HEADER MEMBRANE PROTEIN 23-JAN-18 6FKC TITLE CRYSTAL STRUCTURE OF N2C/D282C STABILIZED OPSIN BOUND TO RS15 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 6FKC 1 COMPND REMARK HETNAM LINK REVDAT 3 2 1 SITE ATOM REVDAT 2 11-APR-18 6FKC 1 JRNL REVDAT 1 04-APR-18 6FKC 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. 2.46 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) : 2.46 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.40 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 45695 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.224 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.240 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.080 REMARK 3 FREE R VALUE TEST SET COUNT : 2323 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 49.4055 - 6.3212 0.99 2651 130 0.2202 0.2118 REMARK 3 2 6.3212 - 5.0189 1.00 2562 162 0.2218 0.2324 REMARK 3 3 5.0189 - 4.3849 1.00 2578 145 0.1936 0.2188 REMARK 3 4 4.3849 - 3.9842 1.00 2543 143 0.1962 0.2125 REMARK 3 5 3.9842 - 3.6987 1.00 2560 140 0.1966 0.2337 REMARK 3 6 3.6987 - 3.4807 1.00 2562 124 0.2056 0.2232 REMARK 3 7 3.4807 - 3.3064 1.00 2548 134 0.2151 0.2379 REMARK 3 8 3.3064 - 3.1625 1.00 2554 149 0.2272 0.2205 REMARK 3 9 3.1625 - 3.0408 1.00 2558 129 0.2298 0.2330 REMARK 3 10 3.0408 - 2.9359 1.00 2531 132 0.2495 0.3122 REMARK 3 11 2.9359 - 2.8441 1.00 2544 134 0.2724 0.2885 REMARK 3 12 2.8441 - 2.7628 1.00 2551 141 0.2814 0.3248 REMARK 3 13 2.7628 - 2.6901 1.00 2529 130 0.2912 0.3210 REMARK 3 14 2.6901 - 2.6245 1.00 2542 114 0.3131 0.3776 REMARK 3 15 2.6245 - 2.5648 1.00 2560 116 0.3127 0.3881 REMARK 3 16 2.5648 - 2.5102 0.99 2504 147 0.3477 0.3859 REMARK 3 17 2.5102 - 2.4600 0.99 2495 153 0.3754 0.3986 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.440 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 : 0.006 2894 REMARK 3 ANGLE : 0.855 3937 REMARK 3 CHIRALITY : 0.043 458 REMARK 3 PLANARITY : 0.005 460 REMARK 3 DIHEDRAL : 13.939 1698 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):-352.2764-170.7895 151.6384 REMARK 3 T TENSOR REMARK 3 T11: 0.6991 T22: 0.5871 REMARK 3 T33: 0.6249 T12: -0.0079 REMARK 3 T13: -0.0869 T23: 0.0433 REMARK 3 L TENSOR REMARK 3 L11: 1.9043 L22: 2.2302 REMARK 3 L33: 0.6644 L12: 1.2575 REMARK 3 L13: 0.0744 L23: 0.1478 REMARK 3 S TENSOR REMARK 3 S11: -0.1006 S12: 0.1622 S13: 0.1264 REMARK 3 S21: -0.3100 S22: 0.0585 S23: 0.1915 REMARK 3 S31: 0.0415 S32: -0.0681 S33: 0.0000 REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 6FKC 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_1200008394. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-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 : 45757 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.460 REMARK 200 RESOLUTION RANGE LOW (A) : 49.400 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) : 0.10010 REMARK 200 R SYM (I) : 0.10010 REMARK 200 FOR THE DATA SET : 15.3000 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) : 2.55 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8 REMARK 200 DATA REDUNDANCY IN SHELL : 11.07 REMARK 200 R MERGE FOR SHELL (I) : 0.95650 REMARK 200 R SYM FOR SHELL (I) : 0.95650 REMARK 200 FOR SHELL : 0.840 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 121.60700 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.20983 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.28600 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.60700 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.20983 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.28600 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.60700 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.20983 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.28600 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.60700 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.20983 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.28600 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.60700 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.20983 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.28600 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.60700 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.20983 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.28600 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.41967 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 74.57200 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.41967 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 74.57200 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.41967 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 74.57200 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.41967 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 74.57200 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.41967 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 74.57200 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.41967 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 74.57200 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: 3540 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17980 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 IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR A 268 O2 BOG A 409 1.27 REMARK 500 O SER A 14 O HOH A 501 2.05 REMARK 500 O MET A 257 O HOH A 502 2.15 REMARK 500 OE1 GLN A 184 O HOH A 503 2.16 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 GLN A 28 43.85 -104.47 REMARK 500 SER A 176 -163.17 63.07 REMARK 500 PHE A 212 -51.05 -141.46 REMARK 500 GLN A 237 42.95 -141.20 REMARK 500 PHE A 276 -73.47 -56.83 REMARK 500 PHE A 287 -72.02 -69.03 REMARK 500 MET A 288 -158.65 44.89 REMARK 500 THR A 289 -13.39 55.88 REMARK 500 ILE A 307 -55.75 -123.01 REMARK 500 REMARK 500 REMARK: NULL REMARK 615 REMARK 615 ZERO OCCUPANCY ATOM REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 615 M RES C SSEQI REMARK 615 BOG A 410 REMARK 615 BOG A 412 DBREF 6FKC A 1 348 UNP P02699 OPSD_BOVIN 1 348 SEQADV 6FKC ACE A 0 UNP P02699 ACETYLATION SEQADV 6FKC CYS A 2 UNP P02699 ASN 2 CONFLICT SEQADV 6FKC 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 DLB A 407 32 HET BOG A 408 20 HET BOG A 409 20 HET BOG A 410 20 HET BOG A 411 20 HET BOG A 412 20 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 DLB 3-[1'-[(2~{S})-2-(4-CHLOROPHENYL)-3-METHYL- HETNAM 2 DLB BUTANOYL]SPIRO[1,3-BENZODIOXOLE-2,4'-PIPERIDINE]-5- HETNAM 3 DLB YL]PROPANOIC ACID HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE 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 DLB C25 H28 CL N O5 FORMUL 5 BOG 5(C14 H28 O6) FORMUL 10 HOH *28(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 LEU A 72 5 3 HELIX 4 AA4 ASN A 73 GLY A 90 1 18 HELIX 5 AA5 GLY A 90 HIS A 100 1 11 HELIX 6 AA6 PHE A 105 LYS A 141 1 37 HELIX 7 AA7 GLY A 149 ALA A 169 1 21 HELIX 8 AA8 PRO A 170 VAL A 173 5 4 HELIX 9 AA9 HIS A 195 THR A 198 5 4 HELIX 10 AB1 ASN A 199 HIS A 211 1 13 HELIX 11 AB2 PHE A 212 GLN A 236 1 25 HELIX 12 AB3 SER A 240 THR A 277 1 38 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 2.06 LINK C ACE A 0 N MET A 1 1555 1555 1.34 LINK ND2 ASN A 15 C1 NAG B 1 1555 1555 1.43 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 1.43 LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.45 LINK O6 BMA B 3 C1 MAN B 5 1555 1555 1.44 CISPEP 1 PHE A 287 MET A 288 0 -5.04 CRYST1 243.214 243.214 111.858 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 0.004112 0.002374 0.000000 0.00000 SCALE2 0.000000 0.004748 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008940 0.00000 HETATM 1 C ACE A 0 -353.387-139.197 152.100 1.00104.27 C ANISOU 1 C ACE A 0 12314 9697 17606 375 -1884 1225 C HETATM 2 O ACE A 0 -354.495-139.046 151.586 1.00118.94 O ANISOU 2 O ACE A 0 14065 11423 19702 423 -2049 1331 O HETATM 3 CH3 ACE A 0 -353.219-139.041 153.590 1.00101.11 C ANISOU 3 CH3 ACE A 0 11825 9302 17289 405 -1638 918 C ATOM 4 N MET A 1 -352.335-139.441 151.305 1.00 91.52 N ANISOU 4 N MET A 1 10892 8211 15670 285 -1928 1388 N ATOM 5 CA MET A 1 -350.922-139.686 151.613 1.00 90.48 C ANISOU 5 CA MET A 1 10902 8244 15232 215 -1775 1323 C ATOM 6 C MET A 1 -350.744-140.759 152.680 1.00 95.64 C ANISOU 6 C MET A 1 11561 9098 15678 229 -1575 1090 C ATOM 7 O MET A 1 -350.274-140.486 153.785 1.00106.05 O ANISOU 7 O MET A 1 12841 10424 17030 232 -1405 889 O ATOM 8 CB MET A 1 -350.218-138.397 152.042 1.00 95.78 C ANISOU 8 CB MET A 1 11540 8757 16094 200 -1715 1276 C ATOM 9 CG MET A 1 -350.058-137.375 150.924 1.00 96.81 C ANISOU 9 CG MET A 1 11710 8713 16358 157 -1906 1535 C ATOM 10 SD MET A 1 -349.420-138.101 149.399 1.00 96.59 S ANISOU 10 SD MET A 1 11909 8865 15925 41 -2041 1817 S ATOM 11 CE MET A 1 -347.902-138.868 149.968 1.00 86.47 C ANISOU 11 CE MET A 1 10759 7839 14255 -22 -1807 1665 C ATOM 12 N CYS A 2 -351.126-141.985 152.329 1.00 79.37 N ANISOU 12 N CYS A 2 9555 7200 13401 227 -1604 1125 N ATOM 13 CA CYS A 2 -351.152-143.078 153.293 1.00 84.88 C ANISOU 13 CA CYS A 2 10248 8074 13927 243 -1441 926 C ATOM 14 C CYS A 2 -349.760-143.639 153.550 1.00 88.07 C ANISOU 14 C CYS A 2 10792 8665 14005 177 -1316 882 C ATOM 15 O CYS A 2 -349.364-143.832 154.705 1.00 99.13 O ANISOU 15 O CYS A 2 12171 10138 15357 176 -1154 689 O ATOM 16 CB CYS A 2 -352.092-144.176 152.793 1.00 84.57 C ANISOU 16 CB CYS A 2 10211 8124 13797 263 -1526 984 C ATOM 17 SG CYS A 2 -353.801-143.630 152.623 1.00 95.92 S ANISOU 17 SG CYS A 2 11452 9348 15646 346 -1669 1013 S ATOM 18 N GLY A 3 -349.008-143.917 152.493 1.00 76.79 N ANISOU 18 N GLY A 3 9505 7319 12354 114 -1389 1058 N ATOM 19 CA GLY A 3 -347.697-144.505 152.633 1.00 71.80 C ANISOU 19 CA GLY A 3 8990 6857 11436 55 -1276 1026 C ATOM 20 C GLY A 3 -346.661-143.748 151.823 1.00 68.79 C ANISOU 20 C GLY A 3 8699 6434 11003 -17 -1318 1174 C ATOM 21 O GLY A 3 -346.788-142.546 151.558 1.00 68.59 O ANISOU 21 O GLY A 3 8633 6232 11198 -20 -1396 1252 O ATOM 22 N THR A 4 -345.624-144.479 151.429 1.00 65.08 N ANISOU 22 N THR A 4 8351 6126 10252 -80 -1262 1210 N ATOM 23 CA THR A 4 -344.529-143.945 150.628 1.00 63.13 C ANISOU 23 CA THR A 4 8202 5875 9910 -166 -1273 1341 C ATOM 24 C THR A 4 -344.347-144.850 149.418 1.00 62.88 C ANISOU 24 C THR A 4 8303 5972 9617 -231 -1322 1479 C ATOM 25 O THR A 4 -343.964-146.013 149.562 1.00 62.87 O ANISOU 25 O THR A 4 8345 6134 9409 -234 -1233 1405 O ATOM 26 CB THR A 4 -343.247-143.855 151.457 1.00 67.18 C ANISOU 26 CB THR A 4 8716 6455 10355 -192 -1121 1214 C ATOM 27 OG1 THR A 4 -343.509-143.099 152.643 1.00 62.57 O ANISOU 27 OG1 THR A 4 8015 5763 9994 -143 -1069 1063 O ATOM 28 CG2 THR A 4 -342.123-143.190 150.671 1.00 62.98 C ANISOU 28 CG2 THR A 4 8268 5903 9760 -285 -1122 1341 C ATOM 29 N GLU A 5 -344.648-144.330 148.235 1.00 64.34 N ANISOU 29 N GLU A 5 8553 6079 9816 -288 -1466 1678 N ATOM 30 CA GLU A 5 -344.409-145.033 146.988 1.00 64.50 C ANISOU 30 CA GLU A 5 8719 6214 9575 -381 -1510 1815 C ATOM 31 C GLU A 5 -342.925-145.025 146.644 1.00 78.89 C ANISOU 31 C GLU A 5 10639 8125 11210 -477 -1390 1829 C ATOM 32 O GLU A 5 -342.130-144.238 147.169 1.00 72.77 O ANISOU 32 O GLU A 5 9825 7292 10532 -483 -1316 1784 O ATOM 33 CB GLU A 5 -345.177-144.395 145.849 1.00 66.43 C ANISOU 33 CB GLU A 5 9011 6345 9887 -435 -1716 2037 C ATOM 34 CG GLU A 5 -346.663-144.364 146.015 1.00 67.02 C ANISOU 34 CG GLU A 5 8979 6317 10167 -349 -1858 2050 C ATOM 35 CD GLU A 5 -347.309-143.646 144.875 1.00 78.10 C ANISOU 35 CD GLU A 5 10427 7596 11652 -413 -2084 2292 C ATOM 36 OE1 GLU A 5 -347.043-142.435 144.705 1.00 77.11 O ANISOU 36 OE1 GLU A 5 10290 7318 11691 -441 -2146 2396 O ATOM 37 OE2 GLU A 5 -348.059-144.297 144.125 1.00 85.43 O ANISOU 37 OE2 GLU A 5 11407 8577 12475 -444 -2208 2387 O ATOM 38 N GLY A 6 -342.571-145.897 145.711 1.00 76.73 N ANISOU 38 N GLY A 6 10491 7989 10675 -560 -1369 1889 N ATOM 39 CA GLY A 6 -341.223-146.007 145.224 1.00 72.19 C ANISOU 39 CA GLY A 6 10008 7506 9914 -662 -1246 1902 C ATOM 40 C GLY A 6 -341.188-147.041 144.129 1.00 67.35 C ANISOU 40 C GLY A 6 9529 7030 9029 -751 -1239 1959 C ATOM 41 O GLY A 6 -342.162-147.758 143.911 1.00 64.13 O ANISOU 41 O GLY A 6 9133 6657 8576 -722 -1320 1967 O ATOM 42 N PRO A 7 -340.083-147.135 143.395 1.00 70.80 N ANISOU 42 N PRO A 7 10071 7548 9283 -871 -1136 1994 N ATOM 43 CA PRO A 7 -339.977-148.204 142.396 1.00 73.51 C ANISOU 43 CA PRO A 7 10542 8032 9358 -966 -1094 2012 C ATOM 44 C PRO A 7 -339.944-149.558 143.094 1.00 74.50 C ANISOU 44 C PRO A 7 10608 8268 9431 -872 -980 1827 C ATOM 45 O PRO A 7 -339.080-149.811 143.938 1.00 75.53 O ANISOU 45 O PRO A 7 10659 8434 9606 -817 -839 1692 O ATOM 46 CB PRO A 7 -338.658-147.887 141.678 1.00 73.97 C ANISOU 46 CB PRO A 7 10692 8137 9276 -1108 -967 2053 C ATOM 47 CG PRO A 7 -338.377-146.432 141.986 1.00 66.75 C ANISOU 47 CG PRO A 7 9728 7079 8554 -1112 -1018 2136 C ATOM 48 CD PRO A 7 -338.892-146.270 143.392 1.00 65.38 C ANISOU 48 CD PRO A 7 9389 6826 8626 -939 -1045 2015 C ATOM 49 N ASN A 8 -340.925-150.407 142.771 1.00 64.62 N ANISOU 49 N ASN A 8 9391 7063 8099 -856 -1058 1831 N ATOM 50 CA ASN A 8 -341.035-151.796 143.229 1.00 68.53 C ANISOU 50 CA ASN A 8 9854 7662 8524 -787 -971 1680 C ATOM 51 C ASN A 8 -341.484-151.945 144.675 1.00 67.71 C ANISOU 51 C ASN A 8 9597 7518 8611 -631 -969 1557 C ATOM 52 O ASN A 8 -341.268-153.009 145.263 1.00 67.83 O ANISOU 52 O ASN A 8 9572 7613 8585 -574 -871 1424 O ATOM 53 CB ASN A 8 -339.720-152.571 143.083 1.00 61.24 C ANISOU 53 CB ASN A 8 8963 6849 7457 -836 -769 1575 C ATOM 54 CG ASN A 8 -339.197-152.570 141.678 1.00 76.43 C ANISOU 54 CG ASN A 8 11041 8831 9167 -1006 -727 1662 C ATOM 55 OD1 ASN A 8 -339.957-152.676 140.715 1.00 78.54 O ANISOU 55 OD1 ASN A 8 11421 9114 9306 -1091 -837 1766 O ATOM 56 ND2 ASN A 8 -337.883-152.450 141.545 1.00 81.40 N ANISOU 56 ND2 ASN A 8 11679 9497 9753 -1068 -564 1618 N ATOM 57 N PHE A 9 -342.083-150.934 145.292 1.00 69.28 N ANISOU 57 N PHE A 9 9709 7595 9020 -566 -1066 1588 N ATOM 58 CA PHE A 9 -342.509-151.119 146.671 1.00 64.84 C ANISOU 58 CA PHE A 9 9014 7009 8615 -439 -1043 1453 C ATOM 59 C PHE A 9 -343.522-150.056 147.051 1.00 63.16 C ANISOU 59 C PHE A 9 8716 6648 8632 -384 -1173 1501 C ATOM 60 O PHE A 9 -343.675-149.032 146.382 1.00 62.78 O ANISOU 60 O PHE A 9 8699 6500 8654 -434 -1276 1640 O ATOM 61 CB PHE A 9 -341.322-151.111 147.650 1.00 64.38 C ANISOU 61 CB PHE A 9 8892 6982 8586 -411 -895 1330 C ATOM 62 CG PHE A 9 -340.599-149.781 147.753 1.00 62.07 C ANISOU 62 CG PHE A 9 8579 6599 8404 -445 -885 1374 C ATOM 63 CD1 PHE A 9 -339.360-149.609 147.154 1.00 59.37 C ANISOU 63 CD1 PHE A 9 8300 6298 7959 -536 -797 1411 C ATOM 64 CD2 PHE A 9 -341.131-148.728 148.490 1.00 67.31 C ANISOU 64 CD2 PHE A 9 9153 7134 9286 -390 -949 1364 C ATOM 65 CE1 PHE A 9 -338.676-148.403 147.262 1.00 70.17 C ANISOU 65 CE1 PHE A 9 9648 7582 9433 -574 -785 1451 C ATOM 66 CE2 PHE A 9 -340.462-147.518 148.597 1.00 62.87 C ANISOU 66 CE2 PHE A 9 8572 6480 8834 -425 -938 1398 C ATOM 67 CZ PHE A 9 -339.228-147.354 147.981 1.00 66.18 C ANISOU 67 CZ PHE A 9 9060 6944 9142 -518 -861 1447 C ATOM 68 N TYR A 10 -344.199-150.327 148.159 1.00 63.55 N ANISOU 68 N TYR A 10 8656 6682 8809 -283 -1161 1380 N ATOM 69 CA TYR A 10 -345.119-149.390 148.784 1.00 59.47 C ANISOU 69 CA TYR A 10 8027 6022 8545 -216 -1241 1369 C ATOM 70 C TYR A 10 -345.017-149.648 150.279 1.00 61.58 C ANISOU 70 C TYR A 10 8194 6315 8890 -141 -1124 1181 C ATOM 71 O TYR A 10 -345.455-150.696 150.758 1.00 68.63 O ANISOU 71 O TYR A 10 9065 7291 9719 -102 -1087 1092 O ATOM 72 CB TYR A 10 -346.548-149.585 148.272 1.00 60.18 C ANISOU 72 CB TYR A 10 8100 6066 8702 -193 -1390 1444 C ATOM 73 CG TYR A 10 -347.563-148.732 148.996 1.00 68.27 C ANISOU 73 CG TYR A 10 8980 6937 10021 -112 -1454 1406 C ATOM 74 CD1 TYR A 10 -347.697-147.374 148.706 1.00 71.37 C ANISOU 74 CD1 TYR A 10 9338 7165 10615 -120 -1551 1509 C ATOM 75 CD2 TYR A 10 -348.369-149.272 149.988 1.00 60.14 C ANISOU 75 CD2 TYR A 10 7846 5921 9082 -32 -1408 1261 C ATOM 76 CE1 TYR A 10 -348.613-146.586 149.379 1.00 69.15 C ANISOU 76 CE1 TYR A 10 8910 6727 10637 -42 -1596 1457 C ATOM 77 CE2 TYR A 10 -349.288-148.491 150.664 1.00 64.83 C ANISOU 77 CE2 TYR A 10 8300 6373 9961 36 -1442 1203 C ATOM 78 CZ TYR A 10 -349.406-147.153 150.358 1.00 74.01 C ANISOU 78 CZ TYR A 10 9418 7364 11338 36 -1533 1296 C ATOM 79 OH TYR A 10 -350.318-146.380 151.036 1.00 85.28 O ANISOU 79 OH TYR A 10 10691 8635 13077 107 -1554 1222 O ATOM 80 N VAL A 11 -344.403-148.719 151.002 1.00 62.19 N ANISOU 80 N VAL A 11 8217 6325 9087 -136 -1067 1123 N ATOM 81 CA VAL A 11 -344.301-148.806 152.455 1.00 62.57 C ANISOU 81 CA VAL A 11 8178 6391 9204 -87 -964 947 C ATOM 82 C VAL A 11 -345.561-148.175 153.036 1.00 68.39 C ANISOU 82 C VAL A 11 8804 7002 10179 -26 -1013 890 C ATOM 83 O VAL A 11 -345.871-147.020 152.720 1.00 64.57 O ANISOU 83 O VAL A 11 8282 6368 9882 -23 -1087 957 O ATOM 84 CB VAL A 11 -343.027-148.118 152.967 1.00 60.96 C ANISOU 84 CB VAL A 11 7970 6179 9013 -124 -880 901 C ATOM 85 CG1 VAL A 11 -342.956-148.141 154.495 1.00 57.01 C ANISOU 85 CG1 VAL A 11 7390 5698 8573 -94 -788 720 C ATOM 86 CG2 VAL A 11 -341.788-148.753 152.336 1.00 57.08 C ANISOU 86 CG2 VAL A 11 7569 5804 8313 -184 -825 953 C ATOM 87 N PRO A 12 -346.344-148.905 153.851 1.00 70.11 N ANISOU 87 N PRO A 12 8963 7267 10409 21 -973 770 N ATOM 88 CA PRO A 12 -347.574-148.322 154.421 1.00 62.61 C ANISOU 88 CA PRO A 12 7891 6194 9703 76 -998 696 C ATOM 89 C PRO A 12 -347.290-147.376 155.578 1.00 61.62 C ANISOU 89 C PRO A 12 7688 5991 9733 79 -903 550 C ATOM 90 O PRO A 12 -347.742-147.577 156.705 1.00 65.72 O ANISOU 90 O PRO A 12 8139 6529 10301 97 -813 386 O ATOM 91 CB PRO A 12 -348.357-149.563 154.877 1.00 57.74 C ANISOU 91 CB PRO A 12 7255 5680 9004 105 -965 613 C ATOM 92 CG PRO A 12 -347.299-150.588 155.169 1.00 63.93 C ANISOU 92 CG PRO A 12 8126 6629 9535 68 -879 578 C ATOM 93 CD PRO A 12 -346.192-150.333 154.194 1.00 61.09 C ANISOU 93 CD PRO A 12 7860 6285 9067 22 -909 706 C ATOM 94 N PHE A 13 -346.518-146.331 155.302 1.00 64.90 N ANISOU 94 N PHE A 13 8120 6320 10218 49 -917 606 N ATOM 95 CA PHE A 13 -346.165-145.346 156.313 1.00 62.41 C ANISOU 95 CA PHE A 13 7740 5922 10052 39 -832 471 C ATOM 96 C PHE A 13 -345.854-144.026 155.618 1.00 64.64 C ANISOU 96 C PHE A 13 8018 6040 10501 24 -906 585 C ATOM 97 O PHE A 13 -345.192-144.004 154.577 1.00 72.99 O ANISOU 97 O PHE A 13 9167 7120 11448 -17 -972 750 O ATOM 98 CB PHE A 13 -344.970-145.816 157.140 1.00 59.33 C ANISOU 98 CB PHE A 13 7401 5674 9467 -12 -718 372 C ATOM 99 CG PHE A 13 -344.752-145.021 158.402 1.00 63.83 C ANISOU 99 CG PHE A 13 7907 6189 10157 -35 -620 194 C ATOM 100 CD1 PHE A 13 -345.434-145.342 159.569 1.00 59.66 C ANISOU 100 CD1 PHE A 13 7321 5694 9654 -29 -532 15 C ATOM 101 CD2 PHE A 13 -343.854-143.963 158.429 1.00 67.04 C ANISOU 101 CD2 PHE A 13 8318 6516 10639 -77 -607 200 C ATOM 102 CE1 PHE A 13 -345.231-144.619 160.734 1.00 60.35 C ANISOU 102 CE1 PHE A 13 7362 5740 9830 -71 -432 -163 C ATOM 103 CE2 PHE A 13 -343.643-143.230 159.593 1.00 61.01 C ANISOU 103 CE2 PHE A 13 7501 5702 9977 -111 -515 25 C ATOM 104 CZ PHE A 13 -344.328-143.557 160.745 1.00 61.02 C ANISOU 104 CZ PHE A 13 7453 5742 9991 -111 -426 -160 C ATOM 105 N SER A 14 -346.335-142.932 156.203 1.00 64.12 N ANISOU 105 N SER A 14 7847 5806 10709 49 -888 492 N ATOM 106 CA SER A 14 -346.134-141.613 155.620 1.00 64.39 C ANISOU 106 CA SER A 14 7864 5657 10946 37 -964 597 C ATOM 107 C SER A 14 -344.692-141.162 155.794 1.00 65.19 C ANISOU 107 C SER A 14 8031 5793 10945 -35 -899 590 C ATOM 108 O SER A 14 -344.091-141.340 156.855 1.00 63.42 O ANISOU 108 O SER A 14 7802 5655 10640 -62 -776 425 O ATOM 109 CB SER A 14 -347.070-140.596 156.266 1.00 65.99 C ANISOU 109 CB SER A 14 7918 5653 11501 89 -950 476 C ATOM 110 OG SER A 14 -346.633-139.273 156.000 1.00 67.40 O ANISOU 110 OG SER A 14 8079 5653 11877 67 -989 536 O ATOM 111 N ASN A 15 -344.141-140.551 154.750 1.00 65.68 N ANISOU 111 N ASN A 15 8155 5786 11015 -76 -987 775 N ATOM 112 CA ASN A 15 -342.780-140.045 154.797 1.00 64.80 C ANISOU 112 CA ASN A 15 8098 5693 10829 -150 -931 784 C ATOM 113 C ASN A 15 -342.712-138.553 155.131 1.00 66.42 C ANISOU 113 C ASN A 15 8231 5686 11319 -159 -931 745 C ATOM 114 O ASN A 15 -341.683-137.918 154.875 1.00 66.82 O ANISOU 114 O ASN A 15 8327 5708 11353 -227 -921 805 O ATOM 115 CB ASN A 15 -342.075-140.335 153.473 1.00 64.65 C ANISOU 115 CB ASN A 15 8201 5746 10617 -212 -998 997 C ATOM 116 CG ASN A 15 -340.572-140.316 153.603 1.00 64.10 C ANISOU 116 CG ASN A 15 8189 5770 10396 -290 -907 979 C ATOM 117 OD1 ASN A 15 -340.029-140.393 154.708 1.00 63.63 O ANISOU 117 OD1 ASN A 15 8089 5768 10318 -295 -801 811 O ATOM 118 ND2 ASN A 15 -339.885-140.213 152.485 1.00 69.11 N ANISOU 118 ND2 ASN A 15 8917 6424 10919 -361 -946 1152 N ATOM 119 N LYS A 16 -343.767-137.974 155.718 1.00 67.48 N ANISOU 119 N LYS A 16 8247 5665 11727 -96 -932 635 N ATOM 120 CA LYS A 16 -343.707-136.539 156.017 1.00 73.28 C ANISOU 120 CA LYS A 16 8907 6178 12758 -104 -927 589 C ATOM 121 C LYS A 16 -342.604-136.200 157.014 1.00 71.87 C ANISOU 121 C LYS A 16 8738 6048 12519 -170 -790 420 C ATOM 122 O LYS A 16 -342.121-135.065 157.017 1.00 78.70 O ANISOU 122 O LYS A 16 9584 6762 13556 -208 -791 427 O ATOM 123 CB LYS A 16 -345.046-136.017 156.540 1.00 73.44 C ANISOU 123 CB LYS A 16 8780 6016 13108 -23 -930 469 C ATOM 124 CG LYS A 16 -345.477-136.595 157.874 1.00 77.02 C ANISOU 124 CG LYS A 16 9170 6566 13528 -2 -777 202 C ATOM 125 CD LYS A 16 -346.974-136.401 158.101 1.00 79.93 C ANISOU 125 CD LYS A 16 9394 6786 14189 85 -791 120 C ATOM 126 CE LYS A 16 -347.416-137.149 159.348 1.00 89.64 C ANISOU 126 CE LYS A 16 10582 8146 15331 88 -631 -133 C ATOM 127 NZ LYS A 16 -348.894-137.326 159.432 1.00105.99 N ANISOU 127 NZ LYS A 16 12523 10128 17620 169 -643 -192 N ATOM 128 N THR A 17 -342.183-137.154 157.846 1.00 69.72 N ANISOU 128 N THR A 17 8497 5981 12012 -192 -683 280 N ATOM 129 CA THR A 17 -341.058-136.953 158.754 1.00 67.03 C ANISOU 129 CA THR A 17 8176 5713 11580 -269 -576 141 C ATOM 130 C THR A 17 -339.723-137.365 158.152 1.00 66.08 C ANISOU 130 C THR A 17 8156 5732 11221 -335 -591 274 C ATOM 131 O THR A 17 -338.699-137.263 158.830 1.00 81.79 O ANISOU 131 O THR A 17 10158 7791 13127 -403 -519 180 O ATOM 132 CB THR A 17 -341.266-137.703 160.077 1.00 75.94 C ANISOU 132 CB THR A 17 9282 6982 12590 -276 -462 -83 C ATOM 133 OG1 THR A 17 -341.322-139.122 159.840 1.00 84.35 O ANISOU 133 OG1 THR A 17 10406 8246 13396 -255 -478 -20 O ATOM 134 CG2 THR A 17 -342.552-137.242 160.768 1.00 70.98 C ANISOU 134 CG2 THR A 17 8544 6216 12208 -226 -412 -251 C ATOM 135 N GLY A 18 -339.702-137.846 156.914 1.00 65.68 N ANISOU 135 N GLY A 18 8172 5724 11057 -325 -678 482 N ATOM 136 CA GLY A 18 -338.451-138.189 156.267 1.00 65.05 C ANISOU 136 CA GLY A 18 8179 5762 10773 -394 -674 600 C ATOM 137 C GLY A 18 -337.795-139.485 156.704 1.00 67.85 C ANISOU 137 C GLY A 18 8570 6345 10863 -408 -606 536 C ATOM 138 O GLY A 18 -336.694-139.793 156.221 1.00 62.97 O ANISOU 138 O GLY A 18 8006 5822 10097 -464 -587 615 O ATOM 139 N VAL A 19 -338.424-140.274 157.586 1.00 62.54 N ANISOU 139 N VAL A 19 7867 5761 10136 -363 -567 398 N ATOM 140 CA VAL A 19 -337.750-141.473 158.111 1.00 67.17 C ANISOU 140 CA VAL A 19 8482 6549 10490 -382 -513 340 C ATOM 141 C VAL A 19 -337.944-142.727 157.260 1.00 63.15 C ANISOU 141 C VAL A 19 8032 6163 9800 -348 -546 455 C ATOM 142 O VAL A 19 -337.205-143.703 157.450 1.00 69.40 O ANISOU 142 O VAL A 19 8850 7106 10414 -367 -509 441 O ATOM 143 CB VAL A 19 -338.204-141.804 159.549 1.00 60.84 C ANISOU 143 CB VAL A 19 7635 5802 9681 -376 -451 139 C ATOM 144 CG1 VAL A 19 -338.106-140.553 160.440 1.00 62.09 C ANISOU 144 CG1 VAL A 19 7738 5835 10020 -420 -404 -5 C ATOM 145 CG2 VAL A 19 -339.613-142.434 159.550 1.00 60.52 C ANISOU 145 CG2 VAL A 19 7575 5764 9655 -301 -468 117 C ATOM 146 N VAL A 20 -338.901-142.738 156.328 1.00 65.05 N ANISOU 146 N VAL A 20 8290 6338 10087 -304 -620 567 N ATOM 147 CA VAL A 20 -339.163-143.946 155.553 1.00 65.89 C ANISOU 147 CA VAL A 20 8457 6561 10018 -280 -649 659 C ATOM 148 C VAL A 20 -337.953-144.290 154.692 1.00 66.89 C ANISOU 148 C VAL A 20 8655 6773 9986 -341 -628 767 C ATOM 149 O VAL A 20 -337.299-143.407 154.116 1.00 68.41 O ANISOU 149 O VAL A 20 8870 6892 10232 -397 -636 852 O ATOM 150 CB VAL A 20 -340.433-143.782 154.698 1.00 64.29 C ANISOU 150 CB VAL A 20 8259 6262 9906 -235 -750 765 C ATOM 151 CG1 VAL A 20 -340.677-145.035 153.841 1.00 59.34 C ANISOU 151 CG1 VAL A 20 7704 5759 9083 -226 -782 857 C ATOM 152 CG2 VAL A 20 -341.638-143.500 155.589 1.00 60.50 C ANISOU 152 CG2 VAL A 20 7685 5695 9606 -171 -752 639 C ATOM 153 N ARG A 21 -337.643-145.584 154.615 1.00 61.73 N ANISOU 153 N ARG A 21 8034 6271 9148 -334 -593 758 N ATOM 154 CA ARG A 21 -336.545-146.111 153.820 1.00 59.70 C ANISOU 154 CA ARG A 21 7834 6106 8745 -387 -550 835 C ATOM 155 C ARG A 21 -337.060-147.220 152.911 1.00 65.32 C ANISOU 155 C ARG A 21 8611 6896 9309 -369 -572 906 C ATOM 156 O ARG A 21 -338.126-147.801 153.147 1.00 64.37 O ANISOU 156 O ARG A 21 8483 6791 9184 -311 -612 875 O ATOM 157 CB ARG A 21 -335.426-146.637 154.719 1.00 59.35 C ANISOU 157 CB ARG A 21 7746 6162 8642 -404 -473 733 C ATOM 158 CG ARG A 21 -334.857-145.572 155.636 1.00 58.96 C ANISOU 158 CG ARG A 21 7637 6044 8720 -438 -455 654 C ATOM 159 CD ARG A 21 -334.012-144.592 154.850 1.00 58.89 C ANISOU 159 CD ARG A 21 7648 5963 8765 -508 -443 747 C ATOM 160 NE ARG A 21 -333.448-143.581 155.734 1.00 66.44 N ANISOU 160 NE ARG A 21 8545 6850 9847 -546 -426 665 N ATOM 161 CZ ARG A 21 -334.028-142.418 156.028 1.00 65.10 C ANISOU 161 CZ ARG A 21 8353 6537 9845 -545 -459 639 C ATOM 162 NH1 ARG A 21 -333.421-141.579 156.851 1.00 67.95 N ANISOU 162 NH1 ARG A 21 8665 6846 10308 -590 -433 549 N ATOM 163 NH2 ARG A 21 -335.213-142.093 155.508 1.00 61.82 N ANISOU 163 NH2 ARG A 21 7956 6023 9508 -500 -521 700 N ATOM 164 N SER A 22 -336.297-147.503 151.858 1.00 57.78 N ANISOU 164 N SER A 22 7723 5994 8237 -430 -537 995 N ATOM 165 CA SER A 22 -336.674-148.571 150.940 1.00 65.04 C ANISOU 165 CA SER A 22 8716 6994 9002 -433 -543 1050 C ATOM 166 C SER A 22 -336.706-149.910 151.672 1.00 56.41 C ANISOU 166 C SER A 22 7588 6010 7835 -374 -499 942 C ATOM 167 O SER A 22 -335.754-150.237 152.394 1.00 58.47 O ANISOU 167 O SER A 22 7796 6325 8094 -374 -431 863 O ATOM 168 CB SER A 22 -335.698-148.647 149.770 1.00 67.26 C ANISOU 168 CB SER A 22 9073 7320 9163 -527 -480 1135 C ATOM 169 OG SER A 22 -335.921-149.812 149.001 1.00 63.07 O ANISOU 169 OG SER A 22 8610 6882 8471 -537 -460 1152 O ATOM 170 N PRO A 23 -337.763-150.713 151.508 1.00 59.37 N ANISOU 170 N PRO A 23 7987 6414 8155 -330 -546 942 N ATOM 171 CA PRO A 23 -337.797-152.037 152.155 1.00 57.09 C ANISOU 171 CA PRO A 23 7672 6223 7795 -281 -507 851 C ATOM 172 C PRO A 23 -336.745-153.008 151.625 1.00 55.72 C ANISOU 172 C PRO A 23 7526 6141 7503 -314 -419 847 C ATOM 173 O PRO A 23 -336.597-154.097 152.193 1.00 62.33 O ANISOU 173 O PRO A 23 8333 7047 8303 -276 -387 777 O ATOM 174 CB PRO A 23 -339.221-152.536 151.858 1.00 54.51 C ANISOU 174 CB PRO A 23 7374 5892 7446 -241 -583 873 C ATOM 175 CG PRO A 23 -339.575-151.875 150.580 1.00 58.73 C ANISOU 175 CG PRO A 23 7982 6368 7965 -292 -647 1002 C ATOM 176 CD PRO A 23 -338.929-150.496 150.637 1.00 60.27 C ANISOU 176 CD PRO A 23 8157 6475 8268 -331 -645 1040 C ATOM 177 N PHE A 24 -336.008-152.647 150.574 1.00 58.77 N ANISOU 177 N PHE A 24 7966 6525 7839 -389 -375 917 N ATOM 178 CA PHE A 24 -334.877-153.428 150.093 1.00 59.95 C ANISOU 178 CA PHE A 24 8123 6749 7908 -428 -265 894 C ATOM 179 C PHE A 24 -333.537-152.975 150.666 1.00 58.58 C ANISOU 179 C PHE A 24 7870 6572 7818 -450 -196 854 C ATOM 180 O PHE A 24 -332.518-153.593 150.355 1.00 72.32 O ANISOU 180 O PHE A 24 9588 8362 9528 -477 -98 824 O ATOM 181 CB PHE A 24 -334.804-153.378 148.560 1.00 56.52 C ANISOU 181 CB PHE A 24 7798 6327 7351 -519 -232 981 C ATOM 182 CG PHE A 24 -336.046-153.860 147.879 1.00 64.04 C ANISOU 182 CG PHE A 24 8836 7290 8207 -516 -309 1028 C ATOM 183 CD1 PHE A 24 -336.468-155.173 148.031 1.00 61.15 C ANISOU 183 CD1 PHE A 24 8468 6986 7781 -467 -296 962 C ATOM 184 CD2 PHE A 24 -336.803-153.005 147.093 1.00 58.92 C ANISOU 184 CD2 PHE A 24 8265 6582 7538 -567 -407 1147 C ATOM 185 CE1 PHE A 24 -337.625-155.628 147.411 1.00 57.72 C ANISOU 185 CE1 PHE A 24 8108 6562 7262 -470 -373 1002 C ATOM 186 CE2 PHE A 24 -337.961-153.455 146.469 1.00 69.06 C ANISOU 186 CE2 PHE A 24 9621 7877 8742 -571 -496 1197 C ATOM 187 CZ PHE A 24 -338.367-154.771 146.630 1.00 66.22 C ANISOU 187 CZ PHE A 24 9258 7587 8316 -523 -475 1119 C ATOM 188 N GLU A 25 -333.499-151.927 151.494 1.00 60.76 N ANISOU 188 N GLU A 25 8093 6784 8208 -441 -242 844 N ATOM 189 CA GLU A 25 -332.214-151.316 151.840 1.00 62.84 C ANISOU 189 CA GLU A 25 8293 7036 8548 -484 -185 823 C ATOM 190 C GLU A 25 -331.998-151.103 153.336 1.00 59.67 C ANISOU 190 C GLU A 25 7798 6628 8247 -446 -220 739 C ATOM 191 O GLU A 25 -330.850-151.059 153.791 1.00 64.66 O ANISOU 191 O GLU A 25 8358 7279 8929 -472 -178 703 O ATOM 192 CB GLU A 25 -332.047-149.965 151.126 1.00 57.30 C ANISOU 192 CB GLU A 25 7634 6253 7883 -559 -190 910 C ATOM 193 CG GLU A 25 -331.642-150.031 149.641 1.00 68.70 C ANISOU 193 CG GLU A 25 9166 7719 9218 -648 -121 994 C ATOM 194 CD GLU A 25 -331.220-148.658 149.058 1.00 99.47 C ANISOU 194 CD GLU A 25 13098 11537 13160 -741 -119 1086 C ATOM 195 OE1 GLU A 25 -331.444-147.603 149.701 1.00 95.72 O ANISOU 195 OE1 GLU A 25 12587 10971 12813 -726 -187 1093 O ATOM 196 OE2 GLU A 25 -330.655-148.638 147.943 1.00113.05 O ANISOU 196 OE2 GLU A 25 14884 13282 14788 -837 -41 1147 O ATOM 197 N ALA A 26 -333.066-150.942 154.114 1.00 57.25 N ANISOU 197 N ALA A 26 7489 6294 7970 -397 -294 703 N ATOM 198 CA ALA A 26 -332.876-150.510 155.494 1.00 55.07 C ANISOU 198 CA ALA A 26 7143 6005 7775 -392 -321 620 C ATOM 199 C ALA A 26 -334.035-150.991 156.349 1.00 57.71 C ANISOU 199 C ALA A 26 7478 6357 8093 -336 -371 558 C ATOM 200 O ALA A 26 -335.151-151.160 155.840 1.00 56.41 O ANISOU 200 O ALA A 26 7360 6171 7904 -301 -400 589 O ATOM 201 CB ALA A 26 -332.746-148.976 155.580 1.00 55.91 C ANISOU 201 CB ALA A 26 7240 6010 7993 -436 -334 629 C ATOM 202 N PRO A 27 -333.814-151.194 157.648 1.00 61.37 N ANISOU 202 N PRO A 27 7891 6858 8568 -339 -385 473 N ATOM 203 CA PRO A 27 -334.871-151.760 158.494 1.00 58.37 C ANISOU 203 CA PRO A 27 7517 6508 8154 -303 -417 410 C ATOM 204 C PRO A 27 -336.086-150.851 158.588 1.00 57.07 C ANISOU 204 C PRO A 27 7363 6257 8064 -288 -436 381 C ATOM 205 O PRO A 27 -335.991-149.629 158.480 1.00 70.59 O ANISOU 205 O PRO A 27 9063 7879 9877 -313 -436 381 O ATOM 206 CB PRO A 27 -334.190-151.929 159.861 1.00 60.87 C ANISOU 206 CB PRO A 27 7786 6880 8462 -342 -429 334 C ATOM 207 CG PRO A 27 -332.916-151.177 159.786 1.00 56.24 C ANISOU 207 CG PRO A 27 7160 6270 7937 -395 -414 348 C ATOM 208 CD PRO A 27 -332.522-151.118 158.345 1.00 54.42 C ANISOU 208 CD PRO A 27 6951 6012 7715 -385 -374 440 C ATOM 209 N GLN A 28 -337.244-151.475 158.783 1.00 64.43 N ANISOU 209 N GLN A 28 8309 7206 8963 -245 -453 354 N ATOM 210 CA GLN A 28 -338.531-150.781 158.765 1.00 61.20 C ANISOU 210 CA GLN A 28 7895 6711 8649 -218 -472 329 C ATOM 211 C GLN A 28 -339.080-150.596 160.170 1.00 59.86 C ANISOU 211 C GLN A 28 7688 6545 8512 -234 -451 193 C ATOM 212 O GLN A 28 -340.270-150.800 160.408 1.00 64.45 O ANISOU 212 O GLN A 28 8258 7111 9118 -204 -451 147 O ATOM 213 CB GLN A 28 -339.522-151.545 157.897 1.00 58.57 C ANISOU 213 CB GLN A 28 7596 6387 8271 -167 -504 393 C ATOM 214 CG GLN A 28 -339.056-151.795 156.476 1.00 61.97 C ANISOU 214 CG GLN A 28 8080 6824 8640 -171 -517 517 C ATOM 215 CD GLN A 28 -339.087-150.542 155.629 1.00 65.87 C ANISOU 215 CD GLN A 28 8588 7209 9231 -191 -548 596 C ATOM 216 OE1 GLN A 28 -340.120-149.880 155.523 1.00 60.84 O ANISOU 216 OE1 GLN A 28 7935 6479 8704 -167 -597 606 O ATOM 217 NE2 GLN A 28 -337.951-150.207 155.025 1.00 66.38 N ANISOU 217 NE2 GLN A 28 8677 7276 9269 -239 -520 656 N ATOM 218 N TYR A 29 -338.228-150.195 161.115 1.00 61.80 N ANISOU 218 N TYR A 29 7914 6813 8756 -294 -428 122 N ATOM 219 CA TYR A 29 -338.621-150.118 162.526 1.00 59.00 C ANISOU 219 CA TYR A 29 7541 6487 8390 -339 -399 -17 C ATOM 220 C TYR A 29 -339.548-148.962 162.829 1.00 61.18 C ANISOU 220 C TYR A 29 7781 6646 8818 -339 -365 -113 C ATOM 221 O TYR A 29 -339.856-148.803 164.022 1.00 67.84 O ANISOU 221 O TYR A 29 8613 7511 9653 -393 -320 -251 O ATOM 222 CB TYR A 29 -337.377-150.058 163.419 1.00 59.00 C ANISOU 222 CB TYR A 29 7536 6551 8329 -420 -401 -57 C ATOM 223 CG TYR A 29 -336.517-151.309 163.336 1.00 62.76 C ANISOU 223 CG TYR A 29 8027 7138 8682 -419 -438 24 C ATOM 224 CD1 TYR A 29 -337.093-152.570 163.174 1.00 60.59 C ANISOU 224 CD1 TYR A 29 7777 6926 8320 -375 -452 62 C ATOM 225 CD2 TYR A 29 -335.136-151.227 163.402 1.00 56.31 C ANISOU 225 CD2 TYR A 29 7188 6349 7858 -461 -460 60 C ATOM 226 CE1 TYR A 29 -336.302-153.718 163.092 1.00 57.43 C ANISOU 226 CE1 TYR A 29 7379 6606 7838 -370 -485 132 C ATOM 227 CE2 TYR A 29 -334.344-152.349 163.318 1.00 53.95 C ANISOU 227 CE2 TYR A 29 6882 6130 7487 -454 -494 130 C ATOM 228 CZ TYR A 29 -334.923-153.594 163.163 1.00 57.41 C ANISOU 228 CZ TYR A 29 7344 6621 7848 -406 -506 165 C ATOM 229 OH TYR A 29 -334.104-154.698 163.082 1.00 63.59 O ANISOU 229 OH TYR A 29 8108 7464 8589 -396 -539 231 O ATOM 230 N TYR A 30 -339.998-148.177 161.842 1.00 66.72 N ANISOU 230 N TYR A 30 8465 7224 9660 -290 -386 -50 N ATOM 231 CA TYR A 30 -341.090-147.224 162.027 1.00 65.83 C ANISOU 231 CA TYR A 30 8301 6981 9730 -268 -363 -132 C ATOM 232 C TYR A 30 -342.451-147.849 161.738 1.00 68.94 C ANISOU 232 C TYR A 30 8678 7370 10148 -204 -376 -124 C ATOM 233 O TYR A 30 -343.474-147.263 162.105 1.00 77.67 O ANISOU 233 O TYR A 30 9721 8380 11409 -186 -344 -220 O ATOM 234 CB TYR A 30 -340.880-145.978 161.141 1.00 65.16 C ANISOU 234 CB TYR A 30 8198 6746 9815 -253 -398 -54 C ATOM 235 CG TYR A 30 -340.450-146.333 159.741 1.00 63.76 C ANISOU 235 CG TYR A 30 8070 6583 9573 -226 -465 133 C ATOM 236 CD1 TYR A 30 -341.377-146.751 158.798 1.00 59.10 C ANISOU 236 CD1 TYR A 30 7492 5970 8993 -168 -523 231 C ATOM 237 CD2 TYR A 30 -339.113-146.301 159.375 1.00 57.00 C ANISOU 237 CD2 TYR A 30 7249 5772 8635 -270 -466 204 C ATOM 238 CE1 TYR A 30 -340.987-147.110 157.519 1.00 60.74 C ANISOU 238 CE1 TYR A 30 7761 6203 9114 -164 -576 391 C ATOM 239 CE2 TYR A 30 -338.713-146.660 158.097 1.00 56.71 C ANISOU 239 CE2 TYR A 30 7264 5757 8526 -262 -504 358 C ATOM 240 CZ TYR A 30 -339.653-147.061 157.175 1.00 60.67 C ANISOU 240 CZ TYR A 30 7792 6239 9019 -214 -557 449 C ATOM 241 OH TYR A 30 -339.258-147.419 155.907 1.00 64.66 O ANISOU 241 OH TYR A 30 8362 6775 9430 -226 -587 590 O ATOM 242 N LEU A 31 -342.484-149.024 161.095 1.00 63.85 N ANISOU 242 N LEU A 31 8078 6818 9365 -172 -418 -21 N ATOM 243 CA LEU A 31 -343.719-149.796 160.972 1.00 61.65 C ANISOU 243 CA LEU A 31 7786 6558 9082 -125 -429 -26 C ATOM 244 C LEU A 31 -344.029-150.589 162.230 1.00 60.52 C ANISOU 244 C LEU A 31 7642 6518 8836 -164 -364 -151 C ATOM 245 O LEU A 31 -345.206-150.829 162.531 1.00 61.84 O ANISOU 245 O LEU A 31 7770 6671 9056 -144 -337 -219 O ATOM 246 CB LEU A 31 -343.631-150.777 159.801 1.00 61.76 C ANISOU 246 CB LEU A 31 7855 6629 8980 -88 -494 123 C ATOM 247 CG LEU A 31 -343.474-150.168 158.417 1.00 65.10 C ANISOU 247 CG LEU A 31 8300 6968 9466 -66 -565 266 C ATOM 248 CD1 LEU A 31 -343.337-151.272 157.387 1.00 59.80 C ANISOU 248 CD1 LEU A 31 7698 6380 8645 -53 -607 383 C ATOM 249 CD2 LEU A 31 -344.659-149.259 158.116 1.00 63.35 C ANISOU 249 CD2 LEU A 31 8016 6601 9455 -26 -609 269 C ATOM 250 N ALA A 32 -342.998-151.044 162.939 1.00 60.04 N ANISOU 250 N ALA A 32 7623 6562 8627 -225 -345 -173 N ATOM 251 CA ALA A 32 -343.174-151.883 164.116 1.00 54.47 C ANISOU 251 CA ALA A 32 6936 5967 7792 -282 -302 -264 C ATOM 252 C ALA A 32 -341.884-151.876 164.916 1.00 56.16 C ANISOU 252 C ALA A 32 7183 6257 7898 -364 -303 -286 C ATOM 253 O ALA A 32 -340.799-151.681 164.363 1.00 57.95 O ANISOU 253 O ALA A 32 7420 6479 8119 -358 -344 -200 O ATOM 254 CB ALA A 32 -343.555-153.317 163.739 1.00 53.54 C ANISOU 254 CB ALA A 32 6851 5934 7557 -246 -336 -186 C ATOM 255 N GLU A 33 -342.023-152.083 166.221 1.00 54.99 N ANISOU 255 N GLU A 33 7050 6180 7663 -451 -257 -402 N ATOM 256 CA GLU A 33 -340.871-152.181 167.097 1.00 55.22 C ANISOU 256 CA GLU A 33 7115 6294 7573 -546 -278 -417 C ATOM 257 C GLU A 33 -340.004-153.382 166.706 1.00 69.76 C ANISOU 257 C GLU A 33 8986 8222 9298 -524 -359 -274 C ATOM 258 O GLU A 33 -340.489-154.336 166.087 1.00 64.72 O ANISOU 258 O GLU A 33 8357 7602 8630 -458 -379 -199 O ATOM 259 CB GLU A 33 -341.341-152.312 168.544 1.00 65.96 C ANISOU 259 CB GLU A 33 8502 7726 8834 -660 -219 -560 C ATOM 260 CG GLU A 33 -341.958-151.053 169.100 1.00 67.38 C ANISOU 260 CG GLU A 33 8647 7821 9134 -705 -120 -733 C ATOM 261 CD GLU A 33 -340.907-150.002 169.326 1.00 92.72 C ANISOU 261 CD GLU A 33 11853 10992 12387 -761 -130 -768 C ATOM 262 OE1 GLU A 33 -340.047-150.215 170.210 1.00101.81 O ANISOU 262 OE1 GLU A 33 13051 12240 13394 -871 -162 -786 O ATOM 263 OE2 GLU A 33 -340.917-148.989 168.597 1.00101.73 O ANISOU 263 OE2 GLU A 33 12944 12003 13708 -699 -120 -765 O ATOM 264 N PRO A 34 -338.707-153.353 167.028 1.00 67.87 N ANISOU 264 N PRO A 34 8753 8025 9009 -577 -408 -237 N ATOM 265 CA PRO A 34 -337.865-154.533 166.751 1.00 55.54 C ANISOU 265 CA PRO A 34 7201 6534 7366 -557 -483 -112 C ATOM 266 C PRO A 34 -338.395-155.825 167.372 1.00 58.40 C ANISOU 266 C PRO A 34 7601 6983 7604 -580 -504 -99 C ATOM 267 O PRO A 34 -338.310-156.885 166.741 1.00 52.90 O ANISOU 267 O PRO A 34 6908 6306 6887 -517 -540 0 O ATOM 268 CB PRO A 34 -336.502-154.127 167.332 1.00 54.47 C ANISOU 268 CB PRO A 34 7052 6427 7216 -635 -531 -107 C ATOM 269 CG PRO A 34 -336.484-152.611 167.206 1.00 55.07 C ANISOU 269 CG PRO A 34 7104 6413 7407 -650 -479 -188 C ATOM 270 CD PRO A 34 -337.913-152.156 167.366 1.00 55.28 C ANISOU 270 CD PRO A 34 7139 6389 7476 -637 -401 -294 C ATOM 271 N TRP A 35 -338.967-155.759 168.577 1.00 54.32 N ANISOU 271 N TRP A 35 7118 6516 7003 -678 -475 -201 N ATOM 272 CA TRP A 35 -339.504-156.960 169.200 1.00 54.25 C ANISOU 272 CA TRP A 35 7155 6590 6869 -717 -493 -182 C ATOM 273 C TRP A 35 -340.712-157.508 168.445 1.00 66.85 C ANISOU 273 C TRP A 35 8743 8153 8504 -625 -449 -170 C ATOM 274 O TRP A 35 -340.970-158.718 168.487 1.00 60.47 O ANISOU 274 O TRP A 35 7961 7394 7621 -617 -482 -106 O ATOM 275 CB TRP A 35 -339.872-156.690 170.661 1.00 55.40 C ANISOU 275 CB TRP A 35 7348 6802 6900 -866 -456 -304 C ATOM 276 CG TRP A 35 -341.105-155.837 170.885 1.00 66.71 C ANISOU 276 CG TRP A 35 8769 8186 8393 -880 -328 -464 C ATOM 277 CD1 TRP A 35 -341.131-154.493 171.123 1.00 65.13 C ANISOU 277 CD1 TRP A 35 8543 7923 8280 -915 -259 -592 C ATOM 278 CD2 TRP A 35 -342.477-156.276 170.931 1.00 61.73 C ANISOU 278 CD2 TRP A 35 8139 7555 7761 -864 -251 -520 C ATOM 279 NE1 TRP A 35 -342.419-154.067 171.302 1.00 62.45 N ANISOU 279 NE1 TRP A 35 8181 7537 8009 -915 -142 -727 N ATOM 280 CE2 TRP A 35 -343.268-155.136 171.189 1.00 60.33 C ANISOU 280 CE2 TRP A 35 7925 7310 7688 -885 -135 -686 C ATOM 281 CE3 TRP A 35 -343.111-157.516 170.773 1.00 66.13 C ANISOU 281 CE3 TRP A 35 8717 8157 8255 -835 -268 -451 C ATOM 282 CZ2 TRP A 35 -344.666-155.196 171.291 1.00 57.03 C ANISOU 282 CZ2 TRP A 35 7479 6867 7323 -875 -33 -785 C ATOM 283 CZ3 TRP A 35 -344.503-157.577 170.875 1.00 63.26 C ANISOU 283 CZ3 TRP A 35 8335 7776 7926 -831 -171 -545 C ATOM 284 CH2 TRP A 35 -345.262-156.423 171.131 1.00 64.44 C ANISOU 284 CH2 TRP A 35 8438 7859 8190 -850 -54 -710 C ATOM 285 N GLN A 36 -341.468-156.648 167.761 1.00 64.07 N ANISOU 285 N GLN A 36 8353 7712 8278 -559 -385 -226 N ATOM 286 CA GLN A 36 -342.558-157.148 166.933 1.00 63.22 C ANISOU 286 CA GLN A 36 8232 7569 8221 -472 -365 -199 C ATOM 287 C GLN A 36 -342.029-157.860 165.702 1.00 54.81 C ANISOU 287 C GLN A 36 7166 6491 7168 -380 -428 -60 C ATOM 288 O GLN A 36 -342.638-158.832 165.238 1.00 51.40 O ANISOU 288 O GLN A 36 6746 6073 6709 -335 -439 -13 O ATOM 289 CB GLN A 36 -343.501-156.002 166.553 1.00 53.26 C ANISOU 289 CB GLN A 36 6919 6205 7112 -431 -300 -285 C ATOM 290 CG GLN A 36 -344.210-155.456 167.777 1.00 58.71 C ANISOU 290 CG GLN A 36 7601 6905 7800 -523 -210 -450 C ATOM 291 CD GLN A 36 -344.933-154.136 167.541 1.00 66.90 C ANISOU 291 CD GLN A 36 8570 7819 9030 -489 -142 -553 C ATOM 292 OE1 GLN A 36 -344.415-153.223 166.893 1.00 67.20 O ANISOU 292 OE1 GLN A 36 8581 7771 9180 -445 -168 -520 O ATOM 293 NE2 GLN A 36 -346.128-154.027 168.096 1.00 61.27 N ANISOU 293 NE2 GLN A 36 7822 7089 8368 -516 -52 -679 N ATOM 294 N PHE A 37 -340.898-157.402 165.162 1.00 51.83 N ANISOU 294 N PHE A 37 6776 6088 6831 -360 -459 -3 N ATOM 295 CA PHE A 37 -340.241-158.162 164.106 1.00 54.10 C ANISOU 295 CA PHE A 37 7065 6374 7114 -295 -500 112 C ATOM 296 C PHE A 37 -339.751-159.503 164.642 1.00 61.47 C ANISOU 296 C PHE A 37 8018 7384 7954 -320 -548 164 C ATOM 297 O PHE A 37 -339.802-160.520 163.939 1.00 52.50 O ANISOU 297 O PHE A 37 6890 6252 6806 -266 -564 231 O ATOM 298 CB PHE A 37 -339.087-157.359 163.502 1.00 51.33 C ANISOU 298 CB PHE A 37 6691 5983 6830 -285 -508 151 C ATOM 299 CG PHE A 37 -339.524-156.345 162.471 1.00 52.22 C ANISOU 299 CG PHE A 37 6793 6006 7042 -238 -481 157 C ATOM 300 CD1 PHE A 37 -339.946-155.078 162.856 1.00 55.12 C ANISOU 300 CD1 PHE A 37 7140 6311 7492 -263 -452 78 C ATOM 301 CD2 PHE A 37 -339.513-156.660 161.116 1.00 51.02 C ANISOU 301 CD2 PHE A 37 6655 5827 6902 -179 -487 242 C ATOM 302 CE1 PHE A 37 -340.356-154.139 161.899 1.00 58.35 C ANISOU 302 CE1 PHE A 37 7536 6623 8012 -221 -446 103 C ATOM 303 CE2 PHE A 37 -339.921-155.729 160.161 1.00 59.60 C ANISOU 303 CE2 PHE A 37 7744 6833 8070 -152 -483 269 C ATOM 304 CZ PHE A 37 -340.342-154.466 160.554 1.00 58.68 C ANISOU 304 CZ PHE A 37 7599 6644 8052 -168 -470 208 C ATOM 305 N SER A 38 -339.290-159.526 165.897 1.00 51.61 N ANISOU 305 N SER A 38 6779 6191 6638 -410 -576 135 N ATOM 306 CA SER A 38 -338.831-160.771 166.493 1.00 59.25 C ANISOU 306 CA SER A 38 7763 7222 7526 -444 -644 202 C ATOM 307 C SER A 38 -339.984-161.748 166.670 1.00 60.33 C ANISOU 307 C SER A 38 7937 7386 7600 -441 -630 199 C ATOM 308 O SER A 38 -339.833-162.951 166.421 1.00 58.87 O ANISOU 308 O SER A 38 7759 7211 7399 -410 -673 278 O ATOM 309 CB SER A 38 -338.154-160.491 167.828 1.00 54.91 C ANISOU 309 CB SER A 38 7227 6730 6906 -562 -694 179 C ATOM 310 OG SER A 38 -337.036-159.657 167.642 1.00 56.94 O ANISOU 310 OG SER A 38 7443 6962 7232 -566 -713 187 O ATOM 311 N MET A 39 -341.144-161.243 167.101 1.00 55.35 N ANISOU 311 N MET A 39 7323 6758 6949 -475 -565 102 N ATOM 312 CA MET