.73 C ANISOU 1903 CG GLU A 239 9625 8203 13985 -3306 -502 267 C ATOM 1904 CD GLU A 239 -382.730-203.169 155.429 1.00 88.84 C ANISOU 1904 CD GLU A 239 10079 8959 14717 -3278 -725 200 C ATOM 1905 OE1 GLU A 239 -383.426-202.165 155.690 1.00 97.83 O ANISOU 1905 OE1 GLU A 239 10963 10214 15995 -3242 -682 222 O ATOM 1906 OE2 GLU A 239 -382.456-203.508 154.260 1.00 82.48 O ANISOU 1906 OE2 GLU A 239 9382 8115 13842 -3298 -944 126 O ATOM 1907 N SER A 240 -379.886-202.004 158.242 1.00 89.32 N ANISOU 1907 N SER A 240 10572 9108 14257 -2859 -220 373 N ATOM 1908 CA SER A 240 -378.446-202.207 158.339 1.00 91.91 C ANISOU 1908 CA SER A 240 11171 9388 14363 -2726 -232 394 C ATOM 1909 C SER A 240 -377.858-201.159 159.279 1.00 93.63 C ANISOU 1909 C SER A 240 11407 9717 14453 -2586 -93 448 C ATOM 1910 O SER A 240 -377.814-199.972 158.942 1.00 97.45 O ANISOU 1910 O SER A 240 11777 10326 14923 -2467 -136 410 O ATOM 1911 CB SER A 240 -377.802-202.130 156.958 1.00 90.29 C ANISOU 1911 CB SER A 240 11047 9178 14082 -2637 -452 303 C ATOM 1912 OG SER A 240 -376.391-202.131 157.052 1.00 94.01 O ANISOU 1912 OG SER A 240 11737 9618 14366 -2487 -447 316 O ATOM 1913 N ALA A 241 -377.402-201.601 160.455 1.00 95.48 N ANISOU 1913 N ALA A 241 11794 9897 14587 -2609 65 541 N ATOM 1914 CA ALA A 241 -376.830-200.677 161.429 1.00 92.40 C ANISOU 1914 CA ALA A 241 11449 9605 14052 -2503 196 593 C ATOM 1915 C ALA A 241 -375.514-200.081 160.944 1.00101.80 C ANISOU 1915 C ALA A 241 12763 10835 15083 -2304 75 571 C ATOM 1916 O ALA A 241 -375.195-198.931 161.276 1.00 97.56 O ANISOU 1916 O ALA A 241 12187 10417 14466 -2191 123 567 O ATOM 1917 CB ALA A 241 -376.624-201.382 162.769 1.00 84.43 C ANISOU 1917 CB ALA A 241 10607 8521 12950 -2601 363 711 C ATOM 1918 N THR A 242 -374.735-200.839 160.169 1.00 95.52 N ANISOU 1918 N THR A 242 12113 9933 14249 -2262 -69 550 N ATOM 1919 CA THR A 242 -373.477-200.309 159.656 1.00 86.96 C ANISOU 1919 CA THR A 242 11131 8878 13031 -2080 -168 521 C ATOM 1920 C THR A 242 -373.720-199.290 158.550 1.00 89.63 C ANISOU 1920 C THR A 242 11326 9334 13397 -2003 -283 422 C ATOM 1921 O THR A 242 -373.002-198.287 158.456 1.00 95.47 O ANISOU 1921 O THR A 242 12073 10165 14035 -1858 -303 411 O ATOM 1922 CB THR A 242 -372.587-201.442 159.148 1.00 85.04 C ANISOU 1922 CB THR A 242 11076 8472 12765 -2061 -259 514 C ATOM 1923 OG1 THR A 242 -373.171-202.017 157.974 1.00 81.94 O ANISOU 1923 OG1 THR A 242 10639 8019 12477 -2144 -371 414 O ATOM 1924 CG2 THR A 242 -372.427-202.516 160.214 1.00 84.63 C ANISOU 1924 CG2 THR A 242 11161 8280 12713 -2150 -170 633 C ATOM 1925 N THR A 243 -374.717-199.536 157.695 1.00 87.76 N ANISOU 1925 N THR A 243 10960 9089 13296 -2107 -373 357 N ATOM 1926 CA THR A 243 -375.084-198.549 156.684 1.00 82.60 C ANISOU 1926 CA THR A 243 10161 8546 12677 -2055 -503 287 C ATOM 1927 C THR A 243 -375.441-197.216 157.330 1.00 79.59 C ANISOU 1927 C THR A 243 9616 8301 12325 -1982 -407 316 C ATOM 1928 O THR A 243 -375.057-196.151 156.831 1.00 74.88 O ANISOU 1928 O THR A 243 8981 7795 11674 -1858 -480 290 O ATOM 1929 CB THR A 243 -376.250-199.064 155.838 1.00 80.83 C ANISOU 1929 CB THR A 243 9809 8290 12615 -2209 -622 235 C ATOM 1930 OG1 THR A 243 -375.872-200.284 155.189 1.00 83.46 O ANISOU 1930 OG1 THR A 243 10314 8486 12912 -2278 -706 188 O ATOM 1931 CG2 THR A 243 -376.647-198.040 154.782 1.00 76.13 C ANISOU 1931 CG2 THR A 243 9067 7803 12055 -2165 -790 186 C ATOM 1932 N GLN A 244 -376.155-197.257 158.457 1.00 82.73 N ANISOU 1932 N GLN A 244 9923 8704 12805 -2065 -229 365 N ATOM 1933 CA GLN A 244 -376.513-196.024 159.148 1.00 83.90 C ANISOU 1933 CA GLN A 244 9922 8966 12991 -2004 -101 374 C ATOM 1934 C GLN A 244 -375.292-195.382 159.799 1.00 86.11 C ANISOU 1934 C GLN A 244 10360 9290 13067 -1864 -32 404 C ATOM 1935 O GLN A 244 -375.160-194.153 159.803 1.00 90.43 O ANISOU 1935 O GLN A 244 10825 9933 13603 -1753 -20 382 O ATOM 1936 CB GLN A 244 -377.603-196.302 160.183 1.00 78.02 C ANISOU 1936 CB GLN A 244 9052 8208 12385 -2149 102 403 C ATOM 1937 CG GLN A 244 -378.832-197.002 159.616 1.00 76.43 C ANISOU 1937 CG GLN A 244 8678 7954 12408 -2305 38 380 C ATOM 1938 CD GLN A 244 -379.397-196.305 158.392 1.00 81.17 C ANISOU 1938 CD GLN A 244 9075 8610 13155 -2264 -164 323 C ATOM 1939 OE1 GLN A 244 -379.736-195.122 158.438 1.00 88.31 O ANISOU 1939 OE1 GLN A 244 9802 9602 14149 -2179 -138 309 O ATOM 1940 NE2 GLN A 244 -379.500-197.038 157.289 1.00 77.75 N ANISOU 1940 NE2 GLN A 244 8676 8119 12747 -2330 -373 294 N ATOM 1941 N LYS A 245 -374.388-196.195 160.355 1.00 87.95 N ANISOU 1941 N LYS A 245 10816 9446 13154 -1869 3 461 N ATOM 1942 CA LYS A 245 -373.140-195.652 160.884 1.00 89.63 C ANISOU 1942 CA LYS A 245 11181 9694 13181 -1739 28 495 C ATOM 1943 C LYS A 245 -372.304-195.020 159.779 1.00 83.90 C ANISOU 1943 C LYS A 245 10474 9007 12397 -1589 -135 441 C ATOM 1944 O LYS A 245 -371.730-193.939 159.966 1.00 79.57 O ANISOU 1944 O LYS A 245 9923 8543 11767 -1472 -119 437 O ATOM 1945 CB LYS A 245 -372.340-196.744 161.596 1.00 91.66 C ANISOU 1945 CB LYS A 245 11661 9842 13325 -1777 57 582 C ATOM 1946 CG LYS A 245 -372.620-196.851 163.085 1.00105.13 C ANISOU 1946 CG LYS A 245 13423 11552 14968 -1878 246 666 C ATOM 1947 CD LYS A 245 -371.917-198.059 163.687 1.00115.08 C ANISOU 1947 CD LYS A 245 14903 12682 16141 -1933 235 775 C ATOM 1948 CE LYS A 245 -372.559-198.472 165.003 1.00118.93 C ANISOU 1948 CE LYS A 245 15444 13152 16593 -2102 419 862 C ATOM 1949 NZ LYS A 245 -372.079-199.803 165.462 1.00118.82 N ANISOU 1949 NZ LYS A 245 15627 12983 16534 -2181 384 983 N ATOM 1950 N ALA A 246 -372.231-195.675 158.617 1.00 70.88 N ANISOU 1950 N ALA A 246 8853 7294 10783 -1602 -283 395 N ATOM 1951 CA ALA A 246 -371.465-195.121 157.506 1.00 67.91 C ANISOU 1951 CA ALA A 246 8511 6954 10337 -1482 -423 338 C ATOM 1952 C ALA A 246 -372.067-193.809 157.020 1.00 81.68 C ANISOU 1952 C ALA A 246 10075 8818 12142 -1434 -471 304 C ATOM 1953 O ALA A 246 -371.337-192.855 156.723 1.00 91.53 O ANISOU 1953 O ALA A 246 11342 10131 13303 -1310 -510 292 O ATOM 1954 CB ALA A 246 -371.390-196.132 156.363 1.00 59.24 C ANISOU 1954 CB ALA A 246 7491 5759 9257 -1538 -551 280 C ATOM 1955 N GLU A 247 -373.397-193.741 156.929 1.00 84.04 N ANISOU 1955 N GLU A 247 10187 9137 12609 -1533 -472 293 N ATOM 1956 CA GLU A 247 -374.047-192.493 156.543 1.00 78.75 C ANISOU 1956 CA GLU A 247 9319 8561 12041 -1484 -522 276 C ATOM 1957 C GLU A 247 -373.723-191.381 157.533 1.00 75.40 C ANISOU 1957 C GLU A 247 8864 8207 11578 -1383 -374 297 C ATOM 1958 O GLU A 247 -373.437-190.244 157.136 1.00 70.97 O ANISOU 1958 O GLU A 247 8252 7712 11002 -1273 -431 284 O ATOM 1959 CB GLU A 247 -375.559-192.700 156.434 1.00 80.04 C ANISOU 1959 CB GLU A 247 9262 8716 12434 -1613 -535 270 C ATOM 1960 CG GLU A 247 -376.341-191.454 156.034 1.00 87.06 C ANISOU 1960 CG GLU A 247 9912 9680 13486 -1564 -602 263 C ATOM 1961 CD GLU A 247 -376.737-190.600 157.224 1.00 96.73 C ANISOU 1961 CD GLU A 247 10999 10946 14806 -1523 -385 273 C ATOM 1962 OE1 GLU A 247 -377.206-191.168 158.234 1.00104.25 O ANISOU 1962 OE1 GLU A 247 11932 11868 15811 -1618 -196 282 O ATOM 1963 OE2 GLU A 247 -376.567-189.365 157.152 1.00 96.66 O ANISOU 1963 OE2 GLU A 247 10915 10995 14816 -1405 -393 268 O ATOM 1964 N LYS A 248 -373.760-191.694 158.832 1.00 70.98 N ANISOU 1964 N LYS A 248 8348 7629 10992 -1431 -182 329 N ATOM 1965 CA LYS A 248 -373.498-190.680 159.848 1.00 72.30 C ANISOU 1965 CA LYS A 248 8506 7860 11106 -1361 -26 336 C ATOM 1966 C LYS A 248 -372.080-190.132 159.736 1.00 78.40 C ANISOU 1966 C LYS A 248 9438 8661 11688 -1224 -85 344 C ATOM 1967 O LYS A 248 -371.864-188.920 159.859 1.00 73.85 O ANISOU 1967 O LYS A 248 8809 8151 11102 -1128 -59 324 O ATOM 1968 CB LYS A 248 -373.739-191.257 161.243 1.00 77.25 C ANISOU 1968 CB LYS A 248 9199 8459 11694 -1468 184 374 C ATOM 1969 CG LYS A 248 -375.176-191.160 161.718 1.00 95.94 C ANISOU 1969 CG LYS A 248 11356 10833 14263 -1579 337 350 C ATOM 1970 CD LYS A 248 -375.273-191.366 163.223 1.00109.27 C ANISOU 1970 CD LYS A 248 13135 12519 15864 -1674 586 379 C ATOM 1971 CE LYS A 248 -376.667-191.032 163.744 1.00117.06 C ANISOU 1971 CE LYS A 248 13892 13521 17064 -1770 786 333 C ATOM 1972 NZ LYS A 248 -376.734-191.106 165.233 1.00123.34 N ANISOU 1972 NZ LYS A 248 14798 14325 17740 -1874 1058 348 N ATOM 1973 N GLU A 249 -371.098-191.003 159.496 1.00 84.54 N ANISOU 1973 N GLU A 249 10403 9381 12339 -1211 -162 369 N ATOM 1974 CA GLU A 249 -369.718-190.537 159.474 1.00 92.11 C ANISOU 1974 CA GLU A 249 11497 10359 13141 -1087 -204 380 C ATOM 1975 C GLU A 249 -369.379-189.813 158.177 1.00 85.89 C ANISOU 1975 C GLU A 249 10668 9611 12355 -991 -352 334 C ATOM 1976 O GLU A 249 -368.576-188.873 158.194 1.00 84.69 O ANISOU 1976 O GLU A 249 10546 9511 12123 -884 -360 332 O ATOM 1977 CB GLU A 249 -368.753-191.700 159.722 1.00102.53 C ANISOU 1977 CB GLU A 249 13010 11587 14358 -1099 -225 428 C ATOM 1978 CG GLU A 249 -368.742-192.783 158.661 1.00123.30 C ANISOU 1978 CG GLU A 249 15684 14128 17034 -1136 -339 399 C ATOM 1979 CD GLU A 249 -367.951-194.006 159.098 1.00142.46 C ANISOU 1979 CD GLU A 249 18282 16437 19411 -1156 -331 452 C ATOM 1980 OE1 GLU A 249 -367.888-194.268 160.318 1.00145.69 O ANISOU 1980 OE1 GLU A 249 18752 16825 19777 -1201 -237 532 O ATOM 1981 OE2 GLU A 249 -367.393-194.704 158.224 1.00149.14 O ANISOU 1981 OE2 GLU A 249 19203 17200 20261 -1133 -419 416 O ATOM 1982 N VAL A 250 -369.981-190.214 157.055 1.00 76.30 N ANISOU 1982 N VAL A 250 9394 8375 11222 -1041 -474 300 N ATOM 1983 CA VAL A 250 -369.787-189.472 155.810 1.00 72.68 C ANISOU 1983 CA VAL A 250 8905 7961 10751 -975 -620 267 C ATOM 1984 C VAL A 250 -370.318-188.053 155.960 1.00 74.23 C ANISOU 1984 C VAL A 250 8936 8236 11031 -916 -603 272 C ATOM 1985 O VAL A 250 -369.664-187.079 155.569 1.00 78.63 O ANISOU 1985 O VAL A 250 9511 8839 11525 -816 -651 270 O ATOM 1986 CB VAL A 250 -370.457-190.203 154.633 1.00 71.05 C ANISOU 1986 CB VAL A 250 8675 7716 10603 -1072 -764 232 C ATOM 1987 CG1 VAL A 250 -370.515-189.296 153.411 1.00 67.98 C ANISOU 1987 CG1 VAL A 250 8239 7386 10204 -1032 -923 215 C ATOM 1988 CG2 VAL A 250 -369.709-191.481 154.311 1.00 63.12 C ANISOU 1988 CG2 VAL A 250 7856 6619 9506 -1106 -780 206 C ATOM 1989 N THR A 251 -371.513-187.917 156.540 1.00 73.21 N ANISOU 1989 N THR A 251 8637 8113 11065 -980 -524 276 N ATOM 1990 CA THR A 251 -372.075-186.595 156.791 1.00 72.97 C ANISOU 1990 CA THR A 251 8433 8135 11158 -920 -480 273 C ATOM 1991 C THR A 251 -371.180-185.790 157.723 1.00 74.40 C ANISOU 1991 C THR A 251 8698 8349 11222 -827 -348 272 C ATOM 1992 O THR A 251 -370.884-184.618 157.462 1.00 81.22 O ANISOU 1992 O THR A 251 9520 9249 12091 -730 -382 266 O ATOM 1993 CB THR A 251 -373.478-186.730 157.381 1.00 66.11 C ANISOU 1993 CB THR A 251 7364 7251 10504 -1011 -374 266 C ATOM 1994 OG1 THR A 251 -374.289-187.524 156.510 1.00 72.69 O ANISOU 1994 OG1 THR A 251 8119 8051 11450 -1111 -516 270 O ATOM 1995 CG2 THR A 251 -374.121-185.365 157.555 1.00 62.32 C ANISOU 1995 CG2 THR A 251 6676 6802 10199 -942 -326 252 C ATOM 1996 N ARG A 252 -370.740-186.410 158.822 1.00 66.02 N ANISOU 1996 N ARG A 252 7764 7269 10053 -866 -208 285 N ATOM 1997 CA ARG A 252 -369.887-185.718 159.782 1.00 70.24 C ANISOU 1997 CA ARG A 252 8395 7834 10458 -802 -96 287 C ATOM 1998 C ARG A 252 -368.590-185.246 159.133 1.00 70.12 C ANISOU 1998 C ARG A 252 8491 7838 10313 -691 -216 293 C ATOM 1999 O ARG A 252 -368.094-184.156 159.442 1.00 64.76 O ANISOU 1999 O ARG A 252 7815 7198 9593 -613 -180 281 O ATOM 2000 CB ARG A 252 -369.599-186.633 160.972 1.00 78.43 C ANISOU 2000 CB ARG A 252 9578 8842 11381 -885 30 321 C ATOM 2001 CG ARG A 252 -368.811-185.983 162.098 1.00101.29 C ANISOU 2001 CG ARG A 252 12586 11771 14129 -853 140 328 C ATOM 2002 CD ARG A 252 -368.607-186.960 163.248 1.00129.50 C ANISOU 2002 CD ARG A 252 16314 15310 17578 -959 238 384 C ATOM 2003 NE ARG A 252 -367.733-188.072 162.879 1.00151.76 N ANISOU 2003 NE ARG A 252 19274 18068 20319 -954 109 446 N ATOM 2004 CZ ARG A 252 -367.609-189.194 163.583 1.00166.23 C ANISOU 2004 CZ ARG A 252 21234 19839 22084 -1047 141 516 C ATOM 2005 NH1 ARG A 252 -366.788-190.150 163.170 1.00169.46 N ANISOU 2005 NH1 ARG A 252 21753 20174 22461 -1023 19 567 N ATOM 2006 NH2 ARG A 252 -368.312-189.366 164.694 1.00171.80 N ANISOU 2006 NH2 ARG A 252 21961 20551 22765 -1169 303 535 N ATOM 2007 N MET A 253 -368.035-186.044 158.218 1.00 65.58 N ANISOU 2007 N MET A 253 8009 7231 9680 -689 -345 304 N ATOM 2008 CA MET A 253 -366.800-185.642 157.554 1.00 64.36 C ANISOU 2008 CA MET A 253 7951 7089 9412 -593 -436 303 C ATOM 2009 C MET A 253 -367.046-184.532 156.540 1.00 73.16 C ANISOU 2009 C MET A 253 8966 8248 10585 -535 -536 285 C ATOM 2010 O MET A 253 -366.235-183.606 156.420 1.00 77.78 O ANISOU 2010 O MET A 253 9584 8865 11106 -448 -550 286 O ATOM 2011 CB MET A 253 -366.144-186.846 156.881 1.00 59.19 C ANISOU 2011 CB MET A 253 7424 6373 8691 -613 -514 303 C ATOM 2012 CG MET A 253 -365.190-187.607 157.786 1.00 80.74 C ANISOU 2012 CG MET A 253 10293 9053 11331 -608 -452 341 C ATOM 2013 SD MET A 253 -363.932-186.557 158.560 1.00 98.54 S ANISOU 2013 SD MET A 253 12607 11356 13478 -506 -413 366 S ATOM 2014 CE MET A 253 -363.069-185.897 157.137 1.00 86.32 C ANISOU 2014 CE MET A 253 11066 9831 11901 -408 -520 327 C ATOM 2015 N VAL A 254 -368.149-184.612 155.792 1.00 67.63 N ANISOU 2015 N VAL A 254 8144 7544 10009 -588 -620 279 N ATOM 2016 CA VAL A 254 -368.458-183.557 154.833 1.00 65.21 C ANISOU 2016 CA VAL A 254 7740 7269 9766 -543 -741 286 C ATOM 2017 C VAL A 254 -368.633-182.228 155.553 1.00 68.21 C ANISOU 2017 C VAL A 254 8012 7676 10230 -469 -651 288 C ATOM 2018 O VAL A 254 -368.133-181.188 155.105 1.00 65.49 O ANISOU 2018 O VAL A 254 7670 7353 9861 -390 -708 299 O ATOM 2019 CB VAL A 254 -369.706-183.926 154.011 1.00 63.84 C ANISOU 2019 CB VAL A 254 7442 7082 9733 -629 -868 293 C ATOM 2020 CG1 VAL A 254 -370.221-182.711 153.244 1.00 72.34 C ANISOU 2020 CG1 VAL A 254 8383 8183 10919 -585 -997 324 C ATOM 2021 CG2 VAL A 254 -369.385-185.055 153.056 1.00 59.84 C ANISOU 2021 