HEADER MEMBRANE PROTEIN 23-JAN-18 6FKB TITLE CRYSTAL STRUCTURE OF N2C/D282C STABILIZED OPSIN BOUND TO RS13 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 6FKB 1 COMPND REMARK HETNAM SITE REVDAT 2 11-APR-18 6FKB 1 JRNL REVDAT 1 04-APR-18 6FKB 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. 3.03 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (DEV_2481: ???) 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) : 3.03 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 45.90 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 94.1 REMARK 3 NUMBER OF REFLECTIONS : 23041 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.258 REMARK 3 R VALUE (WORKING SET) : 0.258 REMARK 3 FREE R VALUE : 0.272 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.950 REMARK 3 FREE R VALUE TEST SET COUNT : 1140 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 45.9000 - 6.0564 0.99 2965 156 0.2310 0.2399 REMARK 3 2 6.0564 - 4.8088 0.99 2874 164 0.2212 0.2292 REMARK 3 3 4.8088 - 4.2014 0.98 2869 137 0.1960 0.2200 REMARK 3 4 4.2014 - 3.8175 0.97 2789 145 0.2495 0.2752 REMARK 3 5 3.8175 - 3.5440 0.95 2750 136 0.2984 0.3149 REMARK 3 6 3.5440 - 3.3351 0.92 2658 153 0.3583 0.3390 REMARK 3 7 3.3351 - 3.1681 0.88 2549 116 0.4000 0.4387 REMARK 3 8 3.1681 - 3.0302 0.85 2447 133 0.4523 0.4637 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) : 0.500 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 33.850 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 : 0.004 2891 REMARK 3 ANGLE : 0.618 3922 REMARK 3 CHIRALITY : 0.039 452 REMARK 3 PLANARITY : 0.004 459 REMARK 3 DIHEDRAL : 13.357 1703 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 240 ) REMARK 3 ORIGIN FOR THE GROUP (A):-228.9737 40.0959 36.8233 REMARK 3 T TENSOR REMARK 3 T11: 0.4953 T22: 0.3950 REMARK 3 T33: 0.5339 T12: 0.0204 REMARK 3 T13: -0.0683 T23: 0.0588 REMARK 3 L TENSOR REMARK 3 L11: 2.3256 L22: 3.3209 REMARK 3 L33: 1.3795 L12: 1.3251 REMARK 3 L13: 0.1208 L23: -0.0479 REMARK 3 S TENSOR REMARK 3 S11: -0.1018 S12: 0.1926 S13: 0.0571 REMARK 3 S21: -0.3768 S22: 0.1800 S23: 0.0253 REMARK 3 S31: -0.0209 S32: -0.0283 S33: 0.0042 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 328 ) REMARK 3 ORIGIN FOR THE GROUP (A):-236.5218 34.4888 46.0263 REMARK 3 T TENSOR REMARK 3 T11: 0.6988 T22: 0.5043 REMARK 3 T33: 0.9162 T12: -0.0688 REMARK 3 T13: -0.1519 T23: -0.0058 REMARK 3 L TENSOR REMARK 3 L11: 3.9693 L22: 2.7989 REMARK 3 L33: 2.6178 L12: 1.3608 REMARK 3 L13: -0.2096 L23: 0.8199 REMARK 3 S TENSOR REMARK 3 S11: -0.2716 S12: 0.1752 S13: 0.4493 REMARK 3 S21: -0.1681 S22: 0.0246 S23: 0.5724 REMARK 3 S31: -0.3676 S32: -0.2258 S33: -0.0548 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 6FKB 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_1200008393. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-NOV-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 : 24484 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.030 REMARK 200 RESOLUTION RANGE LOW (A) : 47.550 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 11.28 REMARK 200 R MERGE (I) : 0.26240 REMARK 200 R SYM (I) : 0.26240 REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.8900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.03 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.13 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 11.81 REMARK 200 R MERGE FOR SHELL (I) : 1.03020 REMARK 200 R SYM FOR SHELL (I) : 1.03020 REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.650 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 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): 8.11 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 121.42600 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.10533 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.15633 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 121.42600 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.10533 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.15633 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 121.42600 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.10533 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.15633 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 121.42600 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.10533 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.15633 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 121.42600 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.10533 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.15633 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 121.42600 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.10533 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.15633 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.21067 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 74.31267 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.21067 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 74.31267 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.21067 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 74.31267 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.21067 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 74.31267 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.21067 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 74.31267 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.21067 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 74.31267 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: 3660 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 18000 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 35.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 CYS A 322 C 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 GLU A 25 -36.60 -130.64 REMARK 500 GLN A 28 51.66 -102.18 REMARK 500 ASN A 145 55.34 -111.43 REMARK 500 SER A 176 -164.19 63.89 REMARK 500 HIS A 195 96.76 -57.87 REMARK 500 PHE A 212 -51.05 -143.79 REMARK 500 GLN A 279 36.52 -89.43 REMARK 500 PRO A 285 26.07 -62.68 REMARK 500 ILE A 286 -54.71 -148.33 REMARK 500 ILE A 307 -56.11 -125.52 REMARK 500 LYS A 325 -157.75 -81.79 REMARK 500 ASN A 326 144.65 175.46 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 NAG A 402 REMARK 610 NAG A 403 REMARK 610 BMA A 404 REMARK 610 MAN A 405 REMARK 610 MAN A 406 REMARK 610 BOG A 409 DBREF 6FKB A 1 328 UNP P02699 OPSD_BOVIN 1 328 SEQADV 6FKB ACE A 0 UNP P02699 ACETYLATION SEQADV 6FKB CYS A 2 UNP P02699 ASN 2 CONFLICT SEQADV 6FKB CYS A 282 UNP P02699 ASP 282 CONFLICT SEQRES 1 A 329 ACE MET CYS GLY THR GLU GLY PRO ASN PHE TYR VAL PRO SEQRES 2 A 329 PHE SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU SEQRES 3 A 329 ALA PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER SEQRES 4 A 329 MET LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY SEQRES 5 A 329 PHE PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN SEQRES 6 A 329 HIS LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU SEQRES 7 A 329 ASN LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY SEQRES 8 A 329 PHE THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE SEQRES 9 A 329 VAL PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE SEQRES 10 A 329 ALA THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL SEQRES 11 A 329 VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO SEQRES 12 A 329 MET SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET SEQRES 13 A 329 GLY VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA SEQRES 14 A 329 ALA PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU SEQRES 15 A 329 GLY MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO SEQRES 16 A 329 HIS GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET SEQRES 17 A 329 PHE VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE SEQRES 18 A 329 PHE CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA SEQRES 19 A 329 ALA ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA SEQRES 20 A 329 GLU LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE SEQRES 21 A 329 ALA PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA SEQRES 22 A 329 PHE TYR ILE PHE THR HIS GLN GLY SER CYS PHE GLY PRO SEQRES 23 A 329 ILE PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER SEQRES 24 A 329 ALA VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS SEQRES 25 A 329 GLN PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY SEQRES 26 A 329 LYS ASN PRO LEU HET ACE A 0 3 HET PLM A 401 17 HET NAG A 402 14 HET NAG A 403 14 HET BMA A 404 11 HET MAN A 405 11 HET MAN A 406 11 HET BOG A 407 20 HET BOG A 408 20 HET BOG A 409 19 HET BOG A 410 20 HET BOG A 411 20 HET DLH A 412 24 HETNAM ACE ACETYL GROUP HETNAM PLM PALMITIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE HETNAM DLH 2-(4-CHLOROPHENYL)-1-SPIRO[1,3-BENZODIOXOLE-2,4'- HETNAM 2 DLH PIPERIDINE]-1'-YL-ETHANONE FORMUL 1 ACE C2 H4 O FORMUL 2 PLM C16 H32 O2 FORMUL 3 NAG 2(C8 H15 N O6) FORMUL 5 BMA C6 H12 O6 FORMUL 6 MAN 2(C6 H12 O6) FORMUL 8 BOG 5(C14 H28 O6) FORMUL 13 DLH C19 H18 CL N O3 FORMUL 14 HOH *2(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 LEU A 99 1 10 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 ILE A 286 MET A 288 5 3 HELIX 14 AB5 THR A 289 LYS A 296 1 8 HELIX 15 AB6 THR A 297 ILE A 307 1 11 HELIX 16 AB7 ASN A 310 LEU A 321 1 12 SHEET 1 AA1 2 THR A 4 GLU A 5 0 SHEET 2 AA1 2 TYR A 10 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 PRO A 180 0 SHEET 2 AA2 2 CYS A 187 ILE A 189 -1 O GLY A 188 N ILE A 179 SSBOND 1 CYS A 2 CYS A 282 1555 1555 2.03 SSBOND 2 CYS A 110 CYS A 187 1555 1555 2.03 LINK C ACE A 0 N MET A 1 1555 1555 1.33 LINK SG CYS A 322 C1 PLM A 401 1555 1555 1.73 CRYST1 242.852 242.852 111.469 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 0.004118 0.002377 0.000000 0.00000 SCALE2 0.000000 0.004755 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008971 0.00000 HETATM 1 C ACE A 0 -231.307 71.145 39.598 1.00 78.00 C HETATM 2 O ACE A 0 -231.340 71.293 40.820 1.00 83.26 O HETATM 3 CH3 ACE A 0 -232.550 71.223 38.760 1.00 80.81 C ATOM 4 N MET A 1 -230.185 70.907 38.916 1.00126.55 N ANISOU 4 N MET A 1 16377 11281 20427 627 -939 1177 N ATOM 5 CA MET A 1 -228.848 70.787 39.502 1.00108.05 C ANISOU 5 CA MET A 1 14134 9074 17846 472 -809 1008 C ATOM 6 C MET A 1 -228.806 69.794 40.653 1.00 97.66 C ANISOU 6 C MET A 1 12761 8001 16345 501 -651 739 C ATOM 7 O MET A 1 -228.562 70.162 41.801 1.00 88.17 O ANISOU 7 O MET A 1 11565 6740 15195 499 -509 483 O ATOM 8 CB MET A 1 -228.339 72.147 39.981 1.00 98.79 C ANISOU 8 CB MET A 1 13028 7611 16899 427 -753 904 C ATOM 9 CG MET A 1 -227.969 73.098 38.856 1.00106.93 C ANISOU 9 CG MET A 1 14159 8429 18040 332 -900 1177 C ATOM 10 SD MET A 1 -227.055 72.291 37.523 1.00111.17 S ANISOU 10 SD MET A 1 14806 9245 18189 137 -1000 1446 S ATOM 11 CE MET A 1 -225.595 71.697 38.378 1.00112.89 C ANISOU 11 CE MET A 1 15060 9718 18113 -16 -822 1197 C ATOM 12 N CYS A 2 -229.053 68.529 40.333 1.00 92.06 N ANISOU 12 N CYS A 2 12009 7561 15411 514 -682 803 N ATOM 13 CA CYS A 2 -229.122 67.488 41.348 1.00 93.77 C ANISOU 13 CA CYS A 2 12170 8008 15451 543 -555 588 C ATOM 14 C CYS A 2 -227.756 66.885 41.621 1.00 84.56 C ANISOU 14 C CYS A 2 11086 7062 13980 385 -502 511 C ATOM 15 O CYS A 2 -227.374 66.700 42.783 1.00 80.67 O ANISOU 15 O CYS A 2 10599 6645 13408 358 -385 282 O ATOM 16 CB CYS A 2 -230.087 66.389 40.909 1.00106.17 C ANISOU 16 CB CYS A 2 13645 9745 16951 635 -617 691 C ATOM 17 SG CYS A 2 -231.800 66.884 40.927 1.00105.29 S ANISOU 17 SG CYS A 2 13374 9411 17221 841 -654 723 S ATOM 18 N GLY A 3 -227.013 66.584 40.554 1.00 79.96 N ANISOU 18 N GLY A 3 10567 6582 13233 273 -588 702 N ATOM 19 CA GLY A 3 -225.718 65.954 40.656 1.00 74.22 C ANISOU 19 CA GLY A 3 9887 6061 12252 130 -543 653 C ATOM 20 C GLY A 3 -224.676 66.710 39.849 1.00 67.60 C ANISOU 20 C GLY A 3 9139 5134 11410 -21 -581 785 C ATOM 21 O GLY A 3 -224.791 67.920 39.605 1.00 71.62 O ANISOU 21 O GLY A 3 9694 5391 12129 -30 -618 851 O ATOM 22 N THR A 4 -223.627 65.983 39.471 1.00 73.20 N ANISOU 22 N THR A 4 9870 6047 11897 -144 -560 817 N ATOM 23 CA THR A 4 -222.535 66.520 38.674 1.00 56.95 C ANISOU 23 CA THR A 4 7886 3952 9802 -310 -566 938 C ATOM 24 C THR A 4 -222.326 65.620 37.470 1.00 67.16 C ANISOU 24 C THR A 4 9203 5428 10884 -371 -590 1109 C ATOM 25 O THR A 4 -222.201 64.400 37.620 1.00 81.16 O ANISOU 25 O THR A 4 10923 7426 12487 -349 -552 1044 O ATOM 26 CB THR A 4 -221.236 66.607 39.485 1.00 56.72 C ANISOU 26 CB THR A 4 7843 3981 9728 -430 -484 771 C ATOM 27 OG1 THR A 4 -221.463 67.354 40.690 1.00 57.60 O ANISOU 27 OG1 THR A 4 7948 3937 9998 -384 -456 581 O ATOM 28 CG2 THR A 4 -220.129 67.283 38.670 1.00 57.99 C ANISOU 28 CG2 THR A 4 8064 4079 9890 -611 -475 895 C ATOM 29 N GLU A 5 -222.283 66.220 36.286 1.00 62.65 N ANISOU 29 N GLU A 5 8725 4756 10321 -458 -650 1326 N ATOM 30 CA GLU A 5 -222.185 65.483 35.035 1.00 57.26 C ANISOU 30 CA GLU A 5 8102 4228 9427 -535 -672 1496 C ATOM 31 C GLU A 5 -220.744 65.436 34.547 1.00 77.69 C ANISOU 31 C GLU A 5 10728 6913 11879 -728 -567 1511 C ATOM 32 O GLU A 5 -219.992 66.403 34.695 1.00 82.31 O ANISOU 32 O GLU A 5 11338 7365 12571 -832 -532 1507 O ATOM 33 CB GLU A 5 -223.066 66.112 33.955 1.00 71.48 C ANISOU 33 CB GLU A 5 9999 5874 11285 -534 -816 1747 C ATOM 34 CG GLU A 5 -224.526 65.698 33.998 1.00 92.18 C ANISOU 34 CG GLU A 5 12566 8485 13975 -360 -931 1783 C ATOM 35 CD GLU A 5 -225.358 66.395 32.935 1.00111.77 C ANISOU 35 CD GLU A 5 15133 10794 16542 -366 -1110 2052 C ATOM 36 OE1 GLU A 5 -225.045 67.557 32.594 1.00112.35 O ANISOU 36 OE1 GLU A 5 15287 10660 16740 -448 -1151 2174 O ATOM 37 OE2 GLU A 5 -226.320 65.774 32.434 1.00123.42 O ANISOU 37 OE2 GLU A 5 16594 12337 17964 -298 -1224 2153 O ATOM 38 N GLY A 6 -220.369 64.304 33.964 1.00 89.42 N ANISOU 38 N GLY A 6 12210 8623 13144 -778 -506 1521 N ATOM 39 CA GLY A 6 -219.098 64.169 33.301 1.00 93.06 C ANISOU 39 CA GLY A 6 12699 9183 13475 -961 -387 1549 C ATOM 40 C GLY A 6 -219.277 63.413 32.005 1.00103.56 C ANISOU 40 C GLY A 6 14123 10651 14575 -1031 -377 1687 C ATOM 41 O GLY A 6 -220.382 62.982 31.658 1.00110.03 O ANISOU 41 O GLY A 6 14982 11490 15335 -939 -485 1763 O ATOM 42 N PRO A 7 -218.189 63.242 31.257 1.00103.74 N ANISOU 42 N PRO A 7 14182 10770 14463 -1207 -240 1715 N ATOM 43 CA PRO A 7 -218.288 62.488 29.999 1.00116.93 C ANISOU 43 CA PRO A 7 15963 12582 15883 -1299 -201 1820 C ATOM 44 C PRO A 7 -218.703 61.036 30.186 1.00125.14 C ANISOU 44 C PRO A 7 16933 13806 16809 -1179 -188 1699 C ATOM 45 O PRO A 7 -219.313 60.459 29.277 1.00140.64 O ANISOU 45 O PRO A 7 19003 15846 18588 -1204 -229 1793 O ATOM 46 CB PRO A 7 -216.874 62.609 29.410 1.00111.99 C ANISOU 46 CB PRO A 7 15352 12022 15176 -1508 -6 1815 C ATOM 47 CG PRO A 7 -215.997 62.990 30.565 1.00106.26 C ANISOU 47 CG PRO A 7 14463 11250 14662 -1485 55 1656 C ATOM 48 CD PRO A 7 -216.850 63.813 31.468 1.00 98.78 C ANISOU 48 CD PRO A 7 13504 10115 13912 -1348 -112 1657 C ATOM 49 N ASN A 8 -218.416 60.428 31.343 1.00109.27 N ANISOU 49 N ASN A 8 14756 11863 14900 -1059 -145 1501 N ATOM 50 CA ASN A 8 -218.693 59.009 31.542 1.00 93.07 C ANISOU 50 CA ASN A 8 12634 9976 12751 -958 -122 1388 C ATOM 51 C ASN A 8 -219.343 58.709 32.889 1.00 80.89 C ANISOU 51 C ASN A 8 10971 8420 11344 -770 -210 1264 C ATOM 52 O ASN A 8 -219.258 57.570 33.361 1.00 84.71 O ANISOU 52 O ASN A 8 11363 9033 11789 -694 -173 1141 O ATOM 53 CB ASN A 8 -217.409 58.186 31.405 1.00 98.69 C ANISOU 53 CB ASN A 8 13261 10836 13400 -1040 66 1267 C ATOM 54 CG ASN A 8 -216.796 58.286 30.026 1.00100.61 C ANISOU 54 CG ASN A 8 13627 11123 13476 -1235 197 1363 C ATOM 55 OD1 ASN A 8 -217.504 58.335 29.022 1.00 95.07 O ANISOU 55 OD1 ASN A 8 13094 10420 12610 -1295 139 1505 O ATOM 56 ND2 ASN A 8 -215.469 58.316 29.969 1.00109.96 N ANISOU 56 ND2 ASN A 8 14728 12351 14700 -1348 374 1288 N ATOM 57 N PHE A 9 -219.993 59.683 33.521 1.00 66.59 N ANISOU 57 N PHE A 9 9162 6449 9692 -697 -316 1290 N ATOM 58 CA PHE A 9 -220.529 59.445 34.855 1.00 73.03 C ANISOU 58 CA PHE A 9 9872 7255 10622 -542 -364 1151 C ATOM 59 C PHE A 9 -221.597 60.476 35.190 1.00 77.36 C ANISOU 59 C PHE A 9 10450 7614 11330 -455 -477 1207 C ATOM 60 O PHE A 9 -221.773 61.479 34.494 1.00 75.78 O ANISOU 60 O PHE A 9 10341 7268 11186 -516 -530 1355 O ATOM 61 CB PHE A 9 -219.416 59.469 35.910 1.00 76.19 C ANISOU 61 CB PHE A 9 10165 7683 11099 -566 -287 989 C ATOM 62 CG PHE A 9 -218.634 60.756 35.946 1.00 80.51 C ANISOU 62 CG PHE A 9 10737 8090 11762 -681 -262 1011 C ATOM 63 CD1 PHE A 9 -219.053 61.819 36.731 1.00 82.67 C ANISOU 63 CD1 PHE A 9 11022 8188 12199 -635 -325 976 C ATOM 64 CD2 PHE A 9 -217.469 60.895 35.208 1.00 79.64 C ANISOU 64 CD2 PHE A 9 10635 8016 11608 -840 -161 1055 C ATOM 65 CE1 PHE A 9 -218.332 62.999 36.770 1.00 84.83 C ANISOU 65 CE1 PHE A 9 11325 8318 12590 -749 -306 991 C ATOM 66 CE2 PHE A 9 -216.744 62.072 35.244 1.00 74.29 C ANISOU 66 CE2 PHE A 9 9977 7206 11045 -959 -138 1080 C ATOM 67 CZ PHE A 9 -217.175 63.125 36.027 1.00 79.29 C ANISOU 67 CZ PHE A 9 10630 7657 11840 -914 -220 1050 C ATOM 68 N TYR A 10 -222.311 60.200 36.282 1.00 72.46 N ANISOU 68 N TYR A 10 9748 6991 10791 -315 -506 1087 N ATOM 69 CA TYR A 10 -223.245 61.143 36.898 1.00 60.80 C ANISOU 69 CA TYR A 10 8263 5330 9509 -215 -572 1076 C ATOM 70 C TYR A 10 -223.157 60.925 38.406 1.00 64.00 C ANISOU 70 C TYR A 10 8583 5767 9969 -145 -517 863 C ATOM 71 O TYR A 10 -223.715 59.957 38.933 1.00 74.68 O ANISOU 71 O TYR A 10 9877 7237 11261 -56 -514 788 O ATOM 72 CB TYR A 10 -224.671 60.952 36.389 1.00 63.56 C ANISOU 72 CB TYR A 10 8616 5644 9888 -111 -679 1192 C ATOM 73 CG TYR A 10 -225.691 61.775 37.148 1.00 65.98 C ANISOU 73 CG TYR A 10 8872 5766 10432 18 -721 1148 C ATOM 74 CD1 TYR A 10 -225.874 63.121 36.864 1.00 64.68 C ANISOU 74 CD1 TYR A 10 8753 5366 10457 9 -777 1243 C ATOM 75 CD2 TYR A 10 -226.469 61.205 38.151 1.00 60.14 C ANISOU 75 CD2 TYR A 10 8037 5078 9737 145 -692 1007 C ATOM 76 CE1 TYR A 10 -226.799 63.877 37.556 1.00 61.39 C ANISOU 76 CE1 TYR A 10 8276 4760 10290 137 -797 1185 C ATOM 77 CE2 TYR A 10 -227.396 61.954 38.849 1.00 68.89 C ANISOU 77 CE2 TYR A 10 9088 6014 11072 261 -695 944 C ATOM 78 CZ TYR A 10 -227.558 63.290 38.547 1.00 68.72 C ANISOU 78 CZ TYR A 10 9102 5751 11259 263 -744 1026 C ATOM 79 OH TYR A 10 -228.483 64.041 39.237 1.00 66.13 O ANISOU 79 OH TYR A 10 8704 5232 11190 388 -731 946 O ATOM 80 N VAL A 11 -222.449 61.817 39.091 1.00 60.97 N ANISOU 80 N VAL A 11 8203 5278 9684 -201 -479 771 N ATOM 81 CA VAL A 11 -222.298 61.739 40.542 1.00 63.82 C ANISOU 81 CA VAL A 11 8513 5660 10074 -167 -437 567 C ATOM 82 C VAL A 11 -223.517 62.381 41.194 1.00 73.87 C ANISOU 82 C VAL A 11 9783 6778 11506 -46 -446 503 C ATOM 83 O VAL A 11 -223.732 63.591 41.042 1.00 75.63 O ANISOU 83 O VAL A 11 10046 6788 11904 -47 -462 536 O ATOM 84 CB VAL A 11 -221.002 62.419 41.009 1.00 61.80 C ANISOU 84 CB VAL A 11 8267 5359 9854 -298 -402 485 C ATOM 85 CG1 VAL A 11 -220.947 62.470 42.530 1.00 52.18 C ANISOU 85 CG1 VAL A 11 7027 4145 8653 -279 -381 277 C ATOM 86 CG2 VAL A 11 -219.793 61.696 40.449 1.00 58.33 C ANISOU 86 CG2 VAL A 11 7793 5081 9289 -406 -374 529 C ATOM 87 N PRO A 12 -224.333 61.626 41.924 1.00 70.75 N ANISOU 87 N PRO A 12 9336 6472 11076 57 -426 409 N ATOM 88 CA PRO A 12 -225.554 62.206 42.500 1.00 64.78 C ANISOU 88 CA PRO A 12 8555 5568 10491 176 -405 339 C ATOM 89 C PRO A 12 -225.279 63.144 43.666 1.00 57.28 C ANISOU 89 C PRO A 12 7636 4486 9643 149 -332 146 C ATOM 90 O PRO A 12 -225.747 62.906 44.784 1.00 56.05 O ANISOU 90 O PRO A 12 7460 4364 9470 195 -259 -24 O ATOM 91 CB PRO A 12 -226.348 60.972 42.955 1.00 53.64 C ANISOU 91 CB PRO A 12 7078 4325 8977 262 -384 290 C ATOM 92 CG PRO A 12 -225.678 59.793 42.294 1.00 62.53 C ANISOU 92 CG PRO A 12 8203 5656 9899 202 -423 382 C ATOM 93 CD PRO A 12 -224.245 60.179 42.165 1.00 67.27 C ANISOU 93 CD PRO A 12 8849 6259 10452 71 -416 377 C ATOM 94 N PHE A 13 -224.534 64.219 43.419 1.00 53.33 N ANISOU 94 N PHE A 13 7194 3832 9239 60 -345 166 N ATOM 95 CA PHE A 13 -224.203 65.174 44.469 1.00 63.70 C ANISOU 95 CA PHE A 13 8552 5003 10648 14 -283 -24 C ATOM 96 C PHE A 13 -224.035 66.552 43.847 1.00 68.77 C ANISOU 96 C PHE A 13 9245 5384 11502 -22 -314 60 C ATOM 97 O PHE A 13 -223.328 66.700 42.846 1.00 71.49 O ANISOU 97 O PHE A 13 9617 5729 11818 -112 -375 230 O ATOM 98 CB PHE A 13 -222.929 64.754 45.210 1.00 54.08 C ANISOU 98 CB PHE A 13 7357 3941 9251 -125 -274 -139 C ATOM 99 CG PHE A 13 -222.659 65.548 46.455 1.00 55.56 C ANISOU 99 CG PHE A 13 7604 4020 9486 -188 -218 -363 C ATOM 100 CD1 PHE A 13 -223.376 65.309 47.615 1.00 55.80 C ANISOU 100 CD1 PHE A 13 7647 4082 9474 -132 -139 -552 C ATOM 101 CD2 PHE A 13 -221.679 66.526 46.469 1.00 63.71 C ANISOU 101 CD2 PHE A 13 8691 4923 10595 -319 -238 -392 C ATOM 102 CE1 PHE A 13 -223.127 66.039 48.764 1.00 63.98 C ANISOU 102 CE1 PHE A 13 8764 5023 10525 -210 -79 -774 C ATOM 103 CE2 PHE A 13 -221.425 67.258 47.614 1.00 67.42 C ANISOU 103 CE2 PHE A 13 9231 5290 11097 -394 -194 -611 C ATOM 104 CZ PHE A 13 -222.150 67.014 48.762 1.00 67.17 C ANISOU 104 CZ PHE A 13 9227 5292 11004 -341 -113 -807 C ATOM 105 N SER A 14 -224.691 67.549 44.439 1.00 66.46 N ANISOU 105 N SER A 14 8967 4860 11425 43 -262 -62 N ATOM 106 CA SER A 14 -224.610 68.907 43.921 1.00 73.78 C ANISOU 106 CA SER A 14 9944 5500 12590 19 -296 14 C ATOM 107 C SER A 14 -223.177 69.416 43.986 1.00 79.79 C ANISOU 107 C SER A 14 10779 6246 13292 -170 -305 -12 C ATOM 108 O SER A 14 -222.392 69.034 44.858 1.00 81.30 O ANISOU 108 O SER A 14 10982 6580 13326 -264 -267 -173 O ATOM 109 CB SER A 14 -225.536 69.840 44.703 1.00 89.41 C ANISOU 109 CB SER A 14 11917 7224 14832 128 -214 -157 C ATOM 110 OG SER A 14 -225.403 71.182 44.262 1.00 84.90 O ANISOU 110 OG SER A 14 11396 6347 14513 102 -251 -90 O ATOM 111 N ASN A 15 -222.838 70.295 43.047 1.00 85.38 N ANISOU 111 N ASN A 15 11534 6775 14133 -234 -367 161 N ATOM 112 CA ASN A 15 -221.463 70.731 42.865 1.00 84.95 C ANISOU 112 CA ASN A 15 11533 6715 14029 -427 -380 184 C ATOM 113 C ASN A 15 -221.237 72.180 43.284 1.00 89.27 C ANISOU 113 C ASN A 15 12152 6955 14810 -490 -362 87 C ATOM 114 O ASN A 15 -220.208 72.767 42.932 1.00 66.48 O ANISOU 114 O ASN A 15 9313 4004 11944 -654 -385 149 O ATOM 115 CB ASN A 15 -221.050 70.525 41.410 1.00 92.91 C ANISOU 115 CB ASN A 15 12554 7787 14962 -501 -448 464 C ATOM 116 CG ASN A 15 -219.562 70.494 41.245 1.00 95.08 C ANISOU 116 CG ASN A 15 12840 8166 15121 -700 -430 475 C ATOM 117 OD1 ASN A 15 -218.840 70.304 42.223 1.00 62.14 O ANISOU 117 OD1 ASN A 15 8641 4085 10884 -770 -393 286 O ATOM 118 ND2 ASN A 15 -219.085 70.695 40.021 1.00 88.55 N ANISOU 118 ND2 ASN A 15 12050 7325 14269 -805 -459 699 N ATOM 119 N LYS A 16 -222.168 72.771 44.036 1.00 94.44 N ANISOU 119 N LYS A 16 12814 7414 15657 -369 -309 -75 N ATOM 120 CA LYS A 16 -222.002 74.158 44.452 1.00 82.34 C ANISOU 120 CA LYS A 16 11356 5563 14368 -422 -282 -189 C ATOM 121 C LYS A 16 -220.803 74.344 45.373 1.00 82.13 C ANISOU 121 C LYS A 16 11384 5593 14228 -609 -247 -394 C ATOM 122 O LYS A 16 -220.286 75.461 45.481 1.00 96.50 O ANISOU 122 O LYS A 16 13277 7176 16212 -719 -250 -443 O ATOM 123 CB LYS A 16 -223.278 74.652 45.134 1.00 81.89 C ANISOU 123 CB LYS A 16 11279 5292 14543 -244 -202 -356 C ATOM 124 CG LYS A 16 -223.704 73.805 46.312 1.00 83.59 C ANISOU 124 CG LYS A 16 11461 5708 14592 -181 -93 -606 C ATOM 125 CD LYS A 16 -225.158 74.041 46.666 1.00 92.07 C ANISOU 125 CD LYS A 16 12472 6616 15893 24 -3 -707 C ATOM 126 CE LYS A 16 -225.588 73.104 47.779 1.00 93.74 C ANISOU 126 CE LYS A 16 12657 7056 15905 68 119 -934 C ATOM 127 NZ LYS A 16 -227.043 72.796 47.717 1.00 88.87 N ANISOU 127 NZ LYS A 16 11921 6403 15442 278 179 -923 N ATOM 128 N THR A 17 -220.345 73.280 46.028 1.00 80.46 N ANISOU 128 N THR A 17 11140 5682 13749 -655 -230 -504 N ATOM 129 CA THR A 17 -219.184 73.353 46.904 1.00 78.07 C ANISOU 129 CA THR A 17 10877 5459 13326 -841 -232 -679 C ATOM 130 C THR A 17 -217.871 73.068 46.184 1.00 70.34 C ANISOU 130 C THR A 17 9858 4624 12243 -1006 -307 -512 C ATOM 131 O THR A 17 -216.804 73.302 46.762 1.00 68.31 O ANISOU 131 O THR A 17 9618 4395 11942 -1180 -332 -623 O ATOM 132 CB THR A 17 -219.342 72.376 48.074 1.00 83.69 C ANISOU 132 CB THR A 17 11578 6409 13812 -817 -192 -881 C ATOM 133 OG1 THR A 17 -219.641 71.067 47.572 1.00 91.58 O ANISOU 133 OG1 THR A 17 