A 39 -342.326-162.089 167.228 1.00 55.40 C ANISOU 312 CA MET A 39 7355 6786 6910 -476 -539 90 C ATOM 313 C MET A 39 -342.796-162.587 165.870 1.00 57.56 C ANISOU 313 C MET A 39 7611 7006 7253 -363 -535 141 C ATOM 314 O MET A 39 -343.299-163.712 165.764 1.00 56.87 O ANISOU 314 O MET A 39 7543 6936 7128 -350 -549 180 O ATOM 315 CB MET A 39 -343.444-161.338 167.947 1.00 54.42 C ANISOU 315 CB MET A 39 7233 6667 6778 -537 -453 -43 C ATOM 316 CG MET A 39 -343.210-161.126 169.438 1.00 58.39 C ANISOU 316 CG MET A 39 7778 7245 7164 -683 -444 -108 C ATOM 317 SD MET A 39 -342.766-162.646 170.316 1.00 70.27 S ANISOU 317 SD MET A 39 9349 8842 8507 -773 -538 0 S ATOM 318 CE MET A 39 -344.146-163.721 169.888 1.00 64.54 C ANISOU 318 CE MET A 39 8629 8110 7782 -725 -495 11 C ATOM 319 N LEU A 40 -342.629-161.780 164.817 1.00 53.74 N ANISOU 319 N LEU A 40 7097 6458 6863 -293 -520 146 N ATOM 320 CA LEU A 40 -342.857-162.298 163.471 1.00 55.73 C ANISOU 320 CA LEU A 40 7348 6671 7155 -206 -528 208 C ATOM 321 C LEU A 40 -341.910-163.454 163.167 1.00 65.21 C ANISOU 321 C LEU A 40 8559 7892 8325 -186 -572 293 C ATOM 322 O LEU A 40 -342.315-164.461 162.570 1.00 63.61 O ANISOU 322 O LEU A 40 8373 7685 8111 -148 -578 328 O ATOM 323 CB LEU A 40 -342.695-161.189 162.434 1.00 49.75 C ANISOU 323 CB LEU A 40 6569 5847 6485 -158 -514 214 C ATOM 324 CG LEU A 40 -342.802-161.690 160.992 1.00 59.06 C ANISOU 324 CG LEU A 40 7765 6997 7678 -92 -527 282 C ATOM 325 CD1 LEU A 40 -344.171-162.323 160.739 1.00 56.26 C ANISOU 325 CD1 LEU A 40 7421 6641 7315 -72 -529 271 C ATOM 326 CD2 LEU A 40 -342.532-160.571 159.999 1.00 66.68 C ANISOU 326 CD2 LEU A 40 8723 7901 8711 -68 -522 307 C ATOM 327 N ALA A 41 -340.643-163.328 163.575 1.00 53.15 N ANISOU 327 N ALA A 41 7015 6379 6801 -213 -603 322 N ATOM 328 CA ALA A 41 -339.697-164.427 163.418 1.00 52.93 C ANISOU 328 CA ALA A 41 6975 6356 6779 -195 -646 397 C ATOM 329 C ALA A 41 -340.104-165.636 164.251 1.00 55.97 C ANISOU 329 C ALA A 41 7387 6779 7101 -231 -689 425 C ATOM 330 O ALA A 41 -340.031-166.771 163.776 1.00 49.84 O ANISOU 330 O ALA A 41 6610 5983 6343 -191 -706 474 O ATOM 331 CB ALA A 41 -338.289-163.968 163.817 1.00 50.30 C ANISOU 331 CB ALA A 41 6602 6028 6482 -224 -682 422 C ATOM 332 N ALA A 42 -340.523-165.410 165.499 1.00 50.42 N ANISOU 332 N ALA A 42 6710 6127 6322 -318 -703 390 N ATOM 333 CA ALA A 42 -340.911-166.519 166.355 1.00 50.76 C ANISOU 333 CA ALA A 42 6789 6209 6289 -375 -747 426 C ATOM 334 C ALA A 42 -342.083-167.286 165.748 1.00 60.80 C ANISOU 334 C ALA A 42 8080 7462 7558 -330 -708 418 C ATOM 335 O ALA A 42 -342.132-168.521 165.805 1.00 60.57 O ANISOU 335 O ALA A 42 8065 7430 7518 -328 -748 479 O ATOM 336 CB ALA A 42 -341.245-166.009 167.751 1.00 51.49 C ANISOU 336 CB ALA A 42 6919 6368 6277 -498 -747 373 C ATOM 337 N TYR A 43 -343.013-166.569 165.124 1.00 50.88 N ANISOU 337 N TYR A 43 6819 6186 6329 -293 -640 347 N ATOM 338 CA TYR A 43 -344.150-167.205 164.477 1.00 57.32 C ANISOU 338 CA TYR A 43 7644 6983 7153 -254 -612 338 C ATOM 339 C TYR A 43 -343.716-168.008 163.254 1.00 56.83 C ANISOU 339 C TYR A 43 7578 6876 7140 -174 -630 397 C ATOM 340 O TYR A 43 -344.202-169.126 163.035 1.00 58.54 O ANISOU 340 O TYR A 43 7812 7084 7345 -163 -640 422 O ATOM 341 CB TYR A 43 -345.166-166.125 164.112 1.00 61.48 C ANISOU 341 CB TYR A 43 8151 7488 7722 -235 -554 257 C ATOM 342 CG TYR A 43 -346.403-166.583 163.403 1.00 64.87 C ANISOU 342 CG TYR A 43 8577 7894 8177 -197 -536 244 C ATOM 343 CD1 TYR A 43 -347.173-167.631 163.888 1.00 62.44 C ANISOU 343 CD1 TYR A 43 8288 7614 7822 -234 -534 245 C ATOM 344 CD2 TYR A 43 -346.834-165.920 162.267 1.00 75.15 C ANISOU 344 CD2 TYR A 43 9856 9145 9552 -135 -529 235 C ATOM 345 CE1 TYR A 43 -348.328-168.026 163.230 1.00 66.36 C ANISOU 345 CE1 TYR A 43 8775 8089 8351 -204 -522 229 C ATOM 346 CE2 TYR A 43 -347.975-166.296 161.611 1.00 74.95 C ANISOU 346 CE2 TYR A 43 9824 9099 9554 -108 -531 229 C ATOM 347 CZ TYR A 43 -348.720-167.346 162.091 1.00 74.59 C ANISOU 347 CZ TYR A 43 9790 9082 9469 -140 -525 221 C ATOM 348 OH TYR A 43 -349.857-167.695 161.409 1.00 74.15 O ANISOU 348 OH TYR A 43 9720 9004 9451 -116 -533 213 O ATOM 349 N MET A 44 -342.808-167.457 162.442 1.00 52.16 N ANISOU 349 N MET A 44 6964 6253 6601 -127 -624 412 N ATOM 350 CA MET A 44 -342.225-168.242 161.354 1.00 54.54 C ANISOU 350 CA MET A 44 7262 6516 6944 -70 -623 453 C ATOM 351 C MET A 44 -341.505-169.474 161.889 1.00 62.08 C ANISOU 351 C MET A 44 8207 7467 7915 -79 -669 509 C ATOM 352 O MET A 44 -341.538-170.540 161.268 1.00 57.10 O ANISOU 352 O MET A 44 7581 6801 7312 -44 -665 528 O ATOM 353 CB MET A 44 -341.244-167.397 160.535 1.00 50.76 C ANISOU 353 CB MET A 44 6761 6013 6515 -39 -597 456 C ATOM 354 CG MET A 44 -341.846-166.216 159.791 1.00 52.76 C ANISOU 354 CG MET A 44 7026 6251 6771 -27 -565 424 C ATOM 355 SD MET A 44 -343.193-166.676 158.696 1.00 62.54 S ANISOU 355 SD MET A 44 8305 7472 7985 1 -556 417 S ATOM 356 CE MET A 44 -344.553-166.038 159.663 1.00 50.19 C ANISOU 356 CE MET A 44 6727 5923 6421 -28 -565 366 C ATOM 357 N PHE A 45 -340.844-169.348 163.038 1.00 54.92 N ANISOU 357 N PHE A 45 7284 6588 6996 -131 -721 539 N ATOM 358 CA PHE A 45 -340.136-170.494 163.588 1.00 55.96 C ANISOU 358 CA PHE A 45 7398 6704 7161 -143 -791 613 C ATOM 359 C PHE A 45 -341.117-171.582 164.010 1.00 59.33 C ANISOU 359 C PHE A 45 7868 7136 7539 -172 -812 634 C ATOM 360 O PHE A 45 -340.906-172.765 163.716 1.00 50.45 O ANISOU 360 O PHE A 45 6734 5962 6474 -141 -837 680 O ATOM 361 CB PHE A 45 -339.259-170.047 164.757 1.00 50.79 C ANISOU 361 CB PHE A 45 6723 6082 6491 -211 -864 651 C ATOM 362 CG PHE A 45 -338.413-171.140 165.350 1.00 55.30 C ANISOU 362 CG PHE A 45 7264 6628 7119 -227 -964 750 C ATOM 363 CD1 PHE A 45 -337.351-171.688 164.640 1.00 53.15 C ANISOU 363 CD1 PHE A 45 6918 6283 6992 -156 -974 786 C ATOM 364 CD2 PHE A 45 -338.655-171.590 166.639 1.00 52.26 C ANISOU 364 CD2 PHE A 45 6921 6286 6650 -324 -1050 807 C ATOM 365 CE1 PHE A 45 -336.556-172.679 165.201 1.00 52.83 C ANISOU 365 CE1 PHE A 45 6831 6200 7041 -165 -1079 883 C ATOM 366 CE2 PHE A 45 -337.855-172.584 167.207 1.00 53.66 C ANISOU 366 CE2 PHE A 45 7068 6429 6892 -344 -1169 921 C ATOM 367 CZ PHE A 45 -336.809-173.123 166.487 1.00 53.49 C ANISOU 367 CZ PHE A 45 6959 6321 7045 -258 -1189 960 C ATOM 368 N LEU A 46 -342.198-171.193 164.690 1.00 57.16 N ANISOU 368 N LEU A 46 7635 6914 7167 -234 -793 593 N ATOM 369 CA LEU A 46 -343.253-172.142 165.026 1.00 59.98 C ANISOU 369 CA LEU A 46 8033 7281 7476 -269 -796 602 C ATOM 370 C LEU A 46 -343.788-172.841 163.779 1.00 59.40 C ANISOU 370 C LEU A 46 7959 7155 7457 -193 -757 586 C ATOM 371 O LEU A 46 -343.946-174.068 163.766 1.00 57.11 O ANISOU 371 O LEU A 46 7681 6831 7188 -192 -785 629 O ATOM 372 CB LEU A 46 -344.381-171.421 165.763 1.00 61.36 C ANISOU 372 CB LEU A 46 8238 7517 7558 -343 -748 531 C ATOM 373 CG LEU A 46 -345.589-172.274 166.149 1.00 56.68 C ANISOU 373 CG LEU A 46 7681 6942 6912 -393 -732 526 C ATOM 374 CD1 LEU A 46 -345.171-173.245 167.200 1.00 59.70 C ANISOU 374 CD1 LEU A 46 8100 7342 7241 -475 -810 619 C ATOM 375 CD2 LEU A 46 -346.716-171.415 166.669 1.00 62.36 C ANISOU 375 CD2 LEU A 46 8407 7711 7576 -451 -656 428 C ATOM 376 N LEU A 47 -344.048-172.078 162.714 1.00 60.37 N ANISOU 376 N LEU A 47 8071 7265 7602 -137 -701 528 N ATOM 377 CA LEU A 47 -344.587-172.668 161.493 1.00 55.02 C ANISOU 377 CA LEU A 47 7404 6547 6953 -84 -670 509 C ATOM 378 C LEU A 47 -343.592-173.621 160.838 1.00 57.16 C ANISOU 378 C LEU A 47 7660 6759 7299 -38 -677 543 C ATOM 379 O LEU A 47 -343.992-174.648 160.281 1.00 56.82 O ANISOU 379 O LEU A 47 7634 6678 7276 -21 -668 539 O ATOM 380 CB LEU A 47 -345.005-171.575 160.515 1.00 48.56 C ANISOU 380 CB LEU A 47 6585 5730 6134 -52 -628 457 C ATOM 381 CG LEU A 47 -346.162-170.678 160.971 1.00 58.79 C ANISOU 381 CG LEU A 47 7878 7059 7401 -83 -613 409 C ATOM 382 CD1 LEU A 47 -346.288-169.454 160.068 1.00 58.19 C ANISOU 382 CD1 LEU A 47 7790 6967 7354 -48 -593 382 C ATOM 383 CD2 LEU A 47 -347.483-171.438 161.032 1.00 49.60 C ANISOU 383 CD2 LEU A 47 6727 5900 6219 -104 -611 391 C ATOM 384 N ILE A 48 -342.298-173.296 160.874 1.00 54.56 N ANISOU 384 N ILE A 48 7291 6415 7025 -20 -686 567 N ATOM 385 CA ILE A 48 -341.294-174.198 160.311 1.00 54.86 C ANISOU 385 CA ILE A 48 7293 6385 7167 25 -680 588 C ATOM 386 C ILE A 48 -341.224-175.482 161.130 1.00 60.40 C ANISOU 386 C ILE A 48 7985 7049 7914 6 -749 653 C ATOM 387 O ILE A 48 -341.299-176.591 160.591 1.00 58.61 O ANISOU 387 O ILE A 48 7759 6759 7753 35 -735 649 O ATOM 388 CB ILE A 48 -339.922-173.498 160.240 1.00 59.04 C ANISOU 388 CB ILE A 48 7763 6905 7764 44 -674 598 C ATOM 389 CG1 ILE A 48 -339.963-172.303 159.285 1.00 58.90 C ANISOU 389 CG1 ILE A 48 7761 6911 7708 58 -603 542 C ATOM 390 CG2 ILE A 48 -338.810-174.480 159.827 1.00 50.90 C ANISOU 390 CG2 ILE A 48 6669 5793 6877 89 -665 615 C ATOM 391 CD1 ILE A 48 -338.896-171.262 159.587 1.00 60.15 C ANISOU 391 CD1 ILE A 48 7871 7083 7899 51 -608 554 C ATOM 392 N MET A 49 -341.128-175.341 162.453 1.00 65.38 N ANISOU 392 N MET A 49 8618 7719 8506 -54 -826 714 N ATOM 393 CA MET A 49 -340.911-176.487 163.323 1.00 61.67 C ANISOU 393 CA MET A 49 8142 7212 8079 -87 -916 804 C ATOM 394 C MET A 49 -342.103-177.438 163.333 1.00 67.09 C ANISOU 394 C MET A 49 8882 7886 8723 -110 -909 803 C ATOM 395 O MET A 49 -341.919-178.648 163.491 1.00 60.88 O ANISOU 395 O MET A 49 8085 7029 8019 -107 -958 864 O ATOM 396 CB MET A 49 -340.584-175.997 164.733 1.00 59.65 C ANISOU 396 CB MET A 49 7895 7017 7753 -172 -1004 870 C ATOM 397 CG MET A 49 -339.258-175.246 164.834 1.00 62.39 C ANISOU 397 CG MET A 49 8177 7362 8165 -156 -1036 889 C ATOM 398 SD MET A 49 -337.815-176.324 164.620 1.00 72.14 S ANISOU 398 SD MET A 49 9310 8479 9620 -94 -1109 973 S ATOM 399 CE MET A 49 -337.482-176.083 162.878 1.00 71.30 C ANISOU 399 CE MET A 49 9157 8320 9612 14 -961 859 C ATOM 400 N LEU A 50 -343.322-176.923 163.167 1.00 66.16 N ANISOU 400 N LEU A 50 8812 7828 8499 -134 -852 737 N ATOM 401 CA LEU A 50 -344.484-177.792 163.039 1.00 56.58 C ANISOU 401 CA LEU A 50 7639 6602 7259 -154 -837 725 C ATOM 402 C LEU A 50 -344.768-178.182 161.595 1.00 63.61 C ANISOU 402 C LEU A 50 8527 7440 8201 -86 -773 658 C ATOM 403 O LEU A 50 -345.262-179.285 161.341 1.00 72.10 O ANISOU 403 O LEU A 50 9620 8465 9310 -87 -775 662 O ATOM 404 CB LEU A 50 -345.733-177.121 163.616 1.00 60.24 C ANISOU 404 CB LEU A 50 8139 7148 7600 -222 -808 683 C ATOM 405 CG LEU A 50 -345.740-176.721 165.091 1.00 64.01 C ANISOU 405 CG LEU A 50 8639 7695 7986 -321 -847 722 C ATOM 406 CD1 LEU A 50 -347.052-176.053 165.454 1.00 56.60 C ANISOU 406 CD1 LEU A 50 7723 6826 6956 -379 -781 644 C ATOM 407 CD2 LEU A 50 -345.497-177.919 165.980 1.00 60.93 C ANISOU 407 CD2 LEU A 50 8275 7279 7597 -385 -931 830 C ATOM 408 N GLY A 51 -344.457-177.314 160.644 1.00 61.06 N ANISOU 408 N GLY A 51 8191 7127 7881 -38 -719 599 N ATOM 409 CA GLY A 51 -344.883-177.520 159.277 1.00 59.28 C ANISOU 409 CA GLY A 51 7987 6876 7662 -2 -660 532 C ATOM 410 C GLY A 51 -343.973-178.401 158.452 1.00 62.43 C ANISOU 410 C GLY A 51 8364 7190 8166 44 -627 516 C ATOM 411 O GLY A 51 -344.455-179.137 157.585 1.00 63.98 O ANISOU 411 O GLY A 51 8589 7350 8371 50 -591 467 O ATOM 412 N PHE A 52 -342.653-178.333 158.679 1.00 58.22 N ANISOU 412 N PHE A 52 7774 6623 7723 72 -635 546 N ATOM 413 CA PHE A 52 -341.774-179.240 157.943 1.00 60.70 C ANISOU 413 CA PHE A 52 8049 6843 8172 117 -590 518 C ATOM 414 C PHE A 52 -341.983-180.696 158.343 1.00 57.37 C ANISOU 414 C PHE A 52 7620 6337 7840 115 -633 554 C ATOM 415 O PHE A 52 -342.182-181.531 157.444 1.00 60.13 O ANISOU 415 O PHE A 52 7985 6624 8239 131 -574 488 O ATOM 416 CB PHE A 52 -340.304-178.835 158.091 1.00 56.22 C ANISOU 416 CB PHE A 52 7401 6248 7711 150 -587 540 C ATOM 417 CG PHE A 52 -339.356-179.850 157.504 1.00 62.15 C ANISOU 417 CG PHE A 52 8087 6885 8643 197 -538 507 C ATOM 418 CD1 PHE A 52 -339.233-179.989 156.129 1.00 71.28 C ANISOU 418 CD1 PHE A 52 9258 8015 9810 214 -414 397 C ATOM 419 CD2 PHE A 52 -338.626-180.696 158.320 1.00 71.07 C ANISOU 419 CD2 PHE A 52 9139 7928 9935 217 -617 585 C ATOM 420 CE1 PHE A 52 -338.379-180.935 155.582 1.00 73.55 C ANISOU 420 CE1 PHE A 52 9479 8190 10278 252 -345 343 C ATOM 421 CE2 PHE A 52 -337.767-181.643 157.779 1.00 70.41 C ANISOU 421 CE2 PHE A 52 8976 7720 10056 267 -567 547 C ATOM 422 CZ PHE A 52 -337.646-181.762 156.409 1.00 71.47 C ANISOU 422 CZ PHE A 52 9120 7826 10209 287 -419 414 C ATOM 423 N PRO A 53 -341.928-181.083 159.627 1.00 59.20 N ANISOU 423 N PRO A 53 7836 6560 8098 86 -735 657 N ATOM 424 CA PRO A 53 -342.039-182.525 159.934 1.00 62.22 C ANISOU 424 CA PRO A 53 8210 6842 8589 82 -781 704 C ATOM 425 C PRO A 53 -343.351-183.136 159.470 1.00 66.62 C ANISOU 425 C PRO A 53 8836 7401 9077 54 -746 653 C ATOM 426 O PRO A 53 -343.339-184.165 158.786 1.00 72.44 O ANISOU 426 O PRO A 53 9567 8042 9917 79 -708 608 O ATOM 427 CB PRO A 53 -341.886-182.579 161.463 1.00 56.37 C ANISOU 427 CB PRO A 53 7463 6122 7834 27 -909 840 C ATOM 428 CG PRO A 53 -341.258-181.299 161.849 1.00 64.52 C ANISOU 428 CG PRO A 53 8473 7236 8806 21 -923 852 C ATOM 429 CD PRO A 53 -341.702-180.280 160.845 1.00 57.81 C ANISOU 429 CD PRO A 53 7652 6455 7856 43 -815 738 C ATOM 430 N ILE A 54 -344.485-182.516 159.803 1.00 63.44 N ANISOU 430 N ILE A 54 8490 7098 8515 2 -754 650 N ATOM 431 CA ILE A 54 -345.783-183.059 159.411 1.00 65.65 C ANISOU 431 CA ILE A 54 8824 7383 8737 -31 -731 605 C ATOM 432 C ILE A 54 -345.851-183.269 157.903 1.00 65.95 C ANISOU 432 C ILE A 54 8876 7386 8796 6 -646 494 C ATOM 433 O ILE A 54 -346.303-184.316 157.427 1.00 68.73 O ANISOU 433 O ILE A 54 9249 7672 9195 -2 -628 458 O ATOM 434 CB ILE A 54 -346.916-182.143 159.901 1.00 70.24 C ANISOU 434 CB ILE A 54 9441 8080 9168 -85 -737 601 C ATOM 435 CG1 ILE A 54 -346.882-182.050 161.423 1.00 76.36 C ANISOU 435 CG1 ILE A 54 10216 8893 9903 -147 -807 698 C ATOM 436 CG2 ILE A 54 -348.265-182.671 159.444 1.00 82.38 C ANISOU 436 CG2 ILE A 54 11017 9620 10664 -118 -717 553 C ATOM 437 CD1 ILE A 54 -347.971-181.188 161.990 1.00 82.86 C ANISOU 437 CD1 ILE A 54 11065 9821 10597 -208 -791 675 C ATOM 438 N ASN A 55 -345.403-182.283 157.126 1.00 59.99 N ANISOU 438 N ASN A 55 8118 6675 7999 34 -591 438 N ATOM 439 CA ASN A 55 -345.534-182.418 155.680 1.00 58.82 C ANISOU 439 CA ASN A 55 8005 6512 7834 42 -511 334 C ATOM 440 C ASN A 55 -344.480-183.355 155.104 1.00 63.87 C ANISOU 440 C ASN A 55 8608 7039 8622 79 -449 285 C ATOM 441 O ASN A 55 -344.767-184.118 154.176 1.00 68.38 O ANISOU 441 O ASN A 55 9213 7560 9207 67 -391 200 O ATOM 442 CB ASN A 55 -345.461-181.047 155.008 1.00 54.81 C ANISOU 442 CB ASN A 55 7517 6087 7222 43 -476 301 C ATOM 443 CG ASN A 55 -346.716-180.209 155.248 1.00 63.46 C ANISOU 443 CG ASN A 55 8645 7272 8196 7 -523 319 C ATOM 444 OD1 ASN A 55 -347.782-180.500 154.708 1.00 64.67 O ANISOU 444 OD1 ASN A 55 8839 7437 8295 -25 -531 285 O ATOM 445 ND2 ASN A 55 -346.581-179.150 156.040 1.00 61.88 N ANISOU 445 ND2 ASN A 55 8418 7128 7965 11 -554 367 N ATOM 446 N PHE A 56 -343.255-183.310 155.632 1.00 60.87 N ANISOU 446 N PHE A 56 8152 6612 8362 121 -459 331 N ATOM 447 CA PHE A 56 -342.244-184.253 155.176 1.00 63.13 C ANISOU 447 CA PHE A 56 8379 6772 8834 163 -398 282 C ATOM 448 C PHE A 56 -342.614-185.676 155.578 1.00 67.09 C ANISOU 448 C PHE A 56 8873 7165 9453 159 -442 309 C ATOM 449 O PHE A 56 -342.531-186.601 154.761 1.00 63.73 O ANISOU 449 O PHE A 56 8447 6644 9122 168 -366 214 O ATOM 450 CB PHE A 56 -340.869-183.872 155.732 1.00 57.35 C ANISOU 450 CB PHE A 56 7550 6010 8232 209 -418 337 C ATOM 451 CG PHE A 56 -339.786-184.822 155.335 1.00 69.43 C ANISOU 451 CG PHE A 56 8990 7396 9996 259 -356 287 C ATOM 452 CD1 PHE A 56 -339.145-184.689 154.116 1.00 73.61 C ANISOU 452 CD1 PHE A 56 9504 7903 10563 273 -209 153 C ATOM 453 CD2 PHE A 56 -339.433-185.873 156.165 1.00 75.30 C ANISOU 453 CD2 PHE A 56 9663 8017 10930 285 -443 370 C ATOM 454 CE1 PHE A 56 -338.154-185.581 153.741 1.00 76.54 C ANISOU 454 CE1 PHE A 56 9777 8130 11174 318 -131 85 C ATOM 455 CE2 PHE A 56 -338.453-186.764 155.797 1.00 77.49 C ANISOU 455 CE2 PHE A 56 9840 8141 11463 339 -387 319 C ATOM 456 CZ PHE A 56 -337.809-186.618 154.584 1.00 79.64 C ANISOU 456 CZ PHE A 56 10085 8389 11787 359 -222 167 C ATOM 457 N LEU A 57 -343.050-185.859 156.827 1.00 64.47 N ANISOU 457 N LEU A 57 8542 6845 9109 135 -560 433 N ATOM 458 CA LEU A 57 -343.433-187.182 157.298 1.00 67.75 C ANISOU 458 CA LEU A 57 8957 7156 9630 120 -615 481 C ATOM 459 C LEU A 57 -344.558-187.769 156.453 1.00 69.86 C ANISOU 459 C LEU A 57 9296 7417 9829 84 -558 384 C ATOM 460 O LEU A 57 -344.602-188.986 156.241 1.00 71.20 O ANISOU 460 O LEU A 57 9456 7463 10132 87 -546 358 O ATOM 461 CB LEU A 57 -343.833-187.115 158.773 1.00 70.06 C ANISOU 461 CB LEU A 57 9262 7494 9865 71 -745 633 C ATOM 462 CG LEU A 57 -344.064-188.443 159.490 1.00 93.80 C ANISOU 462 CG LEU A 57 12264 10388 12989 44 -828 725 C ATOM 463 CD1 LEU A 57 -342.762-189.238 159.633 1.00 95.44 C ANISOU 463 CD1 LEU A 57 12373 10435 13456 104 -866 774 C ATOM 464 CD2 LEU A 57 -344.725-188.202 160.842 1.00101.51 C ANISOU 464 CD2 LEU A 57 13286 11450 13834 -39 -933 856 C ATOM 465 N THR A 58 -345.462-186.923 155.950 1.00 66.86 N ANISOU 465 N THR A 58 8983 7162 9257 47 -529 332 N ATOM 466 CA THR A 58 -346.478-187.395 155.013 1.00 69.46 C ANISOU 466 CA THR A 58 9379 7493 9519 7 -483 235 C ATOM 467 C THR A 58 -345.839-187.986 153.762 1.00 73.52 C ANISOU 467 C THR A 58 9891 7919 10122 27 -371 102 C ATOM 468 O THR A 58 -346.290-189.018 153.253 1.00 78.10 O ANISOU 468 O THR A 58 10499 8422 10753 1 -340 31 O ATOM 469 CB THR A 58 -347.429-186.250 154.641 1.00 64.63 C ANISOU 469 CB THR A 58 8823 7025 8709 -31 -486 213 C ATOM 470 OG1 THR A 58 -348.269-185.940 155.759 1.00 62.63 O ANISOU 470 OG1 THR A 58 8571 6836 8388 -64 -568 307 O ATOM 471 CG2 THR A 58 -348.296-186.634 153.450 1.00 58.55 C ANISOU 471 CG2 THR A 58 8119 6259 7868 -76 -443 106 C ATOM 472 N LEU A 59 -344.784-187.347 153.254 1.00 71.12 N ANISOU 472 N LEU A 59 9556 7627 9842 64 -300 56 N ATOM 473 CA LEU A 59 -344.078-187.911 152.109 1.00 77.77 C ANISOU 473 CA LEU A 59 10389 8383 10776 74 -170 -86 C ATOM 474 C LEU A 59 -343.273-189.140 152.505 1.00 80.48 C ANISOU 474 C LEU A 59 10643 8551 11385 124 -161 -83 C ATOM 475 O LEU A 59 -343.061-190.035 151.680 1.00 84.42 O ANISOU 475 O LEU A 59 11140 8945 11991 119 -59 -211 O ATOM 476 CB LEU A 59 -343.160-186.862 151.483 1.00 73.90 C ANISOU 476 CB LEU A 59 9885 7954 10238 88 -86 -135 C ATOM 477 CG LEU A 59 -343.842-185.558 151.061 1.00 76.67 C ANISOU 477 CG LEU A 59 10318 8465 10350 41 -104 -124 C ATOM 478 CD1 LEU A 59 -342.827-184.572 150.471 1.00 66.82 C ANISOU 478 CD1 LEU A 59 9053 7262 9072 51 -19 -163 C ATOM 479 CD2 LEU A 59 -344.978-185.857 150.083 1.00 71.91 C ANISOU 479 CD2 LEU A 59 9820 7899 9604 -35 -85 -208 C ATOM 480 N TYR A 60 -342.833-189.210 153.759 1.00 74.28 N ANISOU 480 N TYR A 60 9784 7726 10714 165 -270 62 N ATOM 481 CA TYR A 60 -341.922-190.275 154.148 1.00 75.76 C ANISOU 481 CA TYR A 60 9867 7734 11183 219 -281 86 C ATOM 482 C TYR A 60 -342.660-191.587 154.401 1.00 81.54 C ANISOU 482 C TYR A 60 10622 8354 12006 195 -327 104 C ATOM 483 O TYR A 60 -342.186-192.654 153.994 1.00 81.14 O ANISOU 483 O TYR A 60 10517 8137 12176 224 -266 28 O ATOM 484 CB TYR A 60 -341.121-189.859 155.378 1.00 69.39 C ANISOU 484 CB TYR A 60 8976 6926 10464 259 -400 248 C ATOM 485 CG TYR A 60 -340.107-190.898 155.779 1.00 77.73 C ANISOU 485 CG TYR A 60 9908 7787 11837 319 -435 292 C ATOM 486 CD1 TYR A 60 -338.945-191.079 155.042 1.00 84.10 C ANISOU 486 CD1 TYR A 60 10614 8490 12852 379 -317 179 C ATOM 487 CD2 TYR A 60 -340.319-191.713 156.881 1.00 86.97 C ANISOU 487 CD2 TYR A 60 11059 8870 13114 309 -584 447 C ATOM 488 CE1 TYR A 60 -338.015-192.041 155.397 1.00 89.41 C ANISOU 488 CE1 TYR A 60 11150 8964 13856 442 -352 217 C ATOM 489 CE2 TYR A 60 -339.393-192.678 157.245 1.00 92.38 C ANISOU 489 CE2 TYR A 60 11623 9360 14116 365 -636 503 C ATOM 490 CZ TYR A 60 -338.244-192.838 156.499 1.00 92.82 C ANISOU 490 CZ TYR A 60 11563 9303 14402 438 -522 386 C ATOM 491 OH TYR A 60 -337.322-193.797 156.859 1.00100.61 O ANISOU 491 OH TYR A 60 12408 10078 15742 501 -578 441 O ATOM 492 N VAL A 61 -343.820-191.535 155.060 1.00 77.17 N ANISOU 492 N VAL A 61 10142 7881 11300 138 -426 197 N ATOM 493 CA VAL A 61 -344.564-192.756 155.325 1.00 76.77 C ANISOU 493 CA VAL A 61 10115 7727 11327 104 -471 222 C ATOM 494 C VAL A 61 -345.244-193.279 154.070 1.00 84.26 C ANISOU 494 C VAL A 61 11130 8655 12230 65 -359 48 C ATOM 495 O VAL A 61 -345.572-194.468 153.997 1.00 94.14 O ANISOU 495 O VAL A 61 12384 9775 13611 48 -358 20 O ATOM 496 CB VAL A 61 -345.594-192.535 156.446 1.00 77.28 C ANISOU 496 CB VAL A 61 10234 7889 11241 41 -597 369 C ATOM 497 CG1 VAL A 61 -344.909-191.943 157.669 1.00 78.95 C ANISOU 497 CG1 VAL A 61 10395 8137 11463 58 -704 531 C ATOM 498 CG2 VAL A 61 -346.726-191.652 155.959 1.00 79.87 C ANISOU 498 CG2 VAL A 61 10649 8388 11312 -13 -564 306 C ATOM 499 N THR A 62 -345.470-192.424 153.076 1.00 82.59 N ANISOU 499 N THR A 62 10978 8568 11836 41 -272 -67 N ATOM 500 CA THR A 62 -346.011-192.896 151.808 1.00 78.72 C ANISOU 500 CA THR A 62 10558 8063 11289 -11 -169 -237 C ATOM 501 C THR A 62 -344.998-193.759 151.068 1.00 78.32 C ANISOU 501 C THR A 62 10451 7848 11457 23 -39 -379 C ATOM 502 O THR A 62 -345.381-194.687 150.345 1.00 91.40 O ANISOU 502 O THR A 62 12147 9420 13161 -19 31 -506 O ATOM 503 CB THR A 62 -346.453-191.691 150.971 1.00 72.15 C ANISOU 503 CB THR A 62 9807 7408 10200 -57 -130 -299 C ATOM 504 OG1 THR A 62 -347.503-191.010 151.666 1.00 71.81 O ANISOU 504 OG1 THR A 62 9799 7491 9993 -88 -246 -182 O ATOM 505 CG2 THR A 62 -346.956-192.108 149.600 1.00 65.79 C ANISOU 505 CG2 THR A 62 9087 6603 9307 -131 -32 -472 C ATOM 506 N VAL A 63 -343.705-193.496 151.267 1.00 71.99 N ANISOU 506 N VAL A 63 9552 6993 10809 97 -3 -364 N ATOM 507 CA VAL A 63 -342.666-194.317 150.652 1.00 73.54 C ANISOU 507 CA VAL A 63 9666 7015 11259 139 130 -502 C ATOM 508 C VAL A 63 -342.587-195.691 151.319 1.00 81.34 C ANISOU 508 C VAL A 63 10581 7796 12531 175 67 -447 C ATOM 509 O VAL A 63 -342.271-196.694 150.664 1.00 79.84 O ANISOU 509 O VAL A 63 10356 7443 12537 181 179 -595 O ATOM 510 CB VAL A 63 -341.313-193.582 150.715 1.00 74.87 C ANISOU 510 CB VAL A 63 9732 7188 11527 207 180 -494 C ATOM 511 CG1 VAL A 63 -340.203-194.450 150.161 1.00 66.90 C ANISOU 511 CG1 VAL A 63 8611 5983 10823 256 323 -640 C ATOM 512 CG2 VAL A 63 -341.381-192.241 149.967 1.00 69.16 C ANISOU 512 CG2 VAL A 63 9090 6660 10529 161 250 -552 C ATOM 513 N GLN A 64 -342.888-195.767 152.616 1.00 82.33 N ANISOU 513 N GLN A 64 10685 7918 12679 189 -109 -238 N ATOM 514 CA GLN A 64 -342.733-196.998 153.375 1.00 84.85 C ANISOU 514 CA GLN A 64 10932 8037 13270 219 -197 -144 C ATOM 515 C GLN A 64 -343.978-197.876 153.394 1.00 83.58 C ANISOU 515 C GLN A 64 10858 7840 13060 147 -236 -146 C ATOM 516 O GLN A 64 -343.877-199.046 153.787 1.00 87.44 O ANISOU 516 O GLN A 64 11295 8136 13794 163 -282 -102 O ATOM 517 CB GLN A 64 -342.320-196.678 154.819 1.00 89.65 C ANISOU 517 CB GLN A 64 11477 8654 13931 253 -378 98 C ATOM 518 CG GLN A 64 -340.893-196.160 154.957 1.00 97.02 C ANISOU 518 CG GLN A 64 12285 9553 15026 335 -366 119 C ATOM 519 CD GLN A 64 -340.379-196.251 156.382 1.00100.12 C ANISOU 519 CD GLN A 64 12600 9890 15552 362 -562 358 C ATOM 520 OE1 GLN A 64 -341.143-196.491 157.319 1.00 96.32 O ANISOU 520 OE1 GLN A 64 12181 9438 14980 305 -704 517 O ATOM 521 NE2 GLN A 64 -339.074-196.067 156.551 1.00101.63 N ANISOU 521 NE2 GLN A 64 12655 10002 15958 437 -572 386 N ATOM 522 N HIS A 65 -345.136-197.365 152.974 1.00 69.04 N ANISOU 522 N HIS A 65 9138 6167 10928 68 -223 -192 N ATOM 523 CA HIS A 65 -346.395-198.097 153.102 1.00 72.86 C ANISOU 523 CA HIS A 65 9697 6635 11350 -8 -275 -176 C ATOM 524 C HIS A 65 -347.094-198.172 151.750 1.00 84.69 C ANISOU 524 C HIS A 65 11287 8186 12704 -77 -153 -383 C ATOM 525 O HIS A 65 -347.554-197.151 151.230 1.00 89.75 O ANISOU 525 O HIS A 65 11999 9012 13089 -116 -130 -425 O ATOM 526 CB HIS A 65 -347.277-197.442 154.165 1.00 70.21 C ANISOU 526 CB HIS A 65 9409 6453 10812 -53 -415 6 C ATOM 527 CG HIS A 65 -346.660-197.468 155.532 1.00 78.88 C ANISOU 527 CG HIS A 65 10437 7502 12030 -16 -546 214 C ATOM 528 ND1 HIS A 65 -347.021-198.387 156.497 1.00 78.45 N ANISOU 528 ND1 HIS A 65 10379 7343 12087 -50 -660 360 N ATOM 529 CD2 HIS A 65 -345.679-196.713 156.083 1.00 77.62 C ANISOU 529 CD2 HIS A 65 10214 7382 11898 42 -588 305 C ATOM 530 CE1 HIS A 65 -346.303-198.183 157.588 1.00 77.60 C ANISOU 530 CE1 HIS A 65 10214 7217 12053 -21 -774 538 C ATOM 531 NE2 HIS A 65 -345.481-197.173 157.363 1.00 77.44 N ANISOU 531 NE2 HIS A 65 10153 7282 11987 37 -734 504 N ATOM 532 N LYS A 66 -347.177-199.386 151.185 1.00 85.39 N ANISOU 532 N LYS A 66 11376 8106 12960 -98 -82 -510 N ATOM 533 CA LYS A 66 -347.728-199.550 149.840 1.00 85.85 C ANISOU 533 CA LYS A 66 11526 8202 12890 -177 40 -724 C ATOM 534 C LYS A 66 -349.202-199.180 149.786 1.00 81.14 C ANISOU 534 C LYS A 66 11036 7770 12024 -272 -40 -689 C ATOM 535 O LYS A 66 -349.679-198.671 148.764 1.00 86.60 O ANISOU 535 O LYS A 66 11813 8586 12504 -341 19 -813 O ATOM 536 CB LYS A 66 -347.532-200.994 149.350 1.00 90.71 C ANISOU 536 CB LYS A 66 12117 8588 13761 -186 131 -870 C ATOM 537 CG LYS A 66 -347.872-201.191 147.866 1.00 95.13 C ANISOU 537 CG LYS A 66 12771 9176 14198 -278 283 -1125 C ATOM 538 CD LYS A 66 -347.932-202.652 147.440 1.00100.32 C ANISOU 538 CD LYS A 66 13419 9611 15087 -308 363 -1274 C ATOM 539 CE LYS A 66 -347.981-202.771 145.916 1.00107.44 C ANISOU 539 CE LYS A 66 14412 10541 15871 -404 543 -1553 C ATOM 540 NZ LYS A 66 -346.788-202.142 145.255 1.00110.73 N ANISOU 540 NZ LYS A 66 14793 10985 16293 -367 700 -1677 N ATOM 541 N LYS A 67 -349.937-199.424 150.872 1.00 76.16 N ANISOU 541 N LYS A 67 10398 7139 11400 -286 -175 -519 N ATOM 542 CA LYS A 67 -351.371-199.165 150.890 1.00 77.85 C ANISOU 542 CA LYS A 67 10690 7489 11401 -376 -247 -488 C ATOM 543 C LYS A 67 -351.711-197.688 150.710 1.00 86.19 C ANISOU 543 C LYS A 67 11784 8770 12194 -387 -271 -460 C ATOM 544 O LYS A 67 -352.828-197.371 150.284 1.00 86.89 O ANISOU 544 O LYS A 67 11936 8974 12103 -464 -303 -490 O ATOM 545 CB LYS A 67 -351.965-199.682 152.200 1.00 76.43 C ANISOU 545 CB LYS A 67 10484 7262 11293 -391 -370 -305 C ATOM 546 CG LYS A 67 -351.846-201.186 152.379 1.00 82.50 C ANISOU 546 CG LYS A 67 11226 7802 12320 -397 -368 -316 C ATOM 547 CD LYS A 67 -352.728-201.916 151.388 1.00 84.68 C ANISOU 547 CD LYS A 67 11569 8042 12565 -486 -311 -483 C ATOM 548 CE LYS A 67 -352.941-203.359 151.798 1.00101.74 C ANISOU 548 CE LYS A 67 13709 9990 14958 -511 -338 -456 C ATOM 549 NZ LYS A 67 -354.100-203.953 151.075 1.00109.07 N ANISOU 549 NZ LYS A 67 14710 10920 15812 -621 -318 -580 N ATOM 550 N LEU A 68 -350.790-196.775 151.029 1.00 84.25 N ANISOU 550 N LEU A 68 11494 8582 11936 -314 -266 -398 N ATOM 551 CA LEU A 68 -351.082-195.355 150.872 1.00 79.24 C ANISOU 551 CA LEU A 68 10891 8145 11072 -322 -290 -369 C ATOM 552 C LEU A 68 -351.010-194.899 149.422 1.00 75.89 C ANISOU 552 C LEU A 68 10534 7791 10509 -364 -196 -532 C ATOM 553 O LEU A 68 -351.638-193.894 149.073 1.00 75.66 O ANISOU 553 O LEU A 68 10553 7918 10276 -403 -234 -520 O ATOM 554 CB LEU A 68 -350.130-194.510 151.725 1.00 71.35 C ANISOU 554 CB LEU A 68 9825 7182 10102 -240 -319 -247 C ATOM 555 CG LEU A 68 -350.227-194.698 153.245 1.00 66.82 C ANISOU 555 CG LEU A 68 9202 6582 9605 -221 -430 -62 C ATOM 556 CD1 LEU A 68 -349.185-193.888 153.991 1.00 59.69 C ANISOU 556 CD1 LEU A 68 8238 5712 8730 -151 -459 41 C ATOM 557 CD2 LEU A 68 -351.601-194.344 153.743 1.00 65.87 C ANISOU 557 CD2 LEU A 68 9121 6580 9326 -291 -508 7 C ATOM 558 N ARG A 69 -350.290-195.625 148.566 1.00 73.00 N ANISOU 558 N ARG A 69 10175 7311 10251 -366 -74 -687 N ATOM 559 CA ARG A 69 -350.071-195.204 147.183 1.00 76.70 C ANISOU 559 CA ARG A 69 10719 7848 10575 -423 33 -849 C ATOM 560 C ARG A 69 -351.269-195.554 146.294 1.00 83.09 C ANISOU 560 C ARG A 69 11632 8706 11231 -545 17 -947 C ATOM 561 O ARG A 69 -351.168-196.279 145.306 1.00 92.27 O ANISOU 561 O ARG A 69 12850 9803 12405 -612 120 -1122 O ATOM 562 CB ARG A 69 -348.782-195.814 146.650 1.00 72.12 C ANISOU 562 CB ARG A 69 10098 7127 10176 -387 192 -991 C ATOM 563 CG ARG A 69 -347.533-195.328 147.384 1.00 69.79 C ANISOU 563 CG ARG A 69 9694 6798 10026 -273 204 -900 C ATOM 564 CD ARG A 69 -346.251-195.766 146.687 1.00 76.26 C ANISOU 564 CD ARG A 69 10464 7494 11019 -244 381 -1064 C ATOM 565 NE ARG A 69 -346.043-197.210 146.739 1.00 87.23 N ANISOU 565 NE ARG A 69 11800 8668 12677 -227 433 -1147 N ATOM 566 CZ ARG A 69 -345.461-197.845 147.753 1.00 90.12 C ANISOU 566 CZ ARG A 69 12044 8872 13324 -131 377 -1040 C ATOM 567 NH1 ARG A 69 -345.308-199.161 147.711 1.00 85.78 N ANISOU 567 NH1 ARG A 69 11448 8114 13031 -120 424 -1121 N ATOM 568 NH2 ARG A 69 -345.034-197.165 148.810 1.00 83.76 N ANISOU 568 NH2 ARG A 69 11167 8112 12547 -55 266 -850 N ATOM 569 N THR A 70 -352.420-194.996 146.652 1.00 84.94 N ANISOU 569 N THR A 70 11888 9061 11323 -580 -114 -838 N ATOM 570 CA THR A 70 -353.611-195.110 145.823 1.00 88.12 C ANISOU 570 CA THR A 70 12380 9536 11567 -699 -160 -907 C ATOM 571 C THR A 70 -353.833-193.817 145.043 1.00 89.55 C ANISOU 571 C THR A 70 12626 9889 11510 -747 -192 -903 C ATOM 572 O THR A 70 -353.401-192.744 145.478 1.00 86.63 O ANISOU 572 O THR A 70 12219 9597 11102 -680 -216 -802 O ATOM 573 CB THR A 70 -354.845-195.405 146.681 1.00 83.16 C ANISOU 573 CB THR A 70 11721 8915 10962 -716 -289 -795 C ATOM 574 OG1 THR A 70 -355.145-194.263 147.489 1.00 89.44 O ANISOU 574 OG1 THR A 70 12469 9829 11685 -668 -381 -639 O ATOM 575 CG2 THR A 70 -354.578-196.585 147.590 1.00 85.85 C ANISOU 575 CG2 THR A 70 11998 9086 11536 -669 -274 -760 C ATOM 576 N PRO A 71 -354.498-193.889 143.883 1.00 89.57 N ANISOU 576 N PRO A 71 12731 9952 11352 -871 -202 -1007 N ATOM 577 CA PRO A 71 -354.708-192.664 143.085 1.00 81.85 C ANISOU 577 CA PRO A 71 11822 9131 10146 -930 -251 -986 C ATOM 578 C PRO A 71 -355.444-191.558 143.831 1.00 81.18 C ANISOU 578 C PRO A 71 11681 9153 10013 -884 -399 -809 C ATOM 579 O PRO A 71 -355.105-190.377 143.674 1.00 85.44 O ANISOU 579 O PRO A 71 12227 9786 10452 -863 -418 -747 O ATOM 580 CB PRO A 71 -355.513-193.178 141.884 1.00 84.43 C ANISOU 580 CB PRO A 71 12264 9487 10329 -1086 -272 -1110 C ATOM 581 CG PRO A 71 -355.095-194.618 141.753 1.00 75.25 C ANISOU 581 CG PRO A 71 11107 8168 9319 -1101 -144 -1263 C ATOM 582 CD PRO A 71 -354.947-195.098 143.169 1.00 78.85 C ANISOU 582 CD PRO A 71 11436 8512 10012 -971 -161 -1156 C ATOM 583 N LEU A 72 -356.430-191.910 144.656 1.00 75.64 N ANISOU 583 N LEU A 72 10917 8432 9390 -872 -495 -731 N ATOM 584 CA LEU A 72 -357.168-190.917 145.427 1.00 74.12 C ANISOU 584 CA LEU A 72 10656 8329 9177 -831 -615 -583 C ATOM 585 C LEU A 72 -356.276-190.166 146.409 1.00 81.55 C ANISOU 585 C LEU A 72 11524 9275 10185 -712 -582 -486 C ATOM 586 O LEU A 72 -356.657-189.089 146.887 1.00 78.27 O ANISOU 586 O LEU A 72 11063 8943 9732 -679 -657 -382 O ATOM 587 CB LEU A 72 -358.316-191.601 146.170 1.00 72.51 C ANISOU 587 CB LEU A 72 10396 8090 9065 -850 -690 -539 C ATOM 588 CG LEU A 72 -359.590-190.810 146.483 1.00 77.68 C ANISOU 588 CG LEU A 72 10997 8840 9679 -871 -824 -444 C ATOM 589 CD1 LEU A 72 -359.960-189.843 145.357 1.00 76.37 C ANISOU 589 CD1 LEU A 72 10887 8780 9351 -934 -906 -448 C ATOM 590 CD2 LEU A 72 -360.736-191.784 146.757 1.00 73.72 C ANISOU 590 CD2 LEU A 72 10467 8294 9251 -934 -875 -457 C ATOM 591 N ASN A 73 -355.099-190.706 146.719 1.00 74.94 N ANISOU 591 N ASN A 73 10669 8345 9461 -650 -474 -520 N ATOM 592 CA ASN A 73 -354.187-190.074 147.658 1.00 68.41 C ANISOU 592 CA ASN A 73 9771 7516 8704 -547 -451 -429 C ATOM 593 C ASN A 73 -353.114-189.233 146.977 1.00 68.13 C ANISOU 593 C ASN A 73 9766 7525 8595 -527 -378 -464 C ATOM 594 O ASN A 73 -352.358-188.551 147.675 1.00 61.35 O ANISOU 594 O ASN A 73 8850 6679 7780 -447 -367 -389 O ATOM 595 CB ASN A 73 -353.496-191.130 148.539 1.00 67.16 C ANISOU 595 CB ASN A 73 9555 7220 8741 -486 -399 -417 C ATOM 596 CG ASN A 73 -354.417-191.745 149.593 1.00 66.96 C ANISOU 596 CG ASN A 73 9488 7162 8794 -495 -476 -332 C ATOM 597 OD1 ASN A 73 -355.482-191.222 149.921 1.00 70.18 O ANISOU 597 OD1 ASN A 73 9883 7656 9128 -526 -559 -270 O ATOM 598 ND2 ASN A 73 -353.976-192.864 150.149 1.00 74.82 N ANISOU 598 ND2 ASN A 73 10452 8021 9955 -471 -446 -328 N ATOM 599 N TYR A 74 -353.006-189.283 145.644 1.00 65.07 N ANISOU 599 N TYR A 74 9471 7161 8092 -608 -325 -579 N ATOM 600 CA TYR A 74 -352.013-188.458 144.962 1.00 64.96 C ANISOU 600 CA TYR A 74 9492 7196 7992 -607 -247 -612 C ATOM 601 C TYR A 74 -352.204-186.979 145.291 1.00 69.75 C ANISOU 601 C TYR A 74 10076 7914 8510 -576 -337 -483 C ATOM 602 O TYR A 74 -351.227-186.248 145.505 1.00 69.87 O ANISOU 602 O TYR A 74 10061 7944 8542 -518 -287 -451 O ATOM 603 CB TYR A 74 -352.083-188.666 143.445 1.00 70.70 C ANISOU 603 CB TYR A 74 10344 7956 8564 -735 -190 -749 C ATOM 604 CG TYR A 74 -351.630-190.017 142.934 1.00 75.74 C ANISOU 604 CG TYR A 74 11012 8478 9287 -774 -56 -916 C ATOM 605 CD1 TYR A 74 -351.365-191.073 143.800 1.00 81.57 C ANISOU 605 CD1 TYR A 74 11664 9078 10250 -696 -21 -925 C ATOM 606 CD2 TYR A 74 -351.463-190.233 141.571 1.00 80.05 C ANISOU 606 CD2 TYR A 74 11675 9049 9690 -899 35 -1068 C ATOM 607 CE1 TYR A 74 -350.954-192.313 143.318 1.00 82.61 C ANISOU 607 CE1 TYR A 74 11814 9084 10491 -728 103 -1084 C ATOM 608 CE2 TYR A 74 -351.052-191.465 141.083 1.00 87.84 C ANISOU 608 CE2 TYR A 74 12687 9922 10766 -941 175 -1244 C ATOM 609 CZ TYR A 74 -350.799-192.499 141.957 1.00 89.56 C ANISOU 609 CZ TYR A 74 12805 9988 11237 -848 209 -1254 C ATOM 610 OH TYR A 74 -350.392-193.720 141.463 1.00101.00 O ANISOU 610 OH TYR A 74 14269 11305 12803 -885 349 -1435 O ATOM 611 N ILE A 75 -353.457-186.519 145.346 1.00 67.72 N ANISOU 611 N ILE A 75 9824 7727 8179 -612 -471 -412 N ATOM 612 CA ILE A 75 -353.695-185.100 145.579 1.00 66.74 C ANISOU 612 CA ILE A 75 9673 7693 7991 -585 -556 -300 C ATOM 613 C ILE A 75 -353.251-184.704 146.983 1.00 68.45 C ANISOU 613 C ILE A 75 9785 7890 8333 -474 -552 -211 C ATOM 614 O ILE A 75 -352.873-183.548 147.220 1.00 61.26 O ANISOU 614 O ILE A 75 8848 7030 7396 -434 -567 -144 O ATOM 615 CB ILE A 75 -355.175-184.745 145.320 1.00 62.99 C ANISOU 615 CB ILE A 75 9207 7281 7447 -647 -702 -250 C ATOM 616 CG1 ILE A 75 -355.321-183.238 145.094 1.00 66.71 C ANISOU 616 CG1 ILE A 75 9675 7835 7838 -644 -784 -158 C ATOM 617 CG2 ILE A 75 -356.060-185.203 146.466 1.00 56.52 C ANISOU 617 CG2 ILE A 75 8295 6429 6750 -608 -758 -201 C ATOM 618 CD1 ILE A 75 -354.495-182.724 143.932 1.00 66.54 C ANISOU 618 CD1 ILE A 75 9754 7853 7674 -703 -734 -192 C ATOM 619 N LEU A 76 -353.264-185.652 147.927 1.00 62.58 N ANISOU 619 N LEU A 76 8985 7070 7720 -434 -534 -206 N ATOM 620 CA LEU A 76 -352.820-185.347 149.284 1.00 64.62 C ANISOU 620 CA LEU A 76 9159 7315 8080 -350 -537 -118 C ATOM 621 C LEU A 76 -351.306-185.228 149.353 1.00 72.08 C ANISOU 621 C LEU A 76 10086 8221 9080 -292 -446 -131 C ATOM 622 O LEU A 76 -350.773-184.429 150.133 1.00 69.91 O ANISOU 622 O LEU A 76 9760 7973 8832 -235 -456 -57 O ATOM 623 CB LEU A 76 -353.310-186.418 150.257 1.00 63.09 C ANISOU 623 CB LEU A 76 8922 7053 7996 -345 -557 -92 C ATOM 624 CG LEU A 76 -354.819-186.485 150.491 1.00 63.95 C ANISOU 624 CG LEU A 76 9020 7201 8079 -396 -643 -66 C ATOM 625 CD1 LEU A 76 -355.173-187.658 151.411 1.00 64.37 C ANISOU 625 CD1 LEU A 76 9041 7178 8239 -404 -646 -43 C ATOM 626 CD2 LEU A 76 -355.315-185.161 151.058 1.00 58.09 C ANISOU 626 CD2 LEU A 76 8228 6548 7296 -375 -702 12 C ATOM 627 N LEU A 77 -350.593-186.034 148.566 1.00 68.50 N ANISOU 627 N LEU A 77 9669 7699 8659 -309 -351 -234 N ATOM 628 CA LEU A 77 -349.150-185.858 148.474 1.00 68.84 C ANISOU 628 CA LEU A 77 9685 7706 8767 -260 -253 -262 C ATOM 629 C LEU A 77 -348.823-184.515 147.844 1.00 68.14 C ANISOU 629 C LEU A 77 9630 7714 8546 -275 -243 -250 C ATOM 630 O LEU A 77 -347.876-183.834 148.258 1.00 67.29 O ANISOU 630 O LEU A 77 9473 7614 8482 -220 -214 -208 O ATOM 631 CB LEU A 77 -348.535-187.000 147.670 1.00 70.09 C ANISOU 631 CB LEU A 77 9869 7765 8999 -284 -135 -399 C ATOM 632 CG LEU A 77 -348.700-188.397 148.267 1.00 72.85 C ANISOU 632 CG LEU A 77 10176 7987 9514 -264 -139 -411 C ATOM 633 CD1 LEU A 77 -348.223-189.430 147.268 1.00 77.94 C ANISOU 633 CD1 LEU A 77 10855 8535 10222 -302 -12 -574 C ATOM 634 CD2 LEU A 77 -347.931-188.516 149.577 1.00 71.36 C ANISOU 634 CD2 LEU A 77 9884 7732 9498 -171 -167 -308 C ATOM 635 N ASN A 78 -349.614-184.121 146.841 1.00 68.09 N ANISOU 635 N ASN A 78 9710 7780 8381 -359 -278 -277 N ATOM 636 CA ASN A 78 -349.495-182.799 146.238 1.00 68.81 C ANISOU 636 CA ASN A 78 9843 7964 8340 -387 -297 -240 C ATOM 637 C ASN A 78 -349.671-181.706 147.280 1.00 69.63 C ANISOU 637 C ASN A 78 9873 8109 8472 -320 -383 -116 C ATOM 638 O ASN A 78 -348.950-180.700 147.270 1.00 66.67 O ANISOU 638 O ASN A 78 9487 7768 8076 -297 -361 -80 O ATOM 639 CB ASN A 78 -350.536-182.648 145.135 1.00 72.82 C ANISOU 639 CB ASN A 78 10449 8534 8683 -495 -366 -261 C ATOM 640 CG ASN A 78 -350.211-181.533 144.184 1.00 70.00 C ANISOU 640 CG ASN A 78 10165 8254 8178 -555 -364 -243 C ATOM 641 OD1 ASN A 78 -349.084-181.433 143.701 1.00 66.17 O ANISOU 641 OD1 ASN A 78 9706 7762 7672 -567 -242 -301 O ATOM 642 ND2 ASN A 78 -351.195-180.674 143.913 1.00 60.75 N ANISOU 642 ND2 ASN A 78 9021 7150 6912 -596 -500 -157 N ATOM 643 N LEU A 79 -350.629-181.888 148.188 1.00 64.78 N ANISOU 643 N LEU A 79 9210 7492 7910 -297 -470 -59 N ATOM 644 CA LEU A 79 -350.818-180.929 149.267 1.00 58.96 C ANISOU 644 CA LEU A 79 8401 6790 7209 -242 -531 37 C ATOM 645 C LEU A 79 -349.585-180.843 150.155 1.00 61.00 C ANISOU 645 C LEU A 79 8599 7015 7563 -172 -474 63 C ATOM 646 O LEU A 79 -349.176-179.746 150.550 1.00 65.50 O ANISOU 646 O LEU A 79 9138 7624 8127 -140 -485 115 O ATOM 647 CB LEU A 79 -352.047-181.314 150.086 1.00 54.05 C ANISOU 647 CB LEU A 79 7738 6168 6630 -246 -608 72 C ATOM 648 CG LEU A 79 -352.299-180.514 151.359 1.00 56.20 C ANISOU 648 CG LEU A 79 7934 6470 6950 -202 -649 149 C ATOM 649 CD1 LEU A 79 -352.640-179.033 151.068 1.00 51.33 C ANISOU 649 CD1 LEU A 79 7308 5914 6281 -201 -700 188 C ATOM 650 CD2 LEU A 79 -353.395-181.200 152.162 1.00 51.68 C ANISOU 650 CD2 LEU A 79 7326 5886 6426 -222 -689 162 C ATOM 651 N ALA A 80 -348.979-181.990 150.481 1.00 62.69 N ANISOU 651 N ALA A 80 8791 7150 7879 -149 -420 29 N ATOM 652 CA ALA A 80 -347.785-181.986 151.323 1.00 58.20 C ANISOU 652 CA ALA A 80 8155 6540 7420 -86 -386 64 C ATOM 653 C ALA A 80 -346.652-181.210 150.668 1.00 62.28 C ANISOU 653 C ALA A 80 8674 7074 7916 -74 -313 37 C ATOM 654 O ALA A 80 -345.961-180.425 151.329 1.00 59.67 O ANISOU 654 O ALA A 80 8292 6762 7619 -33 -322 93 O ATOM 655 CB ALA A 80 -347.344-183.412 151.626 1.00 53.24 C ANISOU 655 CB ALA A 80 7498 5803 6928 -67 -352 36 C ATOM 656 N VAL A 81 -346.458-181.404 149.364 1.00 61.45 N ANISOU 656 N VAL A 81 8634 6967 7749 -121 -237 -54 N ATOM 657 CA VAL A 81 -345.395-180.695 148.665 1.00 64.46 C ANISOU 657 CA VAL A 81 9024 7367 8100 -128 -151 -87 C ATOM 658 C VAL A 81 -345.665-179.196 148.660 1.00 69.69 C ANISOU 658 C VAL A 81 9704 8119 8656 -138 -213 -11 C ATOM 659 O VAL A 81 -344.760-178.390 148.907 1.00 69.25 O ANISOU 659 O VAL A 81 9608 8075 8629 -108 -185 20 O ATOM 660 CB VAL A 81 -345.236-181.251 147.240 1.00 64.50 C ANISOU 660 CB VAL A 81 9113 7361 8034 -203 -46 -210 C ATOM 661 CG1 VAL A 81 -344.222-180.426 146.469 1.00 66.73 C ANISOU 661 CG1 VAL A 81 9416 7678 8260 -231 51 -244 C ATOM 662 CG2 VAL A 81 -344.821-182.719 147.285 1.00 61.55 C ANISOU 662 CG2 VAL A 81 8703 6875 7806 -183 33 -300 C ATOM 663 N ALA A 82 -346.914-178.801 148.390 1.00 69.21 N ANISOU 663 N ALA A 82 9695 8112 8491 -181 -304 23 N ATOM 664 CA ALA A 82 -347.254-177.383 148.342 1.00 61.73 C ANISOU 664 CA ALA A 82 8756 7230 7469 -189 -373 97 C ATOM 665 C ALA A 82 -346.969-176.705 149.671 1.00 62.73 C ANISOU 665 C ALA A 82 8794 7357 7685 -118 -407 167 C ATOM 666 O ALA A 82 -346.488-175.565 149.708 1.00 67.24 O ANISOU 666 O ALA A 82 9352 7956 8242 -108 -408 207 O ATOM 667 CB ALA A 82 -348.725-177.207 147.972 1.00 52.55 C ANISOU 667 CB ALA A 82 7635 6103 6227 -237 -481 125 C ATOM 668 N ASP A 83 -347.287-177.384 150.776 1.00 60.26 N ANISOU 668 N ASP A 83 8426 7015 7455 -82 -438 183 N ATOM 669 CA ASP A 83 -346.989-176.836 152.092 1.00 58.69 C ANISOU 669 CA ASP A 83 8155 6823 7322 -35 -467 242 C ATOM 670 C ASP A 83 -345.485-176.692 152.301 1.00 66.74 C ANISOU 670 C ASP A 83 9134 7817 8408 -1 -404 242 C ATOM 671 O ASP A 83 -345.035-175.738 152.950 1.00 68.44 O ANISOU 671 O ASP A 83 9309 8056 8639 20 -422 286 O ATOM 672 CB ASP A 83 -347.597-177.717 153.183 1.00 57.89 C ANISOU 672 CB ASP A 83 8019 6699 7277 -27 -508 262 C ATOM 673 CG ASP A 83 -349.131-177.779 153.123 1.00 67.74 C ANISOU 673 CG ASP A 83 9286 7973 8479 -62 -568 262 C ATOM 674 OD1 ASP A 83 -349.759-176.902 152.493 1.00 65.98 O ANISOU 674 OD1 ASP A 83 9083 7789 8199 -81 -602 266 O ATOM 675 OD2 ASP A 83 -349.713-178.712 153.730 1.00 64.83 O ANISOU 675 OD2 ASP A 83 8905 7581 8146 -73 -587 265 O ATOM 676 N LEU A 84 -344.698-177.617 151.745 1.00 59.15 N ANISOU 676 N LEU A 84 8174 6801 7498 3 -328 186 N ATOM 677 CA LEU A 84 -343.249-177.496 151.814 1.00 63.75 C ANISOU 677 CA LEU A 84 8702 7351 8168 35 -261 176 C ATOM 678 C LEU A 84 -342.760-176.285 151.022 1.00 64.70 C ANISOU 678 C LEU A 84 8851 7520 8213 10 -216 169 C ATOM 679 O LEU A 84 -341.839-175.588 151.460 1.00 56.85 O ANISOU 679 O LEU A 84 7801 6529 7271 36 -203 199 O ATOM 680 CB LEU A 84 -342.599-178.794 151.329 1.00 54.53 C ANISOU 680 CB LEU A 84 7520 6100 7100 43 -176 100 C ATOM 681 CG LEU A 84 -342.713-179.945 152.337 1.00 59.95 C ANISOU 681 CG LEU A 84 8153 6714 7909 78 -229 133 C ATOM 682 CD1 LEU A 84 -342.137-181.236 151.765 1.00 53.78 C ANISOU 682 CD1 LEU A 84 7351 5830 7253 89 -143 48 C ATOM 683 CD2 LEU A 84 -342.037-179.588 153.668 1.00 54.86 C ANISOU 683 CD2 LEU A 84 7426 6065 7353 119 -296 226 C ATOM 684 N PHE A 85 -343.378-176.002 149.870 1.00 60.28 N ANISOU 684 N PHE A 85 8379 6998 7527 -48 -202 139 N ATOM 685 CA PHE A 85 -343.090-174.751 149.172 1.00 64.78 C ANISOU 685 CA PHE A 85 8988 7616 8010 -85 -185 160 C ATOM 686 C PHE A 85 -343.386-173.544 150.054 1.00 65.35 C ANISOU 686 C PHE A 85 9020 7719 8090 -56 -273 245 C ATOM 687 O PHE A 85 -342.611-172.582 150.076 1.00 70.96 O ANISOU 687 O PHE A 85 9708 8441 8811 -54 -249 269 O ATOM 688 CB PHE A 85 -343.895-174.659 147.879 1.00 67.56 C ANISOU 688 CB PHE A 85 