CG2 VAL A 254 7072 6547 9116 -700 -978 275 C ATOM 2022 N ILE A 255 -369.338-182.245 156.685 1.00 63.54 N ANISOU 2022 N ILE A 255 7331 7075 9736 -502 -496 270 N ATOM 2023 CA ILE A 255 -369.515-181.030 157.471 1.00 66.01 C ANISOU 2023 CA ILE A 255 7552 7400 10129 -441 -374 248 C ATOM 2024 C ILE A 255 -368.162-180.462 157.880 1.00 69.12 C ANISOU 2024 C ILE A 255 8099 7816 10346 -368 -335 243 C ATOM 2025 O ILE A 255 -367.903-179.263 157.732 1.00 71.34 O ANISOU 2025 O ILE A 255 8342 8107 10658 -288 -349 237 O ATOM 2026 CB ILE A 255 -370.406-181.310 158.693 1.00 65.39 C ANISOU 2026 CB ILE A 255 7390 7307 10150 -513 -175 214 C ATOM 2027 CG1 ILE A 255 -371.827-181.647 158.247 1.00 69.49 C ANISOU 2027 CG1 ILE A 255 7704 7800 10899 -578 -216 218 C ATOM 2028 CG2 ILE A 255 -370.413-180.119 159.631 1.00 62.91 C ANISOU 2028 CG2 ILE A 255 7027 6998 9877 -460 -12 167 C ATOM 2029 CD1 ILE A 255 -372.778-181.907 159.399 1.00 70.14 C ANISOU 2029 CD1 ILE A 255 7684 7865 11103 -659 5 178 C ATOM 2030 N ILE A 256 -367.273-181.322 158.384 1.00 66.57 N ANISOU 2030 N ILE A 256 7947 7495 9854 -395 -298 252 N ATOM 2031 CA ILE A 256 -365.954-180.874 158.826 1.00 61.25 C ANISOU 2031 CA ILE A 256 7408 6839 9025 -335 -276 256 C ATOM 2032 C ILE A 256 -365.187-180.241 157.669 1.00 64.06 C ANISOU 2032 C ILE A 256 7785 7207 9346 -255 -412 269 C ATOM 2033 O ILE A 256 -364.582-179.172 157.812 1.00 64.16 O ANISOU 2033 O ILE A 256 7808 7236 9332 -189 -399 262 O ATOM 2034 CB ILE A 256 -365.169-182.045 159.448 1.00 61.71 C ANISOU 2034 CB ILE A 256 7626 6879 8940 -380 -250 283 C ATOM 2035 CG1 ILE A 256 -365.728-182.391 160.829 1.00 56.51 C ANISOU 2035 CG1 ILE A 256 6985 6217 8271 -466 -93 280 C ATOM 2036 CG2 ILE A 256 -363.680-181.717 159.537 1.00 57.43 C ANISOU 2036 CG2 ILE A 256 7208 6349 8265 -313 -289 300 C ATOM 2037 CD1 ILE A 256 -365.099-183.623 161.446 1.00 55.91 C ANISOU 2037 CD1 ILE A 256 7064 6108 8071 -524 -89 332 C ATOM 2038 N MET A 257 -365.207-180.888 156.501 1.00 61.77 N ANISOU 2038 N MET A 257 7515 6907 9049 -273 -538 284 N ATOM 2039 CA MET A 257 -364.498-180.343 155.348 1.00 67.00 C ANISOU 2039 CA MET A 257 8218 7583 9655 -219 -654 296 C ATOM 2040 C MET A 257 -365.067-178.993 154.933 1.00 76.01 C ANISOU 2040 C MET A 257 9237 8736 10906 -175 -704 310 C ATOM 2041 O MET A 257 -364.316-178.052 154.649 1.00 78.31 O ANISOU 2041 O MET A 257 9562 9040 11152 -112 -728 321 O ATOM 2042 CB MET A 257 -364.560-181.328 154.184 1.00 59.23 C ANISOU 2042 CB MET A 257 7291 6582 8631 -273 -765 296 C ATOM 2043 CG MET A 257 -363.722-182.561 154.396 1.00 65.96 C ANISOU 2043 CG MET A 257 8277 7401 9383 -294 -726 281 C ATOM 2044 SD MET A 257 -363.993-183.809 153.130 1.00 87.95 S ANISOU 2044 SD MET A 257 11129 10146 12141 -376 -826 253 S ATOM 2045 CE MET A 257 -362.910-185.096 153.745 1.00 96.59 C ANISOU 2045 CE MET A 257 12357 11173 13169 -370 -740 238 C ATOM 2046 N VAL A 258 -366.396-178.877 154.905 1.00 71.88 N ANISOU 2046 N VAL A 258 8561 8200 10550 -207 -720 314 N ATOM 2047 CA VAL A 258 -367.025-177.646 154.443 1.00 63.88 C ANISOU 2047 CA VAL A 258 7410 7177 9686 -160 -790 341 C ATOM 2048 C VAL A 258 -366.849-176.535 155.471 1.00 67.07 C ANISOU 2048 C VAL A 258 7767 7569 10146 -93 -650 310 C ATOM 2049 O VAL A 258 -366.653-175.367 155.113 1.00 70.29 O ANISOU 2049 O VAL A 258 8140 7963 10604 -27 -697 331 O ATOM 2050 CB VAL A 258 -368.504-177.908 154.114 1.00 64.80 C ANISOU 2050 CB VAL A 258 7350 7269 10000 -215 -859 358 C ATOM 2051 CG1 VAL A 258 -369.230-176.606 153.838 1.00 68.30 C ANISOU 2051 CG1 VAL A 258 7617 7681 10652 -155 -921 392 C ATOM 2052 CG2 VAL A 258 -368.605-178.836 152.915 1.00 60.22 C ANISOU 2052 CG2 VAL A 258 6837 6699 9344 -291 -1032 387 C ATOM 2053 N ILE A 259 -366.911-176.874 156.759 1.00 69.49 N ANISOU 2053 N ILE A 259 8088 7876 10438 -119 -477 260 N ATOM 2054 CA ILE A 259 -366.621-175.882 157.791 1.00 74.43 C ANISOU 2054 CA ILE A 259 8713 8493 11073 -75 -332 213 C ATOM 2055 C ILE A 259 -365.167-175.435 157.698 1.00 71.82 C ANISOU 2055 C ILE A 259 8533 8185 10571 -26 -367 223 C ATOM 2056 O ILE A 259 -364.854-174.247 157.845 1.00 63.66 O ANISOU 2056 O ILE A 259 7481 7134 9572 32 -343 208 O ATOM 2057 CB ILE A 259 -366.949-176.439 159.189 1.00 75.95 C ANISOU 2057 CB ILE A 259 8929 8690 11240 -142 -139 159 C ATOM 2058 CG1 ILE A 259 -368.441-176.752 159.315 1.00 81.60 C ANISOU 2058 CG1 ILE A 259 9467 9378 12160 -192 -76 140 C ATOM 2059 CG2 ILE A 259 -366.512-175.454 160.266 1.00 72.22 C ANISOU 2059 CG2 ILE A 259 8500 8212 10727 -117 9 98 C ATOM 2060 CD1 ILE A 259 -369.338-175.610 158.900 1.00 91.65 C ANISOU 2060 CD1 ILE A 259 10531 10604 13689 -129 -95 131 C ATOM 2061 N ALA A 260 -364.255-176.381 157.449 1.00 63.74 N ANISOU 2061 N ALA A 260 7650 7188 9382 -50 -420 247 N ATOM 2062 CA ALA A 260 -362.846-176.025 157.313 1.00 61.65 C ANISOU 2062 CA ALA A 260 7505 6940 8981 -6 -453 259 C ATOM 2063 C ALA A 260 -362.628-175.089 156.134 1.00 69.54 C ANISOU 2063 C ALA A 260 8474 7933 10014 47 -566 292 C ATOM 2064 O ALA A 260 -361.859-174.127 156.231 1.00 74.74 O ANISOU 2064 O ALA A 260 9163 8589 10645 93 -556 290 O ATOM 2065 CB ALA A 260 -361.991-177.281 157.160 1.00 56.26 C ANISOU 2065 CB ALA A 260 6948 6267 8162 -35 -487 277 C ATOM 2066 N PHE A 261 -363.300-175.353 155.011 1.00 67.48 N ANISOU 2066 N PHE A 261 8163 7668 9810 28 -684 328 N ATOM 2067 CA PHE A 261 -363.175-174.472 153.856 1.00 63.82 C ANISOU 2067 CA PHE A 261 7687 7198 9365 59 -807 378 C ATOM 2068 C PHE A 261 -363.745-173.090 154.154 1.00 66.13 C ANISOU 2068 C PHE A 261 7854 7448 9823 114 -789 384 C ATOM 2069 O PHE A 261 -363.140-172.073 153.800 1.00 61.94 O ANISOU 2069 O PHE A 261 7350 6902 9281 159 -823 411 O ATOM 2070 CB PHE A 261 -363.873-175.093 152.649 1.00 61.60 C ANISOU 2070 CB PHE A 261 7390 6920 9094 4 -953 419 C ATOM 2071 CG PHE A 261 -363.642-174.349 151.368 1.00 66.03 C ANISOU 2071 CG PHE A 261 7987 7481 9621 9 -1097 484 C ATOM 2072 CD1 PHE A 261 -362.529-174.622 150.589 1.00 69.67 C ANISOU 2072 CD1 PHE A 261 8603 7969 9898 -11 -1122 487 C ATOM 2073 CD2 PHE A 261 -364.536-173.380 150.941 1.00 65.91 C ANISOU 2073 CD2 PHE A 261 7846 7430 9765 29 -1202 546 C ATOM 2074 CE1 PHE A 261 -362.310-173.942 149.404 1.00 74.23 C ANISOU 2074 CE1 PHE A 261 9236 8549 10418 -27 -1241 550 C ATOM 2075 CE2 PHE A 261 -364.323-172.697 149.759 1.00 69.08 C ANISOU 2075 CE2 PHE A 261 8299 7828 10120 20 -1350 625 C ATOM 2076 CZ PHE A 261 -363.209-172.979 148.987 1.00 71.86 C ANISOU 2076 CZ PHE A 261 8831 8218 10254 -16 -1366 627 C ATOM 2077 N LEU A 262 -364.903-173.035 154.816 1.00 69.87 N ANISOU 2077 N LEU A 262 8188 7893 10468 111 -722 356 N ATOM 2078 CA LEU A 262 -365.532-171.751 155.107 1.00 67.66 C ANISOU 2078 CA LEU A 262 7768 7550 10388 170 -687 349 C ATOM 2079 C LEU A 262 -364.682-170.921 156.059 1.00 68.45 C ANISOU 2079 C LEU A 262 7936 7639 10435 209 -551 290 C ATOM 2080 O LEU A 262 -364.643-169.688 155.958 1.00 70.37 O ANISOU 2080 O LEU A 262 8128 7825 10783 267 -559 298 O ATOM 2081 CB LEU A 262 -366.926-171.965 155.688 1.00 66.64 C ANISOU 2081 CB LEU A 262 7464 7388 10470 152 -607 313 C ATOM 2082 CG LEU A 262 -368.040-172.368 154.719 1.00 71.59 C ANISOU 2082 CG LEU A 262 7956 8000 11245 122 -768 380 C ATOM 2083 CD1 LEU A 262 -369.331-172.663 155.467 1.00 65.01 C ANISOU 2083 CD1 LEU A 262 6938 7133 10628 98 -651 331 C ATOM 2084 CD2 LEU A 262 -368.263-171.275 153.684 1.00 68.61 C ANISOU 2084 CD2 LEU A 262 7500 7571 10998 176 -945 470 C ATOM 2085 N ILE A 263 -364.007-171.580 157.006 1.00 66.03 N ANISOU 2085 N ILE A 263 7744 7375 9968 172 -437 236 N ATOM 2086 CA ILE A 263 -363.141-170.864 157.941 1.00 67.63 C ANISOU 2086 CA ILE A 263 8029 7573 10095 188 -329 180 C ATOM 2087 C ILE A 263 -362.021-170.148 157.196 1.00 66.11 C ANISOU 2087 C ILE A 263 7911 7380 9828 228 -428 226 C ATOM 2088 O ILE A 263 -361.598-169.055 157.590 1.00 70.56 O ANISOU 2088 O ILE A 263 8483 7907 10420 260 -381 196 O ATOM 2089 CB ILE A 263 -362.603-171.840 159.007 1.00 70.26 C ANISOU 2089 CB ILE A 263 8484 7955 10255 125 -233 141 C ATOM 2090 CG1 ILE A 263 -363.671-172.109 160.066 1.00 71.48 C ANISOU 2090 CG1 ILE A 263 8577 8096 10486 76 -75 75 C ATOM 2091 CG2 ILE A 263 -361.338-171.309 159.659 1.00 61.04 C ANISOU 2091 CG2 ILE A 263 7440 6800 8953 127 -200 115 C ATOM 2092 CD1 ILE A 263 -363.241-173.126 161.112 1.00 73.31 C ANISOU 2092 CD1 ILE A 263 8943 8371 10538 -5 6 57 C ATOM 2093 N CYS A 264 -361.561-170.718 156.086 1.00 58.14 N ANISOU 2093 N CYS A 264 6956 6404 8729 220 -557 294 N ATOM 2094 CA CYS A 264 -360.524-170.072 155.293 1.00 62.47 C ANISOU 2094 CA CYS A 264 7575 6953 9206 244 -635 339 C ATOM 2095 C CYS A 264 -361.103-169.090 154.274 1.00 70.28 C ANISOU 2095 C CYS A 264 8486 7891 10325 276 -744 407 C ATOM 2096 O CYS A 264 -360.455-168.091 153.946 1.00 81.76 O ANISOU 2096 O CYS A 264 9971 9317 11778 303 -770 435 O ATOM 2097 CB CYS A 264 -359.672-171.130 154.596 1.00 61.72 C ANISOU 2097 CB CYS A 264 7590 6912 8949 211 -692 367 C ATOM 2098 SG CYS A 264 -358.391-170.475 153.534 1.00 74.70 S ANISOU 2098 SG CYS A 264 9322 8562 10501 222 -757 416 S ATOM 2099 N TRP A 265 -362.325-169.336 153.800 1.00 70.77 N ANISOU 2099 N TRP A 265 8443 7935 10512 269 -817 441 N ATOM 2100 CA TRP A 265 -362.945-168.585 152.715 1.00 66.33 C ANISOU 2100 CA TRP A 265 7808 7324 10071 287 -969 533 C ATOM 2101 C TRP A 265 -363.644-167.313 153.189 1.00 73.93 C ANISOU 2101 C TRP A 265 8626 8188 11275 354 -932 527 C ATOM 2102 O TRP A 265 -363.516-166.263 152.547 1.00 76.47 O ANISOU 2102 O TRP A 265 8937 8451 11668 387 -1024 600 O ATOM 2103 CB TRP A 265 -363.947-169.493 151.993 1.00 57.67 C ANISOU 2103 CB TRP A 265 6655 6248 9009 238 -1089 578 C ATOM 2104 CG TRP A 265 -364.540-168.942 150.742 1.00 60.40 C ANISOU 2104 CG TRP A 265 6953 6557 9439 230 -1292 694 C ATOM 2105 CD1 TRP A 265 -364.085-169.127 149.468 1.00 66.48 C ANISOU 2105 CD1 TRP A 265 7853 7364 10044 172 -1441 773 C ATOM 2106 CD2 TRP A 265 -365.720-168.140 150.635 1.00 57.02 C ANISOU 2106 CD2 TRP A 265 6339 6044 9284 272 -1378 751 C ATOM 2107 NE1 TRP A 265 -364.904-168.481 148.575 1.00 66.68 N ANISOU 2107 NE1 TRP A 265 7800 7337 10198 165 -1635 889 N ATOM 2108 CE2 TRP A 265 -365.917-167.869 149.266 1.00 60.90 C ANISOU 2108 CE2 TRP A 265 6860 6524 9754 234 -1609 884 C ATOM 2109 CE3 TRP A 265 -366.627-167.620 151.564 1.00 62.35 C ANISOU 2109 CE3 TRP A 265 6820 6642 10227 335 -1276 701 C ATOM 2110 CZ2 TRP A 265 -366.980-167.097 148.803 1.00 58.03 C ANISOU 2110 CZ2 TRP A 265 6331 6073 9644 264 -1771 986 C ATOM 2111 CZ3 TRP A 265 -367.685-166.854 151.103 1.00 65.39 C ANISOU 2111 CZ3 TRP A 265 7023 6932 10888 375 -1409 786 C ATOM 2112 CH2 TRP A 265 -367.852-166.601 149.733 1.00 61.84 C ANISOU 2112 CH2 TRP A 265 6599 6471 10426 343 -1670 937 C ATOM 2113 N LEU A 266 -364.370-167.385 154.304 1.00 68.06 N ANISOU 2113 N LEU A 266 7776 7417 10664 370 -787 439 N ATOM 2114 CA LEU A 266 -365.160-166.241 154.757 1.00 69.83 C ANISOU 2114 CA LEU A 266 7843 7531 11156 435 -727 413 C ATOM 2115 C LEU A 266 -364.342-165.003 155.116 1.00 81.07 C ANISOU 2115 C LEU A 266 9323 8894 12584 480 -662 383 C ATOM 2116 O LEU A 266 -364.811-163.891 154.814 1.00 74.90 O ANISOU 2116 O LEU A 266 8434 8002 12021 540 -709 424 O ATOM 2117 CB LEU A 266 -366.037-166.669 155.941 1.00 70.04 C ANISOU 2117 CB LEU A 266 7765 7549 11299 425 -541 302 C ATOM 2118 CG LEU A 266 -367.233-167.546 155.558 1.00 75.10 C ANISOU 2118 CG LEU A 266 8270 8203 12063 394 -609 338 C ATOM 2119 CD1 LEU A 266 -367.878-168.172 156.786 1.00 68.08 C ANISOU 2119 CD1 LEU A 266 7319 7325 11221 356 -396 223 C ATOM 2120 CD2 LEU A 266 -368.257-166.737 154.757 1.00 61.47 C ANISOU 2120 CD2 LEU A 266 6344 6376 10637 451 -756 426 C ATOM 2121 N PRO A 267 -363.170-165.095 155.767 1.00 77.76 N ANISOU 2121 N PRO A 267 9058 8528 11960 452 -564 318 N ATOM 2122 CA PRO A 267 -362.419-163.862 156.064 1.00 69.48 C ANISOU 2122 CA PRO A 267 8056 7413 10929 484 -516 291 C ATOM 2123 C PRO A 267 -362.133-163.002 154.844 1.00 73.93 C ANISOU 2123 C PRO A 267 8623 7922 11544 514 -681 415 C ATOM 2124 O PRO A 267 -362.218-161.771 154.937 1.00 77.48 O ANISOU 2124 O PRO A 267 9021 8259 12160 563 -665 414 O ATOM 2125 CB PRO A 267 -361.132-164.398 156.701 1.00 59.35 C ANISOU 2125 CB PRO A 267 6940 6221 9388 430 -446 235 C ATOM 2126 CG PRO A 267 -361.570-165.624 157.387 1.00 58.66 C ANISOU 2126 CG PRO A 267 6857 6205 9228 385 -367 181 C ATOM 2127 CD PRO A 267 -362.558-166.257 156.439 1.00 67.26 C ANISOU 2127 CD PRO A 267 7847 7302 10407 390 -482 260 C ATOM 2128 N TYR A 268 -361.794-163.609 153.704 1.00 67.55 N ANISOU 2128 N TYR A 268 7887 7183 10595 477 -833 521 N ATOM 2129 CA TYR A 268 -361.646-162.828 152.480 1.00 66.81 C ANISOU 2129 CA TYR A 268 7811 7039 10535 485 -997 654 C ATOM 2130 C TYR A 268 -362.952-162.134 152.126 1.00 73.87 C ANISOU 2130 C TYR A 268 8533 7817 11717 540 -1094 724 C ATOM 2131 O TYR A 268 -362.976-160.928 151.852 1.00 82.95 O ANISOU 2131 O TYR A 268 9646 8854 13019 584 -1146 784 O ATOM 2132 CB TYR A 268 -361.192-163.721 151.329 1.00 61.04 C ANISOU 2132 CB TYR A 268 7199 6407 9587 416 -1124 738 C ATOM 2133 CG TYR A 268 -359.809-164.295 151.496 1.00 69.71 C ANISOU 2133 CG TYR A 268 8448 7595 10441 372 -1041 686 C ATOM 2134 CD1 TYR A 268 -359.619-165.544 152.074 1.00 72.36 C ANISOU 2134 CD1 TYR A 268 8819 8017 10657 345 -959 606 C ATOM 2135 CD2 TYR A 268 -358.688-163.592 151.067 1.00 63.22 C ANISOU 2135 CD2 TYR A 268 7726 6765 9531 357 -1046 725 C ATOM 2136 CE1 TYR A 268 -358.351-166.076 152.223 1.00 71.65 C ANISOU 2136 CE1 TYR A 268 8846 7994 10384 313 -895 568 C ATOM 2137 CE2 TYR A 268 -357.419-164.116 151.209 1.00 60.70 C ANISOU 2137 CE2 TYR A 268 7516 6520 9028 320 -970 679 C ATOM 2138 CZ TYR A 268 -357.254-165.356 151.786 1.00 68.73 C ANISOU 2138 CZ TYR A 268 8553 7614 9948 304 -900 602 C ATOM 2139 OH TYR A 268 -355.986-165.869 151.925 1.00 65.13 O ANISOU 2139 OH TYR A 268 8183 7215 9346 276 -837 565 O ATOM 2140 N ALA A 269 -364.054-162.888 152.134 1.00 74.16 N ANISOU 2140 N ALA A 269 8453 7872 11852 537 -1126 721 N ATOM 2141 CA ALA A 269 -365.360-162.312 151.843 1.00 70.49 C ANISOU 2141 CA ALA