12485 7669 14641 -721 -216 -733 O ATOM 134 CG2 THR A 17 -220.464 72.827 48.995 1.00 77.81 C ANISOU 134 CG2 THR A 17 10888 5505 13171 -703 -79 -1108 C ATOM 135 N GLY A 18 -217.922 72.573 44.949 1.00 78.87 N ANISOU 135 N GLY A 18 10886 5796 13286 -967 -338 -257 N ATOM 136 CA GLY A 18 -216.713 72.277 44.206 1.00 78.76 C ANISOU 136 CA GLY A 18 10825 5919 13180 -1122 -372 -107 C ATOM 137 C GLY A 18 -215.921 71.098 44.725 1.00 78.40 C ANISOU 137 C GLY A 18 10692 6181 12917 -1179 -385 -183 C ATOM 138 O GLY A 18 -214.698 71.062 44.559 1.00 80.61 O ANISOU 138 O GLY A 18 10918 6540 13168 -1341 -406 -151 O ATOM 139 N VAL A 19 -216.586 70.123 45.349 1.00 76.02 N ANISOU 139 N VAL A 19 10361 6047 12477 -1051 -376 -274 N ATOM 140 CA VAL A 19 -215.893 68.979 45.937 1.00 65.74 C ANISOU 140 CA VAL A 19 8979 5018 10981 -1096 -407 -341 C ATOM 141 C VAL A 19 -216.037 67.708 45.112 1.00 68.16 C ANISOU 141 C VAL A 19 9198 5544 11154 -1009 -403 -182 C ATOM 142 O VAL A 19 -215.341 66.719 45.397 1.00 57.86 O ANISOU 142 O VAL A 19 7809 4455 9721 -1047 -433 -202 O ATOM 143 CB VAL A 19 -216.384 68.710 47.376 1.00 61.05 C ANISOU 143 CB VAL A 19 8429 4473 10294 -1053 -406 -570 C ATOM 144 CG1 VAL A 19 -216.232 69.956 48.231 1.00 63.42 C ANISOU 144 CG1 VAL A 19 8833 4554 10710 -1153 -397 -759 C ATOM 145 CG2 VAL A 19 -217.827 68.229 47.364 1.00 61.02 C ANISOU 145 CG2 VAL A 19 8438 4483 10263 -853 -348 -567 C ATOM 146 N VAL A 20 -216.910 67.698 44.105 1.00 72.06 N ANISOU 146 N VAL A 20 9712 5982 11683 -897 -378 -26 N ATOM 147 CA VAL A 20 -217.167 66.482 43.347 1.00 71.97 C ANISOU 147 CA VAL A 20 9640 6171 11534 -816 -373 104 C ATOM 148 C VAL A 20 -215.962 66.144 42.480 1.00 63.28 C ANISOU 148 C VAL A 20 8475 5183 10385 -946 -359 223 C ATOM 149 O VAL A 20 -215.377 67.013 41.822 1.00 70.24 O ANISOU 149 O VAL A 20 9386 5941 11362 -1066 -342 313 O ATOM 150 CB VAL A 20 -218.438 66.647 42.497 1.00 69.37 C ANISOU 150 CB VAL A 20 9358 5740 11259 -682 -372 242 C ATOM 151 CG1 VAL A 20 -218.730 65.376 41.722 1.00 54.75 C ANISOU 151 CG1 VAL A 20 7458 4094 9251 -614 -373 363 C ATOM 152 CG2 VAL A 20 -219.612 67.031 43.375 1.00 67.16 C ANISOU 152 CG2 VAL A 20 9111 5333 11073 -551 -362 109 C ATOM 153 N ARG A 21 -215.573 64.876 42.490 1.00 58.46 N ANISOU 153 N ARG A 21 7772 4800 9639 -928 -355 221 N ATOM 154 CA ARG A 21 -214.511 64.381 41.633 1.00 61.79 C ANISOU 154 CA ARG A 21 8113 5344 10023 -1028 -311 318 C ATOM 155 C ARG A 21 -215.060 63.262 40.762 1.00 53.76 C ANISOU 155 C ARG A 21 7082 4470 8876 -930 -277 422 C ATOM 156 O ARG A 21 -216.094 62.664 41.070 1.00 60.86 O ANISOU 156 O ARG A 21 8002 5414 9707 -789 -307 397 O ATOM 157 CB ARG A 21 -213.321 63.876 42.456 1.00 64.10 C ANISOU 157 CB ARG A 21 8280 5764 10313 -1114 -341 205 C ATOM 158 CG ARG A 21 -212.733 64.914 43.391 1.00 62.01 C ANISOU 158 CG ARG A 21 8031 5372 10157 -1233 -395 87 C ATOM 159 CD ARG A 21 -212.120 66.063 42.609 1.00 68.12 C ANISOU 159 CD ARG A 21 8833 5988 11060 -1377 -348 175 C ATOM 160 NE ARG A 21 -211.499 67.053 43.483 1.00 76.11 N ANISOU 160 NE ARG A 21 9859 6871 12187 -1508 -405 56 N ATOM 161 CZ ARG A 21 -212.103 68.156 43.912 1.00 71.97 C ANISOU 161 CZ ARG A 21 9463 6133 11748 -1506 -424 -11 C ATOM 162 NH1 ARG A 21 -211.460 69.001 44.705 1.00 80.73 N ANISOU 162 NH1 ARG A 21 10590 7131 12953 -1643 -474 -134 N ATOM 163 NH2 ARG A 21 -213.350 68.417 43.545 1.00 60.84 N ANISOU 163 NH2 ARG A 21 8159 4612 10346 -1369 -397 42 N ATOM 164 N SER A 22 -214.363 62.993 39.665 1.00 61.13 N ANISOU 164 N SER A 22 7984 5472 9773 -1017 -203 532 N ATOM 165 CA SER A 22 -214.717 61.871 38.811 1.00 52.61 C ANISOU 165 CA SER A 22 6896 4537 8557 -951 -158 609 C ATOM 166 C SER A 22 -214.680 60.574 39.612 1.00 56.00 C ANISOU 166 C SER A 22 7222 5133 8924 -856 -185 498 C ATOM 167 O SER A 22 -213.678 60.296 40.288 1.00 51.24 O ANISOU 167 O SER A 22 6502 4595 8370 -910 -194 409 O ATOM 168 CB SER A 22 -213.752 61.783 37.630 1.00 53.58 C ANISOU 168 CB SER A 22 6994 4715 8648 -1090 -43 704 C ATOM 169 OG SER A 22 -214.002 60.627 36.854 1.00 52.64 O ANISOU 169 OG SER A 22 6871 4742 8389 -1039 15 746 O ATOM 170 N PRO A 23 -215.737 59.757 39.566 1.00 62.07 N ANISOU 170 N PRO A 23 8022 5967 9594 -721 -212 511 N ATOM 171 CA PRO A 23 -215.704 58.468 40.269 1.00 64.14 C ANISOU 171 CA PRO A 23 8194 6381 9796 -640 -238 424 C ATOM 172 C PRO A 23 -214.665 57.501 39.725 1.00 60.41 C ANISOU 172 C PRO A 23 7609 6040 9304 -687 -165 430 C ATOM 173 O PRO A 23 -214.510 56.413 40.286 1.00 49.56 O ANISOU 173 O PRO A 23 6147 4775 7908 -624 -195 369 O ATOM 174 CB PRO A 23 -217.125 57.937 40.071 1.00 55.42 C ANISOU 174 CB PRO A 23 7161 5295 8603 -506 -267 464 C ATOM 175 CG PRO A 23 -217.574 58.565 38.788 1.00 52.37 C ANISOU 175 CG PRO A 23 6874 4824 8200 -540 -237 605 C ATOM 176 CD PRO A 23 -216.999 59.946 38.829 1.00 62.50 C ANISOU 176 CD PRO A 23 8190 5957 9600 -647 -231 619 C ATOM 177 N PHE A 24 -213.922 57.880 38.686 1.00 58.17 N ANISOU 177 N PHE A 24 7320 5740 9041 -802 -64 499 N ATOM 178 CA PHE A 24 -212.820 57.076 38.186 1.00 57.67 C ANISOU 178 CA PHE A 24 7129 5786 8997 -859 40 481 C ATOM 179 C PHE A 24 -211.470 57.568 38.671 1.00 67.50 C ANISOU 179 C PHE A 24 8236 7012 10398 -974 50 427 C ATOM 180 O PHE A 24 -210.457 56.981 38.295 1.00 84.11 O ANISOU 180 O PHE A 24 10199 9193 12566 -1025 146 405 O ATOM 181 CB PHE A 24 -212.812 57.042 36.648 1.00 51.78 C ANISOU 181 CB PHE A 24 6461 5057 8155 -931 180 579 C ATOM 182 CG PHE A 24 -214.108 56.586 36.038 1.00 55.30 C ANISOU 182 CG PHE A 24 7046 5522 8444 -843 153 647 C ATOM 183 CD1 PHE A 24 -214.571 55.294 36.238 1.00 69.55 C ANISOU 183 CD1 PHE A 24 8814 7428 10184 -725 131 595 C ATOM 184 CD2 PHE A 24 -214.849 57.441 35.241 1.00 62.05 C ANISOU 184 CD2 PHE A 24 8065 6284 9227 -886 136 774 C ATOM 185 CE1 PHE A 24 -215.765 54.876 35.675 1.00 66.55 C ANISOU 185 CE1 PHE A 24 8553 7065 9668 -657 95 657 C ATOM 186 CE2 PHE A 24 -216.041 57.029 34.675 1.00 66.69 C ANISOU 186 CE2 PHE A 24 8766 6888 9684 -813 85 846 C ATOM 187 CZ PHE A 24 -216.499 55.747 34.891 1.00 61.47 C ANISOU 187 CZ PHE A 24 8062 6337 8957 -702 67 783 C ATOM 188 N GLU A 25 -211.429 58.618 39.499 1.00 62.61 N ANISOU 188 N GLU A 25 7646 6287 9855 -1020 -43 396 N ATOM 189 CA GLU A 25 -210.166 59.277 39.824 1.00 59.59 C ANISOU 189 CA GLU A 25 7149 5867 9624 -1161 -39 359 C ATOM 190 C GLU A 25 -209.947 59.487 41.322 1.00 53.55 C ANISOU 190 C GLU A 25 6336 5084 8928 -1160 -198 253 C ATOM 191 O GLU A 25 -208.814 59.374 41.805 1.00 58.81 O ANISOU 191 O GLU A 25 6842 5788 9715 -1242 -237 205 O ATOM 192 CB GLU A 25 -210.070 60.624 39.092 1.00 76.17 C ANISOU 192 CB GLU A 25 9352 7828 11760 -1292 28 441 C ATOM 193 CG GLU A 25 -209.904 60.506 37.587 1.00 94.04 C ANISOU 193 CG GLU A 25 11653 10122 13956 -1361 196 551 C ATOM 194 CD GLU A 25 -209.519 61.823 36.941 1.00112.11 C ANISOU 194 CD GLU A 25 14020 12277 16300 -1529 259 642 C ATOM 195 OE1 GLU A 25 -209.997 62.882 37.403 1.00115.13 O ANISOU 195 OE1 GLU A 25 14508 12506 16732 -1539 161 655 O ATOM 196 OE2 GLU A 25 -208.725 61.797 35.976 1.00116.67 O ANISOU 196 OE2 GLU A 25 14554 12897 16880 -1658 417 696 O ATOM 197 N ALA A 26 -211.007 59.789 42.067 1.00 52.58 N ANISOU 197 N ALA A 26 6345 4902 8730 -1080 -290 214 N ATOM 198 CA ALA A 26 -210.882 60.100 43.485 1.00 52.95 C ANISOU 198 CA ALA A 26 6392 4924 8803 -1104 -428 102 C ATOM 199 C ALA A 26 -212.057 59.517 44.256 1.00 63.51 C ANISOU 199 C ALA A 26 7820 6301 10008 -965 -494 52 C ATOM 200 O ALA A 26 -213.154 59.375 43.705 1.00 58.48 O ANISOU 200 O ALA A 26 7277 5647 9295 -859 -439 103 O ATOM 201 CB ALA A 26 -210.809 61.614 43.729 1.00 77.01 C ANISOU 201 CB ALA A 26 9533 7797 11930 -1215 -443 69 C ATOM 202 N PRO A 27 -211.861 59.185 45.535 1.00 55.33 N ANISOU 202 N PRO A 27 6761 5320 8942 -975 -617 -42 N ATOM 203 CA PRO A 27 -212.952 58.597 46.325 1.00 62.55 C ANISOU 203 CA PRO A 27 7765 6282 9719 -863 -664 -91 C ATOM 204 C PRO A 27 -214.139 59.541 46.462 1.00 70.78 C ANISOU 204 C PRO A 27 8970 7193 10732 -819 -616 -136 C ATOM 205 O PRO A 27 -213.997 60.766 46.437 1.00 80.05 O ANISOU 205 O PRO A 27 10203 8222 11991 -897 -598 -168 O ATOM 206 CB PRO A 27 -212.299 58.319 47.687 1.00 59.56 C ANISOU 206 CB PRO A 27 7348 5969 9311 -939 -814 -178 C ATOM 207 CG PRO A 27 -211.101 59.203 47.727 1.00 56.56 C ANISOU 207 CG PRO A 27 6899 5525 9067 -1097 -853 -201 C ATOM 208 CD PRO A 27 -210.623 59.311 46.317 1.00 58.83 C ANISOU 208 CD PRO A 27 7095 5789 9470 -1105 -727 -98 C ATOM 209 N GLN A 28 -215.320 58.951 46.612 1.00 66.89 N ANISOU 209 N GLN A 28 8539 6739 10139 -691 -595 -137 N ATOM 210 CA GLN A 28 -216.573 59.701 46.701 1.00 58.42 C ANISOU 210 CA GLN A 28 7588 5542 9069 -620 -539 -176 C ATOM 211 C GLN A 28 -217.060 59.799 48.142 1.00 63.71 C ANISOU 211 C GLN A 28 8338 6213 9655 -626 -572 -328 C ATOM 212 O GLN A 28 -218.213 59.492 48.446 1.00 57.25 O ANISOU 212 O GLN A 28 7571 5406 8775 -525 -528 -360 O ATOM 213 CB GLN A 28 -217.624 59.052 45.812 1.00 48.13 C ANISOU 213 CB GLN A 28 6286 4272 7729 -484 -483 -73 C ATOM 214 CG GLN A 28 -217.191 58.911 44.364 1.00 56.47 C ANISOU 214 CG GLN A 28 7293 5338 8824 -497 -441 69 C ATOM 215 CD GLN A 28 -217.125 60.246 43.653 1.00 66.40 C ANISOU 215 CD GLN A 28 8610 6424 10195 -556 -404 123 C ATOM 216 OE1 GLN A 28 -218.127 60.954 43.549 1.00 71.13 O ANISOU 216 OE1 GLN A 28 9288 6892 10846 -494 -391 134 O ATOM 217 NE2 GLN A 28 -215.943 60.601 43.163 1.00 69.40 N ANISOU 217 NE2 GLN A 28 8942 6794 10634 -679 -388 162 N ATOM 218 N TYR A 29 -216.190 60.241 49.051 1.00 60.92 N ANISOU 218 N TYR A 29 8000 5850 9295 -759 -646 -429 N ATOM 219 CA TYR A 29 -216.535 60.270 50.470 1.00 64.70 C ANISOU 219 CA TYR A 29 8578 6352 9652 -800 -680 -581 C ATOM 220 C TYR A 29 -217.495 61.399 50.832 1.00 64.59 C ANISOU 220 C TYR A 29 8692 6167 9683 -776 -579 -709 C ATOM 221 O TYR A 29 -217.784 61.578 52.020 1.00 64.78 O ANISOU 221 O TYR A 29 8820 6193 9602 -830 -576 -865 O ATOM 222 CB TYR A 29 -215.266 60.359 51.323 1.00 81.72 C ANISOU 222 CB TYR A 29 10717 8558 11775 -969 -818 -643 C ATOM 223 CG TYR A 29 -214.455 59.080 51.319 1.00 86.75 C ANISOU 223 CG TYR A 29 11224 9370 12369 -978 -934 -541 C ATOM 224 CD1 TYR A 29 -215.072 57.845 51.159 1.00 87.56 C ANISOU 224 CD1 TYR A 29 11294 9590 12385 -855 -920 -464 C ATOM 225 CD2 TYR A 29 -213.076 59.107 51.471 1.00 88.63 C ANISOU 225 CD2 TYR A 29 11357 9640 12677 -1107 -1060 -520 C ATOM 226 CE1 TYR A 29 -214.340 56.676 51.154 1.00 86.99 C ANISOU 226 CE1 TYR A 29 11099 9650 12303 -854 -1025 -374 C ATOM 227 CE2 TYR A 29 -212.335 57.941 51.466 1.00 85.54 C ANISOU 227 CE2 TYR A 29 10823 9387 12290 -1100 -1168 -426 C ATOM 228 CZ TYR A 29 -212.972 56.729 51.308 1.00 88.77 C ANISOU 228 CZ TYR A 29 11213 9898 12619 -970 -1148 -355 C ATOM 229 OH TYR A 29 -212.243 55.563 51.302 1.00 97.39 O ANISOU 229 OH TYR A 29 12159 11101 13744 -955 -1255 -263 O ATOM 230 N TYR A 30 -217.988 62.158 49.853 1.00 75.09 N ANISOU 230 N TYR A 30 10020 7342 11167 -705 -496 -648 N ATOM 231 CA TYR A 30 -219.068 63.108 50.088 1.00 70.48 C ANISOU 231 CA TYR A 30 9528 6580 10672 -641 -393 -751 C ATOM 232 C TYR A 30 -220.439 62.511 49.808 1.00 70.08 C ANISOU 232 C TYR A 30 9458 6559 10610 -471 -316 -706 C ATOM 233 O TYR A 30 -221.441 63.034 50.308 1.00 66.70 O ANISOU 233 O TYR A 30 9087 6020 10236 -407 -221 -824 O ATOM 234 CB TYR A 30 -218.871 64.369 49.238 1.00 55.34 C ANISOU 234 CB TYR A 30 7620 4444 8961 -662 -369 -699 C ATOM 235 CG TYR A 30 -218.462 64.081 47.813 1.00 60.75 C ANISOU 235 CG TYR A 30 8219 5162 9703 -642 -396 -481 C ATOM 236 CD1 TYR A 30 -219.413 63.833 46.832 1.00 70.97 C ANISOU 236 CD1 TYR A 30 9490 6435 11042 -505 -358 -345 C ATOM 237 CD2 TYR A 30 -217.121 64.054 47.447 1.00 54.43 C ANISOU 237 CD2 TYR A 30 7359 4416 8907 -771 -455 -417 C ATOM 238 CE1 TYR A 30 -219.042 63.565 45.528 1.00 76.45 C ANISOU 238 CE1 TYR A 30 10132 7165 11749 -510 -375 -156 C ATOM 239 CE2 TYR A 30 -216.741 63.787 46.146 1.00 53.74 C ANISOU 239 CE2 TYR A 30 7202 4363 8854 -769 -446 -236 C ATOM 240 CZ TYR A 30 -217.705 63.544 45.191 1.00 59.74 C ANISOU 240 CZ TYR A 30 7969 5106 9623 -644 -405 -109 C ATOM 241 OH TYR A 30 -217.332 63.279 43.894 1.00 57.97 O ANISOU 241 OH TYR A 30 7705 4923 9399 -663 -390 62 O ATOM 242 N LEU A 31 -220.508 61.436 49.018 1.00 71.51 N ANISOU 242 N LEU A 31 9554 6880 10738 -400 -349 -548 N ATOM 243 CA LEU A 31 -221.759 60.698 48.883 1.00 60.32 C ANISOU 243 CA LEU A 31 8112 5520 9287 -260 -296 -512 C ATOM 244 C LEU A 31 -222.092 59.955 50.168 1.00 69.09 C ANISOU 244 C LEU A 31 9262 6761 10227 -275 -278 -637 C ATOM 245 O LEU A 31 -223.264 59.846 50.546 1.00 77.41 O ANISOU 245 O LEU A 31 10331 7800 11281 -190 -187 -700 O ATOM 246 CB LEU A 31 -221.674 59.710 47.720 1.00 48.61 C ANISOU 246 CB LEU A 31 6543 4152 7775 -203 -340 -323 C ATOM 247 CG LEU A 31 -221.260 60.210 46.338 1.00 54.38 C ANISOU 247 CG LEU A 31 7248 4799 8615 -214 -358 -172 C ATOM 248 CD1 LEU A 31 -221.206 59.046 45.360 1.00 47.10 C ANISOU 248 CD1 LEU A 31 6262 4020 7615 -173 -384 -26 C ATOM 249 CD2 LEU A 31 -222.222 61.274 45.849 1.00 60.64 C ANISOU 249 CD2 LEU A 31 8075 5390 9576 -140 -318 -143 C ATOM 250 N ALA A 32 -221.074 59.434 50.848 1.00 66.93 N ANISOU 250 N ALA A 32 9002 6615 9814 -391 -368 -667 N ATOM 251 CA ALA A 32 -221.273 58.633 52.045 1.00 60.94 C ANISOU 251 CA ALA A 32 8296 5995 8862 -432 -380 -753 C ATOM 252 C ALA A 32 -219.992 58.656 52.866 1.00 68.00 C ANISOU 252 C ALA A 32 9231 6953 9655 -598 -505 -808 C ATOM 253 O ALA A 32 -218.900 58.843 52.326 1.00 82.38 O ANISOU 253 O ALA A 32 10984 8762 11556 -657 -593 -735 O ATOM 254 CB ALA A 32 -221.663 57.194 51.694 1.00 60.43 C ANISOU 254 CB ALA A 32 8159 6087 8716 -346 -407 -624 C ATOM 255 N GLU A 33 -220.140 58.473 54.178 1.00 53.46 N ANISOU 255 N GLU A 33 7498 5180 7634 -686 -513 -935 N ATOM 256 CA GLU A 33 -218.982 58.433 55.058 1.00 56.32 C ANISOU 256 CA GLU A 33 7910 5613 7877 -860 -665 -979 C ATOM 257 C GLU A 33 -218.122 57.212 54.730 1.00 74.97 C ANISOU 257 C GLU A 33 10148 8123 10213 -860 -825 -806 C ATOM 258 O GLU A 33 -218.607 56.241 54.142 1.00 89.79 O ANISOU 258 O GLU A 33 11948 10072 12097 -739 -800 -688 O ATOM 259 CB GLU A 33 -219.426 58.397 56.520 1.00 61.59 C ANISOU 259 CB GLU A 33 8746 6337 8317 -966 -640 -1141 C ATOM 260 CG GLU A 33 -220.235 59.610 56.957 1.00 82.63 C ANISOU 260 CG GLU A 33 11535 8845 11017 -975 -459 -1350 C ATOM 261 CD GLU A 33 -219.425 60.891 56.932 1.00107.05 C ANISOU 261 CD GLU A 33 14664 11785 14227 -1079 -495 -1445 C ATOM 262 OE1 GLU A 33 -218.200 60.830 57.170 1.00115.26 O ANISOU 262 OE1 GLU A 33 15692 12881 15220 -1218 -676 -1408 O ATOM 263 OE2 GLU A 33 -220.016 61.960 56.672 1.00118.22 O ANISOU 263 OE2 GLU A 33 16109 13011 15800 -1023 -348 -1552 O ATOM 264 N PRO A 34 -216.834 57.241 55.089 1.00 68.81 N ANISOU 264 N PRO A 34 9337 7381 9427 -995 -993 -790 N ATOM 265 CA PRO A 34 -215.981 56.074 54.810 1.00 70.43 C ANISOU 265 CA PRO A 34 9400 7708 9650 -986 -1144 -632 C ATOM 266 C PRO A 34 -216.494 54.779 55.414 1.00 73.94 C ANISOU 266 C PRO A 34 9878 8290 9926 -953 -1192 -574 C ATOM 267 O PRO A 34 -216.268 53.708 54.836 1.00 77.17 O ANISOU 267 O PRO A 34 10161 8767 10393 -868 -1243 -433 O ATOM 268 CB PRO A 34 -214.632 56.483 55.414 1.00 60.80 C ANISOU 268 CB PRO A 34 8161 6495 8446 -1162 -1326 -659 C ATOM 269 CG PRO A 34 -214.627 57.957 55.315 1.00 61.48 C ANISOU 269 CG PRO A 34 8318 6428 8613 -1224 -1237 -787 C ATOM 270 CD PRO A 34 -216.046 58.381 55.588 1.00 66.94 C ANISOU 270 CD PRO A 34 9161 7055 9217 -1153 -1052 -907 C ATOM 271 N TRP A 35 -217.182 54.837 56.558 1.00 69.96 N ANISOU 271 N TRP A 35 9546 7822 9215 -1024 -1167 -682 N ATOM 272 CA TRP A 35 -217.697 53.607 57.149 1.00 78.09 C ANISOU 272 CA TRP A 35 10619 8979 10073 -1010 -1207 -615 C ATOM 273 C TRP A 35 -218.855 53.041 56.340 1.00 81.70 C ANISOU 273 C TRP A 35 11023 9433 10585 -832 -1044 -557 C ATOM 274 O TRP A 35 -219.054 51.821 56.315 1.00 84.45 O ANISOU 274 O TRP A 35 11331 9872 10884 -781 -1094 -441 O ATOM 275 CB TRP A 35 -218.118 53.847 58.601 1.00 79.14 C ANISOU 275 CB TRP A 35 10967 9158 9943 -1162 -1204 -751 C ATOM 276 CG TRP A 35 -219.353 54.683 58.776 1.00 85.99 C ANISOU 276 CG TRP A 35 11954 9945 10775 -1127 -957 -925 C ATOM 277 CD1 TRP A 35 -219.406 56.027 58.998 1.00 87.65 C ANISOU 277 CD1 TRP A 35 12251 10031 11020 -1187 -858 -1106 C ATOM 278 CD2 TRP A 35 -220.712 54.225 58.766 1.00 96.75 C ANISOU 278 CD2 TRP A 35 13344 11332 12084 -1023 -774 -940 C ATOM 279 NE1 TRP A 35 -220.712 56.437 59.118 1.00 92.74 N ANISOU 279 NE1 TRP A 35 12967 10613 11655 -1115 -620 -1235 N ATOM 280 CE2 TRP A 35 -221.533 55.350 58.979 1.00 91.76 C ANISOU 280 CE2 TRP A 35 12801 10584 11479 -1015 -565 -1135 C ATOM 281 CE3 TRP A 35 -221.315 52.973 58.593 1.00 90.35 C ANISOU 281 CE3 TRP A 35 12484 10619 11227 -938 -767 -810 C ATOM 282 CZ2 TRP A 35 -222.924 55.262 59.025 1.00 85.18 C ANISOU 282 CZ2 TRP A 35 11988 9738 10640 -921 -348 -1200 C ATOM 283 CZ3 TRP A 35 -222.695 52.889 58.638 1.00 74.63 C ANISOU 283 CZ3 TRP A 35 10524 8621 9212 -858 -558 -871 C ATOM 284 CH2 TRP A 35 -223.484 54.026 58.852 1.00 78.40 C ANISOU 284 CH2 TRP A 35 11069 8988 9729 -848 -350 -1064 C ATOM 285 N GLN A 36 -219.624 53.904 55.672 1.00 82.91 N ANISOU 285 N GLN A 36 11174 9473 10853 -741 -863 -629 N ATOM 286 CA GLN A 36 -220.700 53.420 54.815 1.00 68.12 C ANISOU 286 CA GLN A 36 9236 7592 9054 -578 -734 -563 C ATOM 287 C GLN A 36 -220.153 52.726 53.575 1.00 70.28 C ANISOU 287 C GLN A 36 9351 7881 9470 -486 -797 -402 C ATOM 288 O GLN A 36 -220.777 51.789 53.065 1.00 77.27 O ANISOU 288 O GLN A 36 10185 8815 10359 -386 -765 -313 O ATOM 289 CB GLN A 36 -221.623 54.577 54.436 1.00 63.85 C ANISOU 289 CB GLN A 36 8724 6911 8624 -509 -555 -669 C ATOM 290 CG GLN A 36 -222.574 54.971 55.556 1.00 65.91 C ANISOU 290 CG GLN A 36 9124 7162 8758 -555 -424 -836 C ATOM 291 CD GLN A 36 -223.076 56.391 55.431 1.00 70.26 C ANISOU 291 CD GLN A 36 9710 7537 9448 -527 -278 -980 C ATOM 292 OE1 GLN A 36 -222.492 57.206 54.720 1.00 62.98 O ANISOU 292 OE1 GLN A 36 8743 6502 8686 -517 -310 -962 O ATOM 293 NE2 GLN A 36 -224.164 56.699 56.129 1.00 88.81 N ANISOU 293 NE2 GLN A 36 12138 9855 11751 -517 -109 -1126 N ATOM 294 N PHE A 37 -218.993 53.163 53.081 1.00 75.40 N ANISOU 294 N PHE A 37 9923 8489 10235 -528 -875 -372 N ATOM 295 CA PHE A 37 -218.316 52.403 52.036 1.00 63.99 C ANISOU 295 CA PHE A 37 8330 7075 8909 -465 -925 -238 C ATOM 296 C PHE A 37 -217.841 51.053 52.560 1.00 58.74 C ANISOU 296 C PHE A 37 7620 6525 8176 -482 -1065 -154 C ATOM 297 O PHE A 37 -217.911 50.047 51.844 1.00 53.51 O ANISOU 297 O PHE A 37 6868 5897 7567 -391 -1061 -56 O ATOM 298 CB PHE A 37 -217.143 53.202 51.471 1.00 47.44 C ANISOU 298 CB PHE A 37 6154 4912 6960 -526 -959 -234 C ATOM 299 CG PHE A 37 -217.547 54.236 50.463 1.00 55.41 C ANISOU 299 CG PHE A 37 7170 5801 8082 -478 -825 -247 C ATOM 300 CD1 PHE A 37 -217.891 55.514 50.866 1.00 60.10 C ANISOU 300 CD1 PHE A 37 7865 6285 8686 -526 -769 -358 C ATOM 301 CD2 PHE A 37 -217.589 53.929 49.112 1.00 51.56 C ANISOU 301 CD2 PHE A 37 6599 5303 7690 -394 -760 -145 C ATOM 302 CE1 PHE A 37 -218.267 56.470 49.941 1.00 62.38 C ANISOU 302 CE1 PHE A 37 8160 6443 9098 -481 -667 -349 C ATOM 303 CE2 PHE A 37 -217.964 54.882 48.181 1.00 56.53 C ANISOU 303 CE2 PHE A 37 7251 5820 8409 -365 -661 -132 C ATOM 304 CZ PHE A 37 -218.304 56.154 48.597 1.00 61.52 C ANISOU 304 CZ PHE A 37 7973 6331 9071 -404 -623 -223 C ATOM 305 N SER A 38 -217.355 51.009 53.804 1.00 56.06 N ANISOU 305 N SER A 38 7348 6236 7717 -606 -1199 -188 N ATOM 306 CA SER A 38 -216.904 49.741 54.374 1.00 51.63 C ANISOU 306 CA SER A 38 6751 5769 7098 -630 -1363 -87 C ATOM 307 C SER A 38 -218.071 48.785 54.580 1.00 56.49 C ANISOU 307 C SER A 38 7433 6440 7589 -561 -1301 -48 C ATOM 308 O SER A 38 -217.930 47.572 54.388 1.00 50.09 O ANISOU 308 O SER A 38 6548 5672 6811 -507 -1375 67 O ATOM 309 CB SER A 38 -216.176 49.979 55.697 1.00 49.88 C ANISOU 309 CB SER A 38 6611 5589 6751 -801 -1544 -121 C ATOM 310 OG SER A 38 -215.026 50.786 55.520 1.00 55.18 O ANISOU 310 OG SER A 38 7199 6210 7556 -876 -1623 -148 O ATOM 311 N MET A 39 -219.230 49.313 54.985 1.00 64.38 N ANISOU 311 N MET A 39 8565 7429 8465 -565 -1159 -147 N ATOM 312 CA MET A 39 -220.409 48.470 55.149 1.00 48.88 C ANISOU 312 CA MET A 39 6653 5517 6403 -507 -1078 -116 C ATOM 313 C MET A 39 -220.887 47.927 53.810 1.00 53.28 C ANISOU 313 C MET A 39 7091 6046 7108 -353 -993 -38 C ATOM 314 O MET A 39 -221.383 46.797 53.735 1.00 57.51 O ANISOU 314 O MET A 39 7609 6628 7613 -304 -1002 45 O ATOM 315 CB MET A 39 -221.522 49.251 55.846 1.00 47.20 C ANISOU 315 CB MET A 39 6582 5290 6061 -546 -919 -258 C ATOM 316 CG MET A 39 -221.356 49.338 57.352 1.00 50.64 C ANISOU 316 CG MET A 39 7183 5794 6265 -718 -988 -328 C ATOM 317 SD MET A 39 -221.059 47.721 58.094 1.00 80.05 S ANISOU 317 SD MET A 39 10936 9643 9837 -785 -1179 -163 S ATOM 318 CE MET A 39 -222.522 46.818 57.580 1.00 84.89 C ANISOU 318 CE MET A 39 11516 10275 10463 -654 -1010 -110 C ATOM 319 N LEU A 40 -220.758 48.721 52.743 1.00 47.77 N ANISOU 319 N LEU A 40 6323 5266 6561 -289 -915 -60 N ATOM 320 CA LEU A 40 -220.989 48.190 51.404 1.00 52.68 C ANISOU 320 CA LEU A 40 6843 5868 7306 -171 -862 22 C ATOM 321 C LEU A 40 -220.028 47.048 51.110 1.00 67.45 C ANISOU 321 C LEU A 40 8611 7779 9238 -158 -979 123 C ATOM 322 O LEU A 40 -220.425 46.018 50.552 1.00 78.29 O ANISOU 322 O LEU A 40 9942 9172 10634 -83 -964 192 O ATOM 323 CB LEU A 40 -220.843 49.298 50.360 1.00 45.95 C ANISOU 323 CB LEU A 40 5953 4922 6583 -138 -779 -5 C ATOM 324 CG LEU A 40 -220.832 48.834 48.899 1.00 54.49 C ANISOU 324 CG LEU A 40 6947 5988 7770 -51 -738 79 C ATOM 325 CD1 LEU A 40 -222.157 48.186 48.524 1.00 56.22 C ANISOU 325 CD1 LEU A 40 7183 6225 7952 34 -674 114 C ATOM 326 CD2 LEU A 40 -220.502 49.984 47.953 1.00 68.20 C ANISOU 326 CD2 LEU A 40 8665 7635 9611 -55 -676 70 C ATOM 327 N ALA A 41 -218.760 47.208 51.496 1.00 65.14 N ANISOU 327 N ALA A 41 8270 7490 8992 -234 -1100 128 N ATOM 328 CA ALA A 41 -217.788 46.136 51.321 1.00 51.80 C ANISOU 328 CA ALA A 41 6458 5823 7402 -217 -1219 220 C ATOM 329 C ALA A 41 -218.162 44.914 52.148 1.00 55.09 C ANISOU 329 C ALA A 41 6918 6296 7717 -221 -1319 292 C ATOM 330 O ALA A 41 -218.035 43.777 51.680 1.00 62.17 O ANISOU 330 O ALA A 41 7733 7191 8699 -150 -1348 371 O ATOM 331 CB ALA A 41 -216.392 46.632 51.696 1.00 44.77 C ANISOU 331 CB ALA A 41 5490 4920 6599 -308 -1345 212 C ATOM 332 N ALA A 42 -218.622 45.131 53.383 1.00 44.50 N ANISOU 332 N ALA A 42 5717 5001 6191 -314 -1365 262 N ATOM 333 CA ALA A 42 -219.048 44.015 54.222 1.00 55.72 C ANISOU 333 CA ALA A 42 7206 6479 7487 -342 -1453 341 C ATOM 334 C ALA A 42 -220.236 43.287 53.609 1.00 56.99 C ANISOU 334 C ALA A 42 7373 6640 7641 -242 -1323 368 C ATOM 335 O ALA A 42 -220.310 42.053 53.655 1.00 67.81 O ANISOU 335 O ALA A 42 8718 8021 9025 -214 -1393 468 O ATOM 336 CB ALA A 42 -219.393 44.514 55.626 1.00 46.35 C ANISOU 336 CB ALA A 42 6195 5349 6068 -484 -1489 285 C ATOM 337 N TYR A 43 -221.177 44.033 53.028 1.00 56.26 N ANISOU 337 N TYR A 43 7309 6525 7544 -191 -1146 285 N ATOM 338 CA TYR A 43 -222.317 43.396 52.379 1.00 65.66 C ANISOU 338 CA TYR A 43 8490 7713 8745 -104 -1038 313 C ATOM 339 C TYR A 43 -221.877 42.605 51.153 1.00 70.04 C ANISOU 339 C TYR A 43 8923 8231 9460 -9 -1052 379 C ATOM 340 O TYR A 43 -222.401 41.517 50.887 1.00 71.46 O ANISOU 340 O TYR A 43 9090 8416 9647 35 -1051 440 O ATOM 341 CB TYR A 43 -223.364 44.446 52.012 1.00 64.63 C ANISOU 341 CB TYR A 43 8396 7554 8608 -69 -871 219 C ATOM 342 CG TYR A 43 -224.588 43.874 51.339 1.00 68.43 C ANISOU 342 CG TYR A 43 8854 8033 9113 12 -777 250 C ATOM 343 CD1 TYR A 43 -225.367 42.913 51.970 1.00 71.51 C ANISOU 343 CD1 TYR A 43 9287 8475 9409 -11 -776 293 C ATOM 344 CD2 TYR A 43 -224.969 44.303 50.077 1.00 75.40 C ANISOU 344 CD2 TYR A 43 9678 8862 10109 95 -700 244 C ATOM 345 CE1 TYR A 43 -226.488 42.389 51.355 1.00 74.44 C ANISOU 345 CE1 TYR A 43 9625 8842 9815 52 -699 321 C ATOM 346 CE2 TYR A 43 -226.086 43.789 49.456 1.00 81.99 C ANISOU 346 CE2 TYR A 43 10488 9696 10967 156 -640 278 C ATOM 347 CZ TYR A 43 -226.842 42.832 50.097 1.00 88.37 C ANISOU 347 CZ TYR A 43 11324 10555 11699 137 -639 311 C ATOM 348 OH TYR A 43 -227.956 42.322 49.473 1.00103.56 O ANISOU 348 OH TYR A 43 13211 12476 13660 187 -589 344 O ATOM 349 N MET A 44 -220.907 43.130 50.398 1.00 70.87 N ANISOU 349 N MET A 44 8942 8293 9692 10 -1054 360 N ATOM 