9450 8006 8213 -168 -193 139 C ATOM 689 CG PHE A 85 -343.280-175.385 146.721 1.00 73.44 C ANISOU 689 CG PHE A 85 10255 8738 8912 -228 -69 40 C ATOM 690 CD1 PHE A 85 -343.185-176.764 146.717 1.00 77.93 C ANISOU 690 CD1 PHE A 85 10809 9249 9550 -217 -9 -45 C ATOM 691 CD2 PHE A 85 -342.826-174.684 145.618 1.00 80.99 C ANISOU 691 CD2 PHE A 85 11285 9734 9752 -308 -6 26 C ATOM 692 CE1 PHE A 85 -342.630-177.430 145.642 1.00 76.69 C ANISOU 692 CE1 PHE A 85 10704 9074 9360 -279 124 -159 C ATOM 693 CE2 PHE A 85 -342.274-175.344 144.542 1.00 83.09 C ANISOU 693 CE2 PHE A 85 11614 9995 9961 -383 129 -82 C ATOM 694 CZ PHE A 85 -342.178-176.721 144.554 1.00 75.32 C ANISOU 694 CZ PHE A 85 10609 8952 9058 -366 200 -184 C ATOM 695 N MET A 86 -344.503-173.569 150.790 1.00 62.87 N ANISOU 695 N MET A 86 8694 7416 7779 -40 -366 280 N ATOM 696 CA MET A 86 -344.779-172.469 151.712 1.00 64.57 C ANISOU 696 CA MET A 86 8864 7652 8018 -17 -430 337 C ATOM 697 C MET A 86 -343.733-172.404 152.824 1.00 60.94 C ANISOU 697 C MET A 86 8329 7178 7649 24 -410 351 C ATOM 698 O MET A 86 -343.335-171.311 153.243 1.00 64.11 O ANISOU 698 O MET A 86 8700 7593 8064 30 -422 380 O ATOM 699 CB MET A 86 -346.188-172.599 152.308 1.00 49.58 C ANISOU 699 CB MET A 86 6956 5764 6117 -15 -511 353 C ATOM 700 CG MET A 86 -347.333-172.343 151.328 1.00 69.11 C ANISOU 700 CG MET A 86 9485 8254 8521 -55 -565 361 C ATOM 701 SD MET A 86 -348.973-172.686 152.035 1.00 73.51 S ANISOU 701 SD MET A 86 10007 8814 9109 -54 -646 364 S ATOM 702 CE MET A 86 -348.989-171.531 153.397 1.00 75.17 C ANISOU 702 CE MET A 86 10137 9032 9393 -19 -660 388 C ATOM 703 N VAL A 87 -343.273-173.561 153.312 1.00 58.38 N ANISOU 703 N VAL A 87 7971 6818 7393 46 -390 335 N ATOM 704 CA VAL A 87 -342.367-173.579 154.460 1.00 60.26 C ANISOU 704 CA VAL A 87 8137 7041 7720 75 -404 366 C ATOM 705 C VAL A 87 -340.989-173.044 154.074 1.00 62.74 C ANISOU 705 C VAL A 87 8413 7342 8082 84 -342 358 C ATOM 706 O VAL A 87 -340.379-172.263 154.816 1.00 59.29 O ANISOU 706 O VAL A 87 7929 6919 7679 91 -366 392 O ATOM 707 CB VAL A 87 -342.274-175.002 155.052 1.00 58.82 C ANISOU 707 CB VAL A 87 7926 6809 7614 91 -419 370 C ATOM 708 CG1 VAL A 87 -341.050-175.136 155.954 1.00 53.46 C ANISOU 708 CG1 VAL A 87 7168 6100 7045 116 -437 410 C ATOM 709 CG2 VAL A 87 -343.536-175.344 155.830 1.00 58.70 C ANISOU 709 CG2 VAL A 87 7932 6815 7557 72 -488 395 C ATOM 710 N PHE A 88 -340.479-173.455 152.914 1.00 57.53 N ANISOU 710 N PHE A 88 7776 6657 7425 74 -253 304 N ATOM 711 CA PHE A 88 -339.127-173.084 152.519 1.00 61.94 C ANISOU 711 CA PHE A 88 8289 7199 8046 77 -173 283 C ATOM 712 C PHE A 88 -339.103-171.844 151.637 1.00 71.89 C ANISOU 712 C PHE A 88 9604 8503 9208 32 -137 285 C ATOM 713 O PHE A 88 -338.241-170.976 151.811 1.00 81.00 O ANISOU 713 O PHE A 88 10714 9663 10399 32 -117 304 O ATOM 714 CB PHE A 88 -338.444-174.248 151.799 1.00 57.60 C ANISOU 714 CB PHE A 88 7719 6589 7577 83 -71 207 C ATOM 715 CG PHE A 88 -338.182-175.428 152.673 1.00 69.18 C ANISOU 715 CG PHE A 88 9111 7988 9186 131 -108 218 C ATOM 716 CD1 PHE A 88 -337.166-175.396 153.620 1.00 72.68 C ANISOU 716 CD1 PHE A 88 9448 8397 9769 168 -145 265 C ATOM 717 CD2 PHE A 88 -338.944-176.578 152.549 1.00 66.36 C ANISOU 717 CD2 PHE A 88 8790 7596 8830 132 -118 191 C ATOM 718 CE1 PHE A 88 -336.918-176.494 154.430 1.00 73.45 C ANISOU 718 CE1 PHE A 88 9478 8424 10005 206 -202 297 C ATOM 719 CE2 PHE A 88 -338.699-177.676 153.353 1.00 68.24 C ANISOU 719 CE2 PHE A 88 8961 7759 9209 171 -162 215 C ATOM 720 CZ PHE A 88 -337.690-177.635 154.291 1.00 71.56 C ANISOU 720 CZ PHE A 88 9278 8143 9769 208 -209 275 C ATOM 721 N GLY A 89 -340.028-171.744 150.687 1.00 72.65 N ANISOU 721 N GLY A 89 9795 8627 9181 -12 -138 272 N ATOM 722 CA GLY A 89 -340.110-170.542 149.881 1.00 70.67 C ANISOU 722 CA GLY A 89 9605 8413 8834 -64 -131 299 C ATOM 723 C GLY A 89 -340.588-169.335 150.657 1.00 75.06 C ANISOU 723 C GLY A 89 10140 8987 9393 -47 -226 369 C ATOM 724 O GLY A 89 -340.229-168.202 150.330 1.00 82.18 O ANISOU 724 O GLY A 89 11054 9899 10273 -74 -219 402 O ATOM 725 N GLY A 90 -341.384-169.552 151.700 1.00 68.86 N ANISOU 725 N GLY A 90 9323 8201 8640 -10 -307 388 N ATOM 726 CA GLY A 90 -342.029-168.448 152.382 1.00 62.22 C ANISOU 726 CA GLY A 90 8466 7373 7803 -3 -384 431 C ATOM 727 C GLY A 90 -341.611-168.260 153.825 1.00 62.69 C ANISOU 727 C GLY A 90 8448 7430 7940 28 -409 438 C ATOM 728 O GLY A 90 -341.107-167.194 154.192 1.00 68.32 O ANISOU 728 O GLY A 90 9131 8144 8681 25 -413 456 O ATOM 729 N PHE A 91 -341.813-169.287 154.656 1.00 53.42 N ANISOU 729 N PHE A 91 7248 6254 6794 47 -430 428 N ATOM 730 CA PHE A 91 -341.593-169.119 156.091 1.00 52.70 C ANISOU 730 CA PHE A 91 7104 6174 6748 53 -471 444 C ATOM 731 C PHE A 91 -340.104-168.985 156.410 1.00 57.31 C ANISOU 731 C PHE A 91 7631 6745 7400 60 -449 455 C ATOM 732 O PHE A 91 -339.719-168.240 157.319 1.00 55.67 O ANISOU 732 O PHE A 91 7386 6552 7212 47 -480 470 O ATOM 733 CB PHE A 91 -342.192-170.291 156.880 1.00 56.17 C ANISOU 733 CB PHE A 91 7540 6614 7189 55 -508 446 C ATOM 734 CG PHE A 91 -343.652-170.564 156.602 1.00 56.91 C ANISOU 734 CG PHE A 91 7676 6717 7231 46 -528 430 C ATOM 735 CD1 PHE A 91 -344.479-169.596 156.049 1.00 52.25 C ANISOU 735 CD1 PHE A 91 7107 6136 6610 38 -539 423 C ATOM 736 CD2 PHE A 91 -344.203-171.806 156.914 1.00 60.12 C ANISOU 736 CD2 PHE A 91 8092 7114 7636 42 -545 428 C ATOM 737 CE1 PHE A 91 -345.816-169.858 155.800 1.00 51.16 C ANISOU 737 CE1 PHE A 91 6991 6001 6447 29 -569 412 C ATOM 738 CE2 PHE A 91 -345.551-172.078 156.668 1.00 57.51 C ANISOU 738 CE2 PHE A 91 7790 6792 7268 29 -564 411 C ATOM 739 CZ PHE A 91 -346.356-171.103 156.109 1.00 59.03 C ANISOU 739 CZ PHE A 91 7994 6996 7436 23 -578 402 C ATOM 740 N THR A 92 -339.256-169.722 155.692 1.00 58.13 N ANISOU 740 N THR A 92 7720 6818 7549 75 -392 441 N ATOM 741 CA THR A 92 -337.824-169.707 155.974 1.00 54.46 C ANISOU 741 CA THR A 92 7178 6331 7182 85 -370 449 C ATOM 742 C THR A 92 -337.206-168.371 155.583 1.00 60.17 C ANISOU 742 C THR A 92 7894 7067 7900 64 -335 450 C ATOM 743 O THR A 92 -336.466-167.758 156.364 1.00 52.81 O ANISOU 743 O THR A 92 6905 6140 7021 58 -365 471 O ATOM 744 CB THR A 92 -337.144-170.860 155.240 1.00 53.43 C ANISOU 744 CB THR A 92 7021 6151 7128 107 -300 416 C ATOM 745 OG1 THR A 92 -337.534-172.093 155.848 1.00 67.04 O ANISOU 745 OG1 THR A 92 8735 7848 8890 127 -350 429 O ATOM 746 CG2 THR A 92 -335.641-170.749 155.333 1.00 64.81 C ANISOU 746 CG2 THR A 92 8368 7562 8697 119 -264 416 C ATOM 747 N THR A 93 -337.509-167.904 154.377 1.00 58.93 N ANISOU 747 N THR A 93 7798 6915 7676 44 -278 433 N ATOM 748 CA THR A 93 -337.044-166.594 153.956 1.00 58.11 C ANISOU 748 CA THR A 93 7700 6819 7560 14 -250 446 C ATOM 749 C THR A 93 -337.496-165.513 154.929 1.00 59.48 C ANISOU 749 C THR A 93 7863 7006 7731 9 -326 473 C ATOM 750 O THR A 93 -336.698-164.657 155.333 1.00 59.72 O ANISOU 750 O THR A 93 7849 7033 7810 -5 -326 482 O ATOM 751 CB THR A 93 -337.554-166.310 152.548 1.00 65.85 C ANISOU 751 CB THR A 93 8770 7805 8444 -23 -204 443 C ATOM 752 OG1 THR A 93 -337.240-167.421 151.701 1.00 65.90 O ANISOU 752 OG1 THR A 93 8795 7803 8442 -30 -123 396 O ATOM 753 CG2 THR A 93 -336.884-165.072 152.007 1.00 78.60 C ANISOU 753 CG2 THR A 93 10391 9419 10054 -64 -165 466 C ATOM 754 N THR A 94 -338.763-165.564 155.349 1.00 53.49 N ANISOU 754 N THR A 94 7139 6259 6927 16 -385 474 N ATOM 755 CA THR A 94 -339.323-164.511 156.189 1.00 51.41 C ANISOU 755 CA THR A 94 6866 6001 6668 5 -436 477 C ATOM 756 C THR A 94 -338.727-164.525 157.587 1.00 56.16 C ANISOU 756 C THR A 94 7410 6619 7311 -3 -469 470 C ATOM 757 O THR A 94 -338.610-163.472 158.214 1.00 55.41 O ANISOU 757 O THR A 94 7295 6524 7234 -27 -486 460 O ATOM 758 CB THR A 94 -340.847-164.657 156.255 1.00 52.51 C ANISOU 758 CB THR A 94 7041 6144 6766 12 -476 467 C ATOM 759 OG1 THR A 94 -341.392-164.415 154.955 1.00 53.80 O ANISOU 759 OG1 THR A 94 7258 6291 6891 7 -471 488 O ATOM 760 CG2 THR A 94 -341.463-163.680 157.263 1.00 48.92 C ANISOU 760 CG2 THR A 94 6561 5688 6338 0 -510 445 C ATOM 761 N LEU A 95 -338.366-165.700 158.101 1.00 53.92 N ANISOU 761 N LEU A 95 7101 6343 7042 7 -486 478 N ATOM 762 CA LEU A 95 -337.609-165.744 159.349 1.00 54.40 C ANISOU 762 CA LEU A 95 7110 6420 7138 -16 -536 492 C ATOM 763 C LEU A 95 -336.306-164.960 159.215 1.00 59.23 C ANISOU 763 C LEU A 95 7668 7019 7817 -27 -516 499 C ATOM 764 O LEU A 95 -335.951-164.158 160.088 1.00 59.39 O ANISOU 764 O LEU A 95 7665 7056 7846 -65 -553 496 O ATOM 765 CB LEU A 95 -337.333-167.197 159.735 1.00 49.83 C ANISOU 765 CB LEU A 95 6509 5834 6589 -2 -569 520 C ATOM 766 CG LEU A 95 -336.443-167.501 160.943 1.00 61.63 C ANISOU 766 CG LEU A 95 7948 7339 8131 -30 -646 562 C ATOM 767 CD1 LEU A 95 -336.994-166.834 162.168 1.00 60.08 C ANISOU 767 CD1 LEU A 95 7780 7192 7854 -94 -699 553 C ATOM 768 CD2 LEU A 95 -336.351-168.995 161.184 1.00 62.27 C ANISOU 768 CD2 LEU A 95 8011 7393 8254 -11 -688 603 C ATOM 769 N TYR A 96 -335.606-165.155 158.101 1.00 55.94 N ANISOU 769 N TYR A 96 7236 6574 7445 -5 -449 500 N ATOM 770 CA TYR A 96 -334.313-164.521 157.903 1.00 61.94 C ANISOU 770 CA TYR A 96 7934 7319 8282 -19 -417 505 C ATOM 771 C TYR A 96 -334.466-163.012 157.693 1.00 64.80 C ANISOU 771 C TYR A 96 8323 7680 8616 -51 -401 498 C ATOM 772 O TYR A 96 -333.811-162.212 158.370 1.00 57.44 O ANISOU 772 O TYR A 96 7347 6751 7726 -81 -428 499 O ATOM 773 CB TYR A 96 -333.609-165.200 156.730 1.00 56.58 C ANISOU 773 CB TYR A 96 7232 6610 7655 3 -325 492 C ATOM 774 CG TYR A 96 -332.219-164.710 156.466 1.00 63.96 C ANISOU 774 CG TYR A 96 8087 7525 8688 -13 -273 489 C ATOM 775 CD1 TYR A 96 -331.134-165.195 157.190 1.00 63.98 C ANISOU 775 CD1 TYR A 96 7980 7509 8819 -2 -312 504 C ATOM 776 CD2 TYR A 96 -331.982-163.778 155.470 1.00 64.69 C ANISOU 776 CD2 TYR A 96 8210 7614 8754 -45 -190 478 C ATOM 777 CE1 TYR A 96 -329.855-164.741 156.938 1.00 59.82 C ANISOU 777 CE1 TYR A 96 7364 6962 8403 -18 -262 497 C ATOM 778 CE2 TYR A 96 -330.708-163.324 155.212 1.00 61.74 C ANISOU 778 CE2 TYR A 96 7760 7225 8474 -68 -131 472 C ATOM 779 CZ TYR A 96 -329.651-163.807 155.947 1.00 61.41 C ANISOU 779 CZ TYR A 96 7598 7164 8570 -52 -162 476 C ATOM 780 OH TYR A 96 -328.378-163.353 155.693 1.00 69.40 O ANISOU 780 OH TYR A 96 8517 8156 9694 -77 -101 466 O ATOM 781 N THR A 97 -335.355-162.601 156.785 1.00 64.17 N ANISOU 781 N THR A 97 8316 7593 8474 -49 -369 495 N ATOM 782 CA THR A 97 -335.567-161.171 156.550 1.00 55.30 C ANISOU 782 CA THR A 97 7216 6450 7345 -77 -366 501 C ATOM 783 C THR A 97 -336.134-160.478 157.784 1.00 51.87 C ANISOU 783 C THR A 97 6772 6021 6916 -91 -428 476 C ATOM 784 O THR A 97 -335.732-159.354 158.114 1.00 56.09 O ANISOU 784 O THR A 97 7284 6535 7492 -122 -431 467 O ATOM 785 CB THR A 97 -336.512-160.970 155.377 1.00 50.62 C ANISOU 785 CB THR A 97 6702 5842 6690 -76 -348 520 C ATOM 786 OG1 THR A 97 -337.763-161.591 155.697 1.00 53.84 O ANISOU 786 OG1 THR A 97 7140 6262 7054 -50 -394 507 O ATOM 787 CG2 THR A 97 -335.939-161.604 154.117 1.00 51.05 C ANISOU 787 CG2 THR A 97 6782 5899 6715 -86 -271 529 C ATOM 788 N SER A 98 -337.083-161.130 158.462 1.00 54.43 N ANISOU 788 N SER A 98 7113 6368 7198 -78 -467 457 N ATOM 789 CA SER A 98 -337.645-160.597 159.702 1.00 59.22 C ANISOU 789 CA SER A 98 7714 6988 7799 -107 -505 415 C ATOM 790 C SER A 98 -336.564-160.112 160.658 1.00 56.36 C ANISOU 790 C SER A 98 7304 6640 7469 -153 -528 403 C ATOM 791 O SER A 98 -336.697-159.046 161.269 1.00 53.74 O ANISOU 791 O SER A 98 6968 6298 7154 -191 -532 360 O ATOM 792 CB SER A 98 -338.489-161.669 160.398 1.00 62.37 C ANISOU 792 CB SER A 98 8131 7424 8142 -103 -535 401 C ATOM 793 OG SER A 98 -339.393-161.087 161.318 1.00 82.74 O ANISOU 793 OG SER A 98 10720 10013 10705 -136 -543 344 O ATOM 794 N LEU A 99 -335.504-160.900 160.828 1.00 55.91 N ANISOU 794 N LEU A 99 7206 6604 7434 -154 -548 437 N ATOM 795 CA LEU A 99 -334.476-160.562 161.799 1.00 51.89 C ANISOU 795 CA LEU A 99 6646 6113 6957 -205 -594 436 C ATOM 796 C LEU A 99 -333.543-159.461 161.298 1.00 58.38 C ANISOU 796 C LEU A 99 7430 6901 7851 -221 -559 436 C ATOM 797 O LEU A 99 -332.776-158.913 162.095 1.00 55.94 O ANISOU 797 O LEU A 99 7080 6602 7572 -273 -598 425 O ATOM 798 CB LEU A 99 -333.697-161.827 162.180 1.00 55.24 C ANISOU 798 CB LEU A 99 7024 6557 7408 -198 -647 486 C ATOM 799 CG LEU A 99 -334.565-162.888 162.883 1.00 59.14 C ANISOU 799 CG LEU A 99 7558 7084 7827 -202 -696 496 C ATOM 800 CD1 LEU A 99 -333.885-164.249 163.014 1.00 53.56 C ANISOU 800 CD1 LEU A 99 6805 6371 7173 -180 -749 560 C ATOM 801 CD2 LEU A 99 -334.986-162.404 164.254 1.00 56.84 C ANISOU 801 CD2 LEU A 99 7299 6840 7456 -284 -748 463 C ATOM 802 N HIS A 100 -333.598-159.115 160.006 1.00 57.30 N ANISOU 802 N HIS A 100 7311 6725 7736 -189 -490 450 N ATOM 803 CA HIS A 100 -332.972-157.895 159.522 1.00 61.17 C ANISOU 803 CA HIS A 100 7785 7177 8282 -217 -453 451 C ATOM 804 C HIS A 100 -333.921-156.705 159.555 1.00 65.62 C ANISOU 804 C HIS A 100 8394 7702 8838 -231 -451 422 C ATOM 805 O HIS A 100 -333.466-155.562 159.409 1.00 69.12 O ANISOU 805 O HIS A 100 8822 8103 9336 -264 -435 418 O ATOM 806 CB HIS A 100 -332.468-158.068 158.084 1.00 56.85 C ANISOU 806 CB HIS A 100 7240 6607 7754 -198 -376 489 C ATOM 807 CG HIS A 100 -331.389-159.092 157.939 1.00 67.22 C ANISOU 807 CG HIS A 100 8485 7936 9119 -184 -353 501 C ATOM 808 ND1 HIS A 100 -331.652-160.446 157.923 1.00 70.57 N ANISOU 808 ND1 HIS A 100 8911 8379 9525 -142 -361 505 N ATOM 809 CD2 HIS A 100 -330.048-158.964 157.801 1.00 57.72 C ANISOU 809 CD2 HIS A 100 7199 6722 8009 -205 -320 508 C ATOM 810 CE1 HIS A 100 -330.518-161.107 157.782 1.00 72.22 C ANISOU 810 CE1 HIS A 100 9036 8579 9824 -133 -335 511 C ATOM 811 NE2 HIS A 100 -329.530-160.231 157.710 1.00 64.00 N ANISOU 811 NE2 HIS A 100 7940 7524 8855 -170 -309 512 N ATOM 812 N GLY A 101 -335.223-156.948 159.723 1.00 61.82 N ANISOU 812 N GLY A 101 7957 7223 8308 -207 -467 400 N ATOM 813 CA GLY A 101 -336.224-155.908 159.708 1.00 51.57 C ANISOU 813 CA GLY A 101 6685 5873 7037 -209 -465 368 C ATOM 814 C GLY A 101 -336.541-155.343 158.345 1.00 52.81 C ANISOU 814 C GLY A 101 6875 5969 7220 -188 -443 425 C ATOM 815 O GLY A 101 -337.162-154.276 158.273 1.00 52.07 O ANISOU 815 O GLY A 101 6787 5808 7188 -192 -452 414 O ATOM 816 N TYR A 102 -336.128-156.012 157.267 1.00 51.64 N ANISOU 816 N TYR A 102 6751 5838 7031 -174 -417 484 N ATOM 817 CA TYR A 102 -336.463-155.588 155.908 1.00 52.41 C ANISOU 817 CA TYR A 102 6902 5894 7119 -176 -404 548 C ATOM 818 C TYR A 102 -336.118-156.720 154.952 1.00 58.50 C ANISOU 818 C TYR A 102 7705 6710 7813 -170 -363 581 C ATOM 819 O TYR A 102 -335.464-157.695 155.329 1.00 58.96 O ANISOU 819 O TYR A 102 7728 6815 7860 -158 -339 555 O ATOM 820 CB TYR A 102 -335.742-154.299 155.504 1.00 52.68 C ANISOU 820 CB TYR A 102 6929 5870 7217 -221 -385 581 C ATOM 821 CG TYR A 102 -334.235-154.389 155.287 1.00 53.04 C ANISOU 821 CG TYR A 102 6940 5941 7271 -258 -326 591 C ATOM 822 CD1 TYR A 102 -333.346-154.377 156.358 1.00 53.06 C ANISOU 822 CD1 TYR A 102 6870 5967 7324 -272 -328 542 C ATOM 823 CD2 TYR A 102 -333.704-154.428 154.003 1.00 53.80 C ANISOU 823 CD2 TYR A 102 7075 6038 7329 -292 -267 649 C ATOM 824 CE1 TYR A 102 -331.966-154.428 156.150 1.00 53.55 C ANISOU 824 CE1 TYR A 102 6880 6044 7422 -304 -278 551 C ATOM 825 CE2 TYR A 102 -332.334-154.472 153.786 1.00 54.05 C ANISOU 825 CE2 TYR A 102 7061 6087 7389 -330 -196 646 C ATOM 826 CZ TYR A 102 -331.469-154.471 154.858 1.00 57.11 C ANISOU 826 CZ TYR A 102 7358 6489 7851 -329 -204 599 C ATOM 827 OH TYR A 102 -330.112-154.519 154.612 1.00 63.60 O ANISOU 827 OH TYR A 102 8117 7322 8725 -365 -136 597 O ATOM 828 N PHE A 103 -336.544-156.566 153.697 1.00 52.19 N ANISOU 828 N PHE A 103 6974 5891 6965 -186 -357 639 N ATOM 829 CA PHE A 103 -336.392-157.634 152.707 1.00 52.26 C ANISOU 829 CA PHE A 103 7031 5942 6884 -194 -309 654 C ATOM 830 C PHE A 103 -335.013-157.536 152.062 1.00 57.04 C ANISOU 830 C PHE A 103 7626 6558 7490 -243 -216 663 C ATOM 831 O PHE A 103 -334.826-156.887 151.028 1.00 57.71 O ANISOU 831 O PHE A 103 7768 6624 7537 -303 -187 717 O ATOM 832 CB PHE A 103 -337.497-157.579 151.656 1.00 52.52 C ANISOU 832 CB PHE A 103 7151 5960 6844 -209 -351 710 C ATOM 833 CG PHE A 103 -337.559-158.817 150.818 1.00 53.44 C ANISOU 833 CG PHE A 103 7321 6126 6857 -219 -308 701 C ATOM 834 CD1 PHE A 103 -338.194-159.960 151.295 1.00 52.85 C ANISOU 834 CD1 PHE A 103 7235 6081 6766 -170 -328 656 C ATOM 835 CD2 PHE A 103 -336.917-158.872 149.591 1.00 54.62 C ANISOU 835 CD2 PHE A 103 7534 6293 6927 -289 -233 728 C ATOM 836 CE1 PHE A 103 -338.217-161.121 150.544 1.00 55.11 C ANISOU 836 CE1 PHE A 103 7567 6403 6969 -181 -282 635 C ATOM 837 CE2 PHE A 103 -336.933-160.036 148.839 1.00 66.20 C ANISOU 837 CE2 PHE A 103 9050 7803 8300 -307 -176 697 C ATOM 838 CZ PHE A 103 -337.590-161.163 149.317 1.00 61.33 C ANISOU 838 CZ PHE A 103 8417 7206 7681 -249 -204 649 C ATOM 839 N VAL A 104 -334.041-158.241 152.656 1.00 56.01 N ANISOU 839 N VAL A 104 7418 6455 7407 -225 -171 613 N ATOM 840 CA VAL A 104 -332.630-158.048 152.312 1.00 55.58 C ANISOU 840 CA VAL A 104 7316 6401 7401 -267 -83 607 C ATOM 841 C VAL A 104 -332.213-158.664 150.987 1.00 60.54 C ANISOU 841 C VAL A 104 7990 7050 7962 -309 27 603 C ATOM 842 O VAL A 104 -331.060-158.480 150.579 1.00 73.28 O ANISOU 842 O VAL A 104 9562 8663 9618 -354 122 591 O ATOM 843 CB VAL A 104 -331.701-158.615 153.405 1.00 59.53 C ANISOU 843 CB VAL A 104 7701 6916 8003 -233 -86 561 C ATOM 844 CG1 VAL A 104 -331.862-157.818 154.677 1.00 62.09 C ANISOU 844 CG1 VAL A 104 7986 7226 8378 -227 -176 557 C ATOM 845 CG2 VAL A 104 -331.991-160.109 153.647 1.00 56.37 C ANISOU 845 CG2 VAL A 104 7288 6542 7590 -180 -94 529 C ATOM 846 N PHE A 105 -333.095-159.378 150.292 1.00 58.88 N ANISOU 846 N PHE A 105 7863 6860 7649 -306 25 605 N ATOM 847 CA PHE A 105 -332.723-160.056 149.056 1.00 54.95 C ANISOU 847 CA PHE A 105 7419 6387 7073 -360 140 581 C ATOM 848 C PHE A 105 -333.001-159.221 147.817 1.00 64.09 C ANISOU 848 C PHE A 105 8695 7547 8111 -458 159 648 C ATOM 849 O PHE A 105 -332.801-159.707 146.699 1.00 69.14 O ANISOU 849 O PHE A 105 9405 8216 8647 -529 256 628 O ATOM 850 CB PHE A 105 -333.445-161.407 148.955 1.00 57.66 C ANISOU 850 CB PHE A 105 7791 6753 7365 -319 132 537 C ATOM 851 CG PHE A 105 -333.066-162.373 150.046 1.00 63.30 C ANISOU 851 CG PHE A 105 8395 7460 8196 -237 120 483 C ATOM 852 CD1 PHE A 105 -331.739-162.758 150.220 1.00 63.84 C ANISOU 852 CD1 PHE A 105 8358 7517 8381 -231 208 435 C ATOM 853 CD2 PHE A 105 -334.029-162.900 150.894 1.00 57.16 C ANISOU 853 CD2 PHE A 105 7614 6684 7419 -174 17 486 C ATOM 854 CE1 PHE A 105 -331.379-163.645 151.227 1.00 63.62 C ANISOU 854 CE1 PHE A 105 8226 7473 8473 -161 172 406 C ATOM 855 CE2 PHE A 105 -333.675-163.791 151.900 1.00 59.57 C ANISOU 855 CE2 PHE A 105 7830 6983 7822 -114 -7 454 C ATOM 856 CZ PHE A 105 -332.351-164.162 152.068 1.00 66.27 C ANISOU 856 CZ PHE A 105 8577 7814 8790 -107 60 422 C ATOM 857 N GLY A 106 -333.459-157.982 147.984 1.00 67.35 N ANISOU 857 N GLY A 106 9134 7923 8534 -472 67 726 N ATOM 858 CA GLY A 106 -333.653-157.087 146.869 1.00 62.19 C ANISOU 858 CA GLY A 106 8588 7257 7784 -572 63 814 C ATOM 859 C GLY A 106 -334.848-157.466 146.022 1.00 75.65 C ANISOU 859 C GLY A 106 10411 8981 9350 -602 -4 860 C ATOM 860 O GLY A 106 -335.505-158.491 146.249 1.00 68.98 O ANISOU 860 O GLY A 106 9565 8161 8483 -545 -30 811 O ATOM 861 N PRO A 107 -335.152-156.633 145.022 1.00 76.36 N ANISOU 861 N PRO A 107 10610 9057 9346 -701 -42 963 N ATOM 862 CA PRO A 107 -336.350-156.880 144.199 1.00 71.87 C ANISOU 862 CA PRO A 107 10158 8503 8648 -742 -139 1028 C ATOM 863 C PRO A 107 -336.321-158.200 143.453 1.00 75.14 C ANISOU 863 C PRO A 107 10637 8991 8921 -786 -46 953 C ATOM 864 O PRO A 107 -337.387-158.754 143.150 1.00 81.73 O ANISOU 864 O PRO A 107 11532 9843 9679 -782 -132 968 O ATOM 865 CB PRO A 107 -336.364-155.685 143.231 1.00 74.76 C ANISOU 865 CB PRO A 107 10626 8839 8941 -863 -187 1166 C ATOM 866 CG PRO A 107 -334.964-155.135 143.266 1.00 68.38 C ANISOU 866 CG PRO A 107 9776 8027 8178 -912 -53 1143 C ATOM 867 CD PRO A 107 -334.474-155.377 144.657 1.00 65.11 C ANISOU 867 CD PRO A 107 9204 7595 7940 -783 -22 1040 C ATOM 868 N THR A 108 -335.133-158.725 143.149 1.00 78.76 N ANISOU 868 N THR A 108 11078 9489 9357 -830 130 864 N ATOM 869 CA THR A 108 -335.039-160.042 142.524 1.00 73.14 C ANISOU 869 CA THR A 108 10412 8835 8544 -865 240 764 C ATOM 870 C THR A 108 -335.519-161.133 143.473 1.00 71.02 C ANISOU 870 C THR A 108 10056 8559 8371 -731 203 683 C ATOM 871 O THR A 108 -336.376-161.948 143.114 1.00 70.94 O ANISOU 871 O THR A 108 10108 8572 8272 -736 163 662 O ATOM 872 CB THR A 108 -333.604-160.316 142.082 1.00 80.96 C ANISOU 872 CB THR A 108 11373 9851 9536 -933 452 672 C ATOM 873 OG1 THR A 108 -333.308-159.534 140.921 1.00 87.36 O ANISOU 873 OG1 THR A 108 12308 10688 10196 -1096 505 742 O ATOM 874 CG2 THR A 108 -333.406-161.797 141.764 1.00 84.65 C ANISOU 874 CG2 THR A 108 11837 10353 9973 -930 581 531 C ATOM 875 N GLY A 109 -334.969-161.171 144.689 1.00 66.43 N ANISOU 875 N GLY A 109 9331 7945 7963 -623 210 639 N ATOM 876 CA GLY A 109 -335.441-162.140 145.658 1.00 63.41 C ANISOU 876 CA GLY A 109 8873 7554 7667 -509 160 582 C ATOM 877 C GLY A 109 -336.909-161.958 145.970 1.00 65.24 C ANISOU 877 C GLY A 109 9142 7774 7872 -468 -4 646 C ATOM 878 O GLY A 109 -337.588-162.912 146.361 1.00 67.37 O ANISOU 878 O GLY A 109 9397 8050 8150 -410 -42 604 O ATOM 879 N CYS A 110 -337.417-160.737 145.786 1.00 62.32 N ANISOU 879 N CYS A 110 8815 7379 7486 -500 -102 747 N ATOM 880 CA CYS A 110 -338.828-160.459 146.011 1.00 62.64 C ANISOU 880 CA CYS A 110 8876 7395 7530 -464 -257 809 C ATOM 881 C CYS A 110 -339.694-161.215 145.023 1.00 63.37 C ANISOU 881 C CYS A 110 9075 7524 7480 -521 -292 819 C ATOM 882 O CYS A 110 -340.727-161.781 145.399 1.00 61.52 O ANISOU 882 O CYS A 110 8825 7288 7263 -466 -375 807 O ATOM 883 CB CYS A 110 -339.082-158.955 145.895 1.00 64.48 C ANISOU 883 CB CYS A 110 9124 7574 7801 -494 -349 918 C ATOM 884 SG CYS A 110 -340.698-158.424 146.494 1.00 71.47 S ANISOU 884 SG CYS A 110 9975 8398 8780 -423 -532 977 S ATOM 885 N ASN A 111 -339.298-161.210 143.749 1.00 57.03 N ANISOU 885 N ASN A 111 8383 6757 6528 -643 -228 840 N ATOM 886 CA ASN A 111 -340.029-161.964 142.741 1.00 61.69 C ANISOU 886 CA ASN A 111 9089 7392 6959 -721 -254 840 C ATOM 887 C ASN A 111 -339.924-163.464 142.995 1.00 69.77 C ANISOU 887 C ASN A 111 10079 8443 7986 -674 -161 706 C ATOM 888 O ASN A 111 -340.894-164.202 142.798 1.00 67.11 O ANISOU 888 O ASN A 111 9783 8120 7594 -673 -229 693 O ATOM 889 CB ASN A 111 -339.506-161.614 141.350 1.00 61.97 C ANISOU 889 CB ASN A 111 9263 7470 6815 -886 -186 881 C ATOM 890 CG ASN A 111 -340.102-160.330 140.802 1.00 73.85 C ANISOU 890 CG ASN A 111 10843 8945 8272 -960 -339 1048 C ATOM 891 OD1 ASN A 111 -341.215-159.947 141.153 1.00 80.75 O ANISOU 891 OD1 ASN A 111 11690 9774 9216 -903 -512 1127 O ATOM 892 ND2 ASN A 111 -339.364-159.666 139.925 1.00 83.51 N ANISOU 892 ND2 ASN A 111 12157 10188 9385 -1092 -274 1104 N ATOM 893 N LEU A 112 -338.755-163.925 143.444 1.00 71.29 N ANISOU 893 N LEU A 112 10192 8634 8262 -634 -14 610 N ATOM 894 CA LEU A 112 -338.555-165.338 143.745 1.00 73.02 C ANISOU 894 CA LEU A 112 10362 8857 8524 -582 71 490 C ATOM 895 C LEU A 112 -339.380-165.766 144.947 1.00 65.30 C ANISOU 895 C LEU A 112 9300 7850 7660 -460 -40 491 C ATOM 896 O LEU A 112 -340.171-166.714 144.869 1.00 64.52 O ANISOU 896 O LEU A 112 9228 7759 7526 -449 -73 455 O ATOM 897 CB LEU A 112 -337.071-165.604 143.997 1.00 74.31 C ANISOU 897 CB LEU A 112 10436 9008 8790 -563 236 404 C ATOM 898 CG LEU A 112 -336.237-165.900 142.758 1.00 77.75 C ANISOU 898 CG LEU A 112 10946 9476 9118 -686 411 330 C ATOM 899 CD1 LEU A 112 -334.745-165.782 143.055 1.00 78.91 C ANISOU 899 CD1 LEU A 112 10980 9600 9401 -668 559 269 C ATOM 900 CD2 LEU A 112 -336.587-167.295 142.274 1.00 70.43 C ANISOU 900 CD2 LEU A 112 10063 8560 8136 -704 474 223 C ATOM 901 N GLU A 113 -339.188-165.087 146.080 1.00 61.79 N ANISOU 901 N GLU A 113 8756 7375 7348 -380 -90 525 N ATOM 902 CA GLU A 113 -339.904-165.459 147.292 1.00 62.01 C ANISOU 902 CA GLU A 113 8707 7382 7472 -282 -178 519 C ATOM 903 C GLU A 113 -341.404-165.273 147.113 1.00 68.49 C ANISOU 903 C GLU A 113 9580 8204 8241 -288 -311 575 C ATOM 904 O GLU A 113 -342.200-166.056 147.641 1.00 66.11 O ANISOU 904 O GLU A 113 9254 7901 7965 -240 -358 547 O ATOM 905 CB GLU A 113 -339.379-164.634 148.472 1.00 56.09 C ANISOU 905 CB GLU A 113 7857 6606 6849 -222 -201 540 C ATOM 906 CG GLU A 113 -339.877-165.088 149.837 1.00 63.17 C ANISOU 906 CG GLU A 113 8674 7491 7836 -139 -264 520 C ATOM 907 CD GLU A 113 -341.211-164.476 150.204 1.00 69.44 C ANISOU 907 CD GLU A 113 9476 8274 8633 -122 -380 565 C ATOM 908 OE1 GLU A 113 -341.477-163.330 149.782 1.00 69.09 O ANISOU 908 OE1 GLU A 113 9460 8211 8581 -152 -426 624 O ATOM 909 OE2 GLU A 113 -341.997-165.139 150.912 1.00 75.38 O ANISOU 909 OE2 GLU A 113 10202 9029 9410 -81 -424 541 O ATOM 910 N GLY A 114 -341.808-164.248 146.360 1.00 66.57 N ANISOU 910 N GLY A 114 9403 7958 7934 -350 -378 660 N ATOM 911 CA GLY A 114 -343.226-164.044 146.121 1.00 56.68 C ANISOU 911 CA GLY A 114 8185 6694 6655 -357 -518 722 C ATOM 912 C GLY A 114 -343.823-165.146 145.267 1.00 62.94 C ANISOU 912 C GLY A 114 9062 7525 7327 -412 -523 690 C ATOM 913 O GLY A 114 -344.893-165.679 145.575 1.00 58.37 O ANISOU 913 O GLY A 114 8463 6941 6772 -377 -603 683 O ATOM 914 N PHE A 115 -343.129-165.507 144.186 1.00 61.07 N ANISOU 914 N PHE A 115 8919 7326 6959 -507 -427 662 N ATOM 915 CA PHE A 115 -343.596-166.580 143.315 1.00 64.64 C ANISOU 915 CA PHE A 115 9462 7816 7282 -577 -414 612 C ATOM 916 C PHE A 115 -343.761-167.892 144.086 1.00 71.58 C ANISOU 916 C PHE A 115 10272 8684 8241 -495 -371 511 C ATOM 917 O PHE A 115 -344.845-168.488 144.091 1.00 68.30 O ANISOU 917 O PHE A 115 9870 8271 7810 -489 -456 509 O ATOM 918 CB PHE A 115 -342.632-166.750 142.134 1.00 61.16 C ANISOU 918 CB PHE A 115 9127 7417 6694 -699 -276 568 C ATOM 919 CG PHE A 115 -342.998-167.881 141.205 1.00 69.32 C ANISOU 919 CG PHE A 115 10263 8491 7584 -788 -237 492 C ATOM 920 CD1 PHE A 115 -343.921-167.694 140.186 1.00 69.51 C ANISOU 920 CD1 PHE A 115 10414 8552 7444 -905 -354 563 C ATOM 921 CD2 PHE A 115 -342.415-169.133 141.352 1.00 65.52 C ANISOU 921 CD2 PHE A 115 9748 8003 7142 -761 -90 349 C ATOM 922 CE1 PHE A 115 -344.263-168.740 139.336 1.00 74.00 C ANISOU 922 CE1 PHE A 115 11085 9162 7871 -1001 -318 483 C ATOM 923 CE2 PHE A 115 -342.751-170.178 140.506 1.00 66.59 C ANISOU 923 CE2 PHE A 115 9978 8167 7155 -847 -45 263 C ATOM 924 CZ PHE A 115 -343.675-169.983 139.497 1.00 69.37 C ANISOU 924 CZ PHE A 115 10466 8567 7323 -972 -155 325 C ATOM 925 N PHE A 116 -342.702-168.350 144.764 1.00 62.84 N ANISOU 925 N PHE A 116 9085 7559 7231 -433 -250 436 N ATOM 926 CA PHE A 116 -342.746-169.684 145.366 1.00 68.59 C ANISOU 926 CA PHE A 116 9760 8268 8034 -371 -207 349 C ATOM 927 C PHE A 116 -343.718-169.745 146.532 1.00 71.01 C ANISOU 927 C PHE A 116 9991 8553 8436 -285 -323 384 C ATOM 928 O PHE A 116 -344.432-170.743 146.698 1.00 66.54 O ANISOU 928 O PHE A 116 9425 7981 7875 -270 -349 346 O ATOM 929 CB PHE A 116 -341.349-170.124 145.806 1.00 61.93 C ANISOU 929 CB PHE A 116 8838 7399 7295 -328 -68 276 C ATOM 930 CG PHE A 116 -340.515-170.615 144.675 1.00 67.96 C ANISOU 930 CG PHE A 116 9663 8174 7985 -412 82 190 C ATOM 931 CD1 PHE A 116 -340.818-171.816 144.055 1.00 66.05 C ANISOU 931 CD1 PHE A 116 9476 7930 7689 -452 137 99 C ATOM 932 CD2 PHE A 116 -339.451-169.864 144.200 1.00 62.35 C ANISOU 932 CD2 PHE A 116 8959 7476 7256 -462 180 190 C ATOM 933 CE1 PHE A 116 -340.063-172.272 142.987 1.00 67.77 C ANISOU 933 CE1 PHE A 116 9755 8159 7836 -543 297 -3 C ATOM 934 CE2 PHE A 116 -338.697-170.312 143.135 1.00 66.45 C ANISOU 934 CE2 PHE A 116 9535 8010 7702 -554 341 95 C ATOM 935 CZ PHE A 116 -339.004-171.523 142.527 1.00 68.12 C ANISOU 935 CZ PHE A 116 9803 8220 7859 -595 405 -8 C ATOM 936 N ALA A 117 -343.754-168.698 147.355 1.00 60.18 N ANISOU 936 N ALA A 117 8555 7169 7142 -236 -383 446 N ATOM 937 CA ALA A 117 -344.722-168.665 148.441 1.00 59.36 C ANISOU 937 CA ALA A 117 8383 7050 7120 -171 -476 467 C ATOM 938 C ALA A 117 -346.148-168.606 147.899 1.00 64.04 C ANISOU 938 C ALA A 117 9022 7650 7661 -205 -588 506 C ATOM 939 O ALA A 117 -347.048-169.267 148.431 1.00 64.26 O ANISOU 939 O ALA A 117 9018 7673 7727 -176 -633 486 O ATOM 940 CB ALA A 117 -344.428-167.486 149.369 1.00 52.28 C ANISOU 940 CB ALA A 117 7413 6136 6313 -127 -501 508 C ATOM 941 N THR A 118 -346.371-167.845 146.823 1.00 65.21 N ANISOU 941 N THR A 118 9245 7808 7725 -275 -639 568 N ATOM 942 CA THR A 118 -347.709-167.789 146.237 1.00 65.73 C ANISOU 942 CA THR A 118 9348 7875 7749 -314 -768 618 C ATOM 943 C THR A 118 -348.054-169.099 145.543 1.00 65.62 C ANISOU 943 C THR A 118 9406 7890 7636 -368 -749 558 C ATOM 944 O THR A 118 -349.193-169.575 145.632 1.00 56.48 O ANISOU 944 O THR A 118 8234 6730 6496 -364 -834 559 O ATOM 945 CB THR A 118 -347.812-166.620 145.256 1.00 62.10 C ANISOU 945 CB THR A 118 8955 7413 7225 -386 -849 720 C ATOM 946 OG1 THR A 118 -347.465-165.402 145.931 1.00 66.86 O ANISOU 946 OG1 THR A 118 9488 7977 7941 -335 -860 767 O ATOM 947 CG2 THR A 118 -349.226-166.507 144.685 1.00 54.95 C ANISOU 947 CG2 THR A 118 8074 6501 6303 -427 -1012 789 C ATOM 948 N LEU A 119 -347.081-169.687 144.845 1.00 67.51 N ANISOU 948 N LEU A 119 9717 8154 7780 -422 -629 497 N ATOM 949 CA LEU A 119 -347.281-170.989 144.218 1.00 69.31 C ANISOU 949 CA LEU A 119 10011 8400 7925 -476 -585 415 C ATOM 950 C LEU A 119 -347.676-172.043 145.248 1.00 74.01 C ANISOU 950 C LEU A 119 10523 8965 8632 -394 -575 356 C ATOM 951 O LEU A 119 -348.628-172.805 145.038 1.00 75.38 O ANISOU 951 O LEU A 119 10720 9141 8779 -419 -632 334 O ATOM 952 CB LEU A 119 -346.011-171.411 143.476 1.00 66.96 C ANISOU 952 CB LEU A 119 9778 8118 7546 -536 -423 334 C ATOM 953 CG LEU A 119 -346.142-172.596 142.513 1.00 67.38 C ANISOU 953 CG LEU A 119 9928 8191 7483 -627 -360 236 C ATOM 954 CD1 LEU A 119 -346.845-172.188 141.215 1.00 63.33 C ANISOU 954 CD1 LEU A 119 9553 7732 6779 -768 -452 292 C ATOM 955 CD2 LEU A 119 -344.781-173.219 142.230 1.00 64.79 C ANISOU 955 CD2 LEU A 119 9603 7850 7162 -643 -161 119 C ATOM 956 N GLY A 120 -346.957-172.102 146.372 1.00 73.98 N ANISOU 956 N GLY A 120 10426 8933 8751 -305 -512 335 N ATOM 957 CA GLY A 120 -347.275-173.095 147.384 1.00 71.38 C ANISOU 957 CA GLY A 120 10027 8575 8519 -241 -508 295 C ATOM 958 C GLY A 120 -348.704-172.973 147.879 1.00 64.75 C ANISOU 958 C GLY A 120 9153 7738 7713 -226 -629 338 C ATOM 959 O GLY A 120 -349.452-173.954 147.912 1.00 64.94 O ANISOU 959 O GLY A 120 9183 7754 7739 -236 -652 303 O ATOM 960 N GLY A 121 -349.106-171.756 148.256 1.00 58.23 N ANISOU 960 N GLY A 121 8284 6914 6927 -203 -703 406 N ATOM 961 CA GLY A 121 -350.460-171.545 148.745 1.00 56.66 C ANISOU 961 CA GLY A 121 8031 6708 6789 -186 -806 436 C ATOM 962 C GLY A 121 -351.520-171.841 147.705 1.00 61.45 C ANISOU 962 C GLY A 121 8694 7326 7327 -253 -898 452 C ATOM 963 O GLY A 121 -352.604-172.322 148.042 1.00 62.47 O ANISOU 963 O GLY A 121 8782 7448 7505 -248 -956 443 O ATOM 964 N GLU A 122 -351.215-171.581 146.431 1.00 60.31 N ANISOU 964 N GLU A 122 8649 7204 7062 -329 -913 477 N ATOM 965 CA GLU A 122 -352.161-171.850 145.355 1.00 61.70 C ANISOU 965 CA GLU A 122 8897 7399 7148 -415 -1017 500 C ATOM 966 C GLU A 122 -352.298-173.346 145.079 1.00 66.50 C ANISOU 966 C GLU A 122 9553 8016 7699 -452 -964 409 C ATOM 967 O GLU A 122 -353.413-173.846 144.894 1.00 64.49 O ANISOU 967 O GLU A 122 9294 7762 7446 -484 -1054 409 O ATOM 968 CB GLU A 122 -351.723-171.109 144.093 1.00 65.05 C ANISOU 968 CB GLU A 122 9431 7851 7435 -507 -1046 559 C ATOM 969 CG GLU A 122 -352.097-169.635 144.072 1.00 65.55 C ANISOU 969 CG GLU A 122 9457 7892 7558 -496 -1166 678 C ATOM 970 CD GLU A 122 -353.576-169.425 143.806 1.00 73.65 C ANISOU 970 CD GLU A 122 10450 8901 8633 -518 -1347 748 C ATOM 971 OE1 GLU A 122 -354.237-168.723 144.600 1.00 75.07 O ANISOU 971 OE1 GLU A 122 10509 9032 8980 -442 -1415 787 O ATOM 972 OE2 GLU A 122 -354.078-169.971 142.800 1.00 75.13 O ANISOU 972 OE2 GLU A 122 10728 9120 8696 -618 -1419 758 O ATOM 973 N ILE A 123 -351.179-174.077 145.029 1.00 65.25 N ANISOU 973 N ILE A 123 9431 7855 7506 -452 -821 328 N ATOM 974 CA ILE A 123 -351.263-175.522 144.837 1.00 63.32 C ANISOU 974 CA ILE A 123 9221 7599 7240 -480 -761 232 C ATOM 975 C ILE A 123 -352.057-176.150 145.972 1.00 65.90 C ANISOU 975 C ILE A 123 9452 7894 7694 -412 -796 225 C ATOM 976 O ILE A 123 -352.890-177.039 145.752 1.00 60.77 O ANISOU 976 O ILE A 123 8819 7238 7033 -451 -834 189 O ATOM 977 CB ILE A 123 -349.858-176.144 144.716 1.00 60.04 C ANISOU 977 CB ILE A 123 8831 7165 6818 -473 -593 143 C ATOM 978 CG1 ILE A 123 -349.105-175.574 143.512 1.00 56.99 C ANISOU 978 CG1 ILE A 123 8547 6818 6290 -563 -538 136 C ATOM 979 CG2 ILE A 123 -349.951-177.667 144.577 1.00 58.97 C ANISOU 979 CG2 ILE A 123 8718 6995 6695 -495 -529 37 C ATOM 980 CD1 ILE A 123 -347.631-175.932 143.499 1.00 55.99 C ANISOU 980 CD1 ILE A 123 8413 6666 6194 -545 -362 51 C ATOM 981 N ALA A 124 -351.829-175.682 147.203 1.00 58.84 N ANISOU 981 N ALA A 124 8460 6982 6915 -324 -781 257 N ATOM 982 CA ALA A 124 -352.612-176.162 148.335 1.00 55.62 C ANISOU 982 CA ALA A 124 7967 6553 6612 -278 -809 257 C ATOM 983 C ALA A 124 -354.098-175.905 148.123 1.00 63.32 C ANISOU 983 C ALA A 124 8919 7541 7600 -309 -934 292 C ATOM 984 O ALA A 124 -354.919-176.824 148.235 1.00 68.15 O ANISOU 984 O ALA A 124 9519 8141 8233 -332 -959 261 O ATOM 985 CB ALA A 124 -352.131-175.502 149.626 1.00 51.35 C ANISOU 985 CB ALA A 124 7341 6005 6165 -202 -778 288 C ATOM 986 N LEU A 125 -354.456-174.655 147.808 1.00 63.10 N ANISOU 986 N LEU A 125 8875 7527 7575 -313 -1019 360 N ATOM 987 CA LEU A 125 -355.858-174.295 147.623 1.00 62.85 C ANISOU 987 CA LEU A 125 8795 7492 7592 -335 -1151 403 C ATOM 988 C LEU A 125 -356.536-175.204 146.608 1.00 60.20 C ANISOU 988 C LEU A 125 8531 7170 7171 -422 -1214 381 C ATOM 989 O LEU A 125 -357.601-175.768 146.877 1.00 56.14 O ANISOU 989 O LEU A 125 7964 6646 6720 -432 -1268 365 O ATOM 990 CB LEU A 125 -355.969-172.835 147.182 1.00 58.73 C ANISOU 990 CB LEU A 125 8261 6969 7087 -335 -1242 490 C ATOM 991 CG LEU A 125 -357.359-172.394 146.709 1.00 59.74 C ANISOU 991 CG LEU A 125 8342 7083 7276 -368 -1406 551 C ATOM 992 CD1 LEU A 125 -358.355-172.479 147.850 1.00 54.40 C ANISOU 992 CD1 LEU A 125 7523 6377 6769 -312 -1411 523 C ATOM 993 CD2 LEU A 125 -357.313-170.981 146.133 1.00 59.14 C ANISOU 993 CD2 LEU A 125 8268 6989 7215 -376 -1505 653 C ATOM 994 N TRP A 126 -355.919-175.374 145.439 1.00 60.12 N ANISOU 994 N TRP A 126 8645 7186 7012 -496 -1201 370 N ATOM 995 CA TRP A 126 -356.539-176.169 144.393 1.00 64.01 C ANISOU 995 CA TRP A 126 9222 7698 7400 -599 -1265 342 C ATOM 996 C TRP A 126 -356.467-177.661 144.676 1.00 72.51 C ANISOU 996 C TRP A 126 10312 8754 8484 -604 -1170 237 C ATOM 997 O TRP A 126 -357.265-178.421 144.115 1.00 71.77 O ANISOU 997 O TRP A 126 10255 8665 8348 -678 -1232 206 O ATOM 998 CB TRP A 126 -355.907-175.832 143.042 1.00 57.27 C ANISOU 998 CB TRP A 126 8509 6885 6366 -700 -1271 357 C ATOM 999 CG TRP A 126 -356.310-174.467 142.594 1.00 75.59 C ANISOU 999 CG TRP A 126 10825 9218 8680 -722 -1415 483 C ATOM 1000 CD1 TRP A 126 -355.529-173.349 142.563 1.00 73.74 C ANISOU 1000 CD1 TRP A 126 10598 8984 8435 -698 -1394 546 C ATOM 1001 CD2 TRP A 126 -357.616-174.057 142.164 1.00 76.33 C ANISOU 1001 CD2 TRP A 126 10887 9309 8803 -769 -1613 570 C ATOM 1002 NE1 TRP A 126 -356.262-172.272 142.117 1.00 77.61 N ANISOU 1002 NE1 TRP A 126 11073 9468 8947 -728 -1568 670 N ATOM 1003 CE2 TRP A 126 -357.546-172.679 141.869 1.00 73.94 C ANISOU 1003 CE2 TRP A 126 10579 9000 8515 -769 -1709 690 C ATOM 1004 CE3 TRP A 126 -358.835-174.724 141.991 1.00 75.86 C ANISOU 1004 CE3 TRP A 126 10799 9248 8775 -812 -1725 562 C ATOM 1005 CZ2 TRP A 126 -358.646-171.956 141.408 1.00 74.74 C ANISOU 1005 CZ2 TRP A 126 10641 9084 8672 -807 -1921 808 C ATOM 1006 CZ3 TRP A 126 -359.928-174.001 141.532 1.00 77.28 C ANISOU 1006 CZ3 TRP A 126 10936 9419 9006 -852 -1933 674 C ATOM 1007 CH2 TRP A 126 -359.825-172.633 141.246 1.00 72.23 C ANISOU 1007 CH2 TRP A 126 10287 8766 8393 -846 -2033 799 C ATOM 1008 N SER A 127 -355.538-178.096 145.531 1.00 66.83 N ANISOU 1008 N SER A 127 9562 8005 7826 -531 -1034 189 N ATOM 1009 CA SER A 127 -355.552-179.483 145.983 1.00 63.88 C ANISOU 1009 CA SER A 127 9179 7592 7501 -523 -961 109 C ATOM 1010 C SER A 127 -356.805-179.773 146.804 1.00 65.34 C ANISOU 1010 C SER A 127 9271 7763 7794 -505 -1035 130 C ATOM 1011 O SER A 127 -357.450-180.810 146.620 1.00 70.55 O ANISOU 1011 O SER A 127 9945 8403 8456 -553 -1051 83 O ATOM 1012 CB SER A 127 -354.287-179.791 146.790 1.00 58.89 C ANISOU 1012 CB SER A 127 8520 6922 6934 -447 -825 78 C ATOM 1013 OG SER A 127 -353.136-179.838 145.960 1.00 54.75 O ANISOU 1013 OG SER A 127 8075 6399 6327 -475 -732 27 O ATOM 1014 N LEU A 128 -357.179-178.856 147.702 1.00 62.21 N ANISOU 1014 N LEU A 128 8775 7372 7490 -443 -1072 194 N ATOM 1015 CA LEU A 128 -358.416-179.030 148.458 1.00 63.32 C ANISOU 1015 CA LEU A 128 8817 7503 7738 -436 -1127 205 C ATOM 1016 C LEU A 128 -359.628-178.994 147.537 1.00 64.79 C ANISOU 1016 C LEU A 128 9007 7704 7907 -509 -1264 222 C ATOM 1017 O LEU A 128 -360.620-179.698 147.768 1.00 68.35 O ANISOU 1017 O LEU A 128 9411 8141 8417 -538 -1300 199 O ATOM 1018 CB LEU A 128 -358.542-177.957 149.532 1.00 59.83 C ANISOU 1018 CB LEU A 128 8270 7064 7398 -366 -1123 250 C ATOM 1019 CG LEU A 128 -357.418-177.878 150.560 1.00 65.94 C ANISOU 1019 CG LEU A 128 9032 7831 8190 -304 -1010 244 C ATOM 1020 CD1 LEU A 128 -357.823-176.951 151.695 1.00 65.96 C ANISOU 1020 CD1 LEU A 128 8929 7839 8292 -260 -1006 268 C ATOM 1021 CD2 LEU A 128 -357.067-179.258 151.085 1.00 66.54 C ANISOU 1021 CD2 LEU A 128 9132 7878 8271 -310 -934 201 C ATOM 1022 N VAL A 129 -359.563-178.186 146.481 1.00 66.07 N ANISOU 1022 N VAL A 129 9225 7892 7986 -548 -1349 269 N ATOM 1023 CA VAL A 129 -360.650-178.149 145.511 1.00 68.53 C ANISOU 1023 CA VAL A 129 9550 8218 8268 -632 -1504 301 C ATOM 1024 C VAL A 129 -360.704-179.451 144.720 1.00 71.04 C ANISOU 1024 C VAL A 129 9974 8543 8474 -726 -1491 225 C ATOM 1025 O VAL A 129 -361.772-180.051 144.560 1.00 72.47 O ANISOU 1025 O VAL A 129 10125 8719 8690 -779 -1574 211 O ATOM 1026 CB VAL A 129 -360.499-176.926 144.589 1.00 63.12 C ANISOU 1026 CB VAL A 129 8911 7557 7512 -663 -1611 391 C ATOM 1027 CG1 VAL A 129 -361.556-176.955 143.502 1.00 59.17 C ANISOU 1027 CG1 VAL A 129 8443 7076 6964 -769 -1793 437 C ATOM 1028 CG2 VAL A 129 -360.589-175.641 145.407 1.00 58.44 C ANISOU 1028 CG2 VAL A 129 8198 6941 7065 -570 -1630 458 C ATOM 1029 N VAL A 130 -359.552-179.907 144.216 1.00 65.66 N ANISOU 1029 N VAL A 130 9411 7869 7669 -751 -1381 165 N ATOM 1030 CA VAL A 130 -359.524-181.114 143.392 1.00 64.54 C ANISOU 1030 CA VAL A 130 9376 7726 7422 -849 -1350 72 C ATOM 1031 C VAL A 130 -359.921-182.331 144.218 1.00 69.01 C ANISOU 1031 C VAL A 130 9883 8239 8099 -822 -1291 6 C ATOM 1032 O VAL A 130 -360.670-183.198 143.753 1.00 63.32 O ANISOU 1032 O VAL A 130 9191 7511 7357 -903 -1341 -42 O ATOM 1033 CB VAL A 130 -358.136-181.289 142.745 1.00 67.64 C ANISOU 1033 CB VAL A 130 9889 8125 7685 -876 -1216 5 C ATOM 1034 CG1 VAL A 130 -357.899-182.754 142.319 1.00 62.19 C ANISOU 1034 CG1 VAL A 130 9278 7401 6951 -940 -1118 -129 C ATOM 1035 CG2 VAL A 130 -357.982-180.348 141.552 1.00 63.52 C ANISOU 1035 CG2 VAL A 130 9469 7666 7000 -966 -1295 60 C ATOM 1036 N LEU A 131 -359.437-182.408 145.458 1.00 65.42 N ANISOU 1036 N LEU A 131 9349 7748 7761 -719 -1193 10 N ATOM 1037 CA LEU A 131 -359.832-183.510 146.325 1.00 66.34 C ANISOU 1037 CA LEU A 131 9410 7814 7984 -701 -1146 -30 C ATOM 1038 C LEU A 131 -361.346-183.542 146.521 1.00 72.32 C ANISOU 1038 C LEU A 131 10084 8579 8814 -737 -1263 -1 C ATOM 1039 O LEU A 131 -361.958-184.614 146.478 1.00 72.79 O ANISOU 1039 O LEU A 131 10148 8609 8900 -791 -1270 -51 O ATOM 1040 CB LEU A 131 -359.105-183.412 147.666 1.00 55.66 C ANISOU 1040 CB LEU A 131 7989 6432 6729 -600 -1047 -5 C ATOM 1041 CG LEU A 131 -359.488-184.504 148.669 1.00 67.12 C ANISOU 1041 CG LEU A 131 9387 7829 8284 -591 -1005 -24 C ATOM 1042 CD1 LEU A 131 -359.248-185.905 148.102 1.00 58.79 C ANISOU 1042 CD1 LEU A 131 8410 6714 7214 -645 -955 -110 C ATOM 1043 CD2 LEU A 131 -358.750-184.324 149.982 1.00 64.89 C ANISOU 1043 CD2 LEU A 131 9051 7529 8075 -510 -927 17 C ATOM 1044 N ALA A 132 -361.972-182.376 146.713 1.00 70.86 N ANISOU 1044 N ALA A 132 9815 8427 8680 -709 -1356 77 N ATOM 1045 CA ALA A 132 -363.423-182.340 146.876 1.00 71.13 C ANISOU 1045 CA ALA A 132 9747 8463 8815 -740 -1466 101 C ATOM 1046 C ALA A 132 -364.126-182.776 145.599 1.00 73.65 C ANISOU 1046 C ALA A 132 10133 8799 9052 -853 -1591 84 C ATOM 1047 O ALA A 132 -365.178-183.427 145.646 1.00 74.30 O ANISOU 1047 O ALA A 132 10161 8866 9201 -904 -1651 63 O ATOM 1048 CB ALA A 132 -363.888-180.945 147.284 1.00 57.50 C ANISOU 1048 CB ALA A 132 7907 6753 7188 -683 -1534 178 C ATOM 1049 N ILE A 133 -363.554-182.435 144.446 1.00 64.86 N ANISOU 1049 N ILE A 133 9140 7718 7785 -907 -1632 92 N ATOM 1050 CA ILE A 133 -364.132-182.874 143.183 1.00 67.68 C ANISOU 1050 CA ILE A 133 9586 8101 8028 -1038 -1750 72 C ATOM 1051 C ILE A 133 -364.000-184.383 143.031 1.00 74.01 C ANISOU 1051 C ILE A 133 10463 8870 8789 -1099 -1660 -46 C ATOM 1052 O ILE A 133 -364.941-185.060 142.602 1.00 79.87 O ANISOU 1052 O ILE A 133 11206 9609 9531 -1189 -1749 -76 O ATOM 1053 CB ILE A 133 -363.471-182.129 142.013 1.00 68.51 C ANISOU 1053 CB ILE A 133 9821 8257 7954 -1100 -1800 109 C ATOM 1054 CG1 ILE A 133 -363.773-180.631 142.105 1.00 68.09 C ANISOU 1054 CG1 ILE A 133 9685 8219 7966 -1050 -1921 239 C ATOM 1055 CG2 ILE A 133 -363.937-182.704 140.694 1.00 63.68 C ANISOU 1055 CG2 ILE A 133 9332 7680 7185 -1262 -1906 73 C ATOM 1056 CD1 ILE A 133 -363.014-179.797 141.101 1.00 64.79 C ANISOU 1056 CD1 ILE A 133 9393 7846 7379 -1105 -1958 294 C ATOM 1057 N GLU A 134 -362.834-184.933 143.379 1.00 68.11 N ANISOU 1057 N GLU A 134 9770 8088 8021 -1050 -1487 -115 N ATOM 1058 CA GLU A 134 -362.612-186.366 143.217 1.00 68.96 C ANISOU 1058 CA GLU A 134 9945 8143 8114 -1101 -1393 -231 C ATOM 1059 C GLU A 134 -363.551-187.167 144.112 1.00 73.81 C ANISOU 1059 C GLU A 134 10456 8708 8881 -1089 -1405 -238 C ATOM 1060 O GLU A 134 -364.216-188.105 143.656 1.00 62.24 O ANISOU 1060 O GLU A 134 9021 7221 7407 -1181 -1444 -301 O ATOM 1061 CB GLU A 134 -361.147-186.698 143.509 1.00 68.74 C ANISOU 1061 CB GLU A 134 9966 8071 8081 -1035 -1213 -290 C ATOM 1062 CG GLU A 134 -360.173-186.029 142.539 1.00 72.20 C ANISOU 1062 CG GLU A 134 10513 8556 8362 -1067 -1177 -305 C ATOM 1063 CD GLU A 134 -358.715-186.346 142.822 1.00 73.95 C ANISOU 1063 CD GLU A 134 10762 8729 8607 -999 -995 -368 C ATOM 1064 OE1 GLU A 134 -358.396-186.780 143.948 1.00 83.85 O ANISOU 1064 OE1 GLU A 134 11932 9918 10009 -902 -922 -360 O ATOM 1065 OE2 GLU A 134 -357.884-186.160 141.909 1.00 70.38 O ANISOU 1065 OE2 GLU A 134 10412 8301 8027 -1051 -928 -424 O ATOM 1066 N ARG A 135 -363.639-186.788 145.388 1.00 66.59 N ANISOU 1066 N ARG A 135 9422 7780 8101 -988 -1370 -174 N ATOM 1067 CA ARG A 135 -364.542-187.469 146.306 1.00 66.67 C ANISOU 1067 CA ARG A 135 9333 7750 8248 -987 -1370 -173 C ATOM 1068 C ARG A 135 -365.989-187.361 145.841 1.00 77.13 C ANISOU 1068 C ARG A 135 10597 9105 9604 -1067 -1524 -155 C ATOM 1069 O ARG A 135 -366.771-188.308 145.988 1.00 77.39 O ANISOU 1069 O ARG A 135 10601 9103 9702 -1126 -1538 -194 O ATOM 1070 CB ARG A 135 -364.374-186.891 147.708 1.00 58.75 C ANISOU 1070 CB ARG A 135 8223 6745 7353 -884 -1306 -108 C ATOM 1071 CG ARG A 135 -363.007-187.171 148.304 1.00 60.38 C ANISOU 1071 CG ARG A 135 8476 6913 7552 -814 -1169 -118 C ATOM 1072 CD ARG A 135 -362.782-186.376 149.577 1.00 60.06 C ANISOU 1072 CD ARG A 135 8347 6890 7583 -728 -1124 -48 C ATOM 1073 NE ARG A 135 -361.723-186.966 150.390 1.00 69.41 N ANISOU 1073 NE ARG A 135 9557 8024 8793 -679 -1012 -48 N ATOM 1074 CZ ARG A 135 -361.196-186.398 151.469 1.00 67.86 C ANISOU 1074 CZ ARG A 135 9314 7840 8631 -614 -961 7 C ATOM 1075 NH1 ARG A 135 -361.615-185.206 151.868 1.00 64.02 N ANISOU 1075 NH1 ARG A 135 8754 7412 8158 -586 -992 49 N ATOM 1076 NH2 ARG A 135 -360.243-187.019 152.141 1.00 73.76 N ANISOU 1076 NH2 ARG A 135 10085 8534 9404 -582 -885 18 N ATOM 1077 N TYR A 136 -366.362-186.214 145.274 1.00 74.25 N ANISOU 1077 N TYR A 136 10207 8797 9208 -1073 -1649 -89 N ATOM 1078 CA TYR A 136 -367.709-186.057 144.746 1.00 74.04 C ANISOU 1078 CA TYR A 136 10112 8792 9226 -1150 -1821 -60 C ATOM 1079 C TYR A 136 -367.957-187.002 143.579 1.00 79.71 C ANISOU 1079 C TYR A 136 10949 9512 9825 -1286 -1886 -130 C ATOM 1080 O TYR A 136 -369.048-187.570 143.452 1.00 79.36 O ANISOU 1080 O TYR A 136 10850 9457 9846 -1360 -1976 -147 O ATOM 1081 CB TYR A 136 -367.931-184.608 144.316 1.00 67.62 C ANISOU 1081 CB TYR A 136 9256 8025 8413 -1128 -1954 39 C ATOM 1082 CG TYR A 136 -369.124-184.420 143.416 1.00 67.40 C ANISOU 1082 CG TYR A 136 9192 8019 8399 -1227 -2167 82 C ATOM 1083 CD1 TYR A 136 -370.408-184.381 143.936 1.00 76.92 C ANISOU 1083 CD1 TYR A 136 10225 9204 9799 -1225 -2248 106 C ATOM 1084 CD2 TYR A 136 -368.967-184.281 142.044 1.00 73.56 C ANISOU 1084 CD2 TYR A 136 10109 8842 8999 -1333 -2289 99 C ATOM 1085 CE1 TYR A 136 -371.510-184.210 143.114 1.00 80.13 C ANISOU 1085 CE1 TYR A 136 10581 9624 10241 -1315 -2461 153 C ATOM 1086 CE2 TYR A 136 -370.062-184.107 141.211 1.00 80.66 C ANISOU 1086 CE2 TYR A 136 10977 9763 9905 -1436 -2510 153 C ATOM 1087 CZ TYR A 136 -371.330-184.072 141.752 1.00 83.08 C ANISOU 1087 CZ TYR A 136 11097 10041 10428 -1421 -2602 183 C ATOM 1088 OH TYR A 136 -372.418-183.901 140.930 1.00 91.48 O ANISOU 1088 OH TYR A 136 12115 11119 11522 -1523 -2838 245 O ATOM 1089 N VAL A 137 -366.959-187.177 142.711 1.00 74.17 N ANISOU 1089 N VAL A 137 10410 8826 8948 -1328 -1836 -181 N ATOM 1090 CA VAL A 137 -367.120-188.062 141.559 1.00 78.73 C ANISOU 1090 CA VAL A 137 11117 9409 9389 -1473 -1881 -269 C ATOM 1091 C VAL A 137 -367.213-189.515 142.011 1.00 79.82 C ANISOU 1091 C VAL A 137 11256 9469 9602 -1492 -1773 -374 C ATOM 1092 O VAL A 137 -368.052-190.281 141.523 1.00 83.16 O ANISOU 1092 O VAL A 137 11694 9882 10021 -1603 -1852 -425 O ATOM 1093 CB VAL A 137 -365.967-187.844 140.559 1.00 70.46 C ANISOU 1093 CB VAL A 137 10241 8397 8134 -1520 -1823 -313 C ATOM 1094 CG1 VAL A 137 -365.958-188.925 139.497 1.00 69.39 C ANISOU 1094 CG1 VAL A 137 10252 8257 7857 -1673 -1811 -442 C ATOM 1095 CG2 VAL A 137 -366.081-186.472 139.917 1.00 67.34 C ANISOU 1095 CG2 VAL A 137 9859 8078 7649 -1540 -1971 -196 C ATOM 1096 N VAL A 138 -366.372-189.909 142.969 1.00 78.96 N ANISOU 1096 N VAL A 138 11128 9299 9573 -1389 -1602 -398 N ATOM 1097 CA VAL A 138 -366.339-191.293 143.426 1.00 75.21 C ANISOU 1097 CA VAL A 138 10659 8734 9182 -1404 -1499 -484 C ATOM 1098 C VAL A 138 -367.623-191.656 144.172 1.00 78.65 C ANISOU 1098 C VAL A 138 10964 9149 9770 -1420 -1565 -447 C ATOM 1099 O VAL A 138 -368.168-192.752 143.997 1.00 77.14 O ANISOU 1099 O VAL A 138 10790 8907 9613 -1504 -1572 -517 O ATOM 1100 CB VAL A 138 -365.087-191.531 144.288 1.00 70.55 C ANISOU 1100 CB VAL A 138 10075 8081 8652 -1290 -1325 -492 C ATOM 1101 CG1 VAL A 138 -365.113-192.917 144.889 1.00 73.82 C ANISOU 1101 CG1 VAL A 138 10478 8386 9184 -1299 -1238 -552 C ATOM 1102 CG2 VAL A 138 -363.829-191.346 143.453 1.00 66.75 C ANISOU 1102 CG2 VAL A 138 9718 7609 8037 -1291 -1243 -555 C ATOM 1103 N VAL A 139 -368.136-190.748 145.001 1.00 75.22 N ANISOU 1103 N VAL A 139 10396 8751 9433 -1347 -1608 -347 N ATOM 1104 CA VAL A 139 -369.296-191.056 145.831 1.00 74.57 C ANISOU 1104 CA VAL A 139 10176 8649 9509 -1360 -1638 -320 C ATOM 1105 C VAL A 139 -370.602-190.820 145.081 1.00 75.67 C ANISOU 1105 C VAL A 139 10256 8831 9665 -1455 -1820 -306 C ATOM 1106 O VAL A 139 -371.459-191.707 145.010 1.00 78.99 O ANISOU 1106 O VAL A 139 10646 9219 10147 -1542 -1859 -350 O ATOM 1107 CB VAL A 139 -369.268-190.241 147.133 1.00 68.12 C ANISOU 1107 CB VAL A 139 9236 7847 8801 -1250 -1576 -240 C ATOM 1108 CG1 VAL A 139 -370.547-190.467 147.925 1.00 68.86 C ANISOU 1108 CG1 VAL A 139 9181 7931 9053 -1281 -1599 -223 C ATOM 1109 CG2 VAL A 139 -368.072-190.644 147.950 1.00 69.16 C ANISOU 1109 CG2 VAL A 139 9421 7931 8926 -1176 -1416 -245 C ATOM 1110 N CYS A 140 -370.777-189.617 144.535 1.00 76.43 N ANISOU 1110 N CYS A 140 10326 8992 9722 -1442 -1943 -238 N ATOM 1111 CA CYS A 140 -372.039-189.261 143.903 1.00 72.42 C ANISOU 1111 CA CYS A 140 9736 8519 9263 -1523 -2141 -199 C ATOM 1112 C CYS A 140 -372.201-189.873 142.523 1.00 78.52 C ANISOU 1112 C CYS A 140 10645 9309 9881 -1670 -2255 -255 C ATOM 1113 O CYS A 140 -373.317-189.843 141.990 1.00 87.24 O ANISOU 1113 O CYS A 140 11685 10433 11029 -1760 -2432 -230 O ATOM 1114 CB CYS A 140 -372.171-187.743 143.807 1.00 71.28 C ANISOU 1114 CB CYS A 140 9512 8422 9151 -1459 -2248 -92 C ATOM 1115 SG CYS A 140 -372.150-186.951 145.411 1.00 84.94 S ANISOU 1115 SG CYS A 140 11069 10132 11070 -1308 -2120 -45 S ATOM 1116 N LYS A 141 -371.128-190.409 141.952 1.00 75.97 N ANISOU 1116 N LYS A 141 10499 8978 9387 -1700 -2158 -334 N ATOM 1117 CA LYS A 141 -371.170-191.110 140.674 1.00 87.79 C ANISOU 1117 CA LYS A 141 12148 10490 10718 -1855 -2226 -419 C ATOM 1118 C LYS A 141 -371.951-190.326 139.628 1.00 96.81 C ANISOU 1118 C LYS A 141 13294 11710 11779 -1958 -2468 -342 C ATOM 1119 O LYS A 141 -373.002-190.780 139.150 1.00102.05 O ANISOU 1119 O LYS A 141 13928 12380 12467 -2076 -2616 -354 O ATOM 1120 CB LYS A 141 -371.745-192.510 140.842 1.00 82.01 C ANISOU 1120 CB LYS A 141 11407 9690 10061 -1932 -2189 -518 C ATOM 1121 CG LYS A 141 -370.874-193.471 141.645 1.00 85.21 C ANISOU 1121 CG LYS A 141 11847 10004 10524 -1862 -1965 -598 C ATOM 1122 CD LYS A 141 -371.570-194.813 141.831 1.00 92.68 C ANISOU 1122 CD LYS A 141 12774 10874 11568 -1944 -1948 -680 C ATOM 1123 CE LYS A 141 -370.791-195.736 142.751 1.00 98.29 C ANISOU 1123 CE LYS A 141 13497 11477 12371 -1869 -1748 -729 C ATOM 1124 NZ LYS A 141 -371.605-196.930 143.118 1.00105.47 N ANISOU 1124 NZ LYS A 141 14358 12305 13409 -1942 -1742 -778 N ATOM 1125 N PRO A 142 -371.503-189.119 139.259 1.00100.31 N ANISOU 1125 N PRO A 142 13766 12210 12138 -1921 -2532 -249 N ATOM 1126 CA PRO A 142 -372.243-188.322 138.275 1.00 98.57 C ANISOU 1126 CA PRO A 142 13547 12055 11851 -2022 -2787 -148 C ATOM 1127 C PRO A 142 -372.054-188.784 136.843 1.00102.00 C ANISOU 1127 C PRO A 142 14191 12542 12021 -2213 -2867 -212 C ATOM 1128 O PRO A 142 -372.803-188.337 135.965 1.00108.16 O ANISOU 1128 O PRO A 142 14985 13377 12735 -2334 -3106 -130 O ATOM 1129 CB PRO A 142 -371.671-186.911 138.476 1.00 95.09 C ANISOU 1129 CB PRO A 142 13074 11640 11414 -1910 -2797 -29 C ATOM 1130 CG PRO A 142 -370.270-187.157 138.912 1.00 90.17 C ANISOU 1130 CG PRO A 142 12549 10998 10715 -1823 -2546 -108 C ATOM 1131 CD PRO A 142 -370.288-188.421 139.733 1.00 96.93 C ANISOU 1131 CD PRO A 142 13367 11783 11678 -1791 -2383 -222 C ATOM 1132 N MET A 143 -371.093-189.664 136.579 1.00103.27 N ANISOU 1132 N MET A 143 14513 12687 12037 -2253 -2678 -357 N ATOM 1133 CA MET A 143 -370.834-190.168 135.236 1.00104.90 C ANISOU 1133 CA MET A 143 14933 12944 11981 -2448 -2712 -452 C ATOM 1134 C MET A 143 -371.203-191.646 135.173 1.00111.03 C ANISOU 1134 C MET A 143 15743 13664 12781 -2540 -2647 -610 C ATOM 1135 O MET A 143 -370.717-192.447 135.980 1.00111.09 O ANISOU 1135 O MET A 143 15719 13585 12907 -2445 -2440 -705 O ATOM 1136 CB MET A 143 -369.374-189.935 134.848 1.00 92.18 C ANISOU 1136 CB MET A 143 13485 11356 10183 -2437 -2533 -512 C ATOM 1137 CG MET A 143 -369.077-188.467 134.623 1.00 98.10 C ANISOU 1137 CG MET A 143 14235 12172 10865 -2396 -2634 -353 C ATOM 1138 SD MET A 143 -367.325-188.060 134.534 1.00110.61 S ANISOU 1138 SD MET A 143 15952 13770 12305 -2332 -2393 -406 S ATOM 1139 CE MET A 143 -367.414-186.299 134.249 1.00111.44 C ANISOU 1139 CE MET A 143 16031 13948 12365 -2309 -2587 -185 C ATOM 1140 N SER A 144 -372.058-191.992 134.209 1.00118.12 N ANISOU 1140 N SER A 144 16705 14605 13568 -2731 -2834 -630 N ATOM 1141 CA SER A 144 -372.667-193.311 134.063 1.00123.91 C ANISOU 1141 CA SER A 144 17456 15289 14335 -2844 -2826 -765 C ATOM 1142 C SER A 144 -371.707-194.469 134.313 1.00126.11 C ANISOU 1142 C SER A 144 17828 15480 14610 -2818 -2545 -955 C ATOM 1143 O SER A 144 -371.887-195.234 135.267 1.00128.63 O ANISOU 1143 O SER A 144 18037 15701 15137 -2727 -2436 -998 O ATOM 1144 CB SER A 144 -373.263-193.443 132.663 1.00131.30 C ANISOU 1144 CB SER A 144 18535 16308 15044 -3092 -3036 -788 C ATOM 1145 OG SER A 144 -372.319-193.045 131.684 1.00137.43 O ANISOU 1145 OG SER A 144 19523 17161 15534 -3190 -2994 -823 O ATOM 1146 N ASN A 145 -370.700-194.618 133.456 1.00124.95 N ANISOU 1146 N ASN A 145 17878 15360 14235 -2906 -2428 -1071 N ATOM 1147 CA ASN A 145 -369.748-195.723 133.528 1.00123.36 C ANISOU 1147 CA ASN A 145 17769 15065 14036 -2898 -2164 -1269 C ATOM 1148 C ASN A 145 -368.354-195.122 133.641 1.00119.07 C ANISOU 1148 C ASN A 145 17282 14529 13430 -2787 -1981 -1272 C ATOM 1149 O ASN A 145 -367.606-195.057 132.664 1.00122.29 O ANISOU 1149 O ASN A 145 17866 14988 13612 -2902 -1907 -1370 O ATOM 1150 CB ASN A 145 -369.873-196.653 132.299 1.00128.94 C ANISOU 1150 CB ASN A 145 18664 15786 14542 -3138 -2166 -1456 C ATOM 1151 CG ASN A 145 -371.281-197.195 132.115 1.00132.19 C ANISOU 1151 CG ASN A 145 19021 16200 15006 -3264 -2370 -1447 C ATOM 1152 OD1 ASN A 145 -372.037-197.343 133.075 1.00131.39 O ANISOU 1152 OD1 ASN A 145 18735 16040 15147 -3158 -2425 -1364 O ATOM 1153 ND2 ASN A 145 -371.637-197.499 130.870 1.00135.80 N ANISOU 1153 ND2 ASN A 145 19642 16727 15229 -3505 -2481 -1538 N ATOM 1154 N PHE A 146 -368.007-194.675 134.849 1.00108.21 N ANISOU 1154 N PHE A 146 15757 13106 12253 -2573 -1905 -1168 N ATOM 1155 CA PHE A 146 -366.733-194.024 135.113 1.00 95.85 C ANISOU 1155 CA PHE A 146 14213 11543 10663 -2450 -1748 -1149 C ATOM 1156 C PHE A 146 -366.046-194.704 136.286 1.00 93.53 C ANISOU 1156 C PHE A 146 13824 11119 10594 -2280 -1543 -1196 C ATOM 1157 O PHE A 146 -366.704-195.146 137.233 1.00 89.11 O ANISOU 1157 O PHE A 146 13130 10492 10234 -2206 -1569 -1151 O ATOM 1158 CB PHE A 146 -366.928-192.527 135.404 1.00 95.56 C ANISOU 1158 CB PHE A 146 14090 11592 10627 -2361 -1891 -943 C ATOM 1159 CG PHE A 146 -365.639-191.763 135.547 1.00 95.52 C ANISOU 1159 CG PHE A 146 14119 11602 10571 -2257 -1749 -918 C ATOM 1160 CD1 PHE A 146 -364.939-191.341 134.428 1.00 97.44 C ANISOU 1160 CD1 PHE A 146 14534 11923 10568 -2375 -1722 -963 C ATOM 1161 CD2 PHE A 146 -365.129-191.468 136.800 1.00 93.66 C ANISOU 1161 CD2 PHE A 146 13748 11308 10529 -2055 -1643 -851 C ATOM 1162 CE1 PHE A 146 -363.753-190.643 134.558 1.00 99.08 C ANISOU 1162 CE1 PHE A 146 14765 12144 10739 -2286 -1586 -943 C ATOM 1163 CE2 PHE A 146 -363.945-190.769 136.936 1.00 96.42 C ANISOU 1163 CE2 PHE A 146 14123 11672 10842 -1965 -1520 -830 C ATOM 1164 CZ PHE A 146 -363.255-190.356 135.814 1.00 98.22 C ANISOU 1164 CZ PHE A 146 14510 11971 10839 -2076 -1489 -876 C ATOM 1165 N ARG A 147 -364.718-194.789 136.212 1.00 97.00 N ANISOU 1165 N ARG A 147 14332 11521 11002 -2228 -1342 -1285 N ATOM 1166 CA ARG A 147 -363.900-195.384 137.265 1.00101.11 C ANISOU 1166 CA ARG A 147 14769 11913 11734 -2069 -1155 -1319 C ATOM 1167 C ARG A 147 -362.651-194.532 137.449 1.00 98.66 C ANISOU 1167 C ARG A 147 14464 11627 11397 -1957 -1040 -1279 C ATOM 1168 O ARG A 147 -361.826-194.435 136.536 1.00 99.27 O ANISOU 1168 O ARG A 147 14667 11734 11316 -2033 -939 -1385 O ATOM 1169 CB ARG A 147 -363.528-196.831 136.918 1.00107.04 C ANISOU 1169 CB ARG A 147 15594 12542 12534 -2140 -1000 -1527 C ATOM 1170 CG ARG A 147 -362.613-197.515 137.929 1.00117.19 C ANISOU 1170 CG ARG A 147 16796 13676 14054 -1984 -818 -1559 C ATOM 1171 CD ARG A 147 -363.337-197.811 139.234 1.00124.64 C ANISOU 1171 CD ARG A 147 17588 14555 15214 -1881 -888 -1433 C ATOM 1172 NE ARG A 147 -362.440-198.381 140.237 1.00127.96 N ANISOU 1172 NE ARG A 147 17934 14837 15849 -1739 -741 -1431 N ATOM 1173 CZ ARG A 147 -361.813-197.673 141.172 1.00126.29 C ANISOU 1173 CZ ARG A 147 17636 14633 15715 -1588 -714 -1302 C ATOM 1174 NH1 ARG A 147 -361.985-196.359 141.243 1.00123.07 N ANISOU 1174 NH1 ARG A 147 17203 14360 15199 -1552 -809 -1175 N ATOM 1175 NH2 ARG A 147 -361.015-198.282 142.040 1.00125.80 N ANISOU 1175 NH2 ARG A 147 17512 14438 15848 -1477 -600 -1298 N ATOM 1176 N PHE A 148 -362.512-193.921 138.626 1.00 95.66 N ANISOU 1176 N PHE A 148 13948 11235 11165 -1789 -1048 -1135 N ATOM 1177 CA PHE A 148 -361.395-193.022 138.914 1.00 84.73 C ANISOU 1177 CA PHE A 148 12549 9876 9769 -1676 -960 -1077 C ATOM 1178 C PHE A 148 -360.101-193.820 139.013 1.00 85.37 C ANISOU 1178 C PHE A 148 12656 9845 9937 -1625 -737 -1213 C ATOM 1179 O PHE A 148 -359.926-194.622 139.935 1.00 90.87 O ANISOU 1179 O PHE A 148 13267 10422 10839 -1532 -667 -1221 O ATOM 1180 CB PHE A 148 -361.661-192.254 140.207 1.00 80.29 C ANISOU 1180 CB PHE A 148 11833 9323 9351 -1524 -1027 -902 C ATOM 1181 CG PHE A 148 -360.570-191.289 140.577 1.00 81.40 C ANISOU 1181 CG PHE A 148 11951 9489 9489 -1410 -950 -836 C ATOM 1182 CD1 PHE A 148 -360.452-190.072 139.923 1.00 79.39 C ANISOU 1182 CD1 PHE A 148 11747 9343 9074 -1443 -1022 -769 C ATOM 1183 CD2 PHE A 148 -359.668-191.594 141.585 1.00 84.04 C ANISOU 1183 CD2 PHE A 148 12212 9735 9985 -1276 -820 -831 C ATOM 1184 CE1 PHE A 148 -359.450-189.180 140.259 1.00 79.62 C ANISOU 1184 CE1 PHE A 148 11753 9392 9106 -1344 -950 -710 C ATOM 1185 CE2 PHE A 148 -358.662-190.703 141.930 1.00 87.42 C ANISOU 1185 CE2 PHE A 148 12614 10188 10415 -1178 -757 -772 C ATOM 1186 CZ PHE A 148 -358.554-189.494 141.265 1.00 84.00 C ANISOU 1186 CZ PHE A 148 12230 9863 9822 -1211 -815 -717 C ATOM 1187 N GLY A 149 -359.184-193.592 138.077 1.00 80.67 N ANISOU 1187 N GLY A 149 12171 9282 9196 -1687 -627 -1314 N ATOM 1188 CA GLY A 149 -357.945-194.343 138.053 1.00 71.55 C ANISOU 1188 CA GLY A 149 11031 8015 8141 -1647 -406 -1463 C ATOM 1189 C GLY A 149 -356.701-193.495 138.208 1.00 79.04 C ANISOU 1189 C GLY A 149 11959 8986 9088 -1552 -299 -1428 C ATOM 1190 O GLY A 149 -356.783-192.304 138.524 1.00 84.50 O ANISOU 1190 O GLY A 149 12613 9772 9720 -1496 -398 -1271 O ATOM 1191 N GLU A 150 -355.538-194.109 137.977 1.00 88.29 N ANISOU 1191 N GLU A 150 13146 10062 10338 -1535 -93 -1581 N ATOM 1192 CA GLU A 150 -354.271-193.399 138.129 1.00 85.61 C ANISOU 1192 CA GLU A 150 12773 9730 10024 -1446 26 -1563 C ATOM 1193 C GLU A 150 -354.186-192.203 137.188 1.00 89.41 C ANISOU 1193 C GLU A 150 13365 10372 10235 -1548 -10 -1530 C ATOM 1194 O GLU A 150 -353.744-191.120 137.588 1.00 87.03 O ANISOU 1194 O GLU A 150 13015 10129 9922 -1464 -38 -1400 O ATOM 1195 CB GLU A 150 -353.105-194.361 137.886 1.00 86.55 C ANISOU 1195 CB GLU A 150 12886 9710 10289 -1432 260 -1761 C ATOM 1196 CG GLU A 150 -351.725-193.730 137.997 1.00100.32 C ANISOU 1196 CG GLU A 150 14582 11448 12086 -1346 401 -1764 C ATOM 1197 CD GLU A 150 -350.599-194.720 137.747 1.00111.75 C ANISOU 1197 CD GLU A 150 16001 12742 13718 -1330 637 -1970 C ATOM 1198 OE1 GLU A 150 -350.885-195.860 137.320 1.00123.05 O ANISOU 1198 OE1 GLU A 150 17473 14077 15203 -1406 704 -2132 O ATOM 1199 OE2 GLU A 150 -349.427-194.357 137.981 1.00109.89 O ANISOU 1199 OE2 GLU A 150 15691 12471 13589 -1240 757 -1976 O ATOM 1200 N ASN A 151 -354.615-192.374 135.934 1.00 92.77 N ANISOU 1200 N ASN A 151 13945 10868 10434 -1742 -17 -1641 N ATOM 1201 CA ASN A 151 -354.508-191.290 134.962 1.00 93.93 C ANISOU 1201 CA ASN A 151 14216 11165 10306 -1865 -55 -1605 C ATOM 1202 C ASN A 151 -355.361-190.091 135.364 1.00 94.01 C ANISOU 1202 C ASN A 151 14184 11280 10254 -1823 -295 -1366 C ATOM 1203 O ASN A 151 -354.936-188.939 135.213 1.00 95.56 O ANISOU 1203 O ASN A 151 14399 11559 10350 -1814 -318 -1265 O ATOM 1204 CB ASN A 151 -354.896-191.788 133.570 1.00102.61 C ANISOU 1204 CB ASN A 151 15501 12323 11162 -2103 -35 -1765 C ATOM 1205 CG ASN A 151 -353.823-192.661 132.942 1.00115.04 C ANISOU 1205 CG ASN A 151 17139 13818 12752 -2171 244 -2024 C ATOM 1206 OD1 ASN A 151 -352.785-192.925 133.550 1.00118.46 O ANISOU 1206 OD1 ASN A 151 17464 14142 13404 -2029 415 -2078 O ATOM 1207 ND2 ASN A 151 -354.073-193.119 131.721 1.00120.86 N ANISOU 1207 ND2 ASN A 151 18049 14607 13265 -2394 289 -2189 N ATOM 1208 N HIS A 152 -356.565-190.337 135.884 1.00 89.76 N ANISOU 1208 N HIS A 152 13582 10731 9793 -1800 -469 -1277 N ATOM 1209 CA HIS A 152 -357.402-189.228 136.330 1.00 85.55 C ANISOU 1209 CA HIS A 152 12982 10277 9245 -1750 -685 -1064 C ATOM 1210 C HIS A 152 -356.747-188.473 137.481 1.00 84.72 C ANISOU 1210 C HIS A 152 12741 10145 9304 -1557 -650 -943 C ATOM 1211 O HIS A 152 -356.793-187.239 137.531 1.00 83.36 O ANISOU 1211 O HIS A 152 12553 10050 9070 -1530 -747 -803 O ATOM 1212 CB HIS A 152 -358.783-189.740 136.738 1.00 80.67 C ANISOU 1212 CB HIS A 152 12299 9638 8714 -1757 -850 -1014 C ATOM 1213 CG HIS A 152 -359.500-190.471 135.648 1.00 90.84 C ANISOU 1213 CG HIS A 152 13715 10955 9846 -1953 -907 -1125 C ATOM 1214 ND1 HIS A 152 -359.564-191.848 135.593 1.00 94.61 N ANISOU 1214 ND1 HIS A 152 14212 11337 10401 -1995 -807 -1289 N ATOM 1215 CD2 HIS A 152 -360.176-190.019 134.565 1.00 93.12 C ANISOU 1215 CD2 HIS A 152 14123 11354 9906 -2127 -1062 -1093 C ATOM 1216 CE1 HIS A 152 -360.254-192.211 134.526 1.00 98.56 C ANISOU 1216 CE1 HIS A 152 14839 11892 10719 -2189 -890 -1366 C ATOM 1217 NE2 HIS A 152 -360.636-191.120 133.886 1.00 99.91 N ANISOU 1217 NE2 HIS A 152 15074 12191 10695 -2276 -1051 -1245 N ATOM 1218 N ALA A 153 -356.118-189.200 138.410 1.00 85.60 N ANISOU 1218 N ALA A 153 12755 10142 9627 -1428 -518 -994 N ATOM 1219 CA ALA A 153 -355.471-188.550 139.544 1.00 83.58 C ANISOU 1219 CA ALA A 153 12375 9862 9522 -1258 -490 -883 C ATOM 1220 C ALA A 153 -354.292-187.698 139.092 1.00 79.82 C ANISOU 1220 C ALA A 153 11942 9430 8954 -1255 -385 -891 C ATOM 1221 O ALA A 153 -354.013-186.643 139.676 1.00 75.06 O ANISOU 1221 O ALA A 153 11274 8864 8381 -1163 -428 -762 O ATOM 1222 CB ALA A 153 -355.019-189.598 140.561 1.00 86.76 C ANISOU 1222 CB ALA A 153 12676 10127 10161 -1143 -385 -931 C ATOM 1223 N ILE A 154 -353.585-188.141 138.055 1.00 75.47 N ANISOU 1223 N ILE A 154 11503 8876 8294 -1363 -238 -1049 N ATOM 1224 CA ILE A 154 -352.480-187.353 137.526 1.00 76.99 C ANISOU 1224 CA ILE A 154 11746 9118 8387 -1384 -124 -1068 C ATOM 1225 C ILE A 154 -352.999-186.076 136.875 1.00 79.63 C ANISOU 1225 C ILE A 154 12165 9588 8501 -1477 -277 -938 C ATOM 1226 O ILE A 154 -352.404-185.002 137.026 1.00 80.77 O ANISOU 1226 O ILE A 154 12288 9776 8625 -1428 -273 -843 O ATOM 1227 CB ILE A 154 -351.649-188.206 136.554 1.00 80.41 C ANISOU 1227 CB ILE A 154 12277 9513 8762 -1494 91 -1292 C ATOM 1228 CG1 ILE A 154 -351.065-189.408 137.295 1.00 85.50 C ANISOU 1228 CG1 ILE A 154 12810 9996 9678 -1379 233 -1402 C ATOM 1229 CG2 ILE A 154 -350.547-187.379 135.932 1.00 73.29 C ANISOU 1229 CG2 ILE A 154 11433 8672 7741 -1539 220 -1318 C ATOM 1230 CD1 ILE A 154 -350.388-190.404 136.392 1.00 89.41 C ANISOU 1230 CD1 ILE A 154 13382 10426 10165 -1482 449 -1646 C ATOM 1231 N MET A 155 -354.119-186.164 136.152 1.00 81.38 N ANISOU 1231 N MET A 155 12480 9873 8567 -1614 -426 -922 N ATOM 1232 CA MET A 155 -354.757-184.957 135.639 1.00 82.42 C ANISOU 1232 CA MET A 155 12671 10117 8528 -1692 -616 -765 C ATOM 1233 C MET A 155 -355.102-183.999 136.771 1.00 80.76 C ANISOU 1233 C MET A 155 12310 9900 8476 -1528 -746 -578 C ATOM 1234 O MET A 155 -354.868-182.789 136.663 1.00 82.24 O ANISOU 1234 O MET A 155 12504 10142 8601 -1520 -805 -458 O ATOM 1235 CB MET A 155 -356.015-185.308 134.848 1.00 93.85 C ANISOU 1235 CB MET A 155 14212 11616 9831 -1851 -787 -764 C ATOM 1236 CG MET A 155 -355.775-185.816 133.438 1.00108.80 C ANISOU 1236 CG MET A 155 16302 13564 11472 -2073 -705 -917 C ATOM 1237 SD MET A 155 -357.323-186.352 132.672 1.00121.28 S ANISOU 1237 SD MET A 155 17974 15196 12912 -2254 -928 -914 S ATOM 1238 CE MET A 155 -358.314-184.866 132.848 1.00117.68 C ANISOU 1238 CE MET A 155 17456 14815 12443 -2225 -1238 -630 C ATOM 1239 N GLY A 156 -355.659-184.521 137.866 1.00 72.52 N ANISOU 1239 N GLY A 156 11133 8785 7637 -1405 -784 -555 N ATOM 1240 CA GLY A 156 -356.018-183.660 138.981 1.00 68.47 C ANISOU 1240 CA GLY A 156 10477 8265 7271 -1263 -888 -400 C ATOM 1241 C GLY A 156 -354.827-182.906 139.541 1.00 75.35 C ANISOU 1241 C GLY A 156 11297 9126 8205 -1153 -777 -364 C ATOM 1242 O GLY A 156 -354.909-181.703 139.808 1.00 79.02 O ANISOU 1242 O GLY A 156 11720 9630 8676 -1107 -866 -233 O ATOM 1243 N VAL A 157 -353.701-183.601 139.718 1.00 71.12 N ANISOU 1243 N VAL A 157 10758 8531 7735 -1111 -585 -480 N ATOM 1244 CA VAL A 157 -352.498-182.952 140.228 1.00 69.78 C ANISOU 1244 CA VAL A 157 10531 8346 7635 -1013 -478 -453 C ATOM 1245 C VAL A 157 -351.992-181.917 139.231 1.00 71.05 C ANISOU 1245 C VAL A 157 10796 8590 7611 -1107 -468 -424 C ATOM 1246 O VAL A 157 -351.683-180.779 139.600 1.00 73.15 O ANISOU 1246 O VAL A 157 11017 8883 7895 -1046 -507 -312 O ATOM 1247 CB VAL A 157 -351.422-184.001 140.560 1.00 70.05 C ANISOU 1247 CB VAL A 157 10527 8285 7802 -955 -284 -587 C ATOM 1248 CG1 VAL A 157 -350.088-183.332 140.828 1.00 64.43 C ANISOU 1248 CG1 VAL A 157 9771 7567 7142 -884 -168 -575 C ATOM 1249 CG2 VAL A 157 -351.851-184.822 141.764 1.00 68.27 C ANISOU 1249 CG2 VAL A 157 10187 7975 7778 -848 -315 -569 C ATOM 1250 N ALA A 158 -351.919-182.292 137.951 1.00 72.89 N ANISOU 1250 N ALA A 158 11176 8864 7655 -1269 -417 -524 N ATOM 1251 CA ALA A 158 -351.469-181.353 136.929 1.00 72.95 C ANISOU 1251 CA ALA A 158 11304 8958 7458 -1388 -407 -493 C ATOM 1252 C ALA A 158 -352.371-180.128 136.872 1.00 80.46 C ANISOU 1252 C ALA A 158 12257 9972 8341 -1405 -636 -299 C ATOM 1253 O ALA A 158 -351.897-179.005 136.655 1.00 83.09 O ANISOU 1253 O ALA A 158 12615 10347 8609 -1418 -652 -206 O ATOM 1254 CB ALA A 158 -351.418-182.042 135.569 1.00 69.75 C ANISOU 1254 CB ALA A 158 11070 8594 6837 -1587 -326 -637 C ATOM 1255 N PHE A 159 -353.674-180.325 137.077 1.00 75.07 N ANISOU 1255 N PHE A 159 11540 9288 7695 -1405 -815 -237 N ATOM 1256 CA PHE A 159 -354.613-179.211 137.045 1.00 71.31 C ANISOU 1256 CA PHE A 159 11042 8853 7200 -1413 -1042 -57 C ATOM 1257 C PHE A 159 -354.290-178.175 138.116 1.00 74.54 C ANISOU 1257 C PHE A 159 11314 9230 7777 -1252 -1054 55 C ATOM 1258 O PHE A 159 -354.392-176.969 137.868 1.00 79.04 O ANISOU 1258 O PHE A 159 11895 9832 8305 -1270 -1165 187 O ATOM 1259 CB PHE A 159 -356.037-179.735 137.212 1.00 64.58 C ANISOU 1259 CB PHE A 159 10142 7988 6408 -1424 -1209 -31 C ATOM 1260 CG PHE A 159 -357.071-178.659 137.330 1.00 65.98 C ANISOU 1260 CG PHE A 159 10254 8183 6634 -1408 -1443 148 C ATOM 1261 CD1 PHE A 159 -357.526-177.987 136.205 1.00 68.84 C ANISOU 1261 CD1 PHE A 159 10728 8609 6819 -1558 -1610 247 C ATOM 1262 CD2 PHE A 159 -357.602-178.325 138.567 1.00 63.77 C ANISOU 1262 CD2 PHE A 159 9798 7850 6582 -1252 -1497 215 C ATOM 1263 CE1 PHE A 159 -358.488-176.996 136.312 1.00 69.29 C ANISOU 1263 CE1 PHE A 159 10706 8662 6958 -1536 -1837 418 C ATOM 1264 CE2 PHE A 159 -358.565-177.339 138.681 1.00 66.09 C ANISOU 1264 CE2 PHE A 159 10012 8144 6955 -1232 -1699 363 C ATOM 1265 CZ PHE A 159 -359.008-176.671 137.550 1.00 70.05 C ANISOU 1265 CZ PHE A 159 10611 8694 7310 -1367 -1875 468 C ATOM 1266 N THR A 160 -353.899-178.617 139.314 1.00 74.38 N ANISOU 1266 N THR A 160 11168 9145 7949 -1102 -949 7 N ATOM 1267 CA THR A 160 -353.548-177.654 140.354 1.00 75.16 C ANISOU 1267 CA THR A 160 11147 9220 8193 -964 -952 98 C ATOM 1268 C THR A 160 -352.308-176.856 139.968 1.00 78.22 C ANISOU 1268 C THR A 160 11586 9630 8503 -981 -850 110 C ATOM 1269 O THR A 160 -352.212-175.664 140.279 1.00 74.99 O ANISOU 1269 O THR A 160 11132 9227 8135 -933 -913 222 O ATOM 1270 CB THR A 160 -353.317-178.349 141.695 1.00 69.79 C ANISOU 1270 CB THR A 160 10339 8472 7706 -825 -861 47 C ATOM 1271 OG1 THR A 160 -352.155-179.183 141.608 1.00 74.62 O ANISOU 1271 OG1 THR A 160 10981 9052 8319 -821 -675 -77 O ATOM 1272 CG2 THR A 160 -354.525-179.189 142.092 1.00 68.77 C ANISOU 1272 CG2 THR A 160 10160 8318 7652 -819 -947 32 C ATOM 1273 N TRP A 161 -351.341-177.495 139.302 1.00 72.49 N ANISOU 1273 N TRP A 161 10949 8912 7681 -1051 -682 -13 N ATOM 1274 CA TRP A 161 -350.147-176.767 138.884 1.00 70.49 C ANISOU 1274 CA TRP A 161 10743 8684 7354 -1081 -569 -12 C ATOM 1275 C TRP A 161 -350.486-175.736 137.817 1.00 76.24 C ANISOU 1275 C TRP A 161 11593 9485 7891 -1218 -691 98 C ATOM 1276 O TRP A 161 -349.908-174.642 137.794 1.00 81.55 O ANISOU 1276 O TRP A 161 12264 10171 8549 -1210 -688 183 O ATOM 1277 CB TRP A 161 -349.077-177.726 138.363 1.00 67.51 C ANISOU 1277 CB TRP A 161 10425 8294 6932 -1135 -347 -186 C ATOM 1278 CG TRP A 161 -348.612-178.751 139.354 1.00 74.88 C ANISOU 1278 CG TRP A 161 11239 9139 8072 -1005 -230 -284 C ATOM 1279 CD1 TRP A 161 -348.899-178.799 140.686 1.00 74.28 C ANISOU 1279 CD1 TRP A 161 11023 9010 8191 -855 -293 -223 C ATOM 1280 CD2 TRP A 161 -347.783-179.888 139.082 1.00 86.92 C ANISOU 1280 CD2 TRP A 161 12777 10615 9636 -1024 -36 -457 C ATOM 1281 NE1 TRP A 161 -348.301-179.891 141.262 1.00 74.77 N ANISOU 1281 NE1 TRP A 161 11015 8993 8401 -782 -167 -328 N ATOM 1282 CE2 TRP A 161 -347.608-180.577 140.299 1.00 89.06 C ANISOU 1282 CE2 TRP A 161 12906 10794 10137 -875 -10 -474 C ATOM 1283 CE3 TRP A 161 -347.170-180.389 137.926 1.00 88.67 C ANISOU 1283 CE3 TRP A 161 13113 10854 9724 -1159 125 -605 C ATOM 1284 CZ2 TRP A 161 -346.846-181.742 140.394 1.00 96.08 C ANISOU 1284 CZ2 TRP A 161 13756 11597 11152 -845 154 -619 C ATOM 1285 CZ3 TRP A 161 -346.414-181.546 138.023 1.00 89.12 C ANISOU 1285 CZ3 TRP A 161 13125 10826 9912 -1127 309 -773 C ATOM 1286 CH2 TRP A 161 -346.259-182.209 139.247 1.00 93.34 C ANISOU 1286 CH2 TRP A 161 13507 11257 10701 -965 315 -772 C ATOM 1287 N VAL A 162 -351.421-176.065 136.927 1.00 76.12 N ANISOU 1287 N VAL A 162 11683 9513 7727 -1351 -809 106 N ATOM 1288 CA VAL A 162 -351.848-175.109 135.912 1.00 74.98 C ANISOU 1288 CA VAL A 162 11658 9434 7398 -1495 -963 236 C ATOM 1289 C VAL A 162 -352.554-173.927 136.565 1.00 82.24 C ANISOU 1289 C VAL A 162 12466 10324 8457 -1396 -1159 420 C ATOM 1290 O VAL A 162 -352.254-172.765 136.270 1.00 83.52 O ANISOU 1290 O VAL A 162 12658 10501 8573 -1427 -1215 539 O ATOM 1291 CB VAL A 162 -352.733-175.806 134.864 1.00 74.56 C ANISOU 1291 CB VAL A 162 11738 9432 7160 -1667 -1064 204 C ATOM 1292 CG1 VAL A 162 -353.360-174.791 133.934 1.00 73.94 C ANISOU 1292 CG1 VAL A 162 11766 9413 6915 -1810 -1281 377 C ATOM 1293 CG2 VAL A 162 -351.907-176.810 134.066 1.00 71.93 C ANISOU 1293 CG2 VAL A 162 11535 9130 6666 -1793 -847 10 C ATOM 1294 N MET A 163 -353.478-174.203 137.490 1.00 80.26 N ANISOU 1294 N MET A 163 12079 10024 8392 -1277 -1254 437 N ATOM 1295 CA MET A 163 -354.168-173.119 138.183 1.00 78.40 C ANISOU 1295 CA MET A 163 11720 9750 8321 -1177 -1416 585 C ATOM 1296 C MET A 163 -353.202-172.287 139.022 1.00 79.39 C ANISOU 1296 C MET A 163 11760 9840 8566 -1056 -1311 607 C ATOM 1297 O MET A 163 -353.331-171.059 139.093 1.00 81.96 O ANISOU 1297 O MET A 163 12050 10146 8944 -1035 -1416 736 O ATOM 1298 CB MET A 163 -355.290-173.679 139.057 1.00 73.83 C ANISOU 1298 CB MET A 163 11007 9126 7918 -1083 -1497 570 C ATOM 1299 CG MET A 163 -356.479-174.209 138.282 1.00 80.56 C ANISOU 1299 CG MET A 163 11914 10005 8690 -1197 -1661 588 C ATOM 1300 SD MET A 163 -357.216-172.927 137.255 1.00 83.94 S ANISOU 1300 SD MET A 163 12403 10457 9033 -1314 -1925 789 S ATOM 1301 CE MET A 163 -356.707-173.494 135.635 1.00 87.99 C ANISOU 1301 CE MET A 163 13168 11065 9200 -1551 -1889 737 C ATOM 1302 N ALA A 164 -352.227-172.934 139.665 1.00 72.86 N ANISOU 1302 N ALA A 164 10894 8995 7794 -980 -1112 485 N ATOM 1303 CA ALA A 164 -351.296-172.199 140.515 1.00 67.63 C ANISOU 1303 CA ALA A 164 10146 8301 7249 -870 -1020 502 C ATOM 1304 C ALA A 164 -350.382-171.303 139.691 1.00 77.43 C ANISOU 1304 C ALA A 164 11485 9576 8361 -956 -977 553 C ATOM 1305 O ALA A 164 -350.098-170.166 140.086 1.00 73.56 O ANISOU 1305 O ALA A 164 10940 9062 7949 -903 -1009 643 O ATOM 1306 CB ALA A 164 -350.473-173.162 141.358 1.00 59.02 C ANISOU 1306 CB ALA A 164 8988 7181 6254 -778 -840 373 C ATOM 1307 N LEU A 165 -349.905-171.798 138.548 1.00 78.02 N ANISOU 1307 N LEU A 165 11705 9704 8237 -1099 -893 488 N ATOM 1308 CA LEU A 165 -349.133-170.948 137.653 1.00 76.16 C ANISOU 1308 CA LEU A 165 11580 9508 7849 -1213 -856 542 C ATOM 1309 C LEU A 165 -349.987-169.823 137.084 1.00 75.43 C ANISOU 1309 C LEU A 165 11538 9427 7694 -1289 -1083 727 C ATOM 1310 O LEU A 165 -349.480-168.720 136.853 1.00 74.63 O ANISOU 1310 O LEU A 165 11464 9325 7567 -1319 -1099 827 O ATOM 1311 CB LEU A 165 -348.523-171.790 136.531 1.00 77.03 C ANISOU 1311 CB LEU A 165 11843 9678 7747 -1371 -705 415 C ATOM 1312 CG LEU A 165 -347.411-172.749 136.954 1.00 77.33 C ANISOU 1312 CG LEU A 165 11827 9689 7865 -1307 -458 234 C ATOM 1313 CD1 LEU A 165 -347.078-173.710 135.827 1.00 81.41 C ANISOU 1313 CD1 LEU A 165 12487 10253 8190 -1468 -317 86 C ATOM 1314 CD2 LEU A 165 -346.181-171.959 137.367 1.00 73.42 C ANISOU 1314 CD2 LEU A 165 11270 9176 7451 -1246 -336 249 C ATOM 1315 N ALA A 166 -351.284-170.071 136.875 1.00 74.70 N ANISOU 1315 N ALA A 166 11449 9336 7598 -1318 -1268 782 N ATOM 1316 CA ALA A 166 -352.165-169.029 136.352 1.00 70.24 C ANISOU 1316 CA ALA A 166 10912 8764 7010 -1384 -1510 970 C ATOM 1317 C ALA A 166 -352.264-167.841 137.302 1.00 77.16 C ANISOU 1317 C ALA A 166 11640 9563 8116 -1239 -1584 1077 C ATOM 1318 O ALA A 166 -352.529-166.716 136.863 1.00 78.24 O ANISOU 1318 O ALA A 166 11802 9678 8249 -1288 -1739 1238 O ATOM 1319 CB ALA A 166 -353.555-169.597 136.078 1.00 65.59 C ANISOU 1319 CB ALA A 166 10322 8181 6418 -1425 -1696 997 C ATOM 1320 N CYS A 167 -352.067-168.066 138.599 1.00 72.15 N ANISOU 1320 N CYS A 167 10853 8879 7681 -1068 -1481 993 N ATOM 1321 CA CYS A 167 -352.075-166.966 139.551 1.00 73.90 C ANISOU 1321 CA CYS A 167 10938 9029 8113 -940 -1521 1066 C ATOM 1322 C CYS A 167 -350.673-166.418 139.815 1.00 73.74 C ANISOU 1322 C CYS A 167 10923 9007 8089 -913 -1357 1041 C ATOM 1323 O CYS A 167 -350.491-165.198 139.882 1.00 78.21 O ANISOU 1323 O CYS A 167 11463 9531 8722 -900 -1417 1148 O ATOM 1324 CB CYS A 167 -352.718-167.412 140.865 1.00 72.82 C ANISOU 1324 CB CYS A 167 10635 8845 8188 -788 -1512 997 C ATOM 1325 SG CYS A 167 -352.128-166.516 142.318 1.00 78.75 S ANISOU 1325 SG CYS A 167 11232 9531 9160 -629 -1426 985 S ATOM 1326 N ALA A 168 -349.676-167.294 139.940 1.00 68.62 N ANISOU 1326 N ALA A 168 10300 8394 7378 -909 -1155 903 N ATOM 1327 CA ALA A 168 -348.363-166.904 140.424 1.00 67.99 C ANISOU 1327 CA ALA A 168 10185 8305 7345 -858 -995 861 C ATOM 1328 C ALA A 168 -347.446-166.351 139.342 1.00 75.31 C ANISOU 1328 C ALA A 168 11242 9272 8099 -994 -930 900 C ATOM 1329 O ALA A 168 -346.540-165.569 139.661 1.00 69.96 O ANISOU 1329 O ALA A 168 10529 8574 7479 -963 -855 920 O ATOM 1330 CB ALA A 168 -347.673-168.095 141.090 1.00 59.09 C ANISOU 1330 CB ALA A 168 9004 7183 6265 -786 -815 701 C ATOM 1331 N ALA A 169 -347.648-166.734 138.085 1.00 76.35 N ANISOU 1331 N ALA A 169 11530 9465 8015 -1155 -953 907 N ATOM 1332 CA ALA A 169 -346.748-166.360 137.002 1.00 72.12 C ANISOU 1332 CA ALA A 169 11138 8982 7281 -1314 -862 924 C ATOM 1333 C ALA A 169 -347.012-164.972 136.402 1.00 74.70 C ANISOU 1333 C ALA A 169 11531 9298 7554 -1402 -1027 1120 C ATOM 1334 O ALA A 169 -346.040-164.266 136.098 1.00 78.30 O ANISOU 1334 O ALA A 169 12033 9763 7956 -1461 -935 1151 O ATOM 1335 CB ALA A 169 -346.788-167.428 135.904 1.00 65.07 C ANISOU 1335 CB ALA A 169 10398 8167 6159 -1472 -792 827 C ATOM 1336 N PRO A 170 -348.261-164.534 136.199 1.00 76.14 N ANISOU 1336 N PRO A 170 11717 9452 7760 -1418 -1270 1261 N ATOM 1337 CA PRO A 170 -348.497-163.201 135.582 1.00 79.55 C ANISOU 1337 CA PRO A 170 12211 9856 8157 -1507 -1445 1466 C ATOM 1338 C PRO A 170 -347.744-162.065 136.264 1.00 79.18 C ANISOU 1338 C PRO A 170 12073 9741 8272 -1416 -1395 1517 C ATOM 1339 O PRO A 170 -347.175-161.217 135.563 1.00 77.09 O ANISOU 1339 O PRO A 170 11907 9484 7900 -1535 -1400 1622 O ATOM 1340 CB PRO A 170 -350.019-163.027 135.696 1.00 79.03 C ANISOU 1340 CB PRO A 170 12082 9739 8208 -1466 -1709 1580 C ATOM 1341 CG PRO A 170 -350.531-164.423 135.568 1.00 70.75 C ANISOU 1341 CG PRO A 170 11059 8748 7076 -1484 -1676 1450 C ATOM 1342 CD PRO A 170 -349.530-165.291 136.300 1.00 74.04 C ANISOU 1342 CD PRO A 170 11418 9184 7529 -1389 -1407 1247 C ATOM 1343 N PRO A 171 -347.696-161.986 137.602 1.00 76.80 N ANISOU 1343 N PRO A 171 11591 9373 8216 -1224 -1346 1449 N ATOM 1344 CA PRO A 171 -346.943-160.878 138.229 1.00 70.39 C ANISOU 1344 CA PRO A 171 10700 8498 7549 -1152 -1298 1491 C ATOM 1345 C PRO A 171 -345.459-160.842 137.868 1.00 76.36 C ANISOU 1345 C PRO A 171 11528 9304 8181 -1230 -1088 1429 C ATOM 1346 O PRO A 171 -344.800-159.831 138.142 1.00 89.02 O ANISOU 1346 O PRO A 171 13095 10861 9869 -1211 -1060 1485 O ATOM 1347 CB PRO A 171 -347.138-161.117 139.734 1.00 73.57 C ANISOU 1347 CB PRO A 171 10915 8846 8193 -954 -1255 1388 C ATOM 1348 CG PRO A 171 -348.383-161.908 139.829 1.00 69.66 C ANISOU 1348 CG PRO A 171 10390 8355 7723 -921 -1367 1367 C ATOM 1349 CD PRO A 171 -348.383-162.798 138.628 1.00 69.71 C ANISOU 1349 CD PRO A 171 10558 8452 7478 -1074 -1347 1345 C ATOM 1350 N LEU A 172 -344.910-161.900 137.270 1.00 79.11 N ANISOU 1350 N LEU A 172 11970 9739 8349 -1318 -931 1307 N ATOM 1351 CA LEU A 172 -343.532-161.852 136.797 1.00 78.19 C ANISOU 1351 CA LEU A 172 11921 9670 8118 -1411 -724 1244 C ATOM 1352 C LEU A 172 -343.433-161.244 135.404 1.00 83.82 C ANISOU 1352 C LEU A 172 12824 10431 8591 -1632 -772 1369 C ATOM 1353 O LEU A 172 -342.370-160.729 135.038 1.00 91.05 O ANISOU 1353 O LEU A 172 13789 11366 9440 -1717 -640 1373 O ATOM 1354 CB LEU A 172 -342.914-163.259 136.790 1.00 68.29 C ANISOU 1354 CB LEU A 172 10668 8474 6806 -1409 -512 1040 C ATOM 1355 CG LEU A 172 -342.881-164.109 138.066 1.00 67.40 C ANISOU 1355 CG LEU A 172 10389 8323 6895 -1219 -444 907 C ATOM 1356 CD1 LEU A 172 -342.350-165.494 137.757 1.00 67.58 C ANISOU 1356 CD1 LEU A 172 10442 8394 6841 -1252 -257 727 C ATOM 1357 CD2 LEU A 172 -342.032-163.482 139.143 1.00 67.96 C ANISOU 1357 CD2 LEU A 172 10317 8340 7164 -1092 -373 896 C ATOM 1358 N VAL A 173 -344.513-161.280 134.620 1.00 82.98 N ANISOU 1358 N VAL A 173 12828 10348 8354 -1737 -965 1478 N ATOM 1359 CA VAL A 173 -344.471-160.881 133.215 1.00 83.26 C ANISOU 1359 CA VAL A 173 13072 10447 8116 -1979 -1020 1596 C ATOM 1360 C VAL A 173 -345.307-159.647 132.918 1.00 87.29 C ANISOU 1360 C VAL A 173 13611 10891 8665 -2021 -1302 1848 C ATOM 1361 O VAL A 173 -345.423-159.270 131.746 1.00 96.53 O ANISOU 1361 O VAL A 173 14963 12109 9605 -2233 -1397 1982 O ATOM 1362 CB VAL A 173 -344.894-162.033 132.285 1.00 83.92 C ANISOU 1362 CB VAL A 173 13303 10630 7953 -2127 -1002 1513 C ATOM 1363 CG1 VAL A 173 -343.846-163.131 132.307 1.00 83.15 C ANISOU 1363 CG1 VAL A 173 13206 10593 7795 -2132 -694 1270 C ATOM 1364 CG2 VAL A 173 -346.272-162.576 132.676 1.00 86.56 C ANISOU 1364 CG2 VAL A 173 13565 10934 8390 -2028 -1199 1529 C ATOM 1365 N GLY A 174 -345.898-159.006 133.924 1.00 82.72 N ANISOU 1365 N GLY A 174 12861 10198 8371 -1836 -1440 1916 N ATOM 1366 CA GLY A 174 -346.561-157.751 133.643 1.00 84.59 C ANISOU 1366 CA GLY A 174 13108 10348 8682 -1873 -1692 2152 C ATOM 1367 C GLY A 174 -347.960-157.532 134.181 1.00 91.45 C ANISOU 1367 C GLY A 174 13848 11121 9778 -1744 -1938 2240 C ATOM 1368 O GLY A 174 -348.390-156.381 134.292 1.00 95.92 O ANISOU 1368 O GLY A 174 14358 11576 10511 -1714 -2119 2410 O ATOM 1369 N TRP A 175 -348.698-158.595 134.500 1.00 88.95 N ANISOU 1369 N TRP A 175 13476 10836 9485 -1672 -1951 2128 N ATOM 1370 CA TRP A 175 -350.036-158.445 135.068 1.00 83.33 C ANISOU 1370 CA TRP A 175 12621 10033 9007 -1546 -2163 2190 C ATOM 1371 C TRP A 175 -349.909-158.499 136.587 1.00 79.59 C ANISOU 1371 C TRP A 175 11939 9493 8809 -1318 -2038 2047 C ATOM 1372 O TRP A 175 -349.583-159.547 137.152 1.00 79.69 O ANISOU 1372 O TRP A 175 11912 9564 8803 -1247 -1862 1862 O ATOM 1373 CB TRP A 175 -350.985-159.515 134.535 1.00 86.43 C ANISOU 1373 CB TRP A 175 13072 10494 9272 -1614 -2263 2162 C ATOM 1374 CG TRP A 175 -352.449-159.158 134.674 1.00 89.74 C ANISOU 1374 CG TRP A 175 13383 10821 9892 -1554 -2543 2292 C ATOM 1375 CD1 TRP A 175 -352.973-157.920 134.906 1.00 88.29 C ANISOU 1375 CD1 TRP A 175 13096 10504 9945 -1493 -2733 2460 C ATOM 1376 CD2 TRP A 175 -353.566-160.058 134.603 1.00 91.76 C ANISOU 1376 CD2 TRP A 175 13609 11103 10154 -1548 -2658 2257 C ATOM 1377 NE1 TRP A 175 -354.344-157.990 134.981 1.00 88.98 N ANISOU 1377 NE1 TRP A 175 13082 10530 10198 -1446 -2957 2530 N ATOM 1378 CE2 TRP A 175 -354.733-159.291 134.798 1.00 91.30 C ANISOU 1378 CE2 TRP A 175 13418 10923 10347 -1482 -2917 2410 C ATOM 1379 CE3 TRP A 175 -353.691-161.436 134.394 1.00 90.44 C ANISOU 1379 CE3 TRP A 175 13505 11039 9819 -1594 -2565 2108 C ATOM 1380 CZ2 TRP A 175 -356.008-159.856 134.788 1.00 92.14 C ANISOU 1380 CZ2 TRP A 175 13451 11018 10539 -1462 -3085 2419 C ATOM 1381 CZ3 TRP A 175 -354.958-161.995 134.385 1.00 88.25 C ANISOU 1381 CZ3 TRP A 175 13166 10751 9614 -1579 -2734 2119 C ATOM 1382 CH2 TRP A 175 -356.098-161.206 134.581 1.00 92.42 C ANISOU 1382 CH2 TRP A 175 13558 11166 10390 -1514 -2991 2275 C ATOM 1383 N SER A 176 -350.158-157.360 137.241 1.00 79.69 N ANISOU 1383 N SER A 176 11821 9380 9077 -1213 -2132 2134 N ATOM 1384 CA SER A 176 -349.850-157.138 138.654 1.00 73.66 C ANISOU 1384 CA SER A 176 10881 8552 8556 -1026 -2004 2012 C ATOM 1385 C SER A 176 -348.341-157.224 138.879 1.00 70.18 C ANISOU 1385 C SER A 176 10479 8168 8017 -1037 -1760 1904 C ATOM 1386 O SER A 176 -347.570-157.142 137.917 1.00 70.11 O ANISOU 1386 O SER A 176 10622 8221 7794 -1186 -1705 1952 O ATOM 1387 CB SER A 176 -350.611-158.123 139.549 1.00 73.80 C ANISOU 1387 CB SER A 176 10774 8580 8686 -898 -1976 1868 C ATOM 1388 OG SER A 176 -350.437-157.804 140.920 1.00 82.90 O ANISOU 1388 OG SER A 176 11762 9668 10069 -737 -1878 1768 O ATOM 1389 N ARG A 177 -347.910-157.389 140.130 1.00 65.13 N ANISOU 1389 N ARG A 177 9706 7510 7532 -891 -1615 1761 N ATOM 1390 CA ARG A 177 -346.490-157.388 140.454 1.00 67.02 C ANISOU 1390 CA ARG A 177 9953 7786 7725 -887 -1404 1667 C ATOM 1391 C ARG A 177 -346.313-157.915 141.870 1.00 64.20 C ANISOU 1391 C ARG A 177 9449 7424 7523 -729 -1283 1504 C ATOM 1392 O ARG A 177 -347.249-157.901 142.672 1.00 69.60 O ANISOU 1392 O ARG A 177 10017 8052 8375 -623 -1363 1482 O ATOM 1393 CB ARG A 177 -345.887-155.978 140.328 1.00 64.42 C ANISOU 1393 CB ARG A 177 9630 7382 7465 -922 -1429 1782 C ATOM 1394 CG ARG A 177 -346.541-154.992 141.273 1.00 67.99 C ANISOU 1394 CG ARG A 177 9930 7701 8202 -796 -1538 1821 C ATOM 1395 CD ARG A 177 -345.828-153.679 141.322 1.00 72.60 C ANISOU 1395 CD ARG A 177 10505 8203 8878 -816 -1533 1902 C ATOM 1396 NE ARG A 177 -346.503-152.750 142.221 1.00 76.63 N ANISOU 1396 NE ARG A 177 10865 8575 9676 -697 -1629 1921 N ATOM 1397 CZ ARG A 177 -346.022-151.553 142.531 1.00 73.74 C ANISOU 1397 CZ ARG A 177 10453 8109 9455 -684 -1629 1968 C ATOM 1398 NH1 ARG A 177 -344.868-151.166 142.012 1.00 65.81 N ANISOU 1398 NH1 ARG A 177 9543 7135 8327 -783 -1540 2011 N ATOM 1399 NH2 ARG A 177 -346.687-150.756 143.358 1.00 68.45 N ANISOU 1399 NH2 ARG A 177 9642 7306 9059 -578 -1704 1963 N ATOM 1400 N TYR A 178 -345.095-158.389 142.163 1.00 64.23 N ANISOU 1400 N TYR A 178 9454 7483 7466 -724 -1089 1391 N ATOM 1401 CA TYR A 178 -344.703-158.759 143.522 1.00 62.03 C ANISOU 1401 CA TYR A 178 9046 7198 7326 -593 -979 1257 C ATOM 1402 C TYR A 178 -343.995-157.583 144.181 1.00 62.56 C ANISOU 1402 C TYR A 178 9041 7199 7531 -553 -948 1277 C ATOM 1403 O TYR A 178 -343.107-156.973 143.581 1.00 66.63 O ANISOU 1403 O TYR A 178 9619 7717 7981 -635 -898 1330 O ATOM 1404 CB TYR A 178 -343.781-159.984 143.536 1.00 64.53 C ANISOU 1404 CB TYR A 178 9385 7598 7534 -602 -803 1126 C ATOM 1405 CG TYR A 178 -344.452-161.271 143.167 1.00 68.52 C ANISOU 1405 CG TYR A 178 9937 8158 7940 -618 -812 1070 C ATOM 1406 CD1 TYR A 178 -345.394-161.858 144.010 1.00 71.81 C ANISOU 1406 CD1 TYR A 178 10268 8559 8459 -521 -869 1021 C ATOM 1407 CD2 TYR A 178 -344.148-161.912 141.976 1.00 73.37 C ANISOU 1407 CD2 TYR A 178 10683 8839 8354 -741 -754 1058 C ATOM 1408 CE1 TYR A 178 -346.021-163.046 143.662 1.00 67.89 C ANISOU 1408 CE1 TYR A 178 9813 8106 7876 -541 -880 971 C ATOM 1409 CE2 TYR A 178 -344.765-163.100 141.622 1.00 74.28 C ANISOU 1409 CE2 TYR A 178 10844 8999 8379 -763 -761 997 C ATOM 1410 CZ TYR A 178 -345.701-163.659 142.466 1.00 72.07 C ANISOU 1410 CZ TYR A 178 10474 8697 8213 -660 -829 958 C ATOM 1411 OH TYR A 178 -346.307-164.839 142.103 1.00 76.12 O ANISOU 1411 OH TYR A 178 11032 9249 8642 -688 -836 898 O ATOM 1412 N ILE A 179 -344.395-157.268 145.408 1.00 56.78 N ANISOU 1412 N ILE A 179 8179 6409 6984 -439 -971 1228 N ATOM 1413 CA ILE A 179 -343.771-156.226 146.222 1.00 62.77 C ANISOU 1413 CA ILE A 179 8858 7105 7887 -396 -935 1217 C