A 269 7787 7292 11702 592 -1225 788 C ATOM 2142 C ALA A 269 -365.685-161.181 152.812 1.00 72.36 C ANISOU 2142 C ALA A 269 7900 7391 12202 677 -1069 700 C ATOM 2143 O ALA A 269 -366.146-160.110 152.404 1.00 71.52 O ANISOU 2143 O ALA A 269 7686 7146 12342 740 -1163 782 O ATOM 2144 CB ALA A 269 -366.431-163.401 151.893 1.00 68.96 C ANISOU 2144 CB ALA A 269 7477 7148 11576 565 -1247 773 C ATOM 2145 N GLY A 270 -365.434-161.397 154.101 1.00 73.66 N ANISOU 2145 N GLY A 270 8090 7583 12314 674 -832 533 N ATOM 2146 CA GLY A 270 -365.639-160.361 155.093 1.00 76.59 C ANISOU 2146 CA GLY A 270 8381 7828 12894 735 -651 418 C ATOM 2147 C GLY A 270 -364.811-159.115 154.842 1.00 85.41 C ANISOU 2147 C GLY A 270 9576 8853 14024 764 -686 455 C ATOM 2148 O GLY A 270 -365.351-158.006 154.789 1.00 84.80 O ANISOU 2148 O GLY A 270 9373 8611 14238 839 -694 474 O ATOM 2149 N VAL A 271 -363.495-159.290 154.682 1.00 82.85 N ANISOU 2149 N VAL A 271 9450 8622 13406 706 -705 468 N ATOM 2150 CA VAL A 271 -362.615-158.152 154.427 1.00 78.06 C ANISOU 2150 CA VAL A 271 8928 7937 12796 717 -734 505 C ATOM 2151 C VAL A 271 -363.009-157.450 153.134 1.00 76.91 C ANISOU 2151 C VAL A 271 8722 7693 12807 752 -954 693 C ATOM 2152 O VAL A 271 -363.088-156.216 153.080 1.00 83.03 O ANISOU 2152 O VAL A 271 9447 8310 13792 805 -967 722 O ATOM 2153 CB VAL A 271 -361.144-158.609 154.400 1.00 74.16 C ANISOU 2153 CB VAL A 271 8635 7572 11970 639 -724 496 C ATOM 2154 CG1 VAL A 271 -360.290-157.631 153.595 1.00 73.97 C ANISOU 2154 CG1 VAL A 271 8694 7488 11924 631 -826 602 C ATOM 2155 CG2 VAL A 271 -360.609-158.750 155.817 1.00 59.98 C ANISOU 2155 CG2 VAL A 271 6903 5812 10073 610 -520 319 C ATOM 2156 N ALA A 272 -363.273-158.219 152.077 1.00 71.02 N ANISOU 2156 N ALA A 272 7991 7031 11961 713 -1137 824 N ATOM 2157 CA ALA A 272 -363.641-157.607 150.804 1.00 74.99 C ANISOU 2157 CA ALA A 272 8466 7453 12575 722 -1375 1022 C ATOM 2158 C ALA A 272 -364.980-156.887 150.898 1.00 87.00 C ANISOU 2158 C ALA A 272 9753 8801 14502 817 -1426 1057 C ATOM 2159 O ALA A 272 -365.136-155.786 150.356 1.00 93.20 O ANISOU 2159 O ALA A 272 10494 9437 15482 861 -1549 1178 O ATOM 2160 CB ALA A 272 -363.678-158.661 149.705 1.00 69.70 C ANISOU 2160 CB ALA A 272 7880 6917 11687 640 -1553 1136 C ATOM 2161 N PHE A 273 -365.961-157.491 151.573 1.00 88.02 N ANISOU 2161 N PHE A 273 9721 8940 14782 849 -1331 959 N ATOM 2162 CA PHE A 273 -367.233-156.805 151.768 1.00 90.91 C ANISOU 2162 CA PHE A 273 9833 9131 15579 947 -1343 971 C ATOM 2163 C PHE A 273 -367.054-155.551 152.612 1.00 97.53 C ANISOU 2163 C PHE A 273 10626 9799 16632 1025 -1161 861 C ATOM 2164 O PHE A 273 -367.713-154.533 152.371 1.00 98.27 O ANISOU 2164 O PHE A 273 10560 9697 17080 1112 -1236 934 O ATOM 2165 CB PHE A 273 -368.258-157.736 152.414 1.00 88.72 C ANISOU 2165 CB PHE A 273 9392 8902 15415 953 -1234 865 C ATOM 2166 CG PHE A 273 -369.535-157.047 152.800 1.00 98.98 C ANISOU 2166 CG PHE A 273 10403 10015 17189 1059 -1184 838 C ATOM 2167 CD1 PHE A 273 -370.476-156.712 151.839 1.00103.49 C ANISOU 2167 CD1 PHE A 273 10792 10479 18051 1104 -1445 1023 C ATOM 2168 CD2 PHE A 273 -369.793-156.725 154.123 1.00103.66 C ANISOU 2168 CD2 PHE A 273 10908 10533 17946 1106 -876 627 C ATOM 2169 CE1 PHE A 273 -371.652-156.075 152.189 1.00 96.21 C ANISOU 2169 CE1 PHE A 273 9575 9369 17612 1211 -1399 1000 C ATOM 2170 CE2 PHE A 273 -370.968-156.087 154.480 1.00102.54 C ANISOU 2170 CE2 PHE A 273 10487 10205 18267 1207 -799 586 C ATOM 2171 CZ PHE A 273 -371.898-155.762 153.512 1.00 97.04 C ANISOU 2171 CZ PHE A 273 9581 9395 17896 1267 -1060 774 C ATOM 2172 N TYR A 274 -366.168-155.603 153.610 1.00100.95 N ANISOU 2172 N TYR A 274 11199 10293 16865 992 -930 687 N ATOM 2173 CA TYR A 274 -365.881-154.400 154.382 1.00102.67 C ANISOU 2173 CA TYR A 274 11411 10352 17246 1043 -762 573 C ATOM 2174 C TYR A 274 -365.178-153.353 153.532 1.00108.66 C ANISOU 2174 C TYR A 274 12261 11012 18015 1050 -924 722 C ATOM 2175 O TYR A 274 -365.346-152.155 153.772 1.00109.40 O ANISOU 2175 O TYR A 274 12279 10904 18384 1120 -874 699 O ATOM 2176 CB TYR A 274 -365.033-154.728 155.612 1.00103.62 C ANISOU 2176 CB TYR A 274 11685 10573 17114 980 -510 364 C ATOM 2177 CG TYR A 274 -364.927-153.578 156.591 1.00110.36 C ANISOU 2177 CG TYR A 274 12524 11260 18147 1020 -302 203 C ATOM 2178 CD1 TYR A 274 -365.726-153.531 157.724 1.00118.65 C ANISOU 2178 CD1 TYR A 274 13459 12242 19382 1049 -54 9 C ATOM 2179 CD2 TYR A 274 -364.034-152.535 156.381 1.00114.78 C ANISOU 2179 CD2 TYR A 274 13192 11727 18692 1016 -341 235 C ATOM 2180 CE1 TYR A 274 -365.639-152.481 158.618 1.00124.74 C ANISOU 2180 CE1 TYR A 274 14234 12854 20309 1073 153 -158 C ATOM 2181 CE2 TYR A 274 -363.946-151.479 157.263 1.00120.46 C ANISOU 2181 CE2 TYR A 274 13908 12284 19579 1044 -152 78 C ATOM 2182 CZ TYR A 274 -364.748-151.457 158.382 1.00126.38 C ANISOU 2182 CZ TYR A 274 14552 12965 20501 1072 97 -125 C ATOM 2183 OH TYR A 274 -364.657-150.409 159.269 1.00133.10 O ANISOU 2183 OH TYR A 274 15416 13648 21507 1087 302 -303 O ATOM 2184 N ILE A 275 -364.384-153.779 152.549 1.00109.19 N ANISOU 2184 N ILE A 275 12493 11207 17789 971 -1103 868 N ATOM 2185 CA ILE A 275 -363.707-152.818 151.684 1.00104.29 C ANISOU 2185 CA ILE A 275 11971 10497 17156 958 -1252 1023 C ATOM 2186 C ILE A 275 -364.646-152.305 150.596 1.00108.28 C ANISOU 2186 C ILE A 275 12347 10869 17927 1008 -1511 1242 C ATOM 2187 O ILE A 275 -364.512-151.161 150.147 1.00114.34 O ANISOU 2187 O ILE A 275 13117 11468 18859 1039 -1607 1357 O ATOM 2188 CB ILE A 275 -362.428-153.446 151.099 1.00 96.08 C ANISOU 2188 CB ILE A 275 11164 9642 15698 843 -1306 1077 C ATOM 2189 CG1 ILE A 275 -361.371-153.598 152.194 1.00 94.48 C ANISOU 2189 CG1 ILE A 275 11079 9521 15300 802 -1077 884 C ATOM 2190 CG2 ILE A 275 -361.871-152.610 149.955 1.00 90.29 C ANISOU 2190 CG2 ILE A 275 10536 8837 14934 807 -1489 1276 C ATOM 2191 CD1 ILE A 275 -360.078-154.201 151.708 1.00 92.78 C ANISOU 2191 CD1 ILE A 275 11059 9471 14722 700 -1107 923 C ATOM 2192 N PHE A 276 -365.626-153.109 150.177 1.00112.55 N ANISOU 2192 N PHE A 276 12768 11467 18529 1014 -1638 1311 N ATOM 2193 CA PHE A 276 -366.581-152.639 149.176 1.00124.10 C ANISOU 2193 CA PHE A 276 14092 12798 20263 1056 -1914 1530 C ATOM 2194 C PHE A 276 -367.461-151.534 149.748 1.00131.55 C ANISOU 2194 C PHE A 276 14794 13484 21706 1194 -1849 1492 C ATOM 2195 O PHE A 276 -367.512-150.422 149.210 1.00136.50 O ANISOU 2195 O PHE A 276 15392 13923 22548 1239 -1992 1641 O ATOM 2196 CB PHE A 276 -367.422-153.802 148.658 1.00133.61 C ANISOU 2196 CB PHE A 276 15217 14127 21420 1017 -2067 1597 C ATOM 2197 CG PHE A 276 -367.988-153.562 147.294 1.00145.76 C ANISOU 2197 CG PHE A 276 16728 15607 23047 993 -2426 1869 C ATOM 2198 CD1 PHE A 276 -367.149-153.271 146.231 1.00149.14 C ANISOU 2198 CD1 PHE A 276 17385 16070 23210 898 -2603 2043 C ATOM 2199 CD2 PHE A 276 -369.353-153.621 147.070 1.00150.30 C ANISOU 2199 CD2 PHE A 276 17049 16090 23970 1052 -2589 1956 C ATOM 2200 CE1 PHE A 276 -367.658-153.045 144.970 1.00153.11 C ANISOU 2200 CE1 PHE A 276 17893 16522 23760 854 -2946 2305 C ATOM 2201 CE2 PHE A 276 -369.871-153.397 145.810 1.00152.68 C ANISOU 2201 CE2 PHE A 276 17333 16336 24345 1016 -2953 2223 C ATOM 2202 CZ PHE A 276 -369.023-153.108 144.757 1.00154.47 C ANISOU 2202 CZ PHE A 276 17817 16603 24272 912 -3137 2401 C ATOM 2203 N THR A 277 -368.164-151.820 150.843 1.00131.97 N ANISOU 2203 N THR A 277 14673 13514 21955 1259 -1622 1293 N ATOM 2204 CA THR A 277 -368.630-150.744 151.699 1.00130.18 C ANISOU 2204 CA THR A 277 14275 13053 22133 1376 -1436 1168 C ATOM 2205 C THR A 277 -367.410-150.041 152.290 1.00139.47 C ANISOU 2205 C THR A 277 15652 14203 23136 1347 -1253 1045 C ATOM 2206 O THR A 277 -366.280-150.492 152.134 1.00147.28 O ANISOU 2206 O THR A 277 16879 15366 23713 1242 -1254 1045 O ATOM 2207 CB THR A 277 -369.539-151.282 152.805 1.00123.06 C ANISOU 2207 CB THR A 277 13178 12156 21421 1424 -1184 953 C ATOM 2208 OG1 THR A 277 -368.744-151.891 153.830 1.00123.23 O ANISOU 2208 OG1 THR A 277 13378 12341 21103 1347 -912 731 O ATOM 2209 CG2 THR A 277 -370.500-152.322 152.246 1.00117.83 C ANISOU 2209 CG2 THR A 277 12371 11597 20802 1407 -1356 1057 C ATOM 2210 N HIS A 278 -367.638-148.915 152.963 1.00139.94 N ANISOU 2210 N HIS A 278 15608 14033 23532 1437 -1095 937 N ATOM 2211 CA HIS A 278 -366.547-148.165 153.595 1.00143.42 C ANISOU 2211 CA HIS A 278 16226 14424 23844 1405 -918 804 C ATOM 2212 C HIS A 278 -365.377-147.952 152.630 1.00145.59 C ANISOU 2212 C HIS A 278 16731 14769 23817 1315 -1117 988 C ATOM 2213 O HIS A 278 -364.208-148.063 153.007 1.00141.27 O ANISOU 2213 O HIS A 278 16389 14339 22950 1227 -1005 893 O ATOM 2214 CB HIS A 278 -366.058-148.866 154.868 1.00139.45 C ANISOU 2214 CB HIS A 278 15833 14083 23069 1337 -619 534 C ATOM 2215 CG HIS A 278 -367.130-149.120 155.882 1.00148.33 C ANISOU 2215 CG HIS A 278 16764 15154 24439 1397 -383 336 C ATOM 2216 ND1 HIS A 278 -367.657-150.373 156.110 1.00151.46 N ANISOU 2216 ND1 HIS A 278 17107 15730 24710 1363 -340 291 N ATOM 2217 CD2 HIS A 278 -367.767-148.285 156.737 1.00158.79 C ANISOU 2217 CD2 HIS A 278 17941 16263 26130 1481 -155 161 C ATOM 2218 CE1 HIS A 278 -368.574-150.298 157.058 1.00158.96 C ANISOU 2218 CE1 HIS A 278 17883 16582 25932 1418 -95 105 C ATOM 2219 NE2 HIS A 278 -368.661-149.042 157.455 1.00163.28 N ANISOU 2219 NE2 HIS A 278 18369 16889 26780 1492 29 16 N ATOM 2220 N GLN A 279 -365.689-147.648 151.368 1.00153.54 N ANISOU 2220 N GLN A 279 17703 15706 24929 1329 -1417 1258 N ATOM 2221 CA GLN A 279 -364.677-147.478 150.326 1.00154.96 C ANISOU 2221 CA GLN A 279 18103 15953 24822 1230 -1610 1453 C ATOM 2222 C GLN A 279 -363.901-146.172 150.521 1.00160.24 C ANISOU 2222 C GLN A 279 18861 16439 25584 1234 -1539 1438 C ATOM 2223 O GLN A 279 -363.324-145.627 149.575 1.00164.38 O ANISOU 2223 O GLN A 279 19513 16919 26025 1178 -1720 1639 O ATOM 2224 CB GLN A 279 -365.355-147.535 148.944 1.00156.06 C ANISOU 2224 CB GLN A 279 18189 16063 25044 1227 -1958 1750 C ATOM 2225 CG GLN A 279 -364.442-147.484 147.707 1.00161.26 C ANISOU 2225 CG GLN A 279 19087 16808 25376 1102 -2173 1975 C ATOM 2226 CD GLN A 279 -364.099-148.846 147.141 1.00170.10 C ANISOU 2226 CD GLN A 279 20350 18211 26068 983 -2243 2005 C ATOM 2227 OE1 GLN A 279 -364.981-149.607 146.743 1.00176.39 O ANISOU 2227 OE1 GLN A 279 21049 19077 26895 986 -2385 2073 O ATOM 2228 NE2 GLN A 279 -362.807-149.155 147.085 1.00172.00 N ANISOU 2228 NE2 GLN A 279 20819 18607 25927 874 -2143 1954 N ATOM 2229 N GLY A 280 -363.854-145.667 151.750 1.00157.10 N ANISOU 2229 N GLY A 280 18414 15933 25344 1284 -1270 1195 N ATOM 2230 CA GLY A 280 -363.287-144.354 151.982 1.00151.10 C ANISOU 2230 CA GLY A 280 17711 14959 24740 1297 -1202 1167 C ATOM 2231 C GLY A 280 -361.950-144.306 152.695 1.00143.72 C ANISOU 2231 C GLY A 280 16984 14127 23495 1193 -1012 994 C ATOM 2232 O GLY A 280 -361.134-143.425 152.413 1.00143.63 O ANISOU 2232 O GLY A 280 17091 14013 23470 1147 -1048 1059 O ATOM 2233 N SER A 281 -361.703-145.236 153.613 1.00137.12 N ANISOU 2233 N SER A 281 16194 13487 22418 1146 -823 784 N ATOM 2234 CA SER A 281 -360.573-145.108 154.521 1.00132.94 C ANISOU 2234 CA SER A 281 15828 13021 21660 1057 -632 591 C ATOM 2235 C SER A 281 -359.336-145.833 154.000 1.00123.53 C ANISOU 2235 C SER A 281 14829 12070 20037 929 -720 676 C ATOM 2236 O SER A 281 -359.378-146.582 153.020 1.00126.57 O ANISOU 2236 O SER A 281 15234 12594 20262 904 -893 853 O ATOM 2237 CB SER A 281 -360.937-145.639 155.907 1.00135.10 C ANISOU 2237 CB SER A 281 16061 13358 21911 1063 -373 313 C ATOM 2238 OG SER A 281 -361.747-144.716 156.612 1.00142.55 O ANISOU 2238 OG SER A 281 16869 14051 23241 1156 -212 169 O ATOM 2239 N CYS A 282 -358.218-145.593 154.681 1.00117.47 N ANISOU 2239 N CYS A 282 14200 11341 19092 842 -592 540 N ATOM 2240 CA CYS A 282 -356.993-146.336 154.439 1.00121.01 C ANISOU 2240 CA CYS A 282 14806 12016 19158 724 -627 572 C ATOM 2241 C CYS A 282 -357.012-147.636 155.231 1.00125.77 C ANISOU 2241 C CYS A 282 15420 12835 19531 697 -520 424 C ATOM 2242 O CYS A 282 -357.556-147.705 156.336 1.00126.45 O ANISOU 2242 O CYS A 282 15454 12891 19701 727 -354 233 O ATOM 2243 CB CYS A 282 -355.767-145.511 154.847 1.00126.13 C ANISOU 2243 CB CYS A 282 15579 12605 19740 636 -555 498 C ATOM 2244 SG CYS A 282 -355.713-143.813 154.222 1.00126.78 S ANISOU 2244 SG CYS A 282 15657 12385 20128 660 -633 627 S ATOM 2245 N PHE A 283 -356.413-148.671 154.655 1.00132.85 N ANISOU 2245 N PHE A 283 16393 13944 20138 633 -606 514 N ATOM 2246 CA PHE A 283 -356.330-149.981 155.285 1.00135.08 C ANISOU 2246 CA PHE A 283 16699 14433 20193 601 -531 406 C ATOM 2247 C PHE A 283 -354.896-150.237 155.725 1.00138.81 C ANISOU 2247 C PHE A 283 17308 15029 20406 494 -482 336 C ATOM 2248 O PHE A 283 -353.965-150.112 154.923 1.00142.05 O ANISOU 2248 O PHE A 283 17790 15477 20703 436 -570 455 O ATOM 2249 CB PHE A 283 -356.795-151.077 154.326 1.00134.84 C ANISOU 2249 CB PHE A 283 16639 14541 20054 614 -665 549 C ATOM 2250 CG PHE A 283 -358.038-150.723 153.563 1.00139.26 C ANISOU 2250 CG PHE A 283 17070 14975 20868 700 -786 681 C ATOM 2251 CD1 PHE A 283 -359.154-150.226 154.215 1.00139.83 C ANISOU 2251 CD1 PHE A 283 16994 14894 21241 792 -702 590 C ATOM 2252 CD2 PHE A 283 -358.084-150.872 152.187 1.00143.66 C ANISOU 2252 CD2 PHE A 283 17653 15562 21370 682 -985 897 C ATOM 2253 CE1 PHE A 283 -360.296-149.896 153.511 1.00142.33 C ANISOU 2253 CE1 PHE A 283 17165 15083 21830 877 -833 723 C ATOM 2254 CE2 PHE A 283 -359.221-150.545 151.477 1.00147.97 C ANISOU 2254 CE2 PHE A 283 18080 15990 22151 752 -1133 1037 C ATOM 2255 CZ PHE A 283 -360.329-150.056 152.140 1.00146.44 C ANISOU 2255 CZ PHE A 283 17713 15639 22290 856 -1066 956 C ATOM 2256 N GLY A 284 -354.721-150.589 156.997 1.00137.33 N ANISOU 2256 N GLY A 284 17152 14900 20129 460 -344 149 N ATOM 2257 CA GLY A 284 -353.416-150.913 157.517 1.00131.85 C ANISOU 2257 CA GLY A 284 16570 14324 19203 358 -319 85 C ATOM 2258 C GLY A 284 -352.814-152.109 156.811 1.00128.72 C ANISOU 2258 C GLY A 284 16206 14121 18583 325 -411 