350 CA MET A 44 -220.333 42.356 49.301 1.00 69.99 C ANISOU 350 CA MET A 44 8718 8148 9727 82 -1051 404 C ATOM 351 C MET A 44 -219.634 41.107 49.823 1.00 76.03 C ANISOU 351 C MET A 44 9426 8916 10548 80 -1193 484 C ATOM 352 O MET A 44 -219.745 40.028 49.230 1.00 79.02 O ANISOU 352 O MET A 44 9755 9267 11001 145 -1183 526 O ATOM 353 CB MET A 44 -219.354 43.213 48.497 1.00 62.93 C ANISOU 353 CB MET A 44 7743 7215 8952 80 -1009 363 C ATOM 354 CG MET A 44 -219.964 44.434 47.825 1.00 61.54 C ANISOU 354 CG MET A 44 7620 7012 8750 84 -883 306 C ATOM 355 SD MET A 44 -221.203 44.039 46.578 1.00 67.71 S ANISOU 355 SD MET A 44 8430 7782 9515 166 -767 327 S ATOM 356 CE MET A 44 -222.700 44.531 47.425 1.00 68.65 C ANISOU 356 CE MET A 44 8653 7916 9514 162 -737 300 C ATOM 357 N PHE A 45 -218.908 41.236 50.936 1.00 71.60 N ANISOU 357 N PHE A 45 8873 8376 9957 1 -1338 510 N ATOM 358 CA PHE A 45 -218.223 40.087 51.518 1.00 65.10 C ANISOU 358 CA PHE A 45 7991 7542 9201 -6 -1510 612 C ATOM 359 C PHE A 45 -219.218 39.022 51.963 1.00 65.15 C ANISOU 359 C PHE A 45 8088 7566 9102 0 -1529 683 C ATOM 360 O PHE A 45 -218.978 37.822 51.786 1.00 65.48 O ANISOU 360 O PHE A 45 8064 7561 9256 50 -1599 763 O ATOM 361 CB PHE A 45 -217.354 40.544 52.689 1.00 65.76 C ANISOU 361 CB PHE A 45 8090 7655 9242 -118 -1688 636 C ATOM 362 CG PHE A 45 -216.512 39.456 53.281 1.00 59.38 C ANISOU 362 CG PHE A 45 7203 6822 8536 -128 -1905 763 C ATOM 363 CD1 PHE A 45 -215.471 38.899 52.557 1.00 46.54 C ANISOU 363 CD1 PHE A 45 5380 5122 7181 -46 -1944 794 C ATOM 364 CD2 PHE A 45 -216.748 39.000 54.568 1.00 61.06 C ANISOU 364 CD2 PHE A 45 7539 7079 8582 -226 -2068 853 C ATOM 365 CE1 PHE A 45 -214.689 37.898 53.100 1.00 48.12 C ANISOU 365 CE1 PHE A 45 5486 5278 7521 -43 -2157 918 C ATOM 366 CE2 PHE A 45 -215.968 38.001 55.119 1.00 56.11 C ANISOU 366 CE2 PHE A 45 6842 6416 8062 -239 -2298 995 C ATOM 367 CZ PHE A 45 -214.936 37.449 54.384 1.00 49.29 C ANISOU 367 CZ PHE A 45 5759 5462 7505 -138 -2350 1030 C ATOM 368 N LEU A 46 -220.345 39.446 52.541 1.00 70.06 N ANISOU 368 N LEU A 46 8851 8243 9524 -54 -1456 649 N ATOM 369 CA LEU A 46 -221.385 38.498 52.929 1.00 64.87 C ANISOU 369 CA LEU A 46 8275 7607 8764 -62 -1446 711 C ATOM 370 C LEU A 46 -221.945 37.770 51.714 1.00 65.12 C ANISOU 370 C LEU A 46 8242 7589 8910 45 -1344 713 C ATOM 371 O LEU A 46 -222.152 36.551 51.750 1.00 55.12 O ANISOU 371 O LEU A 46 6970 6293 7678 64 -1399 796 O ATOM 372 CB LEU A 46 -222.501 39.223 53.681 1.00 51.30 C ANISOU 372 CB LEU A 46 6699 5958 6835 -139 -1342 647 C ATOM 373 CG LEU A 46 -223.706 38.378 54.100 1.00 48.70 C ANISOU 373 CG LEU A 46 6451 5660 6393 -164 -1294 699 C ATOM 374 CD1 LEU A 46 -223.272 37.273 55.047 1.00 47.54 C ANISOU 374 CD1 LEU A 46 6354 5522 6188 -241 -1476 837 C ATOM 375 CD2 LEU A 46 -224.786 39.242 54.738 1.00 43.09 C ANISOU 375 CD2 LEU A 46 5850 5010 5511 -231 -1146 604 C ATOM 376 N LEU A 47 -222.192 38.500 50.623 1.00 66.89 N ANISOU 376 N LEU A 47 8428 7799 9189 106 -1205 628 N ATOM 377 CA LEU A 47 -222.716 37.866 49.419 1.00 59.75 C ANISOU 377 CA LEU A 47 7480 6854 8366 187 -1118 623 C ATOM 378 C LEU A 47 -221.699 36.928 48.784 1.00 57.06 C ANISOU 378 C LEU A 47 7033 6444 8203 243 -1173 653 C ATOM 379 O LEU A 47 -222.086 35.940 48.153 1.00 56.56 O ANISOU 379 O LEU A 47 6957 6338 8196 289 -1145 670 O ATOM 380 CB LEU A 47 -223.156 38.927 48.414 1.00 64.51 C ANISOU 380 CB LEU A 47 8081 7458 8972 219 -981 541 C ATOM 381 CG LEU A 47 -224.367 39.767 48.817 1.00 56.53 C ANISOU 381 CG LEU A 47 7149 6487 7841 192 -901 503 C ATOM 382 CD1 LEU A 47 -224.555 40.897 47.826 1.00 52.73 C ANISOU 382 CD1 LEU A 47 6652 5981 7400 226 -805 444 C ATOM 383 CD2 LEU A 47 -225.622 38.906 48.899 1.00 47.89 C ANISOU 383 CD2 LEU A 47 6089 5411 6697 197 -872 542 C ATOM 384 N ILE A 48 -220.404 37.213 48.932 1.00 74.24 N ANISOU 384 N ILE A 48 9124 8599 10484 238 -1244 652 N ATOM 385 CA ILE A 48 -219.391 36.331 48.361 1.00 72.22 C ANISOU 385 CA ILE A 48 8738 8264 10437 300 -1280 669 C ATOM 386 C ILE A 48 -219.248 35.069 49.200 1.00 66.88 C ANISOU 386 C ILE A 48 8054 7544 9812 300 -1439 780 C ATOM 387 O ILE A 48 -219.171 33.955 48.667 1.00 51.64 O ANISOU 387 O ILE A 48 6070 5532 8018 364 -1434 797 O ATOM 388 CB ILE A 48 -218.049 37.073 48.224 1.00 52.95 C ANISOU 388 CB ILE A 48 6181 5812 8127 294 -1300 632 C ATOM 389 CG1 ILE A 48 -218.177 38.240 47.245 1.00 55.33 C ANISOU 389 CG1 ILE A 48 6494 6137 8390 291 -1134 536 C ATOM 390 CG2 ILE A 48 -216.955 36.120 47.768 1.00 42.95 C ANISOU 390 CG2 ILE A 48 4750 4454 7113 361 -1333 646 C ATOM 391 CD1 ILE A 48 -217.025 39.221 47.313 1.00 58.67 C ANISOU 391 CD1 ILE A 48 6830 6563 8900 251 -1151 503 C ATOM 392 N MET A 49 -219.216 35.221 50.526 1.00 61.55 N ANISOU 392 N MET A 49 7446 6916 9023 217 -1585 857 N ATOM 393 CA MET A 49 -219.038 34.072 51.409 1.00 59.84 C ANISOU 393 CA MET A 49 7239 6656 8840 195 -1766 992 C ATOM 394 C MET A 49 -220.249 33.147 51.400 1.00 61.73 C ANISOU 394 C MET A 49 7577 6884 8994 196 -1721 1035 C ATOM 395 O MET A 49 -220.112 31.950 51.674 1.00 64.28 O ANISOU 395 O MET A 49 7883 7128 9414 212 -1835 1140 O ATOM 396 CB MET A 49 -218.728 34.549 52.828 1.00 65.70 C ANISOU 396 CB MET A 49 8061 7466 9435 75 -1936 1065 C ATOM 397 CG MET A 49 -217.404 35.300 52.973 1.00 77.38 C ANISOU 397 CG MET A 49 9428 8945 11028 58 -2034 1046 C ATOM 398 SD MET A 49 -215.952 34.280 52.636 1.00 72.71 S ANISOU 398 SD MET A 49 8604 8219 10803 151 -2189 1127 S ATOM 399 CE MET A 49 -215.607 34.697 50.926 1.00 60.53 C ANISOU 399 CE MET A 49 6913 6633 9452 268 -1934 963 C ATOM 400 N LEU A 50 -221.432 33.672 51.089 1.00 63.10 N ANISOU 400 N LEU A 50 7842 7125 9010 180 -1564 964 N ATOM 401 CA LEU A 50 -222.626 32.848 50.937 1.00 49.57 C ANISOU 401 CA LEU A 50 6197 5400 7237 178 -1506 993 C ATOM 402 C LEU A 50 -222.920 32.482 49.489 1.00 62.62 C ANISOU 402 C LEU A 50 7791 6993 9008 267 -1377 914 C ATOM 403 O LEU A 50 -223.431 31.388 49.228 1.00 81.81 O ANISOU 403 O LEU A 50 10235 9363 11487 283 -1381 951 O ATOM 404 CB LEU A 50 -223.850 33.552 51.527 1.00 41.61 C ANISOU 404 CB LEU A 50 5310 4497 6003 99 -1416 968 C ATOM 405 CG LEU A 50 -223.822 33.943 52.999 1.00 46.84 C ANISOU 405 CG LEU A 50 6078 5236 6484 -21 -1502 1021 C ATOM 406 CD1 LEU A 50 -225.155 34.568 53.425 1.00 45.36 C ANISOU 406 CD1 LEU A 50 5993 5137 6104 -87 -1356 965 C ATOM 407 CD2 LEU A 50 -223.495 32.737 53.867 1.00 46.03 C ANISOU 407 CD2 LEU A 50 6013 5091 6383 -76 -1682 1179 C ATOM 408 N GLY A 51 -222.603 33.365 48.544 1.00 64.62 N ANISOU 408 N GLY A 51 7992 7260 9299 310 -1269 808 N ATOM 409 CA GLY A 51 -223.000 33.126 47.166 1.00 61.66 C ANISOU 409 CA GLY A 51 7598 6849 8980 364 -1144 731 C ATOM 410 C GLY A 51 -222.126 32.103 46.468 1.00 67.23 C ANISOU 410 C GLY A 51 8214 7442 9889 431 -1152 714 C ATOM 411 O GLY A 51 -222.628 31.179 45.818 1.00 76.64 O ANISOU 411 O GLY A 51 9423 8572 11122 453 -1112 696 O ATOM 412 N PHE A 52 -220.807 32.259 46.578 1.00 74.88 N ANISOU 412 N PHE A 52 9076 8374 11002 461 -1199 708 N ATOM 413 CA PHE A 52 -219.907 31.345 45.877 1.00 69.89 C ANISOU 413 CA PHE A 52 8330 7621 10603 535 -1178 670 C ATOM 414 C PHE A 52 -220.043 29.901 46.343 1.00 69.13 C ANISOU 414 C PHE A 52 8233 7418 10616 558 -1289 757 C ATOM 415 O PHE A 52 -220.203 29.018 45.483 1.00 74.94 O ANISOU 415 O PHE A 52 8960 8061 11454 603 -1209 696 O ATOM 416 CB PHE A 52 -218.455 31.824 45.994 1.00 61.38 C ANISOU 416 CB PHE A 52 7107 6524 9692 560 -1212 655 C ATOM 417 CG PHE A 52 -217.459 30.824 45.485 1.00 61.98 C ANISOU 417 CG PHE A 52 7034 6460 10056 644 -1199 622 C ATOM 418 CD1 PHE A 52 -217.309 30.612 44.124 1.00 66.20 C ANISOU 418 CD1 PHE A 52 7536 6946 10669 686 -1003 484 C ATOM 419 CD2 PHE A 52 -216.690 30.076 46.363 1.00 64.68 C ANISOU 419 CD2 PHE A 52 7271 6711 10593 677 -1382 729 C ATOM 420 CE1 PHE A 52 -216.400 29.682 43.643 1.00 67.98 C ANISOU 420 CE1 PHE A 52 7619 7032 11179 766 -958 427 C ATOM 421 CE2 PHE A 52 -215.779 29.142 45.891 1.00 63.44 C ANISOU 421 CE2 PHE A 52 6954 6402 10748 770 -1365 693 C ATOM 422 CZ PHE A 52 -215.634 28.946 44.528 1.00 59.51 C ANISOU 422 CZ PHE A 52 6416 5853 10341 818 -1137 530 C ATOM 423 N PRO A 53 -219.983 29.579 47.642 1.00 60.50 N ANISOU 423 N PRO A 53 7160 6322 9505 521 -1471 897 N ATOM 424 CA PRO A 53 -220.082 28.158 48.025 1.00 57.87 C ANISOU 424 CA PRO A 53 6828 5864 9296 540 -1584 996 C ATOM 425 C PRO A 53 -221.390 27.514 47.601 1.00 67.12 C ANISOU 425 C PRO A 53 8113 7024 10364 515 -1504 980 C ATOM 426 O PRO A 53 -221.379 26.407 47.049 1.00 83.77 O ANISOU 426 O PRO A 53 10197 8998 12634 564 -1487 959 O ATOM 427 CB PRO A 53 -219.926 28.197 49.553 1.00 49.77 C ANISOU 427 CB PRO A 53 5847 4877 8187 464 -1796 1163 C ATOM 428 CG PRO A 53 -219.227 29.469 49.830 1.00 63.53 C ANISOU 428 CG PRO A 53 7546 6720 9874 439 -1808 1128 C ATOM 429 CD PRO A 53 -219.764 30.434 48.822 1.00 57.87 C ANISOU 429 CD PRO A 53 6859 6087 9043 447 -1592 975 C ATOM 430 N ILE A 54 -222.520 28.186 47.827 1.00 58.61 N ANISOU 430 N ILE A 54 7152 6077 9042 439 -1450 980 N ATOM 431 CA ILE A 54 -223.814 27.601 47.487 1.00 59.43 C ANISOU 431 CA ILE A 54 7344 6177 9058 403 -1388 975 C ATOM 432 C ILE A 54 -223.912 27.346 45.985 1.00 60.82 C ANISOU 432 C ILE A 54 7497 6296 9316 456 -1249 835 C ATOM 433 O ILE A 54 -224.344 26.270 45.550 1.00 68.83 O ANISOU 433 O ILE A 54 8536 7211 10404 460 -1240 825 O ATOM 434 CB ILE A 54 -224.955 28.504 47.994 1.00 61.94 C ANISOU 434 CB ILE A 54 7756 6646 9132 320 -1341 990 C ATOM 435 CG1 ILE A 54 -224.933 28.584 49.524 1.00 68.91 C ANISOU 435 CG1 ILE A 54 8697 7582 9906 241 -1465 1120 C ATOM 436 CG2 ILE A 54 -226.302 27.990 47.510 1.00 57.84 C ANISOU 436 CG2 ILE A 54 7297 6128 8551 284 -1271 975 C ATOM 437 CD1 ILE A 54 -226.028 29.451 50.112 1.00 70.50 C ANISOU 437 CD1 ILE A 54 8985 7922 9881 156 -1391 1115 C ATOM 438 N ASN A 55 -223.493 28.316 45.170 1.00 56.72 N ANISOU 438 N ASN A 55 6941 5833 8776 484 -1139 724 N ATOM 439 CA ASN A 55 -223.601 28.161 43.723 1.00 66.44 C ANISOU 439 CA ASN A 55 8179 7029 10037 507 -1001 589 C ATOM 440 C ASN A 55 -222.532 27.238 43.158 1.00 67.82 C ANISOU 440 C ASN A 55 8266 7052 10449 579 -969 520 C ATOM 441 O ASN A 55 -222.797 26.511 42.195 1.00 60.84 O ANISOU 441 O ASN A 55 7416 6091 9607 583 -883 425 O ATOM 442 CB ASN A 55 -223.540 29.526 43.043 1.00 66.42 C ANISOU 442 CB ASN A 55 8183 7135 9918 494 -895 511 C ATOM 443 CG ASN A 55 -224.757 30.381 43.349 1.00 77.53 C ANISOU 443 CG ASN A 55 9670 8663 11125 435 -900 554 C ATOM 444 OD1 ASN A 55 -225.820 30.197 42.755 1.00 85.22 O ANISOU 444 OD1 ASN A 55 10708 9654 12018 401 -867 535 O ATOM 445 ND2 ASN A 55 -224.609 31.321 44.276 1.00 81.21 N ANISOU 445 ND2 ASN A 55 10126 9207 11524 420 -943 605 N ATOM 446 N PHE A 56 -221.332 27.244 43.737 1.00 75.15 N ANISOU 446 N PHE A 56 9077 7930 11544 632 -1037 558 N ATOM 447 CA PHE A 56 -220.303 26.318 43.280 1.00 67.06 C ANISOU 447 CA PHE A 56 7939 6742 10800 715 -1006 493 C ATOM 448 C PHE A 56 -220.624 24.891 43.704 1.00 72.44 C ANISOU 448 C PHE A 56 8639 7273 11612 733 -1111 568 C ATOM 449 O PHE A 56 -220.372 23.944 42.949 1.00 78.38 O ANISOU 449 O PHE A 56 9362 7876 12545 783 -1032 470 O ATOM 450 CB PHE A 56 -218.931 26.739 43.808 1.00 55.98 C ANISOU 450 CB PHE A 56 6375 5321 9573 767 -1069 526 C ATOM 451 CG PHE A 56 -217.828 25.793 43.442 1.00 64.20 C ANISOU 451 CG PHE A 56 7260 6179 10955 866 -1042 467 C ATOM 452 CD1 PHE A 56 -217.218 25.868 42.201 1.00 67.83 C ANISOU 452 CD1 PHE A 56 7651 6600 11522 904 -826 282 C ATOM 453 CD2 PHE A 56 -217.399 24.828 44.338 1.00 66.41 C ANISOU 453 CD2 PHE A 56 7460 6319 11455 916 -1229 596 C ATOM 454 CE1 PHE A 56 -216.202 24.997 41.861 1.00 67.85 C ANISOU 454 CE1 PHE A 56 7492 6422 11866 1001 -772 206 C ATOM 455 CE2 PHE A 56 -216.384 23.954 44.002 1.00 68.83 C ANISOU 455 CE2 PHE A 56 7599 6433 12121 1022 -1205 540 C ATOM 456 CZ PHE A 56 -215.785 24.040 42.763 1.00 70.96 C ANISOU 456 CZ PHE A 56 7785 6661 12515 1070 -965 334 C ATOM 457 N LEU A 57 -221.183 24.716 44.906 1.00 66.42 N ANISOU 457 N LEU A 57 7936 6541 10760 682 -1280 739 N ATOM 458 CA LEU A 57 -221.573 23.381 45.352 1.00 67.22 C ANISOU 458 CA LEU A 57 8074 6499 10969 679 -1389 835 C ATOM 459 C LEU A 57 -222.667 22.796 44.470 1.00 68.34 C ANISOU 459 C LEU A 57 8323 6611 11033 639 -1279 743 C ATOM 460 O LEU A 57 -222.725 21.576 44.281 1.00 79.99 O ANISOU 460 O LEU A 57 9803 7913 12676 661 -1301 739 O ATOM 461 CB LEU A 57 -222.033 23.423 46.811 1.00 66.34 C ANISOU 461 CB LEU A 57 8032 6453 10721 600 -1573 1039 C ATOM 462 CG LEU A 57 -222.359 22.090 47.486 1.00 91.51 C ANISOU 462 CG LEU A 57 11265 9494 14012 576 -1717 1186 C ATOM 463 CD1 LEU A 57 -221.142 21.177 47.483 1.00 98.72 C ANISOU 463 CD1 LEU A 57 12041 10191 15279 684 -1812 1213 C ATOM 464 CD2 LEU A 57 -222.860 22.318 48.904 1.00101.25 C ANISOU 464 CD2 LEU A 57 12594 10832 15043 466 -1869 1379 C ATOM 465 N THR A 58 -223.541 23.646 43.925 1.00 73.38 N ANISOU 465 N THR A 58 9044 7404 11432 576 -1175 674 N ATOM 466 CA THR A 58 -224.553 23.171 42.986 1.00 70.57 C ANISOU 466 CA THR A 58 8783 7030 11000 526 -1087 583 C ATOM 467 C THR A 58 -223.905 22.572 41.745 1.00 77.29 C ANISOU 467 C THR A 58 9605 7747 12014 581 -957 404 C ATOM 468 O THR A 58 -224.288 21.488 41.289 1.00 83.83 O ANISOU 468 O THR A 58 10483 8442 12926 567 -941 351 O ATOM 469 CB THR A 58 -225.490 24.315 42.598 1.00 57.41 C ANISOU 469 CB THR A 58 7186 5551 9075 458 -1019 551 C ATOM 470 OG1 THR A 58 -226.292 24.684 43.726 1.00 54.11 O ANISOU 470 OG1 THR A 58 6803 5235 8519 397 -1111 694 O ATOM 471 CG2 THR A 58 -226.394 23.892 41.447 1.00 56.03 C ANISOU 471 CG2 THR A 58 7098 5358 8832 402 -940 445 C ATOM 472 N LEU A 59 -222.919 23.271 41.181 1.00 76.36 N ANISOU 472 N LEU A 59 9410 7659 11942 634 -849 300 N ATOM 473 CA LEU A 59 -222.207 22.743 40.024 1.00 75.34 C ANISOU 473 CA LEU A 59 9250 7409 11969 680 -690 112 C ATOM 474 C LEU A 59 -221.403 21.501 40.380 1.00 78.16 C ANISOU 474 C LEU A 59 9502 7538 12658 772 -739 120 C ATOM 475 O LEU A 59 -221.216 20.621 39.533 1.00 78.66 O ANISOU 475 O LEU A 59 9574 7448 12865 796 -624 -31 O ATOM 476 CB LEU A 59 -221.288 23.813 39.439 1.00 76.72 C ANISOU 476 CB LEU A 59 9354 7673 12125 704 -554 14 C ATOM 477 CG LEU A 59 -221.928 25.141 39.037 1.00 83.65 C ANISOU 477 CG LEU A 59 10323 8753 12706 622 -507 12 C ATOM 478 CD1 LEU A 59 -220.881 26.072 38.447 1.00 81.78 C ANISOU 478 CD1 LEU A 59 10012 8573 12488 641 -367 -82 C ATOM 479 CD2 LEU A 59 -223.066 24.914 38.052 1.00 88.39 C ANISOU 479 CD2 LEU A 59 11083 9384 13118 531 -447 -67 C ATOM 480 N TYR A 60 -220.933 21.404 41.624 1.00 78.74 N ANISOU 480 N TYR A 60 9482 7576 12860 819 -916 295 N ATOM 481 CA TYR A 60 -220.060 20.299 42.000 1.00 81.48 C ANISOU 481 CA TYR A 60 9705 7693 13560 918 -992 328 C ATOM 482 C TYR A 60 -220.846 19.012 42.231 1.00 88.97 C ANISOU 482 C TYR A 60 10745 8485 14575 890 -1081 391 C ATOM 483 O TYR A 60 -220.455 17.946 41.744 1.00 99.37 O ANISOU 483 O TYR A 60 12020 9581 16156 955 -1027 293 O ATOM 484 CB TYR A 60 -219.252 20.667 43.245 1.00 79.78 C ANISOU 484 CB TYR A 60 9364 7496 13451 961 -1182 513 C ATOM 485 CG TYR A 60 -218.215 19.636 43.615 1.00 85.51 C ANISOU 485 CG TYR A 60 9928 7979 14582 1075 -1283 563 C ATOM 486 CD1 TYR A 60 -217.038 19.516 42.888 1.00 86.60 C ANISOU 486 CD1 TYR A 60 9890 7999 15017 1185 -1143 405 C ATOM 487 CD2 TYR A 60 -218.410 18.781 44.692 1.00 89.67 C ANISOU 487 CD2 TYR A 60 10474 8388 15210 1070 -1518 774 C ATOM 488 CE1 TYR A 60 -216.086 18.574 43.221 1.00 95.20 C ANISOU 488 CE1 TYR A 60 10801 8846 16524 1303 -1239 450 C ATOM 489 CE2 TYR A 60 -217.463 17.835 45.033 1.00 97.56 C ANISOU 489 CE2 TYR A 60 11317 9144 16608 1180 -1637 840 C ATOM 490 CZ TYR A 60 -216.303 17.736 44.294 1.00100.54 C ANISOU 490 CZ TYR A 60 11497 9396 17307 1305 -1499 675 C ATOM 491 OH TYR A 60 -215.358 16.795 44.631 1.00110.61 O ANISOU 491 OH TYR A 60 12590 10412 19026 1428 -1621 741 O ATOM 492 N VAL A 61 -221.957 19.090 42.970 1.00 82.02 N ANISOU 492 N VAL A 61 9987 7707 13469 790 -1206 546 N ATOM 493 CA VAL A 61 -222.736 17.890 43.253 1.00 77.52 C ANISOU 493 CA VAL A 61 9504 6993 12956 745 -1296 624 C ATOM 494 C VAL A 61 -223.413 17.350 42.002 1.00 85.34 C ANISOU 494 C VAL A 61 10592 7921 13911 702 -1140 430 C ATOM 495 O VAL A 61 -223.737 16.158 41.945 1.00101.67 O ANISOU 495 O VAL A 61 12704 9798 16127 691 -1176 431 O ATOM 496 CB VAL A 61 -223.778 18.153 44.357 1.00 72.85 C ANISOU 496 CB VAL A 61 9015 6543 12124 631 -1442 832 C ATOM 497 CG1 VAL A 61 -223.090 18.611 45.634 1.00 76.89 C ANISOU 497 CG1 VAL A 61 9457 7107 12649 651 -1609 1021 C ATOM 498 CG2 VAL A 61 -224.812 19.172 43.894 1.00 69.35 C ANISOU 498 CG2 VAL A 61 8663 6330 11356 539 -1335 764 C ATOM 499 N THR A 62 -223.641 18.196 40.995 1.00 84.35 N ANISOU 499 N THR A 62 10513 7947 13588 665 -977 268 N ATOM 500 CA THR A 62 -224.157 17.703 39.724 1.00 81.38 C ANISOU 500 CA THR A 62 10240 7513 13167 612 -834 70 C ATOM 501 C THR A 62 -223.140 16.805 39.027 1.00 79.79 C ANISOU 501 C THR A 62 9970 7076 13270 707 -711 -109 C ATOM 502 O THR A 62 -223.523 15.894 38.286 1.00 86.52 O ANISOU 502 O THR A 62 10910 7786 14177 668 -638 -247 O ATOM 503 CB THR A 62 -224.548 18.882 38.829 1.00 76.68 C ANISOU 503 CB THR A 62 9716 7138 12283 543 -709 -39 C ATOM 504 OG1 THR A 62 -225.474 19.723 39.529 1.00 87.73 O ANISOU 504 OG1 THR A 62 11154 8734 13446 472 -818 123 O ATOM 505 CG2 THR A 62 -225.195 18.401 37.539 1.00 54.04 C ANISOU 505 CG2 THR A 62 6983 4230 9318 455 -593 -226 C ATOM 506 N VAL A 63 -221.847 17.030 39.272 1.00 76.25 N ANISOU 506 N VAL A 63 9357 6573 13041 828 -685 -115 N ATOM 507 CA VAL A 63 -220.816 16.208 38.648 1.00 79.59 C ANISOU 507 CA VAL A 63 9678 6760 13800 933 -548 -294 C ATOM 508 C VAL A 63 -220.739 14.833 39.304 1.00 84.47 C ANISOU 508 C VAL A 63 10255 7103 14737 995 -691 -197 C ATOM 509 O VAL A 63 -220.476 13.829 38.628 1.00 71.29 O ANISOU 509 O VAL A 63 8584 5201 13302 1037 -576 -370 O ATOM 510 CB VAL A 63 -219.463 16.940 38.701 1.00 58.48 C ANISOU 510 CB VAL A 63 6813 4122 11285 1040 -475 -325 C ATOM 511 CG1 VAL A 63 -218.353 16.076 38.115 1.00 61.40 C ANISOU 511 CG1 VAL A 63 7040 4234 12054 1162 -319 -513 C ATOM 512 CG2 VAL A 63 -219.555 18.264 37.961 1.00 56.75 C ANISOU 512 CG2 VAL A 63 6653 4155 10755 966 -323 -425 C ATOM 513 N GLN A 64 -220.982 14.754 40.610 1.00 84.82 N ANISOU 513 N GLN A 64 10281 7159 14789 990 -937 75 N ATOM 514 CA GLN A 64 -220.800 13.525 41.372 1.00 83.21 C ANISOU 514 CA GLN A 64 10029 6691 14895 1046 -1108 217 C ATOM 515 C GLN A 64 -222.055 12.663 41.460 1.00 91.68 C ANISOU 515 C GLN A 64 11276 7690 15869 931 -1182 275 C ATOM 516 O GLN A 64 -221.994 11.567 42.029 1.00 96.90 O ANISOU 516 O GLN A 64 11921 8111 16785 961 -1321 395 O ATOM 517 CB GLN A 64 -220.314 13.853 42.787 1.00 83.55 C ANISOU 517 CB GLN A 64 9970 6778 14996 1083 -1354 501 C ATOM 518 CG GLN A 64 -218.899 14.400 42.853 1.00 87.77 C ANISOU 518 CG GLN A 64 10290 7305 15753 1212 -1333 472 C ATOM 519 CD GLN A 64 -218.363 14.442 44.270 1.00 90.19 C ANISOU 519 CD GLN A 64 10499 7594 16174 1243 -1620 762 C ATOM 520 OE1 GLN A 64 -217.183 14.713 44.494 1.00 92.19 O ANISOU 520 OE1 GLN A 64 10556 7803 16667 1348 -1664 781 O ATOM 521 NE2 GLN A 64 -219.232 14.168 45.237 1.00 86.24 N ANISOU 521 NE2 GLN A 64 10137 7130 15500 1138 -1819 991 N ATOM 522 N HIS A 65 -223.184 13.115 40.916 1.00 87.82 N ANISOU 522 N HIS A 65 10943 7389 15036 796 -1104 205 N ATOM 523 CA HIS A 65 -224.446 12.387 41.038 1.00 81.53 C ANISOU 523 CA HIS A 65 10296 6547 14134 668 -1181 272 C ATOM 524 C HIS A 65 -225.138 12.360 39.682 1.00 89.01 C ANISOU 524 C HIS A 65 11370 7535 14913 577 -1003 23 C ATOM 525 O HIS A 65 -225.555 13.405 39.172 1.00 87.39 O ANISOU 525 O HIS A 65 11215 7576 14413 512 -921 -42 O ATOM 526 CB HIS A 65 -225.338 13.018 42.105 1.00 69.89 C ANISOU 526 CB HIS A 65 8877 5293 12385 563 -1336 518 C ATOM 527 CG HIS A 65 -224.716 13.037 43.467 1.00 84.04 C ANISOU 527 CG HIS A 65 10582 7059 14292 618 -1527 768 C ATOM 528 ND1 HIS A 65 -224.932 12.045 44.400 1.00 91.49 N ANISOU 528 ND1 HIS A 65 11555 7831 15376 586 -1709 977 N ATOM 529 CD2 HIS A 65 -223.869 13.920 44.047 1.00 89.21 C ANISOU 529 CD2 HIS A 65 11129 7831 14934 688 -1577 849 C ATOM 530 CE1 HIS A 65 -224.251 12.321 45.498 1.00 94.45 C ANISOU 530 CE1 HIS A 65 11854 8229 15805 629 -1872 1182 C ATOM 531 NE2 HIS A 65 -223.598 13.454 45.310 1.00 92.68 N ANISOU 531 NE2 HIS A 65 11543 8180 15492 692 -1797 1103 N ATOM 532 N LYS A 66 -225.276 11.157 39.114 1.00 96.15 N ANISOU 532 N LYS A 66 12336 8190 16006 563 -957 -108 N ATOM 533 CA LYS A 66 -225.827 11.011 37.770 1.00 92.12 C ANISOU 533 CA LYS A 66 11961 7690 15352 466 -791 -366 C ATOM 534 C LYS A 66 -227.313 11.348 37.720 1.00 82.84 C ANISOU 534 C LYS A 66 10921 6712 13842 288 -868 -291 C ATOM 535 O LYS A 66 -227.801 11.837 36.694 1.00 70.10 O ANISOU 535 O LYS A 66 9406 5238 11989 194 -763 -452 O ATOM 536 CB LYS A 66 -225.585 9.585 37.263 1.00 91.51 C ANISOU 536 CB LYS A 66 11917 7270 15581 491 -729 -530 C ATOM 537 CG LYS A 66 -225.915 9.371 35.789 1.00101.43 C ANISOU 537 CG LYS A 66 13321 8508 16709 393 -533 -843 C ATOM 538 CD LYS A 66 -225.591 7.954 35.331 1.00106.34 C ANISOU 538 CD LYS A 66 13975 8767 17663 426 -455 -1028 C ATOM 539 CE LYS A 66 -225.640 7.841 33.813 1.00105.14 C ANISOU 539 CE LYS A 66 13968 8600 17380 337 -218 -1383 C ATOM 540 NZ LYS A 66 -224.585 8.670 33.163 1.00103.25 N ANISOU 540 NZ LYS A 66 13653 8470 17107 423 2 -1557 N ATOM 541 N LYS A 67 -228.043 11.107 38.812 1.00 86.94 N ANISOU 541 N LYS A 67 11444 7247 14342 231 -1051 -42 N ATOM 542 CA LYS A 67 -229.479 11.361 38.829 1.00 89.87 C ANISOU 542 CA LYS A 67 11912 7790 14444 64 -1118 35 C ATOM 543 C LYS A 67 -229.816 12.844 38.727 1.00 95.53 C ANISOU 543 C LYS A 67 12615 8829 14855 36 -1088 61 C ATOM 544 O LYS A 67 -230.967 13.183 38.430 1.00 99.75 O ANISOU 544 O LYS A 67 13216 9512 15171 -94 -1113 71 O ATOM 545 CB LYS A 67 -230.101 10.773 40.098 1.00 89.02 C ANISOU 545 CB LYS A 67 11800 7623 14399 8 -1294 298 C ATOM 546 CG LYS A 67 -230.062 9.250 40.167 1.00 86.41 C ANISOU 546 CG LYS A 67 11511 6964 14356 -3 -1347 295 C ATOM 547 CD LYS A 67 -230.805 8.625 38.996 1.00 90.68 C ANISOU 547 CD LYS A 67 12175 7420 14860 -123 -1273 81 C ATOM 548 CE LYS A 67 -230.821 7.109 39.091 1.00 96.30 C ANISOU 548 CE LYS A 67 12934 7787 15867 -144 -1328 76 C ATOM 549 NZ LYS A 67 -231.534 6.489 37.939 1.00100.29 N ANISOU 549 NZ LYS A 67 13574 8204 16329 -278 -1259 -151 N ATOM 550 N LEU A 68 -228.847 13.731 38.961 1.00 95.48 N ANISOU 550 N LEU A 68 12513 8920 14846 154 -1042 74 N ATOM 551 CA LEU A 68 -229.096 15.162 38.828 1.00 83.12 C ANISOU 551 CA LEU A 68 10936 7635 13012 133 -1008 90 C ATOM 552 C LEU A 68 -229.033 15.628 37.379 1.00 86.10 C ANISOU 552 C LEU A 68 11383 8082 13248 99 -859 -141 C ATOM 553 O LEU A 68 -229.648 16.642 37.034 1.00 92.71 O ANISOU 553 O LEU A 68 12252 9133 13839 33 -853 -132 O ATOM 554 CB LEU A 68 -228.090 15.960 39.661 1.00 68.04 C ANISOU 554 CB LEU A 68 8905 5801 11149 253 -1026 196 C ATOM 555 CG LEU A 68 -228.118 15.771 41.177 1.00 64.84 C ANISOU 555 CG LEU A 68 8447 5380 10811 267 -1187 446 C ATOM 556 CD1 LEU A 68 -227.049 16.620 41.854 1.00 71.63 C ANISOU 556 CD1 LEU A 68 9197 6320 11700 372 -1209 522 C ATOM 557 CD2 LEU A 68 -229.492 16.108 41.723 1.00 59.42 C ANISOU 557 CD2 LEU A 68 7818 4857 9902 137 -1259 583 C ATOM 558 N ARG A 69 -228.305 14.911 36.523 1.00 78.33 N ANISOU 558 N ARG A 69 10428 6917 12416 136 -735 -346 N ATOM 559 CA ARG A 69 -228.055 15.384 35.167 1.00 72.96 C ANISOU 559 CA ARG A 69 9827 6307 11587 97 -569 -572 C ATOM 560 C ARG A 69 -229.189 15.021 34.217 1.00 78.98 C ANISOU 560 C ARG A 69 10756 7088 12165 -73 -580 -678 C ATOM 561 O ARG A 69 -228.957 14.419 33.165 1.00 79.22 O ANISOU 561 O ARG A 69 10890 7000 12210 -120 -455 -905 O ATOM 562 CB ARG A 69 -226.725 14.832 34.650 1.00 69.39 C ANISOU 562 CB ARG A 69 9329 5660 11375 205 -396 -770 C ATOM 563 CG ARG A 69 -225.535 15.193 35.529 1.00 62.29 C ANISOU 563 CG ARG A 69 8244 4738 10686 371 -401 -667 C ATOM 564 CD ARG A 69 -224.213 14.852 34.858 1.00 65.46 C ANISOU 564 CD ARG A 69 8573 4978 11321 474 -197 -886 C ATOM 565 NE ARG A 69 -224.024 13.414 34.687 1.00 86.17 N ANISOU 565 NE ARG A 69 11206 7300 14233 508 -163 -1002 N ATOM 566 CZ ARG A 69 -223.489 12.617 35.606 1.00 88.17 C ANISOU 566 CZ ARG A 69 11329 7338 14832 629 -268 -886 C ATOM 567 NH1 ARG A 69 -223.350 11.321 35.360 