ATOM 1414 C ILE A 179 -343.767-156.691 147.667 1.00 58.75 C ANISOU 1414 C ILE A 179 8233 6603 7484 -291 -869 1086 C ATOM 1415 O ILE A 179 -344.561-157.557 148.056 1.00 64.32 O ANISOU 1415 O ILE A 179 8910 7336 8193 -244 -889 1030 O ATOM 1416 CB ILE A 179 -344.509-154.867 146.109 1.00 68.33 C ANISOU 1416 CB ILE A 179 9532 7691 8738 -393 -1078 1331 C ATOM 1417 CG1 ILE A 179 -345.959-154.975 146.594 1.00 65.14 C ANISOU 1417 CG1 ILE A 179 9046 7236 8467 -317 -1191 1320 C ATOM 1418 CG2 ILE A 179 -344.468-154.307 144.689 1.00 59.09 C ANISOU 1418 CG2 ILE A 179 8486 6507 7458 -515 -1164 1489 C ATOM 1419 CD1 ILE A 179 -346.650-153.620 146.701 1.00 66.49 C ANISOU 1419 CD1 ILE A 179 9148 7267 8847 -291 -1317 1405 C ATOM 1420 N PRO A 180 -342.875-156.142 148.489 1.00 62.40 N ANISOU 1420 N PRO A 180 8635 7047 8028 -264 -793 1036 N ATOM 1421 CA PRO A 180 -342.976-156.408 149.926 1.00 61.67 C ANISOU 1421 CA PRO A 180 8440 6957 8035 -182 -755 925 C ATOM 1422 C PRO A 180 -344.348-155.993 150.431 1.00 58.07 C ANISOU 1422 C PRO A 180 7919 6433 7712 -130 -850 921 C ATOM 1423 O PRO A 180 -344.982-155.081 149.898 1.00 58.04 O ANISOU 1423 O PRO A 180 7917 6347 7789 -143 -947 1007 O ATOM 1424 CB PRO A 180 -341.854-155.551 150.529 1.00 53.68 C ANISOU 1424 CB PRO A 180 7384 5918 7092 -188 -690 900 C ATOM 1425 CG PRO A 180 -340.841-155.492 149.436 1.00 54.32 C ANISOU 1425 CG PRO A 180 7545 6028 7065 -267 -638 962 C ATOM 1426 CD PRO A 180 -341.642-155.402 148.159 1.00 56.63 C ANISOU 1426 CD PRO A 180 7931 6307 7281 -322 -727 1070 C ATOM 1427 N GLU A 181 -344.832-156.713 151.431 1.00 58.12 N ANISOU 1427 N GLU A 181 7866 6471 7747 -77 -823 825 N ATOM 1428 CA GLU A 181 -346.164-156.483 151.960 1.00 58.73 C ANISOU 1428 CA GLU A 181 7870 6493 7953 -31 -887 798 C ATOM 1429 C GLU A 181 -346.087-156.411 153.475 1.00 59.63 C ANISOU 1429 C GLU A 181 7900 6610 8145 6 -814 675 C ATOM 1430 O GLU A 181 -345.148-156.922 154.092 1.00 59.48 O ANISOU 1430 O GLU A 181 7890 6658 8053 -2 -735 620 O ATOM 1431 CB GLU A 181 -347.143-157.586 151.524 1.00 64.35 C ANISOU 1431 CB GLU A 181 8605 7247 8597 -25 -935 805 C ATOM 1432 CG GLU A 181 -346.772-158.946 152.065 1.00 74.07 C ANISOU 1432 CG GLU A 181 9851 8573 9720 -17 -851 724 C ATOM 1433 CD GLU A 181 -347.549-160.072 151.415 1.00 89.55 C ANISOU 1433 CD GLU A 181 11855 10577 11595 -27 -893 739 C ATOM 1434 OE1 GLU A 181 -348.371-159.794 150.512 1.00100.00 O ANISOU 1434 OE1 GLU A 181 13201 11864 12931 -47 -995 816 O ATOM 1435 OE2 GLU A 181 -347.329-161.237 151.811 1.00 87.64 O ANISOU 1435 OE2 GLU A 181 11623 10397 11278 -19 -833 679 O ATOM 1436 N GLY A 182 -347.085-155.760 154.064 1.00 56.87 N ANISOU 1436 N GLY A 182 7469 6186 7954 39 -844 633 N ATOM 1437 CA GLY A 182 -347.169-155.660 155.505 1.00 57.61 C ANISOU 1437 CA GLY A 182 7490 6285 8112 54 -768 504 C ATOM 1438 C GLY A 182 -345.912-155.076 156.109 1.00 64.75 C ANISOU 1438 C GLY A 182 8399 7198 9004 28 -702 467 C ATOM 1439 O GLY A 182 -345.529-153.933 155.807 1.00 60.50 O ANISOU 1439 O GLY A 182 7853 6581 8554 18 -720 505 O ATOM 1440 N MET A 183 -345.250-155.854 156.955 1.00 53.20 N ANISOU 1440 N MET A 183 6948 5826 7440 12 -637 403 N ATOM 1441 CA MET A 183 -344.026-155.379 157.581 1.00 60.02 C ANISOU 1441 CA MET A 183 7810 6706 8290 -20 -587 370 C ATOM 1442 C MET A 183 -342.829-155.446 156.640 1.00 59.09 C ANISOU 1442 C MET A 183 7747 6609 8097 -39 -588 459 C ATOM 1443 O MET A 183 -341.701-155.226 157.092 1.00 57.82 O ANISOU 1443 O MET A 183 7579 6471 7919 -67 -550 439 O ATOM 1444 CB MET A 183 -343.758-156.158 158.873 1.00 60.96 C ANISOU 1444 CB MET A 183 7918 6909 8333 -43 -537 281 C ATOM 1445 CG MET A 183 -344.705-155.796 160.024 1.00 64.74 C ANISOU 1445 CG MET A 183 8344 7369 8886 -55 -503 165 C ATOM 1446 SD MET A 183 -344.693-156.971 161.418 1.00 67.27 S ANISOU 1446 SD MET A 183 8678 7805 9077 -102 -459 85 S ATOM 1447 CE MET A 183 -343.013-156.844 162.034 1.00 68.44 C ANISOU 1447 CE MET A 183 8848 8005 9152 -156 -453 91 C ATOM 1448 N GLN A 184 -343.061-155.738 155.353 1.00 51.79 N ANISOU 1448 N GLN A 184 6873 5678 7125 -35 -629 551 N ATOM 1449 CA GLN A 184 -342.083-155.552 154.284 1.00 53.94 C ANISOU 1449 CA GLN A 184 7202 5954 7339 -70 -621 635 C ATOM 1450 C GLN A 184 -340.974-156.597 154.307 1.00 60.58 C ANISOU 1450 C GLN A 184 8064 6882 8072 -84 -556 619 C ATOM 1451 O GLN A 184 -339.942-156.424 153.649 1.00 63.55 O ANISOU 1451 O GLN A 184 8467 7266 8413 -119 -518 660 O ATOM 1452 CB GLN A 184 -341.477-154.137 154.330 1.00 54.17 C ANISOU 1452 CB GLN A 184 7210 5907 7465 -96 -618 654 C ATOM 1453 CG GLN A 184 -342.513-153.030 154.383 1.00 53.48 C ANISOU 1453 CG GLN A 184 7083 5708 7528 -77 -681 664 C ATOM 1454 CD GLN A 184 -343.315-152.948 153.104 1.00 60.86 C ANISOU 1454 CD GLN A 184 8065 6599 8459 -81 -769 779 C ATOM 1455 OE1 GLN A 184 -342.788-152.588 152.047 1.00 60.12 O ANISOU 1455 OE1 GLN A 184 8037 6492 8316 -129 -791 883 O ATOM 1456 NE2 GLN A 184 -344.592-153.316 153.181 1.00 56.80 N ANISOU 1456 NE2 GLN A 184 7522 6069 7990 -42 -823 765 N ATOM 1457 N CYS A 185 -341.163-157.687 155.045 1.00 58.93 N ANISOU 1457 N CYS A 185 7838 6732 7821 -60 -540 561 N ATOM 1458 CA CYS A 185 -340.160-158.736 155.113 1.00 62.34 C ANISOU 1458 CA CYS A 185 8273 7228 8186 -64 -491 549 C ATOM 1459 C CYS A 185 -340.474-159.911 154.208 1.00 67.14 C ANISOU 1459 C CYS A 185 8933 7869 8707 -58 -484 571 C ATOM 1460 O CYS A 185 -339.633-160.804 154.069 1.00 66.66 O ANISOU 1460 O CYS A 185 8873 7846 8610 -60 -434 560 O ATOM 1461 CB CYS A 185 -340.009-159.234 156.546 1.00 54.05 C ANISOU 1461 CB CYS A 185 7174 6216 7147 -55 -488 483 C ATOM 1462 SG CYS A 185 -339.292-158.013 157.618 1.00 73.97 S ANISOU 1462 SG CYS A 185 9644 8717 9746 -87 -482 442 S ATOM 1463 N SER A 186 -341.663-159.952 153.619 1.00 63.40 N ANISOU 1463 N SER A 186 8497 7379 8214 -51 -534 597 N ATOM 1464 CA SER A 186 -341.995-160.991 152.661 1.00 62.76 C ANISOU 1464 CA SER A 186 8476 7329 8042 -60 -533 616 C ATOM 1465 C SER A 186 -342.765-160.351 151.523 1.00 59.99 C ANISOU 1465 C SER A 186 8183 6943 7667 -91 -596 689 C ATOM 1466 O SER A 186 -343.274-159.234 151.645 1.00 66.22 O ANISOU 1466 O SER A 186 8948 7675 8539 -86 -654 721 O ATOM 1467 CB SER A 186 -342.787-162.136 153.308 1.00 57.38 C ANISOU 1467 CB SER A 186 7778 6676 7348 -27 -548 569 C ATOM 1468 OG SER A 186 -343.992-161.672 153.872 1.00 72.73 O ANISOU 1468 OG SER A 186 9688 8593 9353 -7 -606 557 O ATOM 1469 N CYS A 187 -342.826-161.064 150.403 1.00 53.91 N ANISOU 1469 N CYS A 187 7489 6203 6790 -129 -588 714 N ATOM 1470 CA CYS A 187 -343.336-160.495 149.161 1.00 56.12 C ANISOU 1470 CA CYS A 187 7846 6462 7014 -186 -655 802 C ATOM 1471 C CYS A 187 -344.574-161.248 148.694 1.00 67.45 C ANISOU 1471 C CYS A 187 9317 7912 8400 -190 -730 812 C ATOM 1472 O CYS A 187 -344.710-162.460 148.912 1.00 66.54 O ANISOU 1472 O CYS A 187 9201 7837 8243 -171 -693 749 O ATOM 1473 CB CYS A 187 -342.268-160.517 148.064 1.00 57.23 C ANISOU 1473 CB CYS A 187 8068 6634 7043 -265 -579 829 C ATOM 1474 SG CYS A 187 -340.888-159.345 148.325 1.00 63.57 S ANISOU 1474 SG CYS A 187 8835 7408 7912 -283 -509 844 S ATOM 1475 N GLY A 188 -345.468-160.516 148.040 1.00 66.77 N ANISOU 1475 N GLY A 188 9257 7783 8328 -218 -845 900 N ATOM 1476 CA GLY A 188 -346.685-161.112 147.552 1.00 54.88 C ANISOU 1476 CA GLY A 188 7778 6286 6789 -229 -938 921 C ATOM 1477 C GLY A 188 -347.322-160.283 146.459 1.00 57.80 C ANISOU 1477 C GLY A 188 8206 6615 7141 -294 -1072 1049 C ATOM 1478 O GLY A 188 -346.769-159.271 146.016 1.00 67.15 O ANISOU 1478 O GLY A 188 9422 7764 8326 -336 -1086 1125 O ATOM 1479 N ILE A 189 -348.497-160.749 146.019 1.00 66.89 N ANISOU 1479 N ILE A 189 9370 7767 8277 -308 -1180 1079 N ATOM 1480 CA ILE A 189 -349.291-160.021 145.044 1.00 61.39 C ANISOU 1480 CA ILE A 189 8716 7025 7584 -369 -1347 1215 C ATOM 1481 C ILE A 189 -349.609-158.647 145.605 1.00 63.86 C ANISOU 1481 C ILE A 189 8926 7228 8108 -311 -1419 1270 C ATOM 1482 O ILE A 189 -349.818-158.472 146.812 1.00 77.34 O ANISOU 1482 O ILE A 189 10513 8897 9975 -218 -1372 1185 O ATOM 1483 CB ILE A 189 -350.591-160.774 144.707 1.00 64.24 C ANISOU 1483 CB ILE A 189 9074 7399 7936 -379 -1461 1225 C ATOM 1484 CG1 ILE A 189 -350.318-162.236 144.353 1.00 80.36 C ANISOU 1484 CG1 ILE A 189 11199 9538 9796 -423 -1371 1139 C ATOM 1485 CG2 ILE A 189 -351.334-160.093 143.562 1.00 62.60 C ANISOU 1485 CG2 ILE A 189 8924 7150 7711 -462 -1655 1385 C ATOM 1486 CD1 ILE A 189 -349.722-162.421 143.004 1.00 85.72 C ANISOU 1486 CD1 ILE A 189 12039 10276 10255 -555 -1362 1190 C ATOM 1487 N ASP A 190 -349.673-157.664 144.716 1.00 63.05 N ANISOU 1487 N ASP A 190 8876 7071 8007 -377 -1536 1413 N ATOM 1488 CA ASP A 190 -349.904-156.276 145.108 1.00 70.09 C ANISOU 1488 CA ASP A 190 9677 7838 9115 -332 -1611 1477 C ATOM 1489 C ASP A 190 -351.402-155.988 145.053 1.00 70.95 C ANISOU 1489 C ASP A 190 9697 7860 9402 -296 -1789 1541 C ATOM 1490 O ASP A 190 -351.943-155.666 143.994 1.00 76.46 O ANISOU 1490 O ASP A 190 10453 8526 10072 -370 -1959 1691 O ATOM 1491 CB ASP A 190 -349.108-155.346 144.203 1.00 66.55 C ANISOU 1491 CB ASP A 190 9331 7365 8592 -426 -1643 1608 C ATOM 1492 CG ASP A 190 -349.394-153.874 144.462 1.00 71.92 C ANISOU 1492 CG ASP A 190 9924 7896 9507 -389 -1742 1694 C ATOM 1493 OD1 ASP A 190 -349.987-153.533 145.506 1.00 73.84 O ANISOU 1493 OD1 ASP A 190 10019 8060 9978 -281 -1740 1617 O ATOM 1494 OD2 ASP A 190 -348.994-153.051 143.617 1.00 68.96 O ANISOU 1494 OD2 ASP A 190 9631 7480 9090 -475 -1813 1836 O ATOM 1495 N TYR A 191 -352.076-156.096 146.202 1.00 71.53 N ANISOU 1495 N TYR A 191 9624 7894 9661 -191 -1753 1428 N ATOM 1496 CA TYR A 191 -353.436-155.590 146.364 1.00 79.35 C ANISOU 1496 CA TYR A 191 10484 8771 10894 -139 -1896 1467 C ATOM 1497 C TYR A 191 -353.463-154.204 146.987 1.00 75.58 C ANISOU 1497 C TYR A 191 9890 8150 10678 -77 -1906 1472 C ATOM 1498 O TYR A 191 -354.532-153.731 147.376 1.00 76.63 O ANISOU 1498 O TYR A 191 9879 8173 11065 -14 -1986 1464 O ATOM 1499 CB TYR A 191 -354.268-156.546 147.225 1.00 77.51 C ANISOU 1499 CB TYR A 191 10153 8576 10722 -74 -1839 1330 C ATOM 1500 CG TYR A 191 -354.056-157.992 146.887 1.00 78.66 C ANISOU 1500 CG TYR A 191 10405 8861 10623 -122 -1781 1284 C ATOM 1501 CD1 TYR A 191 -353.235-158.794 147.668 1.00 68.53 C ANISOU 1501 CD1 TYR A 191 9145 7667 9228 -99 -1599 1151 C ATOM 1502 CD2 TYR A 191 -354.662-158.556 145.773 1.00 87.33 C ANISOU 1502 CD2 TYR A 191 11580 9994 11608 -196 -1916 1376 C ATOM 1503 CE1 TYR A 191 -353.024-160.121 147.347 1.00 80.23 C ANISOU 1503 CE1 TYR A 191 10716 9256 10513 -140 -1546 1108 C ATOM 1504 CE2 TYR A 191 -354.462-159.877 145.446 1.00 91.44 C ANISOU 1504 CE2 TYR A 191 12197 10631 11914 -244 -1855 1321 C ATOM 1505 CZ TYR A 191 -353.644-160.658 146.231 1.00 92.73 C ANISOU 1505 CZ TYR A 191 12375 10869 11991 -211 -1666 1185 C ATOM 1506 OH TYR A 191 -353.455-161.979 145.888 1.00 97.19 O ANISOU 1506 OH TYR A 191 13028 11530 12370 -256 -1607 1130 O ATOM 1507 N TYR A 192 -352.308-153.545 147.102 1.00 77.69 N ANISOU 1507 N TYR A 192 10206 8409 10902 -95 -1821 1476 N ATOM 1508 CA TYR A 192 -352.177-152.358 147.934 1.00 86.32 C ANISOU 1508 CA TYR A 192 11188 9378 12232 -34 -1782 1431 C ATOM 1509 C TYR A 192 -352.043-151.067 147.148 1.00 83.45 C ANISOU 1509 C TYR A 192 10846 8887 11975 -74 -1916 1601 C ATOM 1510 O TYR A 192 -352.299-150.000 147.710 1.00 87.55 O ANISOU 1510 O TYR A 192 11247 9262 12756 -17 -1932 1582 O ATOM 1511 CB TYR A 192 -350.960-152.504 148.859 1.00 82.42 C ANISOU 1511 CB TYR A 192 10713 8957 11645 -20 -1581 1294 C ATOM 1512 CG TYR A 192 -350.857-153.891 149.435 1.00 80.91 C ANISOU 1512 CG TYR A 192 10540 8906 11296 -6 -1463 1165 C ATOM 1513 CD1 TYR A 192 -351.716-154.306 150.443 1.00 81.13 C ANISOU 1513 CD1 TYR A 192 10455 8930 11441 59 -1418 1038 C ATOM 1514 CD2 TYR A 192 -349.919-154.795 148.955 1.00 79.55 C ANISOU 1514 CD2 TYR A 192 10494 8861 10868 -62 -1392 1169 C ATOM 1515 CE1 TYR A 192 -351.639-155.587 150.970 1.00 78.37 C ANISOU 1515 CE1 TYR A 192 10127 8700 10949 64 -1320 936 C ATOM 1516 CE2 TYR A 192 -349.833-156.074 149.472 1.00 84.45 C ANISOU 1516 CE2 TYR A 192 11126 9592 11371 -46 -1295 1061 C ATOM 1517 CZ TYR A 192 -350.696-156.465 150.481 1.00 81.49 C ANISOU 1517 CZ TYR A 192 10646 9210 11106 15 -1267 953 C ATOM 1518 OH TYR A 192 -350.613-157.737 151.002 1.00 80.27 O ANISOU 1518 OH TYR A 192 10507 9157 10835 23 -1179 860 O ATOM 1519 N THR A 193 -351.629-151.133 145.883 1.00 76.97 N ANISOU 1519 N THR A 193 10175 8113 10956 -180 -2006 1759 N ATOM 1520 CA THR A 193 -351.505-149.971 145.028 1.00 79.28 C ANISOU 1520 CA THR A 193 10512 8292 11319 -242 -2151 1948 C ATOM 1521 C THR A 193 -352.173-150.253 143.690 1.00 83.47 C ANISOU 1521 C THR A 193 11140 8841 11734 -338 -2355 2134 C ATOM 1522 O THR A 193 -352.024-151.352 143.141 1.00 81.94 O ANISOU 1522 O THR A 193 11063 8796 11274 -407 -2326 2121 O ATOM 1523 CB THR A 193 -350.029-149.605 144.787 1.00 73.16 C ANISOU 1523 CB THR A 193 9855 7566 10377 -317 -2036 1969 C ATOM 1524 OG1 THR A 193 -349.491-150.450 143.763 1.00 66.32 O ANISOU 1524 OG1 THR A 193 9163 6847 9189 -434 -2021 2029 O ATOM 1525 CG2 THR A 193 -349.216-149.779 146.050 1.00 70.98 C ANISOU 1525 CG2 THR A 193 9517 7336 10117 -246 -1819 1768 C ATOM 1526 N PRO A 194 -352.905-149.283 143.133 1.00 95.19 N ANISOU 1526 N PRO A 194 12579 10172 13416 -352 -2571 2310 N ATOM 1527 CA PRO A 194 -353.436-149.453 141.774 1.00 95.70 C ANISOU 1527 CA PRO A 194 12759 10256 13345 -472 -2792 2517 C ATOM 1528 C PRO A 194 -352.402-149.091 140.718 1.00101.98 C ANISOU 1528 C PRO A 194 13756 11104 13887 -629 -2807 2668 C ATOM 1529 O PRO A 194 -352.345-147.945 140.263 1.00120.99 O ANISOU 1529 O PRO A 194 16175 13381 16415 -674 -2942 2841 O ATOM 1530 CB PRO A 194 -354.629-148.493 141.749 1.00 95.92 C ANISOU 1530 CB PRO A 194 12632 10079 13737 -413 -3022 2643 C ATOM 1531 CG PRO A 194 -354.208-147.376 142.668 1.00 84.73 C ANISOU 1531 CG PRO A 194 11092 8515 12587 -320 -2924 2572 C ATOM 1532 CD PRO A 194 -353.309-147.995 143.728 1.00 88.31 C ANISOU 1532 CD PRO A 194 11546 9094 12914 -264 -2632 2327 C ATOM 1533 N HIS A 195 -351.574-150.055 140.332 1.00 96.13 N ANISOU 1533 N HIS A 195 13170 10547 12809 -717 -2661 2600 N ATOM 1534 CA HIS A 195 -350.494-149.829 139.372 1.00 93.94 C ANISOU 1534 CA HIS A 195 13086 10341 12267 -877 -2624 2707 C ATOM 1535 C HIS A 195 -351.092-149.931 137.976 1.00100.54 C ANISOU 1535 C HIS A 195 14067 11203 12928 -1038 -2851 2918 C ATOM 1536 O HIS A 195 -351.281-151.030 137.452 1.00111.46 O ANISOU 1536 O HIS A 195 15549 12725 14074 -1111 -2839 2879 O ATOM 1537 CB HIS A 195 -349.377-150.848 139.583 1.00 90.14 C ANISOU 1537 CB HIS A 195 12689 10033 11528 -899 -2360 2525 C ATOM 1538 CG HIS A 195 -347.998-150.303 139.362 1.00 91.65 C ANISOU 1538 CG HIS A 195 12972 10248 11603 -980 -2221 2541 C ATOM 1539 ND1 HIS A 195 -347.107-150.865 138.472 1.00 89.92 N ANISOU 1539 ND1 HIS A 195 12931 10170 11063 -1133 -2112 2545 N ATOM 1540 CD2 HIS A 195 -347.352-149.255 139.927 1.00 91.38 C ANISOU 1540 CD2 HIS A 195 12870 10113 11737 -935 -2163 2542 C ATOM 1541 CE1 HIS A 195 -345.976-150.182 138.491 1.00 83.89 C ANISOU 1541 CE1 HIS A 195 12201 9393 10282 -1177 -1994 2555 C ATOM 1542 NE2 HIS A 195 -346.098-149.200 139.367 1.00 85.63 N ANISOU 1542 NE2 HIS A 195 12275 9467 10792 -1059 -2029 2557 N ATOM 1543 N GLU A 196 -351.420-148.782 137.377 1.00 99.40 N ANISOU 1543 N GLU A 196 13937 10921 12909 -1101 -3069 3146 N ATOM 1544 CA GLU A 196 -352.024-148.801 136.049 1.00102.23 C ANISOU 1544 CA GLU A 196 14438 11299 13104 -1270 -3318 3373 C ATOM 1545 C GLU A 196 -351.106-149.472 135.036 1.00100.29 C ANISOU 1545 C GLU A 196 14442 11246 12418 -1473 -3208 3383 C ATOM 1546 O GLU A 196 -351.579-150.034 134.042 1.00104.75 O ANISOU 1546 O GLU A 196 15146 11900 12756 -1619 -3344 3481 O ATOM 1547 CB GLU A 196 -352.370-147.378 135.596 1.00107.83 C ANISOU 1547 CB GLU A 196 15127 11817 14027 -1312 -3568 3634 C ATOM 1548 CG GLU A 196 -353.358-146.639 136.497 1.00118.11 C ANISOU 1548 CG GLU A 196 16171 12903 15802 -1121 -3692 3631 C ATOM 1549 CD GLU A 196 -353.798-145.299 135.915 1.00140.40 C ANISOU 1549 CD GLU A 196 18974 15520 18852 -1172 -3975 3913 C ATOM 1550 OE1 GLU A 196 -353.744-145.135 134.678 1.00145.38 O ANISOU 1550 OE1 GLU A 196 19792 16187 19259 -1368 -4157 4148 O ATOM 1551 OE2 GLU A 196 -354.197-144.406 136.695 1.00149.05 O ANISOU 1551 OE2 GLU A 196 19867 16412 20352 -1023 -4016 3899 O ATOM 1552 N GLU A 197 -349.796-149.442 135.284 1.00 96.10 N ANISOU 1552 N GLU A 197 13966 10781 11765 -1490 -2955 3270 N ATOM 1553 CA GLU A 197 -348.848-149.996 134.328 1.00101.24 C ANISOU 1553 CA GLU A 197 14841 11602 12022 -1688 -2822 3265 C ATOM 1554 C GLU A 197 -348.915-151.514 134.292 1.00102.03 C ANISOU 1554 C GLU A 197 14987 11868 11911 -1692 -2687 3078 C ATOM 1555 O GLU A 197 -348.632-152.120 133.252 1.00109.46 O ANISOU 1555 O GLU A 197 16123 12945 12521 -1881 -2660 3101 O ATOM 1556 CB GLU A 197 -347.438-149.525 134.674 1.00103.95 C ANISOU 1556 CB GLU A 197 15199 11955 12342 -1691 -2585 3187 C ATOM 1557 CG GLU A 197 -347.382-148.076 135.114 1.00115.74 C ANISOU 1557 CG GLU A 197 16588 13259 14127 -1624 -2678 3309 C ATOM 1558 CD GLU A 197 -346.000-147.665 135.567 1.00131.67 C ANISOU 1558 CD GLU A 197 18600 15288 16140 -1617 -2437 3209 C ATOM 1559 OE1 GLU A 197 -345.012-148.166 134.988 1.00139.31 O ANISOU 1559 OE1 GLU A 197 19713 16400 16819 -1754 -2260 3156 O ATOM 1560 OE2 GLU A 197 -345.901-146.849 136.508 1.00133.23 O ANISOU 1560 OE2 GLU A 197 18643 15350 16630 -1479 -2420 3174 O ATOM 1561 N THR A 198 -349.290-152.143 135.408 1.00 95.54 N ANISOU 1561 N THR A 198 13993 11037 11272 -1498 -2599 2889 N ATOM 1562 CA THR A 198 -349.444-153.592 135.482 1.00 93.54 C ANISOU 1562 CA THR A 198 13761 10917 10863 -1484 -2483 2712 C ATOM 1563 C THR A 198 -350.901-154.036 135.613 1.00 94.87 C ANISOU 1563 C THR A 198 13837 11048 11160 -1416 -2680 2734 C ATOM 1564 O THR A 198 -351.146-155.217 135.873 1.00 92.72 O ANISOU 1564 O THR A 198 13548 10865 10817 -1374 -2590 2578 O ATOM 1565 CB THR A 198 -348.623-154.167 136.648 1.00 86.18 C ANISOU 1565 CB THR A 198 12719 10024 10002 -1336 -2205 2467 C ATOM 1566 OG1 THR A 198 -348.974-153.515 137.874 1.00 92.49 O ANISOU 1566 OG1 THR A 198 13314 10692 11137 -1147 -2225 2430 O ATOM 1567 CG2 THR A 198 -347.132-154.004 136.402 1.00 72.21 C ANISOU 1567 CG2 THR A 198 11047 8319 8070 -1422 -1991 2421 C ATOM 1568 N ASN A 199 -351.866-153.131 135.433 1.00 96.34 N ANISOU 1568 N ASN A 199 13957 11100 11549 -1404 -2947 2925 N ATOM 1569 CA ASN A 199 -353.297-153.450 135.505 1.00 96.45 C ANISOU 1569 CA ASN A 199 13864 11063 11718 -1345 -3155 2964 C ATOM 1570 C ASN A 199 -353.639-154.239 136.771 1.00 92.42 C ANISOU 1570 C ASN A 199 13176 10559 11382 -1152 -3005 2733 C ATOM 1571 O ASN A 199 -354.205-155.333 136.727 1.00 91.03 O ANISOU 1571 O ASN A 199 13002 10465 11119 -1153 -3003 2644 O ATOM 1572 CB ASN A 199 -353.751-154.209 134.256 1.00 94.46 C ANISOU 1572 CB ASN A 199 13794 10928 11169 -1536 -3295 3054 C ATOM 1573 CG ASN A 199 -353.631-153.378 133.000 1.00 93.75 C ANISOU 1573 CG ASN A 199 13880 10824 10917 -1744 -3493 3314 C ATOM 1574 OD1 ASN A 199 -354.525-152.602 132.667 1.00 99.02 O ANISOU 1574 OD1 ASN A 199 14496 11367 11759 -1760 -3783 3526 O ATOM 1575 ND2 ASN A 199 -352.518-153.533 132.295 1.00 90.80 N ANISOU 1575 ND2 ASN A 199 13711 10571 10217 -1911 -3339 3302 N ATOM 1576 N ASN A 200 -353.287-153.647 137.914 1.00 91.45 N ANISOU 1576 N ASN A 200 12900 10346 11502 -997 -2880 2638 N ATOM 1577 CA ASN A 200 -353.509-154.311 139.195 1.00 86.09 C ANISOU 1577 CA ASN A 200 12061 9675 10975 -829 -2723 2421 C ATOM 1578 C ASN A 200 -354.992-154.560 139.450 1.00 90.57 C ANISOU 1578 C ASN A 200 12485 10176 11751 -754 -2890 2430 C ATOM 1579 O ASN A 200 -355.367-155.608 139.991 1.00 95.48 O ANISOU 1579 O ASN A 200 13053 10867 12360 -692 -2799 2277 O ATOM 1580 CB ASN A 200 -352.897-153.481 140.328 1.00 79.29 C ANISOU 1580 CB ASN A 200 11072 8721 10332 -701 -2583 2334 C ATOM 1581 CG ASN A 200 -351.384-153.612 140.389 1.00 80.02 C ANISOU 1581 CG ASN A 200 11271 8907 10227 -744 -2357 2251 C ATOM 1582 OD1 ASN A 200 -350.752-154.044 139.426 1.00 84.45 O ANISOU 1582 OD1 ASN A 200 12007 9576 10504 -885 -2321 2292 O ATOM 1583 ND2 ASN A 200 -350.794-153.245 141.526 1.00 73.00 N ANISOU 1583 ND2 ASN A 200 10272 7976 9488 -631 -2200 2125 N ATOM 1584 N GLU A 201 -355.852-153.625 139.044 1.00 87.85 N ANISOU 1584 N GLU A 201 12074 9695 11611 -762 -3140 2614 N ATOM 1585 CA GLU A 201 -357.272-153.734 139.367 1.00 89.31 C ANISOU 1585 CA GLU A 201 12084 9792 12056 -677 -3297 2619 C ATOM 1586 C GLU A 201 -357.890-154.973 138.731 1.00 86.70 C ANISOU 1586 C GLU A 201 11834 9586 11521 -762 -3369 2609 C ATOM 1587 O GLU A 201 -358.623-155.721 139.388 1.00 86.41 O ANISOU 1587 O GLU A 201 11676 9564 11593 -674 -3327 2477 O ATOM 1588 CB GLU A 201 -358.008-152.472 138.926 1.00100.84 C ANISOU 1588 CB GLU A 201 13460 11069 13785 -682 -3571 2840 C ATOM 1589 CG GLU A 201 -359.479-152.452 139.289 1.00112.03 C ANISOU 1589 CG GLU A 201 14662 12370 15533 -584 -3736 2846 C ATOM 1590 CD GLU A 201 -360.106-151.093 139.063 1.00123.68 C ANISOU 1590 CD GLU A 201 16012 13628 17352 -556 -3979 3042 C ATOM 1591 OE1 GLU A 201 -359.352-150.114 138.864 1.00128.68 O ANISOU 1591 OE1 GLU A 201 16707 14190 17995 -587 -3983 3143 O ATOM 1592 OE2 GLU A 201 -361.350-151.002 139.086 1.00128.88 O ANISOU 1592 OE2 GLU A 201 16502 14179 18287 -503 -4168 3095 O ATOM 1593 N SER A 202 -357.597-155.212 137.452 1.00 81.89 N ANISOU 1593 N SER A 202 11438 9071 10606 -945 -3471 2742 N ATOM 1594 CA SER A 202 -358.170-156.368 136.774 1.00 82.11 C ANISOU 1594 CA SER A 202 11558 9217 10424 -1046 -3546 2730 C ATOM 1595 C SER A 202 -357.628-157.679 137.338 1.00 84.51 C ANISOU 1595 C SER A 202 11897 9659 10556 -1008 -3272 2487 C ATOM 1596 O SER A 202 -358.336-158.692 137.334 1.00 88.18 O ANISOU 1596 O SER A 202 12341 10182 10983 -1011 -3295 2411 O ATOM 1597 CB SER A 202 -357.912-156.279 135.270 1.00 84.07 C ANISOU 1597 CB SER A 202 12043 9538 10360 -1274 -3704 2919 C ATOM 1598 OG SER A 202 -356.523-156.247 134.990 1.00 91.84 O ANISOU 1598 OG SER A 202 13198 10613 11083 -1358 -3501 2877 O ATOM 1599 N PHE A 203 -356.393-157.682 137.842 1.00 83.07 N ANISOU 1599 N PHE A 203 11756 9521 10286 -971 -3022 2367 N ATOM 1600 CA PHE A 203 -355.850-158.905 138.425 1.00 77.28 C ANISOU 1600 CA PHE A 203 11041 8899 9422 -927 -2774 2148 C ATOM 1601 C PHE A 203 -356.494-159.209 139.772 1.00 76.87 C ANISOU 1601 C PHE A 203 10780 8793 9635 -750 -2702 2005 C ATOM 1602 O PHE A 203 -356.790-160.370 140.073 1.00 80.98 O ANISOU 1602 O PHE A 203 11287 9385 10097 -729 -2622 1875 O ATOM 1603 CB PHE A 203 -354.332-158.796 138.568 1.00 74.34 C ANISOU 1603 CB PHE A 203 10761 8583 8903 -942 -2543 2072 C ATOM 1604 CG PHE A 203 -353.665-160.097 138.907 1.00 71.16 C ANISOU 1604 CG PHE A 203 10404 8296 8338 -929 -2311 1874 C ATOM 1605 CD1 PHE A 203 -353.406-161.033 137.918 1.00 71.45 C ANISOU 1605 CD1 PHE A 203 10613 8448 8086 -1074 -2277 1848 C ATOM 1606 CD2 PHE A 203 -353.299-160.387 140.213 1.00 72.97 C ANISOU 1606 CD2 PHE A 203 10505 8511 8707 -780 -2130 1714 C ATOM 1607 CE1 PHE A 203 -352.793-162.235 138.223 1.00 70.65 C ANISOU 1607 CE1 PHE A 203 10541 8432 7869 -1056 -2064 1664 C ATOM 1608 CE2 PHE A 203 -352.680-161.589 140.525 1.00 71.29 C ANISOU 1608 CE2 PHE A 203 10329 8391 8369 -767 -1935 1549 C ATOM 1609 CZ PHE A 203 -352.429-162.514 139.527 1.00 71.23 C ANISOU 1609 CZ PHE A 203 10479 8482 8103 -899 -1901 1523 C ATOM 1610 N VAL A 204 -356.717-158.182 140.595 1.00 78.09 N ANISOU 1610 N VAL A 204 10771 8819 10079 -631 -2721 2020 N ATOM 1611 CA VAL A 204 -357.405-158.380 141.870 1.00 80.49 C ANISOU 1611 CA VAL A 204 10877 9069 10638 -481 -2651 1883 C ATOM 1612 C VAL A 204 -358.797-158.965 141.644 1.00 84.50 C ANISOU 1612 C VAL A 204 11307 9565 11234 -487 -2813 1905 C ATOM 1613 O VAL A 204 -359.237-159.863 142.373 1.00 77.42 O ANISOU 1613 O VAL A 204 10331 8707 10380 -425 -2715 1762 O ATOM 1614 CB VAL A 204 -357.467-157.052 142.650 1.00 75.40 C ANISOU 1614 CB VAL A 204 10077 8275 10296 -375 -2658 1902 C ATOM 1615 CG1 VAL A 204 -358.302-157.212 143.906 1.00 70.70 C ANISOU 1615 CG1 VAL A 204 9276 7622 9964 -242 -2589 1758 C ATOM 1616 CG2 VAL A 204 -356.061-156.571 142.993 1.00 71.89 C ANISOU 1616 CG2 VAL A 204 9702 7851 9764 -368 -2481 1857 C ATOM 1617 N ILE A 205 -359.508-158.468 140.630 1.00 82.25 N ANISOU 1617 N ILE A 205 11044 9226 10982 -569 -3070 2093 N ATOM 1618 CA ILE A 205 -360.829-158.999 140.309 1.00 79.79 C ANISOU 1618 CA ILE A 205 10659 8903 10755 -589 -3251 2132 C ATOM 1619 C ILE A 205 -360.719-160.446 139.844 1.00 84.82 C ANISOU 1619 C ILE A 205 11439 9695 11094 -683 -3185 2047 C ATOM 1620 O ILE A 205 -361.480-161.318 140.280 1.00 84.76 O ANISOU 1620 O ILE A 205 11344 9711 11151 -643 -3165 1945 O ATOM 1621 CB ILE A 205 -361.509-158.113 139.251 1.00 74.21 C ANISOU 1621 CB ILE A 205 9958 8103 10134 -674 -3566 2376 C ATOM 1622 CG1 ILE A 205 -361.629-156.680 139.769 1.00 74.61 C ANISOU 1622 CG1 ILE A 205 9849 7976 10524 -569 -3624 2449 C ATOM 1623 CG2 ILE A 205 -362.874-158.684 138.840 1.00 73.17 C ANISOU 1623 CG2 ILE A 205 9750 7963 10087 -709 -3778 2427 C ATOM 1624 CD1 ILE A 205 -362.141-155.708 138.737 1.00 76.19 C ANISOU 1624 CD1 ILE A 205 10062 8067 10820 -652 -3939 2711 C ATOM 1625 N TYR A 206 -359.769-160.718 138.948 1.00 79.96 N ANISOU 1625 N TYR A 206 11045 9184 10154 -816 -3142 2083 N ATOM 1626 CA TYR A 206 -359.542-162.085 138.500 1.00 75.28 C ANISOU 1626 CA TYR A 206 10594 8731 9279 -909 -3051 1981 C ATOM 1627 C TYR A 206 -359.180-162.993 139.668 1.00 77.38 C ANISOU 1627 C TYR A 206 10788 9037 9577 -792 -2794 1762 C ATOM 1628 O TYR A 206 -359.672-164.123 139.762 1.00 82.22 O ANISOU 1628 O TYR A 206 11395 9704 10140 -802 -2765 1665 O ATOM 1629 CB TYR A 206 -358.449-162.104 137.433 1.00 71.54 C ANISOU 1629 CB TYR A 206 10359 8351 8473 -1067 -3004 2032 C ATOM 1630 CG TYR A 206 -357.753-163.434 137.290 1.00 77.83 C ANISOU 1630 CG TYR A 206 11284 9276 9010 -1125 -2797 1864 C ATOM 1631 CD1 TYR A 206 -358.334-164.474 136.575 1.00 79.23 C ANISOU 1631 CD1 TYR A 206 11553 9532 9021 -1238 -2868 1838 C ATOM 1632 CD2 TYR A 206 -356.509-163.648 137.865 1.00 78.68 C ANISOU 1632 CD2 TYR A 206 11419 9421 9056 -1068 -2535 1730 C ATOM 1633 CE1 TYR A 206 -357.693-165.693 136.442 1.00 80.49 C ANISOU 1633 CE1 TYR A 206 11823 9792 8967 -1288 -2672 1673 C ATOM 1634 CE2 TYR A 206 -355.862-164.860 137.738 1.00 79.74 C ANISOU 1634 CE2 TYR A 206 11654 9653 8990 -1113 -2348 1576 C ATOM 1635 CZ TYR A 206 -356.456-165.879 137.027 1.00 83.67 C ANISOU 1635 CZ TYR A 206 12239 10217 9334 -1221 -2411 1544 C ATOM 1636 OH TYR A 206 -355.802-167.084 136.905 1.00 84.21 O ANISOU 1636 OH TYR A 206 12401 10367 9230 -1263 -2216 1380 O ATOM 1637 N MET A 207 -358.323-162.515 140.573 1.00 77.31 N ANISOU 1637 N MET A 207 10725 8999 9650 -690 -2616 1688 N ATOM 1638 CA MET A 207 -357.999-163.293 141.766 1.00 75.85 C ANISOU 1638 CA MET A 207 10466 8844 9511 -583 -2395 1501 C ATOM 1639 C MET A 207 -359.237-163.529 142.613 1.00 74.92 C ANISOU 1639 C MET A 207 10161 8669 9636 -490 -2441 1445 C ATOM 1640 O MET A 207 -359.452-164.630 143.135 1.00 80.50 O ANISOU 1640 O MET A 207 10844 9426 10315 -465 -2339 1320 O ATOM 1641 CB MET A 207 -356.930-162.580 142.593 1.00 61.47 C ANISOU 1641 CB MET A 207 8610 6993 7753 -500 -2231 1452 C ATOM 1642 CG MET A 207 -355.524-162.803 142.099 1.00 73.17 C ANISOU 1642 CG MET A 207 10256 8555 8991 -571 -2091 1429 C ATOM 1643 SD MET A 207 -355.048-164.539 142.142 1.00 78.97 S ANISOU 1643 SD MET A 207 11076 9404 9524 -600 -1915 1265 S ATOM 1644 CE MET A 207 -355.209-164.910 143.895 1.00 67.82 C ANISOU 1644 CE MET A 207 9488 7959 8320 -440 -1778 1122 C ATOM 1645 N PHE A 208 -360.053-162.493 142.780 1.00 71.02 N ANISOU 1645 N PHE A 208 9526 8061 9397 -438 -2587 1534 N ATOM 1646 CA PHE A 208 -361.196-162.609 143.671 1.00 74.38 C ANISOU 1646 CA PHE A 208 9753 8423 10086 -345 -2602 1464 C ATOM 1647 C PHE A 208 -362.218-163.587 143.115 1.00 80.01 C ANISOU 1647 C PHE A 208 10467 9177 10756 -411 -2726 1473 C ATOM 1648 O PHE A 208 -362.821-164.362 143.865 1.00 79.20 O ANISOU 1648 O PHE A 208 10266 9087 10739 -363 -2648 1355 O ATOM 1649 CB PHE A 208 -361.817-161.238 143.888 1.00 73.36 C ANISOU 1649 CB PHE A 208 9462 8147 10265 -278 -2730 1553 C ATOM 1650 CG PHE A 208 -362.987-161.249 144.815 1.00 75.64 C ANISOU 1650 CG PHE A 208 9528 8358 10853 -186 -2727 1467 C ATOM 1651 CD1 PHE A 208 -362.800-161.280 146.188 1.00 76.76 C ANISOU 1651 CD1 PHE A 208 9567 8492 11108 -90 -2511 1300 C ATOM 1652 CD2 PHE A 208 -364.273-161.216 144.316 1.00 73.64 C ANISOU 1652 CD2 PHE A 208 9166 8041 10771 -204 -2939 1552 C ATOM 1653 CE1 PHE A 208 -363.881-161.283 147.045 1.00 75.74 C ANISOU 1653 CE1 PHE A 208 9235 8296 11247 -21 -2487 1209 C ATOM 1654 CE2 PHE A 208 -365.357-161.218 145.166 1.00 82.18 C ANISOU 1654 CE2 PHE A 208 10029 9049 12148 -122 -2922 1463 C ATOM 1655 CZ PHE A 208 -365.162-161.253 146.532 1.00 77.18 C ANISOU 1655 CZ PHE A 208 9299 8411 11616 -33 -2684 1284 C ATOM 1656 N VAL A 209 -362.402-163.583 141.800 1.00 77.88 N ANISOU 1656 N VAL A 209 10318 8932 10340 -534 -2919 1613 N ATOM 1657 CA VAL A 209 -363.408-164.437 141.186 1.00 76.00 C ANISOU 1657 CA VAL A 209 10085 8730 10062 -612 -3065 1634 C ATOM 1658 C VAL A 209 -362.888-165.860 141.030 1.00 85.32 C ANISOU 1658 C VAL A 209 11413 10038 10967 -678 -2915 1509 C ATOM 1659 O VAL A 209 -363.456-166.813 141.575 1.00 80.10 O ANISOU 1659 O VAL A 209 10681 9398 10356 -648 -2851 1396 O ATOM 1660 CB VAL A 209 -363.848-163.853 139.834 1.00 74.43 C ANISOU 1660 CB VAL A 209 9963 8509 9809 -736 -3351 1843 C ATOM 1661 CG1 VAL A 209 -364.821-164.795 139.170 1.00 70.22 C ANISOU 1661 CG1 VAL A 209 9450 8024 9206 -834 -3505 1859 C ATOM 1662 CG2 VAL A 209 -364.464-162.467 140.020 1.00 74.97 C ANISOU 1662 CG2 VAL A 209 9858 8423 10204 -660 -3518 1973 C ATOM 1663 N VAL A 210 -361.788-166.019 140.294 1.00 85.65 N ANISOU 1663 N VAL A 210 11657 10158 10728 -771 -2848 1522 N ATOM 1664 CA VAL A 210 -361.338-167.347 139.896 1.00 77.73 C ANISOU 1664 CA VAL A 210 10804 9263 9466 -856 -2732 1414 C ATOM 1665 C VAL A 210 -360.686-168.090 141.056 1.00 78.56 C ANISOU 1665 C VAL A 210 10866 9389 9594 -751 -2471 1237 C ATOM 1666 O VAL A 210 -360.917-169.290 141.245 1.00 80.54 O ANISOU 1666 O VAL A 210 11127 9682 9792 -763 -2398 1127 O ATOM 1667 CB VAL A 210 -360.391-167.235 138.691 1.00 77.31 C ANISOU 1667 CB VAL A 210 10975 9282 9117 -1002 -2736 1476 C ATOM 1668 CG1 VAL A 210 -359.599-168.516 138.520 1.00 85.19 C ANISOU 1668 CG1 VAL A 210 12109 10375 9885 -1058 -2536 1321 C ATOM 1669 CG2 VAL A 210 -361.186-166.944 137.436 1.00 68.39 C ANISOU 1669 CG2 VAL A 210 9922 8160 7901 -1150 -3010 1639 C ATOM 1670 N HIS A 211 -359.856-167.410 141.844 1.00 70.86 N ANISOU 1670 N HIS A 211 9845 8382 8695 -655 -2336 1211 N ATOM 1671 CA HIS A 211 -359.081-168.079 142.880 1.00 64.46 C ANISOU 1671 CA HIS A 211 9015 7597 7879 -574 -2104 1064 C ATOM 1672 C HIS A 211 -359.636-167.836 144.279 1.00 65.55 C ANISOU 1672 C HIS A 211 8962 7674 8268 -445 -2050 1004 C ATOM 1673 O HIS A 211 -358.954-168.118 145.270 1.00 69.25 O ANISOU 1673 O HIS A 211 9406 8155 8752 -376 -1874 906 O ATOM 1674 CB HIS A 211 -357.614-167.640 142.811 1.00 63.73 C ANISOU 1674 CB HIS A 211 9019 7529 7667 -574 -1968 1057 C ATOM 1675 CG HIS A 211 -356.957-167.940 141.500 1.00 68.04 C ANISOU 1675 CG HIS A 211 9756 8143 7953 -712 -1973 1087 C ATOM 1676 ND1 HIS A 211 -356.199-169.069 141.287 1.00 69.72 N ANISOU 1676 ND1 HIS A 211 10073 8420 7996 -756 -1818 972 N ATOM 1677 CD2 HIS A 211 -356.951-167.258 140.329 1.00 71.18 C ANISOU 1677 CD2 HIS A 211 10261 8551 8231 -826 -2111 1217 C ATOM 1678 CE1 HIS A 211 -355.750-169.070 140.044 1.00 67.96 C ANISOU 1678 CE1 HIS A 211 10013 8251 7557 -894 -1841 1011 C ATOM 1679 NE2 HIS A 211 -356.195-167.984 139.440 1.00 63.24 N ANISOU 1679 NE2 HIS A 211 9430 7628 6970 -946 -2022 1165 N ATOM 1680 N PHE A 212 -360.856-167.332 144.392 1.00 67.36 N ANISOU 1680 N PHE A 212 9056 7838 8699 -420 -2196 1059 N ATOM 1681 CA PHE A 212 -361.391-167.092 145.725 1.00 72.59 C ANISOU 1681 CA PHE A 212 9538 8444 9599 -311 -2120 983 C ATOM 1682 C PHE A 212 -362.875-167.438 145.796 1.00 80.47 C ANISOU 1682 C PHE A 212 10404 9408 10762 -313 -2236 979 C ATOM 1683 O PHE A 212 -363.286-168.196 146.680 1.00 80.52 O ANISOU 1683 O PHE A 212 10334 9428 10832 -280 -2130 870 O ATOM 1684 CB PHE A 212 -361.129-165.644 146.149 1.00 74.79 C ANISOU 1684 CB PHE A 212 9733 8642 10041 -242 -2125 1030 C ATOM 1685 CG PHE A 212 -361.489-165.356 147.577 1.00 74.46 C ANISOU 1685 CG PHE A 212 9524 8550 10216 -144 -2007 925 C ATOM 1686 CD1 PHE A 212 -360.721-165.859 148.610 1.00 70.80 C ANISOU 1686 CD1 PHE A 212 9081 8137 9683 -108 -1806 807 C ATOM 1687 CD2 PHE A 212 -362.600-164.585 147.887 1.00 79.90 C ANISOU 1687 CD2 PHE A 212 10034 9141 11183 -96 -2098 942 C ATOM 1688 CE1 PHE A 212 -361.052-165.603 149.931 1.00 67.58 C ANISOU 1688 CE1 PHE A 212 8537 7695 9445 -42 -1693 706 C ATOM 1689 CE2 PHE A 212 -362.939-164.322 149.204 1.00 73.02 C ANISOU 1689 CE2 PHE A 212 9014 8228 10504 -22 -1966 824 C ATOM 1690 CZ PHE A 212 -362.160-164.835 150.229 1.00 69.73 C ANISOU 1690 CZ PHE A 212 8638 7876 9980 -3 -1761 706 C ATOM 1691 N ILE A 213 -363.684-166.915 144.868 1.00 77.70 N ANISOU 1691 N ILE A 213 10026 9012 10484 -360 -2458 1104 N ATOM 1692 CA ILE A 213 -365.106-167.261 144.850 1.00 77.57 C ANISOU 1692 CA ILE A 213 9874 8961 10639 -369 -2585 1108 C ATOM 1693 C ILE A 213 -365.306-168.686 144.345 1.00 76.74 C ANISOU 1693 C ILE A 213 9874 8943 10342 -459 -2588 1061 C ATOM 1694 O ILE A 213 -365.986-169.496 144.987 1.00 79.11 O ANISOU 1694 O ILE A 213 10085 9249 10725 -442 -2526 966 O ATOM 1695 CB ILE A 213 -365.911-166.261 144.001 1.00 82.78 C ANISOU 1695 CB ILE A 213 10462 9535 11456 -395 -2847 1271 C ATOM 1696 CG1 ILE A 213 -365.848-164.846 144.580 1.00 84.31 C ANISOU 1696 CG1 ILE A 213 10522 9616 11897 -296 -2843 1305 C ATOM 1697 CG2 ILE A 213 -367.363-166.724 143.895 1.00 66.35 C ANISOU 1697 CG2 ILE A 213 8240 7423 9549 -415 -2991 1276 C ATOM 1698 CD1 ILE A 213 -366.403-164.727 145.978 1.00 83.97 C ANISOU 1698 CD1 ILE A 213 10272 9513 12119 -187 -2695 1166 C ATOM 1699 N ILE A 214 -364.743-169.002 143.171 1.00 81.48 N ANISOU 1699 N ILE A 214 10667 9607 10684 -568 -2657 1123 N ATOM 1700 CA ILE A 214 -364.926-170.334 142.578 1.00 78.69 C ANISOU 1700 CA ILE A 214 10424 9330 10144 -669 -2665 1072 C ATOM 1701 C ILE A 214 -364.493-171.460 143.518 1.00 81.86 C ANISOU 1701 C ILE A 214 10833 9770 10499 -624 -2435 911 C ATOM 1702 O ILE A 214 -365.249-172.431 143.668 1.00 75.77 O ANISOU 1702 O ILE A 214 10021 9011 9757 -650 -2440 849 O ATOM 1703 CB ILE A 214 -364.218-170.414 141.221 1.00 76.59 C ANISOU 1703 CB ILE A 214 10378 9130 9591 -801 -2735 1142 C ATOM 1704 CG1 ILE A 214 -364.823-169.425 140.228 1.00 72.74 C ANISOU 1704 CG1 ILE A 214 9891 8606 9141 -873 -3004 1323 C ATOM 1705 CG2 ILE A 214 -364.260-171.843 140.668 1.00 69.98 C ANISOU 1705 CG2 ILE A 214 9667 8370 8553 -907 -2702 1054 C ATOM 1706 CD1 ILE A 214 -366.266-169.649 139.994 1.00 87.82 C ANISOU 1706 CD1 ILE A 214 11681 10482 11204 -907 -3209 1372 C ATOM 1707 N PRO A 215 -363.308-171.417 144.146 1.00 80.07 N ANISOU 1707 N PRO A 215 10658 9560 10203 -565 -2241 848 N ATOM 1708 CA PRO A 215 -362.949-172.527 145.044 1.00 75.30 C ANISOU 1708 CA PRO A 215 10056 8984 9570 -529 -2050 716 C ATOM 1709 C PRO A 215 -363.975-172.763 146.137 1.00 74.70 C ANISOU 1709 C PRO A 215 9806 8871 9706 -471 -2023 659 C ATOM 1710 O PRO A 215 -364.248-173.918 146.483 1.00 74.95 O ANISOU 1710 O PRO A 215 9840 8923 9714 -492 -1954 579 O ATOM 1711 CB PRO A 215 -361.592-172.092 145.611 1.00 65.86 C ANISOU 1711 CB PRO A 215 8906 7795 8321 -466 -1889 689 C ATOM 1712 CG PRO A 215 -361.030-171.203 144.568 1.00 67.94 C ANISOU 1712 CG PRO A 215 9269 8066 8479 -513 -1977 789 C ATOM 1713 CD PRO A 215 -362.210-170.438 144.045 1.00 73.17 C ANISOU 1713 CD PRO A 215 9847 8682 9271 -538 -2194 898 C ATOM 1714 N LEU A 216 -364.564-171.701 146.687 1.00 73.84 N ANISOU 1714 N LEU A 216 9542 8701 9812 -404 -2068 693 N ATOM 1715 CA LEU A 216 -365.567-171.891 147.728 1.00 74.69 C ANISOU 1715 CA LEU A 216 9477 8775 10127 -360 -2022 624 C ATOM 1716 C LEU A 216 -366.810-172.572 147.174 1.00 79.07 C ANISOU 1716 C LEU A 216 9978 9326 10740 -427 -2160 636 C ATOM 1717 O LEU A 216 -367.380-173.458 147.822 1.00 77.13 O ANISOU 1717 O LEU A 216 9671 9090 10547 -435 -2084 553 O ATOM 1718 CB LEU A 216 -365.938-170.552 148.357 1.00 77.94 C ANISOU 1718 CB LEU A 216 9727 9112 10776 -281 -2033 643 C ATOM 1719 CG LEU A 216 -366.964-170.634 149.488 1.00 80.18 C ANISOU 1719 CG LEU A 216 9821 9358 11288 -242 -1957 552 C ATOM 1720 CD1 LEU A 216 -366.296-171.078 150.768 1.00 82.89 C ANISOU 1720 CD1 LEU A 216 10186 9741 11569 -213 -1730 442 C ATOM 1721 CD2 LEU A 216 -367.622-169.296 149.686 1.00 83.53 C ANISOU 1721 CD2 LEU A 216 10069 9686 11983 -182 -2028 583 C ATOM 1722 N ILE A 217 -367.246-172.169 145.978 1.00 78.14 N ANISOU 1722 N ILE A 217 9885 9195 10611 -485 -2371 745 N ATOM 1723 CA ILE A 217 -368.448-172.748 145.386 1.00 71.71 C ANISOU 1723 CA ILE A 217 9015 8376 9856 -558 -2531 768 C ATOM 1724 C ILE A 217 -368.242-174.234 145.115 1.00 75.67 C ANISOU 1724 C ILE A 217 9650 8945 10154 -639 -2465 691 C ATOM 1725 O ILE A 217 -369.099-175.069 145.428 1.00 72.15 O ANISOU 1725 O ILE A 217 9128 8498 9789 -664 -2460 632 O ATOM 1726 CB ILE A 217 -368.833-171.986 144.104 1.00 75.65 C ANISOU 1726 CB ILE A 217 9538 8852 10355 -621 -2791 919 C ATOM 1727 CG1 ILE A 217 -368.988-170.494 144.394 1.00 81.24 C ANISOU 1727 CG1 ILE A 217 10107 9470 11291 -534 -2856 998 C ATOM 1728 CG2 ILE A 217 -370.128-172.523 143.530 1.00 69.18 C ANISOU 1728 CG2 ILE A 217 8642 8023 9619 -700 -2979 950 C ATOM 1729 CD1 ILE A 217 -369.969-170.199 145.495 1.00 84.16 C ANISOU 1729 CD1 ILE A 217 10228 9763 11987 -446 -2804 930 C ATOM 1730 N VAL A 218 -367.089-174.586 144.543 1.00 71.13 N ANISOU 1730 N VAL A 218 9273 8425 9327 -681 -2402 685 N ATOM 1731 CA VAL A 218 -366.834-175.979 144.193 1.00 71.74 C ANISOU 1731 CA VAL A 218 9482 8553 9224 -760 -2337 605 C ATOM 1732 C VAL A 218 -366.745-176.839 145.443 1.00 70.10 C ANISOU 1732 C VAL A 218 9217 8338 9079 -703 -2143 491 C ATOM 1733 O VAL A 218 -367.290-177.948 145.492 1.00 73.82 O ANISOU 1733 O VAL A 218 9686 8815 9547 -754 -2130 430 O ATOM 1734 CB VAL A 218 -365.559-176.089 143.338 1.00 72.16 C ANISOU 1734 CB VAL A 218 9744 8656 9018 -815 -2289 608 C ATOM 1735 CG1 VAL A 218 -365.229-177.548 143.076 1.00 66.39 C ANISOU 1735 CG1 VAL A 218 9135 7958 8131 -885 -2191 501 C ATOM 1736 CG2 VAL A 218 -365.752-175.340 142.032 1.00 69.05 C ANISOU 1736 CG2 VAL A 218 9425 8278 8532 -906 -2495 729 C ATOM 1737 N ILE A 219 -366.066-176.344 146.475 1.00 63.67 N ANISOU 1737 N ILE A 219 8360 7510 8321 -607 -1996 467 N ATOM 1738 CA ILE A 219 -365.941-177.127 147.698 1.00 70.17 C ANISOU 1738 CA ILE A 219 9142 8330 9189 -567 -1823 377 C ATOM 1739 C ILE A 219 -367.306-177.327 148.346 1.00 75.51 C ANISOU 1739 C ILE A 219 9650 8979 10062 -570 -1849 349 C ATOM 1740 O ILE A 219 -367.618-178.415 148.845 1.00 76.94 O ANISOU 1740 O ILE A 219 9823 9163 10245 -601 -1773 284 O ATOM 1741 CB ILE A 219 -364.938-176.463 148.655 1.00 66.87 C ANISOU 1741 CB ILE A 219 8717 7910 8780 -479 -1679 365 C ATOM 1742 CG1 ILE A 219 -363.512-176.815 148.219 1.00 78.21 C ANISOU 1742 CG1 ILE A 219 10320 9375 10021 -486 -1601 356 C ATOM 1743 CG2 ILE A 219 -365.191-176.911 150.077 1.00 64.17 C ANISOU 1743 CG2 ILE A 219 8284 7560 8538 -446 -1541 296 C ATOM 1744 CD1 ILE A 219 -362.428-176.143 149.030 1.00 81.41 C ANISOU 1744 CD1 ILE A 219 10726 9779 10425 -409 -1481 355 C ATOM 1745 N PHE A 220 -368.151-176.295 148.323 1.00 72.46 N ANISOU 1745 N PHE A 220 9120 8556 9856 -542 -1957 398 N ATOM 1746 CA PHE A 220 -369.464-176.411 148.950 1.00 74.55 C ANISOU 1746 CA PHE A 220 9200 8787 10337 -544 -1969 361 C ATOM 1747 C PHE A 220 -370.403-177.297 148.141 1.00 71.37 C ANISOU 1747 C PHE A 220 8796 8391 9931 -636 -2105 368 C ATOM 1748 O PHE A 220 -371.115-178.133 148.709 1.00 74.29 O ANISOU 1748 O PHE A 220 9092 8757 10378 -667 -2046 302 O ATOM 1749 CB PHE A 220 -370.071-175.028 149.156 1.00 70.21 C ANISOU 1749 CB PHE A 220 8479 8180 10017 -481 -2039 401 C ATOM 1750 CG PHE A 220 -369.829-174.475 150.524 1.00 82.93 C ANISOU 1750 CG PHE A 220 9999 9774 11737 -407 -1856 331 C ATOM 1751 CD1 PHE A 220 -368.596-173.947 150.867 1.00 89.82 C ANISOU 1751 CD1 PHE A 220 10967 10663 12497 -356 -1755 333 C ATOM 1752 CD2 PHE A 220 -370.833-174.493 151.474 1.00 91.14 C ANISOU 1752 CD2 PHE A 220 10858 10784 12986 -399 -1777 254 C ATOM 1753 CE1 PHE A 220 -368.372-173.439 152.133 1.00 93.67 C ANISOU 1753 CE1 PHE A 220 11380 11142 13069 -304 -1591 263 C ATOM 1754 CE2 PHE A 220 -370.615-173.987 152.741 1.00100.16 C ANISOU 1754 CE2 PHE A 220 11929 11920 14207 -352 -1597 176 C ATOM 1755 CZ PHE A 220 -369.383-173.455 153.069 1.00 99.55 C ANISOU 1755 CZ PHE A 220 11957 11862 14004 -307 -1510 182 C ATOM 1756 N PHE A 221 -370.423-177.134 146.817 1.00 66.78 N ANISOU 1756 N PHE A 221 8300 7820 9254 -695 -2289 447 N ATOM 1757 CA PHE A 221 -371.278-177.981 145.992 1.00 67.94 C ANISOU 1757 CA PHE A 221 8460 7978 9376 -800 -2430 452 C ATOM 1758 C PHE A 221 -370.880-179.446 146.115 1.00 77.46 C ANISOU 1758 C PHE A 221 9790 9217 10423 -855 -2304 360 C ATOM 1759 O PHE A 221 -371.720-180.309 146.396 1.00 79.05 O ANISOU 1759 O PHE A 221 9922 9409 10705 -901 -2298 308 O ATOM 1760 CB PHE A 221 -371.219-177.530 144.535 1.00 70.01 C ANISOU 1760 CB PHE A 221 8826 8258 9518 -873 -2647 558 C ATOM 1761 CG PHE A 221 -371.986-178.418 143.594 1.00 71.80 C ANISOU 1761 CG PHE A 221 9097 8507 9677 -1002 -2802 562 C ATOM 1762 CD1 PHE A 221 -373.345-178.232 143.397 1.00 74.87 C ANISOU 1762 CD1 PHE A 221 9316 8859 10271 -1034 -2986 609 C ATOM 1763 CD2 PHE A 221 -371.346-179.433 142.898 1.00 71.09 C ANISOU 1763 CD2 PHE A 221 9212 8470 9331 -1096 -2764 510 C ATOM 1764 CE1 PHE A 221 -374.055-179.048 142.528 1.00 72.42 C ANISOU 1764 CE1 PHE A 221 9048 8572 9897 -1163 -3141 613 C ATOM 1765 CE2 PHE A 221 -372.049-180.253 142.030 1.00 79.69 C ANISOU 1765 CE2 PHE A 221 10349 9579 10349 -1227 -2903 500 C ATOM 1766 CZ PHE A 221 -373.405-180.059 141.845 1.00 76.29 C ANISOU 1766 CZ PHE A 221 9756 9120 10109 -1264 -3098 557 C ATOM 1767 N CYS A 222 -369.594-179.743 145.916 1.00 77.23 N ANISOU 1767 N CYS A 222 9939 9219 10186 -852 -2200 338 N ATOM 1768 CA CYS A 222 -369.137-181.130 145.928 1.00 74.50 C ANISOU 1768 CA CYS A 222 9714 8886 9706 -903 -2088 252 C ATOM 1769 C CYS A 222 -369.421-181.795 147.266 1.00 74.85 C ANISOU 1769 C CYS A 222 9663 8905 9870 -866 -1936 185 C ATOM 