195 C ATOM 2259 O GLY A 284 -353.501-152.848 156.096 1.00122.67 O ANISOU 2259 O GLY A 284 15390 13415 17804 372 -475 289 O ATOM 2260 N PRO A 285 -351.508-152.321 156.993 1.00132.38 N ANISOU 2260 N PRO A 285 16745 14674 18879 239 -419 181 N ATOM 2261 CA PRO A 285 -350.881-153.512 156.401 1.00136.21 C ANISOU 2261 CA PRO A 285 17251 15331 19170 211 -480 263 C ATOM 2262 C PRO A 285 -351.500-154.802 156.891 1.00147.78 C ANISOU 2262 C PRO A 285 18698 16916 20535 237 -455 212 C ATOM 2263 O PRO A 285 -351.502-155.803 156.161 1.00154.15 O ANISOU 2263 O PRO A 285 19499 17830 21241 247 -510 295 O ATOM 2264 CB PRO A 285 -349.415-153.388 156.840 1.00127.21 C ANISOU 2264 CB PRO A 285 16168 14237 17927 118 -472 222 C ATOM 2265 CG PRO A 285 -349.461-152.557 158.079 1.00122.84 C ANISOU 2265 CG PRO A 285 15642 13586 17444 88 -398 71 C ATOM 2266 CD PRO A 285 -350.572-151.571 157.851 1.00127.01 C ANISOU 2266 CD PRO A 285 16127 13944 18188 161 -367 73 C ATOM 2267 N ILE A 286 -352.047-154.803 158.106 1.00149.49 N ANISOU 2267 N ILE A 286 18915 17111 20775 240 -362 71 N ATOM 2268 CA ILE A 286 -352.599-156.029 158.660 1.00148.88 C ANISOU 2268 CA ILE A 286 18831 17144 20593 248 -327 22 C ATOM 2269 C ILE A 286 -353.978-156.333 158.081 1.00145.16 C ANISOU 2269 C ILE A 286 18269 16647 20240 330 -337 74 C ATOM 2270 O ILE A 286 -354.297-157.501 157.833 1.00151.27 O ANISOU 2270 O ILE A 286 19027 17527 20920 339 -367 113 O ATOM 2271 CB ILE A 286 -352.636-155.949 160.199 1.00145.77 C ANISOU 2271 CB ILE A 286 18493 16744 20148 194 -215 -146 C ATOM 2272 CG1 ILE A 286 -353.633-154.888 160.671 1.00147.65 C ANISOU 2272 CG1 ILE A 286 18692 16823 20585 233 -103 -248 C ATOM 2273 CG2 ILE A 286 -351.246-155.647 160.750 1.00143.16 C ANISOU 2273 CG2 ILE A 286 18251 16440 19704 100 -241 -186 C ATOM 2274 CD1 ILE A 286 -353.839-154.864 162.172 1.00149.28 C ANISOU 2274 CD1 ILE A 286 18971 17025 20725 168 39 -432 C ATOM 2275 N PHE A 287 -354.793-155.310 157.809 1.00132.08 N ANISOU 2275 N PHE A 287 16540 14840 18804 389 -325 85 N ATOM 2276 CA PHE A 287 -356.226-155.529 157.622 1.00118.22 C ANISOU 2276 CA PHE A 287 14672 13041 17204 464 -315 98 C ATOM 2277 C PHE A 287 -356.527-156.353 156.373 1.00107.99 C ANISOU 2277 C PHE A 287 13344 11827 15860 486 -456 255 C ATOM 2278 O PHE A 287 -357.118-157.436 156.460 1.00 98.88 O ANISOU 2278 O PHE A 287 12158 10765 14647 491 -451 246 O ATOM 2279 CB PHE A 287 -356.970-154.195 157.563 1.00111.44 C ANISOU 2279 CB PHE A 287 13727 11982 16634 530 -286 87 C ATOM 2280 CG PHE A 287 -358.442-154.358 157.356 1.00104.25 C ANISOU 2280 CG PHE A 287 12667 11011 15932 612 -285 107 C ATOM 2281 CD1 PHE A 287 -359.250-154.791 158.394 1.00107.80 C ANISOU 2281 CD1 PHE A 287 13063 11470 16427 621 -129 -38 C ATOM 2282 CD2 PHE A 287 -359.016-154.114 156.120 1.00107.75 C ANISOU 2282 CD2 PHE A 287 13026 11393 16524 669 -445 279 C ATOM 2283 CE1 PHE A 287 -360.605-154.963 158.210 1.00114.32 C ANISOU 2283 CE1 PHE A 287 13727 12239 17472 693 -121 -21 C ATOM 2284 CE2 PHE A 287 -360.373-154.282 155.929 1.00117.06 C ANISOU 2284 CE2 PHE A 287 14047 12514 17918 742 -467 306 C ATOM 2285 CZ PHE A 287 -361.169-154.707 156.977 1.00118.07 C ANISOU 2285 CZ PHE A 287 14097 12648 18118 758 -299 153 C ATOM 2286 N MET A 288 -356.164-155.843 155.196 1.00107.38 N ANISOU 2286 N MET A 288 13283 11712 15803 487 -580 398 N ATOM 2287 CA MET A 288 -356.405-156.598 153.970 1.00104.60 C ANISOU 2287 CA MET A 288 12932 11439 15374 484 -714 541 C ATOM 2288 C MET A 288 -355.583-157.873 153.895 1.00 94.69 C ANISOU 2288 C MET A 288 11761 10354 13862 425 -710 530 C ATOM 2289 O MET A 288 -355.737-158.630 152.932 1.00 95.65 O ANISOU 2289 O MET A 288 11901 10548 13893 410 -800 623 O ATOM 2290 CB MET A 288 -356.093-155.746 152.744 1.00114.48 C ANISOU 2290 CB MET A 288 14217 12616 16665 473 -840 698 C ATOM 2291 CG MET A 288 -356.497-154.303 152.866 1.00121.66 C ANISOU 2291 CG MET A 288 15066 13331 17827 522 -841 712 C ATOM 2292 SD MET A 288 -356.033-153.423 151.371 1.00126.90 S ANISOU 2292 SD MET A 288 15801 13919 18495 485 -1003 926 S ATOM 2293 CE MET A 288 -356.803-154.457 150.128 1.00114.14 C ANISOU 2293 CE MET A 288 14184 12404 16779 472 -1172 1075 C ATOM 2294 N THR A 289 -354.706-158.111 154.866 1.00 84.77 N ANISOU 2294 N THR A 289 10559 9153 12496 387 -614 423 N ATOM 2295 CA THR A 289 -353.870-159.296 154.896 1.00 79.35 C ANISOU 2295 CA THR A 289 9937 8607 11607 340 -610 413 C ATOM 2296 C THR A 289 -354.181-160.213 156.069 1.00 76.46 C ANISOU 2296 C THR A 289 9566 8306 11181 335 -531 304 C ATOM 2297 O THR A 289 -353.490-161.225 156.242 1.00 78.75 O ANISOU 2297 O THR A 289 9903 8697 11322 300 -531 295 O ATOM 2298 CB THR A 289 -352.390-158.895 154.936 1.00 82.18 C ANISOU 2298 CB THR A 289 10361 8978 11883 285 -598 410 C ATOM 2299 OG1 THR A 289 -352.151-158.084 156.091 1.00 85.89 O ANISOU 2299 OG1 THR A 289 10837 9382 12414 271 -527 305 O ATOM 2300 CG2 THR A 289 -352.022-158.107 153.686 1.00 80.02 C ANISOU 2300 CG2 THR A 289 10110 8651 11641 271 -665 530 C ATOM 2301 N ILE A 290 -355.188-159.888 156.888 1.00 68.96 N ANISOU 2301 N ILE A 290 8559 7292 10349 364 -456 223 N ATOM 2302 CA ILE A 290 -355.623-160.820 157.929 1.00 73.28 C ANISOU 2302 CA ILE A 290 9112 7904 10828 345 -373 132 C ATOM 2303 C ILE A 290 -356.100-162.142 157.339 1.00 76.98 C ANISOU 2303 C ILE A 290 9560 8461 11229 351 -429 193 C ATOM 2304 O ILE A 290 -355.696-163.200 157.849 1.00 76.30 O ANISOU 2304 O ILE A 290 9528 8464 11000 313 -409 167 O ATOM 2305 CB ILE A 290 -356.689-160.163 158.824 1.00 76.82 C ANISOU 2305 CB ILE A 290 9498 8257 11433 369 -253 25 C ATOM 2306 CG1 ILE A 290 -356.081-159.059 159.680 1.00 80.88 C ANISOU 2306 CG1 ILE A 290 10070 8695 11965 337 -173 -75 C ATOM 2307 CG2 ILE A 290 -357.332-161.201 159.731 1.00 75.50 C ANISOU 2307 CG2 ILE A 290 9333 8158 11196 341 -161 -51 C ATOM 2308 CD1 ILE A 290 -357.119-158.220 160.398 1.00 86.23 C ANISOU 2308 CD1 ILE A 290 10683 9247 12833 367 -36 -190 C ATOM 2309 N PRO A 291 -356.946-162.170 156.296 1.00 72.25 N ANISOU 2309 N PRO A 291 8889 7837 10728 391 -509 278 N ATOM 2310 CA PRO A 291 -357.330-163.473 155.726 1.00 64.23 C ANISOU 2310 CA PRO A 291 7869 6905 9631 379 -567 327 C ATOM 2311 C PRO A 291 -356.138-164.303 155.276 1.00 64.78 C ANISOU 2311 C PRO A 291 8037 7066 9511 338 -606 361 C ATOM 2312 O PRO A 291 -356.087-165.503 155.563 1.00 70.97 O ANISOU 2312 O PRO A 291 8848 7921 10198 315 -589 339 O ATOM 2313 CB PRO A 291 -358.243-163.082 154.552 1.00 64.37 C ANISOU 2313 CB PRO A 291 7809 6867 9781 412 -682 428 C ATOM 2314 CG PRO A 291 -358.791-161.760 154.924 1.00 73.69 C ANISOU 2314 CG PRO A 291 8906 7921 11170 462 -645 405 C ATOM 2315 CD PRO A 291 -357.677-161.062 155.645 1.00 71.47 C ANISOU 2315 CD PRO A 291 8705 7621 10828 442 -562 336 C ATOM 2316 N ALA A 292 -355.166-163.692 154.595 1.00 69.23 N ANISOU 2316 N ALA A 292 8649 7618 10036 326 -648 413 N ATOM 2317 CA ALA A 292 -353.984-164.435 154.172 1.00 62.36 C ANISOU 2317 CA ALA A 292 7854 6822 9019 290 -658 433 C ATOM 2318 C ALA A 292 -353.160-164.886 155.370 1.00 71.90 C ANISOU 2318 C ALA A 292 9091 8069 10160 270 -593 357 C ATOM 2319 O ALA A 292 -352.605-165.993 155.371 1.00 67.43 O ANISOU 2319 O ALA A 292 8555 7564 9501 253 -594 356 O ATOM 2320 CB ALA A 292 -353.132-163.585 153.235 1.00 53.43 C ANISOU 2320 CB ALA A 292 6761 5664 7877 272 -692 500 C ATOM 2321 N PHE A 293 -353.070-164.039 156.397 1.00 70.17 N ANISOU 2321 N PHE A 293 8867 7805 9989 266 -544 295 N ATOM 2322 CA PHE A 293 -352.345-164.401 157.610 1.00 70.84 C ANISOU 2322 CA PHE A 293 8994 7925 9996 228 -507 231 C ATOM 2323 C PHE A 293 -352.863-165.712 158.193 1.00 65.39 C ANISOU 2323 C PHE A 293 8317 7292 9238 217 -488 210 C ATOM 2324 O PHE A 293 -352.084-166.616 158.513 1.00 66.05 O ANISOU 2324 O PHE A 293 8437 7426 9232 193 -511 219 O ATOM 2325 CB PHE A 293 -352.454-163.268 158.633 1.00 69.16 C ANISOU 2325 CB PHE A 293 8793 7649 9837 209 -449 151 C ATOM 2326 CG PHE A 293 -351.674-163.508 159.895 1.00 72.29 C ANISOU 2326 CG PHE A 293 9255 8081 10131 147 -433 90 C ATOM 2327 CD1 PHE A 293 -350.324-163.195 159.960 1.00 70.15 C ANISOU 2327 CD1 PHE A 293 9010 7819 9826 110 -484 105 C ATOM 2328 CD2 PHE A 293 -352.295-164.034 161.020 1.00 74.79 C ANISOU 2328 CD2 PHE A 293 9612 8420 10386 113 -374 24 C ATOM 2329 CE1 PHE A 293 -349.605-163.411 161.115 1.00 72.84 C ANISOU 2329 CE1 PHE A 293 9410 8190 10075 42 -503 64 C ATOM 2330 CE2 PHE A 293 -351.583-164.253 162.181 1.00 78.28 C ANISOU 2330 CE2 PHE A 293 10138 8896 10710 37 -383 -17 C ATOM 2331 CZ PHE A 293 -350.234-163.942 162.229 1.00 78.94 C ANISOU 2331 CZ PHE A 293 10243 8988 10763 2 -461 7 C ATOM 2332 N PHE A 294 -354.183-165.837 158.329 1.00 69.76 N ANISOU 2332 N PHE A 294 8830 7827 9850 235 -450 188 N ATOM 2333 CA PHE A 294 -354.744-167.044 158.926 1.00 65.83 C ANISOU 2333 CA PHE A 294 8345 7375 9293 213 -420 168 C ATOM 2334 C PHE A 294 -354.889-168.179 157.920 1.00 55.43 C ANISOU 2334 C PHE A 294 7016 6098 7948 227 -481 232 C ATOM 2335 O PHE A 294 -354.882-169.348 158.318 1.00 62.16 O ANISOU 2335 O PHE A 294 7899 6987 8730 203 -476 232 O ATOM 2336 CB PHE A 294 -356.091-166.733 159.579 1.00 62.36 C ANISOU 2336 CB PHE A 294 7857 6897 8941 214 -329 105 C ATOM 2337 CG PHE A 294 -355.969-165.966 160.862 1.00 81.15 C ANISOU 2337 CG PHE A 294 10283 9247 11304 174 -234 11 C ATOM 2338 CD1 PHE A 294 -355.346-166.531 161.963 1.00 89.69 C ANISOU 2338 CD1 PHE A 294 11467 10377 12235 103 -213 -21 C ATOM 2339 CD2 PHE A 294 -356.467-164.678 160.969 1.00 87.47 C ANISOU 2339 CD2 PHE A 294 11034 9961 12238 201 -170 -46 C ATOM 2340 CE1 PHE A 294 -355.225-165.829 163.147 1.00 95.73 C ANISOU 2340 CE1 PHE A 294 12302 11118 12952 43 -131 -114 C ATOM 2341 CE2 PHE A 294 -356.350-163.971 162.151 1.00 86.86 C ANISOU 2341 CE2 PHE A 294 11017 9849 12135 152 -67 -153 C ATOM 2342 CZ PHE A 294 -355.728-164.547 163.241 1.00 93.09 C ANISOU 2342 CZ PHE A 294 11927 10700 12743 65 -47 -191 C ATOM 2343 N ALA A 295 -355.004-167.868 156.627 1.00 54.41 N ANISOU 2343 N ALA A 295 6857 5953 7864 255 -541 288 N ATOM 2344 CA ALA A 295 -355.093-168.914 155.615 1.00 48.92 C ANISOU 2344 CA ALA A 295 6174 5293 7121 250 -594 334 C ATOM 2345 C ALA A 295 -353.803-169.712 155.477 1.00 60.75 C ANISOU 2345 C ALA A 295 7731 6827 8523 236 -599 342 C ATOM 2346 O ALA A 295 -353.816-170.770 154.838 1.00 59.51 O ANISOU 2346 O ALA A 295 7596 6692 8324 227 -618 356 O ATOM 2347 CB ALA A 295 -355.467-168.316 154.257 1.00 45.36 C ANISOU 2347 CB ALA A 295 5704 4819 6713 262 -666 396 C ATOM 2348 N LYS A 296 -352.694-169.229 156.041 1.00 70.48 N ANISOU 2348 N LYS A 296 8982 8057 9740 232 -583 329 N ATOM 2349 CA LYS A 296 -351.451-169.985 155.988 1.00 63.79 C ANISOU 2349 CA LYS A 296 8160 7232 8846 226 -589 339 C ATOM 2350 C LYS A 296 -351.548-171.283 156.782 1.00 63.99 C ANISOU 2350 C LYS A 296 8205 7273 8835 215 -589 329 C ATOM 2351 O LYS A 296 -350.943-172.291 156.393 1.00 55.23 O ANISOU 2351 O LYS A 296 7105 6167 7715 221 -597 344 O ATOM 2352 CB LYS A 296 -350.296-169.133 156.521 1.00 61.93 C ANISOU 2352 CB LYS A 296 7921 6986 8625 215 -591 333 C ATOM 2353 CG LYS A 296 -349.891-167.967 155.646 1.00 64.82 C ANISOU 2353 CG LYS A 296 8274 7327 9026 217 -588 354 C ATOM 2354 CD LYS A 296 -348.859-167.107 156.369 1.00 66.47 C ANISOU 2354 CD LYS A 296 8474 7520 9261 195 -592 339 C ATOM 2355 CE LYS A 296 -348.739-165.716 155.747 1.00 72.04 C ANISOU 2355 CE LYS A 296 9173 8182 10017 189 -584 356 C ATOM 2356 NZ LYS A 296 -347.951-165.721 154.481 1.00 81.30 N ANISOU 2356 NZ LYS A 296 10343 9361 11185 180 -571 403 N ATOM 2357 N THR A 297 -352.306-171.284 157.885 1.00 58.34 N ANISOU 2357 N THR A 297 7500 6559 8108 193 -569 304 N ATOM 2358 CA THR A 297 -352.425-172.480 158.713 1.00 61.70 C ANISOU 2358 CA THR A 297 7961 6996 8487 167 -570 309 C ATOM 2359 C THR A 297 -353.130-173.629 158.004 1.00 62.88 C ANISOU 2359 C THR A 297 8105 7143 8643 173 -571 322 C ATOM 2360 O THR A 297 -353.110-174.752 158.518 1.00 64.71 O ANISOU 2360 O THR A 297 8368 7370 8848 153 -578 338 O ATOM 2361 CB THR A 297 -353.171-172.174 160.017 1.00 59.73 C ANISOU 2361 CB THR A 297 7740 6749 8203 122 -523 272 C ATOM 2362 OG1 THR A 297 -354.473-171.666 159.719 1.00 68.41 O ANISOU 2362 OG1 THR A 297 8791 7837 9364 133 -469 240 O ATOM 2363 CG2 THR A 297 -352.409-171.168 160.857 1.00 52.36 C ANISOU 2363 CG2 THR A 297 6840 5815 7241 95 -527 247 C ATOM 2364 N SER A 298 -353.744-173.384 156.846 1.00 62.33 N ANISOU 2364 N SER A 298 8005 7072 8606 190 -576 322 N ATOM 2365 CA SER A 298 -354.310-174.478 156.068 1.00 62.29 C ANISOU 2365 CA SER A 298 8006 7063 8597 181 -591 329 C ATOM 2366 C SER A 298 -353.248-175.485 155.646 1.00 65.82 C ANISOU 2366 C SER A 298 8489 7496 9022 190 -597 335 C ATOM 2367 O SER A 298 -353.580-176.647 155.393 1.00 65.07 O ANISOU 2367 O SER A 298 8416 7384 8923 175 -598 331 O ATOM 2368 CB SER A 298 -355.043-173.930 154.843 1.00 56.20 C ANISOU 2368 CB SER A 298 7210 6294 7850 182 -623 338 C ATOM 2369 OG SER A 298 -354.143-173.473 153.848 1.00 58.35 O ANISOU 2369 OG SER A 298 7507 6568 8094 193 -637 352 O ATOM 2370 N ALA A 299 -351.981-175.068 155.574 1.00 57.87 N ANISOU 2370 N ALA A 299 7479 6485 8022 213 -594 342 N ATOM 2371 CA ALA A 299 -350.905-176.006 155.284 1.00 49.30 C ANISOU 2371 CA ALA A 299 6402 5372 6959 230 -584 342 C ATOM 2372 C ALA A 299 -350.757-177.059 156.373 1.00 55.49 C ANISOU 2372 C ALA A 299 7197 6127 7760 227 -608 365 C ATOM 2373 O ALA A 299 -350.143-178.106 156.131 1.00 51.77 O ANISOU 2373 O ALA A 299 6726 5610 7334 246 -604 368 O ATOM 2374 CB ALA A 299 -349.586-175.259 155.100 1.00 50.21 C ANISOU 2374 CB ALA A 299 6485 5486 7108 252 -573 348 C ATOM 2375 N VAL A 300 -351.305-176.812 157.558 1.00 55.76 N ANISOU 2375 N VAL A 300 7247 6180 7760 198 -628 382 N ATOM 2376 CA VAL A 300 -351.263-177.769 158.656 1.00 59.83 C ANISOU 2376 CA VAL A 300 7798 6672 8264 174 -659 421 C ATOM 2377 C VAL A 300 -352.594-178.493 158.823 1.00 65.15 C ANISOU 2377 C VAL A 300 8502 7343 8911 134 -632 414 C ATOM 2378 O VAL A 300 -352.629-179.719 158.926 1.00 62.53 O ANISOU 2378 O VAL A 300 8195 6965 8596 124 -645 439 O ATOM 