1.00 89.13 N ANISOU 567 NH1 ARG A 69 11470 7168 15228 658 -229 -1005 N ATOM 568 NH2 ARG A 69 -223.095 13.113 36.771 1.00 78.64 N ANISOU 568 NH2 ARG A 69 9982 6200 13696 714 -422 -648 N ATOM 569 N THR A 70 -230.429 15.398 34.581 1.00 83.36 N ANISOU 569 N THR A 70 11333 7792 12547 -174 -726 -520 N ATOM 570 CA THR A 70 -231.598 15.275 33.728 1.00 88.00 C ANISOU 570 CA THR A 70 12054 8441 12942 -346 -776 -584 C ATOM 571 C THR A 70 -231.846 16.585 32.988 1.00 89.21 C ANISOU 571 C THR A 70 12249 8832 12815 -402 -753 -603 C ATOM 572 O THR A 70 -231.475 17.657 33.476 1.00 95.95 O ANISOU 572 O THR A 70 13009 9828 13619 -317 -745 -497 O ATOM 573 CB THR A 70 -232.837 14.906 34.550 1.00 95.66 C ANISOU 573 CB THR A 70 12997 9427 13924 -428 -949 -394 C ATOM 574 OG1 THR A 70 -233.065 15.901 35.556 1.00103.40 O ANISOU 574 OG1 THR A 70 13860 10585 14842 -375 -1017 -186 O ATOM 575 CG2 THR A 70 -232.647 13.551 35.217 1.00102.12 C ANISOU 575 CG2 THR A 70 13797 9992 15011 -398 -984 -363 C ATOM 576 N PRO A 71 -232.460 16.533 31.801 1.00 84.49 N ANISOU 576 N PRO A 71 11800 8274 12028 -553 -753 -733 N ATOM 577 CA PRO A 71 -232.637 17.771 31.020 1.00 88.86 C ANISOU 577 CA PRO A 71 12409 9039 12316 -613 -745 -739 C ATOM 578 C PRO A 71 -233.395 18.860 31.759 1.00 89.49 C ANISOU 578 C PRO A 71 12377 9309 12316 -595 -881 -510 C ATOM 579 O PRO A 71 -233.103 20.047 31.569 1.00 92.20 O ANISOU 579 O PRO A 71 12701 9799 12532 -562 -850 -473 O ATOM 580 CB PRO A 71 -233.402 17.286 29.781 1.00 89.97 C ANISOU 580 CB PRO A 71 12737 9167 12281 -809 -785 -881 C ATOM 581 CG PRO A 71 -233.022 15.855 29.651 1.00 90.69 C ANISOU 581 CG PRO A 71 12888 9012 12556 -814 -704 -1049 C ATOM 582 CD PRO A 71 -232.910 15.345 31.057 1.00 90.49 C ANISOU 582 CD PRO A 71 12699 8877 12806 -682 -759 -890 C ATOM 583 N LEU A 72 -234.357 18.492 32.606 1.00 83.60 N ANISOU 583 N LEU A 72 11555 8555 11654 -621 -1018 -360 N ATOM 584 CA LEU A 72 -235.131 19.491 33.332 1.00 81.33 C ANISOU 584 CA LEU A 72 11152 8437 11311 -606 -1121 -163 C ATOM 585 C LEU A 72 -234.295 20.248 34.358 1.00 79.86 C ANISOU 585 C LEU A 72 10846 8303 11197 -448 -1058 -65 C ATOM 586 O LEU A 72 -234.745 21.286 34.856 1.00 70.84 O ANISOU 586 O LEU A 72 9619 7306 9990 -424 -1106 64 O ATOM 587 CB LEU A 72 -236.326 18.822 34.012 1.00 82.04 C ANISOU 587 CB LEU A 72 11185 8498 11488 -683 -1249 -42 C ATOM 588 CG LEU A 72 -237.520 19.714 34.349 1.00 90.36 C ANISOU 588 CG LEU A 72 12140 9723 12471 -728 -1361 116 C ATOM 589 CD1 LEU A 72 -237.961 20.511 33.131 1.00 96.79 C ANISOU 589 CD1 LEU A 72 13023 10656 13098 -814 -1421 70 C ATOM 590 CD2 LEU A 72 -238.661 18.861 34.871 1.00 93.43 C ANISOU 590 CD2 LEU A 72 12477 10061 12961 -829 -1462 202 C ATOM 591 N ASN A 73 -233.096 19.760 34.678 1.00 79.09 N ANISOU 591 N ASN A 73 10730 8079 11241 -343 -958 -128 N ATOM 592 CA ASN A 73 -232.197 20.433 35.604 1.00 74.28 C ANISOU 592 CA ASN A 73 10011 7510 10703 -205 -914 -45 C ATOM 593 C ASN A 73 -231.120 21.257 34.910 1.00 70.24 C ANISOU 593 C ASN A 73 9514 7050 10125 -147 -788 -153 C ATOM 594 O ASN A 73 -230.345 21.929 35.598 1.00 64.93 O ANISOU 594 O ASN A 73 8747 6420 9502 -44 -756 -90 O ATOM 595 CB ASN A 73 -231.521 19.413 36.532 1.00 77.04 C ANISOU 595 CB ASN A 73 10304 7685 11283 -123 -915 -9 C ATOM 596 CG ASN A 73 -232.472 18.840 37.559 1.00 90.13 C ANISOU 596 CG ASN A 73 11928 9320 12998 -172 -1037 153 C ATOM 597 OD1 ASN A 73 -233.509 19.432 37.855 1.00 99.70 O ANISOU 597 OD1 ASN A 73 13115 10673 14094 -236 -1101 257 O ATOM 598 ND2 ASN A 73 -232.122 17.685 38.113 1.00 94.68 N ANISOU 598 ND2 ASN A 73 12497 9709 13767 -145 -1063 180 N ATOM 599 N TYR A 74 -231.046 21.219 33.576 1.00 61.87 N ANISOU 599 N TYR A 74 8576 5988 8944 -227 -714 -313 N ATOM 600 CA TYR A 74 -230.015 21.980 32.874 1.00 62.91 C ANISOU 600 CA TYR A 74 8730 6170 9003 -192 -571 -418 C ATOM 601 C TYR A 74 -230.147 23.471 33.154 1.00 76.00 C ANISOU 601 C TYR A 74 10332 8009 10535 -169 -610 -289 C ATOM 602 O TYR A 74 -229.145 24.163 33.367 1.00 82.50 O ANISOU 602 O TYR A 74 11090 8863 11394 -83 -522 -292 O ATOM 603 CB TYR A 74 -230.084 21.720 31.367 1.00 68.02 C ANISOU 603 CB TYR A 74 9551 6805 9488 -321 -489 -603 C ATOM 604 CG TYR A 74 -229.622 20.349 30.914 1.00 73.29 C ANISOU 604 CG TYR A 74 10286 7274 10288 -334 -384 -794 C ATOM 605 CD1 TYR A 74 -229.381 19.329 31.826 1.00 80.12 C ANISOU 605 CD1 TYR A 74 11056 7968 11419 -241 -408 -766 C ATOM 606 CD2 TYR A 74 -229.416 20.080 29.565 1.00 74.77 C ANISOU 606 CD2 TYR A 74 10641 7434 10333 -447 -257 -1005 C ATOM 607 CE1 TYR A 74 -228.961 18.078 31.408 1.00 87.21 C ANISOU 607 CE1 TYR A 74 12008 8656 12471 -244 -312 -944 C ATOM 608 CE2 TYR A 74 -228.993 18.835 29.139 1.00 89.19 C ANISOU 608 CE2 TYR A 74 12532 9064 12293 -459 -139 -1206 C ATOM 609 CZ TYR A 74 -228.767 17.838 30.064 1.00 93.42 C ANISOU 609 CZ TYR A 74 12954 9413 13127 -349 -168 -1175 C ATOM 610 OH TYR A 74 -228.347 16.596 29.643 1.00 95.60 O ANISOU 610 OH TYR A 74 13287 9466 13569 -351 -51 -1377 O ATOM 611 N ILE A 75 -231.380 23.983 33.164 1.00 83.80 N ANISOU 611 N ILE A 75 11334 9106 11398 -243 -744 -176 N ATOM 612 CA ILE A 75 -231.611 25.406 33.395 1.00 75.69 C ANISOU 612 CA ILE A 75 10256 8231 10274 -220 -785 -58 C ATOM 613 C ILE A 75 -231.214 25.807 34.810 1.00 73.85 C ANISOU 613 C ILE A 75 9878 8011 10170 -98 -790 56 C ATOM 614 O ILE A 75 -230.889 26.974 35.058 1.00 79.07 O ANISOU 614 O ILE A 75 10492 8763 10789 -51 -771 110 O ATOM 615 CB ILE A 75 -233.086 25.760 33.094 1.00 73.39 C ANISOU 615 CB ILE A 75 9987 8028 9869 -321 -935 36 C ATOM 616 CG1 ILE A 75 -233.281 27.277 33.056 1.00 65.04 C ANISOU 616 CG1 ILE A 75 8894 7103 8718 -303 -968 135 C ATOM 617 CG2 ILE A 75 -234.012 25.124 34.121 1.00 73.62 C ANISOU 617 CG2 ILE A 75 9926 8029 10020 -318 -1033 139 C ATOM 618 CD1 ILE A 75 -232.483 27.963 31.973 1.00 71.28 C ANISOU 618 CD1 ILE A 75 9789 7929 9364 -336 -881 56 C ATOM 619 N LEU A 76 -231.232 24.860 35.751 1.00 74.50 N ANISOU 619 N LEU A 76 9904 8001 10403 -59 -823 96 N ATOM 620 CA LEU A 76 -230.772 25.149 37.106 1.00 69.87 C ANISOU 620 CA LEU A 76 9207 7425 9917 36 -837 202 C ATOM 621 C LEU A 76 -229.260 25.329 37.148 1.00 74.62 C ANISOU 621 C LEU A 76 9766 7980 10607 128 -739 136 C ATOM 622 O LEU A 76 -228.751 26.179 37.888 1.00 81.48 O ANISOU 622 O LEU A 76 10561 8913 11486 190 -740 204 O ATOM 623 CB LEU A 76 -231.213 24.037 38.058 1.00 75.56 C ANISOU 623 CB LEU A 76 9898 8055 10758 30 -911 280 C ATOM 624 CG LEU A 76 -232.715 23.953 38.336 1.00 78.29 C ANISOU 624 CG LEU A 76 10242 8460 11046 -59 -1002 373 C ATOM 625 CD1 LEU A 76 -233.020 22.781 39.252 1.00 81.10 C ANISOU 625 CD1 LEU A 76 10582 8712 11521 -79 -1058 451 C ATOM 626 CD2 LEU A 76 -233.214 25.255 38.942 1.00 76.38 C ANISOU 626 CD2 LEU A 76 9933 8368 10720 -42 -1018 471 C ATOM 627 N LEU A 77 -228.522 24.535 36.368 1.00 73.42 N ANISOU 627 N LEU A 77 9654 7712 10532 135 -649 -4 N ATOM 628 CA LEU A 77 -227.085 24.758 36.251 1.00 67.75 C ANISOU 628 CA LEU A 77 8874 6951 9916 217 -534 -84 C ATOM 629 C LEU A 77 -226.794 26.120 35.637 1.00 70.12 C ANISOU 629 C LEU A 77 9192 7385 10064 198 -462 -107 C ATOM 630 O LEU A 77 -225.838 26.798 36.034 1.00 82.04 O ANISOU 630 O LEU A 77 10614 8921 11637 265 -417 -91 O ATOM 631 CB LEU A 77 -226.447 23.649 35.418 1.00 64.81 C ANISOU 631 CB LEU A 77 8540 6421 9663 220 -420 -257 C ATOM 632 CG LEU A 77 -226.558 22.232 35.975 1.00 56.72 C ANISOU 632 CG LEU A 77 7494 5222 8837 250 -484 -244 C ATOM 633 CD1 LEU A 77 -226.002 21.245 34.968 1.00 58.61 C ANISOU 633 CD1 LEU A 77 7786 5299 9184 244 -344 -450 C ATOM 634 CD2 LEU A 77 -225.831 22.116 37.307 1.00 46.96 C ANISOU 634 CD2 LEU A 77 6116 3929 7799 361 -562 -114 C ATOM 635 N ASN A 78 -227.611 26.537 34.665 1.00 64.05 N ANISOU 635 N ASN A 78 8539 6697 9100 96 -464 -133 N ATOM 636 CA ASN A 78 -227.466 27.868 34.085 1.00 57.36 C ANISOU 636 CA ASN A 78 7724 5971 8099 64 -421 -124 C ATOM 637 C ASN A 78 -227.673 28.947 35.140 1.00 63.48 C ANISOU 637 C ASN A 78 8406 6836 8877 118 -505 24 C ATOM 638 O ASN A 78 -227.002 29.986 35.118 1.00 77.92 O ANISOU 638 O ASN A 78 10204 8721 10681 142 -451 34 O ATOM 639 CB ASN A 78 -228.459 28.041 32.933 1.00 67.53 C ANISOU 639 CB ASN A 78 9158 7320 9180 -66 -460 -144 C ATOM 640 CG ASN A 78 -228.182 29.278 32.100 1.00 77.35 C ANISOU 640 CG ASN A 78 10468 8663 10261 -119 -405 -144 C ATOM 641 OD1 ASN A 78 -227.050 29.521 31.681 1.00 80.45 O ANISOU 641 OD1 ASN A 78 10862 9044 10662 -108 -255 -235 O ATOM 642 ND2 ASN A 78 -229.222 30.069 31.854 1.00 77.10 N ANISOU 642 ND2 ASN A 78 10481 8721 10094 -181 -529 -35 N ATOM 643 N LEU A 79 -228.591 28.712 36.078 1.00 62.14 N ANISOU 643 N LEU A 79 8196 6676 8738 129 -625 133 N ATOM 644 CA LEU A 79 -228.822 29.673 37.151 1.00 62.17 C ANISOU 644 CA LEU A 79 8121 6757 8743 173 -683 251 C ATOM 645 C LEU A 79 -227.600 29.794 38.052 1.00 63.26 C ANISOU 645 C LEU A 79 8169 6866 9002 257 -650 259 C ATOM 646 O LEU A 79 -227.195 30.902 38.424 1.00 61.21 O ANISOU 646 O LEU A 79 7868 6670 8719 284 -638 293 O ATOM 647 CB LEU A 79 -230.050 29.261 37.962 1.00 47.76 C ANISOU 647 CB LEU A 79 6274 4945 6928 152 -787 348 C ATOM 648 CG LEU A 79 -230.360 30.094 39.205 1.00 55.31 C ANISOU 648 CG LEU A 79 7156 5972 7886 188 -824 451 C ATOM 649 CD1 LEU A 79 -230.707 31.525 38.824 1.00 64.95 C ANISOU 649 CD1 LEU A 79 8376 7281 9019 182 -817 471 C ATOM 650 CD2 LEU A 79 -231.489 29.454 39.989 1.00 54.78 C ANISOU 650 CD2 LEU A 79 7067 5906 7840 152 -892 529 C ATOM 651 N ALA A 80 -226.999 28.658 38.417 1.00 66.96 N ANISOU 651 N ALA A 80 8601 7227 9614 296 -650 233 N ATOM 652 CA ALA A 80 -225.834 28.682 39.297 1.00 66.37 C ANISOU 652 CA ALA A 80 8427 7113 9677 372 -654 258 C ATOM 653 C ALA A 80 -224.649 29.361 38.625 1.00 71.90 C ANISOU 653 C ALA A 80 9090 7822 10408 398 -539 168 C ATOM 654 O ALA A 80 -223.897 30.099 39.273 1.00 73.02 O ANISOU 654 O ALA A 80 9153 7998 10595 435 -552 207 O ATOM 655 CB ALA A 80 -225.468 27.260 39.723 1.00 65.21 C ANISOU 655 CB ALA A 80 8245 6824 9707 411 -694 260 C ATOM 656 N VAL A 81 -224.465 29.121 37.325 1.00 65.18 N ANISOU 656 N VAL A 81 8299 6942 9523 363 -422 44 N ATOM 657 CA VAL A 81 -223.404 29.802 36.590 1.00 66.41 C ANISOU 657 CA VAL A 81 8429 7116 9686 363 -283 -46 C ATOM 658 C VAL A 81 -223.672 31.300 36.540 1.00 71.68 C ANISOU 658 C VAL A 81 9126 7910 10199 324 -296 19 C ATOM 659 O VAL A 81 -222.755 32.116 36.697 1.00 72.15 O ANISOU 659 O VAL A 81 9115 7996 10304 345 -246 18 O ATOM 660 CB VAL A 81 -223.261 29.197 35.181 1.00 56.46 C ANISOU 660 CB VAL A 81 7261 5807 8385 307 -137 -202 C ATOM 661 CG1 VAL A 81 -222.257 29.990 34.357 1.00 56.51 C ANISOU 661 CG1 VAL A 81 7258 5851 8363 281 30 -292 C ATOM 662 CG2 VAL A 81 -222.840 27.737 35.277 1.00 49.50 C ANISOU 662 CG2 VAL A 81 6331 4769 7706 362 -108 -285 C ATOM 663 N ALA A 82 -224.935 31.686 36.340 1.00 72.61 N ANISOU 663 N ALA A 82 9337 8095 10157 268 -370 81 N ATOM 664 CA ALA A 82 -225.278 33.104 36.294 1.00 70.89 C ANISOU 664 CA ALA A 82 9142 7971 9821 239 -393 150 C ATOM 665 C ALA A 82 -224.954 33.796 37.612 1.00 56.99 C ANISOU 665 C ALA A 82 7283 6236 8136 299 -453 228 C ATOM 666 O ALA A 82 -224.420 34.912 37.622 1.00 63.39 O ANISOU 666 O ALA A 82 8072 7084 8930 296 -419 239 O ATOM 667 CB ALA A 82 -226.756 33.275 35.951 1.00 74.80 C ANISOU 667 CB ALA A 82 9723 8514 10185 183 -485 213 C ATOM 668 N ASP A 83 -225.268 33.148 38.736 1.00 51.56 N ANISOU 668 N ASP A 83 6548 5524 7518 338 -542 284 N ATOM 669 CA ASP A 83 -224.959 33.739 40.032 1.00 67.47 C ANISOU 669 CA ASP A 83 8494 7567 9573 372 -603 351 C ATOM 670 C ASP A 83 -223.458 33.862 40.247 1.00 70.16 C ANISOU 670 C ASP A 83 8745 7874 10038 408 -566 315 C ATOM 671 O ASP A 83 -223.005 34.795 40.918 1.00 73.63 O ANISOU 671 O ASP A 83 9143 8352 10481 411 -591 346 O ATOM 672 CB ASP A 83 -225.592 32.917 41.153 1.00 79.88 C ANISOU 672 CB ASP A 83 10056 9123 11170 382 -701 423 C ATOM 673 CG ASP A 83 -227.107 32.909 41.086 1.00 87.86 C ANISOU 673 CG ASP A 83 11125 10176 12082 342 -733 464 C ATOM 674 OD1 ASP A 83 -227.672 33.660 40.261 1.00 89.54 O ANISOU 674 OD1 ASP A 83 11377 10429 12213 316 -705 451 O ATOM 675 OD2 ASP A 83 -227.734 32.152 41.856 1.00 87.52 O ANISOU 675 OD2 ASP A 83 11082 10120 12051 332 -793 520 O ATOM 676 N LEU A 84 -222.673 32.938 39.689 1.00 68.71 N ANISOU 676 N LEU A 84 8521 7612 9974 433 -505 242 N ATOM 677 CA LEU A 84 -221.223 33.072 39.774 1.00 60.74 C ANISOU 677 CA LEU A 84 7395 6564 9119 469 -457 201 C ATOM 678 C LEU A 84 -220.725 34.263 38.966 1.00 65.71 C ANISOU 678 C LEU A 84 8033 7248 9686 427 -342 151 C ATOM 679 O LEU A 84 -219.721 34.883 39.337 1.00 73.31 O ANISOU 679 O LEU A 84 8897 8215 10740 437 -333 152 O ATOM 680 CB LEU A 84 -220.547 31.783 39.312 1.00 49.57 C ANISOU 680 CB LEU A 84 5921 5035 7881 514 -395 120 C ATOM 681 CG LEU A 84 -220.705 30.596 40.263 1.00 47.67 C ANISOU 681 CG LEU A 84 5642 4709 7763 562 -527 189 C ATOM 682 CD1 LEU A 84 -219.944 29.397 39.736 1.00 59.33 C ANISOU 682 CD1 LEU A 84 7044 6042 9456 618 -452 96 C ATOM 683 CD2 LEU A 84 -220.234 30.960 41.667 1.00 50.55 C ANISOU 683 CD2 LEU A 84 5925 5094 8188 584 -675 305 C ATOM 684 N PHE A 85 -221.406 34.598 37.865 1.00 62.07 N ANISOU 684 N PHE A 85 7690 6825 9070 368 -266 117 N ATOM 685 CA PHE A 85 -221.110 35.847 37.168 1.00 62.39 C ANISOU 685 CA PHE A 85 7765 6919 9020 310 -182 105 C ATOM 686 C PHE A 85 -221.399 37.045 38.062 1.00 66.79 C ANISOU 686 C PHE A 85 8314 7529 9536 311 -277 196 C ATOM 687 O PHE A 85 -220.614 38.000 38.113 1.00 57.72 O ANISOU 687 O PHE A 85 7118 6394 8419 291 -238 194 O ATOM 688 CB PHE A 85 -221.919 35.940 35.873 1.00 62.36 C ANISOU 688 CB PHE A 85 7911 6945 8837 233 -125 81 C ATOM 689 CG PHE A 85 -221.301 35.213 34.710 1.00 71.82 C ANISOU 689 CG PHE A 85 9143 8106 10040 194 34 -45 C ATOM 690 CD1 PHE A 85 -221.130 33.839 34.741 1.00 85.50 C ANISOU 690 CD1 PHE A 85 10839 9759 11886 238 60 -122 C ATOM 691 CD2 PHE A 85 -220.917 35.905 33.573 1.00 71.75 C ANISOU 691 CD2 PHE A 85 9213 8134 9916 102 168 -89 C ATOM 692 CE1 PHE A 85 -220.571 33.171 33.668 1.00 78.07 C ANISOU 692 CE1 PHE A 85 9933 8773 10958 200 231 -265 C ATOM 693 CE2 PHE A 85 -220.358 35.241 32.497 1.00 68.87 C ANISOU 693 CE2 PHE A 85 8893 7740 9534 49 343 -224 C ATOM 694 CZ PHE A 85 -220.186 33.873 32.545 1.00 66.21 C ANISOU 694 CZ PHE A 85 8514 7321 9323 102 383 -324 C ATOM 695 N MET A 86 -222.526 37.012 38.776 1.00 67.81 N ANISOU 695 N MET A 86 8483 7680 9602 326 -390 266 N ATOM 696 CA MET A 86 -222.832 38.077 39.725 1.00 63.41 C ANISOU 696 CA MET A 86 7918 7160 9016 328 -462 329 C ATOM 697 C MET A 86 -221.826 38.107 40.864 1.00 73.98 C ANISOU 697 C MET A 86 9156 8486 10466 354 -511 334 C ATOM 698 O MET A 86 -221.454 39.181 41.349 1.00 78.94 O ANISOU 698 O MET A 86 9766 9134 11093 335 -525 346 O ATOM 699 CB MET A 86 -224.241 37.897 40.279 1.00 61.67 C ANISOU 699 CB MET A 86 7746 6962 8723 336 -544 386 C ATOM 700 CG MET A 86 -225.327 38.010 39.240 1.00 75.98 C ANISOU 700 CG MET A 86 9642 8789 10438 305 -534 400 C ATOM 701 SD MET A 86 -226.957 37.676 39.927 1.00 74.92 S ANISOU 701 SD MET A 86 9522 8677 10270 316 -622 462 S ATOM 702 CE MET A 86 -226.968 38.798 41.323 1.00 77.96 C ANISOU 702 CE MET A 86 9865 9084 10672 338 -641 486 C ATOM 703 N VAL A 87 -221.381 36.934 41.313 1.00 80.13 N ANISOU 703 N VAL A 87 9873 9225 11349 391 -553 332 N ATOM 704 CA VAL A 87 -220.463 36.872 42.444 1.00 79.95 C ANISOU 704 CA VAL A 87 9755 9188 11434 408 -642 362 C ATOM 705 C VAL A 87 -219.092 37.403 42.050 1.00 82.87 C ANISOU 705 C VAL A 87 10022 9540 11925 401 -577 313 C ATOM 706 O VAL A 87 -218.485 38.200 42.773 1.00 82.74 O ANISOU 706 O VAL A 87 9956 9543 11937 377 -635 333 O ATOM 707 CB VAL A 87 -220.378 35.435 42.983 1.00 79.48 C ANISOU 707 CB VAL A 87 9655 9070 11474 450 -725 396 C ATOM 708 CG1 VAL A 87 -219.120 35.258 43.817 1.00 84.80 C ANISOU 708 CG1 VAL A 87 10203 9708 12310 469 -820 426 C ATOM 709 CG2 VAL A 87 -221.611 35.112 43.809 1.00 80.05 C ANISOU 709 CG2 VAL A 87 9816 9173 11425 433 -812 468 C ATOM 710 N PHE A 88 -218.583 36.974 40.898 1.00 80.53 N ANISOU 710 N PHE A 88 9692 9206 11700 410 -448 239 N ATOM 711 CA PHE A 88 -217.228 37.339 40.505 1.00 73.25 C ANISOU 711 CA PHE A 88 8646 8261 10923 400 -360 184 C ATOM 712 C PHE A 88 -217.189 38.594 39.646 1.00 70.66 C ANISOU 712 C PHE A 88 8379 7979 10489 328 -242 156 C ATOM 713 O PHE A 88 -216.298 39.432 39.817 1.00 86.16 O ANISOU 713 O PHE A 88 10262 9950 12526 295 -225 152 O ATOM 714 CB PHE A 88 -216.569 36.178 39.759 1.00 64.82 C ANISOU 714 CB PHE A 88 7494 7118 10017 444 -252 101 C ATOM 715 CG PHE A 88 -216.257 35.002 40.634 1.00 68.71 C ANISOU 715 CG PHE A 88 7885 7535 10688 520 -378 138 C ATOM 716 CD1 PHE A 88 -215.203 35.055 41.528 1.00 65.02 C ANISOU 716 CD1 PHE A 88 7256 7039 10411 545 -486 183 C ATOM 717 CD2 PHE A 88 -217.013 33.843 40.562 1.00 76.93 C ANISOU 717 CD2 PHE A 88 8992 8525 11714 556 -405 141 C ATOM 718 CE1 PHE A 88 -214.907 33.979 42.334 1.00 74.02 C ANISOU 718 CE1 PHE A 88 8305 8097 11722 609 -630 242 C ATOM 719 CE2 PHE A 88 -216.720 32.760 41.367 1.00 83.69 C ANISOU 719 CE2 PHE A 88 9762 9294 12745 621 -532 193 C ATOM 720 CZ PHE A 88 -215.663 32.829 42.254 1.00 86.52 C ANISOU 720 CZ PHE A 88 9961 9620 13291 649 -650 251 C ATOM 721 N GLY A 89 -218.135 38.742 38.719 1.00 55.85 N ANISOU 721 N GLY A 89 6646 6128 8445 294 -173 148 N ATOM 722 CA GLY A 89 -218.144 39.923 37.877 1.00 65.32 C ANISOU 722 CA GLY A 89 7920 7360 9537 217 -82 147 C ATOM 723 C GLY A 89 -218.618 41.167 38.595 1.00 72.64 C ANISOU 723 C GLY A 89 8890 8313 10398 198 -179 220 C ATOM 724 O GLY A 89 -218.155 42.270 38.296 1.00 67.31 O ANISOU 724 O GLY A 89 8219 7641 9716 139 -128 226 O ATOM 725 N GLY A 90 -219.527 41.015 39.555 1.00 70.64 N ANISOU 725 N GLY A 90 8669 8070 10101 239 -306 268 N ATOM 726 CA GLY A 90 -220.094 42.168 40.223 1.00 63.81 C ANISOU 726 CA GLY A 90 7851 7218 9175 224 -374 314 C ATOM 727 C GLY A 90 -219.660 42.340 41.663 1.00 65.86 C ANISOU 727 C GLY A 90 8045 7481 9497 235 -476 321 C ATOM 728 O GLY A 90 -219.099 43.378 42.025 1.00 82.81 O ANISOU 728 O GLY A 90 10171 9620 11673 194 -484 314 O ATOM 729 N PHE A 91 -219.915 41.329 42.496 1.00 52.39 N ANISOU 729 N PHE A 91 6318 5783 7803 275 -561 338 N ATOM 730 CA PHE A 91 -219.681 41.485 43.929 1.00 62.36 C ANISOU 730 CA PHE A 91 7558 7060 9076 263 -677 359 C ATOM 731 C PHE A 91 -218.196 41.626 44.237 1.00 67.72 C ANISOU 731 C PHE A 91 8116 7722 9891 239 -714 345 C ATOM 732 O PHE A 91 -217.809 42.412 45.109 1.00 74.12 O ANISOU 732 O PHE A 91 8922 8544 10696 190 -786 345 O ATOM 733 CB PHE A 91 -220.266 40.299 44.700 1.00 72.45 C ANISOU 733 CB PHE A 91 8853 8349 10326 294 -764 401 C ATOM 734 CG PHE A 91 -221.729 40.043 44.434 1.00 84.50 C ANISOU 734 CG PHE A 91 10472 9891 11742 312 -732 417 C ATOM 735 CD1 PHE A 91 -222.550 41.022 43.897 1.00 86.27 C ANISOU 735 CD1 PHE A 91 10760 10124 11895 302 -668 404 C ATOM 736 CD2 PHE A 91 -222.283 38.811 44.741 1.00 90.88 C ANISOU 736 CD2 PHE A 91 11293 10697 12541 335 -779 454 C ATOM 737 CE1 PHE A 91 -223.888 40.768 43.660 1.00 84.80 C ANISOU 737 CE1 PHE A 91 10631 9950 11641 319 -655 426 C ATOM 738 CE2 PHE A 91 -223.618 38.554 44.510 1.00 86.94 C ANISOU 738 CE2 PHE A 91 10860 10214 11960 341 -755 469 C ATOM 739 CZ PHE A 91 -224.422 39.533 43.970 1.00 81.98 C ANISOU 739 CZ PHE A 91 10277 9601 11271 335 -695 455 C ATOM 740 N THR A 92 -217.352 40.872 43.530 1.00 75.40 N ANISOU 740 N THR A 92 8986 8663 11000 267 -662 324 N ATOM 741 CA THR A 92 -215.921 40.882 43.818 1.00 64.62 C ANISOU 741 CA THR A 92 7467 7275 9813 253 -700 315 C ATOM 742 C THR A 92 -215.293 42.222 43.460 1.00 60.03 C ANISOU 742 C THR A 92 6862 6697 9249 183 -630 281 C ATOM 743 O THR A 92 -214.573 42.817 44.271 1.00 64.36 O ANISOU 743 O THR A 92 7348 7249 9857 135 -726 290 O ATOM 744 CB THR A 92 -215.234 39.740 43.069 1.00 56.23 C ANISOU 744 CB THR A 92 6284 6161 8921 309 -627 282 C ATOM 745 OG1 THR A 92 -215.553 38.496 43.703 1.00 64.24 O ANISOU 745 OG1 THR A 92 7291 7147 9971 368 -740 330 O ATOM 746 CG2 THR A 92 -213.727 39.929 43.056 1.00 51.88 C ANISOU 746 CG2 THR A 92 5543 5580 8591 294 -618 257 C ATOM 747 N THR A 93 -215.556 42.717 42.248 1.00 54.29 N ANISOU 747 N THR A 93 6194 5969 8464 163 -474 249 N ATOM 748 CA THR A 93 -214.996 44.001 41.837 1.00 68.17 C ANISOU 748 CA THR A 93 7945 7720 10236 85 -402 232 C ATOM 749 C THR A 93 -215.509 45.133 42.718 1.00 72.47 C ANISOU 749 C THR A 93 8580 8269 10686 44 -495 253 C ATOM 750 O THR A 93 -214.757 46.055 43.059 1.00 75.34 O ANISOU 750 O THR A 93 8897 8617 11112 -24 -518 241 O ATOM 751 CB THR A 93 -215.333 44.279 40.376 1.00 73.99 C ANISOU 751 CB THR A 93 8765 8455 10891 58 -233 217 C ATOM 752 OG1 THR A 93 -216.716 44.636 40.276 1.00 86.72 O ANISOU 752 OG1 THR A 93 10539 10076 12333 69 -261 256 O ATOM 753 CG2 THR A 93 -215.078 43.045 39.530 1.00 42.53 C ANISOU 753 CG2 THR A 93 4732 4466 6960 97 -127 172 C ATOM 754 N THR A 94 -216.790 45.082 43.095 1.00 63.99 N ANISOU 754 N THR A 94 7631 7209 9473 79 -540 275 N ATOM 755 CA THR A 94 -217.348 46.111 43.965 1.00 59.51 C ANISOU 755 CA THR A 94 7150 6635 8827 47 -602 271 C ATOM 756 C THR A 94 -216.675 46.103 45.331 1.00 61.53 C ANISOU 756 C THR A 94 7354 6905 9117 9 -738 260 C ATOM 757 O THR A 94 -216.364 47.165 45.882 1.00 71.46 O ANISOU 757 O THR A 94 8634 8144 10374 -60 -772 230 O ATOM 758 CB THR A 94 -218.857 45.917 44.111 1.00 55.60 C ANISOU 758 CB THR A 94 6769 6152 8206 98 -606 289 C ATOM 759 OG1 THR A 94 -219.477 46.022 42.824 1.00 71.56 O ANISOU 759 OG1 THR A 94 8842 8157 10193 117 -511 311 O ATOM 760 CG2 THR A 94 -219.443 46.973 45.037 1.00 43.31 C ANISOU 760 CG2 THR A 94 5292 4577 6588 69 -639 261 C ATOM 761 N LEU A 95 -216.440 44.914 45.891 1.00 59.37 N ANISOU 761 N LEU A 95 7022 6660 8875 42 -830 289 N ATOM 762 CA LEU A 95 -215.717 44.819 47.156 1.00 60.40 C ANISOU 762 CA LEU A 95 7106 6807 9036 -9 -991 302 C ATOM 763 C LEU A 95 -214.343 45.470 47.054 1.00 64.12 C ANISOU 763 C LEU A 95 7450 7255 9659 -74 -1012 282 C ATOM 764 O LEU A 95 -213.857 46.072 48.019 1.00 69.55 O ANISOU 764 O LEU A 95 8139 7949 10338 -156 -1133 272 O ATOM 765 CB LEU A 95 -215.589 43.353 47.573 1.00 49.36 C ANISOU 765 CB LEU A 95 5649 5423 7684 43 -1094 362 C ATOM 766 CG LEU A 95 -214.689 43.021 48.767 1.00 46.50 C ANISOU 766 CG LEU A 95 5216 5071 7382 -9 -1297 410 C ATOM 767 CD1 LEU A 95 -215.177 43.706 50.030 1.00 45.88 C ANISOU 767 CD1 LEU A 95 5283 5035 7113 -101 -1395 400 C ATOM 768 CD2 LEU A 95 -214.613 41.518 48.975 1.00 56.90 C ANISOU 768 CD2 LEU A 95 6470 6373 8775 56 -1390 487 C ATOM 769 N TYR A 96 -213.707 45.371 45.887 1.00 50.34 N ANISOU 769 N TYR A 96 5595 5483 8048 -52 -890 270 N ATOM 770 CA TYR A 96 -212.399 45.987 45.700 1.00 53.62 C ANISOU 770 CA TYR A 96 5868 5875 8628 -121 -883 250 C ATOM 771 C TYR A 96 -212.516 47.498 45.520 1.00 60.99 C ANISOU 771 C TYR A 96 6890 6784 9499 -206 -819 214 C ATOM 772 O TYR A 96 -211.766 48.264 46.137 1.00 59.59 O ANISOU 772 O TYR A 96 6666 6593 9382 -296 -903 197 O ATOM 773 CB TYR A 96 -211.688 45.348 44.506 1.00 45.59 C ANISOU 773 CB TYR A 96 4706 4839 7776 -79 -738 236 C ATOM 774 CG TYR A 96 -210.317 45.920 44.226 1.00 51.68 C ANISOU 774 CG TYR A 96 5302 5587 8745 -153 -699 212 C ATOM 775 CD1 TYR A 96 -209.207 45.503 44.949 1.00 52.85 C ANISOU 775 CD1 TYR A 96 5256 5728 9098 -164 -844 231 C ATOM 776 CD2 TYR A 96 -210.133 46.877 43.239 1.00 56.76 C ANISOU 776 CD2 TYR A 96 5970 6215 9382 -220 -527 181 C ATOM 777 CE1 TYR A 96 -207.952 46.024 44.696 1.00 52.41 C ANISOU 777 CE1 TYR A 96 5014 5652 9250 -237 -807 209 C ATOM 778 CE2 TYR A 96 -208.884 47.403 42.977 1.00 66.74 C ANISOU 778 CE2 TYR A 96 7067 7460 10832 -301 -475 160 C ATOM 779 CZ TYR A 96 -207.796 46.974 43.708 1.00 65.56 C ANISOU 779 CZ TYR A 96 6705 7306 10900 -308 -611 168 C ATOM 780 OH TYR A 96 -206.550 47.498 43.449 1.00 78.14 O ANISOU 780 OH TYR A 96 8105 8878 12705 -393 -559 147 O ATOM 781 N THR A 97 -213.458 47.946 44.683 1.00 60.41 N ANISOU 781 N THR A 97 6946 6695 9314 -183 -686 209 N ATOM 782 CA THR A 97 -213.615 49.378 44.452 1.00 44.28 C ANISOU 782 CA THR A 97 4989 4603 7235 -256 -630 190 C ATOM 783 C THR A 97 -214.195 50.086 45.669 1.00 48.09 C ANISOU 783 C THR A 97 5584 5070 7617 -288 -738 157 C ATOM 784 O THR A 97 -213.866 51.253 45.916 1.00 49.46 O ANISOU 784 O THR A 97 5785 5190 7815 -373 -746 122 O ATOM 785 CB THR A 97 -214.502 49.628 43.235 1.00 44.26 C ANISOU 785 CB THR A 97 5093 4577 7148 -223 -488 215 C ATOM 786 OG1 THR A 97 -215.788 49.034 43.460 1.00 54.03 O ANISOU 786 OG1 THR A 97 6430 5838 8261 -137 -516 230 O ATOM 787 CG2 THR A 97 -213.878 49.024 41.989 1.00 43.86 C ANISOU 787 CG2 THR A 97 4957 4543 7166 -221 -356 227 C ATOM 788 N SER A 98 -215.064 49.411 46.427 1.00 49.18 N ANISOU 788 N SER A 98 5796 5249 7642 -231 -806 160 N ATOM 789 CA SER A 98 -215.667 50.045 47.595 1.00 67.64 C ANISOU 789 CA SER A 98 8254 7579 9868 -271 -875 109 C ATOM 790 C SER A 98 -214.608 50.429 48.622 1.00 60.94 C ANISOU 790 C SER A 98 7361 6736 9056 -382 -1012 75 C ATOM 791 O SER A 98 -214.722 51.467 49.284 1.00 58.88 O ANISOU 791 O SER A 98 7194 6435 8744 -460 -1034 6 O ATOM 792 CB SER A 98 -216.711 49.113 48.217 1.00 79.02 C ANISOU 792 CB SER A 98 9769 9075 11179 -207 -908 123 C ATOM 793 OG SER A 98 -216.737 49.222 49.627 1.00 94.94 O ANISOU 793 OG SER A 98 11856 11121 13094 -276 -1020 83 O ATOM 794 N LEU A 99 -213.562 49.613 48.759 1.00 61.69 N ANISOU 794 N LEU A 99 7312 6871 9257 -394 -1113 121 N ATOM 795 CA LEU A 99 -212.506 49.902 49.719 1.00 69.36 C ANISOU 795 CA LEU A 99 8222 7852 10280 -507 -1281 107 C ATOM 796 C LEU A 99 -211.586 51.035 49.274 1.00 70.55 C ANISOU 796 C LEU A 99 8297 7942 10566 -599 -1242 71 C ATOM 797 O LEU A 99 -210.792 51.524 50.086 1.00 56.36 O ANISOU 797 O LEU A 99 6470 6142 8804 -716 -1382 45 O ATOM 798 CB LEU A 99 -211.697 48.633 49.996 1.00 70.37 C ANISOU 798 CB LEU A 99 8194 8026 10518 -481 -1421 185 C ATOM 799 CG LEU A 99 -212.487 47.584 50.782 1.00 61.64 C ANISOU 799 CG LEU A 99 7181 6974 9266 -433 -1513 231 C ATOM 800 CD1 LEU A 99 -211.619 46.379 51.091 1.00 74.61 C ANISOU 800 CD1 LEU A 99 8665 8636 11049 -409 -1678 323 C ATOM 801 CD2 LEU A 99 -213.050 48.189 52.063 1.00 48.21 C ANISOU 801 CD2 LEU A 99 5668 5300 7349 -533 -1602 180 C ATOM 802 N HIS A 100 -211.670 51.459 48.014 1.00 73.56 N ANISOU 802 N HIS A 100 8657 8276 11015 -565 -1065 75 N ATOM 803 CA HIS A 100 -211.016 52.682 47.570 1.00 76.51 C ANISOU 803 CA HIS A 100 9003 8579 11490 -665 -1004 45 C ATOM 804 C HIS A 100 -211.909 53.904 47.721 1.00 82.09 C ANISOU 804 C HIS A 100 9896 9206 12088 -695 -948 -12 C ATOM 805 O HIS A 100 -211.400 55.014 47.914 1.00 86.71 O ANISOU 805 O HIS A 100 10495 9720 12730 -806 -964 -57 O ATOM 806 CB HIS A 100 -210.590 52.561 46.105 1.00 76.39 C ANISOU 806 CB HIS A 100 8881 8549 11595 -638 -834 88 C ATOM 807 CG HIS A 100 -209.482 51.583 45.870 1.00 81.26 C ANISOU 807 CG HIS A 100 9278 9214 12385 -624 -854 119 C ATOM 808 ND1 HIS A 100 -209.678 50.219 45.880 1.00 78.83 N ANISOU 808 ND1 HIS A 100 8915 8959 12078 -514 -880 150 N ATOM 809 CD2 HIS A 100 -208.167 51.772 45.604 1.00 86.74 C ANISOU 809 CD2 HIS A 100 9777 9896 13284 -703 -844 119 C ATOM 810 CE1 HIS A 100 -208.532 49.609 45.638 1.00 84.31 C ANISOU 810 CE1 HIS A 100 9389 9664 12982 -516 -885 164 C ATOM 811 NE2 HIS A 100 -207.598 50.528 45.467 1.00 86.06 N ANISOU 811 NE2 HIS A 100 9513 9852 13333 -629 -860 145 N ATOM 812 N GLY A 101 -213.225 53.723 47.644 1.00 73.49 N ANISOU 812 N GLY A 101 8941 8116 10867 -599 -884 -13 N ATOM 813 CA GLY A 101 -214.155 54.828 47.641 1.00 63.66 C ANISOU 813 CA GLY A 101 7846 6776 9564 -599 -812 -62 C ATOM 814 C GLY A 101 -214.605 55.273 46.269 1.00 54.16 C ANISOU 814 C GLY A 101 6666 5505 8407 -552 -670 -1 C ATOM 815 O GLY A 101 -215.426 56.195 46.174 1.00 60.98 O ANISOU 815 O GLY A 101 7642 6269 9257 -538 -619 -23 O ATOM 816 N TYR A 102 -214.097 54.652 45.206 1.00 52.53 N ANISOU 816 N TYR A 102 6360 5342 8256 -533 -606 74 N ATOM 817 CA TYR A 102 -214.476 55.012 43.847 1.00 56.38 C ANISOU 817 CA TYR A 102 6890 5780 8753 -514 -481 145 C ATOM 818 C TYR A 102 -214.121 53.860 42.919 1.00 63.42 C ANISOU 818 C TYR A 102 7690 6758 9647 -473 -413 199 C ATOM 819 O TYR A 102 -213.382 52.940 43.285 1.00 70.50 O ANISOU 819 O TYR A 102 8463 7731 10595 -465 -456 180 O ATOM 820 CB TYR A 102 -213.796 56.310 43.399 1.00 62.28 C ANISOU 820 CB TYR A 102 7643 6422 9598 -631 -435 155 C ATOM 821 CG TYR A 102 -212.294 56.225 43.202 1.00 65.71 C ANISOU 821 CG TYR A 102 7921 6890 10154 -736 -421 155 C ATOM 822 CD1 TYR A 102 -211.426 56.176 44.289 1.00 49.93 C ANISOU 822 CD1 TYR A 102 5827 4920 8226 -799 -540 90 C ATOM 823 CD2 TYR A 102 -211.743 56.223 41.926 1.00 56.07 C ANISOU 823 CD2 TYR A 102 6649 5673 8980 -783 -288 220 C ATOM 824 CE1 TYR A 102 -210.056 56.113 44.109 1.00 58.64 C ANISOU 824 CE1 TYR A 102 6755 6046 9478 -892 -535 94 C ATOM 825 CE2 TYR A 102 -210.375 56.159 41.736 1.00 50.48 C ANISOU 825 CE2 TYR A 102 5776 4993 8411 -880 -249 211 C ATOM 826 CZ TYR A 102 -209.535 56.107 42.830 1.00 63.79 C ANISOU 826 CZ TYR A 102 7337 6699 10200 -927 -377 150 C ATOM 827 OH TYR A 102 -208.171 56.042 42.644 1.00 67.62 O ANISOU 827 OH TYR A 102 7626 7206 10859 -1021 -347 145 O ATOM 828 N PHE A 103 -214.664 53.923 41.705 1.00 56.02 N ANISOU 828 N PHE A 103 6821 5803 8662 -452 -311 266 N ATOM 829 CA PHE A 103 -214.451 52.878 40.705 1.00 49.10 C ANISOU 829 CA PHE A 103 5893 5000 7761 -425 -221 299 C ATOM 830 C PHE A 103 -213.070 53.083 40.096 1.00 61.26 C ANISOU 830 C PHE A 103 7318 6544 9415 -532 -124 297 C ATOM 831 O PHE A 103 -212.886 53.850 39.153 1.00 77.84 O ANISOU 831 O PHE A 103 9471 8597 11508 -617 -23 345 O ATOM 832 CB PHE A 103 -215.543 52.915 39.645 1.00 51.80 C ANISOU 832 CB PHE A 103 6368 5325 7986 -390 -163 372 C ATOM 833 CG PHE A 103 -215.589 51.688 38.791 1.00 56.56 C ANISOU 833 CG PHE A 103 6953 6010 8528 -354 -89 383 C ATOM 834 CD1 PHE A 103 -216.253 50.555 39.227 1.00 55.79 C ANISOU 834 CD1 PHE A 103 6847 5969 8381 -250 -147 360 C ATOM 835 CD2 PHE A 103 -214.953 51.656 37.564 1.00 54.33 C ANISOU 835 CD2 PHE A 103 6669 5743 8232 -435 51 407 C ATOM 836 CE1 PHE A 103 -216.291 49.413 38.451 1.00 59.58 C ANISOU 836 CE1 PHE A 103 7315 6507 8814 -221 -77 356 C ATOM 837 CE2 PHE A 103 -214.987 50.516 36.782 1.00 64.80 C ANISOU 837 CE2 PHE A 103 7991 7137 9495 -410 136 391 C ATOM 838 CZ PHE A 103 -215.658 49.391 37.225 1.00 61.49 C ANISOU 838 CZ PHE A 103 7562 6761 9041 -299 67 363 C ATOM 839 N VAL A 104 -212.081 52.370 40.644 1.00 60.14 N ANISOU 839 N VAL A 104 7008 6455 9389 -531 -155 247 N ATOM 840 CA VAL A 104 -210.677 52.584 40.289 1.00 62.61 C ANISOU 840 CA VAL A 104 7163 6767 9859 -632 -74 231 C ATOM 841 C VAL A 104 -210.292 51.997 38.944 1.00 68.45 C ANISOU 841 C VAL A 104 7861 7543 10602 -650 122 239 C ATOM 842 O VAL A 104 -209.146 52.177 38.506 1.00 82.63 O ANISOU 842 O VAL A 104 9521 9341 12535 -741 234 220 O ATOM 843 CB VAL A 104 -209.743 51.988 41.361 1.00 57.86 C ANISOU 843 CB VAL A 104 6371 6200 9413 -621 -198 184 C ATOM 844 CG1 VAL A 104 -209.868 52.760 42.648 1.00 60.40 C ANISOU 844 CG1 VAL A 104 6742 6485 9722 -659 -376 163 C ATOM 845 CG2 VAL A 104 -210.071 50.520 41.583 1.00 57.31 C ANISOU 845 CG2 VAL A 104 6257 6192 9327 -493 -241 175 C ATOM 846 N PHE A 105 -211.200 51.298 38.275 1.00 63.34 N ANISOU 846 N PHE A 105 7326 6929 9812 -577 175 257 N ATOM 847 CA PHE A 105 -210.875 50.631 37.023 1.00 66.65 C ANISOU 847 CA PHE A 105 7728 7389 10207 -601 368 242 C ATOM 848 C PHE A 105 -211.121 51.496 35.794 1.00 77.08 C ANISOU 848 C PHE A 105 9207 8685 11393 -716 500 307 C ATOM 849 O PHE A 105 -210.903 51.022 34.675 1.00 72.19 O ANISOU 849 O PHE A 105 8613 8105 10709 -765 676 292 O ATOM 850 CB PHE A 105 -211.666 49.325 36.896 1.00 66.70 C ANISOU 850 CB PHE A 105 7778 7441 10124 -481 353 220 C ATOM 851 CG PHE A 105 -211.352 48.321 37.966 1.00 69.22 C ANISOU 851 CG PHE A 105 7944 7779 10579 -377 235 172 C ATOM 852 CD1 PHE A 105 -210.068 47.825 38.109 1.00 64.79 C ANISOU 852 CD1 PHE A 105 7161 7222 10235 -384 285 116 C ATOM 853 CD2 PHE A 105 -212.340 47.871 38.825 1.00 73.16 C ANISOU 853 CD2 PHE A 105 8514 8285 10998 -278 72 192 C ATOM 854 CE1 PHE A 105 -209.772 46.905 39.093 1.00 58.74 C ANISOU 854 CE1 PHE A 105 6254 6459 9606 -291 147 97 C ATOM 855 CE2 PHE A 105 -212.051 46.947 39.810 1.00 76.28 C ANISOU 855 CE2 PHE A 105 8787 8694 11503 -200 -48 169 C ATOM 856 CZ PHE A 105 -210.764 46.464 39.944 1.00 69.98 C ANISOU 856 CZ PHE A 105 7776 7892 10923 -205 -25 130 C ATOM 857 N GLY A 106 -211.566 52.739 35.967 1.00 94.38 N ANISOU 857 N GLY A 106 11515 10806 13540 -769 422 379 N ATOM 858 CA GLY A 106 -211.764 53.639 34.856 1.00 98.27 C ANISOU 858 CA GLY A 106 12162 11258 13920 -888 517 468 C ATOM 859 C GLY A 106 -212.980 53.287 34.023 1.00100.62 C ANISOU 859 C GLY A 106 12648 11574 14009 -852 511 534 C ATOM 860 O GLY A 106 -213.724 52.350 34.330 1.00105.99 O ANISOU 860 O GLY A 106 13337 12297 14638 -730 437 503 O ATOM 861 N PRO A 107 -213.203 54.038 32.942 1.00 98.56 N ANISOU 861 N PRO A 107 12546 11279 13623 -971 576 638 N ATOM 862 CA PRO A 107 -214.397 53.789 32.116 1.00 98.61 C ANISOU 862 CA PRO A 107 12742 11299 13426 -955 534 722 C ATOM 863 C PRO A 107 -214.382 52.446 31.407 1.00 99.05 C ANISOU 863 C PRO A 107 12805 11462 13368 -943 649 652 C ATOM 864 O PRO A 107 -215.452 51.868 31.182 1.00 95.08 O ANISOU 864 O PRO A 107 12404 10983 12739 -875 562 678 O ATOM 865 CB PRO A 107 -214.378 54.956 31.120 1.00 97.67 C ANISOU 865 CB PRO A 107 12782 11114 13213 -1118 577 862 C ATOM 866 CG PRO A 107 -212.950 55.383 31.069 1.00101.02 C ANISOU 866 CG PRO A 107 13090 11537 13755 -1244 738 816 C ATOM 867 CD PRO A 107 -212.416 55.180 32.452 1.00 99.54 C ANISOU 867 CD PRO A 107 12691 11343 13785 -1137 670 699 C ATOM 868 N THR A 108 -213.205 51.929 31.047 1.00103.43 N ANISOU 868 N THR A 108 13247 12072 13979 -1010 846 554 N ATOM 869 CA THR A 108 -213.140 50.626 30.390 1.00 98.39 C ANISOU 869 CA THR A 108 12611 11517 13255 -996 978 459 C ATOM 870 C THR A 108 -213.603 49.515 31.326 1.00 88.74 C ANISOU 870 C THR A 108 11285 10313 12118 -813 856 380 C ATOM 871 O THR A 108 -214.412 48.662 30.942 1.00 75.58 O ANISOU 871 O THR A 108 9714 8681 10320 -766 831 366 O ATOM 872 CB THR A 108 -211.719 50.356 29.890 1.00 97.07 C ANISOU 872 CB THR A 108 12311 11388 13183 -1096 1237 354 C ATOM 873 OG1 THR A 108 -211.410 51.246 28.808 1.00106.44 O ANISOU 873 OG1 THR A 108 13639 12574 14231 -1294 1379 433 O ATOM 874 CG2 THR A 108 -211.584 48.917 29.415 1.00 93.27 C ANISOU 874 CG2 THR A 108 11795 10970 12673 -1051 1380 218 C ATOM 875 N GLY A 109 -213.102 49.509 32.563 1.00 84.49 N ANISOU 875 N GLY A 109 10561 9751 11791 -723 771 334 N ATOM 876 CA GLY A 109 -213.577 48.545 33.538 1.00 80.54 C ANISOU 876 CA GLY A 109 9981 9261 11358 -565 634 286 C ATOM 877 C GLY A 109 -215.034 48.727 33.898 1.00 83.28 C ANISOU 877 C GLY A 109 10467 9590 11584 -491 451 366 C ATOM 878 O GLY A 109 -215.677 47.778 34.358 1.00 90.03 O ANISOU 878 O GLY A 109 11310 10467 12430 -384 367 337 O ATOM 879 N CYS A 110 -215.571 49.931 33.692 1.00 88.29 N ANISOU 879 N CYS A 110 11226 10175 12147 -549 389 469 N ATOM 880 CA CYS A 110 -216.987 50.170 33.943 1.00 85.67 C ANISOU 880 CA CYS A 110 11006 9812 11731 -478 228 547 C ATOM 881 C CYS A 110 -217.853 49.399 32.957 1.00 77.81 C ANISOU 881 C CYS A 110 10140 8863 10561 -483 235 575 C ATOM 882 O CYS A 110 -218.871 48.812 33.343 1.00 86.45 O ANISOU 882 O CYS A 110 11251 9968 11627 -386 122 581 O ATOM 883 CB CYS A 110 -217.280 51.667 33.869 1.00 85.53 C ANISOU 883 CB CYS A 110 11077 9704 11716 -538 167 652 C ATOM 884 SG CYS A 110 -218.879 52.170 34.534 1.00 84.50 S ANISOU 884 SG CYS A 110 11016 9502 11586 -426 -29 724 S ATOM 885 N ASN A 111 -217.466 49.386 31.681 1.00 63.16 N ANISOU 885 N ASN A 111 8381 7037 8579 -610 371 591 N ATOM 886 CA ASN A 111 -218.199 48.595 30.699 1.00 69.00 C ANISOU 886 CA ASN A 111 9258 7827 9130 -640 381 602 C ATOM 887 C ASN A 111 -218.052 47.104 30.969 1.00 81.12 C ANISOU 887 C ASN A 111 10702 9413 10706 -555 432 468 C ATOM 888 O ASN A 111 -219.005 46.339 30.782 1.00 87.65 O ANISOU 888 O ASN A 111 11601 10264 11440 -512 353 470 O ATOM 889 CB ASN A 111 -217.720 48.935 29.291 1.00 62.05 C ANISOU 889 CB ASN A 111 8524 6974 8080 -823 533 638 C ATOM 890 CG ASN A 111 -218.307 50.230 28.777 1.00 62.90 C ANISOU 890 CG ASN A 111 8786 7023 8090 -914 426 816 C ATOM 891 OD1 ASN A 111 -219.432 50.596 29.123 1.00 73.12 O ANISOU 891 OD1 ASN A 111 10119 8267 9395 -837 229 914 O ATOM 892 ND2 ASN A 111 -217.551 50.932 27.943 1.00 59.69 N ANISOU 892 ND2 ASN A 111 8462 6614 7605 -1080 561 863 N ATOM 893 N LEU A 112 -216.870 46.670 31.408 1.00 80.55 N ANISOU 893 N LEU A 112 10464 9349 10792 -530 554 356 N ATOM 894 CA LEU A 112 -216.653 45.250 31.664 1.00 65.22 C ANISOU 894 CA LEU A 112 8424 7430 8926 -444 600 235 C ATOM 895 C LEU A 112 -217.462 44.778 32.865 1.00 58.88 C ANISOU 895 C LEU A 112 7561 6611 8199 -299 407 252 C ATOM 896 O LEU A 112 -218.274 43.850 32.756 1.00 59.91 O ANISOU 896 O LEU A 112 7746 6756 8262 -251 355 236 O ATOM 897 CB LEU A 112 -215.165 44.973 31.874 1.00 67.52 C ANISOU 897 CB LEU A 112 8526 7716 9413 -446 758 127 C ATOM 898 CG LEU A 112 -214.348 44.768 30.600 1.00 69.35 C ANISOU 898 CG LEU A 112 8793 7976 9582 -573 1017 43 C ATOM 899 CD1 LEU A 112 -212.966 44.265 30.959 1.00 68.33 C ANISOU 899 CD1 LEU A 112 8423 7829 9711 -537 1161 -79 C ATOM 900 CD2 LEU A 112 -215.053 43.798 29.663 1.00 75.51 C ANISOU 900 CD2 LEU A 112 9732 8786 10173 -599 1074 -11 C ATOM 901 N GLU A 113 -217.251 45.407 34.027 1.00 51.94 N ANISOU 901 N GLU A 113 6577 5703 7453 -244 306 282 N ATOM 902 CA GLU A 113 -217.999 45.018 35.219 1.00 57.20 C ANISOU 902 CA GLU A 113 7201 6362 8170 -128 141 297 C ATOM 903 C GLU A 113 -219.491 45.230 35.023 1.00 73.56 C ANISOU 903 C GLU A 113 9412 8434 10105 -112 30 379 C ATOM 904 O GLU A 113 -220.305 44.420 35.480 1.00 82.28 O ANISOU 904 O GLU A 113 10515 9550 11197 -37 -55 375 O ATOM 905 CB GLU A 113 -217.522 45.799 36.442 1.00 52.46 C ANISOU 905 CB GLU A 113 6499 5734 7698 -103 58 308 C ATOM 906 CG GLU A 113 -218.225 45.348 37.716 1.00 70.37 C ANISOU 906 CG GLU A 113 8737 8006 9995 -5 -91 314 C ATOM 907 CD GLU A 113 -218.768 46.488 38.554 1.00 90.42 C ANISOU 907 CD GLU A 113 11313 10514 12529 -1 -189 358 C ATOM 908 OE1 GLU A 113 -218.002 47.060 39.359 1.00102.60 O ANISOU 908 OE1 GLU A 113 12781 12039 14162 -21 -218 335 O ATOM 909 OE2 GLU A 113 -219.968 46.804 38.413 1.00 97.16 O ANISOU 909 OE2 GLU A 113 12264 11355 13298 21 -239 408 O ATOM 910 N GLY A 114 -219.870 46.320 34.355 1.00 79.63 N ANISOU 910 N GLY A 114 10289 9180 10785 -185 22 463 N ATOM 911 CA GLY A 114 -221.276 46.542 34.070 1.00 79.58 C ANISOU 911 CA GLY A 114 10394 9163 10679 -170 -96 552 C ATOM 912 C GLY A 114 -221.875 45.423 33.242 1.00 67.37 C ANISOU 912 C GLY A 114 8926 7662 9008 -186 -90 537 C ATOM 913 O GLY A 114 -222.942 44.898 33.564 1.00 79.28 O ANISOU 913 O GLY A 114 10442 9177 10504 -122 -198 557 O ATOM 914 N PHE A 115 -221.182 45.031 32.171 1.00 51.02 N ANISOU 914 N PHE A 115 6917 5622 6846 -281 48 488 N ATOM 915 CA PHE A 115 -221.686 43.977 31.295 1.00 68.07 C ANISOU 915 CA PHE A 115 9175 7819 8868 -319 67 453 C ATOM 916 C PHE A 115 -221.846 42.662 32.049 1.00 86.56 C ANISOU 916 C PHE A 115 11419 10165 11305 -212 43 364 C ATOM 917 O PHE A 115 -222.935 42.079 32.082 1.00100.84 O ANISOU 917 O PHE A 115 13271 11981 13064 -182 -67 391 O ATOM 918 CB PHE A 115 -220.751 43.806 30.095 1.00 70.00 C ANISOU 918 CB PHE A 115 9500 8093 9002 -450 262 384 C ATOM 919 CG PHE A 115 -221.116 42.657 29.193 1.00 71.77 C ANISOU 919 CG PHE A 115 9837 8352 9080 -505 311 309 C ATOM 920 CD1 PHE A 115 -222.084 42.807 28.213 1.00 81.29 C ANISOU 920 CD1 PHE A 115 11235 9584 10069 -609 221 394 C ATOM 921 CD2 PHE A 115 -220.481 41.431 29.318 1.00 74.04 C ANISOU 921 CD2 PHE A 115 10040 8635 9457 -459 439 153 C ATOM 922 CE1 PHE A 115 -222.419 41.752 27.379 1.00 86.03 C ANISOU 922 CE1 PHE A 115 11954 10215 10518 -679 260 314 C ATOM 923 CE2 PHE A 115 -220.812 40.371 28.488 1.00 80.52 C ANISOU 923 CE2 PHE A 115 10974 9471 10148 -515 494 65 C ATOM 924 CZ PHE A 115 -221.782 40.533 27.517 1.00 83.44 C ANISOU 924 CZ PHE A 115 11549 9878 10277 -632 407 139 C ATOM 925 N PHE A 116 -220.767 42.181 32.673 1.00 79.67 N ANISOU 925 N PHE A 116 10407 9280 10584 -159 135 269 N ATOM 926 CA PHE A 116 -220.805 40.856 33.286 1.00 77.20 C ANISOU 926 CA PHE A 116 10009 8954 10368 -69 115 195 C ATOM 927 C PHE A 116 -221.755 40.810 34.478 1.00 82.62 C ANISOU 927 C PHE A 116 10651 9634 11106 24 -58 263 C ATOM 928 O PHE A 116 -222.484 39.826 34.654 1.00 92.08 O ANISOU 928 O PHE A 116 11862 10830 12295 63 -120 253 O ATOM 929 CB PHE A 116 -219.400 40.424 33.699 1.00 70.18 C ANISOU 929 CB PHE A 116 8963 8039 9662 -31 229 100 C ATOM 930 CG PHE A 116 -218.578 39.897 32.562 1.00 70.75 C ANISOU 930 CG PHE A 116 9057 8109 9714 -102 434 -15 C ATOM 931 CD1 PHE A 116 -218.844 38.650 32.019 1.00 63.58 C ANISOU 931 CD1 PHE A 116 8201 7185 8774 -98 489 -105 C ATOM 932 CD2 PHE A 116 -217.543 40.648 32.031 1.00 71.60 C ANISOU 932 CD2 PHE A 116 9137 8228 9839 -183 587 -42 C ATOM 933 CE1 PHE A 116 -218.092 38.161 30.967 1.00 64.70 C ANISOU 933 CE1 PHE A 116 8370 7318 8894 -170 706 -237 C ATOM 934 CE2 PHE A 116 -216.786 40.164 30.981 1.00 70.48 C ANISOU 934 CE2 PHE A 116 9014 8087 9676 -258 811 -163 C ATOM 935 CZ PHE A 116 -217.061 38.919 30.448 1.00 65.84 C ANISOU 935 CZ PHE A 116 8483 7482 9050 -250 877 -269 C ATOM 936 N ALA A 117 -221.760 41.854 35.310 1.00 80.52 N ANISOU 936 N ALA A 117 10338 9361 10894 50 -126 324 N ATOM 937 CA ALA A 117 -222.691 41.878 36.434 1.00 82.85 C ANISOU 937 CA ALA A 117 10604 9655 11222 123 -260 374 C ATOM 938 C ALA A 117 -224.134 41.995 35.960 1.00 79.67 C ANISOU 938 C ALA A 117 10296 9260 10715 112 -344 444 C ATOM 939 O ALA A 117 -225.040 41.446 36.597 1.00 80.49 O ANISOU 939 O ALA A 117 10378 9369 10835 163 -425 461 O ATOM 940 CB ALA A 117 -222.351 43.023 37.387 1.00 90.75 C ANISOU 940 CB ALA A 117 11549 10639 12295 140 -294 399 C ATOM 941 N THR A 118 -224.368 42.703 34.854 1.00 73.63 N ANISOU 941 N THR A 118 9631 8494 9850 37 -333 495 N ATOM 942 CA THR A 118 -225.710 42.741 34.286 1.00 75.16 C ANISOU 942 CA THR A 118 9907 8693 9959 17 -438 574 C ATOM 943 C THR A 118 -226.033 41.439 33.568 1.00 79.08 C ANISOU 943 C THR A 118 10464 9217 10367 -20 -432 528 C ATOM 944 O THR A 118 -227.162 40.942 33.649 1.00 80.91 O ANISOU 944 O THR A 118 10701 9455 10586 -2 -535 563 O ATOM 945 CB THR A 118 -225.848 43.929 33.333 1.00 69.96 C ANISOU 945 CB THR A 118 9346 8014 9219 -63 -460 667 C ATOM 946 OG1 THR A 118 -225.539 45.141 34.033 1.00 66.73 O ANISOU 946 OG1 THR A 118 8882 7559 8912 -29 -462 700 O ATOM 947 CG2 THR A 118 -227.261 44.017 32.780 1.00 73.03 C ANISOU 947 CG2 THR A 118 9800 8399 9548 -81 -605 770 C ATOM 948 N LEU A 119 -225.048 40.866 32.872 1.00 81.26 N ANISOU 948 N LEU A 119 10778 9503 10595 -75 -302 439 N ATOM 949 CA LEU A 119 -225.268 39.609 32.164 1.00 74.79 C ANISOU 949 CA LEU A 119 10028 8695 9696 -118 -274 367 C ATOM 950 C LEU A 119 -225.648 38.495 33.131 1.00 78.25 C ANISOU 950 C LEU A 119 10373 9113 10246 -26 -326 329 C ATOM 951 O LEU A 119 -226.601 37.747 32.889 1.00 81.86 O ANISOU 951 O LEU A 119 10877 9572 10654 -44 -405 337 O ATOM 952 CB LEU A 119 -224.018 39.229 31.371 1.00 64.99 C ANISOU 952 CB LEU A 119 8821 7453 8419 -183 -85 249 C ATOM 953 CG LEU A 119 -224.143 38.045 30.415 1.00 59.37 C ANISOU 953 CG LEU A 119 8216 6742 7599 -254 -19 147 C ATOM 954 CD1 LEU A 119 -225.011 38.413 29.224 1.00 62.90 C ANISOU 954 CD1 LEU A 119 8853 7232 7816 -388 -93 216 C ATOM 955 CD2 LEU A 119 -222.767 37.590 29.962 1.00 61.02 C ANISOU 955 CD2 LEU A 119 8402 6933 7851 -280 205 -1 C ATOM 956 N GLY A 120 -224.915 38.376 34.240 1.00 78.72 N ANISOU 956 N GLY A 120 10305 9151 10456 59 -297 299 N ATOM 957 CA GLY A 120 -225.212 37.325 35.201 1.00 78.67 C ANISOU 957 CA GLY A 120 10222 9120 10548 133 -353 283 C ATOM 958 C GLY A 120 -226.605 37.448 35.787 1.00 78.30 C ANISOU 958 C GLY A 120 10173 9091 10485 155 -487 372 C ATOM 959 O GLY A 120 -227.352 36.469 35.861 1.00 91.21 O ANISOU 959 O GLY A 120 11818 10717 12119 156 -540 370 O ATOM 960 N GLY A 121 -226.974 38.659 36.209 1.00 78.56 N ANISOU 960 N GLY A 121 10186 9142 10521 171 -533 444 N ATOM 961 CA GLY A 121 -228.310 38.871 36.740 1.00 78.38 C ANISOU 961 CA GLY A 121 10141 9130 10510 195 -635 517 C ATOM 962 C GLY A 121 -229.400 38.688 35.704 1.00 68.98 C ANISOU 962 C GLY A 121 9022 7949 9237 137 -710 562 C ATOM 963 O GLY A 121 -230.510 38.263 36.036 1.00 59.36 O ANISOU 963 O GLY A 121 7770 6738 8047 148 -788 600 O ATOM 964 N GLU A 122 -229.105 39.000 34.441 1.00 67.87 N ANISOU 964 N GLU A 122 8984 7814 8988 60 -691 564 N ATOM 965 CA GLU A 122 -230.096 38.812 33.387 1.00 70.36 C ANISOU 965 CA GLU A 122 9389 8144 9202 -20 -789 615 C ATOM 966 C GLU A 122 -230.247 37.340 33.023 1.00 75.78 C ANISOU 966 C GLU A 122 10120 8830 9844 -62 -783 538 C ATOM 967 O GLU A 122 -231.361 36.877 32.750 1.00 77.64 O ANISOU 967 O GLU A 122 10372 9072 10056 -99 -896 578 O ATOM 968 CB GLU A 122 -229.719 39.636 32.158 1.00 71.04 C ANISOU 968 CB GLU A 122 9599 8239 9155 -114 -778 652 C ATOM 969 CG GLU A 122 -230.091 41.096 32.273 1.00 75.45 C ANISOU 969 CG GLU A 122 10133 8776 9759 -92 -851 770 C ATOM 970 CD GLU A 122 -231.588 41.312 32.207 1.00 83.55 C ANISOU 970 CD GLU A 122 11125 9793 10828 -84 -1026 881 C ATOM 971 OE1 GLU A 122 -232.180 41.089 31.129 1.00 83.20 O ANISOU 971 OE1 GLU A 122 11181 9765 10665 -181 -1131 937 O ATOM 972 OE2 GLU A 122 -232.176 41.690 33.239 1.00 83.63 O ANISOU 972 OE2 GLU A 122 11005 9778 10992 13 -1056 908 O ATOM 973 N ILE A 123 -229.142 36.590 33.007 1.00 76.08 N ANISOU 973 N ILE A 123 10169 8848 9890 -57 -654 424 N ATOM 974 CA ILE A 123 -229.232 35.151 32.770 1.00 63.96 C ANISOU 974 CA ILE A 123 8669 7285 8350 -83 -637 337 C ATOM 975 C ILE A 123 -230.070 34.491 33.855 1.00 65.15 C ANISOU 975 C ILE A 123 8722 7419 8615 -21 -724 376 C ATOM 976 O ILE A 123 -230.881 33.599 33.581 1.00 85.16 O ANISOU 976 O ILE A 123 11289 9939 11129 -68 -791 369 O ATOM 977 CB ILE A 123 -227.826 34.526 32.685 1.00 53.36 C ANISOU 977 CB ILE A 123 7320 5900 7055 -64 -473 206 C ATOM 978 CG1 ILE A 123 -227.068 35.056 31.470 1.00 58.92 C ANISOU 978 CG1 ILE A 123 8135 6626 7626 -155 -357 151 C ATOM 979 CG2 ILE A 123 -227.920 33.014 32.600 1.00 42.23 C ANISOU 979 CG2 ILE A 123 5929 4430 5688 -71 -455 112 C ATOM 980 CD1 ILE A 123 -225.633 34.594 31.398 1.00 62.31 C ANISOU 980 CD1 ILE A 123 8524 7014 8139 -130 -170 17 C ATOM 981 N ALA A 124 -229.901 34.934 35.102 1.00 55.20 N ANISOU 981 N ALA A 124 7348 6160 7465 68 -721 419 N ATOM 982 CA ALA A 124 -230.654 34.354 36.209 1.00 62.89 C ANISOU 982 CA ALA A 124 8240 7127 8529 111 -783 460 C ATOM 983 C ALA A 124 -232.144 34.653 36.081 1.00 75.70 C ANISOU 983 C ALA A 124 9847 8781 10136 79 -894 544 C ATOM 984 O ALA A 124 -232.983 33.763 36.264 1.00 85.50 O ANISOU 984 O ALA A 124 11069 10011 11406 53 -950 557 O ATOM 985 CB ALA A 124 -230.109 34.877 37.538 1.00 58.50 C ANISOU 985 CB ALA A 124 7593 6577 8057 190 -751 482 C ATOM 986 N LEU A 125 -232.490 35.907 35.770 1.00 75.31 N ANISOU 986 N LEU A 125 9794 8759 10063 79 -930 607 N ATOM 987 CA LEU A 125 -233.894 36.288 35.640 1.00 64.74 C ANISOU 987 CA LEU A 125 8408 7436 8754 62 -1045 696 C ATOM 988 C LEU A 125 -234.605 35.434 34.598 1.00 60.67 C ANISOU 988 C LEU A 125 7964 6922 8167 -36 -1141 699 C ATOM 989 O LEU A 125 -235.689 34.897 34.851 1.00 65.71 O ANISOU 989 O LEU A 125 8537 7562 8867 -54 -1220 736 O ATOM 990 CB LEU A 125 -234.006 37.769 35.276 1.00 68.44 C ANISOU 990 CB LEU A 125 8874 7908 9223 76 -1080 766 C ATOM 991 CG LEU A 125 -235.351 38.203 34.682 1.00 64.77 C ANISOU 991 CG LEU A 125 8377 7443 8790 43 -1229 870 C ATOM 992 CD1 LEU A 125 -236.437 38.257 35.747 1.00 48.54 C ANISOU 992 CD1 LEU A 125 6160 5384 6897 107 -1248 905 C ATOM 993 CD2 LEU A 125 -235.231 39.534 33.956 1.00 66.79 C ANISOU 993 CD2 LEU A 125 8678 7681 9020 33 -1281 948 C ATOM 994 N TRP A 126 -234.003 35.293 33.417 1.00 51.32 N ANISOU 994 N TRP A 126 6918 5737 6845 -113 -1129 653 N ATOM 995 CA TRP A 126 -234.632 34.522 32.354 1.00 58.11 C ANISOU 995 CA TRP A 126 7876 6599 7603 -230 -1224 642 C ATOM 996 C TRP A 126 -234.501 33.020 32.566 1.00 72.60 C ANISOU 996 C TRP A 126 9730 8396 9460 -250 -1177 542 C ATOM 997 O TRP A 126 -235.295 32.260 32.003 1.00 74.35 O ANISOU 997 O TRP A 126 9998 8611 9642 -341 -1274 537 O ATOM 998 CB TRP A 126 -234.050 34.929 31.000 1.00 63.41 C ANISOU 998 CB TRP A 126 8715 7288 8089 -329 -1213 621 C ATOM 999 CG TRP A 126 -234.476 36.303 30.587 1.00 84.65 C ANISOU 999 CG TRP A 126 11408 10003 10754 -342 -1317 754 C ATOM 1000 CD1 TRP A 126 -233.725 37.441 30.623 1.00 94.84 C ANISOU 1000 CD1 TRP A 126 12705 11292 12038 -303 -1248 