1770 O CYS A 222 -369.972-182.903 147.320 1.00 76.86 O ANISOU 1770 O CYS A 222 9916 9149 10139 -930 -1925 133 O ATOM 1771 CB CYS A 222 -367.647-181.189 145.605 1.00 68.88 C ANISOU 1771 CB CYS A 222 9177 8197 8798 -888 -1986 237 C ATOM 1772 SG CYS A 222 -367.286-180.868 143.866 1.00 74.90 S ANISOU 1772 SG CYS A 222 10106 9003 9350 -990 -2138 288 S ATOM 1773 N TYR A 223 -369.064-181.128 148.363 1.00 68.35 N ANISOU 1773 N TYR A 223 8765 8073 9130 -774 -1819 187 N ATOM 1774 CA TYR A 223 -369.261-181.740 149.670 1.00 71.36 C ANISOU 1774 CA TYR A 223 9077 8441 9596 -758 -1669 130 C ATOM 1775 C TYR A 223 -370.728-181.746 150.077 1.00 77.30 C ANISOU 1775 C TYR A 223 9650 9175 10546 -788 -1713 114 C ATOM 1776 O TYR A 223 -371.164-182.664 150.778 1.00 81.05 O ANISOU 1776 O TYR A 223 10091 9640 11064 -828 -1626 63 O ATOM 1777 CB TYR A 223 -368.396-181.030 150.709 1.00 66.24 C ANISOU 1777 CB TYR A 223 8418 7798 8951 -671 -1532 132 C ATOM 1778 CG TYR A 223 -366.959-181.484 150.651 1.00 69.31 C ANISOU 1778 CG TYR A 223 8967 8197 9169 -652 -1444 127 C ATOM 1779 CD1 TYR A 223 -366.646-182.827 150.458 1.00 67.03 C ANISOU 1779 CD1 TYR A 223 8780 7894 8793 -703 -1402 88 C ATOM 1780 CD2 TYR A 223 -365.911-180.580 150.765 1.00 66.81 C ANISOU 1780 CD2 TYR A 223 8693 7894 8798 -584 -1402 157 C ATOM 1781 CE1 TYR A 223 -365.334-183.261 150.396 1.00 66.35 C ANISOU 1781 CE1 TYR A 223 8821 7802 8588 -681 -1319 77 C ATOM 1782 CE2 TYR A 223 -364.584-181.008 150.702 1.00 58.33 C ANISOU 1782 CE2 TYR A 223 7749 6822 7592 -566 -1321 149 C ATOM 1783 CZ TYR A 223 -364.305-182.350 150.516 1.00 68.83 C ANISOU 1783 CZ TYR A 223 9165 8132 8853 -612 -1279 108 C ATOM 1784 OH TYR A 223 -363.002-182.796 150.453 1.00 72.58 O ANISOU 1784 OH TYR A 223 9748 8594 9233 -589 -1197 94 O ATOM 1785 N GLY A 224 -371.503-180.748 149.651 1.00 76.70 N ANISOU 1785 N GLY A 224 9452 9086 10606 -772 -1848 159 N ATOM 1786 CA GLY A 224 -372.929-180.780 149.930 1.00 67.97 C ANISOU 1786 CA GLY A 224 8158 7953 9715 -804 -1899 138 C ATOM 1787 C GLY A 224 -373.610-181.942 149.230 1.00 74.57 C ANISOU 1787 C GLY A 224 9025 8790 10518 -907 -1993 122 C ATOM 1788 O GLY A 224 -374.416-182.662 149.827 1.00 78.10 O ANISOU 1788 O GLY A 224 9379 9224 11070 -952 -1936 68 O ATOM 1789 N GLN A 225 -373.280-182.143 147.952 1.00 74.48 N ANISOU 1789 N GLN A 225 9151 8796 10351 -958 -2134 162 N ATOM 1790 CA GLN A 225 -373.839-183.262 147.205 1.00 77.83 C ANISOU 1790 CA GLN A 225 9629 9224 10719 -1070 -2225 137 C ATOM 1791 C GLN A 225 -373.405-184.589 147.808 1.00 78.63 C ANISOU 1791 C GLN A 225 9821 9320 10734 -1100 -2056 56 C ATOM 1792 O GLN A 225 -374.200-185.531 147.907 1.00 85.97 O ANISOU 1792 O GLN A 225 10706 10232 11726 -1175 -2062 12 O ATOM 1793 CB GLN A 225 -373.410-183.168 145.741 1.00 72.62 C ANISOU 1793 CB GLN A 225 9127 8594 9872 -1133 -2385 185 C ATOM 1794 CG GLN A 225 -374.072-182.032 144.981 1.00 84.81 C ANISOU 1794 CG GLN A 225 10580 10134 11509 -1138 -2608 287 C ATOM 1795 CD GLN A 225 -375.553-182.273 144.753 1.00 91.14 C ANISOU 1795 CD GLN A 225 11221 10913 12496 -1207 -2768 298 C ATOM 1796 OE1 GLN A 225 -376.401-181.754 145.481 1.00 92.53 O ANISOU 1796 OE1 GLN A 225 11182 11049 12928 -1153 -2766 303 O ATOM 1797 NE2 GLN A 225 -375.869-183.066 143.737 1.00 90.55 N ANISOU 1797 NE2 GLN A 225 11244 10861 12299 -1334 -2903 294 N ATOM 1798 N LEU A 226 -372.147-184.672 148.232 1.00 78.38 N ANISOU 1798 N LEU A 226 9911 9295 10575 -1044 -1911 42 N ATOM 1799 CA LEU A 226 -371.640-185.903 148.818 1.00 77.31 C ANISOU 1799 CA LEU A 226 9861 9139 10374 -1065 -1762 -18 C ATOM 1800 C LEU A 226 -372.385-186.246 150.102 1.00 76.94 C ANISOU 1800 C LEU A 226 9679 9073 10482 -1070 -1657 -44 C ATOM 1801 O LEU A 226 -372.830-187.385 150.290 1.00 74.06 O ANISOU 1801 O LEU A 226 9320 8681 10137 -1142 -1624 -85 O ATOM 1802 CB LEU A 226 -370.140-185.758 149.069 1.00 70.95 C ANISOU 1802 CB LEU A 226 9184 8338 9435 -994 -1644 -13 C ATOM 1803 CG LEU A 226 -369.373-187.021 149.430 1.00 66.29 C ANISOU 1803 CG LEU A 226 8706 7711 8770 -1012 -1518 -61 C ATOM 1804 CD1 LEU A 226 -367.970-186.907 148.867 1.00 70.40 C ANISOU 1804 CD1 LEU A 226 9374 8235 9140 -973 -1479 -63 C ATOM 1805 CD2 LEU A 226 -369.348-187.199 150.940 1.00 62.03 C ANISOU 1805 CD2 LEU A 226 8097 7158 8316 -978 -1379 -56 C ATOM 1806 N VAL A 227 -372.526-185.272 151.004 1.00 69.90 N ANISOU 1806 N VAL A 227 8667 8193 9698 -1002 -1593 -27 N ATOM 1807 CA VAL A 227 -373.250-185.528 152.244 1.00 68.40 C ANISOU 1807 CA VAL A 227 8352 7995 9643 -1024 -1475 -62 C ATOM 1808 C VAL A 227 -374.693-185.900 151.944 1.00 78.17 C ANISOU 1808 C VAL A 227 9453 9215 11032 -1102 -1566 -86 C ATOM 1809 O VAL A 227 -375.271-186.781 152.591 1.00 76.73 O ANISOU 1809 O VAL A 227 9227 9018 10908 -1170 -1485 -125 O ATOM 1810 CB VAL A 227 -373.165-184.314 153.184 1.00 69.28 C ANISOU 1810 CB VAL A 227 8357 8123 9841 -948 -1386 -59 C ATOM 1811 CG1 VAL A 227 -374.092-184.518 154.368 1.00 68.80 C ANISOU 1811 CG1 VAL A 227 8154 8061 9926 -994 -1263 -110 C ATOM 1812 CG2 VAL A 227 -371.719-184.094 153.646 1.00 67.64 C ANISOU 1812 CG2 VAL A 227 8284 7933 9482 -885 -1283 -38 C ATOM 1813 N PHE A 228 -375.293-185.248 150.947 1.00 75.79 N ANISOU 1813 N PHE A 228 9082 8914 10801 -1102 -1745 -55 N ATOM 1814 CA PHE A 228 -376.646-185.607 150.544 1.00 76.24 C ANISOU 1814 CA PHE A 228 9006 8952 11009 -1182 -1861 -70 C ATOM 1815 C PHE A 228 -376.707-187.057 150.077 1.00 75.76 C ANISOU 1815 C PHE A 228 9060 8880 10844 -1283 -1881 -103 C ATOM 1816 O PHE A 228 -377.573-187.825 150.511 1.00 77.68 O ANISOU 1816 O PHE A 228 9217 9104 11196 -1356 -1843 -145 O ATOM 1817 CB PHE A 228 -377.135-184.660 149.447 1.00 79.68 C ANISOU 1817 CB PHE A 228 9371 9387 11518 -1169 -2084 -8 C ATOM 1818 CG PHE A 228 -378.489-185.011 148.914 1.00 78.87 C ANISOU 1818 CG PHE A 228 9131 9264 11573 -1255 -2239 -10 C ATOM 1819 CD1 PHE A 228 -379.636-184.556 149.545 1.00 84.03 C ANISOU 1819 CD1 PHE A 228 9537 9887 12502 -1245 -2229 -32 C ATOM 1820 CD2 PHE A 228 -378.618-185.805 147.787 1.00 85.18 C ANISOU 1820 CD2 PHE A 228 10042 10071 12250 -1354 -2390 -1 C ATOM 1821 CE1 PHE A 228 -380.890-184.886 149.061 1.00 79.68 C ANISOU 1821 CE1 PHE A 228 8843 9313 12118 -1325 -2378 -33 C ATOM 1822 CE2 PHE A 228 -379.871-186.144 147.297 1.00 85.60 C ANISOU 1822 CE2 PHE A 228 9968 10107 12449 -1442 -2546 -2 C ATOM 1823 CZ PHE A 228 -381.006-185.681 147.934 1.00 79.13 C ANISOU 1823 CZ PHE A 228 8890 9255 11918 -1425 -2546 -12 C ATOM 1824 N THR A 229 -375.784-187.451 149.193 1.00 70.81 N ANISOU 1824 N THR A 229 8629 8261 10015 -1295 -1929 -94 N ATOM 1825 CA THR A 229 -375.765-188.824 148.695 1.00 73.52 C ANISOU 1825 CA THR A 229 9090 8581 10262 -1392 -1938 -141 C ATOM 1826 C THR A 229 -375.556-189.827 149.825 1.00 73.05 C ANISOU 1826 C THR A 229 9052 8487 10218 -1407 -1752 -181 C ATOM 1827 O THR A 229 -376.242-190.852 149.893 1.00 78.21 O ANISOU 1827 O THR A 229 9683 9108 10927 -1497 -1749 -220 O ATOM 1828 CB THR A 229 -374.675-188.983 147.635 1.00 73.31 C ANISOU 1828 CB THR A 229 9270 8567 10019 -1398 -1983 -142 C ATOM 1829 OG1 THR A 229 -375.034-188.238 146.466 1.00 78.28 O ANISOU 1829 OG1 THR A 229 9895 9230 10618 -1427 -2183 -97 O ATOM 1830 CG2 THR A 229 -374.483-190.446 147.260 1.00 66.88 C ANISOU 1830 CG2 THR A 229 8585 7712 9114 -1488 -1949 -213 C ATOM 1831 N VAL A 230 -374.629-189.539 150.733 1.00 71.77 N ANISOU 1831 N VAL A 230 8932 8330 10008 -1327 -1605 -165 N ATOM 1832 CA VAL A 230 -374.336-190.490 151.798 1.00 69.73 C ANISOU 1832 CA VAL A 230 8712 8036 9746 -1350 -1447 -181 C ATOM 1833 C VAL A 230 -375.514-190.607 152.761 1.00 71.50 C ANISOU 1833 C VAL A 230 8770 8261 10136 -1405 -1385 -196 C ATOM 1834 O VAL A 230 -375.890-191.714 153.164 1.00 78.34 O ANISOU 1834 O VAL A 230 9645 9089 11032 -1489 -1329 -217 O ATOM 1835 CB VAL A 230 -373.032-190.089 152.507 1.00 67.39 C ANISOU 1835 CB VAL A 230 8502 7750 9354 -1260 -1328 -148 C ATOM 1836 CG1 VAL A 230 -372.881-190.826 153.817 1.00 62.82 C ANISOU 1836 CG1 VAL A 230 7930 7145 8792 -1290 -1179 -139 C ATOM 1837 CG2 VAL A 230 -371.856-190.381 151.587 1.00 62.53 C ANISOU 1837 CG2 VAL A 230 8057 7115 8586 -1231 -1359 -152 C ATOM 1838 N LYS A 231 -376.132-189.477 153.127 1.00 69.62 N ANISOU 1838 N LYS A 231 8372 8059 10020 -1365 -1388 -190 N ATOM 1839 CA LYS A 231 -377.280-189.531 154.028 1.00 68.92 C ANISOU 1839 CA LYS A 231 8110 7971 10104 -1424 -1310 -223 C ATOM 1840 C LYS A 231 -378.466-190.233 153.378 1.00 79.56 C ANISOU 1840 C LYS A 231 9372 9293 11564 -1522 -1420 -252 C ATOM 1841 O LYS A 231 -379.235-190.918 154.060 1.00 68.77 O ANISOU 1841 O LYS A 231 7925 7909 10294 -1607 -1336 -285 O ATOM 1842 CB LYS A 231 -377.668-188.123 154.479 1.00 66.52 C ANISOU 1842 CB LYS A 231 7643 7698 9933 -1355 -1285 -229 C ATOM 1843 CG LYS A 231 -376.706-187.523 155.515 1.00 67.50 C ANISOU 1843 CG LYS A 231 7823 7851 9972 -1289 -1129 -219 C ATOM 1844 CD LYS A 231 -377.177-186.167 156.025 1.00 66.31 C ANISOU 1844 CD LYS A 231 7499 7720 9975 -1233 -1084 -247 C ATOM 1845 CE LYS A 231 -376.232-185.603 157.082 1.00 75.41 C ANISOU 1845 CE LYS A 231 8717 8906 11031 -1186 -927 -247 C ATOM 1846 NZ LYS A 231 -376.156-186.476 158.284 1.00 74.07 N ANISOU 1846 NZ LYS A 231 8599 8752 10792 -1276 -757 -264 N ATOM 1847 N GLU A 232 -378.618-190.081 152.066 1.00 74.40 N ANISOU 1847 N GLU A 232 8740 8637 10892 -1523 -1610 -240 N ATOM 1848 CA GLU A 232 -379.704-190.744 151.362 1.00 72.06 C ANISOU 1848 CA GLU A 232 8373 8319 10690 -1626 -1739 -265 C ATOM 1849 C GLU A 232 -379.522-192.257 151.385 1.00 83.59 C ANISOU 1849 C GLU A 232 9962 9736 12062 -1718 -1684 -298 C ATOM 1850 O GLU A 232 -380.458-193.006 151.693 1.00 89.35 O ANISOU 1850 O GLU A 232 10601 10439 12908 -1814 -1663 -331 O ATOM 1851 CB GLU A 232 -379.769-190.225 149.931 1.00 79.23 C ANISOU 1851 CB GLU A 232 9306 9240 11556 -1620 -1966 -233 C ATOM 1852 CG GLU A 232 -381.146-190.201 149.332 1.00 96.84 C ANISOU 1852 CG GLU A 232 11368 11463 13965 -1697 -2139 -236 C ATOM 1853 CD GLU A 232 -381.139-189.603 147.946 1.00111.94 C ANISOU 1853 CD GLU A 232 13323 13396 15814 -1701 -2379 -182 C ATOM 1854 OE1 GLU A 232 -380.091-189.692 147.272 1.00121.65 O ANISOU 1854 OE1 GLU A 232 14759 14643 16818 -1690 -2402 -169 O ATOM 1855 OE2 GLU A 232 -382.171-189.033 147.536 1.00112.53 O ANISOU 1855 OE2 GLU A 232 13222 13467 16068 -1722 -2546 -151 O ATOM 1856 N ALA A 233 -378.311-192.723 151.075 1.00 83.23 N ANISOU 1856 N ALA A 233 10121 9675 11829 -1691 -1654 -292 N ATOM 1857 CA ALA A 233 -378.060-194.158 151.038 1.00 76.95 C ANISOU 1857 CA ALA A 233 9450 8818 10970 -1771 -1606 -326 C ATOM 1858 C ALA A 233 -378.166-194.773 152.429 1.00 75.05 C ANISOU 1858 C ALA A 233 9176 8548 10792 -1802 -1430 -319 C ATOM 1859 O ALA A 233 -378.707-195.875 152.587 1.00 73.82 O ANISOU 1859 O ALA A 233 9018 8341 10691 -1904 -1407 -345 O ATOM 1860 CB ALA A 233 -376.693-194.432 150.416 1.00 68.46 C ANISOU 1860 CB ALA A 233 8582 7722 9708 -1725 -1601 -330 C ATOM 1861 N ALA A 234 -377.676-194.071 153.452 1.00 76.57 N ANISOU 1861 N ALA A 234 9346 8774 10972 -1729 -1308 -281 N ATOM 1862 CA ALA A 234 -377.810-194.583 154.812 1.00 79.65 C ANISOU 1862 CA ALA A 234 9712 9149 11401 -1780 -1145 -266 C ATOM 1863 C ALA A 234 -379.272-194.671 155.236 1.00 82.89 C ANISOU 1863 C ALA A 234 9936 9571 11988 -1876 -1123 -301 C ATOM 1864 O ALA A 234 -379.645-195.593 155.971 1.00 77.65 O ANISOU 1864 O ALA A 234 9271 8874 11360 -1975 -1027 -301 O ATOM 1865 CB ALA A 234 -377.017-193.711 155.787 1.00 67.12 C ANISOU 1865 CB ALA A 234 8141 7609 9753 -1697 -1029 -225 C ATOM 1866 N ALA A 235 -380.111-193.733 154.779 1.00 77.93 N ANISOU 1866 N ALA A 235 9144 8983 11485 -1852 -1213 -327 N ATOM 1867 CA ALA A 235 -381.525-193.750 155.141 1.00 76.29 C ANISOU 1867 CA ALA A 235 8729 8778 11477 -1937 -1192 -369 C ATOM 1868 C ALA A 235 -382.214-195.018 154.651 1.00 81.22 C ANISOU 1868 C ALA A 235 9363 9350 12149 -2060 -1258 -395 C ATOM 1869 O ALA A 235 -383.152-195.503 155.294 1.00 81.40 O ANISOU 1869 O ALA A 235 9267 9361 12301 -2162 -1176 -423 O ATOM 1870 CB ALA A 235 -382.225-192.515 154.579 1.00 72.43 C ANISOU 1870 CB ALA A 235 8060 8322 11139 -1876 -1311 -384 C ATOM 1871 N GLN A 236 -381.765-195.563 153.524 1.00 80.09 N ANISOU 1871 N GLN A 236 9357 9174 11901 -2062 -1396 -393 N ATOM 1872 CA GLN A 236 -382.286-196.801 152.971 1.00 79.61 C ANISOU 1872 CA GLN A 236 9331 9054 11864 -2181 -1463 -427 C ATOM 1873 C GLN A 236 -381.667-198.045 153.595 1.00 73.85 C ANISOU 1873 C GLN A 236 8752 8256 11052 -2235 -1336 -416 C ATOM 1874 O GLN A 236 -381.976-199.155 153.147 1.00 77.47 O ANISOU 1874 O GLN A 236 9260 8649 11527 -2333 -1382 -448 O ATOM 1875 CB GLN A 236 -382.058-196.831 151.459 1.00 81.15 C ANISOU 1875 CB GLN A 236 9619 9244 11971 -2175 -1661 -445 C ATOM 1876 CG GLN A 236 -383.169-196.202 150.655 1.00 84.39 C ANISOU 1876 CG GLN A 236 9862 9690 12513 -2205 -1844 -457 C ATOM 1877 CD GLN A 236 -384.433-197.042 150.674 1.00 93.15 C ANISOU 1877 CD GLN A 236 10844 10763 13785 -2343 -1877 -499 C ATOM 1878 OE1 GLN A 236 -384.416-198.217 150.314 1.00 94.39 O ANISOU 1878 OE1 GLN A 236 11108 10865 13889 -2438 -1893 -535 O ATOM 1879 NE2 GLN A 236 -385.533-196.442 151.102 1.00 96.01 N ANISOU 1879 NE2 GLN A 236 10968 11149 14361 -2356 -1881 -502 N ATOM 1880 N GLN A 237 -380.799-197.892 154.593 1.00 72.71 N ANISOU 1880 N GLN A 237 8683 8117 10826 -2180 -1191 -367 N ATOM 1881 CA GLN A 237 -380.133-199.007 155.262 1.00 72.53 C ANISOU 1881 CA GLN A 237 8801 8020 10735 -2225 -1085 -331 C ATOM 1882 C GLN A 237 -380.030-198.739 156.753 1.00 75.85 C ANISOU 1882 C GLN A 237 9190 8476 11152 -2237 -915 -277 C ATOM 1883 O GLN A 237 -378.992-198.983 157.374 1.00 78.64 O ANISOU 1883 O GLN A 237 9677 8805 11399 -2204 -840 -215 O ATOM 1884 CB GLN A 237 -378.738-199.268 154.690 1.00 81.43 C ANISOU 1884 CB GLN A 237 10123 9101 11716 -2141 -1118 -314 C ATOM 1885 CG GLN A 237 -378.696-199.800 153.268 1.00 97.17 C ANISOU 1885 CG GLN A 237 12192 11047 13680 -2161 -1256 -380 C ATOM 1886 CD GLN A 237 -377.413-200.571 152.972 1.00106.98 C ANISOU 1886 CD GLN A 237 13626 12201 14821 -2124 -1231 -380 C ATOM 1887 OE1 GLN A 237 -376.805-201.157 153.870 1.00104.79 O ANISOU 1887 OE1 GLN A 237 13413 11861 14541 -2122 -1127 -324 O ATOM 1888 NE2 GLN A 237 -377.001-200.574 151.708 1.00110.63 N ANISOU 1888 NE2 GLN A 237 14174 12654 15206 -2102 -1328 -444 N ATOM 1889 N GLN A 238 -381.105-198.228 157.352 1.00 78.66 N ANISOU 1889 N GLN A 238 9369 8890 11630 -2291 -850 -304 N ATOM 1890 CA GLN A 238 -381.068-197.922 158.776 1.00 79.60 C ANISOU 1890 CA GLN A 238 9460 9055 11731 -2324 -673 -270 C ATOM 1891 C GLN A 238 -380.926-199.163 159.648 1.00 81.45 C ANISOU 1891 C GLN A 238 9797 9227 11922 -2447 -573 -211 C ATOM 1892 O GLN A 238 -380.639-199.027 160.843 1.00 87.30 O ANISOU 1892 O GLN A 238 10571 10004 12596 -2486 -435 -161 O ATOM 1893 CB GLN A 238 -382.319-197.153 159.178 1.00 79.44 C ANISOU 1893 CB GLN A 238 9212 9100 11872 -2368 -609 -335 C ATOM 1894 CG GLN A 238 -382.455-195.796 158.530 1.00 86.15 C ANISOU 1894 CG GLN A 238 9943 10003 12788 -2245 -698 -376 C ATOM 1895 CD GLN A 238 -383.712-195.093 158.976 1.00103.11 C ANISOU 1895 CD GLN A 238 11846 12194 15139 -2288 -625 -448 C ATOM 1896 OE1 GLN A 238 -384.314-195.463 159.982 1.00107.88 O ANISOU 1896 OE1 GLN A 238 12384 12810 15798 -2406 -464 -471 O ATOM 1897 NE2 GLN A 238 -384.125-194.084 158.225 1.00113.85 N ANISOU 1897 NE2 GLN A 238 13064 13572 16622 -2200 -743 -483 N ATOM 1898 N GLU A 239 -381.108-200.363 159.091 1.00 76.62 N ANISOU 1898 N GLU A 239 9246 8522 11346 -2517 -642 -212 N ATOM 1899 CA GLU A 239 -380.869-201.576 159.863 1.00 81.65 C ANISOU 1899 CA GLU A 239 9994 9079 11951 -2628 -565 -139 C ATOM 1900 C GLU A 239 -379.387-201.824 160.129 1.00 88.03 C ANISOU 1900 C GLU A 239 10992 9838 12619 -2551 -564 -49 C ATOM 1901 O GLU A 239 -379.061-202.703 160.932 1.00 99.16 O ANISOU 1901 O GLU A 239 12497 11181 13998 -2634 -504 39 O ATOM 1902 CB GLU A 239 -381.475-202.792 159.150 1.00 81.73 C ANISOU 1902 CB GLU A 239 10010 8987 12058 -2723 -643 -173 C ATOM 1903 CG GLU A 239 -380.744-203.213 157.874 1.00 75.68 C ANISOU 1903 CG GLU A 239 9361 8141 11254 -2640 -784 -204 C ATOM 1904 CD GLU A 239 -381.208-202.471 156.619 1.00 83.64 C ANISOU 1904 CD GLU A 239 10279 9205 12297 -2578 -919 -297 C ATOM 1905 OE1 GLU A 239 -381.828-201.389 156.725 1.00 84.44 O ANISOU 1905 OE1 GLU A 239 10230 9406 12446 -2548 -916 -322 O ATOM 1906 OE2 GLU A 239 -380.948-202.987 155.511 1.00 75.69 O ANISOU 1906 OE2 GLU A 239 9351 8134 11271 -2566 -1032 -345 O ATOM 1907 N SER A 240 -378.486-201.079 159.495 1.00 83.11 N ANISOU 1907 N SER A 240 10419 9239 11920 -2400 -633 -60 N ATOM 1908 CA SER A 240 -377.049-201.312 159.624 1.00 87.96 C ANISOU 1908 CA SER A 240 11196 9798 12427 -2318 -643 15 C ATOM 1909 C SER A 240 -376.433-200.259 160.543 1.00 83.66 C ANISOU 1909 C SER A 240 10657 9349 11781 -2258 -565 68 C ATOM 1910 O SER A 240 -376.326-199.087 160.169 1.00 86.64 O ANISOU 1910 O SER A 240 10976 9810 12133 -2156 -586 21 O ATOM 1911 CB SER A 240 -376.378-201.295 158.254 1.00 87.57 C ANISOU 1911 CB SER A 240 11212 9703 12358 -2206 -762 -42 C ATOM 1912 OG SER A 240 -374.971-201.248 158.392 1.00 92.10 O ANISOU 1912 OG SER A 240 11910 10240 12842 -2107 -758 18 O ATOM 1913 N ALA A 241 -376.014-200.687 161.738 1.00 83.99 N ANISOU 1913 N ALA A 241 10776 9374 11762 -2329 -482 172 N ATOM 1914 CA ALA A 241 -375.405-199.768 162.695 1.00 86.57 C ANISOU 1914 CA ALA A 241 11123 9792 11976 -2296 -408 225 C ATOM 1915 C ALA A 241 -374.084-199.210 162.180 1.00 94.43 C ANISOU 1915 C ALA A 241 12200 10781 12898 -2133 -479 242 C ATOM 1916 O ALA A 241 -373.728-198.068 162.499 1.00 91.35 O ANISOU 1916 O ALA A 241 11784 10486 12438 -2065 -445 234 O ATOM 1917 CB ALA A 241 -375.198-200.463 164.041 1.00 78.02 C ANISOU 1917 CB ALA A 241 10128 8688 10828 -2430 -327 349 C ATOM 1918 N THR A 242 -373.354-199.990 161.380 1.00 88.68 N ANISOU 1918 N THR A 242 11562 9938 12194 -2074 -567 255 N ATOM 1919 CA THR A 242 -372.101-199.501 160.812 1.00 83.43 C ANISOU 1919 CA THR A 242 10965 9262 11472 -1925 -624 258 C ATOM 1920 C THR A 242 -372.347-198.462 159.726 1.00 83.30 C ANISOU 1920 C THR A 242 10875 9320 11455 -1827 -673 150 C ATOM 1921 O THR A 242 -371.661-197.434 159.682 1.00 86.42 O ANISOU 1921 O THR A 242 11274 9780 11780 -1725 -675 151 O ATOM 1922 CB THR A 242 -371.286-200.666 160.245 1.00 83.58 C ANISOU 1922 CB THR A 242 11091 9127 11540 -1898 -686 283 C ATOM 1923 OG1 THR A 242 -371.922-201.160 159.063 1.00 86.71 O ANISOU 1923 OG1 THR A 242 11461 9473 12012 -1911 -741 177 O ATOM 1924 CG2 THR A 242 -371.181-201.791 161.266 1.00 77.82 C ANISOU 1924 CG2 THR A 242 10426 8302 10841 -2008 -659 403 C ATOM 1925 N THR A 243 -373.313-198.714 158.836 1.00 81.17 N ANISOU 1925 N THR A 243 10539 9039 11263 -1864 -725 64 N ATOM 1926 CA THR A 243 -373.645-197.730 157.808 1.00 77.99 C ANISOU 1926 CA THR A 243 10064 8707 10863 -1790 -794 -20 C ATOM 1927 C THR A 243 -374.008-196.389 158.431 1.00 77.99 C ANISOU 1927 C THR A 243 9956 8825 10852 -1760 -741 -22 C ATOM 1928 O THR A 243 -373.608-195.332 157.927 1.00 74.74 O ANISOU 1928 O THR A 243 9529 8469 10402 -1657 -782 -44 O ATOM 1929 CB THR A 243 -374.793-198.241 156.935 1.00 76.73 C ANISOU 1929 CB THR A 243 9836 8522 10796 -1866 -866 -98 C ATOM 1930 OG1 THR A 243 -374.392-199.450 156.281 1.00 79.89 O ANISOU 1930 OG1 THR A 243 10344 8806 11205 -1893 -910 -115 O ATOM 1931 CG2 THR A 243 -375.179-197.207 155.876 1.00 72.30 C ANISOU 1931 CG2 THR A 243 9199 8033 10239 -1803 -964 -164 C ATOM 1932 N GLN A 244 -374.750-196.413 159.539 1.00 77.82 N ANISOU 1932 N GLN A 244 9861 8840 10866 -1857 -641 -5 N ATOM 1933 CA GLN A 244 -375.083-195.174 160.229 1.00 80.23 C ANISOU 1933 CA GLN A 244 10062 9249 11173 -1839 -564 -25 C ATOM 1934 C GLN A 244 -373.840-194.542 160.844 1.00 87.36 C ANISOU 1934 C GLN A 244 11055 10186 11951 -1762 -523 34 C ATOM 1935 O GLN A 244 -373.695-193.314 160.839 1.00 88.71 O ANISOU 1935 O GLN A 244 11170 10427 12109 -1683 -512 4 O ATOM 1936 CB GLN A 244 -376.146-195.439 161.293 1.00 76.14 C ANISOU 1936 CB GLN A 244 9453 8762 10717 -1982 -443 -35 C ATOM 1937 CG GLN A 244 -377.391-196.118 160.751 1.00 74.14 C ANISOU 1937 CG GLN A 244 9100 8471 10600 -2070 -481 -91 C ATOM 1938 CD GLN A 244 -377.952-195.416 159.531 1.00 79.21 C ANISOU 1938 CD GLN A 244 9628 9130 11339 -1992 -602 -167 C ATOM 1939 OE1 GLN A 244 -378.271-194.226 159.573 1.00 87.57 O ANISOU 1939 OE1 GLN A 244 10567 10254 12450 -1935 -588 -209 O ATOM 1940 NE2 GLN A 244 -378.079-196.154 158.432 1.00 75.83 N ANISOU 1940 NE2 GLN A 244 9237 8637 10938 -1998 -727 -184 N ATOM 1941 N LYS A 245 -372.932-195.364 161.376 1.00 86.90 N ANISOU 1941 N LYS A 245 11132 10072 11815 -1785 -508 122 N ATOM 1942 CA LYS A 245 -371.678-194.834 161.901 1.00 88.08 C ANISOU 1942 CA LYS A 245 11368 10245 11853 -1713 -490 187 C ATOM 1943 C LYS A 245 -370.846-194.204 160.791 1.00 80.45 C ANISOU 1943 C LYS A 245 10429 9272 10866 -1563 -579 157 C ATOM 1944 O LYS A 245 -370.336-193.088 160.943 1.00 74.11 O ANISOU 1944 O LYS A 245 9613 8535 10011 -1486 -564 153 O ATOM 1945 CB LYS A 245 -370.891-195.935 162.613 1.00 95.85 C ANISOU 1945 CB LYS A 245 12481 11151 12786 -1771 -485 301 C ATOM 1946 CG LYS A 245 -371.447-196.309 163.983 1.00106.64 C ANISOU 1946 CG LYS A 245 13850 12550 14118 -1930 -384 360 C ATOM 1947 CD LYS A 245 -370.677-197.467 164.608 1.00111.79 C ANISOU 1947 CD LYS A 245 14634 13108 14735 -1993 -411 496 C ATOM 1948 CE LYS A 245 -371.333-197.940 165.901 1.00116.83 C ANISOU 1948 CE LYS A 245 15287 13777 15326 -2180 -318 563 C ATOM 1949 NZ LYS A 245 -370.645-199.134 166.468 1.00119.76 N ANISOU 1949 NZ LYS A 245 15785 14039 15679 -2251 -368 717 N ATOM 1950 N ALA A 246 -370.714-194.896 159.656 1.00 74.09 N ANISOU 1950 N ALA A 246 9665 8388 10098 -1532 -666 129 N ATOM 1951 CA ALA A 246 -369.967-194.332 158.536 1.00 74.29 C ANISOU 1951 CA ALA A 246 9725 8413 10091 -1412 -740 93 C ATOM 1952 C ALA A 246 -370.601-193.037 158.045 1.00 82.64 C ANISOU 1952 C ALA A 246 10674 9559 11166 -1366 -769 33 C ATOM 1953 O ALA A 246 -369.893-192.090 157.681 1.00 91.83 O ANISOU 1953 O ALA A 246 11854 10761 12277 -1268 -793 31 O ATOM 1954 CB ALA A 246 -369.869-195.343 157.398 1.00 62.53 C ANISOU 1954 CB ALA A 246 8297 6828 8632 -1417 -812 52 C ATOM 1955 N GLU A 247 -371.934-192.975 158.029 1.00 83.80 N ANISOU 1955 N GLU A 247 10703 9733 11404 -1435 -771 -14 N ATOM 1956 CA GLU A 247 -372.603-191.748 157.614 1.00 75.87 C ANISOU 1956 CA GLU A 247 9574 8796 10456 -1391 -809 -62 C ATOM 1957 C GLU A 247 -372.298-190.608 158.578 1.00 70.93 C ANISOU 1957 C GLU A 247 8906 8239 9806 -1348 -720 -49 C ATOM 1958 O GLU A 247 -372.060-189.472 158.153 1.00 73.58 O ANISOU 1958 O GLU A 247 9204 8612 10142 -1259 -760 -63 O ATOM 1959 CB GLU A 247 -374.112-191.987 157.511 1.00 72.04 C ANISOU 1959 CB GLU A 247 8952 8314 10106 -1481 -825 -113 C ATOM 1960 CG GLU A 247 -374.916-190.752 157.142 1.00 83.77 C ANISOU 1960 CG GLU A 247 10281 9851 11697 -1439 -874 -157 C ATOM 1961 CD GLU A 247 -375.333-189.942 158.356 1.00 91.19 C ANISOU 1961 CD GLU A 247 11104 10844 12699 -1452 -740 -177 C ATOM 1962 OE1 GLU A 247 -375.722-190.557 159.372 1.00 98.22 O ANISOU 1962 OE1 GLU A 247 11981 11737 13600 -1552 -620 -180 O ATOM 1963 OE2 GLU A 247 -375.260-188.696 158.294 1.00 88.03 O ANISOU 1963 OE2 GLU A 247 10632 10480 12335 -1372 -749 -194 O ATOM 1964 N LYS A 248 -372.301-190.896 159.882 1.00 68.57 N ANISOU 1964 N LYS A 248 8617 7957 9482 -1421 -600 -21 N ATOM 1965 CA LYS A 248 -372.046-189.856 160.873 1.00 73.54 C ANISOU 1965 CA LYS A 248 9212 8656 10075 -1404 -502 -22 C ATOM 1966 C LYS A 248 -370.627-189.314 160.758 1.00 76.80 C ANISOU 1966 C LYS A 248 9730 9076 10377 -1299 -531 24 C ATOM 1967 O LYS A 248 -370.406-188.102 160.866 1.00 76.54 O ANISOU 1967 O LYS A 248 9650 9091 10341 -1233 -512 0 O ATOM 1968 CB LYS A 248 -372.295-190.396 162.280 1.00 82.20 C ANISOU 1968 CB LYS A 248 10325 9774 11133 -1533 -371 3 C ATOM 1969 CG LYS A 248 -373.757-190.391 162.716 1.00 92.63 C ANISOU 1969 CG LYS A 248 11499 11124 12573 -1638 -285 -69 C ATOM 1970 CD LYS A 248 -373.889-190.747 164.196 1.00102.82 C ANISOU 1970 CD LYS A 248 12823 12454 13790 -1780 -134 -45 C ATOM 1971 CE LYS A 248 -375.329-190.627 164.690 1.00110.79 C ANISOU 1971 CE LYS A 248 13673 13499 14924 -1891 -17 -137 C ATOM 1972 NZ LYS A 248 -375.459-190.926 166.151 1.00114.64 N ANISOU 1972 NZ LYS A 248 14205 14040 15314 -2052 148 -120 N ATOM 1973 N GLU A 249 -369.649-190.193 160.535 1.00 76.89 N ANISOU 1973 N GLU A 249 9873 9028 10314 -1282 -573 87 N ATOM 1974 CA GLU A 249 -368.269-189.729 160.523 1.00 87.10 C ANISOU 1974 CA GLU A 249 11254 10324 11516 -1190 -590 132 C ATOM 1975 C GLU A 249 -367.946-188.998 159.224 1.00 83.06 C ANISOU 1975 C GLU A 249 10735 9813 11012 -1081 -678 95 C ATOM 1976 O GLU A 249 -367.185-188.023 159.231 1.00 77.77 O ANISOU 1976 O GLU A 249 10077 9177 10296 -1002 -677 104 O ATOM 1977 CB GLU A 249 -367.313-190.898 160.767 1.00 93.75 C ANISOU 1977 CB GLU A 249 12222 11092 12309 -1208 -603 211 C ATOM 1978 CG GLU A 249 -367.351-191.992 159.725 1.00116.10 C ANISOU 1978 CG GLU A 249 15095 13829 15187 -1207 -673 195 C ATOM 1979 CD GLU A 249 -366.542-193.210 160.134 1.00132.18 C ANISOU 1979 CD GLU A 249 17233 15771 17218 -1234 -675 273 C ATOM 1980 OE1 GLU A 249 -366.336-193.409 161.351 1.00134.60 O ANISOU 1980 OE1 GLU A 249 17566 16088 17489 -1296 -628 353 O ATOM 1981 OE2 GLU A 249 -366.111-193.966 159.238 1.00138.56 O ANISOU 1981 OE2 GLU A 249 18095 16491 18062 -1201 -724 255 O ATOM 1982 N VAL A 250 -368.531-189.434 158.105 1.00 75.18 N ANISOU 1982 N VAL A 250 9721 8779 10065 -1087 -758 56 N ATOM 1983 CA VAL A 250 -368.365-188.697 156.853 1.00 73.16 C ANISOU 1983 CA VAL A 250 9461 8534 9802 -1010 -850 26 C ATOM 1984 C VAL A 250 -368.922-187.287 156.994 1.00 75.17 C ANISOU 1984 C VAL A 250 9598 8852 10112 -972 -851 4 C ATOM 1985 O VAL A 250 -368.288-186.305 156.590 1.00 82.68 O ANISOU 1985 O VAL A 250 10561 9826 11027 -891 -882 13 O ATOM 1986 CB VAL A 250 -369.031-189.451 155.688 1.00 71.92 C ANISOU 1986 CB VAL A 250 9311 8337 9680 -1053 -942 -14 C ATOM 1987 CG1 VAL A 250 -369.145-188.542 154.471 1.00 71.70 C ANISOU 1987 CG1 VAL A 250 9262 8338 9643 -1003 -1050 -35 C ATOM 1988 CG2 VAL A 250 -368.245-190.702 155.353 1.00 65.03 C ANISOU 1988 CG2 VAL A 250 8564 7386 8757 -1068 -940 -8 C ATOM 1989 N THR A 251 -370.116-187.165 157.575 1.00 71.47 N ANISOU 1989 N THR A 251 9004 8403 9746 -1034 -810 -29 N ATOM 1990 CA THR A 251 -370.701-185.845 157.774 1.00 71.29 C ANISOU 1990 CA THR A 251 8848 8423 9817 -998 -798 -63 C ATOM 1991 C THR A 251 -369.835-184.996 158.694 1.00 72.90 C ANISOU 1991 C THR A 251 9078 8665 9957 -953 -705 -50 C ATOM 1992 O THR A 251 -369.617-183.807 158.435 1.00 73.75 O ANISOU 1992 O THR A 251 9141 8788 10090 -877 -731 -58 O ATOM 1993 CB THR A 251 -372.110-185.977 158.347 1.00 70.51 C ANISOU 1993 CB THR A 251 8600 8331 9858 -1082 -743 -116 C ATOM 1994 OG1 THR A 251 -372.895-186.816 157.490 1.00 65.99 O ANISOU 1994 OG1 THR A 251 8006 7722 9345 -1132 -839 -125 O ATOM 1995 CG2 THR A 251 -372.769-184.608 158.457 1.00 61.05 C ANISOU 1995 CG2 THR A 251 7241 7155 8800 -1038 -733 -163 C ATOM 1996 N ARG A 252 -369.328-185.597 159.772 1.00 70.90 N ANISOU 1996 N ARG A 252 8898 8421 9619 -1007 -606 -23 N ATOM 1997 CA ARG A 252 -368.560-184.846 160.757 1.00 66.67 C ANISOU 1997 CA ARG A 252 8390 7929 9012 -988 -519 -12 C ATOM 1998 C ARG A 252 -367.215-184.408 160.188 1.00 68.86 C ANISOU 1998 C ARG A 252 8764 8198 9203 -887 -581 34 C ATOM 1999 O ARG A 252 -366.722-183.319 160.508 1.00 67.54 O ANISOU 1999 O ARG A 252 8580 8063 9018 -837 -552 25 O ATOM 2000 CB ARG A 252 -368.377-185.688 162.018 1.00 76.26 C ANISOU 2000 CB ARG A 252 9671 9158 10145 -1093 -422 23 C ATOM 2001 CG ARG A 252 -367.612-184.995 163.132 1.00 97.26 C ANISOU 2001 CG ARG A 252 12371 11871 12711 -1103 -336 37 C ATOM 2002 CD ARG A 252 -367.884-185.648 164.481 1.00112.61 C ANISOU 2002 CD ARG A 252 14349 13848 14588 -1246 -229 56 C ATOM 2003 NE ARG A 252 -367.298-184.889 165.584 1.00125.47 N ANISOU 2003 NE ARG A 252 16012 15542 16119 -1280 -144 54 N ATOM 2004 CZ ARG A 252 -367.879-183.844 166.170 1.00136.11 C ANISOU 2004 CZ ARG A 252 17265 16946 17504 -1310 -36 -44 C ATOM 2005 NH1 ARG A 252 -367.267-183.219 167.166 1.00140.99 N ANISOU 2005 NH1 ARG A 252 17932 17623 18014 -1353 39 -49 N ATOM 2006 NH2 ARG A 252 -369.069-183.421 165.762 1.00137.74 N ANISOU 2006 NH2 ARG A 252 17323 17143 17868 -1299 -4 -140 N ATOM 2007 N MET A 253 -366.617-185.243 159.336 1.00 63.74 N ANISOU 2007 N MET A 253 8209 7501 8506 -862 -658 72 N ATOM 2008 CA MET A 253 -365.387-184.865 158.657 1.00 61.83 C ANISOU 2008 CA MET A 253 8049 7249 8196 -772 -708 102 C ATOM 2009 C MET A 253 -365.628-183.750 157.649 1.00 67.43 C ANISOU 2009 C MET A 253 8702 7972 8947 -705 -781 75 C ATOM 2010 O MET A 253 -364.842-182.798 157.575 1.00 79.63 O ANISOU 2010 O MET A 253 10263 9535 10456 -638 -783 89 O ATOM 2011 CB MET A 253 -364.772-186.086 157.976 1.00 64.33 C ANISOU 2011 CB MET A 253 8469 7502 8471 -773 -753 128 C ATOM 2012 CG MET A 253 -363.941-186.960 158.902 1.00 73.25 C ANISOU 2012 CG MET A 253 9676 8600 9554 -802 -703 187 C ATOM 2013 SD MET A 253 -362.606-186.068 159.757 1.00 90.41 S ANISOU 2013 SD MET A 253 11885 10812 11654 -748 -663 237 S ATOM 2014 CE MET A 253 -361.741-185.272 158.394 1.00 71.70 C ANISOU 2014 CE MET A 253 9541 8436 9265 -635 -721 215 C ATOM 2015 N VAL A 254 -366.705-183.843 156.867 1.00 68.36 N ANISOU 2015 N VAL A 254 8753 8078 9143 -729 -853 45 N ATOM 2016 CA VAL A 254 -366.986-182.805 155.878 1.00 67.97 C ANISOU 2016 CA VAL A 254 8651 8035 9139 -677 -949 41 C ATOM 2017 C VAL A 254 -367.198-181.467 156.566 1.00 70.65 C ANISOU 2017 C VAL A 254 8885 8400 9557 -637 -902 24 C ATOM 2018 O VAL A 254 -366.782-180.414 156.065 1.00 73.66 O ANISOU 2018 O VAL A 254 9262 8784 9942 -571 -951 43 O ATOM 2019 CB VAL A 254 -368.204-183.198 155.027 1.00 60.20 C ANISOU 2019 CB VAL A 254 7603 7033 8239 -725 -1049 20 C ATOM 2020 CG1 VAL A 254 -368.678-182.011 154.196 1.00 59.89 C ANISOU 2020 CG1 VAL A 254 7481 6996 8277 -683 -1162 32 C ATOM 2021 CG2 VAL A 254 -367.853-184.353 154.137 1.00 57.37 C ANISOU 2021 CG2 VAL A 254 7363 6645 7789 -760 -1103 25 C ATOM 2022 N ILE A 255 -367.849-181.491 157.726 1.00 66.29 N ANISOU 2022 N ILE A 255 8250 7865 9072 -686 -798 -16 N ATOM 2023 CA ILE A 255 -368.055-180.266 158.482 1.00 64.86 C ANISOU 2023 CA ILE A 255 7967 7703 8972 -661 -726 -57 C ATOM 2024 C ILE A 255 -366.714-179.689 158.907 1.00 68.25 C ANISOU 2024 C ILE A 255 8487 8155 9288 -612 -681 -29 C ATOM 2025 O ILE A 255 -366.459-178.489 158.754 1.00 65.36 O ANISOU 2025 O ILE A 255 8082 7787 8966 -548 -695 -36 O ATOM 2026 CB ILE A 255 -368.972-180.536 159.685 1.00 65.08 C ANISOU 2026 CB ILE A 255 7904 7752 9072 -748 -597 -121 C ATOM 2027 CG1 ILE A 255 -370.399-180.815 159.204 1.00 70.76 C ANISOU 2027 CG1 ILE A 255 8490 8444 9952 -785 -647 -158 C ATOM 2028 CG2 ILE A 255 -368.960-179.362 160.631 1.00 66.59 C ANISOU 2028 CG2 ILE A 255 8018 7966 9315 -736 -486 -181 C ATOM 2029 CD1 ILE A 255 -371.340-181.186 160.323 1.00 69.36 C ANISOU 2029 CD1 ILE A 255 8221 8286 9848 -884 -508 -227 C ATOM 2030 N ILE A 256 -365.829-180.548 159.422 1.00 64.83 N ANISOU 2030 N ILE A 256 8175 7735 8723 -641 -636 8 N ATOM 2031 CA ILE A 256 -364.504-180.110 159.845 1.00 62.19 C ANISOU 2031 CA ILE A 256 7925 7419 8285 -601 -604 41 C ATOM 2032 C ILE A 256 -363.754-179.485 158.676 1.00 68.83 C ANISOU 2032 C ILE A 256 8806 8241 9106 -512 -696 73 C ATOM 2033 O ILE A 256 -363.165-178.406 158.803 1.00 64.50 O ANISOU 2033 O ILE A 256 8249 7704 8554 -461 -684 74 O ATOM 2034 CB ILE A 256 -363.721-181.285 160.461 1.00 64.73 C ANISOU 2034 CB ILE A 256 8359 7740 8494 -649 -572 93 C ATOM 2035 CG1 ILE A 256 -364.268-181.635 161.847 1.00 58.77 C ANISOU 2035 CG1 ILE A 256 7582 7021 7727 -754 -467 73 C ATOM 2036 CG2 ILE A 256 -362.236-180.947 160.566 1.00 59.93 C ANISOU 2036 CG2 ILE A 256 7837 7138 7796 -594 -578 141 C ATOM 2037 CD1 ILE A 256 -363.813-182.995 162.359 1.00 58.15 C ANISOU 2037 CD1 ILE A 256 7604 6926 7566 -820 -462 141 C ATOM 2038 N MET A 257 -363.773-180.146 157.515 1.00 61.21 N ANISOU 2038 N MET A 257 7889 7246 8123 -503 -785 97 N ATOM 2039 CA MET A 257 -363.047-179.608 156.367 1.00 59.07 C ANISOU 2039 CA MET A 257 7672 6964 7809 -440 -863 126 C ATOM 2040 C MET A 257 -363.625-178.275 155.925 1.00 71.16 C ANISOU 2040 C MET A 257 9110 8494 9433 -402 -920 120 C ATOM 2041 O MET A 257 -362.881-177.321 155.664 1.00 76.26 O ANISOU 2041 O MET A 257 9777 9143 10057 -349 -935 144 O ATOM 2042 CB MET A 257 -363.067-180.597 155.211 1.00 54.39 C ANISOU 2042 CB MET A 257 7153 6345 7168 -463 -936 135 C ATOM 2043 CG MET A 257 -362.267-181.852 155.492 1.00 63.82 C ANISOU 2043 CG MET A 257 8443 7517 8291 -483 -885 144 C ATOM 2044 SD MET A 257 -362.536-183.114 154.240 1.00 81.87 S ANISOU 2044 SD MET A 257 10799 9760 10547 -528 -949 121 S ATOM 2045 CE MET A 257 -361.511-184.446 154.889 1.00 89.15 C ANISOU 2045 CE MET A 257 11804 10631 11436 -537 -872 134 C ATOM 2046 N VAL A 258 -364.950-178.188 155.845 1.00 64.83 N ANISOU 2046 N VAL A 258 8197 7680 8754 -430 -957 92 N ATOM 2047 CA VAL A 258 -365.569-176.963 155.371 1.00 61.15 C ANISOU 2047 CA VAL A 258 7626 7193 8414 -392 -1033 97 C ATOM 2048 C VAL A 258 -365.360-175.843 156.378 1.00 66.26 C ANISOU 2048 C VAL A 258 8203 7844 9130 -355 -939 62 C ATOM 2049 O VAL A 258 -365.056-174.702 156.005 1.00 67.70 O ANISOU 2049 O VAL A 258 8363 8005 9357 -300 -985 86 O ATOM 2050 CB VAL A 258 -367.057-177.206 155.074 1.00 61.87 C ANISOU 2050 CB VAL A 258 7596 7261 8650 -432 -1100 74 C ATOM 2051 CG1 VAL A 258 -367.757-175.887 154.864 1.00 61.24 C ANISOU 2051 CG1 VAL A 258 7373 7143 8752 -388 -1166 76 C ATOM 2052 CG2 VAL A 258 -367.186-178.083 153.843 1.00 58.76 C ANISOU 2052 CG2 VAL A 258 7283 6863 8179 -469 -1222 113 C ATOM 2053 N ILE A 259 -365.495-176.151 157.669 1.00 62.58 N ANISOU 2053 N ILE A 259 7709 7402 8665 -397 -806 6 N ATOM 2054 CA ILE A 259 -365.200-175.151 158.689 1.00 65.14 C ANISOU 2054 CA ILE A 259 7987 7738 9025 -381 -702 -42 C ATOM 2055 C ILE A 259 -363.746-174.706 158.593 1.00 72.56 C ANISOU 2055 C ILE A 259 9039 8692 9840 -333 -705 5 C ATOM 2056 O ILE A 259 -363.442-173.512 158.699 1.00 67.53 O ANISOU 2056 O ILE A 259 8363 8039 9257 -288 -696 -7 O ATOM 2057 CB ILE A 259 -365.528-175.688 160.094 1.00 72.15 C ANISOU 2057 CB ILE A 259 8857 8666 9891 -463 -555 -107 C ATOM 2058 CG1 ILE A 259 -367.037-175.877 160.263 1.00 75.90 C ANISOU 2058 CG1 ILE A 259 9190 9124 10526 -511 -528 -173 C ATOM 2059 CG2 ILE A 259 -364.960-174.753 161.160 1.00 72.49 C ANISOU 2059 CG2 ILE A 259 8894 8734 9915 -465 -444 -158 C ATOM 2060 CD1 ILE A 259 -367.845-174.655 159.920 1.00 84.76 C ANISOU 2060 CD1 ILE A 259 10150 10192 11864 -457 -561 -218 C ATOM 2061 N ALA A 260 -362.824-175.651 158.380 1.00 65.56 N ANISOU 2061 N ALA A 260 8282 7824 8803 -343 -718 56 N ATOM 2062 CA ALA A 260 -361.421-175.269 158.281 1.00 65.00 C ANISOU 2062 CA ALA A 260 8303 7764 8632 -300 -718 98 C ATOM 2063 C ALA A 260 -361.175-174.396 157.060 1.00 69.64 C ANISOU 2063 C ALA A 260 8894 8321 9245 -239 -815 137 C ATOM 2064 O ALA A 260 -360.394-173.441 157.119 1.00 75.75 O ANISOU 2064 O ALA A 260 9680 9093 10009 -199 -805 150 O ATOM 2065 CB ALA A 260 -360.523-176.503 158.240 1.00 54.60 C ANISOU 2065 CB ALA A 260 7104 6456 7186 -318 -713 140 C ATOM 2066 N PHE A 261 -361.833-174.704 155.943 1.00 62.82 N ANISOU 2066 N PHE A 261 8025 7436 8408 -244 -917 162 N ATOM 2067 CA PHE A 261 -361.667-173.870 154.760 1.00 61.63 C ANISOU 2067 CA PHE A 261 7887 7260 8268 -208 -1023 214 C ATOM 2068 C PHE A 261 -362.226-172.475 155.008 1.00 71.97 C ANISOU 2068 C PHE A 261 9076 8534 9736 -171 -1040 203 C ATOM 2069 O PHE A 261 -361.631-171.474 154.595 1.00 65.41 O ANISOU 2069 O PHE A 261 8260 7683 8909 -132 -1077 243 O ATOM 2070 CB PHE A 261 -362.336-174.528 153.558 1.00 57.60 C ANISOU 2070 CB PHE A 261 7403 6742 7742 -243 -1139 244 C ATOM 2071 CG PHE A 261 -362.184-173.762 152.279 1.00 64.63 C ANISOU 2071 CG PHE A 261 8328 7615 8613 -232 -1263 312 C ATOM 2072 CD1 PHE A 261 -361.063-173.931 151.481 1.00 71.81 C ANISOU 2072 CD1 PHE A 261 9373 8544 9367 -239 -1269 347 C ATOM 2073 CD2 PHE A 261 -363.172-172.885 151.861 1.00 69.35 C ANISOU 2073 CD2 PHE A 261 8822 8173 9356 -224 -1375 345 C ATOM 2074 CE1 PHE A 261 -360.922-173.224 150.293 1.00 68.98 C ANISOU 2074 CE1 PHE A 261 9062 8177 8969 -251 -1380 415 C ATOM 2075 CE2 PHE A 261 -363.037-172.178 150.676 1.00 74.17 C ANISOU 2075 CE2 PHE A 261 9475 8767 9941 -229 -1508 429 C ATOM 2076 CZ PHE A 261 -361.910-172.351 149.892 1.00 69.52 C ANISOU 2076 CZ PHE A 261 9039 8209 9166 -249 -1508 465 C ATOM 2077 N LEU A 262 -363.356-172.390 155.711 1.00 70.55 N ANISOU 2077 N LEU A 262 8767 8338 9701 -186 -1004 143 N ATOM 2078 CA LEU A 262 -363.958-171.090 155.985 1.00 75.69 C ANISOU 2078 CA LEU A 262 9280 8936 10542 -149 -1007 115 C ATOM 2079 C LEU A 262 -363.081-170.263 156.916 1.00 78.59 C ANISOU 2079 C LEU A 262 9658 9311 10891 -124 -895 74 C ATOM 2080 O LEU A 262 -363.014-169.034 156.788 1.00 74.68 O ANISOU 2080 O LEU A 262 9105 8764 10507 -79 -921 80 O ATOM 2081 CB LEU A 262 -365.357-171.267 156.571 1.00 70.37 C ANISOU 2081 CB LEU A 262 8455 8242 10041 -178 -968 39 C ATOM 2082 CG LEU A 262 -366.447-171.708 155.593 1.00 68.14 C ANISOU 2082 CG LEU A 262 8111 7930 9848 -195 -1108 79 C ATOM 2083 CD1 LEU A 262 -367.768-171.917 156.317 1.00 69.65 C ANISOU 2083 CD1 LEU A 262 8140 8102 10221 -227 -1043 -9 C ATOM 2084 CD2 LEU A 262 -366.603-170.685 154.477 1.00 65.70 C ANISOU 2084 CD2 LEU A 262 7763 7557 9642 -148 -1275 164 C ATOM 2085 N ILE A 263 -362.396-170.924 157.856 1.00 74.94 N ANISOU 2085 N ILE A 263 9273 8908 10294 -160 -781 39 N ATOM 2086 CA ILE A 263 -361.534-170.224 158.807 1.00 71.23 C ANISOU 2086 CA ILE A 263 8823 8456 9786 -155 -681 0 C ATOM 2087 C ILE A 263 -360.391-169.533 158.080 1.00 72.77 C ANISOU 2087 C ILE A 263 9094 8636 9921 -104 -743 71 C ATOM 2088 O ILE A 263 -359.897-168.481 158.511 1.00 67.13 O ANISOU 2088 O ILE A 263 8357 7903 9245 -81 -702 46 O ATOM 2089 CB ILE A 263 -361.030-171.215 159.876 1.00 74.74 C ANISOU 2089 CB ILE A 263 9346 8969 10084 -219 -579 -25 C ATOM 2090 CG1 ILE A 263 -362.128-171.520 160.889 1.00 80.55 C ANISOU 2090 CG1 ILE A 263 9995 9721 10888 -287 -479 -115 C ATOM 2091 CG2 ILE A 263 -359.810-170.683 160.593 1.00 65.67 C ANISOU 2091 CG2 ILE A 263 8260 7848 8844 -219 -519 -29 C ATOM 2092 CD1 ILE A 263 -361.695-172.517 161.952 1.00 85.53 C ANISOU 2092 CD1 ILE A 263 10714 10420 11366 -369 -393 -121 C ATOM 2093 N CYS A 264 -359.979-170.086 156.953 1.00 72.02 N ANISOU 2093 N CYS A 264 9086 8545 9732 -93 -836 151 N ATOM 2094 CA CYS A 264 -358.986-169.444 156.113 1.00 66.97 C ANISOU 2094 CA CYS A 264 8516 7892 9036 -58 -894 220 C ATOM 2095 C CYS A 264 -359.600-168.497 155.082 1.00 73.36 C ANISOU 2095 C CYS A 264 9270 8639 9963 -30 -1015 273 C ATOM 2096 O CYS A 264 -358.924-167.568 154.631 1.00 89.27 O ANISOU 2096 O CYS A 264 11313 10629 11979 -3 -1049 320 O ATOM 2097 CB CYS A 264 -358.162-170.523 155.416 1.00 69.35 C ANISOU 2097 CB CYS A 264 8946 8231 9173 -74 -914 267 C ATOM 2098 SG CYS A 264 -356.844-169.891 154.433 1.00 83.30 S ANISOU 2098 SG CYS A 264 10808 9994 10851 -50 -951 336 S ATOM 2099 N TRP A 265 -360.868-168.691 154.721 1.00 68.45 N ANISOU 2099 N TRP A 265 8567 7989 9453 -41 -1088 273 N ATOM 2100 CA TRP A 265 -361.485-167.949 153.629 1.00 64.34 C ANISOU 2100 CA TRP A 265 8000 7406 9039 -25 -1239 349 C ATOM 2101 C TRP A 265 -362.183-166.681 154.113 1.00 71.49 C ANISOU 2101 C TRP A 265 8748 8229 10186 17 -1242 317 C ATOM 2102 O TRP A 265 -362.037-165.620 153.497 1.00 79.86 O ANISOU 2102 O TRP A 265 9792 9226 11325 47 -1333 387 O ATOM 2103 CB TRP A 265 -362.478-168.859 152.898 1.00 58.03 C ANISOU 2103 CB TRP A 265 7191 6615 8243 -66 -1340 375 C ATOM 2104 CG TRP A 265 -363.088-168.304 151.639 1.00 64.53 C ANISOU 2104 CG TRP A 265 7991 7388 9140 -73 -1530 476 C ATOM 2105 CD1 TRP A 265 -362.630-168.477 150.362 1.00 66.76 C ANISOU 2105 CD1 TRP A 265 8404 7693 9269 -114 -1643 570 C ATOM 2106 CD2 TRP A 265 -364.297-167.531 151.528 1.00 63.39 C ANISOU 2106 CD2 TRP A 265 7683 7160 9244 -50 -1635 495 C ATOM 2107 NE1 TRP A 265 -363.465-167.845 149.466 1.00 69.97 N ANISOU 2107 NE1 TRP A 265 8751 8041 9792 -127 -1827 663 N ATOM 2108 CE2 TRP A 265 -364.496-167.260 150.155 1.00 64.81 C ANISOU 2108 CE2 TRP A 265 7908 7315 9401 -81 -1833 623 C ATOM 2109 CE3 TRP A 265 -365.222-167.035 152.453 1.00 70.97 C ANISOU 2109 CE3 TRP A 265 8457 8058 10450 -13 -1578 414 C ATOM 2110 CZ2 TRP A 265 -365.581-166.513 149.688 1.00 63.14 C ANISOU 2110 CZ2 TRP A 265 7559 7014 9419 -68 -1999 690 C ATOM 2111 CZ3 TRP A 265 -366.306-166.292 151.982 1.00 72.27 C ANISOU 2111 CZ3 TRP A 265 8470 8126 10863 8 -1723 463 C ATOM 2112 CH2 TRP A 265 -366.473-166.040 150.614 1.00 63.85 C ANISOU 2112 CH2 TRP A 265 7447 7031 9781 -16 -1943 609 C ATOM 2113 N LEU A 266 -362.932-166.780 155.213 1.00 67.47 N ANISOU 2113 N LEU A 266 8122 7712 9799 15 -1135 208 N ATOM 2114 CA LEU A 266 -363.704-165.644 155.709 1.00 69.69 C ANISOU 2114 CA LEU A 266 8234 7904 10341 52 -1116 150 C ATOM 2115 C LEU A 266 -362.864-164.420 156.068 1.00 76.56 C ANISOU 2115 C LEU A 266 9108 8732 11250 90 -1066 137 C ATOM 2116 O LEU A 266 -363.309-163.299 155.762 1.00 69.29 O ANISOU 2116 O LEU A 266 8078 7705 10542 134 -1138 159 O ATOM 2117 CB LEU A 266 -364.554-166.085 156.910 1.00 66.73 C ANISOU 2117 CB LEU A 266 7750 7546 10058 22 -971 12 C ATOM 2118 CG LEU A 266 -365.737-167.000 156.572 1.00 75.70 C ANISOU 2118 CG LEU A 266 8818 8687 11258 -10 -1030 14 C ATOM 2119 CD1 LEU A 266 -366.418-167.542 157.832 1.00 66.73 C ANISOU 2119 CD1 LEU A 266 7600 7585 10170 -59 -859 -124 C ATOM 2120 CD2 LEU A 266 -366.749-166.289 155.664 1.00 72.72 C ANISOU 2120 CD2 LEU A 266 8298 8204 11127 29 -1199 76 C ATOM 2121 N PRO A 267 -361.696-164.531 156.722 1.00 75.92 N ANISOU 2121 N PRO A 267 9135 8716 10994 75 -953 104 N ATOM 2122 CA PRO A 267 -360.944-163.300 157.016 1.00 66.01 C ANISOU 2122 CA PRO A 267 7875 7414 9792 106 -916 91 C ATOM 2123 C PRO A 267 -360.634-162.483 155.773 1.00 71.64 C ANISOU 2123 C PRO A 267 8615 8058 10547 142 -1071 222 C ATOM 2124 O PRO A 267 -360.782-161.255 155.794 1.00 72.24 O ANISOU 2124 O PRO A 267 8603 8034 10812 180 -1093 219 O ATOM 2125 CB PRO A 267 -359.682-163.825 157.708 1.00 65.69 C ANISOU 2125 CB PRO A 267 7967 7471 9522 72 -808 64 C ATOM 2126 CG PRO A 267 -360.153-165.054 158.397 1.00 68.70 C ANISOU 2126 CG PRO A 267 8354 7925 9822 21 -730 2 C ATOM 2127 CD PRO A 267 -361.087-165.695 157.396 1.00 71.82 C ANISOU 2127 CD PRO A 267 8723 8303 10261 26 -850 66 C ATOM 2128 N TYR A 268 -360.244-163.131 154.674 1.00 72.55 