2379 CB VAL A 300 -350.838-177.064 159.964 1.00 61.93 C ANISOU 2379 CB VAL A 300 8087 6960 8483 141 -696 445 C ATOM 2380 CG1 VAL A 300 -350.868-178.042 161.127 1.00 58.82 C ANISOU 2380 CG1 VAL A 300 7756 6544 8048 94 -741 501 C ATOM 2381 CG2 VAL A 300 -349.449-176.462 159.809 1.00 67.63 C ANISOU 2381 CG2 VAL A 300 8765 7677 9254 173 -738 457 C ATOM 2382 N TYR A 301 -353.710-177.757 158.837 1.00 60.33 N ANISOU 2382 N TYR A 301 7876 6768 8279 111 -592 382 N ATOM 2383 CA TYR A 301 -354.978-178.391 159.174 1.00 60.19 C ANISOU 2383 CA TYR A 301 7867 6747 8254 63 -558 377 C ATOM 2384 C TYR A 301 -355.626-179.116 157.996 1.00 68.24 C ANISOU 2384 C TYR A 301 8865 7748 9315 65 -564 361 C ATOM 2385 O TYR A 301 -356.439-180.018 158.225 1.00 67.55 O ANISOU 2385 O TYR A 301 8789 7641 9237 21 -549 366 O ATOM 2386 CB TYR A 301 -355.955-177.375 159.797 1.00 56.64 C ANISOU 2386 CB TYR A 301 7391 6331 7798 34 -498 343 C ATOM 2387 CG TYR A 301 -356.544-176.294 158.902 1.00 62.70 C ANISOU 2387 CG TYR A 301 8082 7111 8628 68 -490 310 C ATOM 2388 CD1 TYR A 301 -357.440-176.603 157.881 1.00 71.16 C ANISOU 2388 CD1 TYR A 301 9104 8177 9757 69 -510 306 C ATOM 2389 CD2 TYR A 301 -356.263-174.950 159.135 1.00 58.05 C ANISOU 2389 CD2 TYR A 301 7476 6533 8049 90 -473 288 C ATOM 2390 CE1 TYR A 301 -357.989-175.616 157.087 1.00 71.14 C ANISOU 2390 CE1 TYR A 301 9034 8179 9817 95 -532 298 C ATOM 2391 CE2 TYR A 301 -356.816-173.955 158.351 1.00 59.55 C ANISOU 2391 CE2 TYR A 301 7596 6716 8313 122 -478 273 C ATOM 2392 CZ TYR A 301 -357.675-174.293 157.326 1.00 67.16 C ANISOU 2392 CZ TYR A 301 8509 7675 9333 126 -515 287 C ATOM 2393 OH TYR A 301 -358.229-173.310 156.537 1.00 71.93 O ANISOU 2393 OH TYR A 301 9046 8267 10019 154 -549 295 O ATOM 2394 N ASN A 302 -355.291-178.762 156.749 1.00 62.82 N ANISOU 2394 N ASN A 302 8160 7065 8645 100 -584 341 N ATOM 2395 CA ASN A 302 -355.832-179.528 155.625 1.00 59.51 C ANISOU 2395 CA ASN A 302 7747 6626 8236 81 -600 320 C ATOM 2396 C ASN A 302 -355.303-180.958 155.595 1.00 65.66 C ANISOU 2396 C ASN A 302 8576 7345 9027 76 -596 320 C ATOM 2397 O ASN A 302 -356.120-181.889 155.492 1.00 63.78 O ANISOU 2397 O ASN A 302 8353 7079 8803 31 -598 312 O ATOM 2398 CB ASN A 302 -355.575-178.794 154.305 1.00 54.12 C ANISOU 2398 CB ASN A 302 7063 5964 7537 98 -621 302 C ATOM 2399 CG ASN A 302 -356.686-177.829 153.951 1.00 65.54 C ANISOU 2399 CG ASN A 302 8456 7443 9001 83 -655 309 C ATOM 2400 OD1 ASN A 302 -357.785-177.891 154.510 1.00 63.74 O ANISOU 2400 OD1 ASN A 302 8180 7218 8820 58 -653 312 O ATOM 2401 ND2 ASN A 302 -356.410-176.933 153.008 1.00 68.50 N ANISOU 2401 ND2 ASN A 302 8837 7836 9356 95 -685 318 N ATOM 2402 N PRO A 303 -353.992-181.218 155.672 1.00 68.74 N ANISOU 2402 N PRO A 303 8982 7700 9435 119 -592 329 N ATOM 2403 CA PRO A 303 -353.555-182.622 155.744 1.00 69.95 C ANISOU 2403 CA PRO A 303 9168 7771 9638 123 -588 334 C ATOM 2404 C PRO A 303 -354.065-183.343 156.979 1.00 68.90 C ANISOU 2404 C PRO A 303 9059 7610 9509 84 -607 389 C ATOM 2405 O PRO A 303 -354.257-184.563 156.936 1.00 70.02 O ANISOU 2405 O PRO A 303 9234 7680 9691 63 -607 394 O ATOM 2406 CB PRO A 303 -352.021-182.518 155.729 1.00 70.73 C ANISOU 2406 CB PRO A 303 9245 7838 9792 186 -584 344 C ATOM 2407 CG PRO A 303 -351.725-181.133 156.170 1.00 70.24 C ANISOU 2407 CG PRO A 303 9149 7846 9691 198 -600 365 C ATOM 2408 CD PRO A 303 -352.835-180.303 155.614 1.00 66.18 C ANISOU 2408 CD PRO A 303 8633 7395 9115 167 -589 334 C ATOM 2409 N VAL A 304 -354.308-182.626 158.076 1.00 66.86 N ANISOU 2409 N VAL A 304 8797 7403 9203 63 -615 428 N ATOM 2410 CA VAL A 304 -354.873-183.259 159.264 1.00 64.28 C ANISOU 2410 CA VAL A 304 8514 7059 8850 2 -616 480 C ATOM 2411 C VAL A 304 -356.297-183.734 158.994 1.00 73.89 C ANISOU 2411 C VAL A 304 9725 8277 10073 -59 -577 452 C ATOM 2412 O VAL A 304 -356.698-184.820 159.432 1.00 72.39 O ANISOU 2412 O VAL A 304 9576 8033 9896 -109 -573 485 O ATOM 2413 CB VAL A 304 -354.809-182.292 160.462 1.00 62.55 C ANISOU 2413 CB VAL A 304 8312 6899 8555 -24 -613 507 C ATOM 2414 CG1 VAL A 304 -355.643-182.811 161.617 1.00 64.62 C ANISOU 2414 CG1 VAL A 304 8635 7159 8759 -114 -582 547 C ATOM 2415 CG2 VAL A 304 -353.369-182.093 160.904 1.00 64.06 C ANISOU 2415 CG2 VAL A 304 8516 7075 8749 15 -682 555 C ATOM 2416 N ILE A 305 -357.074-182.948 158.247 1.00 69.99 N ANISOU 2416 N ILE A 305 9173 7835 9583 -59 -557 399 N ATOM 2417 CA ILE A 305 -358.468-183.301 158.000 1.00 71.40 C ANISOU 2417 CA ILE A 305 9318 8017 9793 -120 -536 376 C ATOM 2418 C ILE A 305 -358.586-184.347 156.897 1.00 69.09 C ANISOU 2418 C ILE A 305 9046 7669 9536 -135 -569 348 C ATOM 2419 O ILE A 305 -359.330-185.323 157.034 1.00 75.76 O ANISOU 2419 O ILE A 305 9903 8472 10411 -198 -561 352 O ATOM 2420 CB ILE A 305 -359.279-182.034 157.675 1.00 70.40 C ANISOU 2420 CB ILE A 305 9106 7956 9687 -114 -524 344 C ATOM 2421 CG1 ILE A 305 -359.402-181.163 158.924 1.00 70.75 C ANISOU 2421 CG1 ILE A 305 9139 8037 9706 -121 -460 352 C ATOM 2422 CG2 ILE A 305 -360.662-182.392 157.138 1.00 72.15 C ANISOU 2422 CG2 ILE A 305 9264 8175 9976 -170 -532 323 C ATOM 2423 CD1 ILE A 305 -360.107-179.859 158.676 1.00 67.07 C ANISOU 2423 CD1 ILE A 305 8579 7609 9293 -100 -439 317 C ATOM 2424 N TYR A 306 -357.853-184.174 155.799 1.00 56.85 N ANISOU 2424 N TYR A 306 7509 6114 7976 -89 -595 311 N ATOM 2425 CA TYR A 306 -357.995-185.029 154.629 1.00 57.30 C ANISOU 2425 CA TYR A 306 7604 6124 8045 -117 -614 260 C ATOM 2426 C TYR A 306 -357.109-186.267 154.654 1.00 65.92 C ANISOU 2426 C TYR A 306 8760 7113 9175 -99 -593 254 C ATOM 2427 O TYR A 306 -357.349-187.193 153.871 1.00 74.58 O ANISOU 2427 O TYR A 306 9900 8148 10289 -138 -592 202 O ATOM 2428 CB TYR A 306 -357.710-184.232 153.356 1.00 54.03 C ANISOU 2428 CB TYR A 306 7193 5752 7583 -97 -637 217 C ATOM 2429 CG TYR A 306 -358.790-183.236 153.025 1.00 61.53 C ANISOU 2429 CG TYR A 306 8079 6774 8526 -127 -686 226 C ATOM 2430 CD1 TYR A 306 -358.774-181.952 153.572 1.00 65.86 C ANISOU 2430 CD1 TYR A 306 8565 7378 9081 -83 -681 260 C ATOM 2431 CD2 TYR A 306 -359.831-183.577 152.174 1.00 58.42 C ANISOU 2431 CD2 TYR A 306 7681 6381 8135 -200 -748 203 C ATOM 2432 CE1 TYR A 306 -359.770-181.039 153.275 1.00 68.50 C ANISOU 2432 CE1 TYR A 306 8824 7755 9447 -99 -727 273 C ATOM 2433 CE2 TYR A 306 -360.828-182.674 151.870 1.00 73.49 C ANISOU 2433 CE2 TYR A 306 9510 8342 10070 -221 -815 227 C ATOM 2434 CZ TYR A 306 -360.795-181.407 152.421 1.00 69.77 C ANISOU 2434 CZ TYR A 306 8967 7914 9629 -164 -801 263 C ATOM 2435 OH TYR A 306 -361.794-180.519 152.109 1.00 74.56 O ANISOU 2435 OH TYR A 306 9479 8551 10299 -176 -869 290 O ATOM 2436 N ILE A 307 -356.102-186.320 155.522 1.00 63.93 N ANISOU 2436 N ILE A 307 8512 6831 8947 -44 -584 305 N ATOM 2437 CA ILE A 307 -355.157-187.433 155.497 1.00 70.05 C ANISOU 2437 CA ILE A 307 9325 7491 9800 -10 -573 307 C ATOM 2438 C ILE A 307 -355.090-188.102 156.864 1.00 68.76 C ANISOU 2438 C ILE A 307 9181 7272 9672 -23 -601 403 C ATOM 2439 O ILE A 307 -355.310-189.311 156.982 1.00 70.87 O ANISOU 2439 O ILE A 307 9490 7438 10000 -55 -603 418 O ATOM 2440 CB ILE A 307 -353.769-186.962 155.031 1.00 67.11 C ANISOU 2440 CB ILE A 307 8930 7111 9458 74 -552 283 C ATOM 2441 CG1 ILE A 307 -353.840-186.505 153.574 1.00 66.69 C ANISOU 2441 CG1 ILE A 307 8891 7097 9351 64 -513 188 C ATOM 2442 CG2 ILE A 307 -352.752-188.068 155.186 1.00 64.31 C ANISOU 2442 CG2 ILE A 307 8581 6622 9230 124 -541 296 C ATOM 2443 CD1 ILE A 307 -352.711-185.604 153.168 1.00 72.62 C ANISOU 2443 CD1 ILE A 307 9609 7882 10100 125 -480 171 C ATOM 2444 N MET A 308 -354.799-187.324 157.907 1.00 71.53 N ANISOU 2444 N MET A 308 9517 7683 9976 -12 -627 472 N ATOM 2445 CA MET A 308 -354.712-187.889 159.247 1.00 78.26 C ANISOU 2445 CA MET A 308 10416 8493 10828 -46 -666 577 C ATOM 2446 C MET A 308 -356.044-188.445 159.736 1.00 81.29 C ANISOU 2446 C MET A 308 10837 8875 11175 -147 -637 596 C ATOM 2447 O MET A 308 -356.054-189.312 160.617 1.00 84.91 O ANISOU 2447 O MET A 308 11356 9263 11643 -193 -662 682 O ATOM 2448 CB MET A 308 -354.193-186.842 160.229 1.00 83.99 C ANISOU 2448 CB MET A 308 11138 9296 11479 -37 -700 632 C ATOM 2449 CG MET A 308 -352.783-186.363 159.941 1.00102.10 C ANISOU 2449 CG MET A 308 13385 11581 13828 52 -740 632 C ATOM 2450 SD MET A 308 -351.604-186.877 161.202 1.00123.04 S ANISOU 2450 SD MET A 308 16065 14159 16526 64 -858 770 S ATOM 2451 CE MET A 308 -352.336-186.150 162.667 1.00121.59 C ANISOU 2451 CE MET A 308 15966 14076 16156 -46 -873 829 C ATOM 2452 N MET A 309 -357.163-187.967 159.199 1.00 87.03 N ANISOU 2452 N MET A 309 11523 9672 11871 -188 -591 528 N ATOM 2453 CA MET A 309 -358.473-188.516 159.526 1.00 87.48 C ANISOU 2453 CA MET A 309 11589 9724 11928 -287 -553 534 C ATOM 2454 C MET A 309 -358.940-189.554 158.515 1.00 89.04 C ANISOU 2454 C MET A 309 11791 9841 12199 -316 -558 481 C ATOM 2455 O MET A 309 -360.009-190.143 158.697 1.00 96.64 O ANISOU 2455 O MET A 309 12753 10784 13183 -406 -533 485 O ATOM 2456 CB MET A 309 -359.502-187.390 159.649 1.00 82.63 C ANISOU 2456 CB MET A 309 10904 9221 11272 -321 -503 497 C ATOM 2457 CG MET A 309 -359.219-186.461 160.818 1.00 89.39 C ANISOU 2457 CG MET A 309 11777 10142 12046 -321 -474 537 C ATOM 2458 SD MET A 309 -360.532-185.285 161.190 1.00101.04 S ANISOU 2458 SD MET A 309 13167 11714 13509 -369 -377 486 S ATOM 2459 CE MET A 309 -359.942-184.666 162.763 1.00110.87 C ANISOU 2459 CE MET A 309 14501 12997 14628 -398 -337 533 C ATOM 2460 N ASN A 310 -358.170-189.782 157.457 1.00 86.39 N ANISOU 2460 N ASN A 310 11463 9458 11904 -253 -578 423 N ATOM 2461 CA ASN A 310 -358.412-190.903 156.560 1.00 92.38 C ANISOU 2461 CA ASN A 310 12257 10118 12726 -287 -577 363 C ATOM 2462 C ASN A 310 -357.989-192.192 157.260 1.00 89.81 C ANISOU 2462 C ASN A 310 11994 9650 12481 -295 -584 431 C ATOM 2463 O ASN A 310 -356.853-192.302 157.734 1.00 87.26 O ANISOU 2463 O ASN A 310 11685 9273 12198 -221 -606 488 O ATOM 2464 CB ASN A 310 -357.643-190.689 155.257 1.00 97.30 C ANISOU 2464 CB ASN A 310 12886 10732 13351 -225 -571 268 C ATOM 2465 CG ASN A 310 -357.913-191.761 154.222 1.00 98.68 C ANISOU 2465 CG ASN A 310 13117 10810 13569 -275 -558 178 C ATOM 2466 OD1 ASN A 310 -357.794-192.955 154.496 1.00 98.94 O ANISOU 2466 OD1 ASN A 310 13195 10710 13689 -292 -547 191 O ATOM 2467 ND2 ASN A 310 -358.267-191.335 153.016 1.00 94.00 N ANISOU 2467 ND2 ASN A 310 12531 10273 12910 -307 -565 87 N ATOM 2468 N LYS A 311 -358.905-193.163 157.331 1.00 98.74 N ANISOU 2468 N LYS A 311 13155 10712 13651 -388 -575 434 N ATOM 2469 CA LYS A 311 -358.672-194.363 158.134 1.00106.96 C ANISOU 2469 CA LYS A 311 14261 11611 14767 -414 -587 523 C ATOM 2470 C LYS A 311 -357.420-195.110 157.686 1.00 99.30 C ANISOU 2470 C LYS A 311 13320 10494 13914 -322 -601 506 C ATOM 2471 O LYS A 311 -356.671-195.634 158.520 1.00 89.94 O ANISOU 2471 O LYS A 311 12163 9212 12797 -285 -642 614 O ATOM 2472 CB LYS A 311 -359.896-195.278 158.063 1.00114.22 C ANISOU 2472 CB LYS A 311 15204 12473 15722 -538 -567 510 C ATOM 2473 CG LYS A 311 -359.887-196.440 159.046 1.00117.81 C ANISOU 2473 CG LYS A 311 15733 12790 16240 -592 -577 626 C ATOM 2474 CD LYS A 311 -361.133-197.297 158.871 1.00122.51 C ANISOU 2474 CD LYS A 311 16342 13329 16878 -725 -549 600 C ATOM 2475 CE LYS A 311 -361.256-198.347 159.961 1.00123.98 C ANISOU 2475 CE LYS A 311 16609 13389 17108 -802 -551 735 C ATOM 2476 NZ LYS A 311 -362.480-199.176 159.786 1.00124.40 N ANISOU 2476 NZ LYS A 311 16668 13384 17215 -942 -517 709 N ATOM 2477 N GLN A 312 -357.172-195.165 156.376 1.00100.75 N ANISOU 2477 N GLN A 312 13498 10655 14128 -289 -567 372 N ATOM 2478 CA GLN A 312 -356.011-195.890 155.868 1.00106.03 C ANISOU 2478 CA GLN A 312 14183 11171 14931 -202 -544 328 C ATOM 2479 C GLN A 312 -354.714-195.163 156.198 1.00106.87 C ANISOU 2479 C GLN A 312 14234 11308 15064 -83 -561 376 C ATOM 2480 O GLN A 312 -353.804-195.739 156.807 1.00109.94 O ANISOU 2480 O GLN A 312 14614 11574 15586 -17 -596 461 O ATOM 2481 CB GLN A 312 -356.137-196.096 154.358 1.00114.51 C ANISOU 2481 CB GLN A 312 15287 12221 16000 -222 -480 154 C ATOM 2482 CG GLN A 312 -356.901-197.339 153.959 1.00126.41 C ANISOU 2482 CG GLN A 312 16865 13598 17568 -318 -464 94 C ATOM 2483 CD GLN A 312 -356.823-197.606 152.469 1.00140.12 C ANISOU 2483 CD GLN A 312 18657 15292 19290 -343 -397 -89 C ATOM 2484 OE1 GLN A 312 -356.441-196.731 151.690 1.00140.51 O ANISOU 2484 OE1 GLN A 312 18696 15444 19246 -311 -367 -164 O ATOM 2485 NE2 GLN A 312 -357.181-198.820 152.065 1.00148.14 N ANISOU 2485 NE2 GLN A 312 19746 16151 20388 -412 -371 -162 N ATOM 2486 N PHE A 313 -354.609-193.892 155.788 1.00 99.20 N ANISOU 2486 N PHE A 313 13218 10493 13981 -58 -546 330 N ATOM 2487 CA PHE A 313 -353.387-193.124 156.015 1.00 88.05 C ANISOU 2487 CA PHE A 313 11744 9115 12595 44 -559 365 C ATOM 2488 C PHE A 313 -352.968-193.158 157.478 1.00 86.76 C ANISOU 2488 C PHE A 313 11571 8934 12460 62 -650 528 C ATOM 2489 O PHE A 313 -351.778-193.275 157.788 1.00 95.83 O ANISOU 2489 O PHE A 313 12675 10007 13727 147 -688 583 O ATOM 2490 CB PHE A 313 -353.579-191.675 155.559 1.00 85.35 C ANISOU 2490 CB PHE A 313 11367 8952 12110 43 -543 316 C ATOM 2491 CG PHE A 313 -353.308-191.448 154.097 1.00 82.97 C ANISOU 2491 CG PHE A 313 11072 8660 11792 58 -465 175 C ATOM 2492 CD1 PHE A 313 -352.010-191.292 153.635 1.00 83.53 C ANISOU 2492 CD1 PHE A 313 11103 8687 11947 146 -410 133 C ATOM 2493 CD2 PHE A 313 -354.353-191.368 153.187 1.00 81.10 C ANISOU 2493 CD2 PHE A 313 10883 8480 11453 -27 -449 89 C ATOM 2494 CE1 PHE A 313 -351.756-191.076 152.289 1.00 79.77 C ANISOU 2494 CE1 PHE A 313 10653 8224 11432 141 -316 -1 C ATOM 2495 CE2 PHE A 313 -354.107-191.152 151.840 1.00 75.98 C ANISOU 2495 CE2 PHE A 313 10270 7846 10754 -36 -385 -33 C ATOM 2496 CZ PHE A 313 -352.806-191.007 151.390 1.00 71.78 C ANISOU 2496 CZ PHE A 313 9718 7272 10285 44 -307 -82 C ATOM 2497 N ARG A 314 -353.937-193.075 158.391 1.00 82.74 N ANISOU 2497 N ARG A 314 11105 8487 11845 -28 -686 609 N ATOM 2498 CA ARG A 314 -353.614-192.990 159.811 1.00 90.25 C ANISOU 2498 CA ARG