785 C ATOM 1001 CD2 TRP A 126 -235.765 36.688 30.095 1.00 90.93 C ANISOU 1001 CD2 TRP A 126 12186 10810 11553 -397 -1523 884 C ATOM 1002 NE1 TRP A 126 -234.464 38.510 30.173 1.00 98.58 N ANISOU 1002 NE1 TRP A 126 13179 11766 12510 -327 -1396 929 N ATOM 1003 CE2 TRP A 126 -235.720 38.074 29.843 1.00 91.04 C ANISOU 1003 CE2 TRP A 126 12202 10819 11569 -380 -1572 995 C ATOM 1004 CE3 TRP A 126 -236.952 35.994 29.838 1.00 85.15 C ANISOU 1004 CE3 TRP A 126 11428 10084 10840 -463 -1681 923 C ATOM 1005 CZ2 TRP A 126 -236.814 38.778 29.347 1.00 89.20 C ANISOU 1005 CZ2 TRP A 126 11941 10580 11372 -415 -1782 1151 C ATOM 1006 CZ3 TRP A 126 -238.036 36.695 29.346 1.00 82.19 C ANISOU 1006 CZ3 TRP A 126 11015 9715 10497 -503 -1890 1073 C ATOM 1007 CH2 TRP A 126 -237.961 38.072 29.106 1.00 90.23 C ANISOU 1007 CH2 TRP A 126 12032 10722 11531 -474 -1943 1190 C ATOM 1008 N SER A 127 -233.530 32.574 33.368 1.00 69.91 N ANISOU 1008 N SER A 127 9350 8019 9195 -171 -1048 470 N ATOM 1009 CA SER A 127 -233.490 31.165 33.744 1.00 69.52 C ANISOU 1009 CA SER A 127 9296 7908 9210 -175 -1022 401 C ATOM 1010 C SER A 127 -234.696 30.800 34.601 1.00 75.18 C ANISOU 1010 C SER A 127 9908 8630 10029 -168 -1116 485 C ATOM 1011 O SER A 127 -235.259 29.708 34.461 1.00 88.83 O ANISOU 1011 O SER A 127 11657 10318 11777 -230 -1165 462 O ATOM 1012 CB SER A 127 -232.186 30.848 34.475 1.00 68.79 C ANISOU 1012 CB SER A 127 9166 7766 9204 -85 -891 334 C ATOM 1013 OG SER A 127 -231.073 30.972 33.605 1.00 69.55 O ANISOU 1013 OG SER A 127 9347 7848 9230 -104 -781 235 O ATOM 1014 N LEU A 128 -235.111 31.705 35.492 1.00 66.46 N ANISOU 1014 N LEU A 128 8688 7569 8995 -101 -1129 574 N ATOM 1015 CA LEU A 128 -236.340 31.488 36.250 1.00 63.35 C ANISOU 1015 CA LEU A 128 8184 7191 8696 -106 -1194 650 C ATOM 1016 C LEU A 128 -237.558 31.511 35.334 1.00 73.48 C ANISOU 1016 C LEU A 128 9465 8494 9959 -196 -1335 700 C ATOM 1017 O LEU A 128 -238.505 30.738 35.527 1.00 68.53 O ANISOU 1017 O LEU A 128 8785 7857 9398 -250 -1399 726 O ATOM 1018 CB LEU A 128 -236.481 32.543 37.349 1.00 45.97 C ANISOU 1018 CB LEU A 128 5868 5029 6569 -20 -1149 709 C ATOM 1019 CG LEU A 128 -235.422 32.558 38.451 1.00 58.82 C ANISOU 1019 CG LEU A 128 7487 6646 8217 53 -1041 678 C ATOM 1020 CD1 LEU A 128 -235.834 33.485 39.592 1.00 61.84 C ANISOU 1020 CD1 LEU A 128 7768 7069 8659 107 -1000 724 C ATOM 1021 CD2 LEU A 128 -235.160 31.151 38.962 1.00 56.89 C ANISOU 1021 CD2 LEU A 128 7263 6350 8002 32 -1025 653 C ATOM 1022 N VAL A 129 -237.553 32.397 34.336 1.00 72.49 N ANISOU 1022 N VAL A 129 9398 8396 9749 -223 -1397 726 N ATOM 1023 CA VAL A 129 -238.655 32.445 33.381 1.00 70.42 C ANISOU 1023 CA VAL A 129 9146 8152 9459 -322 -1567 790 C ATOM 1024 C VAL A 129 -238.686 31.173 32.543 1.00 70.63 C ANISOU 1024 C VAL A 129 9302 8150 9386 -445 -1613 711 C ATOM 1025 O VAL A 129 -239.754 30.594 32.305 1.00 74.20 O ANISOU 1025 O VAL A 129 9719 8600 9875 -530 -1741 747 O ATOM 1026 CB VAL A 129 -238.541 33.706 32.503 1.00 59.31 C ANISOU 1026 CB VAL A 129 7794 6772 7968 -333 -1636 855 C ATOM 1027 CG1 VAL A 129 -239.610 33.712 31.428 1.00 47.47 C ANISOU 1027 CG1 VAL A 129 6324 5290 6423 -452 -1847 936 C ATOM 1028 CG2 VAL A 129 -238.638 34.955 33.364 1.00 53.42 C ANISOU 1028 CG2 VAL A 129 6910 6033 7355 -211 -1596 926 C ATOM 1029 N VAL A 130 -237.516 30.707 32.099 1.00 67.34 N ANISOU 1029 N VAL A 130 9028 7700 8856 -460 -1501 593 N ATOM 1030 CA VAL A 130 -237.452 29.498 31.280 1.00 71.65 C ANISOU 1030 CA VAL A 130 9713 8200 9309 -577 -1515 486 C ATOM 1031 C VAL A 130 -237.884 28.279 32.086 1.00 70.95 C ANISOU 1031 C VAL A 130 9552 8050 9356 -573 -1509 464 C ATOM 1032 O VAL A 130 -238.646 27.433 31.600 1.00 65.82 O ANISOU 1032 O VAL A 130 8944 7373 8693 -688 -1611 444 O ATOM 1033 CB VAL A 130 -236.038 29.323 30.693 1.00 69.68 C ANISOU 1033 CB VAL A 130 9612 7920 8943 -578 -1356 348 C ATOM 1034 CG1 VAL A 130 -235.806 27.883 30.257 1.00 58.32 C ANISOU 1034 CG1 VAL A 130 8283 6396 7480 -656 -1309 201 C ATOM 1035 CG2 VAL A 130 -235.838 30.271 29.520 1.00 71.39 C ANISOU 1035 CG2 VAL A 130 9958 8198 8970 -658 -1389 366 C ATOM 1036 N LEU A 131 -237.416 28.172 33.333 1.00 68.27 N ANISOU 1036 N LEU A 131 9111 7685 9144 -457 -1402 474 N ATOM 1037 CA LEU A 131 -237.815 27.048 34.174 1.00 67.19 C ANISOU 1037 CA LEU A 131 8912 7486 9132 -462 -1400 478 C ATOM 1038 C LEU A 131 -239.319 27.049 34.420 1.00 78.06 C ANISOU 1038 C LEU A 131 10172 8901 10584 -523 -1528 583 C ATOM 1039 O LEU A 131 -239.952 25.986 34.443 1.00 93.54 O ANISOU 1039 O LEU A 131 12132 10811 12599 -608 -1582 574 O ATOM 1040 CB LEU A 131 -237.054 27.082 35.500 1.00 53.93 C ANISOU 1040 CB LEU A 131 7155 5786 7551 -340 -1283 497 C ATOM 1041 CG LEU A 131 -237.426 25.984 36.501 1.00 49.76 C ANISOU 1041 CG LEU A 131 6571 5194 7142 -351 -1282 531 C ATOM 1042 CD1 LEU A 131 -237.184 24.604 35.905 1.00 63.98 C ANISOU 1042 CD1 LEU A 131 8480 6874 8956 -421 -1289 433 C ATOM 1043 CD2 LEU A 131 -236.664 26.148 37.809 1.00 42.12 C ANISOU 1043 CD2 LEU A 131 5545 4221 6240 -247 -1193 571 C ATOM 1044 N ALA A 132 -239.911 28.231 34.602 1.00 76.71 N ANISOU 1044 N ALA A 132 9892 8812 10443 -483 -1574 681 N ATOM 1045 CA ALA A 132 -241.359 28.307 34.767 1.00 75.29 C ANISOU 1045 CA ALA A 132 9571 8666 10370 -535 -1691 778 C ATOM 1046 C ALA A 132 -242.080 27.819 33.516 1.00 73.93 C ANISOU 1046 C ALA A 132 9471 8486 10134 -683 -1863 771 C ATOM 1047 O ALA A 132 -243.122 27.159 33.608 1.00 77.33 O ANISOU 1047 O ALA A 132 9819 8904 10657 -768 -1955 808 O ATOM 1048 CB ALA A 132 -241.778 29.736 35.106 1.00 79.29 C ANISOU 1048 CB ALA A 132 9942 9238 10946 -451 -1700 869 C ATOM 1049 N ILE A 133 -241.540 28.133 32.337 1.00 69.49 N ANISOU 1049 N ILE A 133 9069 7933 9402 -731 -1909 723 N ATOM 1050 CA ILE A 133 -242.142 27.651 31.098 1.00 68.53 C ANISOU 1050 CA ILE A 133 9056 7808 9173 -897 -2079 705 C ATOM 1051 C ILE A 133 -241.959 26.146 30.968 1.00 80.44 C ANISOU 1051 C ILE A 133 10673 9230 10660 -986 -2043 582 C ATOM 1052 O ILE A 133 -242.884 25.426 30.572 1.00 85.15 O ANISOU 1052 O ILE A 133 11269 9808 11278 -1119 -2184 589 O ATOM 1053 CB ILE A 133 -241.548 28.394 29.889 1.00 65.03 C ANISOU 1053 CB ILE A 133 8787 7403 8520 -944 -2119 685 C ATOM 1054 CG1 ILE A 133 -241.829 29.890 29.998 1.00 67.73 C ANISOU 1054 CG1 ILE A 133 9017 7807 8910 -862 -2181 825 C ATOM 1055 CG2 ILE A 133 -242.108 27.831 28.591 1.00 60.80 C ANISOU 1055 CG2 ILE A 133 8403 6868 7830 -1142 -2298 655 C ATOM 1056 CD1 ILE A 133 -241.265 30.696 28.858 1.00 67.82 C ANISOU 1056 CD1 ILE A 133 9200 7852 8715 -917 -2226 835 C ATOM 1057 N GLU A 134 -240.764 25.649 31.296 1.00 85.13 N ANISOU 1057 N GLU A 134 11352 9759 11233 -915 -1862 469 N ATOM 1058 CA GLU A 134 -240.489 24.220 31.180 1.00 83.15 C ANISOU 1058 CA GLU A 134 11204 9395 10993 -983 -1815 344 C ATOM 1059 C GLU A 134 -241.424 23.409 32.068 1.00 75.09 C ANISOU 1059 C GLU A 134 10049 8331 10150 -1010 -1866 412 C ATOM 1060 O GLU A 134 -242.043 22.440 31.616 1.00 77.10 O ANISOU 1060 O GLU A 134 10356 8525 10412 -1147 -1959 369 O ATOM 1061 CB GLU A 134 -239.027 23.937 31.534 1.00 84.98 C ANISOU 1061 CB GLU A 134 11502 9555 11232 -871 -1614 234 C ATOM 1062 CG GLU A 134 -238.016 24.472 30.525 1.00 87.47 C ANISOU 1062 CG GLU A 134 11970 9893 11370 -876 -1531 130 C ATOM 1063 CD GLU A 134 -236.579 24.192 30.932 1.00101.31 C ANISOU 1063 CD GLU A 134 13744 11568 13181 -757 -1330 25 C ATOM 1064 OE1 GLU A 134 -236.362 23.766 32.085 1.00106.83 O ANISOU 1064 OE1 GLU A 134 14331 12208 14050 -657 -1280 65 O ATOM 1065 OE2 GLU A 134 -235.668 24.396 30.100 1.00105.49 O ANISOU 1065 OE2 GLU A 134 14398 12095 13588 -771 -1224 -92 O ATOM 1066 N ARG A 135 -241.546 23.802 33.339 1.00 65.38 N ANISOU 1066 N ARG A 135 8653 7132 9056 -897 -1800 515 N ATOM 1067 CA ARG A 135 -242.440 23.097 34.251 1.00 63.23 C ANISOU 1067 CA ARG A 135 8251 6829 8943 -935 -1824 590 C ATOM 1068 C ARG A 135 -243.889 23.180 33.785 1.00 76.99 C ANISOU 1068 C ARG A 135 9896 8625 10730 -1059 -2001 666 C ATOM 1069 O ARG A 135 -244.657 22.224 33.946 1.00 81.85 O ANISOU 1069 O ARG A 135 10473 9188 11440 -1167 -2061 680 O ATOM 1070 CB ARG A 135 -242.296 23.666 35.661 1.00 50.42 C ANISOU 1070 CB ARG A 135 6488 5252 7418 -806 -1708 681 C ATOM 1071 CG ARG A 135 -240.960 23.364 36.323 1.00 51.62 C ANISOU 1071 CG ARG A 135 6712 5337 7563 -701 -1564 631 C ATOM 1072 CD ARG A 135 -240.767 24.247 37.539 1.00 55.93 C ANISOU 1072 CD ARG A 135 7145 5957 8149 -586 -1471 715 C ATOM 1073 NE ARG A 135 -239.728 23.763 38.442 1.00 53.34 N ANISOU 1073 NE ARG A 135 6858 5562 7847 -513 -1371 706 N ATOM 1074 CZ ARG A 135 -239.325 24.430 39.517 1.00 64.27 C ANISOU 1074 CZ ARG A 135 8183 6999 9237 -425 -1290 763 C ATOM 1075 NH1 ARG A 135 -239.875 25.602 39.800 1.00 67.27 N ANISOU 1075 NH1 ARG A 135 8463 7491 9608 -392 -1274 813 N ATOM 1076 NH2 ARG A 135 -238.378 23.937 40.303 1.00 70.76 N ANISOU 1076 NH2 ARG A 135 9047 7756 10084 -373 -1234 769 N ATOM 1077 N TYR A 136 -244.283 24.315 33.206 1.00 83.66 N ANISOU 1077 N TYR A 136 10693 9566 11529 -1051 -2098 726 N ATOM 1078 CA TYR A 136 -245.645 24.451 32.702 1.00 80.65 C ANISOU 1078 CA TYR A 136 10200 9229 11214 -1166 -2297 812 C ATOM 1079 C TYR A 136 -245.906 23.490 31.547 1.00 83.71 C ANISOU 1079 C TYR A 136 10747 9563 11496 -1350 -2444 731 C ATOM 1080 O TYR A 136 -246.968 22.860 31.483 1.00 84.81 O ANISOU 1080 O TYR A 136 10801 9686 11738 -1477 -2575 770 O ATOM 1081 CB TYR A 136 -245.900 25.895 32.273 1.00 72.59 C ANISOU 1081 CB TYR A 136 9107 8300 10175 -1109 -2386 902 C ATOM 1082 CG TYR A 136 -247.108 26.062 31.386 1.00 68.55 C ANISOU 1082 CG TYR A 136 8525 7824 9697 -1241 -2641 987 C ATOM 1083 CD1 TYR A 136 -248.387 26.090 31.922 1.00 84.04 C ANISOU 1083 CD1 TYR A 136 10234 9806 11889 -1263 -2721 1094 C ATOM 1084 CD2 TYR A 136 -246.970 26.194 30.011 1.00 62.10 C ANISOU 1084 CD2 TYR A 136 7893 7021 8682 -1356 -2805 963 C ATOM 1085 CE1 TYR A 136 -249.497 26.240 31.114 1.00 91.42 C ANISOU 1085 CE1 TYR A 136 11080 10768 12886 -1385 -2979 1183 C ATOM 1086 CE2 TYR A 136 -248.074 26.345 29.194 1.00 72.03 C ANISOU 1086 CE2 TYR A 136 9092 8312 9965 -1491 -3075 1058 C ATOM 1087 CZ TYR A 136 -249.335 26.368 29.750 1.00 84.13 C ANISOU 1087 CZ TYR A 136 10350 9858 11758 -1499 -3172 1172 C ATOM 1088 OH TYR A 136 -250.437 26.520 28.941 1.00 81.13 O ANISOU 1088 OH TYR A 136 9887 9505 11433 -1633 -3464 1277 O ATOM 1089 N VAL A 137 -244.947 23.366 30.626 1.00 87.06 N ANISOU 1089 N VAL A 137 11404 9959 11716 -1379 -2417 608 N ATOM 1090 CA VAL A 137 -245.136 22.498 29.467 1.00 86.85 C ANISOU 1090 CA VAL A 137 11563 9882 11555 -1569 -2542 504 C ATOM 1091 C VAL A 137 -245.167 21.036 29.891 1.00 92.47 C ANISOU 1091 C VAL A 137 12306 10465 12365 -1631 -2481 415 C ATOM 1092 O VAL A 137 -245.957 20.239 29.369 1.00 89.98 O ANISOU 1092 O VAL A 137 12026 10107 12057 -1804 -2629 389 O ATOM 1093 CB VAL A 137 -244.039 22.764 28.420 1.00 76.82 C ANISOU 1093 CB VAL A 137 10541 8615 10033 -1587 -2481 377 C ATOM 1094 CG1 VAL A 137 -244.128 21.761 27.279 1.00 77.86 C ANISOU 1094 CG1 VAL A 137 10896 8682 10005 -1793 -2568 230 C ATOM 1095 CG2 VAL A 137 -244.149 24.184 27.891 1.00 71.69 C ANISOU 1095 CG2 VAL A 137 9875 8084 9280 -1563 -2581 489 C ATOM 1096 N VAL A 138 -244.319 20.662 30.851 1.00 93.65 N ANISOU 1096 N VAL A 138 12442 10541 12601 -1497 -2280 378 N ATOM 1097 CA VAL A 138 -244.251 19.270 31.282 1.00 82.63 C ANISOU 1097 CA VAL A 138 11085 8998 11312 -1546 -2223 307 C ATOM 1098 C VAL A 138 -245.507 18.868 32.049 1.00 82.35 C ANISOU 1098 C VAL A 138 10859 8966 11465 -1616 -2311 437 C ATOM 1099 O VAL A 138 -245.969 17.725 31.942 1.00 83.25 O ANISOU 1099 O VAL A 138 11012 8972 11645 -1750 -2369 394 O ATOM 1100 CB VAL A 138 -242.973 19.049 32.114 1.00 65.38 C ANISOU 1100 CB VAL A 138 8928 6732 9180 -1381 -2011 259 C ATOM 1101 CG1 VAL A 138 -242.932 17.642 32.683 1.00 84.49 C ANISOU 1101 CG1 VAL A 138 11372 8983 11746 -1420 -1968 222 C ATOM 1102 CG2 VAL A 138 -241.742 19.308 31.261 1.00 54.23 C ANISOU 1102 CG2 VAL A 138 7696 5302 7605 -1334 -1912 109 C ATOM 1103 N VAL A 139 -246.095 19.788 32.812 1.00 81.11 N ANISOU 1103 N VAL A 139 10490 8922 11404 -1537 -2312 588 N ATOM 1104 CA VAL A 139 -247.219 19.446 33.678 1.00 74.92 C ANISOU 1104 CA VAL A 139 9505 8147 10814 -1593 -2342 706 C ATOM 1105 C VAL A 139 -248.542 19.647 32.951 1.00 76.92 C ANISOU 1105 C VAL A 139 9647 8466 11112 -1740 -2562 769 C ATOM 1106 O VAL A 139 -249.341 18.713 32.824 1.00 84.85 O ANISOU 1106 O VAL A 139 10624 9410 12206 -1899 -2663 771 O ATOM 1107 CB VAL A 139 -247.184 20.267 34.978 1.00 72.46 C ANISOU 1107 CB VAL A 139 9018 7916 10599 -1440 -2197 818 C ATOM 1108 CG1 VAL A 139 -248.459 20.045 35.774 1.00 74.28 C ANISOU 1108 CG1 VAL A 139 9026 8175 11020 -1517 -2214 935 C ATOM 1109 CG2 VAL A 139 -245.966 19.889 35.804 1.00 60.36 C ANISOU 1109 CG2 VAL A 139 7586 6308 9042 -1326 -2015 777 C ATOM 1110 N CYS A 140 -248.787 20.871 32.479 1.00 82.39 N ANISOU 1110 N CYS A 140 10269 9274 11762 -1691 -2652 831 N ATOM 1111 CA CYS A 140 -250.059 21.185 31.841 1.00 90.58 C ANISOU 1111 CA CYS A 140 11166 10374 12874 -1814 -2886 921 C ATOM 1112 C CYS A 140 -250.210 20.527 30.475 1.00 97.73 C ANISOU 1112 C CYS A 140 12268 11238 13626 -2010 -3091 834 C ATOM 1113 O CYS A 140 -251.339 20.406 29.986 1.00108.19 O ANISOU 1113 O CYS A 140 13487 12588 15033 -2160 -3314 901 O ATOM 1114 CB CYS A 140 -250.216 22.701 31.715 1.00 93.37 C ANISOU 1114 CB CYS A 140 11396 10841 13241 -1697 -2936 1022 C ATOM 1115 SG CYS A 140 -250.297 23.566 33.304 1.00 99.44 S ANISOU 1115 SG CYS A 140 11908 11663 14210 -1493 -2709 1115 S ATOM 1116 N LYS A 141 -249.105 20.100 29.858 1.00 98.32 N ANISOU 1116 N LYS A 141 12622 11247 13487 -2020 -3018 679 N ATOM 1117 CA LYS A 141 -249.092 19.404 28.575 1.00105.98 C ANISOU 1117 CA LYS A 141 13826 12166 14273 -2216 -3166 554 C ATOM 1118 C LYS A 141 -249.901 20.154 27.520 1.00115.43 C ANISOU 1118 C LYS A 141 15008 13469 15381 -2339 -3446 643 C ATOM 1119 O LYS A 141 -250.938 19.655 27.066 1.00115.18 O ANISOU 1119 O LYS A 141 14928 13430 15404 -2525 -3669 676 O ATOM 1120 CB LYS A 141 -249.627 17.979 28.741 1.00 99.82 C ANISOU 1120 CB LYS A 141 13057 11264 13607 -2369 -3200 494 C ATOM 1121 CG LYS A 141 -248.855 17.147 29.756 1.00 91.92 C ANISOU 1121 CG LYS A 141 12083 10136 12706 -2264 -2955 427 C ATOM 1122 CD LYS A 141 -249.504 15.791 29.986 1.00 97.64 C ANISOU 1122 CD LYS A 141 12796 10729 13573 -2422 -3003 399 C ATOM 1123 CE LYS A 141 -248.761 14.998 31.052 1.00 98.36 C ANISOU 1123 CE LYS A 141 12908 10683 13780 -2316 -2782 369 C ATOM 1124 NZ LYS A 141 -249.424 13.697 31.346 1.00101.72 N ANISOU 1124 NZ LYS A 141 13316 10969 14364 -2474 -2829 364 N ATOM 1125 N PRO A 142 -249.469 21.349 27.102 1.00120.68 N ANISOU 1125 N PRO A 142 15713 14226 15915 -2250 -3462 694 N ATOM 1126 CA PRO A 142 -250.233 22.096 26.093 1.00118.56 C ANISOU 1126 CA PRO A 142 15434 14047 15565 -2370 -3758 807 C ATOM 1127 C PRO A 142 -250.017 21.608 24.672 1.00119.78 C ANISOU 1127 C PRO A 142 15908 14190 15413 -2594 -3907 685 C ATOM 1128 O PRO A 142 -250.771 22.013 23.776 1.00123.40 O ANISOU 1128 O PRO A 142 16380 14714 15790 -2745 -4203 784 O ATOM 1129 CB PRO A 142 -249.716 23.529 26.264 1.00112.55 C ANISOU 1129 CB PRO A 142 14618 13366 14779 -2183 -3687 905 C ATOM 1130 CG PRO A 142 -248.303 23.344 26.702 1.00112.38 C ANISOU 1130 CG PRO A 142 14751 13297 14653 -2046 -3375 759 C ATOM 1131 CD PRO A 142 -248.269 22.086 27.540 1.00116.45 C ANISOU 1131 CD PRO A 142 15227 13709 15310 -2044 -3226 666 C ATOM 1132 N MET A 143 -249.015 20.768 24.435 1.00120.23 N ANISOU 1132 N MET A 143 16221 14160 15300 -2623 -3716 472 N ATOM 1133 CA MET A 143 -248.767 20.171 23.131 1.00125.01 C ANISOU 1133 CA MET A 143 17151 14739 15606 -2849 -3808 310 C ATOM 1134 C MET A 143 -249.045 18.676 23.224 1.00139.92 C ANISOU 1134 C MET A 143 19097 16493 17572 -2983 -3792 163 C ATOM 1135 O MET A 143 -248.498 17.993 24.096 1.00145.66 O ANISOU 1135 O MET A 143 19785 17111 18450 -2860 -3554 77 O ATOM 1136 CB MET A 143 -247.332 20.443 22.674 1.00110.44 C ANISOU 1136 CB MET A 143 15564 12890 13506 -2782 -3572 156 C ATOM 1137 CG MET A 143 -246.940 21.911 22.773 1.00106.57 C ANISOU 1137 CG MET A 143 15001 12513 12977 -2624 -3544 303 C ATOM 1138 SD MET A 143 -245.210 22.228 22.384 1.00111.15 S ANISOU 1138 SD MET A 143 15840 13086 13305 -2535 -3231 127 S ATOM 1139 CE MET A 143 -245.086 23.965 22.802 1.00115.18 C ANISOU 1139 CE MET A 143 16172 13714 13875 -2342 -3245 355 C ATOM 1140 N SER A 144 -249.892 18.177 22.320 1.00143.41 N ANISOU 1140 N SER A 144 19639 16936 17914 -3244 -4063 144 N ATOM 1141 CA SER A 144 -250.495 16.858 22.499 1.00155.68 C ANISOU 1141 CA SER A 144 21178 18367 19608 -3389 -4113 58 C ATOM 1142 C SER A 144 -249.448 15.750 22.502 1.00164.33 C ANISOU 1142 C SER A 144 22509 19296 20632 -3383 -3842 -207 C ATOM 1143 O SER A 144 -249.415 14.916 23.415 1.00168.33 O ANISOU 1143 O SER A 144 22909 19675 21375 -3310 -3701 -238 O ATOM 1144 CB SER A 144 -251.540 16.610 21.410 1.00162.89 C ANISOU 1144 CB SER A 144 22178 19318 20393 -3691 -4477 78 C ATOM 1145 OG SER A 144 -250.997 16.831 20.120 1.00165.06 O ANISOU 1145 OG SER A 144 22795 19639 20279 -3842 -4537 -43 O ATOM 1146 N ASN A 145 -248.590 15.714 21.485 1.00164.22 N ANISOU 1146 N ASN A 145 22817 19274 20306 -3465 -3763 -397 N ATOM 1147 CA ASN A 145 -247.612 14.638 21.377 1.00161.43 C ANISOU 1147 CA ASN A 145 22686 18746 19906 -3468 -3505 -672 C ATOM 1148 C ASN A 145 -246.197 15.155 21.601 1.00151.05 C ANISOU 1148 C ASN A 145 21434 17431 18526 -3244 -3192 -752 C ATOM 1149 O ASN A 145 -245.317 14.951 20.759 1.00159.34 O ANISOU 1149 O ASN A 145 22761 18442 19338 -3309 -3044 -972 O ATOM 1150 CB ASN A 145 -247.718 13.958 20.011 1.00171.05 C ANISOU 1150 CB ASN A 145 24240 19920 20830 -3767 -3620 -888 C ATOM 1151 CG ASN A 145 -249.083 13.340 19.769 1.00179.63 C ANISOU 1151 CG ASN A 145 25272 20990 21989 -4011 -3940 -826 C ATOM 1152 OD1 ASN A 145 -249.739 12.869 20.699 1.00181.36 O ANISOU 1152 OD1 ASN A 145 25243 21141 22523 -3960 -3978 -718 O ATOM 1153 ND2 ASN A 145 -249.517 13.339 18.515 1.00183.66 N ANISOU 1153 ND2 ASN A 145 26017 21564 22200 -4291 -4176 -891 N ATOM 1154 N PHE A 146 -245.961 15.808 22.736 1.00135.68 N ANISOU 1154 N PHE A 146 19234 15526 16791 -2991 -3080 -586 N ATOM 1155 CA PHE A 146 -244.691 16.463 23.010 1.00115.90 C ANISOU 1155 CA PHE A 146 16750 13044 14243 -2777 -2819 -624 C ATOM 1156 C PHE A 146 -244.026 15.856 24.237 1.00108.86 C ANISOU 1156 C PHE A 146 15724 12011 13629 -2568 -2583 -652 C ATOM 1157 O PHE A 146 -244.679 15.611 25.257 1.00105.21 O ANISOU 1157 O PHE A 146 15039 11521 13415 -2507 -2638 -507 O ATOM 1158 CB PHE A 146 -244.885 17.967 23.219 1.00107.15 C ANISOU 1158 CB PHE A 146 15483 12121 13110 -2664 -2905 -395 C ATOM 1159 CG PHE A 146 -243.600 18.734 23.355 1.00 99.86 C ANISOU 1159 CG PHE A 146 14599 11233 12111 -2478 -2662 -433 C ATOM 1160 CD1 PHE A 146 -242.913 19.166 22.232 1.00 96.81 C ANISOU 1160 CD1 PHE A 146 14463 10903 11418 -2569 -2607 -549 C ATOM 1161 CD2 PHE A 146 -243.082 19.030 24.605 1.00 92.79 C ANISOU 1161 CD2 PHE A 146 13497 10318 11442 -2231 -2490 -351 C ATOM 1162 CE1 PHE A 146 -241.730 19.874 22.354 1.00 91.31 C ANISOU 1162 CE1 PHE A 146 13788 10238 10667 -2409 -2377 -582 C ATOM 1163 CE2 PHE A 146 -241.900 19.737 24.734 1.00 87.05 C ANISOU 1163 CE2 PHE A 146 12796 9622 10659 -2072 -2281 -385 C ATOM 1164 CZ PHE A 146 -241.225 20.160 23.607 1.00 89.70 C ANISOU 1164 CZ PHE A 146 13360 10008 10712 -2158 -2222 -499 C ATOM 1165 N ARG A 147 -242.720 15.620 24.128 1.00109.20 N ANISOU 1165 N ARG A 147 15899 11963 13628 -2467 -2323 -834 N ATOM 1166 CA ARG A 147 -241.896 15.144 25.231 1.00114.04 C ANISOU 1166 CA ARG A 147 16396 12440 14492 -2255 -2106 -854 C ATOM 1167 C ARG A 147 -240.674 16.041 25.344 1.00109.74 C ANISOU 1167 C ARG A 147 15847 11961 13889 -2069 -1902 -869 C ATOM 1168 O ARG A 147 -239.945 16.230 24.364 1.00109.53 O ANISOU 1168 O ARG A 147 16018 11950 13648 -2124 -1792 -1036 O ATOM 1169 CB ARG A 147 -241.472 13.685 25.027 1.00125.81 C ANISOU 1169 CB ARG A 147 18036 13694 16074 -2317 -1987 -1087 C ATOM 1170 CG ARG A 147 -240.438 13.179 26.029 1.00132.13 C ANISOU 1170 CG ARG A 147 18741 14332 17131 -2096 -1765 -1118 C ATOM 1171 CD ARG A 147 -241.035 12.968 27.415 1.00134.62 C ANISOU 1171 CD ARG A 147 18818 14620 17711 -2003 -1843 -895 C ATOM 1172 NE ARG A 147 -240.061 12.406 28.350 1.00133.93 N ANISOU 1172 NE ARG A 147 18662 14365 17861 -1816 -1666 -911 N ATOM 1173 CZ ARG A 147 -239.418 13.109 29.277 1.00131.70 C ANISOU 1173 CZ ARG A 147 18228 14147 17664 -1613 -1577 -778 C ATOM 1174 NH1 ARG A 147 -239.648 14.409 29.407 1.00128.84 N ANISOU 1174 NH1 ARG A 147 17769 14007 17178 -1564 -1627 -633 N ATOM 1175 NH2 ARG A 147 -238.547 12.510 30.079 1.00127.55 N ANISOU 1175 NH2 ARG A 147 17649 13456 17357 -1463 -1450 -787 N ATOM 1176 N PHE A 148 -240.457 16.592 26.535 1.00106.09 N ANISOU 1176 N PHE A 148 15164 11539 13607 -1866 -1849 -699 N ATOM 1177 CA PHE A 148 -239.364 17.528 26.772 1.00101.15 C ANISOU 1177 CA PHE A 148 14501 10983 12950 -1689 -1681 -685 C ATOM 1178 C PHE A 148 -238.058 16.762 26.954 1.00 99.55 C ANISOU 1178 C PHE A 148 14353 10606 12866 -1576 -1437 -868 C ATOM 1179 O PHE A 148 -237.902 16.013 27.925 1.00 96.16 O ANISOU 1179 O PHE A 148 13814 10040 12683 -1476 -1394 -837 O ATOM 1180 CB PHE A 148 -239.672 18.385 27.998 1.00 95.94 C ANISOU 1180 CB PHE A 148 13593 10425 12435 -1532 -1726 -446 C ATOM 1181 CG PHE A 148 -238.577 19.344 28.361 1.00 88.15 C ANISOU 1181 CG PHE A 148 12553 9502 11438 -1353 -1568 -421 C ATOM 1182 CD1 PHE A 148 -238.431 20.538 27.676 1.00 82.84 C ANISOU 1182 CD1 PHE A 148 11932 8976 10567 -1370 -1586 -389 C ATOM 1183 CD2 PHE A 148 -237.702 19.057 29.396 1.00 83.45 C ANISOU 1183 CD2 PHE A 148 11856 8815 11037 -1180 -1418 -418 C ATOM 1184 CE1 PHE A 148 -237.426 21.425 28.009 1.00 79.78 C ANISOU 1184 CE1 PHE A 148 11493 8640 10178 -1218 -1442 -367 C ATOM 1185 CE2 PHE A 148 -236.695 19.941 29.734 1.00 78.87 C ANISOU 1185 CE2 PHE A 148 11219 8293 10454 -1028 -1289 -396 C ATOM 1186 CZ PHE A 148 -236.558 21.126 29.039 1.00 82.42 C ANISOU 1186 CZ PHE A 148 11719 8888 10710 -1048 -1293 -377 C ATOM 1187 N GLY A 149 -237.119 16.959 26.030 1.00100.26 N ANISOU 1187 N GLY A 149 14606 10697 12793 -1594 -1277 -1050 N ATOM 1188 CA GLY A 149 -235.875 16.213 26.045 1.00102.02 C ANISOU 1188 CA GLY A 149 14874 10742 13146 -1496 -1034 -1252 C ATOM 1189 C GLY A 149 -234.630 17.068 26.165 1.00103.25 C ANISOU 1189 C GLY A 149 14975 10956 13298 -1338 -841 -1268 C ATOM 1190 O GLY A 149 -234.707 18.245 26.531 1.00108.36 O ANISOU 1190 O GLY A 149 15517 11770 13884 -1269 -899 -1090 O ATOM 1191 N GLU A 150 -233.471 16.480 25.853 1.00108.95 N ANISOU 1191 N GLU A 150 15759 11532 14105 -1280 -604 -1488 N ATOM 1192 CA GLU A 150 -232.206 17.189 26.018 1.00108.55 C ANISOU 1192 CA GLU A 150 15628 11516 14099 -1125 -407 -1512 C ATOM 1193 C GLU A 150 -232.086 18.351 25.039 1.00107.41 C ANISOU 1193 C GLU A 150 15609 11568 13632 -1228 -371 -1526 C ATOM 1194 O GLU A 150 -231.569 19.417 25.393 1.00113.11 O ANISOU 1194 O GLU A 150 16224 12407 14345 -1121 -330 -1410 O ATOM 1195 CB GLU A 150 -231.036 16.219 25.846 1.00116.45 C ANISOU 1195 CB GLU A 150 16648 12297 15300 -1046 -157 -1759 C ATOM 1196 CG GLU A 150 -229.660 16.853 26.011 1.00117.09 C ANISOU 1196 CG GLU A 150 16620 12396 15473 -888 58 -1799 C ATOM 1197 CD GLU A 150 -228.527 15.880 25.734 1.00124.69 C ANISOU 1197 CD GLU A 150 17586 13131 16660 -814 317 -2062 C ATOM 1198 OE1 GLU A 150 -228.810 14.742 25.303 1.00130.23 O ANISOU 1198 OE1 GLU A 150 18407 13660 17415 -899 343 -2235 O ATOM 1199 OE2 GLU A 150 -227.354 16.252 25.947 1.00126.31 O ANISOU 1199 OE2 GLU A 150 17664 13320 17008 -672 495 -2100 O ATOM 1200 N ASN A 151 -232.559 18.165 23.805 1.00108.20 N ANISOU 1200 N ASN A 151 15948 11705 13460 -1448 -395 -1661 N ATOM 1201 CA ASN A 151 -232.464 19.226 22.807 1.00107.78 C ANISOU 1201 CA ASN A 151 16046 11833 13073 -1574 -374 -1663 C ATOM 1202 C ASN A 151 -233.288 20.442 23.208 1.00104.99 C ANISOU 1202 C ASN A 151 15588 11667 12636 -1562 -615 -1367 C ATOM 1203 O ASN A 151 -232.858 21.585 23.012 1.00105.76 O ANISOU 1203 O ASN A 151 15682 11895 12607 -1538 -571 -1287 O ATOM 1204 CB ASN A 151 -232.909 18.699 21.443 1.00114.13 C ANISOU 1204 CB ASN A 151 17148 12635 13583 -1840 -387 -1854 C ATOM 1205 CG ASN A 151 -231.953 17.668 20.881 1.00122.09 C ANISOU 1205 