N ANISOU 2128 N TYR A 268 8851 8220 10497 122 -1177 336 N ATOM 2129 CA TYR A 268 -360.098-162.407 153.416 1.00 67.90 C ANISOU 2129 CA TYR A 268 8294 7571 9933 131 -1336 472 C ATOM 2130 C TYR A 268 -361.421-161.767 152.990 1.00 77.17 C ANISOU 2130 C TYR A 268 9319 8635 11368 157 -1469 510 C ATOM 2131 O TYR A 268 -361.443-160.623 152.512 1.00 73.38 O ANISOU 2131 O TYR A 268 8794 8056 11033 184 -1566 587 O ATOM 2132 CB TYR A 268 -359.580-163.339 152.326 1.00 67.87 C ANISOU 2132 CB TYR A 268 8447 7646 9694 83 -1410 564 C ATOM 2133 CG TYR A 268 -358.093-163.673 152.376 1.00 76.63 C ANISOU 2133 CG TYR A 268 9701 8832 10583 65 -1318 563 C ATOM 2134 CD1 TYR A 268 -357.647-164.937 152.765 1.00 73.72 C ANISOU 2134 CD1 TYR A 268 9406 8553 10051 41 -1224 508 C ATOM 2135 CD2 TYR A 268 -357.140-162.738 151.989 1.00 68.01 C ANISOU 2135 CD2 TYR A 268 8663 7713 9463 70 -1331 625 C ATOM 2136 CE1 TYR A 268 -356.278-165.245 152.782 1.00 81.91 C ANISOU 2136 CE1 TYR A 268 10556 9647 10921 29 -1147 510 C ATOM 2137 CE2 TYR A 268 -355.790-163.036 152.000 1.00 69.61 C ANISOU 2137 CE2 TYR A 268 8981 7981 9488 53 -1247 622 C ATOM 2138 CZ TYR A 268 -355.351-164.292 152.395 1.00 84.18 C ANISOU 2138 CZ TYR A 268 10885 9909 11188 36 -1156 563 C ATOM 2139 OH TYR A 268 -353.988-164.571 152.388 1.00 94.68 O ANISOU 2139 OH TYR A 268 12310 11291 12375 24 -1079 562 O ATOM 2140 N ALA A 269 -362.539-162.479 153.166 1.00 71.02 N ANISOU 2140 N ALA A 269 8450 7862 10671 148 -1479 464 N ATOM 2141 CA ALA A 269 -363.827-161.914 152.763 1.00 75.85 C ANISOU 2141 CA ALA A 269 8898 8363 11559 174 -1615 502 C ATOM 2142 C ALA A 269 -364.229-160.746 153.657 1.00 76.91 C ANISOU 2142 C ALA A 269 8858 8381 11983 231 -1534 405 C ATOM 2143 O ALA A 269 -364.763-159.741 153.173 1.00 81.36 O ANISOU 2143 O ALA A 269 9309 8814 12791 270 -1664 475 O ATOM 2144 CB ALA A 269 -364.915-162.993 152.770 1.00 68.27 C ANISOU 2144 CB ALA A 269 7875 7440 10625 144 -1637 465 C ATOM 2145 N GLY A 270 -363.978-160.856 154.963 1.00 75.54 N ANISOU 2145 N GLY A 270 8662 8248 11791 230 -1323 246 N ATOM 2146 CA GLY A 270 -364.251-159.741 155.853 1.00 77.66 C ANISOU 2146 CA GLY A 270 8782 8413 12313 271 -1218 129 C ATOM 2147 C GLY A 270 -363.422-158.511 155.527 1.00 85.79 C ANISOU 2147 C GLY A 270 9846 9362 13390 305 -1267 197 C ATOM 2148 O GLY A 270 -363.919-157.384 155.588 1.00 88.73 O ANISOU 2148 O GLY A 270 10070 9587 14055 354 -1297 179 O ATOM 2149 N VAL A 271 -362.149-158.708 155.174 1.00 84.66 N ANISOU 2149 N VAL A 271 9888 9303 12977 279 -1272 273 N ATOM 2150 CA VAL A 271 -361.317-157.578 154.771 1.00 81.40 C ANISOU 2150 CA VAL A 271 9517 8817 12592 301 -1325 351 C ATOM 2151 C VAL A 271 -361.842-156.959 153.482 1.00 84.86 C ANISOU 2151 C VAL A 271 9917 9145 13182 320 -1555 525 C ATOM 2152 O VAL A 271 -361.892-155.729 153.344 1.00 91.29 O ANISOU 2152 O VAL A 271 10650 9820 14215 359 -1615 563 O ATOM 2153 CB VAL A 271 -359.847-158.008 154.628 1.00 72.03 C ANISOU 2153 CB VAL A 271 8530 7750 11087 262 -1278 395 C ATOM 2154 CG1 VAL A 271 -359.109-157.028 153.718 1.00 69.06 C ANISOU 2154 CG1 VAL A 271 8219 7307 10714 267 -1391 534 C ATOM 2155 CG2 VAL A 271 -359.186-158.093 156.002 1.00 62.69 C ANISOU 2155 CG2 VAL A 271 7363 6631 9824 247 -1073 238 C ATOM 2156 N ALA A 272 -362.230-157.795 152.515 1.00 82.27 N ANISOU 2156 N ALA A 272 9650 8872 12736 286 -1696 637 N ATOM 2157 CA ALA A 272 -362.853-157.282 151.298 1.00 91.06 C ANISOU 2157 CA ALA A 272 10727 9887 13985 285 -1937 811 C ATOM 2158 C ALA A 272 -364.052-156.402 151.625 1.00100.16 C ANISOU 2158 C ALA A 272 11640 10869 15548 350 -1990 775 C ATOM 2159 O ALA A 272 -364.168-155.277 151.123 1.00102.72 O ANISOU 2159 O ALA A 272 11901 11050 16080 379 -2126 882 O ATOM 2160 CB ALA A 272 -363.280-158.437 150.395 1.00 89.54 C ANISOU 2160 CB ALA A 272 10618 9788 13616 226 -2062 898 C ATOM 2161 N PHE A 273 -364.953-156.901 152.479 1.00 93.53 N ANISOU 2161 N PHE A 273 10659 10034 14844 369 -1879 623 N ATOM 2162 CA PHE A 273 -366.122-156.124 152.872 1.00 93.97 C ANISOU 2162 CA PHE A 273 10464 9924 15316 431 -1897 558 C ATOM 2163 C PHE A 273 -365.732-154.811 153.541 1.00 97.38 C ANISOU 2163 C PHE A 273 10814 10228 15957 483 -1796 477 C ATOM 2164 O PHE A 273 -366.469-153.824 153.438 1.00 98.85 O ANISOU 2164 O PHE A 273 10813 10230 16514 541 -1883 494 O ATOM 2165 CB PHE A 273 -367.015-156.947 153.803 1.00 89.32 C ANISOU 2165 CB PHE A 273 9754 9385 14800 427 -1743 379 C ATOM 2166 CG PHE A 273 -368.322-156.277 154.141 1.00 97.74 C ANISOU 2166 CG PHE A 273 10543 10282 16312 485 -1756 301 C ATOM 2167 CD1 PHE A 273 -369.390-156.321 153.255 1.00102.14 C ANISOU 2167 CD1 PHE A 273 10975 10754 17080 498 -1983 426 C ATOM 2168 CD2 PHE A 273 -368.487-155.612 155.346 1.00102.60 C ANISOU 2168 CD2 PHE A 273 11017 10823 17146 518 -1540 96 C ATOM 2169 CE1 PHE A 273 -370.596-155.709 153.563 1.00100.89 C ANISOU 2169 CE1 PHE A 273 10538 10428 17368 557 -1997 353 C ATOM 2170 CE2 PHE A 273 -369.693-154.997 155.660 1.00106.53 C ANISOU 2170 CE2 PHE A 273 11242 11154 18082 572 -1532 6 C ATOM 2171 CZ PHE A 273 -370.747-155.046 154.767 1.00104.10 C ANISOU 2171 CZ PHE A 273 10794 10752 18007 598 -1762 136 C ATOM 2172 N TYR A 274 -364.587-154.777 154.230 1.00 94.91 N ANISOU 2172 N TYR A 274 10631 10001 15429 463 -1619 389 N ATOM 2173 CA TYR A 274 -364.070-153.539 154.801 1.00100.85 C ANISOU 2173 CA TYR A 274 11335 10643 16342 498 -1528 317 C ATOM 2174 C TYR A 274 -363.314-152.692 153.784 1.00109.94 C ANISOU 2174 C TYR A 274 12582 11722 17469 501 -1700 514 C ATOM 2175 O TYR A 274 -362.973-151.547 154.090 1.00118.01 O ANISOU 2175 O TYR A 274 13550 12619 18670 533 -1663 482 O ATOM 2176 CB TYR A 274 -363.161-153.841 156.000 1.00103.52 C ANISOU 2176 CB TYR A 274 11769 11105 16459 461 -1277 142 C ATOM 2177 CG TYR A 274 -362.980-152.681 156.966 1.00109.00 C ANISOU 2177 CG TYR A 274 12362 11685 17368 487 -1126 -15 C ATOM 2178 CD1 TYR A 274 -363.828-152.522 158.055 1.00113.43 C ANISOU 2178 CD1 TYR A 274 12751 12194 18155 496 -953 -230 C ATOM 2179 CD2 TYR A 274 -361.953-151.756 156.797 1.00111.67 C ANISOU 2179 CD2 TYR A 274 12779 11971 17680 491 -1144 41 C ATOM 2180 CE1 TYR A 274 -363.668-151.470 158.941 1.00115.59 C ANISOU 2180 CE1 TYR A 274 12937 12363 18620 507 -801 -394 C ATOM 2181 CE2 TYR A 274 -361.789-150.699 157.675 1.00116.64 C ANISOU 2181 CE2 TYR A 274 13318 12492 18507 508 -1006 -112 C ATOM 2182 CZ TYR A 274 -362.647-150.563 158.747 1.00121.82 C ANISOU 2182 CZ TYR A 274 13808 13096 19382 514 -832 -334 C ATOM 2183 OH TYR A 274 -362.483-149.515 159.627 1.00132.66 O ANISOU 2183 OH TYR A 274 15096 14360 20947 519 -680 -506 O ATOM 2184 N ILE A 275 -363.039-153.213 152.592 1.00110.38 N ANISOU 2184 N ILE A 275 12784 11851 17306 457 -1879 709 N ATOM 2185 CA ILE A 275 -362.481-152.381 151.529 1.00107.85 C ANISOU 2185 CA ILE A 275 12547 11453 16979 444 -2060 912 C ATOM 2186 C ILE A 275 -363.583-151.813 150.645 1.00111.62 C ANISOU 2186 C ILE A 275 12888 11767 17755 469 -2314 1071 C ATOM 2187 O ILE A 275 -363.554-150.630 150.295 1.00117.29 O ANISOU 2187 O ILE A 275 13547 12319 18699 496 -2428 1172 O ATOM 2188 CB ILE A 275 -361.446-153.171 150.704 1.00 98.79 C ANISOU 2188 CB ILE A 275 11649 10476 15411 362 -2100 1033 C ATOM 2189 CG1 ILE A 275 -360.180-153.425 151.526 1.00 96.05 C ANISOU 2189 CG1 ILE A 275 11421 10248 14825 345 -1877 905 C ATOM 2190 CG2 ILE A 275 -361.095-152.425 149.418 1.00 94.98 C ANISOU 2190 CG2 ILE A 275 11257 9921 14912 323 -2317 1267 C ATOM 2191 CD1 ILE A 275 -359.122-154.220 150.785 1.00 93.23 C ANISOU 2191 CD1 ILE A 275 11287 10048 14087 271 -1888 998 C ATOM 2192 N PHE A 276 -364.569-152.637 150.281 1.00112.08 N ANISOU 2192 N PHE A 276 12891 11863 17833 457 -2415 1100 N ATOM 2193 CA PHE A 276 -365.709-152.184 149.494 1.00118.47 C ANISOU 2193 CA PHE A 276 13551 12519 18945 478 -2671 1249 C ATOM 2194 C PHE A 276 -366.407-151.034 150.213 1.00125.64 C ANISOU 2194 C PHE A 276 14198 13204 20334 574 -2633 1152 C ATOM 2195 O PHE A 276 -366.295-149.878 149.794 1.00137.97 O ANISOU 2195 O PHE A 276 15714 14598 22109 600 -2765 1274 O ATOM 2196 CB PHE A 276 -366.671-153.349 149.236 1.00123.10 C ANISOU 2196 CB PHE A 276 14097 13192 19482 450 -2740 1246 C ATOM 2197 CG PHE A 276 -367.711-153.057 148.187 1.00132.17 C ANISOU 2197 CG PHE A 276 15139 14218 20860 443 -3053 1445 C ATOM 2198 CD1 PHE A 276 -367.387-153.097 146.838 1.00134.56 C ANISOU 2198 CD1 PHE A 276 15617 14561 20951 355 -3297 1690 C ATOM 2199 CD2 PHE A 276 -369.016-152.749 148.548 1.00133.20 C ANISOU 2199 CD2 PHE A 276 14992 14196 21422 514 -3103 1387 C ATOM 2200 CE1 PHE A 276 -368.341-152.827 145.871 1.00135.57 C ANISOU 2200 CE1 PHE A 276 15654 14579 21278 333 -3608 1889 C ATOM 2201 CE2 PHE A 276 -369.973-152.479 147.585 1.00133.39 C ANISOU 2201 CE2 PHE A 276 14904 14100 21677 507 -3412 1582 C ATOM 2202 CZ PHE A 276 -369.635-152.518 146.246 1.00135.48 C ANISOU 2202 CZ PHE A 276 15356 14409 21713 414 -3676 1841 C ATOM 2203 N THR A 277 -367.128-151.337 151.289 1.00118.35 N ANISOU 2203 N THR A 277 13104 12272 19590 620 -2446 928 N ATOM 2204 CA THR A 277 -367.496-150.313 152.255 1.00113.57 C ANISOU 2204 CA THR A 277 12283 11489 19378 700 -2305 758 C ATOM 2205 C THR A 277 -366.262-149.925 153.068 1.00123.76 C ANISOU 2205 C THR A 277 13699 12836 20490 688 -2078 628 C ATOM 2206 O THR A 277 -365.301-150.688 153.167 1.00131.17 O ANISOU 2206 O THR A 277 14851 13970 21018 627 -1980 615 O ATOM 2207 CB THR A 277 -368.605-150.819 153.182 1.00109.01 C ANISOU 2207 CB THR A 277 11499 10905 19013 730 -2147 542 C ATOM 2208 OG1 THR A 277 -368.026-151.463 154.323 1.00103.85 O ANISOU 2208 OG1 THR A 277 10941 10418 18099 693 -1849 322 O ATOM 2209 CG2 THR A 277 -369.494-151.821 152.453 1.00107.57 C ANISOU 2209 CG2 THR A 277 11295 10791 18787 700 -2320 650 C ATOM 2210 N HIS A 278 -366.289-148.722 153.648 1.00119.59 N ANISOU 2210 N HIS A 278 13027 12124 20287 746 -1998 530 N ATOM 2211 CA HIS A 278 -365.136-148.169 154.374 1.00117.14 C ANISOU 2211 CA HIS A 278 12821 11838 19849 731 -1808 416 C ATOM 2212 C HIS A 278 -363.909-148.066 153.464 1.00118.34 C ANISOU 2212 C HIS A 278 13213 12065 19687 680 -1937 626 C ATOM 2213 O HIS A 278 -362.793-148.419 153.847 1.00126.18 O ANISOU 2213 O HIS A 278 14382 13211 20348 631 -1794 569 O ATOM 2214 CB HIS A 278 -364.800-148.993 155.624 1.00120.37 C ANISOU 2214 CB HIS A 278 13291 12430 20016 689 -1515 170 C ATOM 2215 CG HIS A 278 -365.809-148.890 156.724 1.00136.00 C ANISOU 2215 CG HIS A 278 15048 14334 22294 720 -1325 -80 C ATOM 2216 ND1 HIS A 278 -367.093-149.379 156.607 1.00150.00 N ANISOU 2216 ND1 HIS A 278 16651 16071 24272 745 -1377 -98 N ATOM 2217 CD2 HIS A 278 -365.716-148.375 157.973 1.00141.84 C ANISOU 2217 CD2 HIS A 278 15708 15034 23150 716 -1070 -333 C ATOM 2218 CE1 HIS A 278 -367.751-149.158 157.731 1.00155.10 C ANISOU 2218 CE1 HIS A 278 17117 16654 25160 758 -1153 -354 C ATOM 2219 NE2 HIS A 278 -366.938-148.549 158.577 1.00152.11 N ANISOU 2219 NE2 HIS A 278 16795 16275 24726 737 -961 -504 N ATOM 2220 N GLN A 279 -364.120-147.571 152.243 1.00124.61 N ANISOU 2220 N GLN A 279 14009 12746 20590 684 -2212 876 N ATOM 2221 CA GLN A 279 -363.028-147.482 151.279 1.00139.17 C ANISOU 2221 CA GLN A 279 16082 14661 22134 617 -2338 1086 C ATOM 2222 C GLN A 279 -362.104-146.289 151.517 1.00150.30 C ANISOU 2222 C GLN A 279 17522 15961 23624 625 -2280 1081 C ATOM 2223 O GLN A 279 -360.945-146.325 151.087 1.00155.91 O ANISOU 2223 O GLN A 279 18436 16774 24029 561 -2282 1177 O ATOM 2224 CB GLN A 279 -363.589-147.423 149.855 1.00144.41 C ANISOU 2224 CB GLN A 279 16761 15260 22849 590 -2663 1368 C ATOM 2225 CG GLN A 279 -362.534-147.577 148.770 1.00149.12 C ANISOU 2225 CG GLN A 279 17618 15971 23069 492 -2783 1580 C ATOM 2226 CD GLN A 279 -363.125-147.877 147.410 1.00154.31 C ANISOU 2226 CD GLN A 279 18328 16629 23674 431 -3082 1834 C ATOM 2227 OE1 GLN A 279 -364.328-147.730 147.197 1.00155.51 O ANISOU 2227 OE1 GLN A 279 18301 16653 24132 473 -3246 1889 O ATOM 2228 NE2 GLN A 279 -362.279-148.309 146.479 1.00156.34 N ANISOU 2228 NE2 GLN A 279 18829 17031 23540 323 -3154 1986 N ATOM 2229 N GLY A 280 -362.573-145.248 152.200 1.00151.86 N ANISOU 2229 N GLY A 280 17518 15951 24231 698 -2216 960 N ATOM 2230 CA GLY A 280 -361.804-144.026 152.358 1.00150.67 C ANISOU 2230 CA GLY A 280 17378 15663 24208 706 -2184 965 C ATOM 2231 C GLY A 280 -360.438-144.136 153.013 1.00149.62 C ANISOU 2231 C GLY A 280 17416 15680 23752 654 -1971 846 C ATOM 2232 O GLY A 280 -359.424-143.816 152.387 1.00152.32 O ANISOU 2232 O GLY A 280 17921 16050 23904 601 -2041 996 O ATOM 2233 N SER A 281 -360.396-144.590 154.265 1.00147.61 N ANISOU 2233 N SER A 281 17127 15524 23432 657 -1716 581 N ATOM 2234 CA SER A 281 -359.195-144.474 155.082 1.00143.04 C ANISOU 2234 CA SER A 281 16667 15046 22638 613 -1514 442 C ATOM 2235 C SER A 281 -358.079-145.390 154.576 1.00131.15 C ANISOU 2235 C SER A 281 15404 13769 20658 537 -1529 557 C ATOM 2236 O SER A 281 -358.272-146.244 153.704 1.00125.99 O ANISOU 2236 O SER A 281 14834 13218 19818 515 -1661 709 O ATOM 2237 CB SER A 281 -359.509-144.789 156.545 1.00144.91 C ANISOU 2237 CB SER A 281 16813 15338 22908 616 -1252 139 C ATOM 2238 OG SER A 281 -360.332-143.790 157.124 1.00150.68 O ANISOU 2238 OG SER A 281 17322 15846 24083 675 -1190 -7 O ATOM 2239 N CYS A 282 -356.890-145.189 155.148 1.00124.16 N ANISOU 2239 N CYS A 282 14624 12958 19592 495 -1387 474 N ATOM 2240 CA CYS A 282 -355.701-145.964 154.833 1.00119.80 C ANISOU 2240 CA CYS A 282 14281 12609 18629 426 -1366 549 C ATOM 2241 C CYS A 282 -355.722-147.291 155.594 1.00121.31 C ANISOU 2241 C CYS A 282 14516 13003 18573 405 -1222 406 C ATOM 2242 O CYS A 282 -356.679-147.621 156.298 1.00121.63 O ANISOU 2242 O CYS A 282 14437 13035 18741 433 -1144 262 O ATOM 2243 CB CYS A 282 -354.442-145.162 155.169 1.00123.43 C ANISOU 2243 CB CYS A 282 14813 13050 19033 390 -1282 518 C ATOM 2244 SG CYS A 282 -354.381-143.442 154.556 1.00125.87 S ANISOU 2244 SG CYS A 282 15053 13091 19679 412 -1415 647 S ATOM 2245 N PHE A 283 -354.654-148.071 155.449 1.00126.96 N ANISOU 2245 N PHE A 283 15401 13897 18942 349 -1185 447 N ATOM 2246 CA PHE A 283 -354.519-149.331 156.176 1.00135.86 C ANISOU 2246 CA PHE A 283 16583 15210 19828 322 -1058 330 C ATOM 2247 C PHE A 283 -353.047-149.539 156.494 1.00145.02 C ANISOU 2247 C PHE A 283 17880 16494 20727 268 -967 313 C ATOM 2248 O PHE A 283 -352.223-149.613 155.578 1.00147.02 O ANISOU 2248 O PHE A 283 18248 16788 20824 240 -1045 463 O ATOM 2249 CB PHE A 283 -355.061-150.513 155.361 1.00132.22 C ANISOU 2249 CB PHE A 283 16172 14846 19218 319 -1160 439 C ATOM 2250 CG PHE A 283 -356.450-150.308 154.829 1.00131.37 C ANISOU 2250 CG PHE A 283 15934 14615 19363 366 -1292 497 C ATOM 2251 CD1 PHE A 283 -357.552-150.695 155.570 1.00135.26 C ANISOU 2251 CD1 PHE A 283 16294 15097 20000 395 -1220 356 C ATOM 2252 CD2 PHE A 283 -356.651-149.736 153.585 1.00130.18 C ANISOU 2252 CD2 PHE A 283 15793 14361 19309 371 -1493 699 C ATOM 2253 CE1 PHE A 283 -358.829-150.510 155.082 1.00140.83 C ANISOU 2253 CE1 PHE A 283 16862 15684 20964 440 -1346 409 C ATOM 2254 CE2 PHE A 283 -357.924-149.547 153.092 1.00136.05 C ANISOU 2254 CE2 PHE A 283 16408 14985 20299 411 -1638 766 C ATOM 2255 CZ PHE A 283 -359.016-149.934 153.840 1.00141.12 C ANISOU 2255 CZ PHE A 283 16902 15612 21107 451 -1565 619 C ATOM 2256 N GLY A 284 -352.716-149.644 157.779 1.00149.52 N ANISOU 2256 N GLY A 284 18436 17125 21248 243 -805 132 N ATOM 2257 CA GLY A 284 -351.344-149.807 158.191 1.00152.39 C ANISOU 2257 CA GLY A 284 18909 17598 21394 189 -728 110 C ATOM 2258 C GLY A 284 -350.782-151.169 157.803 1.00148.57 C ANISOU 2258 C GLY A 284 18547 17286 20616 163 -745 188 C ATOM 2259 O GLY A 284 -351.403-151.917 157.042 1.00148.89 O ANISOU 2259 O GLY A 284 18603 17356 20611 182 -826 276 O ATOM 2260 N PRO A 285 -349.598-151.510 158.324 1.00137.25 N ANISOU 2260 N PRO A 285 17194 15960 18995 117 -670 153 N ATOM 2261 CA PRO A 285 -349.056-152.859 158.101 1.00135.61 C ANISOU 2261 CA PRO A 285 17083 15903 18538 96 -670 205 C ATOM 2262 C PRO A 285 -350.002-153.999 158.512 1.00160.14 C ANISOU 2262 C PRO A 285 20170 19083 21593 103 -646 147 C ATOM 2263 O PRO A 285 -349.772-155.149 158.118 1.00162.79 O ANISOU 2263 O PRO A 285 20578 19518 21758 96 -667 206 O ATOM 2264 CB PRO A 285 -347.763-152.866 158.936 1.00111.54 C ANISOU 2264 CB PRO A 285 14082 12931 15365 47 -587 143 C ATOM 2265 CG PRO A 285 -347.905-151.740 159.888 1.00110.66 C ANISOU 2265 CG PRO A 285 13897 12736 15412 31 -520 15 C ATOM 2266 CD PRO A 285 -348.715-150.696 159.183 1.00119.17 C ANISOU 2266 CD PRO A 285 14901 13652 16727 79 -586 59 C ATOM 2267 N ILE A 286 -351.041-153.699 159.304 1.00174.98 N ANISOU 2267 N ILE A 286 21950 20910 23626 112 -591 25 N ATOM 2268 CA ILE A 286 -352.155-154.610 159.561 1.00166.85 C ANISOU 2268 CA ILE A 286 20879 19922 22596 120 -575 -23 C ATOM 2269 C ILE A 286 -353.305-154.211 158.637 1.00168.59 C ANISOU 2269 C ILE A 286 21014 20024 23017 175 -681 46 C ATOM 2270 O ILE A 286 -354.295-153.608 159.072 1.00186.37 O ANISOU 2270 O ILE A 286 23141 22178 25492 198 -649 -47 O ATOM 2271 CB ILE A 286 -352.570-154.584 161.051 1.00155.30 C ANISOU 2271 CB ILE A 286 19357 18483 21167 77 -433 -211 C ATOM 2272 CG1 ILE A 286 -352.618-153.144 161.565 1.00149.92 C ANISOU 2272 CG1 ILE A 286 18593 17679 20692 77 -375 -316 C ATOM 2273 CG2 ILE A 286 -351.570-155.320 161.906 1.00150.71 C ANISOU 2273 CG2 ILE A 286 18872 18040 20350 9 -364 -249 C ATOM 2274 CD1 ILE A 286 -352.936-152.982 163.041 1.00147.11 C ANISOU 2274 CD1 ILE A 286 18190 17347 20358 13 -216 -522 C ATOM 2275 N PHE A 287 -353.191-154.566 157.360 1.00143.39 N ANISOU 2275 N PHE A 287 17889 16842 19751 190 -807 207 N ATOM 2276 CA PHE A 287 -354.013-153.974 156.301 1.00117.04 C ANISOU 2276 CA PHE A 287 14494 13385 16592 228 -948 318 C ATOM 2277 C PHE A 287 -355.534-154.381 156.377 1.00103.51 C ANISOU 2277 C PHE A 287 12665 11635 15030 257 -978 275 C ATOM 2278 O PHE A 287 -356.319-153.510 156.760 1.00100.48 O ANISOU 2278 O PHE A 287 12141 11123 14911 291 -967 205 O ATOM 2279 CB PHE A 287 -353.352-154.276 154.941 1.00104.93 C ANISOU 2279 CB PHE A 287 13087 11891 14890 207 -1065 496 C ATOM 2280 CG PHE A 287 -353.665-153.281 153.862 1.00 99.36 C ANISOU 2280 CG PHE A 287 12360 11056 14336 219 -1217 640 C ATOM 2281 CD1 PHE A 287 -352.758-152.280 153.533 1.00102.86 C ANISOU 2281 CD1 PHE A 287 12847 11439 14797 202 -1234 708 C ATOM 2282 CD2 PHE A 287 -354.858-153.357 153.164 1.00 95.89 C ANISOU 2282 CD2 PHE A 287 11859 10553 14022 239 -1353 718 C ATOM 2283 CE1 PHE A 287 -353.050-151.364 152.535 1.00109.10 C ANISOU 2283 CE1 PHE A 287 13625 12103 15724 203 -1386 858 C ATOM 2284 CE2 PHE A 287 -355.159-152.453 152.169 1.00102.07 C ANISOU 2284 CE2 PHE A 287 12625 11212 14945 241 -1517 871 C ATOM 2285 CZ PHE A 287 -354.257-151.453 151.851 1.00111.93 C ANISOU 2285 CZ PHE A 287 13925 12397 16206 221 -1534 946 C ATOM 2286 N MET A 288 -356.030-155.597 156.079 1.00 92.34 N ANISOU 2286 N MET A 288 11283 10311 13493 246 -1009 302 N ATOM 2287 CA MET A 288 -355.422-156.821 155.536 1.00 88.51 C ANISOU 2287 CA MET A 288 10938 9960 12732 210 -1029 374 C ATOM 2288 C MET A 288 -354.089-157.233 156.145 1.00107.53 C ANISOU 2288 C MET A 288 13450 12475 14933 177 -918 330 C ATOM 2289 O MET A 288 -353.788-156.882 157.290 1.00128.16 O ANISOU 2289 O MET A 288 16028 15093 17574 167 -803 212 O ATOM 2290 CB MET A 288 -355.277-156.706 154.014 1.00 90.32 C ANISOU 2290 CB MET A 288 11244 10165 12909 201 -1191 553 C ATOM 2291 CG MET A 288 -355.802-157.903 153.253 1.00109.35 C ANISOU 2291 CG MET A 288 13708 12649 15192 178 -1267 614 C ATOM 2292 SD MET A 288 -355.881-157.702 151.471 1.00119.94 S ANISOU 2292 SD MET A 288 15135 13959 16477 141 -1469 816 S ATOM 2293 CE MET A 288 -356.681-159.233 150.997 1.00106.18 C ANISOU 2293 CE MET A 288 13430 12309 14606 110 -1518 821 C ATOM 2294 N THR A 289 -353.325-158.041 155.407 1.00 81.70 N ANISOU 2294 N THR A 289 10301 9288 11454 152 -950 417 N ATOM 2295 CA THR A 289 -352.136-158.707 155.938 1.00 79.25 C ANISOU 2295 CA THR A 289 10075 9081 10956 123 -856 381 C ATOM 2296 C THR A 289 -352.472-159.541 157.177 1.00 73.79 C ANISOU 2296 C THR A 289 9354 8457 10226 108 -759 264 C ATOM 2297 O THR A 289 -351.654-160.346 157.633 1.00 77.85 O ANISOU 2297 O THR A 289 9934 9058 10587 82 -703 247 O ATOM 2298 CB THR A 289 -351.013-157.701 156.264 1.00 76.28 C ANISOU 2298 CB THR A 289 9712 8677 10593 116 -812 372 C ATOM 2299 OG1 THR A 289 -351.398-156.868 157.367 1.00 80.02 O ANISOU 2299 OG1 THR A 289 10092 9094 11219 122 -744 258 O ATOM 2300 CG2 THR A 289 -350.664-156.835 155.049 1.00 77.54 C ANISOU 2300 CG2 THR A 289 9908 8767 10788 117 -905 497 C ATOM 2301 N ILE A 290 -353.657-159.340 157.746 1.00 70.65 N ANISOU 2301 N ILE A 290 8854 8015 9974 118 -737 184 N ATOM 2302 CA ILE A 290 -354.141-160.123 158.878 1.00 75.78 C ANISOU 2302 CA ILE A 290 9477 8729 10586 87 -641 75 C ATOM 2303 C ILE A 290 -354.638-161.463 158.344 1.00 72.96 C ANISOU 2303 C ILE A 290 9159 8430 10132 81 -688 125 C ATOM 2304 O ILE A 290 -354.225-162.507 158.869 1.00 70.61 O ANISOU 2304 O ILE A 290 8924 8220 9686 46 -637 107 O ATOM 2305 CB ILE A 290 -355.220-159.364 159.670 1.00 76.89 C ANISOU 2305 CB ILE A 290 9485 8797 10932 90 -577 -47 C ATOM 2306 CG1 ILE A 290 -354.643-158.071 160.249 1.00 87.72 C ANISOU 2306 CG1 ILE A 290 10826 10109 12393 87 -519 -113 C ATOM 2307 CG2 ILE A 290 -355.784-160.220 160.786 1.00 79.64 C ANISOU 2307 CG2 ILE A 290 9816 9221 11225 38 -470 -157 C ATOM 2308 CD1 ILE A 290 -355.662-157.251 161.010 1.00 89.39 C ANISOU 2308 CD1 ILE A 290 10900 10233 12830 89 -437 -254 C ATOM 2309 N PRO A 291 -355.504-161.498 157.316 1.00 71.20 N ANISOU 2309 N PRO A 291 8904 8157 9991 107 -792 193 N ATOM 2310 CA PRO A 291 -355.801-162.796 156.685 1.00 64.28 C ANISOU 2310 CA PRO A 291 8085 7339 8998 92 -842 244 C ATOM 2311 C PRO A 291 -354.561-163.538 156.224 1.00 63.13 C ANISOU 2311 C PRO A 291 8071 7264 8650 74 -841 305 C ATOM 2312 O PRO A 291 -354.462-164.755 156.425 1.00 72.01 O ANISOU 2312 O PRO A 291 9245 8454 9661 51 -810 292 O ATOM 2313 CB PRO A 291 -356.703-162.411 155.504 1.00 66.36 C ANISOU 2313 CB PRO A 291 8306 7531 9378 114 -981 327 C ATOM 2314 CG PRO A 291 -357.376-161.182 155.956 1.00 73.14 C ANISOU 2314 CG PRO A 291 9031 8288 10471 146 -975 277 C ATOM 2315 CD PRO A 291 -356.361-160.429 156.760 1.00 67.05 C ANISOU 2315 CD PRO A 291 8278 7517 9682 145 -875 220 C ATOM 2316 N ALA A 292 -353.611-162.843 155.594 1.00 63.89 N ANISOU 2316 N ALA A 292 8220 7342 8714 82 -870 369 N ATOM 2317 CA ALA A 292 -352.366-163.502 155.213 1.00 65.45 C ANISOU 2317 CA ALA A 292 8525 7600 8744 65 -847 408 C ATOM 2318 C ALA A 292 -351.645-164.043 156.439 1.00 68.27 C ANISOU 2318 C ALA A 292 8891 8014 9035 51 -748 341 C ATOM 2319 O ALA A 292 -351.173-165.188 156.439 1.00 70.66 O ANISOU 2319 O ALA A 292 9250 8369 9228 37 -726 348 O ATOM 2320 CB ALA A 292 -351.472-162.534 154.444 1.00 66.63 C ANISOU 2320 CB ALA A 292 8716 7716 8885 66 -877 478 C ATOM 2321 N PHE A 293 -351.582-163.240 157.506 1.00 67.20 N ANISOU 2321 N PHE A 293 8699 7863 8972 48 -692 275 N ATOM 2322 CA PHE A 293 -350.888-163.659 158.719 1.00 72.98 C ANISOU 2322 CA PHE A 293 9446 8653 9629 17 -616 221 C ATOM 2323 C PHE A 293 -351.420-164.993 159.230 1.00 64.80 C ANISOU 2323 C PHE A 293 8423 7671 8526 -11 -595 198 C ATOM 2324 O PHE A 293 -350.646-165.854 159.661 1.00 65.75 O ANISOU 2324 O PHE A 293 8594 7842 8546 -33 -575 212 O ATOM 2325 CB PHE A 293 -351.018-162.576 159.794 1.00 70.25 C ANISOU 2325 CB PHE A 293 9039 8284 9370 -1 -557 135 C ATOM 2326 CG PHE A 293 -350.092-162.759 160.964 1.00 72.15 C ANISOU 2326 CG PHE A 293 9310 8586 9519 -51 -498 94 C ATOM 2327 CD1 PHE A 293 -348.757-162.388 160.872 1.00 72.12 C ANISOU 2327 CD1 PHE A 293 9342 8589 9471 -51 -506 133 C ATOM 2328 CD2 PHE A 293 -350.559-163.273 162.165 1.00 73.33 C ANISOU 2328 CD2 PHE A 293 9450 8785 9625 -109 -439 21 C ATOM 2329 CE1 PHE A 293 -347.902-162.544 161.949 1.00 70.88 C ANISOU 2329 CE1 PHE A 293 9208 8487 9237 -103 -473 106 C ATOM 2330 CE2 PHE A 293 -349.703-163.428 163.250 1.00 78.07 C ANISOU 2330 CE2 PHE A 293 10089 9446 10128 -172 -405 -2 C ATOM 2331 CZ PHE A 293 -348.377-163.061 163.140 1.00 72.94 C ANISOU 2331 CZ PHE A 293 9471 8801 9444 -167 -431 43 C ATOM 2332 N PHE A 294 -352.732-165.195 159.167 1.00 65.91 N ANISOU 2332 N PHE A 294 8513 7793 8736 -10 -605 169 N ATOM 2333 CA PHE A 294 -353.321-166.402 159.736 1.00 72.77 C ANISOU 2333 CA PHE A 294 9389 8709 9551 -47 -577 142 C ATOM 2334 C PHE A 294 -353.498-167.538 158.737 1.00 61.62 C ANISOU 2334 C PHE A 294 8027 7305 8083 -35 -636 204 C ATOM 2335 O PHE A 294 -353.401-168.698 159.138 1.00 72.93 O ANISOU 2335 O PHE A 294 9497 8776 9438 -65 -616 206 O ATOM 2336 CB PHE A 294 -354.658-166.069 160.403 1.00 73.33 C ANISOU 2336 CB PHE A 294 9367 8760 9733 -68 -533 55 C ATOM 2337 CG PHE A 294 -354.499-165.306 161.685 1.00 84.34 C ANISOU 2337 CG PHE A 294 10730 10168 11148 -110 -440 -37 C ATOM 2338 CD1 PHE A 294 -353.870-165.888 162.775 1.00 87.54 C ANISOU 2338 CD1 PHE A 294 11193 10646 11423 -178 -385 -57 C ATOM 2339 CD2 PHE A 294 -354.947-163.998 161.794 1.00 95.77 C ANISOU 2339 CD2 PHE A 294 12092 11550 12747 -90 -414 -102 C ATOM 2340 CE1 PHE A 294 -353.705-165.187 163.954 1.00 96.91 C ANISOU 2340 CE1 PHE A 294 12364 11854 12603 -237 -301 -146 C ATOM 2341 CE2 PHE A 294 -354.786-163.291 162.971 1.00 93.19 C ANISOU 2341 CE2 PHE A 294 11740 11233 12434 -140 -316 -206 C ATOM 2342 CZ PHE A 294 -354.165-163.886 164.052 1.00 98.15 C ANISOU 2342 CZ PHE A 294 12439 11949 12904 -221 -258 -231 C ATOM 2343 N ALA A 295 -353.711-167.244 157.446 1.00 54.63 N ANISOU 2343 N ALA A 295 7148 6380 7227 -4 -711 256 N ATOM 2344 CA ALA A 295 -353.713-168.293 156.426 1.00 57.18 C ANISOU 2344 CA ALA A 295 7537 6716 7474 -7 -760 305 C ATOM 2345 C ALA A 295 -352.414-169.091 156.393 1.00 66.12 C ANISOU 2345 C ALA A 295 8748 7879 8494 -12 -726 327 C ATOM 2346 O ALA A 295 -352.406-170.207 155.857 1.00 64.14 O ANISOU 2346 O ALA A 295 8546 7639 8186 -23 -737 341 O ATOM 2347 CB ALA A 295 -353.956-167.700 155.040 1.00 50.20 C ANISOU 2347 CB ALA A 295 6667 5794 6611 6 -849 365 C ATOM 2348 N LYS A 296 -351.314-168.539 156.921 1.00 62.57 N ANISOU 2348 N LYS A 296 8305 7439 8031 -4 -686 328 N ATOM 2349 CA LYS A 296 -350.043-169.262 156.910 1.00 58.96 C ANISOU 2349 CA LYS A 296 7900 7000 7503 -4 -658 351 C ATOM 2350 C LYS A 296 -350.150-170.563 157.690 1.00 59.65 C ANISOU 2350 C LYS A 296 7997 7109 7559 -28 -640 340 C ATOM 2351 O LYS A 296 -349.559-171.577 157.297 1.00 54.55 O ANISOU 2351 O LYS A 296 7390 6456 6879 -24 -636 359 O ATOM 2352 CB LYS A 296 -348.916-168.393 157.492 1.00 57.85 C ANISOU 2352 CB LYS A 296 7747 6864 7370 1 -629 353 C ATOM 2353 CG LYS A 296 -348.525-167.172 156.654 1.00 67.98 C ANISOU 2353 CG LYS A 296 9032 8118 8679 20 -644 378 C ATOM 2354 CD LYS A 296 -347.386-166.372 157.295 1.00 67.53 C ANISOU 2354 CD LYS A 296 8958 8064 8635 18 -613 375 C ATOM 2355 CE LYS A 296 -347.177-165.039 156.575 1.00 72.63 C ANISOU 2355 CE LYS A 296 9600 8671 9324 29 -628 399 C ATOM 2356 NZ LYS A 296 -347.007-165.194 155.098 1.00 82.30 N ANISOU 2356 NZ LYS A 296 10881 9885 10505 29 -652 452 N ATOM 2357 N THR A 297 -350.908-170.556 158.797 1.00 48.61 N ANISOU 2357 N THR A 297 6560 5730 6178 -59 -622 305 N ATOM 2358 CA THR A 297 -351.050-171.759 159.614 1.00 61.90 C ANISOU 2358 CA THR A 297 8260 7434 7825 -98 -609 308 C ATOM 2359 C THR A 297 -351.743-172.900 158.880 1.00 59.91 C ANISOU 2359 C THR A 297 8030 7163 7568 -99 -632 315 C ATOM 2360 O THR A 297 -351.786-174.010 159.416 1.00 61.89 O ANISOU 2360 O THR A 297 8301 7418 7798 -130 -627 329 O ATOM 2361 CB THR A 297 -351.830-171.482 160.908 1.00 61.62 C ANISOU 2361 CB THR A 297 8187 7431 7793 -154 -571 261 C ATOM 2362 OG1 THR A 297 -353.145-171.006 160.600 1.00 66.91 O ANISOU 2362 OG1 THR A 297 8804 8087 8533 -151 -566 213 O ATOM 2363 CG2 THR A 297 -351.110-170.465 161.754 1.00 51.39 C ANISOU 2363 CG2 THR A 297 6881 6157 6488 -172 -544 242 C ATOM 2364 N SER A 298 -352.294-172.663 157.684 1.00 57.21 N ANISOU 2364 N SER A 298 7689 6800 7247 -76 -665 312 N ATOM 2365 CA SER A 298 -352.888-173.761 156.935 1.00 59.80 C ANISOU 2365 CA SER A 298 8047 7113 7561 -87 -691 313 C ATOM 2366 C SER A 298 -351.839-174.809 156.583 1.00 62.25 C ANISOU 2366 C SER A 298 8414 7405 7833 -80 -676 332 C ATOM 2367 O SER A 298 -352.168-175.997 156.461 1.00 63.36 O ANISOU 2367 O SER A 298 8577 7526 7970 -99 -679 327 O ATOM 2368 CB SER A 298 -353.600-173.247 155.682 1.00 55.24 C ANISOU 2368 CB SER A 298 7469 6521 6998 -79 -746 315 C ATOM 2369 OG SER A 298 -352.690-172.731 154.719 1.00 62.35 O ANISOU 2369 OG SER A 298 8416 7414 7860 -59 -755 341 O ATOM 2370 N ALA A 299 -350.570-174.403 156.460 1.00 50.62 N ANISOU 2370 N ALA A 299 6955 5927 6351 -52 -654 350 N ATOM 2371 CA ALA A 299 -349.504-175.372 156.222 1.00 49.66 C ANISOU 2371 CA ALA A 299 6863 5774 6230 -40 -629 359 C ATOM 2372 C ALA A 299 -349.389-176.386 157.352 1.00 52.84 C ANISOU 2372 C ALA A 299 7255 6164 6657 -58 -632 382 C ATOM 2373 O ALA A 299 -348.771-177.437 157.165 1.00 55.47 O ANISOU 2373 O ALA A 299 7602 6450 7022 -48 -622 390 O ATOM 2374 CB ALA A 299 -348.165-174.660 156.036 1.00 50.39 C ANISOU 2374 CB ALA A 299 6952 5865 6329 -10 -602 372 C ATOM 2375 N VAL A 300 -349.970-176.098 158.511 1.00 54.98 N ANISOU 2375 N VAL A 300 7502 6470 6920 -91 -642 392 N ATOM 2376 CA VAL A 300 -349.956-177.009 159.646 1.00 53.49 C ANISOU 2376 CA VAL A 300 7314 6277 6731 -133 -653 428 C ATOM 2377 C VAL A 300 -351.301-177.715 159.827 1.00 65.13 C ANISOU 2377 C VAL A 300 8793 7755 8198 -179 -656 411 C ATOM 2378 O VAL A 300 -351.351-178.942 159.933 1.00 58.03 O ANISOU 2378 O VAL A 300 7915 6817 7316 -199 -668 436 O ATOM 2379 CB VAL A 300 -349.533-176.257 160.927 1.00 55.93 C ANISOU 2379 CB VAL A 300 7607 6633 7012 -166 -655 451 C ATOM 2380 CG1 VAL A 300 -349.555-177.188 162.126 1.00 55.67 C ANISOU 2380 CG1 VAL A 300 7591 6604 6957 -232 -680 504 C ATOM 2381 CG2 VAL A 300 -348.143-175.656 160.745 1.00 61.53 C ANISOU 2381 CG2 VAL A 300 8304 7332 7741 -124 -660 472 C ATOM 2382 N TYR A 301 -352.416-176.969 159.843 1.00 61.56 N ANISOU 2382 N TYR A 301 8312 7339 7739 -197 -643 368 N ATOM 2383 CA TYR A 301 -353.675-177.622 160.190 1.00 58.90 C ANISOU 2383 CA TYR A 301 7964 7008 7406 -251 -638 350 C ATOM 2384 C TYR A 301 -354.317-178.358 159.015 1.00 63.81 C ANISOU 2384 C TYR A 301 8598 7592 8053 -238 -662 330 C ATOM 2385 O TYR A 301 -355.114-179.274 159.243 1.00 65.99 O ANISOU 2385 O TYR A 301 8876 7857 8339 -284 -663 327 O ATOM 2386 CB TYR A 301 -354.671-176.628 160.819 1.00 55.47 C ANISOU 2386 CB TYR A 301 7475 6620 6983 -284 -604 300 C ATOM 2387 CG TYR A 301 -355.209-175.522 159.936 1.00 54.52 C ANISOU 2387 CG TYR A 301 7307 6495 6914 -237 -617 258 C ATOM 2388 CD1 TYR A 301 -356.162-175.785 158.958 1.00 60.92 C ANISOU 2388 CD1 TYR A 301 8099 7283 7766 -229 -654 242 C ATOM 2389 CD2 TYR A 301 -354.819-174.198 160.127 1.00 52.03 C ANISOU 2389 CD2 TYR A 301 6963 6193 6614 -212 -601 241 C ATOM 2390 CE1 TYR A 301 -356.672-174.778 158.164 1.00 60.52 C ANISOU 2390 CE1 TYR A 301 8004 7221 7772 -194 -690 225 C ATOM 2391 CE2 TYR A 301 -355.332-173.178 159.336 1.00 49.72 C ANISOU 2391 CE2 TYR A 301 6624 5881 6388 -172 -626 219 C ATOM 2392 CZ TYR A 301 -356.256-173.479 158.356 1.00 67.42 C ANISOU 2392 CZ TYR A 301 8848 8098 8671 -164 -677 218 C ATOM 2393 OH TYR A 301 -356.781-172.492 157.555 1.00 70.79 O ANISOU 2393 OH TYR A 301 9228 8499 9170 -131 -728 216 O ATOM 2394 N ASN A 302 -353.983-178.009 157.769 1.00 61.50 N ANISOU 2394 N ASN A 302 8324 7283 7762 -190 -682 317 N ATOM 2395 CA ASN A 302 -354.507-178.797 156.655 1.00 55.49 C ANISOU 2395 CA ASN A 302 7591 6490 7002 -197 -707 294 C ATOM 2396 C ASN A 302 -353.963-180.220 156.646 1.00 62.20 C ANISOU 2396 C ASN A 302 8484 7287 7863 -207 -695 305 C ATOM 2397 O ASN A 302 -354.770-181.164 156.574 1.00 61.67 O ANISOU 2397 O ASN A 302 8424 7197 7812 -246 -706 291 O ATOM 2398 CB ASN A 302 -354.260-178.076 155.330 1.00 50.02 C ANISOU 2398 CB ASN A 302 6922 5799 6284 -168 -731 281 C ATOM 2399 CG ASN A 302 -355.385-177.151 154.985 1.00 61.00 C ANISOU 2399 CG ASN A 302 8269 7214 7695 -176 -778 272 C ATOM 2400 OD1 ASN A 302 -356.477-177.275 155.540 1.00 68.17 O ANISOU 2400 OD1 ASN A 302 9124 8130 8648 -204 -787 258 O ATOM 2401 ND2 ASN A 302 -355.141-176.213 154.079 1.00 58.48 N ANISOU 2401 ND2 ASN A 302 7964 6901 7354 -156 -810 284 N ATOM 2402 N PRO A 303 -352.649-180.462 156.715 1.00 62.60 N ANISOU 2402 N PRO A 303 8554 7306 7926 -173 -674 327 N ATOM 2403 CA PRO A 303 -352.196-181.860 156.804 1.00 55.00 C ANISOU 2403 CA PRO A 303 7614 6271 7013 -179 -667 339 C ATOM 2404 C PRO A 303 -352.707-182.570 158.045 1.00 61.01 C ANISOU 2404 C PRO A 303 8364 7025 7792 -230 -684 388 C ATOM 2405 O PRO A 303 -352.919-183.788 158.005 1.00 64.33 O ANISOU 2405 O PRO A 303 8803 7383 8257 -254 -691 393 O ATOM 2406 CB PRO A 303 -350.661-181.745 156.796 1.00 58.38 C ANISOU 2406 CB PRO A 303 8037 6666 7477 -129 -645 359 C ATOM 2407 CG PRO A 303 -350.367-180.316 157.166 1.00 68.38 C ANISOU 2407 CG PRO A 303 9279 8001 8700 -112 -646 376 C ATOM 2408 CD PRO A 303 -351.514-179.515 156.647 1.00 61.15 C ANISOU 2408 CD PRO A 303 8363 7137 7733 -129 -657 340 C ATOM 2409 N VAL A 304 -352.935-181.847 159.144 1.00 58.94 N ANISOU 2409 N VAL A 304 8078 6824 7494 -258 -687 421 N ATOM 2410 CA VAL A 304 -353.503-182.486 160.329 1.00 58.49 C ANISOU 2410 CA VAL A 304 8022 6774 7428 -331 -695 465 C ATOM 2411 C VAL A 304 -354.907-182.999 160.031 1.00 69.01 C ANISOU 2411 C VAL A 304 9347 8105 8766 -378 -689 424 C ATOM 2412 O VAL A 304 -355.266-184.121 160.408 1.00 71.78 O ANISOU 2412 O VAL A 304 9718 8416 9141 -429 -698 454 O ATOM 2413 CB VAL A 304 -353.493-181.516 161.527 1.00 58.74 C ANISOU 2413 CB VAL A 304 8036 6882 7401 -371 -682 486 C ATOM 2414 CG1 VAL A 304 -354.338-182.063 162.650 1.00 63.71 C ANISOU 2414 CG1 VAL A 304 8675 7537 7996 -472 -672 514 C ATOM 2415 CG2 VAL A 304 -352.064-181.276 162.025 1.00 55.54 C ANISOU 2415 CG2 VAL A 304 7640 6469 6993 -346 -707 546 C ATOM 2416 N ILE A 305 -355.704-182.207 159.309 1.00 63.85 N ANISOU 2416 N ILE A 305 8665 7491 8106 -362 -683 362 N ATOM 2417 CA ILE A 305 -357.100-182.550 159.061 1.00 64.40 C ANISOU 2417 CA ILE A 305 8708 7565 8195 -409 -686 322 C ATOM 2418 C ILE A 305 -357.223-183.597 157.957 1.00 61.21 C ANISOU 2418 C ILE A 305 8341 7098 7818 -405 -713 299 C ATOM 2419 O ILE A 305 -357.942-184.587 158.109 1.00 68.79 O ANISOU 2419 O ILE A 305 9305 8027 8806 -459 -717 297 O ATOM 2420 CB ILE A 305 -357.903-181.277 158.732 1.00 69.92 C ANISOU 2420 CB ILE A 305 9347 8316 8903 -394 -688 274 C ATOM 2421 CG1 ILE A 305 -358.075-180.439 159.996 1.00 70.74 C ANISOU 2421 CG1 ILE A 305 9408 8476 8996 -424 -639 272 C ATOM 2422 CG2 ILE A 305 -359.262-181.626 158.147 1.00 73.97 C ANISOU 2422 CG2 ILE A 305 9822 8822 9459 -429 -714 233 C ATOM 2423 CD1 ILE A 305 -358.564-179.063 159.734 1.00 70.69 C ANISOU 2423 CD1 ILE A 305 9334 8499 9025 -392 -636 226 C ATOM 2424 N TYR A 306 -356.526-183.400 156.835 1.00 58.20 N ANISOU 2424 N TYR A 306 7991 6695 7426 -352 -724 273 N ATOM 2425 CA TYR A 306 -356.676-184.263 155.669 1.00 56.17 C ANISOU 2425 CA TYR A 306 7776 6387 7178 -361 -739 227 C ATOM 2426 C TYR A 306 -355.796-185.512 155.689 1.00 67.08 C ANISOU 2426 C TYR A 306 9199 7681 8608 -354 -715 235 C ATOM 2427 O TYR A 306 -356.057-186.445 154.920 1.00 69.02 O ANISOU 2427 O TYR A 306 9478 7871 8875 -379 -716 186 O ATOM 2428 CB TYR A 306 -356.380-183.483 154.386 1.00 52.10 C ANISOU 2428 CB TYR A 306 7287 5896 6613 -330 -753 188 C ATOM 2429 CG TYR A 306 -357.450-182.474 154.032 1.00 66.44 C ANISOU 2429 CG TYR A 306 9062 7771 8410 -345 -805 181 C ATOM 2430 CD1 TYR A 306 -357.448-181.197 154.589 1.00 60.83 C ANISOU 2430 CD1 TYR A 306 8300 7109 7704 -314 -805 208 C ATOM 2431 CD2 TYR A 306 -358.465-182.803 153.151 1.00 67.00 C ANISOU 2431 CD2 TYR A 306 9140 7842 8474 -392 -860 147 C ATOM 2432 CE1 TYR A 306 -358.437-180.283 154.274 1.00 66.37 C ANISOU 2432 CE1 TYR A 306 8948 7844 8426 -321 -858 203 C ATOM 2433 CE2 TYR A 306 -359.452-181.893 152.827 1.00 70.13 C ANISOU 2433 CE2 TYR A 306 9484 8279 8882 -403 -926 152 C ATOM 2434 CZ TYR A 306 -359.437-180.642 153.388 1.00 64.83 C ANISOU 2434 CZ TYR A 306 8752 7643 8238 -363 -924 181 C ATOM 2435 OH TYR A 306 -360.431-179.759 153.048 1.00 67.16 O ANISOU 2435 OH TYR A 306 8980 7959 8579 -369 -996 187 O ATOM 2436 N ILE A 307 -354.760-185.567 156.522 1.00 62.17 N ANISOU 2436 N ILE A 307 8572 7035 8016 -324 -699 292 N ATOM 2437 CA ILE A 307 -353.807-186.670 156.511 1.00 64.83 C ANISOU 2437 CA ILE A 307 8928 7269 8435 -304 -686 305 C ATOM 2438 C ILE A 307 -353.718-187.343 157.873 1.00 65.56 C ANISOU 2438 C ILE A 307 9009 7326 8576 -337 -712 400 C ATOM 2439 O ILE A 307 -353.927-188.553 157.994 1.00 68.06 O ANISOU 2439 O ILE A 307 9339 7558 8963 -370 -723 415 O ATOM 2440 CB ILE A 307 -352.413-186.204 156.037 1.00 67.03 C ANISOU 2440 CB ILE A 307 9205 7531 8733 -235 -654 292 C ATOM 2441 CG1 ILE A 307 -352.500-185.665 154.611 1.00 61.61 C ANISOU 2441 CG1 ILE A 307 8549 6876 7982 -225 -625 202 C ATOM 2442 CG2 ILE A 307 -351.418-187.341 156.116 1.00 60.22 C ANISOU 2442 CG2 ILE A 307 8338 6547 7998 -208 -639 305 C ATOM 2443 CD1 ILE A 307 -351.279-184.919 154.172 1.00 56.11 C ANISOU 2443 CD1 ILE A 307 7851 6190 7280 -172 -585 188 C ATOM 2444 N MET A 308 -353.420-186.571 158.913 1.00 67.78 N ANISOU 2444 N MET A 308 9270 7669 8814 -342 -726 467 N ATOM 2445 CA MET A 308 -353.270-187.146 160.240 1.00 70.44 C ANISOU 2445 CA MET A 308 9611 7985 9170 -393 -762 570 C ATOM 2446 C MET A 308 -354.584-187.667 160.802 1.00 75.39 C ANISOU 2446 C MET A 308 10247 8631 9765 -487 -763 583 C ATOM 2447 O MET A 308 -354.563-188.500 161.713 1.00 79.05 O ANISOU 2447 O MET A 308 10731 9052 10252 -548 -795 670 O ATOM 2448 CB MET A 308 -352.664-186.117 161.186 1.00 70.72 C ANISOU 2448 CB MET A 308 9633 8096 9142 -395 -775 626 C ATOM 2449 CG MET A 308 -351.515-186.666 161.992 1.00 96.53 C ANISOU 2449 CG MET A 308 12904 11302 12472 -394 -832 734 C ATOM 2450 SD MET A 308 -349.943-185.892 161.579 1.00114.12 S ANISOU 2450 SD MET A 308 15095 13518 14748 -296 -835 729 S ATOM 2451 CE MET A 308 -349.883-186.099 159.801 1.00112.43 C ANISOU 2451 CE MET A 308 14875 13246 14598 -217 -767 602 C ATOM 2452 N MET A 309 -355.719-187.198 160.298 1.00 80.37 N ANISOU 2452 N MET A 309 10863 9323 10352 -505 -735 505 N ATOM 2453 CA MET A 309 -357.010-187.740 160.695 1.00 85.63 C ANISOU 2453 CA MET A 309 11523 10000 11010 -594 -726 502 C ATOM 2454 C MET A 309 -357.496-188.827 159.749 1.00 87.32 C ANISOU 2454 C MET A 309 11752 10132 11293 -600 -735 454 C ATOM 2455 O MET A 309 -358.533-189.443 160.011 1.00 94.44 O ANISOU 2455 O MET A 309 12649 11027 12206 -677 -732 453 O ATOM 2456 CB MET A 309 -358.044-186.616 160.797 1.00 83.12 C ANISOU 2456 CB MET A 309 11158 9788 10636 -617 -693 444 C ATOM 2457 CG MET A 309 -357.753-185.657 161.936 1.00 87.26 C ANISOU 2457 CG MET A 309 11670 10391 11093 -640 -668 478 C ATOM 2458 SD MET A 309 -359.083-184.498 162.306 1.00 97.98 S ANISOU 2458 SD MET A 309 12955 11849 12423 -685 -607 400 S ATOM 2459 CE MET A 309 -358.511-183.931 163.905 1.00103.54 C ANISOU 2459 CE MET A 309 13683 12622 13035 -753 -569 452 C ATOM 2460 N ASN A 310 -356.774-189.066 158.660 1.00 89.26 N ANISOU 2460 N ASN A 310 12017 10315 11582 -532 -738 407 N ATOM 2461 CA ASN A 310 -357.022-190.219 157.807 1.00 92.08 C ANISOU 2461 CA ASN A 310 12400 10578 12009 -545 -740 355 C ATOM 2462 C ASN A 310 -356.653-191.493 158.564 1.00 83.07 C ANISOU 2462 C ASN A 310 11277 9326 10962 -577 -758 435 C ATOM 2463 O ASN A 310 -355.597-191.564 159.200 1.00 87.20 O ANISOU 2463 O ASN A 310 11799 9808 11525 -545 -777 514 O ATOM 2464 CB ASN A 310 -356.204-190.069 156.520 1.00 99.19 C ANISOU 2464 CB ASN A 310 13321 11445 12921 -475 -719 274 C ATOM 2465 CG ASN A 310 -356.530-191.111 155.481 1.00 99.27 C ANISOU 2465 CG ASN A 310 13365 11373 12981 -501 -707 187 C ATOM 2466 OD1 ASN A 310 -356.753-192.277 155.798 1.00 96.54 O ANISOU 2466 OD1 ASN A 310 13028 10934 12720 -541 -714 206 O ATOM 2467 ND2 ASN A 310 -356.539-190.694 154.215 1.00 90.84 N ANISOU 2467 ND2 ASN A 310 12323 10335 11855 -488 -691 92 N ATOM 2468 N LYS A 311 -357.533-192.495 158.508 1.00 91.10 N ANISOU 2468 N LYS A 311 12305 10287 12023 -646 -765 422 N ATOM 2469 CA LYS A 311 -357.382-193.669 159.368 1.00100.10 C ANISOU 2469 CA LYS A 311 13461 11322 13249 -696 -793 519 C ATOM 2470 C LYS A 311 -356.101-194.440 159.063 1.00 95.74 C ANISOU 2470 C LYS A 311 12917 10625 12833 -628 -805 535 C ATOM 2471 O LYS A 311 -355.407-194.896 159.982 1.00 92.56 O ANISOU 2471 O LYS A 311 12515 10155 12500 -633 -850 655 O ATOM 2472 CB LYS A 311 -358.602-194.583 159.223 1.00102.05 C ANISOU 2472 CB LYS A 311 13717 11530 13527 -784 -791 490 C ATOM 2473 CG LYS A 311 -358.594-195.798 160.139 1.00106.39 C ANISOU 2473 CG LYS A 311 14290 11971 14164 -855 -824 601 C ATOM 2474 CD LYS A 311 -359.803-196.689 159.886 1.00109.31 C ANISOU 2474 CD LYS A 311 14664 12298 14569 -944 -816 560 C ATOM 2475 CE LYS A 311 -359.770-197.934 160.758 1.00107.87 C ANISOU 2475 CE LYS A 311 14510 11993 14482 -1020 -853 680 C ATOM 2476 NZ LYS A 311 -360.921-198.838 160.480 1.00110.12 N ANISOU 2476 NZ LYS A 311 14799 12226 14814 -1110 -842 636 N ATOM 2477 N GLN A 312 -355.760-194.586 157.781 1.00 93.86 N ANISOU 2477 N GLN A 312 12683 10336 12641 -571 -765 413 N ATOM 2478 CA GLN A 312 -354.596-195.389 157.425 1.00100.17 C ANISOU 2478 CA GLN A 312 13476 10983 13601 -509 -754 401 C ATOM 2479 C GLN A 312 -353.288-194.627 157.633 1.00 94.15 C ANISOU 2479 C GLN A 312 12681 10238 12852 -424 -754 440 C ATOM 2480 O GLN A 312 -352.321-195.200 158.153 1.00 92.53 O ANISOU 2480 O GLN A 312 12447 9918 12791 -389 -788 520 O ATOM 2481 CB GLN A 312 -354.720-195.888 155.981 1.00107.99 C ANISOU 2481 CB GLN A 312 14489 11912 14632 -500 -692 237 C ATOM 2482 CG GLN A 312 -355.093-194.823 154.963 1.00116.94 C ANISOU 2482 CG GLN A 312 15642 13180 15609 -494 -655 127 C ATOM 2483 CD GLN A 312 -355.237-195.387 153.560 1.00120.95 C ANISOU 2483 CD GLN A 312 16191 13633 16132 -514 -599 -32 C ATOM 2484 OE1 GLN A 312 -354.953-196.562 153.318 1.00117.82 O ANISOU 2484 OE1 GLN A 312 15800 13087 15878 -520 -571 -79 O ATOM 2485 NE2 GLN A 312 -355.681-194.549 152.627 1.00119.90 N ANISOU 2485 NE2 GLN A 312 16089 13616 15852 -533 -587 -115 N ATOM 2486 N PHE A 313 -353.238-193.345 157.242 1.00 90.03 N ANISOU 2486 N PHE A 313 12158 9852 12198 -393 -725 391 N ATOM 2487 CA PHE A 313 -352.026-192.550 157.439 1.00 83.87 C ANISOU 2487 CA PHE A 313 11345 9096 11425 -320 -723 425 C ATOM 2488 C PHE A 313 -351.564-192.604 158.893 1.00 82.91 C ANISOU 2488 C PHE A 313 11202 8963 11337 -335 -801 588 C ATOM 2489 O PHE A 313 -350.373-192.788 159.173 1.00 84.12 O ANISOU 2489 O PHE A 313 11317 9036 11610 -281 -827 644 O ATOM 2490 CB PHE A 313 -352.254-191.095 157.005 1.00 83.07 C ANISOU 2490 CB PHE A 313 11250 9150 11163 -305 -695 373 C ATOM 2491 CG PHE A 313 -351.991-190.824 155.526 1.00 84.99 C ANISOU 2491 CG PHE A 313 11512 9397 11384 -270 -624 234 C ATOM 2492 CD1 PHE A 313 -350.696-190.654 155.050 1.00 83.98 C ANISOU 2492 CD1 PHE A 313 11361 9223 11325 -203 -575 197 C ATOM 2493 CD2 PHE A 313 -353.044-190.696 154.623 1.00 84.13 C ANISOU 2493 CD2 PHE A 313 11444 9345 11178 -318 -610 145 C ATOM 2494 CE1 PHE A 313 -350.454-190.390 153.694 1.00 76.25 C ANISOU 2494 CE1 PHE A 313 10412 8257 10303 -193 -497 66 C ATOM 2495 CE2 PHE A 313 -352.806-190.432 153.267 1.00 79.46 C ANISOU 2495 CE2 PHE A 313 10887 8767 10537 -310 -554 27 C ATOM 2496 CZ PHE A 313 -351.507-190.279 152.806 1.00 66.85 C ANISOU 2496 CZ PHE A 313 9279 7128 8992 -252 -489 -15 C ATOM 2497 N ARG A 314 -352.501-192.483 159.833 1.00 79.76 N ANISOU 2497 N ARG A 314 10827 8642 10838 -419 -840 664 N ATOM 2498 CA ARG A 314 -352.130-192.411 161.242 1.00 85.53 C ANISOU 2498 CA ARG A 314 11557 9389 11552 -461 -914 818 C ATOM 2499 C ARG A 314 -351.416-193.681 161.692 1.00 95.96 C ANISOU 2499 C ARG A 314 12867 10542 13054 -461 -984 924 C ATOM 2500 O ARG A 314 -350.334-193.617 162.287 1.00103.86 O ANISOU 2500 O ARG A 314 13838 11502 14124 -431 -1049 1024 O ATOM 2501 CB ARG A 314 -353.377-192.152 162.085 1.00 94.67 C ANISOU 2501 CB ARG A 314 12748 10657 12566 -572 -917 857 C ATOM 2502 CG ARG A 314 -353.106-191.695 163.503 1.00103.35 C ANISOU 2502 CG ARG A 314 13863 11829 13576 -639 -971 987 C ATOM 2503 CD ARG A 314 -354.347-191.868 164.373 1.00115.65 C ANISOU 2503 CD ARG A 314 15459 13457 15026 -773 -961 1026 C ATOM 2504 NE ARG A 314 -355.542-191.281 163.767 1.00121.32 N ANISOU 2504 NE ARG A 314 16160 14266 15670 -782 -878 895 N ATOM 2505 CZ ARG A 314 -356.480-191.974 163.125 1.00129.79 C ANISOU 2505 CZ ARG A 314 17232 15296 16788 -805 -851 831 C ATOM 2506 NH1 ARG A 314 -356.370-193.290 162.997 1.00135.07 N ANISOU 2506 NH1 ARG A 314 17918 15827 17573 -820 -887 875 N ATOM 2507 NH2 ARG A 314 -357.527-191.350 162.606 1.00133.66 N ANISOU 2507 NH2 ARG A 314 17694 15870 17221 -813 -794 724 N ATOM 2508 N ASN A 315 -351.997-194.850 161.395 1.00 95.21 N ANISOU 2508 N ASN A 315 12788 10336 13052 -495 -981 907 N ATOM 2509 CA ASN A 315 -351.368-196.113 161.778 1.00 92.47 C ANISOU 2509 CA ASN A 315 12424 9804 12907 -493 -1052 1009 C ATOM 2510 C ASN A 315 -350.009-196.279 161.111 1.00 85.35 C ANISOU 2510 C ASN A 315 11455 8779 12196 -374 -1039 964 C ATOM 2511 O ASN A 315 -349.064-196.794 161.722 1.00 93.12 O ANISOU 2511 O ASN A 315 12396 9643 13342 -350 -1126 1087 O ATOM 2512 CB ASN A 315 -352.277-197.291 161.418 1.00103.17 C ANISOU 2512 CB ASN A 315 13807 11056 14338 -547 -1034 971 C ATOM 2513 CG ASN A 315 -353.683-197.135 161.965 1.00112.28 C ANISOU 2513 CG ASN A 315 15012 12331 15318 -667 -1028 994 C ATOM 2514 OD1 ASN A 315 -353.914-196.377 162.905 1.00123.68 O ANISOU 2514 OD1 ASN A 315 16475 13907 16609 -727 -1052 1075 O ATOM 2515 ND2 ASN A 315 -354.632-197.856 161.376 1.00106.00 N ANISOU 2515 ND2 ASN A 315 14236 11488 14552 -709 -988 912 N ATOM 2516 N CYS A 316 -349.892-195.842 159.857 1.00 73.62 N ANISOU 2516 N CYS A 316 9955 7319 10696 -307 -932 789 N ATOM 2517 CA CYS A 316 -348.625-195.961 159.149 1.00 73.41 C ANISOU 2517 CA CYS A 316 9863 7184 10847 -203 -889 720 C ATOM 2518 C CYS A 316 -347.560-195.047 159.747 1.00 81.99 C ANISOU 2518 C CYS A 316 10900 8329 11924 -155 -937 806 C ATOM 2519 O CYS A 316 -346.390-195.436 159.840 1.00 87.00 O ANISOU 2519 O CYS A 316 11457 8832 12765 -89 -968 847 O ATOM 2520 CB CYS A 316 -348.844-195.680 157.664 1.00 72.49 C ANISOU 2520 CB CYS A 316 9763 7101 10677 -173 -756 511 C ATOM 2521 SG CYS A 316 -349.915-196.915 156.848 1.00 82.57 S ANISOU 2521 SG CYS A 316 11091 8279 12004 -232 -704 392 S ATOM 2522 N MET A 317 -347.944-193.844 160.193 1.00 87.12 N ANISOU 2522 N MET A 317 11585 9164 12352 -190 -947 835 N ATOM 2523 CA MET A 317 -346.971-192.953 160.821 1.00 88.95 C ANISOU 2523 CA MET A 317 11777 9456 12565 -158 -998 916 C ATOM 2524 C MET A 317 -346.581-193.439 162.211 1.00 89.07 C ANISOU 2524 C MET A 317 11781 9416 12645 -207 -1144 1119 C ATOM 2525 O MET A 317 -345.423-193.294 162.619 1.00 84.51 O ANISOU 2525 O MET A 317 11140 8790 12179 -163 -1213 1200 O ATOM 2526 CB MET A 317 -347.519-191.533 160.888 1.00 97.68 C ANISOU 2526 CB MET A 317 12923 10763 13428 -186 -962 878 C ATOM 2527 CG MET A 317 -347.752-190.951 159.523 1.00111.30 C ANISOU 2527 CG MET A 317 14658 12541 15091 -140 -843 705 C ATOM 2528 SD MET A 317 -348.246-189.229 159.515 1.00113.85 S ANISOU 2528 SD MET A 317 15009 13070 15180 -156 -811 666 S ATOM 2529 CE MET A 317 -348.757-189.080 157.809 1.00111.33 C ANISOU 2529 CE MET A 317 14719 12766 14816 -131 -702 487 C ATOM 2530 N VAL A 318 -347.533-194.007 162.955 1.00 89.48 N ANISOU 2530 N VAL A 318 11896 9476 12625 -309 -1199 1208 N ATOM 2531 CA VAL A 318 -347.204-194.604 164.246 1.00 89.76 C ANISOU 2531 CA VAL A 318 11938 9449 12716 -379 -1348 1414 C ATOM 2532 C VAL A 318 -346.176-195.706 164.058 1.00 97.89 C ANISOU 2532 C VAL A 318 12886 10252 14054 -305 -1413 1471 C ATOM 2533 O VAL A 318 -345.176-195.783 164.782 1.00106.83 O ANISOU 2533 O VAL A 318 13968 11323 15300 -294 -1537 1616 O ATOM 2534 CB VAL A 318 -348.475-195.130 164.936 1.00 94.31 C ANISOU 2534 CB VAL A 318 12601 10064 13168 -512 -1372 1484 C ATOM 2535 CG1 VAL A 318 -348.114-195.919 166.188 1.00 99.20 C ANISOU 2535 CG1 VAL A 318 13239 10596 13856 -598 -1534 1710 C ATOM 2536 CG2 VAL A 318 -349.402-193.981 165.276 1.00 94.71 C ANISOU 2536 CG2 VAL A 318 12712 10331 12943 -586 -1310 1434 C ATOM 2537 N THR A 319 -346.401-196.565 163.064 1.00 96.35 N ANISOU 2537 N THR A 319 12671 9926 14013 -255 -1330 1350 N ATOM 2538 CA THR A 319 -345.462-197.642 162.771 1.00 88.50 C ANISOU 2538 CA THR A 319 11585 8695 13347 -177 -1366 1370 C ATOM 2539 C THR A 319 -344.102-197.099 162.355 1.00 84.99 C ANISOU 2539 C THR A 319 11033 8216 13042 -64 -1342 1321 C ATOM 2540 O THR A 319 -343.060-197.633 162.753 1.00 89.90 O ANISOU 2540 O THR A 319 11561 8681 13917 -16 -1444 1431 O ATOM 2541 CB THR A 319 -346.032-198.527 161.667 1.00 88.33 C ANISOU 2541 CB THR A 319 11570 8559 13433 -154 -1249 1206 C ATOM 2542 OG1 THR A 319 -347.327-198.997 162.055 1.00 96.98 O ANISOU 2542 OG1 THR A 319 12758 9692 14397 -265 -1270 1250 O ATOM 2543 CG2 THR A 319 -345.131-199.696 161.437 1.00 92.57 C ANISOU 2543 CG2 THR A 319 12008 8834 14331 -81 -1278 1220 C ATOM 2544 N THR A 320 -344.094-196.042 161.543 1.00 77.17 N ANISOU 2544 N THR A 320 10050 7365 11906 -22 -1213 1161 N ATOM 2545 CA THR A 320 -342.840-195.471 161.070 1.00 80.10 C ANISOU 2545 CA THR A 320 10322 7715 12398 76 -1168 1098 C ATOM 2546 C THR A 320 -342.097-194.763 162.195 1.00 90.30 C ANISOU 2546 C THR A 320 11581 9075 13654 61 -1308 1271 C ATOM 2547 O THR A 320 -340.870-194.881 162.310 1.00 96.33 O ANISOU 2547 O THR A 320 12230 9728 14643 130 -1362 1320 O ATOM 2548 CB THR A 320 -343.123-194.511 159.913 1.00 79.33 C ANISOU 2548 CB THR A 320 10259 7756 12125 102 -998 895 C ATOM 2549 OG1 THR A 320 -343.705-195.242 158.826 1.00 73.99 O ANISOU 2549 OG1 THR A 320 9612 7005 11494 107 -878 733 O ATOM 2550 CG2 THR A 320 -341.848-193.819 159.446 1.00 77.47 C ANISOU 2550 CG2 THR A 320 9929 7517 11990 188 -941 831 C ATOM 2551 N LEU A 321 -342.821-194.029 163.035 1.00 92.14 N ANISOU 2551 N LEU A 321 11909 9486 13615 -34 -1366 1356 N ATOM 2552 CA LEU A 321 -342.214-193.306 164.143 1.00 94.88 C ANISOU 2552 CA LEU A 321 12246 9918 13886 -74 -1496 1510 C ATOM 2553 C LEU A 321 -341.769-194.274 165.232 1.00107.20 C ANISOU 2553 C LEU A 321 13780 11342 15610 -121 -1691 1732 C ATOM 2554 O LEU A 321 -340.743-194.065 165.885 1.00108.34 O ANISOU 2554 O LEU A 321 13858 11458 15850 -112 -1819 1859 O ATOM 2555 CB LEU A 321 -343.192-192.270 164.701 1.00 86.15 C ANISOU 2555 CB LEU A 321 11253 9036 12443 -174 -1479 1512 C ATOM 2556 CG LEU A 321 -343.425-191.084 163.759 1.00 81.57 C ANISOU 2556 CG LEU A 321 10685 8594 11716 -126 -1325 1328 C ATOM 2557 CD1 LEU A 321 -344.463-190.135 164.316 1.00 72.19 C ANISOU 2557 CD1 LEU A 321 9592 7600 10238 -221 -1306 1324 C ATOM 2558 CD2 LEU A 321 -342.114-190.358 163.491 1.00 75.90 C ANISOU 2558 CD2 LEU A 321 9873 7870 11094 -42 -1319 1304 C ATOM 2559 N CYS A 322 -342.536-195.346 165.405 1.00107.73 N ANISOU 2559 N CYS A 322 13899 11319 15717 -176 -1721 1784 N ATOM 2560 CA CYS A 322 -342.230-196.346 166.395 1.00115.47 C ANISOU 2560 CA CYS A 322 14866 12157 16850 -233 -1911 2007 C ATOM 2561 C CYS A 322 -341.256-197.433 165.949 1.00117.13 C ANISOU 2561 C CYS A 322 14939 12099 17467 -124 -1956 2027 C ATOM 2562 O CYS A 322 -341.279-198.583 166.401 1.00122.84 O ANISOU 2562 O CYS A 322 15652 12650 18372 -156 -2076 2168 O ATOM 2563 CB CYS A 322 -343.464-197.014 166.988 1.00126.09 C ANISOU 2563 CB CYS A 322 16331 13521 18055 -365 -1947 2093 C ATOM 2564 SG CYS A 322 -343.822-196.457 168.627 1.00135.63 S ANISOU 2564 SG CYS A 322 17659 14909 18967 -551 -2098 2306 S ATOM 2565 N CYS A 323 -340.382-197.046 165.024 1.00112.03 N ANISOU 2565 N CYS A 323 14180 11411 16975 5 -1849 1875 N ATOM 2566 CA CYS A 323 -339.279-197.893 164.571 1.00111.31 C ANISOU 2566 CA CYS A 323 13928 11070 17295 121 -1868 1865 C ATOM 2567 C CYS A 323 -339.749-199.275 164.117 1.00104.34 C ANISOU 2567 C CYS A 323 13038 9981 16625 136 -1833 1825 C ATOM 2568 O CYS A 323 -339.112-200.287 164.395 1.00107.97 O ANISOU 2568 O CYS A 323 13397 10207 17419 173 -1950 1939 O ATOM 2569 CB CYS A 323 -338.238-198.026 165.683 1.00114.85 C ANISOU 2569 CB CYS A 323 14290 11433 17916 110 -2107 2111 C ATOM 2570 SG CYS A 323 -338.029-196.508 166.653 1.00120.48 S ANISOU 2570 SG CYS A 323 15068 12414 18294 23 -2203 2218 S ATOM 2571 N GLY A 324 -340.883-199.312 163.422 1.00 97.81 N ANISOU 2571 N GLY A 324 12316 9234 15612 102 -1679 1665 N ATOM 2572 CA GLY A 324 -341.409-200.522 162.856 1.00 92.26 C ANISOU 2572 CA GLY A 324 11618 8356 15081 109 -1617 1588 C ATOM 2573 C GLY A 324 -342.505-201.173 163.671 1.00 99.70 C ANISOU 2573 C GLY A 324 12678 9304 15900 -19 -1724 1741 C ATOM 2574 O GLY A 324 -343.393-201.812 163.097 1.00 99.14 O ANISOU 2574 O GLY A 324 12663 9188 15817 -45 -1628 1631 O ATOM 2575 N LYS A 325 -342.466-201.030 164.991 1.00112.45 N ANISOU 2575 N LYS A 325 14335 10975 17414 -111 -1916 1988 N ATOM 2576 CA LYS A 325 -343.404-201.724 165.859 1.00119.21 C ANISOU 2576 CA LYS A 325 15300 11822 18171 -249 -2026 2156 C ATOM 2577 C LYS A 325 -344.634-200.859 166.130 1.00120.92 C ANISOU 2577 C LYS A 325 15664 12311 17969 -367 -1952 2114 C ATOM 2578 O LYS A 325 -344.672-199.668 165.811 1.00123.96 O ANISOU 2578 O LYS A 325 16065 12888 18146 -343 -1853 1993 O ATOM 2579 CB LYS A 325 -342.719-202.120 167.167 1.00118.04 C ANISOU 2579 CB LYS A 325 15130 11582 18137 -312 -2282 2458 C ATOM 2580 CG LYS A 325 -341.518-203.042 166.989 1.00119.86 C ANISOU 2580 CG LYS A 325 15195 11517 18830 -196 -2381 2525 C ATOM 2581 CD LYS A 325 -341.933-204.387 166.406 1.00119.33 C ANISOU 2581 CD LYS A 325 15105 11212 19023 -169 -2330 2463 C ATOM 2582 CE LYS A 325 -340.791-205.394 166.444 1.00124.87 C ANISOU 2582 CE LYS A 325 15637 11593 20213 -71 -2459 2568 C ATOM 2583 NZ LYS A 325 -339.648-204.977 165.587 1.00129.91 N ANISOU 2583 NZ LYS A 325 16110 12168 21083 94 -2351 2393 N ATOM 2584 N ASN A 326 -345.650-201.484 166.720 1.00123.97 N ANISOU 2584 N ASN A 326 16152 12701 18251 -496 -1999 2215 N ATOM 2585 CA ASN A 326 -346.905-200.817 167.074 1.00126.34 C ANISOU 2585 CA ASN A 326 16580 13235 18189 -622 -1930 2184 C ATOM 2586 C ASN A 326 -347.574-200.188 165.850 1.00123.07 C ANISOU 2586 C ASN A 326 16172 12935 17654 -558 -1720 1912 C ATOM 2587 O ASN A 326 -348.783-200.328 165.647 1.00120.30 O ANISOU 2587 O ASN A 326 15893 12653 17164 -630 -1638 1837 O ATOM 2588 CB ASN A 326 -346.665-199.752 168.152 1.00131.06 C ANISOU 2588 CB ASN A 326 17227 14027 18541 -706 -2017 2311 C ATOM 2589 CG ASN A 326 -347.950-199.295 168.825 1.00135.63 C ANISOU 2589 CG ASN A 326 17937 14812 18786 -868 -1972 2325 C ATOM 2590 OD1 ASN A 326 -349.051-199.526 168.322 1.00136.77 O ANISOU 2590 OD1 ASN A 326 18121 14985 18860 -897 -1852 2204 O ATOM 2591 ND2 ASN A 326 -347.812-198.639 169.973 1.00134.84 N ANISOU 2591 ND2 ASN A 326 17898 14853 18482 -983 -2065 2466 N TER 2592 ASN A 326 HETATM 2593 C1 NAG B 1 -338.461-140.186 152.611 1.00 64.10 C ANISOU 2593 C1 NAG B 1 8318 5873 10166 -434 -851 1127 C HETATM 2594 C2 NAG B 1 -337.761-140.879 151.446 1.00 63.83 C ANISOU 2594 C2 NAG B 1 8395 5964 9893 -505 -846 1269 C HETATM 2595 C3 NAG B 1 -336.245-140.685 151.529 1.00 68.39 C ANISOU 2595 C3 NAG B 1 8989 6601 10395 -586 -745 1248 C HETATM 2596 C4 NAG B 1 -335.855-139.242 151.824 1.00 68.68 C ANISOU 2596 C4 NAG B 1 8983 6474 10638 -625 -751 1249 C HETATM 2597 C5 NAG B 1 -336.687-138.685 152.972 1.00 70.05 C ANISOU 2597 C5 NAG B 1 9055 6530 11031 -548 -767 1103 C HETATM 2598 C6 NAG B 1 -336.482-137.207 153.190 1.00 66.72 C ANISOU 2598 C6 NAG B 1 8589 5915 10848 -582 -783 1104 C HETATM 2599 C7 NAG B 1 -338.464-142.967 150.350 1.00 62.51 C ANISOU 2599 C7 NAG B 1 8338 6019 9395 -484 -877 1351 C HETATM 2600 C8 NAG B 1 -338.685-144.440 150.530 1.00 61.08 C ANISOU 2600 C8 NAG B 1 8169 5998 9041 -441 -833 1275 C HETATM 2601 N2 NAG B 1 -338.069-142.300 151.439 1.00 62.47 N ANISOU 2601 N2 NAG B 1 8248 5954 9534 -464 -821 1227 N HETATM 2602 O3 NAG B 1 -335.657-141.105 150.303 1.00 64.02 O ANISOU 2602 O3 NAG B 1 8537 6131 9656 -667 -733 1388 O HETATM 2603 O4 NAG B 1 -334.494-139.233 152.236 1.00 69.65 O ANISOU 2603 O4 NAG B 1 9092 6673 10699 -686 -647 1179 O HETATM 2604 O5 NAG B 1 -338.073-138.852 152.666 1.00 65.97 O ANISOU 2604 O5 NAG B 1 8527 5950 10588 -476 -863 1152 O HETATM 2605 O6 NAG B 1 -336.831-136.497 152.011 1.00 68.17 O ANISOU 2605 O6 NAG B 1 8824 5963 11113 -616 -894 1312 O HETATM 2606 O7 NAG B 1 -338.643-142.408 149.272 1.00 66.40 O ANISOU 2606 O7 NAG B 1 8899 6438 9894 -542 -964 1520 O HETATM 2607 C1 NAG B 2 -333.678-138.310 151.494 1.00 66.04 C ANISOU 2607 C1 NAG B 2 8676 6138 10280 -787 -644 1301 C HETATM 2608 C2 NAG B 2 -332.430-138.071 152.341 1.00 65.85 C ANISOU 2608 C2 NAG B 2 8591 6153 10276 -831 -544 1177 C HETATM 2609 C3 NAG B 2 -331.479-137.122 151.611 1.00 67.24 C ANISOU 2609 C3 NAG B 2 8802 6254 10493 -946 -525 1295 C HETATM 2610 C4 NAG B 2 -331.203-137.618 150.196 1.00 67.57 C ANISOU 2610 C4 NAG B 2 8951 6376 10348 -1019 -515 1464 C HETATM 2611 C5 NAG B 2 -332.499-137.916 149.457 1.00 67.69 C ANISOU 2611 C5 NAG B 2 9035 6363 10322 -975 -625 1578 C HETATM 2612 C6 NAG B 2 -332.256-138.566 148.116 1.00 68.01 C ANISOU 2612 C6 NAG B 2 9194 6509 10136 -1059 -607 1720 C HETATM 2613 C7 NAG B 2 -332.856-138.242 154.764 1.00 71.52 C ANISOU 2613 C7 NAG B 2 9166 6890 11117 -731 -503 846 C HETATM 2614 C8 NAG B 2 -333.274-137.493 155.993 1.00 65.11 C ANISOU 2614 C8 NAG B 2 8280 5976 10484 -707 -499 682 C HETATM 2615 N2 NAG B 2 -332.800-137.523 153.637 1.00 68.07 N ANISOU 2615 N2 NAG B 2 8783 6350 10730 -781 -547 1015 N HETATM 2616 O3 NAG B 2 -330.260-137.004 152.339 1.00 68.15 O ANISOU 2616 O3 NAG B 2 8855 6421 10620 -993 -435 1184 O HETATM 2617 O4 NAG B 2 -330.540-136.613 149.446 1.00 74.24 O ANISOU 2617 O4 NAG B 2 9840 7126 11240 -1136 -512 1595 O HETATM 2618 O5 NAG B 2 -333.298-138.826 150.223 1.00 66.25 O ANISOU 2618 O5 NAG B 2 8804 6252 10116 -858 -636 1450 O HETATM 2619 O6 NAG B 2 -333.337-138.390 147.213 1.00 68.89 O ANISOU 2619 O6 NAG B 2 9388 6549 10237 -1066 -741 1882 O HETATM 2620 O7 NAG B 2 -332.572-139.442 154.794 1.00 72.05 O ANISOU 2620 O7 NAG B 2 9248 7123 11004 -713 -467 824 O HETATM 2621 C1 BMA B 3 -329.175-136.955 149.183 1.00 84.72 C ANISOU 2621 C1 BMA B 3 11171 8573 12447 -1227 -385 1581 C HETATM 2622 C2 BMA B 3 -328.704-135.921 148.194 1.00 88.27 C ANISOU 2622 C2 BMA B 3 11693 8920 12927 -1362 -392 1751 C HETATM 2623 C3 BMA B 3 -327.256-136.204 147.826 1.00 99.16 C ANISOU 2623 C3 BMA B 3 13070 10415 14193 -1472 -244 1739 C HETATM 2624 C4 BMA B 3 -326.360-136.418 149.073 1.00119.77 C ANISOU 2624 C4 BMA B 3 15543 13085 16881 -1431 -162 1545 C HETATM 2625 C5 BMA B 3 -327.042-137.307 150.151 1.00119.47 C ANISOU 2625 C5 BMA B 3 15438 13116 16837 -1286 -198 1392 C HETATM 2626 C6 BMA B 3 -326.346-137.227 151.495 1.00124.72 C ANISOU 2626 C6 BMA B 3 15981 13801 17606 -1260 -164 1221 C HETATM 2627 O2 BMA B 3 -328.752-134.626 148.792 1.00 89.33 O ANISOU 2627 O2 BMA B 3 11771 8871 13301 -1364 -446 1737 O HETATM 2628 O3 BMA B 3 -326.721-135.154 147.037 1.00 91.24 O ANISOU 2628 O3 BMA B 3 12126 9313 13230 -1612 -236 1884 O HETATM 2629 O4 BMA B 3 -325.149-137.039 148.670 1.00130.39 O ANISOU 2629 O4 BMA B 3 16871 14563 18109 -1509 -25 1526 O HETATM 2630 O5 BMA B 3 -328.397-136.865 150.344 1.00101.25 O ANISOU 2630 O5 BMA B 3 13155 10689 14627 -1208 -320 1417 O HETATM 2631 O6 BMA B 3 -326.693-135.967 152.063 1.00127.64 O ANISOU 2631 O6 BMA B 3 16325 14001 18172 -1263 -230 1200 O HETATM 2632 C1 MAN B 4 -326.791-135.473 145.629 1.00 84.24 C ANISOU 2632 C1 MAN B 4 11378 8486 12142 -1718 -221 2049 C HETATM 2633 C2 MAN B 4 -325.849-134.496 144.921 1.00 87.55 C ANISOU 2633 C2 MAN B 4 11845 8839 12581 -1891 -163 2171 C HETATM 2634 C3 MAN B 4 -326.404-133.075 145.017 1.00 83.20 C ANISOU 2634 C3 MAN B 4 11305 8059 12248 -1903 -307 2285 C HETATM 2635 C4 MAN B 4 -327.844-132.988 144.463 1.00 84.95 C ANISOU 2635 C4 MAN B 4 11618 8194 12464 -1858 -485 2434 C HETATM 2636 C5 MAN B 4 -328.753-134.039 145.144 1.00 85.11 C ANISOU 2636 C5 MAN B 4 11584 8300 12455 -1686 -523 2296 C HETATM 2637 C6 MAN B 4 -330.156-134.137 144.493 1.00 80.51 C ANISOU 2637 C6 MAN B 4 11087 7659 11844 -1648 -694 2443 C HETATM 2638 O2 MAN B 4 -325.789-134.790 143.531 1.00 92.05 O ANISOU 2638 O2 MAN B 4 12564 9483 12929 -2028 -128 2326 O HETATM 2639 O3 MAN B 4 -325.566-132.157 144.331 1.00 94.72 O ANISOU 2639 O3 MAN B 4 12817 9448 13723 -2074 -260 2415 O HETATM 2640 O4 MAN B 4 -328.385-131.686 144.690 1.00 91.84 O ANISOU 2640 O4 MAN B 4 12470 8833 13593 -1846 -622 2520 O HETATM 2641 O5 MAN B 4 -328.112-135.360 145.099 1.00 87.01 O ANISOU 2641 O5 MAN B 4 11819 8761 12479 -1684 -376 2181 O HETATM 2642 O6 MAN B 4 -331.045-134.945 145.301 1.00 74.55 O ANISOU 2642 O6 MAN B 4 10257 6952 11117 -1481 -730 2299 O HETATM 2643 C1 MAN B 5 -326.181-135.861 153.405 1.00130.56 C ANISOU 2643 C1 MAN B 5 16591 14388 18627 -1247 -212 1027 C HETATM 2644 C2 MAN B 5 -326.794-134.542 154.039 1.00131.39 C ANISOU 2644 C2 MAN B 5 16675 14297 18949 -1241 -278 980 C HETATM 2645 C3 MAN B 5 -325.939-133.276 153.746 1.00137.50 C ANISOU 2645 C3 MAN B 5 17439 14942 19862 -1357 -257 1039 C HETATM 2646 C4 MAN B 5 -324.422-133.560 153.824 1.00135.39 C ANISOU 2646 C4 MAN B 5 17117 14792 19532 -1445 -166 1006 C HETATM 2647 C5 MAN B 5 -324.092-134.722 152.893 1.00132.95 C ANISOU 2647 C5 MAN B 5 16849 14644 19024 -1448 -105 1092 C HETATM 2648 C6 MAN B 5 -322.607-135.009 152.774 1.00126.14 C ANISOU 2648 C6 MAN B 5 15921 13882 18124 -1536 -3 1074 C HETATM 2649 O2 MAN B 5 -326.934-134.622 155.464 1.00127.96 O ANISOU 2649 O2 MAN B 5 16167 13883 18570 -1195 -284 788 O HETATM 2650 O3 MAN B 5 -326.293-132.180 154.598 1.00140.89 O ANISOU 2650 O3 MAN B 5 17823 15206 20501 -1353 -298 942 O HETATM 2651 O4 MAN B 5 -323.680-132.409 153.434 1.00134.18 O ANISOU 2651 O4 MAN B 5 16962 14519 19502 -1560 -143 1076 O HETATM 2652 O5 MAN B 5 -324.748-135.906 153.408 1.00134.53 O ANISOU 2652 O5 MAN B 5 17040 14962 19114 -1335 -128 1008 O HETATM 2653 O6 MAN B 5 -322.410-135.746 151.571 1.00123.21 O ANISOU 2653 O6 MAN B 5 15613 13605 17598 -1567 68 1183 O HETATM 2654 C1 PLM A 401 -344.013-194.744 168.513 1.00122.57 C ANISOU 2654 C1 PLM A 401 16041 13514 17016 -554 -1976 2163 C HETATM 2655 O2 PLM A 401 -345.032-194.201 168.085 1.00125.77 O ANISOU 2655 O2 PLM A 401 16507 14050 17228 -574 -1829 2015 O HETATM 2656 C2 PLM A 401 -343.102-194.098 169.522 1.00112.25 C ANISOU 2656 C2 PLM A 401 14724 12274 15650 -606 -2125 2313 C HETATM 2657 C3 PLM A 401 -341.624-194.280 169.233 1.00108.41 C ANISOU 2657 C3 PLM A 401 14094 11636 15462 -481 -2214 2357 C HETATM 2658 C4 PLM A 401 -340.743-193.343 170.040 1.00 99.99 C ANISOU 2658 C4 PLM A 401 13011 10672 14309 -521 -2332 2458 C HETATM 2659 C5 PLM A 401 -341.160-191.894 169.871 1.00 97.77 C ANISOU 2659 C5 PLM A 401 12785 10615 13749 -537 -2190 2302 C HETATM 2660 C6 PLM A 401 -341.443-191.242 171.211 1.00 94.93 C ANISOU 2660 C6 PLM A 401 12538 10427 13102 -714 -2288 2423 C HETATM 2661 C7 PLM A 401 -340.837-189.861 171.327 1.00 88.65 C ANISOU 2661 C7 PLM A 401 11721 9772 12189 -703 -2266 2359 C HETATM 2662 C8 PLM A 401 -341.759-188.802 170.768 1.00 84.82 C ANISOU 2662 C8 PLM A 401 11290 9448 11490 -691 -2058 2148 C HETATM 2663 C9 PLM A 401 -341.335-187.416 171.220 1.00 81.18 C ANISOU 2663 C9 PLM A 401 10840 9140 10863 -731 -2056 2114 C HETATM 2664 CA PLM A 401 -341.839-186.350 170.270 1.00 81.89 C ANISOU 2664 CA PLM A 401 10923 9327 10866 -650 -1854 1893 C HETATM 2665 CB PLM A 401 -341.991-185.007 170.957 1.00 86.75 C ANISOU 2665 CB PLM A 401 11598 10120 11244 -743 -1826 1849 C HETATM 2666 CC PLM A 401 -340.792-184.104 170.750 1.00 84.22 C ANISOU 2666 CC PLM A 401 11194 9810 10997 -671 -1852 1825 C HETATM 2667 CD PLM A 401 -341.108-182.681 171.163 1.00 84.56 C ANISOU 2667 CD PLM A 401 11291 10020 10817 -743 -1779 1730 C HETATM 2668 CE PLM A 401 -339.931-181.747 170.947 1.00 79.03 C ANISOU 2668 CE PLM A 401 10509 9329 10190 -678 -1801 1703 C HETATM 2669 CF PLM A 401 -340.265-180.344 171.411 1.00 75.03 C ANISOU 2669 CF PLM A 401 10060 8976 9471 -757 -1730 1607 C HETATM 2670 CG PLM A 401 -339.412-179.288 170.762 1.00 71.99 C ANISOU 2670 CG PLM A 401 9592 8597 9164 -661 -1682 1520 C HETATM 2671 C10 DLB A 407 -355.801-167.316 148.475 1.00 74.94 C ANISOU 2671 C10 DLB A 407 10049 8875 9549 -162 -1378 710 C HETATM 2672 C11 DLB A 407 -355.703-167.224 149.865 1.00 69.55 C ANISOU 2672 C11 DLB A 407 9273 8181 8971 -96 -1277 635 C HETATM 2673 C13 DLB A 407 -357.752-168.425 150.049 1.00 80.74 C ANISOU 2673 C13 DLB A 407 10595 9596 10488 -115 -1358 590 C HETATM 2674 C15 DLB A 407 -356.897-167.956 147.885 1.00 71.62 C ANISOU 2674 C15 DLB A 407 9628 8460 9125 -205 -1482 725 C HETATM 2675 C17 DLB A 407 -353.374-167.482 147.776 1.00 76.09 C ANISOU 2675 C17 DLB A 407 10378 9084 9448 -205 -1222 704 C HETATM 2676 C18 DLB A 407 -352.331-167.110 146.699 1.00 72.01 C ANISOU 2676 C18 DLB A 407 9979 8590 8792 -269 -1204 753 C HETATM 2677 C19 DLB A 407 -353.617-169.009 147.765 1.00 74.37 C ANISOU 2677 C19 DLB A 407 10194 8905 9160 -227 -1179 631 C HETATM 2678 C21 DLB A 407 -359.453-160.979 148.249 1.00101.01 C ANISOU 2678 C21 DLB A 407 12805 11680 13895 -6 -1961 1053 C HETATM 2679 C22 DLB A 407 -358.685-160.366 147.247 1.00100.76 C ANISOU 2679 C22 DLB A 407 12896 11642 13747 -59 -2044 1183 C HETATM 2680 C24 DLB A 407 -358.990-159.151 146.709 1.00107.79 C ANISOU 2680 C24 DLB A 407 13741 12420 14795 -59 -2198 1312 C HETATM 2681 C25 DLB A 407 -360.135-158.540 147.223 1.00115.67 C ANISOU 2681 C25 DLB A 407 14544 13297 16109 11 -2268 1297 C HETATM 2682 C26 DLB A 407 -360.889-159.140 148.206 1.00116.66 C ANISOU 2682 C26 DLB A 407 14541 13431 16354 64 -2170 1152 C HETATM 2683 C27 DLB A 407 -360.569-160.391 148.754 1.00110.64 C ANISOU 2683 C27 DLB A 407 13841 12793 15402 51 -2014 1030 C HETATM 2684 C28 DLB A 407 -360.533-157.203 146.684 1.00123.60 C ANISOU 2684 C28 DLB A 407 15474 14152 17335 22 -2448 1442 C HETATM 2685 C1 DLB A 407 -357.018-164.668 147.396 1.00 71.86 C ANISOU 2685 C1 DLB A 407 9559 8340 9404 -165 -1678 925 C HETATM 2686 C2 DLB A 407 -357.846-163.517 146.847 1.00 81.73 C ANISOU 2686 C2 DLB A 407 10742 9501 10812 -167 -1857 1042 C HETATM 2687 C3 DLB A 407 -357.748-162.309 147.768 1.00 87.96 C ANISOU 2687 C3 DLB A 407 11409 10202 11809 -86 -1813 1022 C HETATM 2688 C4 DLB A 407 -356.556-162.302 148.729 1.00 80.90 C ANISOU 2688 C4 DLB A 407 10536 9345 10857 -48 -1621 924 C HETATM 2689 C5 DLB A 407 -355.353-162.917 148.066 1.00 77.11 C ANISOU 2689 C5 DLB A 407 10218 8951 10128 -108 -1559 939 C HETATM 2690 N6 DLB A 407 -355.615-164.323 147.773 1.00 77.81 N ANISOU 2690 N6 DLB A 407 10366 9114 10083 -147 -1543 896 N HETATM 2691 C7 DLB A 407 -354.550-165.210 147.897 1.00 78.71 C ANISOU 2691 C7 DLB A 407 10569 9302 10037 -161 -1407 829 C HETATM 2692 O8 DLB A 407 -353.460-164.745 148.230 1.00 86.69 O ANISOU 2692 O8 DLB A 407 11598 10314 11025 -143 -1316 816 O HETATM 2693 C9 DLB A 407 -354.727-166.708 147.600 1.00 78.87 C ANISOU 2693 C9 DLB A 407 10653 9384 9931 -202 -1377 773 C HETATM 2694 C12 DLB A 407 -356.681-167.789 150.668 1.00 69.59 C ANISOU 2694 C12 DLB A 407 9189 8182 9069 -77 -1263 574 C HETATM 2695 C14 DLB A 407 -357.882-168.520 148.679 1.00 77.43 C ANISOU 2695 C14 DLB A 407 10262 9186 9971 -176 -1473 664 C HETATM 2696 CL DLB A 407 -358.980-169.131 151.029 1.00 83.37 CL ANISOU 2696 CL DLB A 407 10810 9924 10944 -102 -1331 512 CL HETATM 2697 O20 DLB A 407 -358.902-162.183 148.576 1.00 91.95 O ANISOU 2697 O20 DLB A 407 11745 10646 12546 -27 -1826 961 O HETATM 2698 O23 DLB A 407 -357.642-161.170 146.936 1.00 96.31 O ANISOU 2698 O23 DLB A 407 12491 11191 12911 -113 -1945 1159 O HETATM 2699 C29 DLB A 407 -360.193-156.149 147.753 1.00127.25 C ANISOU 2699 C29 DLB A 407 15821 14513 18015 108 -2320 1349 C HETATM 2700 C30 DLB A 407 -358.710-155.902 147.835 1.00129.93 C ANISOU 2700 C30 DLB A 407 16302 14912 18153 83 -2192 1339 C HETATM 2701 O31 DLB A 407 -358.042-156.884 148.495 1.00133.26 O ANISOU 2701 O31 DLB A 407 16793 15467 18374 80 -2003 1202 O HETATM 2702 O32 DLB A 407 -358.084-154.947 147.399 1.00129.48 O ANISOU 2702 O32 DLB A 407 16294 14793 18108 63 -2243 1440 O HETATM 2703 C1 BOG A 408 -327.993-157.892 161.474 1.00 96.65 C ANISOU 2703 C1 BOG A 408 11938 11701 13084 -344 -582 497 C HETATM 2704 O1 BOG A 408 -327.960-159.203 160.912 1.00 92.85 O ANISOU 2704 O1 BOG A 408 11435 11217 12627 -281 -556 526 O HETATM 2705 C2 BOG A 408 -326.557-157.373 161.542 1.00102.67 C ANISOU 2705 C2 BOG A 408 12592 12447 13971 -387 -588 507 C HETATM 2706 O2 BOG A 408 -325.831-158.138 162.522 1.00105.34 O ANISOU 2706 O2 BOG A 408 12847 12810 14367 -404 -704 541 O HETATM 2707 C3 BOG A 408 -326.477-155.883 161.864 1.00102.49 C ANISOU 2707 C3 BOG A 408 12589 12410 13943 -456 -589 470 C HETATM 2708 O3 BOG A 408 -325.146-155.416 161.623 1.00108.31 O ANISOU 2708 O3 BOG A 408 13223 13123 14806 -491 -569 481 O HETATM 2709 C4 BOG A 408 -327.422-155.088 160.976 1.00 98.74 C ANISOU 2709 C4 BOG A 408 12208 11897 13412 -439 -499 450 C HETATM 2710 O4 BOG A 408 -327.444-153.721 161.409 1.00 92.81 O ANISOU 2710 O4 BOG A 408 11474 11118 12672 -501 -509 411 O HETATM 2711 C5 BOG A 408 -328.829-155.676 161.038 1.00100.41 C ANISOU 2711 C5 BOG A 408 12511 12127 13514 -392 -509 440 C HETATM 2712 O5 BOG A 408 -328.821-157.058 160.665 1.00 98.01 O ANISOU 2712 O5 BOG A 408 12193 11845 13203 -335 -502 473 O HETATM 2713 C6 BOG A 408 -329.806-154.913 160.139 1.00 93.62 C ANISOU 2713 C6 BOG A 408 11732 11221 12617 -373 -442 433 C HETATM 2714 O6 BOG A 408 -331.135-154.995 160.671 1.00 82.20 O ANISOU 2714 O6 BOG A 408 10353 9785 11094 -357 -474 399 O HETATM 2715 C1' BOG A 408 -329.117-159.988 161.179 1.00 79.94 C ANISOU 2715 C1' BOG A 408 9876 9605 10892 -250 -587 526 C HETATM 2716 C2' BOG A 408 -328.778-161.430 160.822 1.00 70.99 C ANISOU 2716 C2' BOG A 408 8693 8459 9822 -194 -582 558 C HETATM 2717 C3' BOG A 408 -329.967-162.344 161.091 1.00 72.51 C ANISOU 2717 C3' BOG A 408 8962 8672 9918 -165 -615 564 C HETATM 2718 C4' BOG A 408 -329.617-163.813 160.884 1.00 71.08 C ANISOU 2718 C4' BOG A 408 8727 8464 9816 -113 -624 595 C HETATM 2719 C5' BOG A 408 -330.800-164.688 161.283 1.00 74.35 C ANISOU 2719 C5' BOG A 408 9219 8899 10133 -98 -668 606 C HETATM 2720 C6' BOG A 408 -330.502-166.178 161.130 1.00 77.25 C ANISOU 2720 C6' BOG A 408 9534 9225 10592 -48 -685 639 C HETATM 2721 C7' BOG A 408 -331.748-166.997 161.465 1.00 79.41 C ANISOU 2721 C7' BOG A 408 9893 9516 10762 -40 -721 650 C HETATM 2722 C8' BOG A 408 -331.465-168.485 161.486 1.00 88.15 C ANISOU 2722 C8' BOG A 408 10949 10572 11972 2 -757 691 C HETATM 2723 C1 BOG A 409 -351.243-165.861 150.903 1.00 87.86 C ANISOU 2723 C1 BOG A 409 11698 10535 11148 -47 -973 605 C HETATM 2724 O1 BOG A 409 -351.716-166.876 151.785 1.00 88.64 O ANISOU 2724 O1 BOG A 409 11757 10657 11265 -28 -932 537 O HETATM 2725 C2 BOG A 409 -351.581-164.469 151.442 1.00 85.90 C ANISOU 2725 C2 BOG A 409 11365 10228 11044 -13 -1007 622 C HETATM 2726 O2 BOG A 409 -353.014-164.342 151.611 1.00 90.03 O ANISOU 2726 O2 BOG A 409 11808 10714 11686 2 -1083 618 O HETATM 2727 C3 BOG A 409 -350.948-163.410 150.530 1.00 86.24 C ANISOU 2727 C3 BOG A 409 11459 10242 11066 -39 -1048 706 C HETATM 2728 O3 BOG A 409 -351.177-162.088 151.034 1.00 86.36 O ANISOU 2728 O3 BOG A 409 11393 10186 11235 -6 -1075 719 O HETATM 2729 C4 BOG A 409 -349.447-163.689 150.389 1.00 81.08 C ANISOU 2729 C4 BOG A 409 10876 9633 10298 -59 -947 693 C HETATM 2730 O4 BOG A 409 -348.818-162.815 149.447 1.00 81.71 O ANISOU 2730 O4 BOG A 409 11017 9695 10335 -101 -972 771 O HETATM 2731 C5 BOG A 409 -349.206-165.105 149.881 1.00 81.11 C ANISOU 2731 C5 BOG A 409 10952 9694 10170 -89 -905 661 C HETATM 2732 O5 BOG A 409 -349.838-166.055 150.733 1.00 78.06 O ANISOU 2732 O5 BOG A 409 10518 9324 9818 -58 -887 597 O HETATM 2733 C6 BOG A 409 -347.719-165.434 149.829 1.00 76.69 C ANISOU 2733 C6 BOG A 409 10436 9167 9538 -100 -793 633 C HETATM 2734 O6 BOG A 409 -347.248-165.607 151.170 1.00 74.13 O ANISOU 2734 O6 BOG A 409 10038 8844 9282 -49 -730 576 O HETATM 2735 C1' BOG A 409 -351.764-168.134 151.115 1.00 83.54 C ANISOU 2735 C1' BOG A 409 11181 10044 10517 -62 -930 526 C HETATM 2736 C2' BOG A 409 -352.448-169.147 152.017 1.00 87.90 C ANISOU 2736 C2' BOG A 409 11687 10608 11105 -50 -905 468 C HETATM 2737 C3' BOG A 409 -352.885-170.361 151.212 1.00 89.30 C ANISOU 2737 C3' BOG A 409 11924 10802 11205 -90 -930 458 C HETATM 2738 C4' BOG A 409 -353.791-171.236 152.066 1.00 90.70 C ANISOU 2738 C4' BOG A 409 12046 10982 11435 -85 -922 413 C HETATM 2739 C5' BOG A 409 -354.550-172.240 151.209 1.00 87.69 C ANISOU 2739 C5' BOG A 409 11709 10605 11004 -131 -974 407 C HETATM 2740 C6' BOG A 409 -355.509-173.057 152.062 1.00 83.27 C ANISOU 2740 C6' BOG A 409 11088 10044 10507 -134 -966 366 C HETATM 2741 C7' BOG A 409 -356.949-172.834 151.625 1.00 83.24 C ANISOU 2741 C7' BOG A 409 11031 10027 10570 -156 -1069 381 C HETATM 2742 C8' BOG A 409 -357.880-173.299 152.719 1.00 86.56 C ANISOU 2742 C8' BOG A 409 11362 10444 11082 -155 -1038 336 C HETATM 2743 C1 BOG A 410 -377.118-183.268 160.161 0.00 70.52 C ANISOU 2743 C1 BOG A 410 7760 8351 10685 -1195 -482 -439 C HETATM 2744 O1 BOG A 410 -376.170-182.222 159.954 0.00 69.47 O ANISOU 2744 O1 BOG A 410 7683 8220 10491 -1086 -520 -410 O HETATM 2745 C2 BOG A 410 -376.964-183.831 161.571 0.00 70.67 C ANISOU 2745 C2 BOG A 410 7842 8418 10590 -1306 -272 -474 C HETATM 2746 O2 BOG A 410 -375.667-184.420 161.713 0.00 69.29 O ANISOU 2746 O2 BOG A 410 7893 8265 10168 -1302 -282 -388 O HETATM 2747 C3 BOG A 410 -378.032-184.877 161.859 0.00 71.97 C ANISOU 2747 C3 BOG A 410 7936 8578 10833 -1435 -215 -507 C HETATM 2748 O3 BOG A 410 -377.957-185.276 163.231 0.00 72.38 O ANISOU 2748 O3 BOG A 410 8041 8680 10779 -1555 -11 -538 O HETATM 2749 C4 BOG A 410 -379.409-184.301 161.567 0.00 73.55 C ANISOU 2749 C4 BOG A 410 7878 8743 11324 -1431 -229 -593 C HETATM 2750 O4 BOG A 410 -380.399-185.323 161.727 0.00 74.80 O ANISOU 2750 O4 BOG A 410 7967 8893 11560 -1553 -189 -620 O HETATM 2751 C5 BOG A 410 -379.459-183.763 160.142 0.00 73.30 C ANISOU 2751 C5 BOG A 410 7796 8661 11393 -1314 -464 -542 C HETATM 2752 O5 BOG A 410 -378.444-182.776 159.942 0.00 72.09 O ANISOU 2752 O5 BOG A 410 7721 8513 11157 -1200 -505 -507 O HETATM 2753 C6 BOG A 410 -380.825-183.159 159.835 0.00 75.06 C ANISOU 2753 C6 BOG A 410 7747 8836 11936 -1305 -506 -611 C HETATM 2754 O6 BOG A 410 -380.893-182.813 158.447 0.00 75.02 O ANISOU 2754 O6 BOG A 410 7716 8786 12003 -1220 -758 -538 O HETATM 2755 C1' BOG A 410 -376.154-181.807 158.591 0.00 69.31 C ANISOU 2755 C1' BOG A 410 7647 8160 10526 -999 -729 -353 C HETATM 2756 C2' BOG A 410 -374.827-181.132 158.270 0.00 67.87 C ANISOU 2756 C2' BOG A 410 7606 7989 10194 -904 -776 -293 C HETATM 2757 C3' BOG A 410 -374.685-180.942 156.766 0.00 67.73 C ANISOU 2757 C3' BOG A 410 7623 7939 10170 -844 -997 -216 C HETATM 2758 C4' BOG A 410 -373.311-180.397 156.398 0.00 66.35 C ANISOU 2758 C4' BOG A 410 7603 7779 9829 -764 -1034 -155 C HETATM 2759 C5' BOG A 410 -373.212-180.187 154.892 0.00 66.45 C ANISOU 2759 C5' BOG A 410 7659 7769 9822 -728 -1245 -81 C HETATM 2760 C6' BOG A 410 -371.913-179.488 154.512 0.00 65.30 C ANISOU 2760 C6' BOG A 410 7644 7634 9533 -653 -1271 -26 C HETATM 2761 C7' BOG A 410 -371.918-179.117 153.034 0.00 65.72 C ANISOU 2761 C7' BOG A 410 7730 7669 9570 -635 -1478 49 C HETATM 2762 C8' BOG A 410 -370.677-178.338 152.662 0.00 64.74 C ANISOU 2762 C8' BOG A 410 7725 7555 9318 -569 -1495 101 C HETATM 2763 C1 BOG A 411 -347.418-159.288 157.919 1.00 81.56 C ANISOU 2763 C1 BOG A 411 10543 9589 10858 34 -619 306 C HETATM 2764 O1 BOG A 411 -348.244-158.163 158.213 1.00 85.15 O ANISOU 2764 O1 BOG A 411 10925 9960 11467 45 -621 258 O HETATM 2765 C2 BOG A 411 -348.156-160.240 156.980 1.00 87.16 C ANISOU 2765 C2 BOG A 411 11283 10315 11521 50 -670 362 C HETATM 2766 O2 BOG A 411 -349.326-160.719 157.642 1.00 86.39 O ANISOU 2766 O2 BOG A 411 11137 10225 11461 53 -658 297 O HETATM 2767 C3 BOG A 411 -347.303-161.442 156.602 1.00 85.46 C ANISOU 2767 C3 BOG A 411 11137 10169 11163 40 -656 399 C HETATM 2768 O3 BOG A 411 -347.976-162.154 155.549 1.00 81.56 O ANISOU 2768 O3 BOG A 411 10681 9679 10629 45 -706 448 O HETATM 2769 C4 BOG A 411 -345.913-160.975 156.166 1.00 76.86 C ANISOU 2769 C4 BOG A 411 10083 9081 10041 28 -637 442 C HETATM 2770 O4 BOG A 411 -345.055-162.111 156.016 1.00 74.28 O ANISOU 2770 O4 BOG A 411 9797 8811 9617 21 -607 453 O HETATM 2771 C5 BOG A 411 -345.291-159.995 157.169 1.00 75.12 C ANISOU 2771 C5 BOG A 411 9819 8842 9880 15 -602 394 C HETATM 2772 O5 BOG A 411 -346.159-158.878 157.381 1.00 71.49 O ANISOU 2772 O5 BOG A 411 9307 8311 9544 24 -619 364 O HETATM 2773 C6 BOG A 411 -343.893-159.496 156.769 1.00 69.85 C ANISOU 2773 C6 BOG A 411 9173 8172 9194 -1 -582 434 C HETATM 2774 O6 BOG A 411 -343.853-158.964 155.436 1.00 60.93 O ANISOU 2774 O6 BOG A 411 8081 7000 8069 -4 -613 513 O HETATM 2775 C1' BOG A 411 -347.937-157.629 159.497 1.00 86.84 C ANISOU 2775 C1' BOG A 411 11104 10180 11710 14 -549 155 C HETATM 2776 C2' BOG A 411 -349.229-157.479 160.291 1.00 95.98 C ANISOU 2776 C2' BOG A 411 12186 11309 12972 11 -507 48 C HETATM 2777 C3' BOG A 411 -350.094-158.724 160.141 1.00 99.71 C ANISOU 2777 C3' BOG A 411 12665 11834 13386 18 -522 61 C HETATM 2778 C4' BOG A 411 -351.195-158.787 161.192 1.00104.62 C ANISOU 2778 C4' BOG A 411 13218 12457 14076 -8 -448 -64 C HETATM 2779 C5' BOG A 411 -350.689-159.362 162.512 1.00100.60 C ANISOU 2779 C5' BOG A 411 12750 12046 13428 -83 -367 -139 C HETATM 2780 C6' BOG A 411 -351.855-159.794 163.396 1.00 92.15 C ANISOU 2780 C6' BOG A 411 11634 11001 12379 -126 -291 -246 C HETATM 2781 C7' BOG A 411 -351.357-160.382 164.708 1.00 86.18 C ANISOU 2781 C7' BOG A 411 10936 10348 11459 -223 -223 -304 C HETATM 2782 C8' BOG A 411 -352.505-160.685 165.644 1.00 85.87 C ANISOU 2782 C8' BOG A 411 10855 10337 11434 -287 -126 -423 C HETATM 2783 C1 BOG A 412 -344.909-153.320 175.574 0.00 67.04 C ANISOU 2783 C1 BOG A 412 8887 8299 8285 -1434 287 -1367 C HETATM 2784 O1 BOG A 412 -345.297-154.689 175.669 0.00 66.47 O ANISOU 2784 O1 BOG A 412 8863 8322 8071 -1446 245 -1259 O HETATM 2785 C2 BOG A 412 -343.570-153.172 176.296 0.00 67.60 C ANISOU 2785 C2 BOG A 412 9041 8456 8189 -1566 191 -1334 C HETATM 2786 O2 BOG A 412 -343.770-153.330 177.707 0.00 69.25 O ANISOU 2786 O2 BOG A 412 9347 8786 8178 -1786 262 -1462 O HETATM 2787 C3 BOG A 412 -342.910-151.829 176.027 0.00 67.95 C ANISOU 2787 C3 BOG A 412 9035 8397 8385 -1538 198 -1401 C HETATM 2788 O3 BOG A 412 -341.586-151.830 176.571 0.00 68.33 O ANISOU 2788 O3 BOG A 412 9149 8527 8284 -1648 80 -1337 O HETATM 2789 C4 BOG A 412 -342.843-151.590 174.528 0.00 66.47 C ANISOU 2789 C4 BOG A 412 8752 8077 8426 -1323 142 -1276 C HETATM 2790 O4 BOG A 412 -342.279-150.300 174.268 0.00 66.91 O ANISOU 2790 O4 BOG A 412 8763 8028 8634 -1304 154 -1336 O HETATM 2791 C5 BOG A 412 -344.246-151.668 173.944 0.00 66.17 C ANISOU 2791 C5 BOG A 412 8642 7958 8543 -1213 237 -1323 C HETATM 2792 O5 BOG A 412 -344.819-152.954 174.193 0.00 65.77 O ANISOU 2792 O5 BOG A 412 8635 8009 8346 -1237 230 -1265 O HETATM 2793 C6 BOG A 412 -344.220-151.405 172.443 0.00 64.93 C ANISOU 2793 C6 BOG A 412 8403 7673 8595 -1019 170 -1191 C HETATM 2794 O6 BOG A 412 -343.498-150.195 172.185 0.00 65.33 O ANISOU 2794 O6 BOG A 412 8421 7627 8774 -1006 160 -1219 O HETATM 2795 C1' BOG A 412 -346.554-154.971 175.058 0.00 66.02 C ANISOU 2795 C1' BOG A 412 8732 8201 8150 -1339 322 -1282 C HETATM 2796 C2' BOG A 412 -346.689-156.487 174.970 0.00 65.16 C ANISOU 2796 C2' BOG A 412 8677 8184 7898 -1333 239 -1125 C HETATM 2797 C3' BOG A 412 -348.097-156.933 174.595 0.00 65.00 C ANISOU 2797 C3' BOG A 412 8595 8126 7975 -1267 328 -1165 C HETATM 2798 C4' BOG A 412 -348.153-158.455 174.559 0.00 64.25 C ANISOU 2798 C4' BOG A 412 8560 8119 7731 -1274 242 -1009 C HETATM 2799 C5' BOG A 412 -349.582-158.974 174.652 0.00 64.61 C ANISOU 2799 C5' BOG A 412 8571 8168 7810 -1283 354 -1084 C HETATM 2800 C6' BOG A 412 -349.583-160.439 175.073 0.00 64.44 C ANISOU 2800 C6' BOG A 412 8641 8257 7588 -1362 291 -961 C HETATM 2801 C7' BOG A 412 -350.991-160.916 175.408 0.00 65.16 C ANISOU 2801 C7' BOG A 412 8706 8367 7683 -1415 424 -1057 C HETATM 2802 C8' BOG A 412 -350.951-162.258 176.108 0.00 65.44 C ANISOU 2802 C8' BOG A 412 8853 8521 7489 -1543 376 -954 C HETATM 2803 O HOH A 501 -343.249-140.056 158.210 1.00 71.47 O HETATM 2804 O HOH A 502 -361.103-177.483 154.459 1.00 67.95 O HETATM 2805 O HOH A 503 -343.364-152.861 149.987 1.00 52.98 O HETATM 2806 O HOH A 504 -343.875-148.214 142.539 1.00 64.88 O HETATM 2807 O HOH A 505 -331.776-158.655 164.109 1.00 65.06 O HETATM 2808 O HOH A 506 -381.936-201.788 153.805 1.00 67.91 O HETATM 2809 O HOH A 507 -355.532-186.053 141.684 1.00 64.85 O HETATM 2810 O HOH A 508 -355.575-187.920 143.966 1.00 73.14 O HETATM 2811 O HOH A 509 -341.842-149.460 140.603 1.00 78.45 O HETATM 2812 O HOH A 510 -339.233-144.088 147.453 1.00 52.65 O HETATM 2813 O HOH A 511 -383.820-197.753 156.324 1.00 69.38 O HETATM 2814 O HOH A 512 -343.288-158.736 140.210 1.00 73.45 O HETATM 2815 O HOH A 513 -361.160-180.719 150.125 1.00 58.91 O HETATM 2816 O HOH A 514 -341.294-139.649 150.233 1.00 67.28 O HETATM 2817 O HOH A 515 -335.030-149.844 146.419 1.00 60.94 O HETATM 2818 O HOH A 516 -345.343-140.221 152.289 1.00 60.37 O HETATM 2819 O HOH A 517 -334.706-136.001 147.592 1.00 64.15 O HETATM 2820 O HOH A 518 -335.419-157.203 163.165 1.00 63.00 O HETATM 2821 O HOH A 519 -357.288-167.515 159.162 1.00 64.51 O HETATM 2822 O HOH A 520 -338.214-153.567 170.250 1.00 59.85 O HETATM 2823 O HOH A 521 -346.991-153.164 150.894 1.00 65.36 O HETATM 2824 O HOH A 522 -335.182-135.199 149.947 1.00 62.63 O HETATM 2825 O HOH A 523 -335.807-157.447 169.183 1.00 52.85 O HETATM 2826 O HOH A 524 -348.755-153.786 152.548 1.00 69.39 O HETATM 2827 O HOH A 525 -335.525-157.689 165.934 1.00 58.50 O HETATM 2828 O HOH A 526 -333.230-134.360 153.528 1.00 71.41 O HETATM 2829 O HOH A 527 -344.209-141.080 148.060 1.00 67.28 O HETATM 2830 O HOH A 528 -333.679-147.044 146.861 1.00 69.26 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 2674 2693 CONECT 2672 2671 2694 CONECT 2673 2694 2695 2696 CONECT 2674 2671 2695 CONECT 2675 2676 2677 2693 CONECT 2676 2675 CONECT 2677 2675 CONECT 2678 2679 2683 2697 CONECT 2679 2678 2680 2698 CONECT 2680 2679 2681 CONECT 2681 2680 2682 2684 CONECT 2682 2681 2683 CONECT 2683 2678 2682 CONECT 2684 2681 2699 CONECT 2685 2686 2690 CONECT 2686 2685 2687 CONECT 2687 2686 2688 2697 2698 CONECT 2688 2687 2689 CONECT 2689 2688 2690 CONECT 2690 2685 2689 2691 CONECT 2691 2690 2692 2693 CONECT 2692 2691 CONECT 2693 2671 2675 2691 CONECT 2694 2672 2673 CONECT 2695 2673 2674 CONECT 2696 2673 CONECT 2697 2678 2687 CONECT 2698 2679 2687 CONECT 2699 2684 2700 CONECT 2700 2699 2701 2702 CONECT 2701 2700 CONECT 2702 2700 CONECT 2703 2704 2705 2712 CONECT 2704 2703 2715 CONECT 2705 2703 2706 2707 CONECT 2706 2705 CONECT 2707 2705 2708 2709 CONECT 2708 2707 CONECT 2709 2707 2710 2711 CONECT 2710 2709 CONECT 2711 2709 2712 2713 CONECT 2712 2703 2711 CONECT 2713 2711 2714 CONECT 2714 2713 CONECT 2715 2704 2716 CONECT 2716 2715 2717 CONECT 2717 2716 2718 CONECT 2718 2717 2719 CONECT 2719 2718 2720 CONECT 2720 2719 2721 CONECT 2721 2720 2722 CONECT 2722 2721 CONECT 2723 2724 2725 2732 CONECT 2724 2723 2735 CONECT 2725 2723 2726 2727 CONECT 2726 2725 CONECT 2727 2725 2728 2729 CONECT 2728 2727 CONECT 2729 2727 2730 2731 CONECT 2730 2729 CONECT 2731 2729 2732 2733 CONECT 2732 2723 2731 CONECT 2733 2731 2734 CONECT 2734 2733 CONECT 2735 2724 2736 CONECT 2736 2735 2737 CONECT 2737 2736 2738 CONECT 2738 2737 2739 CONECT 2739 2738 2740 CONECT 2740 2739 2741 CONECT 2741 2740 2742 CONECT 2742 2741 CONECT 2743 2744 2745 2752 CONECT 2744 2743 2755 CONECT 2745 2743 2746 2747 CONECT 2746 2745 CONECT 2747 2745 2748 2749 CONECT 2748 2747 CONECT 2749 2747 2750 2751 CONECT 2750 2749 CONECT 2751 2749 2752 2753 CONECT 2752 2743 2751 CONECT 2753 2751 2754 CONECT 2754 2753 CONECT 2755 2744 2756 CONECT 2756 2755 2757 CONECT 2757 2756 2758 CONECT 2758 2757 2759 CONECT 2759 2758 2760 CONECT 2760 2759 2761 CONECT 2761 2760 2762 CONECT 2762 2761 CONECT 2763 2764 2765 2772 CONECT 2764 2763 2775 CONECT 2765 2763 2766 2767 CONECT 2766 2765 CONECT 2767 2765 2768 2769 CONECT 2768 2767 CONECT 2769 2767 2770 2771 CONECT 2770 2769 CONECT 2771 2769 2772 2773 CONECT 2772 2763 2771 CONECT 2773 2771 2774 CONECT 2774 2773 CONECT 2775 2764 2776 CONECT 2776 2775 2777 CONECT 2777 2776 2778 CONECT 2778 2777 2779 CONECT 2779 2778 2780 CONECT 2780 2779 2781 CONECT 2781 2780 2782 CONECT 2782 2781 CONECT 2783 2784 2785 2792 CONECT 2784 2783 2795 CONECT 2785 2783 2786 2787 CONECT 2786 2785 CONECT 2787 2785 2788 2789 CONECT 2788 2787 CONECT 2789 2787 2790 2791 CONECT 2790 2789 CONECT 2791 2789 2792 2793 CONECT 2792 2783 2791 CONECT 2793 2791 2794 CONECT 2794 2793 CONECT 2795 2784 2796 CONECT 2796 2795 2797 CONECT 2797 2796 2798 CONECT 2798 2797 2799 CONECT 2799 2798 2800 CONECT 2800 2799 2801 CONECT 2801 2800 2802 CONECT 2802 2801 MASTER 356 0 13 15 4 0 0 6 2829 1 220 27 END