A 314 12079 9443 12768 -41 -772 763 C ATOM 2499 C ARG A 314 -352.874-194.236 160.282 1.00 94.35 C ANISOU 2499 C ARG A 314 12624 9774 13452 -9 -841 865 C ATOM 2500 O ARG A 314 -351.811-194.140 160.909 1.00 95.87 O ANISOU 2500 O ARG A 314 12789 9928 13710 52 -931 964 O ATOM 2501 CB ARG A 314 -354.892-192.778 160.622 1.00 90.81 C ANISOU 2501 CB ARG A 314 12206 9606 12693 -163 -759 809 C ATOM 2502 CG ARG A 314 -354.668-192.222 162.019 1.00 91.24 C ANISOU 2502 CG ARG A 314 12301 9726 12638 -200 -821 935 C ATOM 2503 CD ARG A 314 -355.917-192.362 162.887 1.00 99.56 C ANISOU 2503 CD ARG A 314 13428 10826 13572 -337 -778 983 C ATOM 2504 NE ARG A 314 -357.145-192.051 162.159 1.00106.66 N ANISOU 2504 NE ARG A 314 14280 11800 14445 -382 -677 866 N ATOM 2505 CZ ARG A 314 -358.018-192.962 161.739 1.00117.62 C ANISOU 2505 CZ ARG A 314 15678 13120 15893 -445 -638 836 C ATOM 2506 NH1 ARG A 314 -357.803-194.249 161.976 1.00125.16 N ANISOU 2506 NH1 ARG A 314 16697 13922 16935 -469 -676 909 N ATOM 2507 NH2 ARG A 314 -359.105-192.587 161.081 1.00122.00 N ANISOU 2507 NH2 ARG A 314 16173 13749 16434 -488 -572 738 N ATOM 2508 N ASN A 315 -353.415-195.419 159.973 1.00 98.22 N ANISOU 2508 N ASN A 315 13161 10133 14027 -50 -811 845 N ATOM 2509 CA ASN A 315 -352.792-196.663 160.417 1.00 93.99 C ANISOU 2509 CA ASN A 315 12649 9390 13670 -20 -879 949 C ATOM 2510 C ASN A 315 -351.414-196.851 159.793 1.00 84.60 C ANISOU 2510 C ASN A 315 11370 8085 12689 122 -879 906 C ATOM 2511 O ASN A 315 -350.492-197.357 160.444 1.00 91.35 O ANISOU 2511 O ASN A 315 12200 8811 13700 182 -982 1034 O ATOM 2512 CB ASN A 315 -353.697-197.848 160.083 1.00103.25 C ANISOU 2512 CB ASN A 315 13889 10439 14901 -97 -829 913 C ATOM 2513 CG ASN A 315 -355.053-197.755 160.757 1.00111.01 C ANISOU 2513 CG ASN A 315 14944 11521 15714 -244 -817 964 C ATOM 2514 OD1 ASN A 315 -355.224-197.029 161.736 1.00121.62 O ANISOU 2514 OD1 ASN A 315 16310 12988 16912 -291 -855 1059 O ATOM 2515 ND2 ASN A 315 -356.026-198.497 160.237 1.00103.98 N ANISOU 2515 ND2 ASN A 315 14088 10571 14847 -326 -755 892 N ATOM 2516 N CYS A 316 -351.256-196.447 158.532 1.00 75.50 N ANISOU 2516 N CYS A 316 10167 6973 11548 171 -766 731 N ATOM 2517 CA CYS A 316 -349.963-196.580 157.870 1.00 83.02 C ANISOU 2517 CA CYS A 316 11026 7819 12700 297 -725 666 C ATOM 2518 C CYS A 316 -348.923-195.651 158.484 1.00 87.33 C ANISOU 2518 C CYS A 316 11482 8441 13260 369 -811 758 C ATOM 2519 O CYS A 316 -347.751-196.023 158.612 1.00 90.11 O ANISOU 2519 O CYS A 316 11743 8660 13836 469 -853 808 O ATOM 2520 CB CYS A 316 -350.118-196.311 156.376 1.00 86.98 C ANISOU 2520 CB CYS A 316 11523 8361 13162 302 -570 454 C ATOM 2521 SG CYS A 316 -351.162-197.522 155.548 1.00 85.27 S ANISOU 2521 SG CYS A 316 11414 8025 12961 213 -482 329 S ATOM 2522 N MET A 317 -349.330-194.442 158.877 1.00 90.74 N ANISOU 2522 N MET A 317 11928 9076 13474 317 -839 780 N ATOM 2523 CA MET A 317 -348.397-193.531 159.530 1.00 87.66 C ANISOU 2523 CA MET A 317 11465 8760 13080 365 -932 867 C ATOM 2524 C MET A 317 -348.031-194.024 160.924 1.00 90.27 C ANISOU 2524 C MET A 317 11824 9015 13462 348 -1107 1072 C ATOM 2525 O MET A 317 -346.882-193.876 161.358 1.00 91.24 O ANISOU 2525 O MET A 317 11860 9090 13716 417 -1213 1160 O ATOM 2526 CB MET A 317 -348.990-192.127 159.592 1.00 94.71 C ANISOU 2526 CB MET A 317 12380 9873 13732 307 -908 828 C ATOM 2527 CG MET A 317 -349.216-191.520 158.226 1.00104.71 C ANISOU 2527 CG MET A 317 13619 11217 14948 323 -767 653 C ATOM 2528 SD MET A 317 -349.721-189.797 158.262 1.00102.33 S ANISOU 2528 SD MET A 317 13318 11143 14420 278 -755 621 S ATOM 2529 CE MET A 317 -349.766-189.459 156.507 1.00104.53 C ANISOU 2529 CE MET A 317 13576 11450 14689 301 -610 441 C ATOM 2530 N VAL A 318 -348.994-194.609 161.641 1.00 88.87 N ANISOU 2530 N VAL A 318 11765 8822 13179 245 -1146 1156 N ATOM 2531 CA VAL A 318 -348.698-195.196 162.945 1.00 91.42 C ANISOU 2531 CA VAL A 318 12146 9059 13532 207 -1317 1365 C ATOM 2532 C VAL A 318 -347.682-196.318 162.798 1.00 95.31 C ANISOU 2532 C VAL A 318 12561 9314 14340 313 -1387 1430 C ATOM 2533 O VAL A 318 -346.698-196.395 163.544 1.00105.05 O ANISOU 2533 O VAL A 318 13745 10478 15691 355 -1554 1583 O ATOM 2534 CB VAL A 318 -349.989-195.694 163.617 1.00 96.13 C ANISOU 2534 CB VAL A 318 12893 9673 13961 65 -1310 1429 C ATOM 2535 CG1 VAL A 318 -349.662-196.510 164.866 1.00101.41 C ANISOU 2535 CG1 VAL A 318 13644 10218 14670 16 -1486 1656 C ATOM 2536 CG2 VAL A 318 -350.897-194.527 163.953 1.00 88.36 C ANISOU 2536 CG2 VAL A 318 11965 8911 12698 -34 -1248 1381 C ATOM 2537 N THR A 319 -347.906-197.205 161.825 1.00 94.11 N ANISOU 2537 N THR A 319 12393 9026 14340 354 -1263 1312 N ATOM 2538 CA THR A 319 -346.966-198.293 161.578 1.00 96.41 C ANISOU 2538 CA THR A 319 12598 9065 14967 465 -1295 1344 C ATOM 2539 C THR A 319 -345.598-197.759 161.172 1.00 94.16 C ANISOU 2539 C THR A 319 12138 8763 14875 600 -1297 1305 C ATOM 2540 O THR A 319 -344.564-198.296 161.586 1.00 94.09 O ANISOU 2540 O THR A 319 12030 8587 15134 687 -1421 1427 O ATOM 2541 CB THR A 319 -347.515-199.221 160.495 1.00 96.15 C ANISOU 2541 CB THR A 319 12593 8902 15036 471 -1127 1180 C ATOM 2542 OG1 THR A 319 -348.867-199.579 160.808 1.00102.55 O ANISOU 2542 OG1 THR A 319 13552 9756 15656 332 -1114 1202 O ATOM 2543 CG2 THR A 319 -346.679-200.473 160.414 1.00 95.22 C ANISOU 2543 CG2 THR A 319 12406 8494 15279 574 -1158 1227 C ATOM 2544 N THR A 320 -345.574-196.697 160.364 1.00 87.34 N ANISOU 2544 N THR A 320 11228 8066 13893 614 -1166 1143 N ATOM 2545 CA THR A 320 -344.306-196.134 159.912 1.00 88.68 C ANISOU 2545 CA THR A 320 11228 8227 14240 728 -1141 1093 C ATOM 2546 C THR A 320 -343.586-195.416 161.046 1.00 95.85 C ANISOU 2546 C THR A 320 12081 9210 15127 727 -1348 1272 C ATOM 2547 O THR A 320 -342.364-195.544 161.194 1.00 96.97 O ANISOU 2547 O THR A 320 12069 9240 15536 826 -1434 1340 O ATOM 2548 CB THR A 320 -344.550-195.189 158.734 1.00 81.34 C ANISOU 2548 CB THR A 320 10289 7455 13162 721 -944 882 C ATOM 2549 OG1 THR A 320 -344.957-195.948 157.589 1.00 77.03 O ANISOU 2549 OG1 THR A 320 9781 6808 12677 728 -762 710 O ATOM 2550 CG2 THR A 320 -343.294-194.392 158.390 1.00 76.61 C ANISOU 2550 CG2 THR A 320 9524 6884 12698 812 -917 845 C ATOM 2551 N LEU A 321 -344.322-194.666 161.859 1.00 97.18 N ANISOU 2551 N LEU A 321 12372 9559 14992 611 -1430 1346 N ATOM 2552 CA LEU A 321 -343.725-193.947 162.978 1.00103.78 C ANISOU 2552 CA LEU A 321 13193 10478 15762 581 -1630 1505 C ATOM 2553 C LEU A 321 -343.291-194.909 164.082 1.00115.14 C ANISOU 2553 C LEU A 321 14653 11754 17341 573 -1858 1735 C ATOM 2554 O LEU A 321 -342.396-194.601 164.869 1.00120.94 O ANISOU 2554 O LEU A 321 15326 12484 18142 581 -2057 1882 O ATOM 2555 CB LEU A 321 -344.703-192.905 163.526 1.00 95.16 C ANISOU 2555 CB LEU A 321 12244 9613 14302 448 -1624 1496 C ATOM 2556 CG LEU A 321 -344.874-191.681 162.621 1.00 87.11 C ANISOU 2556 CG LEU A 321 11178 8759 13160 462 -1461 1314 C ATOM 2557 CD1 LEU A 321 -345.973-190.762 163.132 1.00 80.58 C ANISOU 2557 CD1 LEU A 321 10486 8124 12008 339 -1437 1297 C ATOM 2558 CD2 LEU A 321 -343.554-190.933 162.483 1.00 77.90 C ANISOU 2558 CD2 LEU A 321 9854 7608 12138 542 -1511 1314 C ATOM 2559 N CYS A 322 -343.920-196.078 164.128 1.00117.96 N ANISOU 2559 N CYS A 322 15099 11971 17748 549 -1843 1774 N ATOM 2560 CA CYS A 322 -343.587-197.070 165.119 1.00128.07 C ANISOU 2560 CA CYS A 322 16417 13078 19164 535 -2059 2005 C ATOM 2561 C CYS A 322 -342.572-198.118 164.666 1.00126.97 C ANISOU 2561 C CYS A 322 16110 12668 19467 688 -2090 2033 C ATOM 2562 O CYS A 322 -342.533-199.269 165.113 1.00122.94 O ANISOU 2562 O CYS A 322 15633 11952 19127 695 -2204 2179 O ATOM 2563 CB CYS A 322 -344.802-197.771 165.718 1.00137.69 C ANISOU 2563 CB CYS A 322 17844 14281 20189 399 -2067 2086 C ATOM 2564 SG CYS A 322 -345.068-197.350 167.415 1.00144.14 S ANISOU 2564 SG CYS A 322 18845 15222 20698 225 -2296 2324 S ATOM 2565 N CYS A 323 -341.730-197.693 163.727 1.00126.06 N ANISOU 2565 N CYS A 323 15804 12542 19550 813 -1971 1883 N ATOM 2566 CA CYS A 323 -340.608-198.495 163.238 1.00127.85 C ANISOU 2566 CA CYS A 323 15828 12519 20232 974 -1968 1880 C ATOM 2567 C CYS A 323 -341.040-199.837 162.642 1.00124.10 C ANISOU 2567 C CYS A 323 15389 11819 19945 1014 -1839 1810 C ATOM 2568 O CYS A 323 -340.210-200.721 162.424 1.00128.66 O ANISOU 2568 O CYS A 323 15819 12142 20924 1140 -1856 1837 O ATOM 2569 CB CYS A 323 -339.599-198.731 164.366 1.00133.54 C ANISOU 2569 CB CYS A 323 16454 13123 21160 1005 -2285 2149 C ATOM 2570 SG CYS A 323 -339.394-197.317 165.476 1.00136.08 S ANISOU 2570 SG CYS A 323 16831 13710 21164 886 -2508 2288 S ATOM 2571 N GLY A 324 -342.340-199.987 162.380 1.00114.47 N ANISOU 2571 N GLY A 324 14357 10682 18453 906 -1710 1715 N ATOM 2572 CA GLY A 324 -342.895-201.184 161.773 1.00105.54 C ANISOU 2572 CA GLY A 324 13287 9360 17454 916 -1576 1625 C ATOM 2573 C GLY A 324 -343.952-201.869 162.618 1.00108.72 C ANISOU 2573 C GLY A 324 13890 9734 17684 782 -1683 1776 C ATOM 2574 O GLY A 324 -344.838-202.534 162.072 1.00108.00 O ANISOU 2574 O GLY A 324 13899 9581 17554 732 -1541 1663 O ATOM 2575 N LYS A 325 -343.871-201.725 163.935 1.00121.19 N ANISOU 2575 N LYS A 325 15536 11356 19155 710 -1929 2027 N ATOM 2576 CA LYS A 325 -344.800-202.389 164.835 1.00130.85 C ANISOU 2576 CA LYS A 325 16957 12544 20214 569 -2033 2193 C ATOM 2577 C LYS A 325 -346.052-201.537 165.039 1.00133.11 C ANISOU 2577 C LYS A 325 17407 13109 20061 406 -1942 2125 C ATOM 2578 O LYS A 325 -346.110-200.369 164.651 1.00130.36 O ANISOU 2578 O LYS A 325 17018 12977 19534 406 -1848 1989 O ATOM 2579 CB LYS A 325 -344.119-202.687 166.171 1.00132.65 C ANISOU 2579 CB LYS A 325 17204 12677 20521 549 -2345 2506 C ATOM 2580 CG LYS A 325 -342.909-203.613 166.065 1.00135.02 C ANISOU 2580 CG LYS A 325 17325 12670 21305 713 -2465 2605 C ATOM 2581 CD LYS A 325 -343.297-204.982 165.519 1.00133.69 C ANISOU 2581 CD LYS A 325 17184 12235 21378 751 -2353 2553 C ATOM 2582 CE LYS A 325 -342.173-205.994 165.692 1.00141.30 C ANISOU 2582 CE LYS A 325 17984 12964 22740 878 -2469 2656 C ATOM 2583 NZ LYS A 325 -340.975-205.669 164.869 1.00146.72 N ANISOU 2583 NZ LYS A 325 18404 13619 23725 1055 -2370 2498 N ATOM 2584 N ASN A 326 -347.064-202.147 165.653 1.00138.79 N ANISOU 2584 N ASN A 326 18303 13806 20624 266 -1964 2224 N ATOM 2585 CA ASN A 326 -348.345-201.490 165.922 1.00141.01 C ANISOU 2585 CA ASN A 326 18732 14320 20527 105 -1867 2170 C ATOM 2586 C ASN A 326 -348.943-200.889 164.649 1.00135.18 C ANISOU 2586 C ASN A 326 17936 13715 19709 130 -1627 1889 C ATOM 2587 O ASN A 326 -350.148-200.981 164.414 1.00132.29 O ANISOU 2587 O ASN A 326 17662 13420 19183 24 -1502 1802 O ATOM 2588 CB ASN A 326 -348.179-200.408 166.996 1.00144.95 C ANISOU 2588 CB ASN A 326 19290 15022 20762 22 -2000 2294 C ATOM 2589 CG ASN A 326 -349.505-199.965 167.598 1.00146.62 C ANISOU 2589 CG ASN A 326 19675 15421 20613 -164 -1920 2292 C ATOM 2590 OD1 ASN A 326 -350.509-199.829 166.899 1.00144.89 O ANISOU 2590 OD1 ASN A 326 19465 15283 20302 -202 -1725 2118 O ATOM 2591 ND2 ASN A 326 -349.510-199.737 168.907 1.00148.91 N ANISOU 2591 ND2 ASN A 326 20102 15778 20701 -290 -2070 2485 N TER 2592 ASN A 326 HETATM 2593 C1 NAG B 1 -339.871-140.780 151.729 1.00 62.01 C ANISOU 2593 C1 NAG B 1 8208 4657 10695 -901 -473 966 C HETATM 2594 C2 NAG B 1 -339.176-141.443 150.537 1.00 61.71 C ANISOU 2594 C2 NAG B 1 8171 4769 10505 -969 -436 1116 C HETATM 2595 C3 NAG B 1 -337.656-141.265 150.630 1.00 63.55 C ANISOU 2595 C3 NAG B 1 8349 5042 10755 -1123 -370 1087 C HETATM 2596 C4 NAG B 1 -337.261-139.825 150.936 1.00 65.89 C ANISOU 2596 C4 NAG B 1 8672 5121 11243 -1221 -374 1077 C HETATM 2597 C5 NAG B 1 -338.086-139.268 152.094 1.00 69.19 C ANISOU 2597 C5 NAG B 1 9108 5398 11784 -1140 -426 924 C HETATM 2598 C6 NAG B 1 -337.884-137.787 152.316 1.00 66.42 C ANISOU 2598 C6 NAG B 1 8802 4795 11639 -1224 -428 915 C HETATM 2599 C7 NAG B 1 -339.868-143.495 149.360 1.00 63.42 C ANISOU 2599 C7 NAG B 1 8399 5283 10414 -860 -435 1226 C HETATM 2600 C8 NAG B 1 -340.142-144.963 149.504 1.00 57.71 C ANISOU 2600 C8 NAG B 1 7632 4761 9533 -778 -429 1161 C HETATM 2601 N2 NAG B 1 -339.507-142.858 150.479 1.00 59.89 N ANISOU 2601 N2 NAG B 1 7907 4747 10102 -884 -435 1089 N HETATM 2602 O3 NAG B 1 -337.059-141.665 149.401 1.00 62.62 O ANISOU 2602 O3 NAG B 1 8245 5021 10526 -1197 -302 1234 O HETATM 2603 O4 NAG B 1 -335.892-139.836 151.325 1.00 73.02 O ANISOU 2603 O4 NAG B 1 9490 6085 12169 -1354 -331 1006 O HETATM 2604 O5 NAG B 1 -339.479-139.442 151.818 1.00 63.86 O ANISOU 2604 O5 NAG B 1 8476 4683 11104 -991 -467 976 O HETATM 2605 O6 NAG B 1 -338.397-137.036 151.224 1.00 76.34 O ANISOU 2605 O6 NAG B 1 10137 5892 12977 -1215 -443 1114 O HETATM 2606 O7 NAG B 1 -339.970-142.916 148.284 1.00 72.26 O ANISOU 2606 O7 NAG B 1 9602 6320 11532 -912 -443 1397 O HETATM 2607 C1 NAG B 2 -335.098-138.876 150.606 1.00 66.51 C ANISOU 2607 C1 NAG B 2 8689 5141 11440 -1501 -280 1123 C HETATM 2608 C2 NAG B 2 -333.858-138.609 151.452 1.00 67.23 C ANISOU 2608 C2 NAG B 2 8678 5237 11628 -1632 -271 996 C HETATM 2609 C3 NAG B 2 -332.942-137.621 150.739 1.00 69.31 C ANISOU 2609 C3 NAG B 2 8949 5379 12007 -1803 -205 1112 C HETATM 2610 C4 NAG B 2 -332.624-138.124 149.336 1.00 69.44 C ANISOU 2610 C4 NAG B 2 8979 5501 11902 -1844 -100 1290 C HETATM 2611 C5 NAG B 2 -333.904-138.440 148.575 1.00 68.64 C ANISOU 2611 C5 NAG B 2 9003 5406 11671 -1714 -130 1408 C HETATM 2612 C6 NAG B 2 -333.663-139.061 147.221 1.00 69.34 C ANISOU 2612 C6 NAG B 2 9134 5618 11593 -1761 -30 1566 C HETATM 2613 C7 NAG B 2 -334.287-138.914 153.845 1.00 72.85 C ANISOU 2613 C7 NAG B 2 9352 5973 12356 -1552 -398 657 C HETATM 2614 C8 NAG B 2 -334.698-138.254 155.125 1.00 71.31 C ANISOU 2614 C8 NAG B 2 9210 5647 12239 -1552 -455 475 C HETATM 2615 N2 NAG B 2 -334.227-138.120 152.771 1.00 69.20 N ANISOU 2615 N2 NAG B 2 8942 5384 11968 -1605 -347 819 N HETATM 2616 O3 NAG B 2 -331.735-137.479 151.479 1.00 71.40 O ANISOU 2616 O3 NAG B 2 9094 5666 12368 -1933 -204 998 O HETATM 2617 O4 NAG B 2 -331.928-137.121 