CG ASN A 151 18285 13463 14641 -1862 -89 -2188 C ATOM 1206 OD1 ASN A 151 -231.025 17.232 21.561 1.00128.89 O ANISOU 1206 OD1 ASN A 151 18987 14180 15807 -1666 101 -2264 O ATOM 1207 ND2 ASN A 151 -232.176 17.271 19.634 1.00120.64 N ANISOU 1207 ND2 ASN A 151 18389 13282 14165 -2106 -51 -2392 N ATOM 1208 N HIS A 152 -234.475 20.219 23.778 1.00101.52 N ANISOU 1208 N HIS A 152 15054 11234 12286 -1577 -861 -1205 N ATOM 1209 CA HIS A 152 -235.321 21.339 24.175 1.00 87.52 C ANISOU 1209 CA HIS A 152 13160 9621 10474 -1558 -1081 -937 C ATOM 1210 C HIS A 152 -234.715 22.104 25.344 1.00 83.41 C ANISOU 1210 C HIS A 152 12413 9129 10151 -1328 -1005 -798 C ATOM 1211 O HIS A 152 -234.789 23.338 25.390 1.00 96.29 O ANISOU 1211 O HIS A 152 13992 10894 11700 -1296 -1064 -647 O ATOM 1212 CB HIS A 152 -236.722 20.839 24.527 1.00 81.34 C ANISOU 1212 CB HIS A 152 12307 8826 9773 -1632 -1334 -817 C ATOM 1213 CG HIS A 152 -237.405 20.115 23.409 1.00 86.65 C ANISOU 1213 CG HIS A 152 13197 9475 10252 -1876 -1448 -940 C ATOM 1214 ND1 HIS A 152 -237.349 18.746 23.264 1.00 89.01 N ANISOU 1214 ND1 HIS A 152 13587 9604 10629 -1941 -1380 -1133 N ATOM 1215 CD2 HIS A 152 -238.155 20.572 22.378 1.00 89.83 C ANISOU 1215 CD2 HIS A 152 13753 9994 10384 -2080 -1640 -895 C ATOM 1216 CE1 HIS A 152 -238.039 18.389 22.195 1.00 95.85 C ANISOU 1216 CE1 HIS A 152 14659 10489 11270 -2183 -1517 -1217 C ATOM 1217 NE2 HIS A 152 -238.538 19.479 21.640 1.00 96.77 N ANISOU 1217 NE2 HIS A 152 14817 10784 11165 -2275 -1685 -1068 N ATOM 1218 N ALA A 153 -234.111 21.390 26.299 1.00 76.29 N ANISOU 1218 N ALA A 153 11380 8095 9512 -1173 -886 -841 N ATOM 1219 CA ALA A 153 -233.495 22.055 27.444 1.00 87.86 C ANISOU 1219 CA ALA A 153 12643 9584 11154 -972 -825 -716 C ATOM 1220 C ALA A 153 -232.314 22.917 27.021 1.00 89.06 C ANISOU 1220 C ALA A 153 12828 9795 11216 -922 -644 -779 C ATOM 1221 O ALA A 153 -232.067 23.971 27.620 1.00 80.48 O ANISOU 1221 O ALA A 153 11619 8798 10161 -818 -653 -639 O ATOM 1222 CB ALA A 153 -233.051 21.021 28.478 1.00 84.51 C ANISOU 1222 CB ALA A 153 12097 8995 11018 -840 -757 -745 C ATOM 1223 N ILE A 154 -231.575 22.485 25.998 1.00 85.46 N ANISOU 1223 N ILE A 154 12536 9285 10650 -1005 -466 -998 N ATOM 1224 CA ILE A 154 -230.467 23.285 25.489 1.00 83.30 C ANISOU 1224 CA ILE A 154 12301 9071 10276 -987 -272 -1069 C ATOM 1225 C ILE A 154 -230.982 24.581 24.877 1.00 90.96 C ANISOU 1225 C ILE A 154 13359 10222 10981 -1095 -392 -928 C ATOM 1226 O ILE A 154 -230.393 25.651 25.071 1.00100.11 O ANISOU 1226 O ILE A 154 14448 11460 12128 -1024 -332 -844 O ATOM 1227 CB ILE A 154 -229.643 22.462 24.483 1.00 76.75 C ANISOU 1227 CB ILE A 154 11637 8140 9384 -1073 -31 -1355 C ATOM 1228 CG1 ILE A 154 -228.965 21.294 25.197 1.00 72.02 C ANISOU 1228 CG1 ILE A 154 10909 7336 9117 -925 97 -1477 C ATOM 1229 CG2 ILE A 154 -228.616 23.337 23.785 1.00 70.25 C ANISOU 1229 CG2 ILE A 154 10880 7401 8411 -1101 178 -1430 C ATOM 1230 CD1 ILE A 154 -228.371 20.276 24.259 1.00 69.92 C ANISOU 1230 CD1 ILE A 154 10797 6930 8838 -1008 321 -1779 C ATOM 1231 N MET A 155 -232.088 24.509 24.131 1.00 87.99 N ANISOU 1231 N MET A 155 13132 9902 10399 -1273 -578 -892 N ATOM 1232 CA MET A 155 -232.681 25.722 23.575 1.00 81.83 C ANISOU 1232 CA MET A 155 12424 9276 9391 -1374 -739 -725 C ATOM 1233 C MET A 155 -233.049 26.709 24.676 1.00 80.24 C ANISOU 1233 C MET A 155 11996 9135 9355 -1217 -868 -487 C ATOM 1234 O MET A 155 -232.809 27.916 24.545 1.00 89.53 O ANISOU 1234 O MET A 155 13166 10403 10448 -1203 -874 -376 O ATOM 1235 CB MET A 155 -233.913 25.377 22.739 1.00 85.04 C ANISOU 1235 CB MET A 155 12993 9719 9601 -1583 -967 -701 C ATOM 1236 CG MET A 155 -233.607 24.737 21.397 1.00104.77 C ANISOU 1236 CG MET A 155 15779 12198 11829 -1796 -857 -926 C ATOM 1237 SD MET A 155 -235.089 24.072 20.612 1.00125.22 S ANISOU 1237 SD MET A 155 18539 14803 14237 -2042 -1154 -912 S ATOM 1238 CE MET A 155 -236.211 25.463 20.751 1.00122.67 C ANISOU 1238 CE MET A 155 18108 14632 13868 -2051 -1492 -567 C ATOM 1239 N GLY A 156 -233.621 26.213 25.775 1.00 70.96 N ANISOU 1239 N GLY A 156 10643 7905 8415 -1106 -961 -411 N ATOM 1240 CA GLY A 156 -234.016 27.101 26.857 1.00 75.09 C ANISOU 1240 CA GLY A 156 10961 8483 9088 -968 -1063 -209 C ATOM 1241 C GLY A 156 -232.836 27.812 27.488 1.00 88.03 C ANISOU 1241 C GLY A 156 12498 10127 10823 -816 -892 -205 C ATOM 1242 O GLY A 156 -232.904 29.008 27.785 1.00 94.50 O ANISOU 1242 O GLY A 156 13243 11023 11638 -762 -943 -66 O ATOM 1243 N VAL A 157 -231.735 27.089 27.698 1.00 89.07 N ANISOU 1243 N VAL A 157 12618 10165 11061 -746 -695 -359 N ATOM 1244 CA VAL A 157 -230.532 27.707 28.246 1.00 77.81 C ANISOU 1244 CA VAL A 157 11087 8740 9738 -614 -538 -364 C ATOM 1245 C VAL A 157 -229.945 28.701 27.250 1.00 78.94 C ANISOU 1245 C VAL A 157 11351 8966 9677 -697 -446 -387 C ATOM 1246 O VAL A 157 -229.612 29.838 27.606 1.00 82.37 O ANISOU 1246 O VAL A 157 11709 9464 10126 -634 -441 -280 O ATOM 1247 CB VAL A 157 -229.508 26.628 28.644 1.00 62.07 C ANISOU 1247 CB VAL A 157 9035 6610 7938 -523 -367 -519 C ATOM 1248 CG1 VAL A 157 -228.190 27.267 29.052 1.00 56.76 C ANISOU 1248 CG1 VAL A 157 8255 5941 7371 -408 -208 -536 C ATOM 1249 CG2 VAL A 157 -230.061 25.775 29.776 1.00 60.21 C ANISOU 1249 CG2 VAL A 157 8676 6292 7909 -439 -475 -452 C ATOM 1250 N ALA A 158 -229.818 28.290 25.985 1.00 69.01 N ANISOU 1250 N ALA A 158 10296 7707 8217 -855 -367 -528 N ATOM 1251 CA ALA A 158 -229.318 29.202 24.960 1.00 64.28 C ANISOU 1251 CA ALA A 158 9844 7195 7386 -969 -277 -542 C ATOM 1252 C ALA A 158 -230.240 30.400 24.784 1.00 85.01 C ANISOU 1252 C ALA A 158 12496 9928 9874 -1027 -499 -321 C ATOM 1253 O ALA A 158 -229.788 31.483 24.395 1.00 97.16 O ANISOU 1253 O ALA A 158 14081 11534 11301 -1062 -455 -256 O ATOM 1254 CB ALA A 158 -229.146 28.461 23.634 1.00 57.04 C ANISOU 1254 CB ALA A 158 9169 6261 6244 -1156 -159 -741 C ATOM 1255 N PHE A 159 -231.532 30.226 25.069 1.00 87.35 N ANISOU 1255 N PHE A 159 12753 10235 10203 -1039 -738 -201 N ATOM 1256 CA PHE A 159 -232.469 31.340 24.979 1.00 82.82 C ANISOU 1256 CA PHE A 159 12165 9742 9561 -1072 -962 15 C ATOM 1257 C PHE A 159 -232.175 32.396 26.036 1.00 71.62 C ANISOU 1257 C PHE A 159 10553 8336 8325 -901 -949 143 C ATOM 1258 O PHE A 159 -232.282 33.599 25.766 1.00 79.14 O ANISOU 1258 O PHE A 159 11524 9340 9204 -922 -1022 277 O ATOM 1259 CB PHE A 159 -233.902 30.829 25.114 1.00 77.00 C ANISOU 1259 CB PHE A 159 11389 9001 8867 -1113 -1205 100 C ATOM 1260 CG PHE A 159 -234.923 31.917 25.209 1.00 63.27 C ANISOU 1260 CG PHE A 159 9572 7321 7145 -1110 -1440 326 C ATOM 1261 CD1 PHE A 159 -235.324 32.606 24.078 1.00 60.75 C ANISOU 1261 CD1 PHE A 159 9416 7065 6602 -1269 -1587 423 C ATOM 1262 CD2 PHE A 159 -235.486 32.251 26.429 1.00 52.65 C ANISOU 1262 CD2 PHE A 159 7994 5962 6048 -953 -1511 442 C ATOM 1263 CE1 PHE A 159 -236.266 33.611 24.160 1.00 59.28 C ANISOU 1263 CE1 PHE A 159 9140 6910 6474 -1253 -1817 641 C ATOM 1264 CE2 PHE A 159 -236.430 33.256 26.519 1.00 49.87 C ANISOU 1264 CE2 PHE A 159 7550 5646 5751 -937 -1709 635 C ATOM 1265 CZ PHE A 159 -236.821 33.936 25.382 1.00 51.64 C ANISOU 1265 CZ PHE A 159 7917 5917 5787 -1079 -1869 739 C ATOM 1266 N THR A 160 -231.811 31.968 27.248 1.00 61.06 N ANISOU 1266 N THR A 160 9037 6941 7221 -739 -867 106 N ATOM 1267 CA THR A 160 -231.462 32.929 28.290 1.00 67.99 C ANISOU 1267 CA THR A 160 9749 7830 8256 -591 -845 204 C ATOM 1268 C THR A 160 -230.251 33.758 27.886 1.00 75.50 C ANISOU 1268 C THR A 160 10751 8803 9135 -599 -684 170 C ATOM 1269 O THR A 160 -230.181 34.956 28.184 1.00 82.28 O ANISOU 1269 O THR A 160 11552 9691 10020 -554 -717 286 O ATOM 1270 CB THR A 160 -231.192 32.210 29.613 1.00 80.34 C ANISOU 1270 CB THR A 160 11146 9332 10048 -446 -786 164 C ATOM 1271 OG1 THR A 160 -230.048 31.357 29.472 1.00 93.46 O ANISOU 1271 OG1 THR A 160 12836 10930 11744 -432 -601 -4 O ATOM 1272 CG2 THR A 160 -232.393 31.375 30.021 1.00 80.87 C ANISOU 1272 CG2 THR A 160 11164 9376 10187 -455 -931 203 C ATOM 1273 N TRP A 161 -229.286 33.140 27.203 1.00 75.59 N ANISOU 1273 N TRP A 161 10864 8791 9067 -661 -496 3 N ATOM 1274 CA TRP A 161 -228.105 33.880 26.773 1.00 75.70 C ANISOU 1274 CA TRP A 161 10917 8827 9018 -685 -318 -40 C ATOM 1275 C TRP A 161 -228.470 34.959 25.763 1.00 80.96 C ANISOU 1275 C TRP A 161 11742 9567 9450 -828 -402 77 C ATOM 1276 O TRP A 161 -227.926 36.069 25.805 1.00 92.53 O ANISOU 1276 O TRP A 161 13186 11057 10913 -816 -356 153 O ATOM 1277 CB TRP A 161 -227.071 32.920 26.191 1.00 69.63 C ANISOU 1277 CB TRP A 161 10217 8013 8227 -729 -80 -260 C ATOM 1278 CG TRP A 161 -226.518 31.968 27.200 1.00 75.44 C ANISOU 1278 CG TRP A 161 10780 8654 9228 -576 3 -356 C ATOM 1279 CD1 TRP A 161 -226.565 32.091 28.560 1.00 73.26 C ANISOU 1279 CD1 TRP A 161 10309 8352 9175 -418 -81 -262 C ATOM 1280 CD2 TRP A 161 -225.839 30.739 26.931 1.00 89.51 C ANISOU 1280 CD2 TRP A 161 12576 10346 11086 -573 177 -559 C ATOM 1281 NE1 TRP A 161 -225.951 31.015 29.153 1.00 75.84 N ANISOU 1281 NE1 TRP A 161 10532 8582 9704 -322 8 -373 N ATOM 1282 CE2 TRP A 161 -225.497 30.169 28.174 1.00 94.19 C ANISOU 1282 CE2 TRP A 161 12969 10855 11965 -404 167 -557 C ATOM 1283 CE3 TRP A 161 -225.484 30.064 25.760 1.00 89.29 C ANISOU 1283 CE3 TRP A 161 12716 10293 10915 -703 345 -749 C ATOM 1284 CZ2 TRP A 161 -224.818 28.957 28.277 1.00 99.54 C ANISOU 1284 CZ2 TRP A 161 13593 11409 12817 -346 303 -721 C ATOM 1285 CZ3 TRP A 161 -224.811 28.861 25.864 1.00 87.90 C ANISOU 1285 CZ3 TRP A 161 12486 9995 10917 -642 507 -939 C ATOM 1286 CH2 TRP A 161 -224.485 28.320 27.113 1.00 89.89 C ANISOU 1286 CH2 TRP A 161 12521 10150 11484 -458 477 -916 C ATOM 1287 N VAL A 162 -229.399 34.655 24.854 1.00 72.70 N ANISOU 1287 N VAL A 162 10862 8552 8209 -975 -542 104 N ATOM 1288 CA VAL A 162 -229.844 35.651 23.884 1.00 71.79 C ANISOU 1288 CA VAL A 162 10909 8502 7867 -1124 -669 246 C ATOM 1289 C VAL A 162 -230.577 36.791 24.583 1.00 80.18 C ANISOU 1289 C VAL A 162 11831 9565 9067 -1023 -869 466 C ATOM 1290 O VAL A 162 -230.379 37.967 24.256 1.00 90.98 O ANISOU 1290 O VAL A 162 13246 10953 10368 -1062 -895 588 O ATOM 1291 CB VAL A 162 -230.716 34.988 22.803 1.00 63.41 C ANISOU 1291 CB VAL A 162 10052 7470 6569 -1312 -808 230 C ATOM 1292 CG1 VAL A 162 -231.335 36.037 21.895 1.00 59.71 C ANISOU 1292 CG1 VAL A 162 9738 7063 5885 -1464 -1007 424 C ATOM 1293 CG2 VAL A 162 -229.889 34.001 21.992 1.00 57.08 C ANISOU 1293 CG2 VAL A 162 9421 6662 5606 -1432 -571 -11 C ATOM 1294 N MET A 163 -231.425 36.467 25.561 1.00 83.59 N ANISOU 1294 N MET A 163 12091 9967 9703 -897 -1000 515 N ATOM 1295 CA MET A 163 -232.154 37.512 26.275 1.00 88.91 C ANISOU 1295 CA MET A 163 12618 10631 10533 -794 -1162 697 C ATOM 1296 C MET A 163 -231.217 38.366 27.120 1.00 87.48 C ANISOU 1296 C MET A 163 12317 10426 10495 -667 -1021 699 C ATOM 1297 O MET A 163 -231.343 39.596 27.147 1.00 88.12 O ANISOU 1297 O MET A 163 12377 10499 10605 -650 -1093 834 O ATOM 1298 CB MET A 163 -233.243 36.898 27.152 1.00 86.06 C ANISOU 1298 CB MET A 163 12097 10248 10356 -701 -1292 725 C ATOM 1299 CG MET A 163 -234.406 36.312 26.379 1.00 79.03 C ANISOU 1299 CG MET A 163 11291 9377 9362 -829 -1494 771 C ATOM 1300 SD MET A 163 -235.143 37.509 25.252 1.00 80.31 S ANISOU 1300 SD MET A 163 11574 9571 9371 -962 -1736 982 S ATOM 1301 CE MET A 163 -234.595 36.864 23.671 1.00 82.63 C ANISOU 1301 CE MET A 163 12188 9916 9294 -1208 -1681 872 C ATOM 1302 N ALA A 164 -230.278 37.729 27.821 1.00 88.26 N ANISOU 1302 N ALA A 164 12332 10503 10698 -579 -834 555 N ATOM 1303 CA ALA A 164 -229.341 38.478 28.650 1.00 80.79 C ANISOU 1303 CA ALA A 164 11271 9538 9889 -472 -715 550 C ATOM 1304 C ALA A 164 -228.431 39.352 27.798 1.00 82.96 C ANISOU 1304 C ALA A 164 11661 9831 10028 -569 -608 561 C ATOM 1305 O ALA A 164 -228.158 40.504 28.153 1.00 91.62 O ANISOU 1305 O ALA A 164 12705 10914 11194 -528 -613 648 O ATOM 1306 CB ALA A 164 -228.519 37.521 29.507 1.00 69.49 C ANISOU 1306 CB ALA A 164 9728 8076 8598 -374 -568 407 C ATOM 1307 N LEU A 165 -227.950 38.823 26.671 1.00 77.38 N ANISOU 1307 N LEU A 165 11121 9153 9126 -709 -499 467 N ATOM 1308 CA LEU A 165 -227.182 39.653 25.750 1.00 76.68 C ANISOU 1308 CA LEU A 165 11169 9093 8874 -836 -392 488 C ATOM 1309 C LEU A 165 -228.036 40.769 25.166 1.00 89.02 C ANISOU 1309 C LEU A 165 12835 10668 10321 -922 -597 696 C ATOM 1310 O LEU A 165 -227.529 41.864 24.904 1.00 92.33 O ANISOU 1310 O LEU A 165 13296 11083 10702 -968 -561 782 O ATOM 1311 CB LEU A 165 -226.592 38.797 24.632 1.00 71.81 C ANISOU 1311 CB LEU A 165 10726 8508 8050 -987 -218 329 C ATOM 1312 CG LEU A 165 -225.428 37.882 25.008 1.00 70.24 C ANISOU 1312 CG LEU A 165 10427 8277 7984 -916 35 116 C ATOM 1313 CD1 LEU A 165 -225.073 37.006 23.824 1.00 67.93 C ANISOU 1313 CD1 LEU A 165 10323 8005 7483 -1074 202 -53 C ATOM 1314 CD2 LEU A 165 -224.224 38.694 25.459 1.00 74.94 C ANISOU 1314 CD2 LEU A 165 10903 8862 8711 -859 195 110 C ATOM 1315 N ALA A 166 -229.333 40.517 24.965 1.00 89.29 N ANISOU 1315 N ALA A 166 12900 10707 10317 -945 -824 789 N ATOM 1316 CA ALA A 166 -230.229 41.551 24.459 1.00 81.62 C ANISOU 1316 CA ALA A 166 11998 9730 9283 -1010 -1057 1006 C ATOM 1317 C ALA A 166 -230.350 42.731 25.411 1.00 86.69 C ANISOU 1317 C ALA A 166 12470 10309 10160 -863 -1117 1128 C ATOM 1318 O ALA A 166 -230.749 43.819 24.984 1.00 92.70 O ANISOU 1318 O ALA A 166 13286 11039 10897 -911 -1262 1306 O ATOM 1319 CB ALA A 166 -231.614 40.963 24.193 1.00 74.27 C ANISOU 1319 CB ALA A 166 11084 8810 8324 -1046 -1298 1074 C ATOM 1320 N CYS A 167 -230.023 42.545 26.687 1.00 84.45 N ANISOU 1320 N CYS A 167 11991 9996 10101 -693 -1017 1037 N ATOM 1321 CA CYS A 167 -230.072 43.627 27.660 1.00 82.40 C ANISOU 1321 CA CYS A 167 11581 9674 10056 -561 -1047 1116 C ATOM 1322 C CYS A 167 -228.696 44.188 27.985 1.00 86.42 C ANISOU 1322 C CYS A 167 12067 10168 10600 -544 -849 1048 C ATOM 1323 O CYS A 167 -228.543 45.406 28.116 1.00 88.27 O ANISOU 1323 O CYS A 167 12287 10349 10902 -532 -875 1147 O ATOM 1324 CB CYS A 167 -230.742 43.146 28.950 1.00 77.16 C ANISOU 1324 CB CYS A 167 10720 8989 9607 -400 -1087 1074 C ATOM 1325 SG CYS A 167 -230.293 44.105 30.415 1.00 84.06 S ANISOU 1325 SG CYS A 167 11417 9802 10721 -241 -1009 1061 S ATOM 1326 N ALA A 168 -227.689 43.322 28.096 1.00 83.22 N ANISOU 1326 N ALA A 168 11652 9800 10170 -547 -655 882 N ATOM 1327 CA ALA A 168 -226.372 43.743 28.553 1.00 79.26 C ANISOU 1327 CA ALA A 168 11082 9284 9750 -518 -474 807 C ATOM 1328 C ALA A 168 -225.496 44.297 27.436 1.00 78.71 C ANISOU 1328 C ALA A 168 11162 9235 9511 -676 -351 821 C ATOM 1329 O ALA A 168 -224.581 45.079 27.718 1.00 76.03 O ANISOU 1329 O ALA A 168 10771 8870 9248 -673 -246 819 O ATOM 1330 CB ALA A 168 -225.660 42.570 29.235 1.00 80.73 C ANISOU 1330 CB ALA A 168 11157 9485 10032 -439 -334 634 C ATOM 1331 N ALA A 169 -225.750 43.923 26.185 1.00 80.11 N ANISOU 1331 N ALA A 169 11530 9459 9451 -831 -359 833 N ATOM 1332 CA ALA A 169 -224.897 44.332 25.071 1.00 85.77 C ANISOU 1332 CA ALA A 169 12413 10208 9969 -1009 -210 832 C ATOM 1333 C ALA A 169 -225.225 45.708 24.482 1.00 86.07 C ANISOU 1333 C ALA A 169 12572 10217 9915 -1111 -341 1044 C ATOM 1334 O ALA A 169 -224.290 46.427 24.106 1.00 81.02 O ANISOU 1334 O ALA A 169 11987 9574 9224 -1206 -199 1061 O ATOM 1335 CB ALA A 169 -224.939 43.280 23.960 1.00 87.23 C ANISOU 1335 CB ALA A 169 12779 10460 9906 -1157 -134 729 C ATOM 1336 N PRO A 170 -226.493 46.110 24.350 1.00 84.91 N ANISOU 1336 N PRO A 170 12465 10038 9758 -1102 -605 1216 N ATOM 1337 CA PRO A 170 -226.798 47.421 23.732 1.00 81.99 C ANISOU 1337 CA PRO A 170 12215 9619 9320 -1201 -749 1438 C ATOM 1338 C PRO A 170 -226.068 48.582 24.391 1.00 71.48 C ANISOU 1338 C PRO A 170 10779 8207 8172 -1137 -673 1478 C ATOM 1339 O PRO A 170 -225.607 49.488 23.680 1.00 70.63 O ANISOU 1339 O PRO A 170 10806 8077 7954 -1277 -646 1592 O ATOM 1340 CB PRO A 170 -228.319 47.543 23.899 1.00 84.48 C ANISOU 1340 CB PRO A 170 12487 9888 9725 -1126 -1052 1587 C ATOM 1341 CG PRO A 170 -228.788 46.154 23.842 1.00 85.24 C ANISOU 1341 CG PRO A 170 12581 10056 9749 -1119 -1060 1461 C ATOM 1342 CD PRO A 170 -227.731 45.323 24.530 1.00 83.98 C ANISOU 1342 CD PRO A 170 12311 9930 9667 -1038 -793 1227 C ATOM 1343 N PRO A 171 -225.941 48.626 25.726 1.00 65.53 N ANISOU 1343 N PRO A 171 9804 7407 7687 -946 -640 1394 N ATOM 1344 CA PRO A 171 -225.156 49.721 26.325 1.00 60.77 C ANISOU 1344 CA PRO A 171 9118 6728 7243 -909 -560 1414 C ATOM 1345 C PRO A 171 -223.711 49.768 25.862 1.00 70.46 C ANISOU 1345 C PRO A 171 10399 8000 8373 -1036 -312 1326 C ATOM 1346 O PRO A 171 -223.078 50.825 25.971 1.00 84.13 O ANISOU 1346 O PRO A 171 12119 9668 10177 -1073 -262 1386 O ATOM 1347 CB PRO A 171 -225.253 49.443 27.829 1.00 68.13 C ANISOU 1347 CB PRO A 171 9824 7632 8429 -704 -555 1299 C ATOM 1348 CG PRO A 171 -226.533 48.736 27.977 1.00 75.72 C ANISOU 1348 CG PRO A 171 10757 8610 9403 -627 -718 1320 C ATOM 1349 CD PRO A 171 -226.619 47.844 26.780 1.00 75.75 C ANISOU 1349 CD PRO A 171 10926 8702 9152 -769 -704 1306 C ATOM 1350 N LEU A 172 -223.166 48.667 25.346 1.00 72.55 N ANISOU 1350 N LEU A 172 10712 8362 8493 -1107 -144 1180 N ATOM 1351 CA LEU A 172 -221.799 48.684 24.843 1.00 69.04 C ANISOU 1351 CA LEU A 172 10301 7958 7971 -1232 118 1085 C ATOM 1352 C LEU A 172 -221.695 49.267 23.440 1.00 79.40 C ANISOU 1352 C LEU A 172 11866 9297 9007 -1470 148 1210 C ATOM 1353 O LEU A 172 -220.589 49.624 23.015 1.00 91.96 O ANISOU 1353 O LEU A 172 13491 10906 10544 -1595 363 1172 O ATOM 1354 CB LEU A 172 -221.213 47.270 24.846 1.00 67.25 C ANISOU 1354 CB LEU A 172 10015 7808 7730 -1209 311 862 C ATOM 1355 CG LEU A 172 -220.979 46.588 26.195 1.00 54.39 C ANISOU 1355 CG LEU A 172 8140 6159 6366 -1003 327 726 C ATOM 1356 CD1 LEU A 172 -220.504 45.161 25.984 1.00 56.02 C ANISOU 1356 CD1 LEU A 172 8318 6418 6548 -996 496 529 C ATOM 1357 CD2 LEU A 172 -219.976 47.365 27.027 1.00 51.92 C ANISOU 1357 CD2 LEU A 172 7662 5800 6265 -950 410 709 C ATOM 1358 N VAL A 173 -222.807 49.376 22.712 1.00 85.64 N ANISOU 1358 N VAL A 173 12832 10088 9619 -1546 -67 1366 N ATOM 1359 CA VAL A 173 -222.771 49.771 21.312 1.00 90.67 C ANISOU 1359 CA VAL A 173 13745 10765 9942 -1798 -59 1491 C ATOM 1360 C VAL A 173 -223.579 51.041 21.053 1.00 92.13 C ANISOU 1360 C VAL A 173 14026 10853 10126 -1840 -332 1775 C ATOM 1361 O VAL A 173 -223.769 51.426 19.898 1.00108.71 O ANISOU 1361 O VAL A 173 16373 12974 11956 -2053 -401 1932 O ATOM 1362 CB VAL A 173 -223.250 48.620 20.402 1.00 90.27 C ANISOU 1362 CB VAL A 173 13870 10816 9613 -1914 -63 1415 C ATOM 1363 CG1 VAL A 173 -222.616 48.706 19.027 1.00 99.43 C ANISOU 1363 CG1 VAL A 173 15302 12055 10422 -2200 112 1423 C ATOM 1364 CG2 VAL A 173 -222.933 47.271 21.038 1.00 85.80 C ANISOU 1364 CG2 VAL A 173 13140 10294 9167 -1775 97 1153 C ATOM 1365 N GLY A 174 -224.062 51.706 22.101 1.00 82.83 N ANISOU 1365 N GLY A 174 12664 9561 9246 -1647 -490 1847 N ATOM 1366 CA GLY A 174 -224.679 53.011 21.945 1.00 88.87 C ANISOU 1366 CA GLY A 174 13489 10200 10079 -1668 -718 2103 C ATOM 1367 C GLY A 174 -226.146 53.108 22.308 1.00 97.74 C ANISOU 1367 C GLY A 174 14539 11247 11350 -1524 -1030 2230 C ATOM 1368 O GLY A 174 -226.729 54.187 22.126 1.00107.87 O ANISOU 1368 O GLY A 174 15863 12406 12717 -1533 -1239 2453 O ATOM 1369 N TRP A 175 -226.802 52.053 22.788 1.00 87.41 N ANISOU 1369 N TRP A 175 13118 9996 10096 -1397 -1077 2108 N ATOM 1370 CA TRP A 175 -228.172 52.150 23.291 1.00 77.18 C ANISOU 1370 CA TRP A 175 11703 8626 8996 -1243 -1344 2207 C ATOM 1371 C TRP A 175 -228.104 52.073 24.811 1.00 77.78 C ANISOU 1371 C TRP A 175 11515 8655 9384 -1008 -1258 2052 C ATOM 1372 O TRP A 175 -227.838 51.003 25.368 1.00 80.46 O ANISOU 1372 O TRP A 175 11759 9082 9731 -935 -1123 1855 O ATOM 1373 CB TRP A 175 -229.069 51.053 22.720 1.00 76.72 C ANISOU 1373 CB TRP A 175 11715 8663 8773 -1291 -1478 2201 C ATOM 1374 CG TRP A 175 -230.530 51.338 22.892 1.00 85.66 C ANISOU 1374 CG TRP A 175 12757 9712 10079 -1190 -1789 2366 C ATOM 1375 CD1 TRP A 175 -231.103 52.543 23.184 1.00 77.16 C ANISOU 1375 CD1 TRP A 175 11598 8480 9240 -1104 -1967 2549 C ATOM 1376 CD2 TRP A 175 -231.603 50.397 22.794 1.00 94.53 C ANISOU 1376 CD2 TRP A 175 13843 10890 11183 -1165 -1952 2356 C ATOM 1377 NE1 TRP A 175 -232.467 52.410 23.270 1.00 80.04 N ANISOU 1377 NE1 TRP A 175 11861 8802 9749 -1018 -2226 2654 N ATOM 1378 CE2 TRP A 175 -232.800 51.102 23.035 1.00 96.45 C ANISOU 1378 CE2 TRP A 175 13964 11013 11667 -1060 -2226 2543 C ATOM 1379 CE3 TRP A 175 -231.669 49.026 22.525 1.00 90.06 C ANISOU 1379 CE3 TRP A 175 13330 10453 10438 -1222 -1892 2205 C ATOM 1380 CZ2 TRP A 175 -234.048 50.481 23.014 1.00102.33 C ANISOU 1380 CZ2 TRP A 175 14625 11775 12480 -1017 -2441 2587 C ATOM 1381 CZ3 TRP A 175 -232.907 48.414 22.505 1.00 90.35 C ANISOU 1381 CZ3 TRP A 175 13302 10502 10525 -1187 -2111 2249 C ATOM 1382 CH2 TRP A 175 -234.079 49.140 22.747 1.00 96.31 C ANISOU 1382 CH2 TRP A 175 13923 11148 11521 -1088 -2383 2441 C ATOM 1383 N SER A 176 -228.337 53.214 25.470 1.00 79.03 N ANISOU 1383 N SER A 176 11567 8668 9792 -901 -1338 2142 N ATOM 1384 CA SER A 176 -228.026 53.415 26.883 1.00 82.14 C ANISOU 1384 CA SER A 176 11753 9008 10449 -722 -1226 1997 C ATOM 1385 C SER A 176 -226.517 53.317 27.082 1.00 85.60 C ANISOU 1385 C SER A 176 12195 9503 10826 -782 -966 1847 C ATOM 1386 O SER A 176 -225.758 53.393 26.108 1.00 98.03 O ANISOU 1386 O SER A 176 13928 11126 12194 -959 -872 1884 O ATOM 1387 CB SER A 176 -228.774 52.417 27.774 1.00 80.84 C ANISOU 1387 CB SER A 176 11425 8895 10396 -562 -1249 1867 C ATOM 1388 OG SER A 176 -228.563 52.703 29.143 1.00 81.84 O ANISOU 1388 OG SER A 176 11374 8965 10755 -408 -1160 1745 O ATOM 1389 N ARG A 177 -226.069 53.152 28.323 1.00 66.79 N ANISOU 1389 N ARG A 177 9641 7117 8620 -648 -850 1682 N ATOM 1390 CA ARG A 177 -224.639 53.162 28.610 1.00 73.57 C ANISOU 1390 CA ARG A 177 10467 8012 9473 -696 -633 1554 C ATOM 1391 C ARG A 177 -224.408 52.610 30.010 1.00 72.66 C ANISOU 1391 C ARG A 177 10162 7920 9525 -540 -560 1373 C ATOM 1392 O ARG A 177 -225.335 52.496 30.816 1.00 75.50 O ANISOU 1392 O ARG A 177 10425 8246 10014 -403 -664 1359 O ATOM 1393 CB ARG A 177 -224.058 54.573 28.488 1.00 75.69 C ANISOU 1393 CB ARG A 177 10781 8162 9816 -770 -617 1655 C ATOM 1394 CG ARG A 177 -224.684 55.562 29.447 1.00 71.86 C ANISOU 1394 CG ARG A 177 10193 7523 9589 -634 -736 1696 C ATOM 1395 CD ARG A 177 -224.007 56.915 29.381 1.00 81.34 C ANISOU 1395 CD ARG A 177 11435 8592 10877 -712 -707 1776 C ATOM 1396 NE ARG A 177 -224.566 57.823 30.378 1.00 85.92 N ANISOU 1396 NE ARG A 177 11913 9011 11720 -575 -796 1776 N ATOM 1397 CZ ARG A 177 -224.121 59.052 30.606 1.00 83.13 C ANISOU 1397 CZ ARG A 177 11569 8508 11509 -607 -786 1819 C ATOM 1398 NH1 ARG A 177 -223.102 59.531 29.906 1.00 91.04 N ANISOU 1398 NH1 ARG A 177 12672 9506 12414 -778 -695 1881 N ATOM 1399 NH2 ARG A 177 -224.696 59.801 31.535 1.00 88.61 N ANISOU 1399 NH2 ARG A 177 12172 9050 12445 -476 -854 1791 N ATOM 1400 N TYR A 178 -223.147 52.282 30.292 1.00 65.02 N ANISOU 1400 N TYR A 178 9138 7009 8558 -572 -381 1241 N ATOM 1401 CA TYR A 178 -222.721 51.845 31.617 1.00 67.25 C ANISOU 1401 CA TYR A 178 9252 7310 8990 -452 -323 1088 C ATOM 1402 C TYR A 178 -222.032 53.004 32.328 1.00 73.25 C ANISOU 1402 C TYR A 178 9951 7977 9905 -453 -293 1079 C ATOM 1403 O TYR A 178 -221.055 53.561 31.815 1.00 87.86 O ANISOU 1403 O TYR A 178 11841 9813 11730 -573 -193 1100 O ATOM 1404 CB TYR A 178 -221.782 50.640 31.529 1.00 65.50 C ANISOU 1404 CB TYR A 178 8982 7199 8705 -477 -169 948 C ATOM 1405 CG TYR A 178 -222.478 49.335 31.212 1.00 61.54 C ANISOU 1405 CG TYR A 178 8507 6776 8099 -443 -200 910 C ATOM 1406 CD1 TYR A 178 -223.340 48.748 32.126 1.00 63.00 C ANISOU 1406 CD1 TYR A 178 8606 6965 8366 -310 -300 875 C ATOM 1407 CD2 TYR A 178 -222.266 48.687 30.002 1.00 68.12 C ANISOU 1407 CD2 TYR A 178 9459 7676 8746 -558 -117 901 C ATOM 1408 CE1 TYR A 178 -223.981 47.559 31.843 1.00 67.51 C ANISOU 1408 CE1 TYR A 178 9200 7597 8853 -289 -332 844 C ATOM 1409 CE2 TYR A 178 -222.901 47.493 29.710 1.00 73.78 C ANISOU 1409 CE2 TYR A 178 10210 8454 9371 -537 -148 854 C ATOM 1410 CZ TYR A 178 -223.757 46.935 30.636 1.00 68.74 C ANISOU 1410 CZ TYR A 178 9475 7810 8834 -401 -263 831 C ATOM 1411 OH TYR A 178 -224.395 45.749 30.358 1.00 56.04 O ANISOU 1411 OH TYR A 178 7897 6251 7146 -389 -298 788 O ATOM 1412 N ILE