148.610 1.00 80.49 O ANISOU 2617 O4 NAG B 2 10415 6768 13400 -2008 -28 1416 O HETATM 2618 O5 NAG B 2 -334.707-139.362 149.322 1.00 67.24 O ANISOU 2618 O5 NAG B 2 8795 5340 11414 -1552 -199 1284 O HETATM 2619 O6 NAG B 2 -334.804-138.953 146.383 1.00 68.88 O ANISOU 2619 O6 NAG B 2 9225 5505 11442 -1689 -85 1718 O HETATM 2620 O7 NAG B 2 -334.008-140.107 153.787 1.00 82.06 O ANISOU 2620 O7 NAG B 2 10441 7343 13396 -1513 -393 655 O HETATM 2621 C1 BMA B 3 -330.591-137.532 148.284 1.00 90.84 C ANISOU 2621 C1 BMA B 3 11601 8203 14712 -2142 90 1420 C HETATM 2622 C2 BMA B 3 -330.126-136.509 147.267 1.00 95.28 C ANISOU 2622 C2 BMA B 3 12246 8623 15336 -2307 183 1593 C HETATM 2623 C3 BMA B 3 -328.663-136.725 146.913 1.00104.20 C ANISOU 2623 C3 BMA B 3 13233 9846 16514 -2474 335 1597 C HETATM 2624 C4 BMA B 3 -327.790-136.866 148.169 1.00122.50 C ANISOU 2624 C4 BMA B 3 15351 12205 18989 -2507 277 1408 C HETATM 2625 C5 BMA B 3 -328.392-137.888 149.150 1.00126.31 C ANISOU 2625 C5 BMA B 3 15782 12823 19388 -2328 156 1256 C HETATM 2626 C6 BMA B 3 -327.655-137.904 150.472 1.00134.25 C ANISOU 2626 C6 BMA B 3 16632 13847 20532 -2372 54 1083 C HETATM 2627 O2 BMA B 3 -330.231-135.207 147.828 1.00 92.16 O ANISOU 2627 O2 BMA B 3 11898 7993 15127 -2361 104 1572 O HETATM 2628 O3 BMA B 3 -328.190-135.650 146.125 1.00 98.24 O ANISOU 2628 O3 BMA B 3 12553 8936 15836 -2649 423 1745 O HETATM 2629 O4 BMA B 3 -326.490-137.294 147.797 1.00134.84 O ANISOU 2629 O4 BMA B 3 16744 13879 20609 -2633 419 1412 O HETATM 2630 O5 BMA B 3 -329.756-137.526 149.421 1.00111.13 O ANISOU 2630 O5 BMA B 3 14020 10794 17411 -2196 47 1254 O HETATM 2631 O6 BMA B 3 -328.006-136.713 151.170 1.00135.86 O ANISOU 2631 O6 BMA B 3 16928 13847 20846 -2412 -46 1027 O HETATM 2632 C1 MAN B 4 -328.249-135.980 144.720 1.00 98.48 C ANISOU 2632 C1 MAN B 4 12696 9036 15686 -2700 563 1919 C HETATM 2633 C2 MAN B 4 -327.293-135.010 144.006 1.00105.19 C ANISOU 2633 C2 MAN B 4 13567 9766 16635 -2933 702 2046 C HETATM 2634 C3 MAN B 4 -327.843-133.587 144.094 1.00103.92 C ANISOU 2634 C3 MAN B 4 13554 9334 16598 -2971 585 2144 C HETATM 2635 C4 MAN B 4 -329.286-133.506 143.576 1.00103.94 C ANISOU 2635 C4 MAN B 4 13767 9267 16457 -2836 467 2279 C HETATM 2636 C5 MAN B 4 -330.164-134.529 144.263 1.00105.83 C ANISOU 2636 C5 MAN B 4 13960 9646 16606 -2610 354 2138 C HETATM 2637 C6 MAN B 4 -331.510-134.613 143.599 1.00100.09 C ANISOU 2637 C6 MAN B 4 13415 8884 15732 -2490 253 2283 C HETATM 2638 O2 MAN B 4 -327.215-135.318 142.621 1.00112.58 O ANISOU 2638 O2 MAN B 4 14623 10776 17375 -3021 866 2211 O HETATM 2639 O3 MAN B 4 -327.032-132.672 143.376 1.00109.36 O ANISOU 2639 O3 MAN B 4 14285 9898 17368 -3194 711 2282 O HETATM 2640 O4 MAN B 4 -329.830-132.213 143.825 1.00109.20 O ANISOU 2640 O4 MAN B 4 14539 9660 17292 -2841 343 2345 O HETATM 2641 O5 MAN B 4 -329.561-135.859 144.194 1.00105.52 O ANISOU 2641 O5 MAN B 4 13789 9866 16438 -2593 468 2043 O HETATM 2642 O6 MAN B 4 -332.389-135.344 144.483 1.00 87.19 O ANISOU 2642 O6 MAN B 4 11721 7330 14077 -2279 132 2130 O HETATM 2643 C1 MAN B 5 -327.548-136.820 152.531 1.00139.31 C ANISOU 2643 C1 MAN B 5 17262 14312 21359 -2440 -173 847 C HETATM 2644 C2 MAN B 5 -328.419-135.858 153.407 1.00138.98 C ANISOU 2644 C2 MAN B 5 17370 14078 21360 -2411 -281 744 C HETATM 2645 C3 MAN B 5 -327.973-134.384 153.291 1.00141.19 C ANISOU 2645 C3 MAN B 5 17698 14120 21829 -2578 -263 774 C HETATM 2646 C4 MAN B 5 -326.432-134.223 153.253 1.00144.95 C ANISOU 2646 C4 MAN B 5 17999 14629 22446 -2779 -233 781 C HETATM 2647 C5 MAN B 5 -325.837-135.177 152.215 1.00142.33 C ANISOU 2647 C5 MAN B 5 17543 14484 22051 -2776 -100 908 C HETATM 2648 C6 MAN B 5 -324.329-135.087 152.104 1.00134.01 C ANISOU 2648 C6 MAN B 5 16285 13465 21166 -2964 -44 919 C HETATM 2649 O2 MAN B 5 -328.343-136.183 154.800 1.00142.05 O ANISOU 2649 O2 MAN B 5 17716 14523 21734 -2402 -415 553 O HETATM 2650 O3 MAN B 5 -328.523-133.599 154.351 1.00139.41 O ANISOU 2650 O3 MAN B 5 17573 13727 21668 -2574 -363 623 O HETATM 2651 O4 MAN B 5 -326.079-132.879 152.917 1.00145.90 O ANISOU 2651 O4 MAN B 5 18176 14524 22734 -2936 -191 843 O HETATM 2652 O5 MAN B 5 -326.169-136.523 152.597 1.00143.46 O ANISOU 2652 O5 MAN B 5 17627 14835 22046 -2621 -148 840 O HETATM 2653 O6 MAN B 5 -323.901-136.088 151.184 1.00127.60 O ANISOU 2653 O6 MAN B 5 15363 12829 20289 -2935 103 1010 O HETATM 2654 C1 PLM A 401 -345.735-195.758 167.357 1.00125.35 C ANISOU 2654 C1 PLM A 401 16521 13146 17959 140 -2160 2167 C HETATM 2655 O2 PLM A 401 -346.768-195.439 166.768 1.00121.70 O ANISOU 2655 O2 PLM A 401 16105 12792 17342 100 -1957 2003 O HETATM 2656 C2 PLM A 401 -344.978-194.862 168.295 1.00117.89 C ANISOU 2656 C2 PLM A 401 15583 12307 16905 95 -2351 2285 C HETATM 2657 C3 PLM A 401 -343.470-194.998 168.190 1.00115.36 C ANISOU 2657 C3 PLM A 401 15069 11856 16906 229 -2519 2368 C HETATM 2658 C4 PLM A 401 -342.730-194.220 169.264 1.00109.56 C ANISOU 2658 C4 PLM A 401 14358 11213 16058 157 -2759 2518 C HETATM 2659 C5 PLM A 401 -342.749-192.723 169.012 1.00104.30 C ANISOU 2659 C5 PLM A 401 13663 10764 15201 137 -2653 2358 C HETATM 2660 C6 PLM A 401 -342.710-191.942 170.311 1.00 98.54 C ANISOU 2660 C6 PLM A 401 13088 10172 14180 -24 -2834 2480 C HETATM 2661 C7 PLM A 401 -342.121-190.555 170.145 1.00 90.50 C ANISOU 2661 C7 PLM A 401 11976 9301 13110 -10 -2826 2375 C HETATM 2662 C8 PLM A 401 -343.162-189.527 169.753 1.00 88.09 C ANISOU 2662 C8 PLM A 401 11751 9182 12537 -64 -2577 2170 C HETATM 2663 C9 PLM A 401 -342.748-188.129 170.171 1.00 79.48 C ANISOU 2663 C9 PLM A 401 10667 8244 11288 -127 -2631 2128 C HETATM 2664 CA PLM A 401 -343.331-187.084 169.243 1.00 84.00 C ANISOU 2664 CA PLM A 401 11193 8945 11779 -89 -2374 1899 C HETATM 2665 CB PLM A 401 -343.466-185.734 169.920 1.00 90.71 C ANISOU 2665 CB PLM A 401 12143 9956 12366 -207 -2385 1849 C HETATM 2666 CC PLM A 401 -342.193-184.917 169.832 1.00 94.86 C ANISOU 2666 CC PLM A 401 12521 10497 13023 -162 -2509 1852 C HETATM 2667 CD PLM A 401 -342.424-183.508 170.339 1.00 93.30 C ANISOU 2667 CD PLM A 401 12424 10453 12574 -274 -2479 1764 C HETATM 2668 CE PLM A 401 -341.300-182.565 169.957 1.00 89.84 C ANISOU 2668 CE PLM A 401 11816 10035 12282 -218 -2539 1720 C HETATM 2669 CF PLM A 401 -341.499-181.199 170.583 1.00 89.82 C ANISOU 2669 CF PLM A 401 11933 10166 12030 -345 -2529 1642 C HETATM 2670 CG PLM A 401 -341.091-180.074 169.666 1.00 79.48 C ANISOU 2670 CG PLM A 401 10471 8902 10827 -268 -2410 1498 C HETATM 2671 C1 BOG A 407 -352.586-166.623 149.698 1.00 73.68 C ANISOU 2671 C1 BOG A 407 9520 8406 10071 155 -773 613 C HETATM 2672 O1 BOG A 407 -353.118-167.549 150.645 1.00 74.16 O ANISOU 2672 O1 BOG A 407 9531 8487 10159 186 -755 550 O HETATM 2673 C2 BOG A 407 -352.965-165.207 150.121 1.00 71.19 C ANISOU 2673 C2 BOG A 407 9150 8020 9878 185 -805 647 C HETATM 2674 O2 BOG A 407 -354.390-165.055 150.067 1.00 63.79 O ANISOU 2674 O2 BOG A 407 8158 7049 9028 210 -889 680 O HETATM 2675 C3 BOG A 407 -352.284-164.167 149.244 1.00 73.67 C ANISOU 2675 C3 BOG A 407 9520 8301 10170 147 -819 721 C HETATM 2676 O3 BOG A 407 -352.565-162.856 149.745 1.00 81.62 O ANISOU 2676 O3 BOG A 407 10474 9223 11315 180 -840 742 O HETATM 2677 C4 BOG A 407 -350.783-164.414 149.239 1.00 66.95 C ANISOU 2677 C4 BOG A 407 8704 7486 9248 116 -719 682 C HETATM 2678 O4 BOG A 407 -350.154-163.523 148.316 1.00 71.15 O ANISOU 2678 O4 BOG A 407 9296 7991 9747 62 -715 754 O HETATM 2679 C5 BOG A 407 -350.492-165.840 148.791 1.00 69.21 C ANISOU 2679 C5 BOG A 407 9033 7841 9423 92 -677 641 C HETATM 2680 O5 BOG A 407 -351.167-166.790 149.619 1.00 68.56 O ANISOU 2680 O5 BOG A 407 8903 7779 9367 134 -687 585 O HETATM 2681 C6 BOG A 407 -348.998-166.132 148.829 1.00 64.89 C ANISOU 2681 C6 BOG A 407 8488 7315 8852 74 -568 598 C HETATM 2682 O6 BOG A 407 -348.611-166.329 150.192 1.00 69.59 O ANISOU 2682 O6 BOG A 407 9004 7909 9529 122 -547 538 O HETATM 2683 C1' BOG A 407 -353.239-168.852 150.079 1.00 75.21 C ANISOU 2683 C1' BOG A 407 9710 8662 10204 158 -756 533 C HETATM 2684 C2' BOG A 407 -353.951-169.774 151.059 1.00 79.22 C ANISOU 2684 C2' BOG A 407 10168 9181 10751 182 -746 483 C HETATM 2685 C3' BOG A 407 -354.153-171.150 150.443 1.00 80.13 C ANISOU 2685 C3' BOG A 407 10334 9324 10788 148 -753 462 C HETATM 2686 C4' BOG A 407 -355.464-171.763 150.917 1.00 82.52 C ANISOU 2686 C4' BOG A 407 10584 9625 11144 149 -792 451 C HETATM 2687 C5' BOG A 407 -355.689-173.106 150.236 1.00 86.53 C ANISOU 2687 C5' BOG A 407 11150 10150 11578 103 -807 429 C HETATM 2688 C6' BOG A 407 -356.748-173.923 150.966 1.00 86.27 C ANISOU 2688 C6' BOG A 407 11061 10113 11605 100 -817 406 C HETATM 2689 C7' BOG A 407 -358.119-173.265 150.882 1.00 80.76 C ANISOU 2689 C7' BOG A 407 10278 9403 11005 97 -898 447 C HETATM 2690 C8' BOG A 407 -359.090-173.976 151.800 1.00 77.86 C ANISOU 2690 C8' BOG A 407 9836 9029 10717 93 -871 417 C HETATM 2691 C1 BOG A 408 -348.640-159.861 157.093 1.00 95.71 C ANISOU 2691 C1 BOG A 408 12179 10870 13316 122 -541 257 C HETATM 2692 O1 BOG A 408 -349.393-158.708 157.464 1.00 97.13 O ANISOU 2692 O1 BOG A 408 12358 10944 13602 135 -507 210 O HETATM 2693 C2 BOG A 408 -349.445-160.743 156.141 1.00 96.13 C ANISOU 2693 C2 BOG A 408 12215 10966 13343 170 -558 322 C HETATM 2694 O2 BOG A 408 -350.673-161.120 156.767 1.00 96.79 O ANISOU 2694 O2 BOG A 408 12286 11048 13442 203 -532 272 O HETATM 2695 C3 BOG A 408 -348.665-161.995 155.769 1.00 94.18 C ANISOU 2695 C3 BOG A 408 11972 10813 12999 158 -573 352 C HETATM 2696 O3 BOG A 408 -349.358-162.693 154.724 1.00 89.63 O ANISOU 2696 O3 BOG A 408 11398 10266 12392 187 -588 408 O HETATM 2697 C4 BOG A 408 -347.265-161.614 155.300 1.00 89.98 C ANISOU 2697 C4 BOG A 408 11434 10282 12472 116 -573 385 C HETATM 2698 O4 BOG A 408 -346.479-162.805 155.162 1.00 89.83 O ANISOU 2698 O4 BOG A 408 11399 10335 12397 111 -570 392 O HETATM 2699 C5 BOG A 408 -346.574-160.658 156.275 1.00 83.59 C ANISOU 2699 C5 BOG A 408 10624 9427 11710 71 -575 332 C HETATM 2700 O5 BOG A 408 -347.380-159.503 156.521 1.00 89.04 O ANISOU 2700 O5 BOG A 408 11330 10027 12475 81 -561 305 O HETATM 2701 C6 BOG A 408 -345.200-160.220 155.772 1.00 75.30 C ANISOU 2701 C6 BOG A 408 9548 8371 10693 22 -574 369 C HETATM 2702 O6 BOG A 408 -345.321-159.448 154.572 1.00 73.66 O ANISOU 2702 O6 BOG A 408 9354 8113 10520 18 -553 440 O HETATM 2703 C1' BOG A 408 -349.514-158.643 158.882 1.00 96.28 C ANISOU 2703 C1' BOG A 408 12285 10831 13466 101 -461 93 C HETATM 2704 C2' BOG A 408 -350.928-159.088 159.235 1.00 96.44 C ANISOU 2704 C2' BOG A 408 12286 10848 13508 148 -406 50 C HETATM 2705 C3' BOG A 408 -351.097-159.405 160.715 1.00 99.50 C ANISOU 2705 C3' BOG A 408 12733 11263 13811 96 -342 -68 C HETATM 2706 C4' BOG A 408 -352.443-160.087 160.928 1.00100.82 C ANISOU 2706 C4' BOG A 408 12868 11445 13993 136 -277 -94 C HETATM 2707 C5' BOG A 408 -352.970-159.895 162.344 1.00100.74 C ANISOU 2707 C5' BOG A 408 12916 11411 13948 83 -159 -234 C HETATM 2708 C6' BOG A 408 -352.624-161.083 163.230 1.00 97.14 C ANISOU 2708 C6' BOG A 408 12543 11066 13299 12 -171 -248 C HETATM 2709 C7' BOG A 408 -353.452-161.056 164.508 1.00 97.61 C ANISOU 2709 C7' BOG A 408 12669 11110 13309 -46 -30 -378 C HETATM 2710 C8' BOG A 408 -353.206-162.307 165.323 1.00 99.79 C ANISOU 2710 C8' BOG A 408 13038 11492 13385 -124 -54 -365 C HETATM 2711 C1 BOG A 409 -329.379-158.419 160.362 1.00110.70 C ANISOU 2711 C1 BOG A 409 12711 12798 16553 -804 -1383 473 C HETATM 2712 O1 BOG A 409 -329.366-159.708 159.756 1.00104.45 O ANISOU 2712 O1 BOG A 409 11828 12038 15821 -682 -1301 514 O HETATM 2713 C2 BOG A 409 -327.938-157.913 160.397 1.00113.20 C ANISOU 2713 C2 BOG A 409 12815 13077 17120 -907 -1450 499 C HETATM 2714 O2 BOG A 409 -327.172-158.727 161.296 1.00110.44 O ANISOU 2714 O2 BOG A 409 12327 12748 16888 -920 -1674 550 O HETATM 2715 C3 BOG A 409 -327.853-156.453 160.820 1.00115.78 C ANISOU 2715 C3 BOG A 409 13227 13351 17412 -1047 -1502 450 C HETATM 2716 O3 BOG A 409 -326.515-155.976 160.642 1.00124.22 O ANISOU 2716 O3 BOG A 409 14080 14382 18736 -1143 -1530 478 O HETATM 2717 C4 BOG A 409 -328.798-155.617 159.974 1.00112.23 C ANISOU 2717 C4 BOG A 409 12943 12866 16835 -1024 -1296 411 C HETATM 2718 O4 BOG A 409 -328.784-154.268 160.451 1.00106.46 O ANISOU 2718 O4 BOG A 409 12302 12067 16080 -1150 -1349 358 O HETATM 2719 C5 BOG A 409 -330.211-156.185 160.063 1.00116.30 C ANISOU 2719 C5 BOG A 409 13650 13420 17120 -915 -1256 386 C HETATM 2720 O5 BOG A 409 -330.238-157.546 159.622 1.00114.39 O ANISOU 2720 O5 BOG A 409 13328 13236 16901 -797 -1209 433 O HETATM 2721 C6 BOG A 409 -331.194-155.361 159.236 1.00113.14 C ANISOU 2721 C6 BOG A 409 13400 12974 16615 -887 -1081 362 C HETATM 2722 O6 BOG A 409 -332.535-155.724 159.587 1.00100.59 O ANISOU 2722 O6 BOG A 409 11984 11410 14827 -808 -1081 327 O HETATM 2723 C1' BOG A 409 -330.467-160.525 160.133 1.00 88.00 C ANISOU 2723 C1' BOG A 409 9897 9995 13543 -600 -1330 507 C HETATM 2724 C2' BOG A 409 -330.076-161.971 159.856 1.00 75.65 C ANISOU 2724 C2' BOG A 409 8191 8448 12104 -498 -1323 558 C HETATM 2725 C3' BOG A 409 -331.291-162.885 159.937 1.00 77.99 C ANISOU 2725 C3' BOG A 409 8643 8781 12208 -403 -1299 551 C HETATM 2726 C4' BOG A 409 -330.889-164.347 159.777 1.00 74.32 C ANISOU 2726 C4' BOG A 409 8045 8313 11879 -306 -1310 601 C HETATM 2727 C5' BOG A 409 -332.129-165.224 159.877 1.00 74.12 C ANISOU 2727 C5' BOG A 409 8183 8319 11659 -226 -1288 593 C HETATM 2728 C6' BOG A 409 -331.787-166.685 160.127 1.00 81.80 C ANISOU 2728 C6' BOG A 409 9054 9276 12752 -147 -1367 651 C HETATM 2729 C7' BOG A 409 -333.069-167.444 160.450 1.00 89.59 C ANISOU 2729 C7' BOG A 409 10225 10292 13524 -97 -1375 647 C HETATM 2730 C8' BOG A 409 -332.918-168.932 160.231 1.00 91.67 C ANISOU 2730 C8' BOG A 409 10401 10521 13906 3 -1368 689 C HETATM 2731 C1 BOG A 410 -378.210-183.942 158.600 1.00119.80 C ANISOU 2731 C1 BOG A 410 13091 14023 18406 -1031 -21 186 C HETATM 2732 O1 BOG A 410 -377.087-183.113 158.316 1.00106.27 O ANISOU 2732 O1 BOG A 410 11531 12339 16506 -903 -100 194 O HETATM 2733 C2 BOG A 410 -378.134-184.369 160.064 1.00121.83 C ANISOU 2733 C2 BOG A 410 13447 14279 18562 -1104 292 139 C HETATM 2734 O2 BOG A 410 -377.061-185.305 160.217 1.00113.63 O ANISOU 2734 O2 BOG A 410 12709 13255 17209 -1141 265 169 O HETATM 2735 C3 BOG A 410 -379.422-185.012 160.558 1.00135.27 C ANISOU 2735 C3 BOG A 410 14953 15945 20497 -1240 446 119 C HETATM 2736 O3 BOG A 410 -379.365-185.134 161.983 1.00135.73 O ANISOU 2736 O3 BOG A 410 15106 16009 20456 -1305 766 72 O HETATM 2737 C4 BOG A 410 -380.624-184.166 160.162 1.00145.56 C ANISOU 2737 C4 BOG A 410 15896 17218 22193 -1201 420 101 C HETATM 2738 O4 BOG A 410 -381.835-184.842 160.525 1.00152.57 O ANISOU 2738 O4 BOG A 410 16579 18069 23323 -1337 549 84 O HETATM 2739 C5 BOG A 410 -380.604-183.919 158.659 1.00142.53 C ANISOU 2739 C5 BOG A 410 15443 16834 21876 -1137 55 167 C HETATM 2740 O5 BOG A 410 -379.411-183.219 158.304 1.00132.40 O ANISOU 2740 O5 BOG A 410 14359 15586 20362 -1010 -51 182 O HETATM 2741 C6 BOG A 410 -381.824-183.118 158.217 1.00146.68 C ANISOU 2741 C6 BOG A 410 15597 17316 22820 -1100 -17 175 C HETATM 2742 O6 BOG A 410 -383.007-183.894 158.444 1.00147.51 O ANISOU 2742 O6 BOG A 410 15489 17386 23174 -1238 60 165 O HETATM 2743 C1' BOG A 410 -377.111-182.633 156.976 1.00 95.31 C ANISOU 2743 C1' BOG A 410 10076 10953 15184 -844 -382 245 C HETATM 2744 C2' BOG A 410 -375.895-181.744 156.763 1.00 88.41 C ANISOU 2744 C2' BOG A 410 9369 10109 14113 -718 -432 253 C HETATM 2745 C3' BOG A 410 -375.533-181.681 155.288 1.00 84.33 C ANISOU 2745 C3' BOG A 410 8914 9606 13520 -697 -734 315 C HETATM 2746 C4' BOG A 410 -374.301-180.814 155.075 1.00 83.98 C ANISOU 2746 C4' BOG A 410 9035 9589 13284 -583 -766 324 C HETATM 2747 C5' BOG A 410 -373.892-180.873 153.612 1.00 89.09 C ANISOU 2747 C5' BOG A 410 9781 10254 13817 -588 -1041 381 C HETATM 2748 C6' BOG A 410 -372.919-179.758 153.261 1.00 86.69 C ANISOU 2748 C6' BOG A 410 9574 9969 13397 -476 -1089 404 C HETATM 2749 C7' BOG A 410 -372.633-179.780 151.767 1.00 88.88 C ANISOU 2749 C7' BOG A 410 9948 10263 13561 -504 -1353 464 C HETATM 2750 C8' BOG A 410 -371.802-178.585 151.363 1.00 89.56 C ANISOU 2750 C8' BOG A 410 10106 10360 13562 -404 -1405 500 C HETATM 2751 C1 BOG A 411 -346.135-153.773 174.924 1.00132.81 C ANISOU 2751 C1 BOG A 411 18693 15319 16448 -1611 -255 -1505 C HETATM 2752 O1 BOG A 411 -346.585-155.115 175.097 1.00126.66 O ANISOU 2752 O1 BOG A 411 17927 14665 15533 -1586 -268 -1402 O HETATM 2753 C2 BOG A 411 -344.814-153.625 175.681 1.00137.91 C ANISOU 2753 C2 BOG A 411 19471 16014 16914 -1813 -497 -1493 C HETATM 2754 O2 BOG A 411 -345.058-153.705 177.092 1.00142.59 O ANISOU 2754 O2 BOG A 411 20342 16642 17195 -2026 -449 -1634 O HETATM 2755 C3 BOG A 411 -344.106-152.318 175.350 1.00138.11 C ANISOU 2755 C3 BOG A 411 19450 15917 17107 -1840 -536 -1559 C HETATM 2756 O3 BOG A 411 -342.819-152.289 175.980 1.00142.04 O ANISOU 2756 O3 BOG A 411 20038 16472 17459 -2025 -797 -1522 O HETATM 2757 C4 BOG A 411 -343.952-152.201 173.841 1.00129.57 C ANISOU 2757 C4 BOG A 411 18099 14795 16339 -1626 -556 -1413 C HETATM 2758 O4 BOG A 411 -343.314-150.961 173.512 1.00127.55 O ANISOU 2758 O4 BOG A 411 17803 14415 16246 -1657 -581 -1467 O HETATM 2759 C5 BOG A 411 -345.327-152.282 173.187 1.00125.53 C ANISOU 2759 C5 BOG A 411 17491 14227 15976 -1440 -318 -1435 C HETATM 2760 O5 BOG A 411 -345.983-153.511 173.524 1.00129.58 O ANISOU 2760 O5 BOG A 411 18043 14858 16335 -1420 -284 -1386 O HETATM 2761 C6 BOG A 411 -345.235-152.169 171.668 1.00116.94 C ANISOU 2761 C6 BOG A 411 16163 13100 15168 -1245 -344 -1284 C HETATM 2762 O6 BOG A 411 -344.248-151.198 171.309 1.00113.56 O ANISOU 2762 O6 BOG A 411 15691 12592 14866 -1289 -443 -1276 O HETATM 2763 C1' BOG A 411 -347.773-155.422 174.370 1.00119.62 C ANISOU 2763 C1' BOG A 411 16898 13746 14806 -1405 -78 -1389 C HETATM 2764 C2' BOG A 411 -347.775-156.923 174.111 1.00115.24 C ANISOU 2764 C2' BOG A 411 16281 13327 14177 -1346 -195 -1201 C HETATM 2765 C3' BOG A 411 -349.173-157.488 173.894 1.00111.01 C ANISOU 2765 C3' BOG A 411 15690 12792 13696 -1240 16 -1222 C HETATM 2766 C4' BOG A 411 -349.067-158.874 173.269 1.00107.28 C ANISOU 2766 C4' BOG A 411 15106 12428 13228 -1143 -119 -1017 C HETATM 2767 C5' BOG A 411 -350.387-159.631 173.343 1.00109.93 C ANISOU 2767 C5' BOG A 411 15431 12786 13552 -1092 63 -1035 C HETATM 2768 C6' BOG A 411 -350.511-160.617 172.187 1.00108.77 C ANISOU 2768 C6' BOG A 411 15094 12688 13547 -928 -22 -857 C HETATM 2769 C7' BOG A 411 -349.307-161.548 172.120 1.00106.76 C ANISOU 2769 C7' BOG A 411 14842 12527 13195 -956 -282 -684 C HETATM 2770 C8' BOG A 411 -349.233-162.267 170.791 1.00104.67 C ANISOU 2770 C8' BOG A 411 14379 12284 13107 -786 -359 -531 C HETATM 2771 C10 DN5 A 412 -357.464-168.087 147.609 1.00 63.95 C ANISOU 2771 C10 DN5 A 412 8232 7175 8889 83 -1189 768 C HETATM 2772 C11 DN5 A 412 -357.210-168.020 148.980 1.00 63.18 C ANISOU 2772 C11 DN5 A 412 8056 7066 8883 150 -1072 690 C HETATM 2773 C13 DN5 A 412 -359.261-169.149 149.421 1.00 74.87 C ANISOU 2773 C13 DN5 A 412 9399 8549 10500 152 -1146 667 C HETATM 2774 C15 DN5 A 412 -358.638-168.678 147.144 1.00 64.48 C ANISOU 2774 C15 DN5 A 412 8271 7250 8978 49 -1307 798 C HETATM 2775 C18 DN5 A 412 -355.099-168.228 146.704 1.00 69.51 C ANISOU 2775 C18 DN5 A 412 9141 7933 9337 13 -1042 738 C HETATM 2776 C19 DN5 A 412 -355.298-169.745 146.647 1.00 60.66 C ANISOU 2776 C19 DN5 A 412 8051 6856 8142 -13 -1015 665 C HETATM 2777 C20 DN5 A 412 -354.222-167.805 145.520 1.00 69.26 C ANISOU 2777 C20 DN5 A 412 9242 7913 9163 -63 -1027 787 C HETATM 2778 C22 DN5 A 412 -360.616-161.394 145.762 1.00 77.48 C ANISOU 2778 C22 DN5 A 412 9624 8381 11433 220 -1849 1381 C HETATM 2779 C23 DN5 A 412 -360.916-162.046 146.972 1.00 76.21 C ANISOU 2779 C23 DN5 A 412 9349 8248 11358 282 -1700 1228 C HETATM 2780 C25 DN5 A 412 -361.983-161.688 147.738 1.00 80.66 C ANISOU 2780 C25 DN5 A 412 9721 8725 12202 367 -1691 1199 C HETATM 2781 C26 DN5 A 412 -362.755-160.632 147.229 1.00 86.75 C ANISOU 2781 C26 DN5 A 412 10395 9367 13201 405 -1853 1334 C HETATM 2782 C27 DN5 A 412 -362.461-159.984 146.044 1.00 79.84 C ANISOU 2782 C27 DN5 A 412 9630 8457 12249 349 -2027 1501 C HETATM 2783 C28 DN5 A 412 -361.367-160.358 145.266 1.00 81.50 C ANISOU 2783 C28 DN5 A 412 10060 8769 12139 245 -2023 1528 C HETATM 2784 C1 DN5 A 412 -358.668-165.394 146.342 1.00 72.31 C ANISOU 2784 C1 DN5 A 412 9228 8086 10161 90 -1478 1028 C HETATM 2785 C2 DN5 A 412 -359.100-164.316 145.368 1.00 81.43 C ANISOU 2785 C2 DN5 A 412 10402 9173 11366 63 -1651 1184 C HETATM 2786 C3 DN5 A 412 -359.091-162.994 146.112 1.00 79.88 C ANISOU 2786 C3 DN5 A 412 10099 8870 11380 152 -1613 1198 C HETATM 2787 C4 DN5 A 412 -357.710-162.663 146.654 1.00 70.80 C ANISOU 2787 C4 DN5 A 412 9014 7734 10152 161 -1441 1122 C HETATM 2788 C5 DN5 A 412 -357.270-163.765 147.606 1.00 75.03 C ANISOU 2788 C5 DN5 A 412 9537 8349 10620 179 -1286 972 C HETATM 2789 N6 DN5 A 412 -357.363-165.103 146.972 1.00 75.96 N ANISOU 2789 N6 DN5 A 412 9731 8557 10574 115 -1313 956 N HETATM 2790 C7 DN5 A 412 -356.273-166.000 147.032 1.00 75.99 C ANISOU 2790 C7 DN5 A 412 9823 8635 10414 83 -1190 873 C HETATM 2791 O8 DN5 A 412 -355.182-165.578 147.422 1.00 72.98 O ANISOU 2791 O8 DN5 A 412 9463 8250 10016 97 -1085 838 O HETATM 2792 C9 DN5 A 412 -356.470-167.482 146.650 1.00 74.09 C ANISOU 2792 C9 DN5 A 412 9638 8464 10048 33 -1190 823 C HETATM 2793 C12 DN5 A 412 -358.102-168.554 149.887 1.00 67.23 C ANISOU 2793 C12 DN5 A 412 8472 7576 9495 181 -1048 639 C HETATM 2794 C14 DN5 A 412 -359.527-169.209 148.067 1.00 76.41 C ANISOU 2794 C14 DN5 A 412 9661 8754 10616 88 -1284 746 C HETATM 2795 CL6 DN5 A 412 -360.963-169.941 147.518 1.00 83.29 CL ANISOU 2795 CL6 DN5 A 412 10475 9630 11540 37 -1431 782 CL HETATM 2796 CL7 DN5 A 412 -360.353-169.802 150.548 1.00 84.83 CL ANISOU 2796 CL7 DN5 A 412 10533 9803 11895 177 -1092 603 CL HETATM 2797 O21 DN5 A 412 -359.504-161.958 145.217 1.00 84.81 O ANISOU 2797 O21 DN5 A 412 10736 9411 12078 132 -1788 1360 O HETATM 2798 O24 DN5 A 412 -359.997-163.041 147.210 1.00 75.84 O ANISOU 2798 O24 DN5 A 412 9412 8316 11087 239 -1567 1124 O HETATM 2799 O HOH A 501 -362.032-178.569 153.169 1.00 61.87 O HETATM 2800 O HOH A 502 -357.103-186.742 140.763 1.00 73.40 O HETATM 2801 O HOH A 503 -362.442-181.196 148.809 1.00 60.19 O HETATM 2802 O HOH A 504 -344.742-140.409 157.499 1.00 69.46 O HETATM 2803 O HOH A 505 -345.416-148.747 141.379 1.00 78.01 O HETATM 2804 O HOH A 506 -345.970-166.806 153.255 1.00 65.18 O HETATM 2805 O HOH A 507 -339.453-154.372 169.058 1.00 58.79 O HETATM 2806 O HOH A 508 -344.993-159.164 139.168 1.00 73.31 O HETATM 2807 O HOH A 509 -340.779-144.599 146.432 1.00 63.99 O HETATM 2808 O HOH A 510 -344.846-153.372 148.459 1.00 54.04 O HETATM 2809 O HOH A 511 -336.048-136.507 146.482 1.00 66.01 O HETATM 2810 O HOH A 512 -348.395-153.584 149.981 1.00 72.44 O HETATM 2811 O HOH A 513 -342.697-140.378 149.158 1.00 55.98 O HETATM 2812 O HOH A 514 -360.332-176.745 153.877 1.00 76.01 O HETATM 2813 O HOH A 515 -336.674-135.894 149.202 1.00 58.79 O HETATM 2814 O HOH A 516 -336.785-145.295 158.756 1.00 74.54 O HETATM 2815 O HOH A 517 -350.189-154.252 151.800 1.00 74.51 O HETATM 2816 O HOH A 518 -336.929-158.075 168.480 1.00 67.29 O HETATM 2817 O HOH A 519 -335.003-147.417 145.846 1.00 65.56 O CONECT 1 2 3 4 CONECT 2 1 CONECT 3 1 CONECT 4 1 CONECT 17 2244 CONECT 118 2593 CONECT 884 1474 CONECT 1474 884 CONECT 2244 17 CONECT 2564 2654 CONECT 2593 118 2594 2604 CONECT 2594 2593 2595 2601 CONECT 2595 2594 2596 2602 CONECT 2596 2595 2597 2603 CONECT 2597 2596 2598 2604 CONECT 2598 2597 2605 CONECT 2599 2600 2601 2606 CONECT 2600 2599 CONECT 2601 2594 2599 CONECT 2602 2595 CONECT 2603 2596 2607 CONECT 2604 2593 2597 CONECT 2605 2598 CONECT 2606 2599 CONECT 2607 2603 2608 2618 CONECT 2608 2607 2609 2615 CONECT 2609 2608 2610 2616 CONECT 2610 2609 2611 2617 CONECT 2611 2610 2612 2618 CONECT 2612 2611 2619 CONECT 2613 2614 2615 2620 CONECT 2614 2613 CONECT 2615 2608 2613 CONECT 2616 2609 CONECT 2617 2610 2621 CONECT 2618 2607 2611 CONECT 2619 2612 CONECT 2620 2613 CONECT 2621 2617 2622 2630 CONECT 2622 2621 2623 2627 CONECT 2623 2622 2624 2628 CONECT 2624 2623 2625 2629 CONECT 2625 2624 2626 2630 CONECT 2626 2625 2631 CONECT 2627 2622 CONECT 2628 2623 2632 CONECT 2629 2624 CONECT 2630 2621 2625 CONECT 2631 2626 2643 CONECT 2632 2628 2633 2641 CONECT 2633 2632 2634 2638 CONECT 2634 2633 2635 2639 CONECT 2635 2634 2636 2640 CONECT 2636 2635 2637 2641 CONECT 2637 2636 2642 CONECT 2638 2633 CONECT 2639 2634 CONECT 2640 2635 CONECT 2641 2632 2636 CONECT 2642 2637 CONECT 2643 2631 2644 2652 CONECT 2644 2643 2645 2649 CONECT 2645 2644 2646 2650 CONECT 2646 2645 2647 2651 CONECT 2647 2646 2648 2652 CONECT 2648 2647 2653 CONECT 2649 2644 CONECT 2650 2645 CONECT 2651 2646 CONECT 2652 2643 2647 CONECT 2653 2648 CONECT 2654 2564 2655 2656 CONECT 2655 2654 CONECT 2656 2654 2657 CONECT 2657 2656 2658 CONECT 2658 2657 2659 CONECT 2659 2658 2660 CONECT 2660 2659 2661 CONECT 2661 2660 2662 CONECT 2662 2661 2663 CONECT 2663 2662 2664 CONECT 2664 2663 2665 CONECT 2665 2664 2666 CONECT 2666 2665 2667 CONECT 2667 2666 2668 CONECT 2668 2667 2669 CONECT 2669 2668 2670 CONECT 2670 2669 CONECT 2671 2672 2673 2680 CONECT 2672 2671 2683 CONECT 2673 2671 2674 2675 CONECT 2674 2673 CONECT 2675 2673 2676 2677 CONECT 2676 2675 CONECT 2677 2675 2678 2679 CONECT 2678 2677 CONECT 2679 2677 2680 2681 CONECT 2680 2671 2679 CONECT 2681 2679 2682 CONECT 2682 2681 CONECT 2683 2672 2684 CONECT 2684 2683 2685 CONECT 2685 2684 2686 CONECT 2686 2685 2687 CONECT 2687 2686 2688 CONECT 2688 2687 2689 CONECT 2689 2688 2690 CONECT 2690 2689 CONECT 2691 2692 2693 2700 CONECT 2692 2691 2703 CONECT 2693 2691 2694 2695 CONECT 2694 2693 CONECT 2695 2693 2696 2697 CONECT 2696 2695 CONECT 2697 2695 2698 2699 CONECT 2698 2697 CONECT 2699 2697 2700 2701 CONECT 2700 2691 2699 CONECT 2701 2699 2702 CONECT 2702 2701 CONECT 2703 2692 2704 CONECT 2704 2703 2705 CONECT 2705 2704 2706 CONECT 2706 2705 2707 CONECT 2707 2706 2708 CONECT 2708 2707 2709 CONECT 2709 2708 2710 CONECT 2710 2709 CONECT 2711 2712 2713 2720 CONECT 2712 2711 2723 CONECT 2713 2711 2714 2715 CONECT 2714 2713 CONECT 2715 2713 2716 2717 CONECT 2716 2715 CONECT 2717 2715 2718 2719 CONECT 2718 2717 CONECT 2719 2717 2720 2721 CONECT 2720 2711 2719 CONECT 2721 2719 2722 CONECT 2722 2721 CONECT 2723 2712 2724 CONECT 2724 2723 2725 CONECT 2725 2724 2726 CONECT 2726 2725 2727 CONECT 2727 2726 2728 CONECT 2728 2727 2729 CONECT 2729 2728 2730 CONECT 2730 2729 CONECT 2731 2732 2733 2740 CONECT 2732 2731 2743 CONECT 2733 2731 2734 2735 CONECT 2734 2733 CONECT 2735 2733 2736 2737 CONECT 2736 2735 CONECT 2737 2735 2738 2739 CONECT 2738 2737 CONECT 2739 2737 2740 2741 CONECT 2740 2731 2739 CONECT 2741 2739 2742 CONECT 2742 2741 CONECT 2743 2732 2744 CONECT 2744 2743 2745 CONECT 2745 2744 2746 CONECT 2746 2745 2747 CONECT 2747 2746 2748 CONECT 2748 2747 2749 CONECT 2749 2748 2750 CONECT 2750 2749 CONECT 2751 2752 2753 2760 CONECT 2752 2751 2763 CONECT 2753 2751 2754 2755 CONECT 2754 2753 CONECT 2755 2753 2756 2757 CONECT 2756 2755 CONECT 2757 2755 2758 2759 CONECT 2758 2757 CONECT 2759 2757 2760 2761 CONECT 2760 2751 2759 CONECT 2761 2759 2762 CONECT 2762 2761 CONECT 2763 2752 2764 CONECT 2764 2763 2765 CONECT 2765 2764 2766 CONECT 2766 2765 2767 CONECT 2767 2766 2768 CONECT 2768 2767 2769 CONECT 2769 2768 2770 CONECT 2770 2769 CONECT 2771 2772 2774 2792 CONECT 2772 2771 2793 CONECT 2773 2793 2794 2796 CONECT 2774 2771 2794 CONECT 2775 2776 2777 2792 CONECT 2776 2775 CONECT 2777 2775 CONECT 2778 2779 2783 2797 CONECT 2779 2778 2780 2798 CONECT 2780 2779 2781 CONECT 2781 2780 2782 CONECT 2782 2781 2783 CONECT 2783 2778 2782 CONECT 2784 2785 2789 CONECT 2785 2784 2786 CONECT 2786 2785 2787 2797 2798 CONECT 2787 2786 2788 CONECT 2788 2787 2789 CONECT 2789 2784 2788 2790 CONECT 2790 2789 2791 2792 CONECT 2791 2790 CONECT 2792 2771 2775 2790 CONECT 2793 2772 2773 CONECT 2794 2773 2774 2795 CONECT 2795 2794 CONECT 2796 2773 CONECT 2797 2778 2786 CONECT 2798 2779 2786 MASTER 349 0 13 15 4 0 0 6 2816 1 216 27 END