A 179 -222.545 53.366 33.500 1.00 60.37 N ANISOU 1412 N ILE A 179 8229 6281 8427 -333 -369 1041 N ATOM 1413 CA ILE A 179 -221.955 54.427 34.313 1.00 57.16 C ANISOU 1413 CA ILE A 179 7770 5779 8170 -333 -349 1006 C ATOM 1414 C ILE A 179 -221.884 53.945 35.755 1.00 59.14 C ANISOU 1414 C ILE A 179 7894 6063 8513 -227 -347 862 C ATOM 1415 O ILE A 179 -222.621 53.032 36.158 1.00 62.98 O ANISOU 1415 O ILE A 179 8344 6611 8975 -137 -387 823 O ATOM 1416 CB ILE A 179 -222.766 55.742 34.222 1.00 65.21 C ANISOU 1416 CB ILE A 179 8849 6639 9290 -317 -456 1125 C ATOM 1417 CG1 ILE A 179 -224.170 55.545 34.792 1.00 78.73 C ANISOU 1417 CG1 ILE A 179 10516 8320 11077 -175 -567 1125 C ATOM 1418 CG2 ILE A 179 -222.830 56.251 32.791 1.00 58.72 C ANISOU 1418 CG2 ILE A 179 8170 5779 8363 -440 -487 1298 C ATOM 1419 CD1 ILE A 179 -224.942 56.832 34.947 1.00 90.35 C ANISOU 1419 CD1 ILE A 179 12002 9611 12717 -128 -659 1207 C ATOM 1420 N PRO A 180 -220.998 54.532 36.557 1.00 61.35 N ANISOU 1420 N PRO A 180 8115 6304 8893 -252 -307 787 N ATOM 1421 CA PRO A 180 -221.019 54.246 37.996 1.00 57.64 C ANISOU 1421 CA PRO A 180 7554 5853 8492 -171 -331 664 C ATOM 1422 C PRO A 180 -222.348 54.666 38.607 1.00 70.36 C ANISOU 1422 C PRO A 180 9182 7388 10165 -71 -407 667 C ATOM 1423 O PRO A 180 -222.830 55.780 38.387 1.00 88.31 O ANISOU 1423 O PRO A 180 11504 9530 12521 -71 -440 729 O ATOM 1424 CB PRO A 180 -219.852 55.077 38.541 1.00 55.56 C ANISOU 1424 CB PRO A 180 7252 5538 8321 -249 -295 607 C ATOM 1425 CG PRO A 180 -218.936 55.244 37.378 1.00 56.27 C ANISOU 1425 CG PRO A 180 7365 5640 8375 -368 -212 673 C ATOM 1426 CD PRO A 180 -219.838 55.357 36.179 1.00 63.67 C ANISOU 1426 CD PRO A 180 8420 6551 9222 -376 -234 805 C ATOM 1427 N GLU A 181 -222.944 53.756 39.371 1.00 57.77 N ANISOU 1427 N GLU A 181 7538 5867 8543 13 -427 601 N ATOM 1428 CA GLU A 181 -224.253 53.964 39.967 1.00 66.83 C ANISOU 1428 CA GLU A 181 8680 6963 9751 109 -471 588 C ATOM 1429 C GLU A 181 -224.139 54.100 41.480 1.00 65.08 C ANISOU 1429 C GLU A 181 8420 6739 9569 134 -449 452 C ATOM 1430 O GLU A 181 -223.209 53.575 42.101 1.00 67.85 O ANISOU 1430 O GLU A 181 8740 7170 9870 92 -435 381 O ATOM 1431 CB GLU A 181 -225.199 52.809 39.623 1.00 75.70 C ANISOU 1431 CB GLU A 181 9787 8173 10802 169 -505 627 C ATOM 1432 CG GLU A 181 -224.812 51.484 40.259 1.00 89.51 C ANISOU 1432 CG GLU A 181 11489 10053 12470 180 -483 549 C ATOM 1433 CD GLU A 181 -225.769 50.361 39.907 1.00106.47 C ANISOU 1433 CD GLU A 181 13627 12271 14557 229 -517 587 C ATOM 1434 OE1 GLU A 181 -226.430 50.448 38.852 1.00115.46 O ANISOU 1434 OE1 GLU A 181 14804 13385 15679 226 -561 684 O ATOM 1435 OE2 GLU A 181 -225.864 49.392 40.690 1.00110.04 O ANISOU 1435 OE2 GLU A 181 14038 12798 14975 259 -513 528 O ATOM 1436 N GLY A 182 -225.102 54.811 42.065 1.00 63.77 N ANISOU 1436 N GLY A 182 8255 6475 9498 196 -448 414 N ATOM 1437 CA GLY A 182 -225.173 54.989 43.503 1.00 61.17 C ANISOU 1437 CA GLY A 182 7916 6142 9184 208 -410 271 C ATOM 1438 C GLY A 182 -223.923 55.598 44.102 1.00 67.15 C ANISOU 1438 C GLY A 182 8697 6876 9942 114 -399 190 C ATOM 1439 O GLY A 182 -223.589 56.755 43.832 1.00 76.17 O ANISOU 1439 O GLY A 182 9871 7888 11180 74 -393 198 O ATOM 1440 N MET A 183 -223.220 54.817 44.920 1.00 63.13 N ANISOU 1440 N MET A 183 8170 6483 9334 71 -412 122 N ATOM 1441 CA MET A 183 -221.971 55.261 45.521 1.00 61.56 C ANISOU 1441 CA MET A 183 7976 6279 9134 -30 -431 53 C ATOM 1442 C MET A 183 -220.798 55.214 44.548 1.00 57.11 C ANISOU 1442 C MET A 183 7373 5734 8593 -97 -444 133 C ATOM 1443 O MET A 183 -219.654 55.423 44.970 1.00 46.62 O ANISOU 1443 O MET A 183 6016 4417 7280 -186 -469 89 O ATOM 1444 CB MET A 183 -221.662 54.422 46.762 1.00 60.14 C ANISOU 1444 CB MET A 183 7789 6216 8845 -60 -469 -28 C ATOM 1445 CG MET A 183 -222.677 54.590 47.880 1.00 53.84 C ANISOU 1445 CG MET A 183 7050 5404 8004 -31 -428 -134 C ATOM 1446 SD MET A 183 -222.280 53.600 49.331 1.00 73.22 S ANISOU 1446 SD MET A 183 9529 8002 10289 -99 -489 -203 S ATOM 1447 CE MET A 183 -223.561 54.133 50.461 1.00 79.66 C ANISOU 1447 CE MET A 183 10435 8774 11058 -85 -383 -346 C ATOM 1448 N GLN A 184 -221.061 54.935 43.268 1.00 60.18 N ANISOU 1448 N GLN A 184 7757 6128 8981 -67 -424 247 N ATOM 1449 CA GLN A 184 -220.085 55.061 42.187 1.00 68.49 C ANISOU 1449 CA GLN A 184 8792 7182 10051 -143 -397 321 C ATOM 1450 C GLN A 184 -218.929 54.070 42.319 1.00 71.24 C ANISOU 1450 C GLN A 184 9050 7647 10369 -185 -397 295 C ATOM 1451 O GLN A 184 -217.822 54.333 41.843 1.00 74.07 O ANISOU 1451 O GLN A 184 9365 8002 10777 -270 -362 310 O ATOM 1452 CB GLN A 184 -219.552 56.496 42.094 1.00 69.79 C ANISOU 1452 CB GLN A 184 8991 7211 10314 -227 -383 320 C ATOM 1453 CG GLN A 184 -220.629 57.584 42.109 1.00 50.66 C ANISOU 1453 CG GLN A 184 6644 4633 7971 -178 -390 334 C ATOM 1454 CD GLN A 184 -221.463 57.627 40.839 1.00 53.51 C ANISOU 1454 CD GLN A 184 7048 4955 8327 -136 -397 478 C ATOM 1455 OE1 GLN A 184 -220.944 57.858 39.745 1.00 45.99 O ANISOU 1455 OE1 GLN A 184 6126 3988 7359 -212 -380 583 O ATOM 1456 NE2 GLN A 184 -222.767 57.411 40.981 1.00 63.67 N ANISOU 1456 NE2 GLN A 184 8339 6225 9627 -27 -425 488 N ATOM 1457 N CYS A 185 -219.169 52.922 42.954 1.00 67.69 N ANISOU 1457 N CYS A 185 8563 7295 9859 -126 -434 262 N ATOM 1458 CA CYS A 185 -218.170 51.867 43.061 1.00 59.00 C ANISOU 1458 CA CYS A 185 7364 6289 8763 -144 -449 250 C ATOM 1459 C CYS A 185 -218.444 50.686 42.143 1.00 77.70 C ANISOU 1459 C CYS A 185 9715 8724 11084 -90 -408 300 C ATOM 1460 O CYS A 185 -217.548 49.858 41.943 1.00 90.76 O ANISOU 1460 O CYS A 185 11278 10431 12775 -102 -391 292 O ATOM 1461 CB CYS A 185 -218.071 51.369 44.508 1.00 51.15 C ANISOU 1461 CB CYS A 185 6346 5347 7743 -137 -541 186 C ATOM 1462 SG CYS A 185 -217.460 52.612 45.653 1.00 69.04 S ANISOU 1462 SG CYS A 185 8636 7550 10048 -236 -600 101 S ATOM 1463 N SER A 186 -219.652 50.579 41.597 1.00 80.09 N ANISOU 1463 N SER A 186 10095 9017 11321 -34 -395 346 N ATOM 1464 CA SER A 186 -219.996 49.554 40.625 1.00 80.72 C ANISOU 1464 CA SER A 186 10182 9148 11339 -2 -361 389 C ATOM 1465 C SER A 186 -220.673 50.221 39.436 1.00 72.37 C ANISOU 1465 C SER A 186 9218 8041 10240 -22 -330 469 C ATOM 1466 O SER A 186 -221.005 51.409 39.467 1.00 73.20 O ANISOU 1466 O SER A 186 9371 8060 10381 -38 -347 498 O ATOM 1467 CB SER A 186 -220.908 48.480 41.230 1.00 86.76 C ANISOU 1467 CB SER A 186 10945 9967 12053 79 -414 378 C ATOM 1468 OG SER A 186 -222.261 48.892 41.198 1.00 95.56 O ANISOU 1468 OG SER A 186 12126 11046 13136 123 -438 412 O ATOM 1469 N CYS A 187 -220.887 49.442 38.382 1.00 70.26 N ANISOU 1469 N CYS A 187 8983 7819 9895 -26 -295 507 N ATOM 1470 CA CYS A 187 -221.374 49.969 37.118 1.00 71.10 C ANISOU 1470 CA CYS A 187 9192 7891 9932 -75 -281 599 C ATOM 1471 C CYS A 187 -222.592 49.185 36.654 1.00 72.73 C ANISOU 1471 C CYS A 187 9449 8130 10053 -27 -336 641 C ATOM 1472 O CYS A 187 -222.759 48.008 36.986 1.00 76.99 O ANISOU 1472 O CYS A 187 9947 8733 10573 22 -342 591 O ATOM 1473 CB CYS A 187 -220.267 49.932 36.054 1.00 80.46 C ANISOU 1473 CB CYS A 187 10394 9100 11076 -181 -166 603 C ATOM 1474 SG CYS A 187 -218.993 51.196 36.312 1.00 80.19 S ANISOU 1474 SG CYS A 187 10313 9003 11152 -270 -108 591 S ATOM 1475 N GLY A 188 -223.444 49.857 35.889 1.00 71.62 N ANISOU 1475 N GLY A 188 9397 7940 9877 -47 -392 744 N ATOM 1476 CA GLY A 188 -224.650 49.231 35.389 1.00 66.52 C ANISOU 1476 CA GLY A 188 8794 7319 9163 -15 -470 800 C ATOM 1477 C GLY A 188 -225.358 50.126 34.396 1.00 70.43 C ANISOU 1477 C GLY A 188 9388 7747 9626 -63 -549 939 C ATOM 1478 O GLY A 188 -224.828 51.154 33.971 1.00 62.33 O ANISOU 1478 O GLY A 188 8414 6657 8611 -132 -528 996 O ATOM 1479 N ILE A 189 -226.573 49.711 34.027 1.00 81.92 N ANISOU 1479 N ILE A 189 10865 9212 11050 -32 -656 1004 N ATOM 1480 CA ILE A 189 -227.357 50.472 33.063 1.00 76.87 C ANISOU 1480 CA ILE A 189 10312 8507 10390 -76 -775 1160 C ATOM 1481 C ILE A 189 -227.634 51.867 33.615 1.00 74.61 C ANISOU 1481 C ILE A 189 9984 8083 10282 -21 -820 1212 C ATOM 1482 O ILE A 189 -227.784 52.065 34.828 1.00 82.06 O ANISOU 1482 O ILE A 189 10822 8991 11365 77 -790 1122 O ATOM 1483 CB ILE A 189 -228.675 49.752 32.730 1.00 85.27 C ANISOU 1483 CB ILE A 189 11371 9601 11426 -45 -904 1216 C ATOM 1484 CG1 ILE A 189 -228.446 48.259 32.487 1.00 92.58 C ANISOU 1484 CG1 ILE A 189 12318 10647 12212 -77 -846 1125 C ATOM 1485 CG2 ILE A 189 -229.346 50.383 31.518 1.00 79.02 C ANISOU 1485 CG2 ILE A 189 10688 8758 10579 -122 -1052 1397 C ATOM 1486 CD1 ILE A 189 -227.868 47.934 31.137 1.00 92.16 C ANISOU 1486 CD1 ILE A 189 12418 10647 11950 -223 -808 1152 C ATOM 1487 N ASP A 190 -227.706 52.845 32.714 1.00 71.20 N ANISOU 1487 N ASP A 190 9646 7565 9840 -94 -892 1357 N ATOM 1488 CA ASP A 190 -227.967 54.234 33.085 1.00 73.02 C ANISOU 1488 CA ASP A 190 9851 7634 10260 -48 -943 1420 C ATOM 1489 C ASP A 190 -229.474 54.469 33.087 1.00 77.96 C ANISOU 1489 C ASP A 190 10416 8177 11027 47 -1103 1516 C ATOM 1490 O ASP A 190 -230.072 54.758 32.047 1.00 84.27 O ANISOU 1490 O ASP A 190 11290 8933 11794 -5 -1250 1689 O ATOM 1491 CB ASP A 190 -227.257 55.188 32.131 1.00 76.57 C ANISOU 1491 CB ASP A 190 10430 8013 10649 -181 -945 1544 C ATOM 1492 CG ASP A 190 -227.462 56.648 32.499 1.00 71.95 C ANISOU 1492 CG ASP A 190 9824 7234 10279 -138 -999 1610 C ATOM 1493 OD1 ASP A 190 -227.935 56.923 33.622 1.00 69.62 O ANISOU 1493 OD1 ASP A 190 9408 6868 10175 -8 -989 1513 O ATOM 1494 OD2 ASP A 190 -227.152 57.524 31.663 1.00 73.26 O ANISOU 1494 OD2 ASP A 190 10101 7311 10422 -243 -1043 1755 O ATOM 1495 N TYR A 191 -230.091 54.341 34.260 1.00 78.63 N ANISOU 1495 N TYR A 191 10362 8242 11271 179 -1076 1407 N ATOM 1496 CA TYR A 191 -231.461 54.784 34.477 1.00 78.93 C ANISOU 1496 CA TYR A 191 10300 8172 11519 288 -1190 1472 C ATOM 1497 C TYR A 191 -231.521 56.163 35.115 1.00 83.69 C ANISOU 1497 C TYR A 191 10854 8587 12359 358 -1169 1458 C ATOM 1498 O TYR A 191 -232.616 56.653 35.407 1.00 81.47 O ANISOU 1498 O TYR A 191 10465 8187 12304 466 -1236 1490 O ATOM 1499 CB TYR A 191 -232.213 53.784 35.361 1.00 71.97 C ANISOU 1499 CB TYR A 191 9291 7378 10675 381 -1151 1355 C ATOM 1500 CG TYR A 191 -231.989 52.339 34.992 1.00 72.65 C ANISOU 1500 CG TYR A 191 9420 7640 10541 318 -1136 1323 C ATOM 1501 CD1 TYR A 191 -232.524 51.810 33.826 1.00 85.10 C ANISOU 1501 CD1 TYR A 191 11060 9265 12010 252 -1272 1450 C ATOM 1502 CD2 TYR A 191 -231.252 51.498 35.817 1.00 74.90 C ANISOU 1502 CD2 TYR A 191 9689 8034 10737 320 -998 1166 C ATOM 1503 CE1 TYR A 191 -232.326 50.488 33.485 1.00 96.11 C ANISOU 1503 CE1 TYR A 191 12502 10803 13214 191 -1249 1401 C ATOM 1504 CE2 TYR A 191 -231.049 50.172 35.485 1.00 91.53 C ANISOU 1504 CE2 TYR A 191 11829 10274 12675 271 -984 1133 C ATOM 1505 CZ TYR A 191 -231.588 49.674 34.317 1.00 97.64 C ANISOU 1505 CZ TYR A 191 12667 11085 13347 208 -1099 1241 C ATOM 1506 OH TYR A 191 -231.396 48.354 33.974 1.00 99.41 O ANISOU 1506 OH TYR A 191 12934 11426 13413 155 -1076 1191 O ATOM 1507 N TYR A 192 -230.370 56.798 35.328 1.00 97.91 N ANISOU 1507 N TYR A 192 12722 10349 14131 298 -1072 1404 N ATOM 1508 CA TYR A 192 -230.279 58.003 36.138 1.00100.14 C ANISOU 1508 CA TYR A 192 12963 10459 14626 356 -1019 1338 C ATOM 1509 C TYR A 192 -230.163 59.281 35.318 1.00 88.72 C ANISOU 1509 C TYR A 192 11597 8828 13283 305 -1114 1505 C ATOM 1510 O TYR A 192 -230.399 60.367 35.859 1.00 96.46 O ANISOU 1510 O TYR A 192 12534 9619 14497 373 -1105 1477 O ATOM 1511 CB TYR A 192 -229.079 57.892 37.088 1.00104.68 C ANISOU 1511 CB TYR A 192 13550 11102 15123 315 -859 1154 C ATOM 1512 CG TYR A 192 -228.926 56.506 37.680 1.00111.16 C ANISOU 1512 CG TYR A 192 14326 12119 15790 326 -787 1030 C ATOM 1513 CD1 TYR A 192 -229.689 56.108 38.768 1.00118.44 C ANISOU 1513 CD1 TYR A 192 15148 13065 16788 426 -741 909 C ATOM 1514 CD2 TYR A 192 -228.030 55.591 37.141 1.00112.00 C ANISOU 1514 CD2 TYR A 192 14491 12378 15686 233 -757 1035 C ATOM 1515 CE1 TYR A 192 -229.562 54.843 39.310 1.00122.26 C ANISOU 1515 CE1 TYR A 192 15602 13716 17134 427 -688 817 C ATOM 1516 CE2 TYR A 192 -227.895 54.322 37.676 1.00118.13 C ANISOU 1516 CE2 TYR A 192 15223 13308 16352 250 -704 933 C ATOM 1517 CZ TYR A 192 -228.664 53.954 38.760 1.00125.08 C ANISOU 1517 CZ TYR A 192 16015 14206 17303 344 -681 834 C ATOM 1518 OH TYR A 192 -228.535 52.692 39.296 1.00132.34 O ANISOU 1518 OH TYR A 192 16902 15267 18112 350 -640 753 O ATOM 1519 N THR A 193 -229.814 59.180 34.037 1.00 78.69 N ANISOU 1519 N THR A 193 10452 7602 11844 181 -1200 1675 N ATOM 1520 CA THR A 193 -229.691 60.335 33.164 1.00 72.97 C ANISOU 1520 CA THR A 193 9830 6710 11185 106 -1304 1867 C ATOM 1521 C THR A 193 -230.466 60.091 31.878 1.00 87.51 C ANISOU 1521 C THR A 193 11742 8568 12941 54 -1502 2096 C ATOM 1522 O THR A 193 -230.458 58.972 31.350 1.00105.23 O ANISOU 1522 O THR A 193 14031 10998 14952 -9 -1509 2099 O ATOM 1523 CB THR A 193 -228.221 60.627 32.825 1.00 71.22 C ANISOU 1523 CB THR A 193 9732 6523 10803 -53 -1194 1859 C ATOM 1524 OG1 THR A 193 -227.372 59.974 33.774 1.00 70.70 O ANISOU 1524 OG1 THR A 193 9608 6591 10662 -46 -1019 1636 O ATOM 1525 CG2 THR A 193 -227.952 62.126 32.863 1.00 91.61 C ANISOU 1525 CG2 THR A 193 12355 8871 13583 -75 -1218 1932 C ATOM 1526 N PRO A 194 -231.153 61.111 31.356 1.00 77.43 N ANISOU 1526 N PRO A 194 10479 7090 11852 75 -1678 2293 N ATOM 1527 CA PRO A 194 -231.812 61.012 30.048 1.00 77.13 C ANISOU 1527 CA PRO A 194 10534 7054 11717 -6 -1905 2547 C ATOM 1528 C PRO A 194 -230.861 61.288 28.887 1.00 89.02 C ANISOU 1528 C PRO A 194 12269 8594 12960 -225 -1920 2702 C ATOM 1529 O PRO A 194 -231.127 62.133 28.030 1.00108.98 O ANISOU 1529 O PRO A 194 14899 10978 15530 -298 -2100 2946 O ATOM 1530 CB PRO A 194 -232.918 62.068 30.148 1.00 73.95 C ANISOU 1530 CB PRO A 194 10022 6392 11683 125 -2086 2687 C ATOM 1531 CG PRO A 194 -232.326 63.114 31.033 1.00 68.67 C ANISOU 1531 CG PRO A 194 9316 5549 11224 182 -1942 2566 C ATOM 1532 CD PRO A 194 -231.474 62.375 32.040 1.00 67.80 C ANISOU 1532 CD PRO A 194 9171 5615 10974 189 -1686 2281 C ATOM 1533 N HIS A 195 -229.731 60.575 28.872 1.00 82.46 N ANISOU 1533 N HIS A 195 11515 7949 11868 -334 -1723 2562 N ATOM 1534 CA HIS A 195 -228.676 60.803 27.891 1.00 83.99 C ANISOU 1534 CA HIS A 195 11909 8190 11813 -549 -1667 2661 C ATOM 1535 C HIS A 195 -229.213 60.640 26.474 1.00 92.44 C ANISOU 1535 C HIS A 195 13152 9297 12673 -693 -1867 2907 C ATOM 1536 O HIS A 195 -229.305 59.519 25.962 1.00106.90 O ANISOU 1536 O HIS A 195 15043 11319 14257 -760 -1859 2871 O ATOM 1537 CB HIS A 195 -227.507 59.844 28.142 1.00 83.22 C ANISOU 1537 CB HIS A 195 11820 8301 11500 -618 -1418 2446 C ATOM 1538 CG HIS A 195 -226.171 60.400 27.755 1.00102.78 C ANISOU 1538 CG HIS A 195 14412 10774 13867 -787 -1269 2458 C ATOM 1539 ND1 HIS A 195 -225.476 59.966 26.646 1.00110.24 N ANISOU 1539 ND1 HIS A 195 15527 11853 14506 -990 -1192 2516 N ATOM 1540 CD2 HIS A 195 -225.401 61.353 28.332 1.00110.85 C ANISOU 1540 CD2 HIS A 195 15399 11670 15047 -794 -1173 2412 C ATOM 1541 CE1 HIS A 195 -224.336 60.629 26.557 1.00113.40 C ANISOU 1541 CE1 HIS A 195 15979 12215 14892 -1112 -1047 2511 C ATOM 1542 NE2 HIS A 195 -224.267 61.477 27.567 1.00111.98 N ANISOU 1542 NE2 HIS A 195 15676 11877 14994 -998 -1044 2453 N ATOM 1543 N GLU A 196 -229.573 61.756 25.834 1.00 99.72 N ANISOU 1543 N GLU A 196 14165 10031 13693 -749 -2059 3161 N ATOM 1544 CA GLU A 196 -230.232 61.692 24.534 1.00110.09 C ANISOU 1544 CA GLU A 196 15643 11359 14826 -884 -2305 3426 C ATOM 1545 C GLU A 196 -229.314 61.152 23.444 1.00113.81 C ANISOU 1545 C GLU A 196 16360 12019 14863 -1145 -2197 3456 C ATOM 1546 O GLU A 196 -229.804 60.642 22.431 1.00113.21 O ANISOU 1546 O GLU A 196 16432 12039 14544 -1274 -2354 3596 O ATOM 1547 CB GLU A 196 -230.754 63.077 24.142 1.00113.85 C ANISOU 1547 CB GLU A 196 16162 11568 15529 -887 -2544 3708 C ATOM 1548 CG GLU A 196 -231.749 63.677 25.121 1.00114.73 C ANISOU 1548 CG GLU A 196 16027 11464 16100 -629 -2652 3685 C ATOM 1549 CD GLU A 196 -232.119 65.103 24.768 1.00137.79 C ANISOU 1549 CD GLU A 196 18947 14163 19244 -615 -2805 3863 C ATOM 1550 OE1 GLU A 196 -231.648 65.599 23.723 1.00147.25 O ANISOU 1550 OE1 GLU A 196 20349 15374 20227 -814 -2858 4036 O ATOM 1551 OE2 GLU A 196 -232.877 65.731 25.538 1.00146.28 O ANISOU 1551 OE2 GLU A 196 19809 15074 20697 -406 -2841 3795 O ATOM 1552 N GLU A 197 -227.994 61.248 23.629 1.00120.73 N ANISOU 1552 N GLU A 197 17279 12950 15641 -1234 -1928 3319 N ATOM 1553 CA GLU A 197 -227.068 60.774 22.606 1.00126.70 C ANISOU 1553 CA GLU A 197 18255 13879 16008 -1485 -1782 3327 C ATOM 1554 C GLU A 197 -227.137 59.261 22.440 1.00117.32 C ANISOU 1554 C GLU A 197 17068 12925 14584 -1496 -1691 3152 C ATOM 1555 O GLU A 197 -226.830 58.744 21.360 1.00119.85 O ANISOU 1555 O GLU A 197 17596 13383 14557 -1706 -1650 3197 O ATOM 1556 CB GLU A 197 -225.640 61.211 22.944 1.00134.78 C ANISOU 1556 CB GLU A 197 19273 14899 17037 -1561 -1502 3203 C ATOM 1557 CG GLU A 197 -225.419 62.723 22.970 1.00136.13 C ANISOU 1557 CG GLU A 197 19483 14836 17406 -1599 -1571 3380 C ATOM 1558 CD GLU A 197 -225.767 63.358 24.309 1.00136.44 C ANISOU 1558 CD GLU A 197 19291 14690 17858 -1355 -1603 3279 C ATOM 1559 OE1 GLU A 197 -226.732 62.908 24.961 1.00139.11 O ANISOU 1559 OE1 GLU A 197 19472 15024 18360 -1153 -1705 3201 O ATOM 1560 OE2 GLU A 197 -225.067 64.310 24.712 1.00137.81 O ANISOU 1560 OE2 GLU A 197 19445 14724 18192 -1377 -1514 3270 O ATOM 1561 N THR A 198 -227.541 58.537 23.484 1.00111.83 N ANISOU 1561 N THR A 198 16154 12270 14065 -1283 -1653 2952 N ATOM 1562 CA THR A 198 -227.638 57.083 23.431 1.00102.84 C ANISOU 1562 CA THR A 198 15000 11329 12746 -1276 -1572 2780 C ATOM 1563 C THR A 198 -229.065 56.582 23.622 1.00101.82 C ANISOU 1563 C THR A 198 14770 11191 12725 -1141 -1806 2824 C ATOM 1564 O THR A 198 -229.267 55.374 23.798 1.00 99.93 O ANISOU 1564 O THR A 198 14480 11090 12399 -1100 -1750 2668 O ATOM 1565 CB THR A 198 -226.715 56.450 24.475 1.00 76.37 C ANISOU 1565 CB THR A 198 11484 8060 9473 -1172 -1294 2491 C ATOM 1566 OG1 THR A 198 -226.963 57.039 25.758 1.00 64.24 O ANISOU 1566 OG1 THR A 198 9739 6391 8276 -967 -1312 2429 O ATOM 1567 CG2 THR A 198 -225.261 56.667 24.094 1.00 68.51 C ANISOU 1567 CG2 THR A 198 10585 7115 8330 -1337 -1047 2433 C ATOM 1568 N ASN A 199 -230.054 57.474 23.585 1.00 97.42 N ANISOU 1568 N ASN A 199 14174 10464 12376 -1072 -2066 3034 N ATOM 1569 CA ASN A 199 -231.469 57.121 23.704 1.00 88.32 C ANISOU 1569 CA ASN A 199 12905 9286 11368 -951 -2309 3103 C ATOM 1570 C ASN A 199 -231.725 56.272 24.951 1.00 85.51 C ANISOU 1570 C ASN A 199 12313 8992 11186 -747 -2179 2851 C ATOM 1571 O ASN A 199 -232.166 55.124 24.882 1.00 89.30 O ANISOU 1571 O ASN A 199 12769 9606 11554 -743 -2194 2765 O ATOM 1572 CB ASN A 199 -231.959 56.410 22.440 1.00 86.18 C ANISOU 1572 CB ASN A 199 12827 9138 10780 -1135 -2483 3233 C ATOM 1573 CG ASN A 199 -231.935 57.308 21.219 1.00 94.44 C ANISOU 1573 CG ASN A 199 14114 10108 11660 -1342 -2671 3527 C ATOM 1574 OD1 ASN A 199 -232.795 58.173 21.054 1.00109.38 O ANISOU 1574 OD1 ASN A 199 15970 11832 13759 -1295 -2949 3765 O ATOM 1575 ND2 ASN A 199 -230.952 57.101 20.350 1.00 94.43 N ANISOU 1575 ND2 ASN A 199 14360 10229 11292 -1577 -2518 3517 N ATOM 1576 N ASN A 200 -231.436 56.868 26.111 1.00 82.28 N ANISOU 1576 N ASN A 200 11740 8478 11047 -590 -2051 2735 N ATOM 1577 CA ASN A 200 -231.644 56.162 27.371 1.00 85.08 C ANISOU 1577 CA ASN A 200 11885 8883 11558 -411 -1924 2506 C ATOM 1578 C ASN A 200 -233.125 55.940 27.648 1.00 90.87 C ANISOU 1578 C ASN A 200 12461 9569 12496 -276 -2117 2561 C ATOM 1579 O ASN A 200 -233.506 54.916 28.229 1.00 90.85 O ANISOU 1579 O ASN A 200 12345 9674 12501 -197 -2060 2414 O ATOM 1580 CB ASN A 200 -231.004 56.935 28.522 1.00 78.67 C ANISOU 1580 CB ASN A 200 10961 7966 10965 -302 -1757 2375 C ATOM 1581 CG ASN A 200 -229.496 56.838 28.518 1.00 80.80 C ANISOU 1581 CG ASN A 200 11324 8321 11057 -413 -1531 2257 C ATOM 1582 OD1 ASN A 200 -228.884 56.544 27.490 1.00 77.75 O ANISOU 1582 OD1 ASN A 200 11108 8028 10405 -588 -1497 2315 O ATOM 1583 ND2 ASN A 200 -228.886 57.081 29.672 1.00 77.83 N ANISOU 1583 ND2 ASN A 200 10832 7912 10829 -321 -1369 2085 N ATOM 1584 N GLU A 201 -233.972 56.889 27.243 1.00 95.23 N ANISOU 1584 N GLU A 201 12993 9954 13237 -250 -2349 2779 N ATOM 1585 CA GLU A 201 -235.397 56.797 27.549 1.00 94.60 C ANISOU 1585 CA GLU A 201 12722 9805 13418 -108 -2530 2836 C ATOM 1586 C GLU A 201 -236.019 55.563 26.910 1.00 89.06 C ANISOU 1586 C GLU A 201 12054 9269 12516 -187 -2652 2860 C ATOM 1587 O GLU A 201 -236.769 54.824 27.560 1.00 91.57 O ANISOU 1587 O GLU A 201 12197 9638 12958 -75 -2642 2751 O ATOM 1588 CB GLU A 201 -236.111 58.067 27.084 1.00111.21 C ANISOU 1588 CB GLU A 201 14802 11681 15770 -78 -2780 3092 C ATOM 1589 CG GLU A 201 -237.616 58.059 27.308 1.00122.88 C ANISOU 1589 CG GLU A 201 16056 13067 17566 69 -2986 3173 C ATOM 1590 CD GLU A 201 -238.294 59.298 26.753 1.00134.75 C ANISOU 1590 CD GLU A 201 17522 14370 19307 89 -3216 3398 C ATOM 1591 OE1 GLU A 201 -237.592 60.150 26.170 1.00138.06 O ANISOU 1591 OE1 GLU A 201 18113 14717 19626 -21 -3230 3510 O ATOM 1592 OE2 GLU A 201 -239.529 59.419 26.898 1.00141.24 O ANISOU 1592 OE2 GLU A 201 18125 15146 20394 200 -3333 3409 O ATOM 1593 N SER A 202 -235.709 55.315 25.635 1.00 80.02 N ANISOU 1593 N SER A 202 11146 8210 11049 -394 -2758 2994 N ATOM 1594 CA SER A 202 -236.289 54.166 24.947 1.00 78.77 C ANISOU 1594 CA SER A 202 11048 8201 10679 -495 -2886 3013 C ATOM 1595 C SER A 202 -235.764 52.850 25.505 1.00 86.08 C ANISOU 1595 C SER A 202 11953 9303 11452 -482 -2640 2743 C ATOM 1596 O SER A 202 -236.491 51.851 25.517 1.00102.48 O ANISOU 1596 O SER A 202 13964 11468 13507 -472 -2710 2695 O ATOM 1597 CB SER A 202 -236.010 54.254 23.447 1.00 84.03 C ANISOU 1597 CB SER A 202 12007 8919 11003 -745 -3040 3207 C ATOM 1598 OG SER A 202 -234.619 54.222 23.181 1.00 93.93 O ANISOU 1598 OG SER A 202 13451 10253 11985 -875 -2792 3105 O ATOM 1599 N PHE A 203 -234.513 52.826 25.969 1.00 74.54 N ANISOU 1599 N PHE A 203 10537 7885 9901 -485 -2363 2574 N ATOM 1600 CA PHE A 203 -233.968 51.595 26.531 1.00 78.55 C ANISOU 1600 CA PHE A 203 11013 8538 10295 -464 -2143 2331 C ATOM 1601 C PHE A 203 -234.624 51.261 27.865 1.00 82.80 C ANISOU 1601 C PHE A 203 11299 9053 11107 -264 -2093 2202 C ATOM 1602 O PHE A 203 -234.845 50.084 28.176 1.00 83.92 O ANISOU 1602 O PHE A 203 11390 9303 11195 -245 -2039 2075 O ATOM 1603 CB PHE A 203 -232.453 51.715 26.687 1.00 74.82 C ANISOU 1603 CB PHE A 203 10630 8105 9693 -518 -1881 2200 C ATOM 1604 CG PHE A 203 -231.777 50.418 27.022 1.00 69.19 C ANISOU 1604 CG PHE A 203 9913 7535 8842 -524 -1675 1977 C ATOM 1605 CD1 PHE A 203 -231.499 49.492 26.030 1.00 64.01 C ANISOU 1605 CD1 PHE A 203 9427 6998 7896 -683 -1650 1946 C ATOM 1606 CD2 PHE A 203 -231.421 50.122 28.327 1.00 63.91 C ANISOU 1606 CD2 PHE A 203 9077 6871 8336 -378 -1511 1799 C ATOM 1607 CE1 PHE A 203 -230.878 48.296 26.333 1.00 67.30 C ANISOU 1607 CE1 PHE A 203 9828 7519 8223 -677 -1460 1739 C ATOM 1608 CE2 PHE A 203 -230.797 48.929 28.635 1.00 60.26 C ANISOU 1608 CE2 PHE A 203 8604 6520 7772 -380 -1345 1616 C ATOM 1609 CZ PHE A 203 -230.527 48.014 27.638 1.00 65.45 C ANISOU 1609 CZ PHE A 203 9413 7278 8177 -521 -1318 1584 C ATOM 1610 N VAL A 204 -234.945 52.281 28.665 1.00 81.02 N ANISOU 1610 N VAL A 204 10925 8684 11176 -122 -2100 2227 N ATOM 1611 CA VAL A 204 -235.655 52.048 29.921 1.00 80.33 C ANISOU 1611 CA VAL A 204 10606 8571 11345 54 -2043 2107 C ATOM 1612 C VAL A 204 -237.041 51.479 29.650 1.00 85.04 C ANISOU 1612 C VAL A 204 11098 9184 12032 77 -2242 2194 C ATOM 1613 O VAL A 204 -237.496 50.554 30.335 1.00 81.22 O ANISOU 1613 O VAL A 204 10490 8775 11593 139 -2176 2070 O ATOM 1614 CB VAL A 204 -235.724 53.346 30.747 1.00 75.10 C ANISOU 1614 CB VAL A 204 9823 7734 10976 187 -2000 2108 C ATOM 1615 CG1 VAL A 204 -236.617 53.158 31.963 1.00 65.77 C ANISOU 1615 CG1 VAL A 204 8410 6522 10057 353 -1942 1991 C ATOM 1616 CG2 VAL A 204 -234.330 53.777 31.171 1.00 79.97 C ANISOU 1616 CG2 VAL A 204 10526 8350 11509 160 -1794 1993 C ATOM 1617 N ILE A 205 -237.735 52.021 28.647 1.00 83.06 N ANISOU 1617 N ILE A 205 10890 8858 11810 16 -2500 2418 N ATOM 1618 CA ILE A 205 -239.031 51.473 28.257 1.00 77.80 C ANISOU 1618 CA ILE A 205 10125 8211 11223 12 -2726 2520 C ATOM 1619 C ILE A 205 -238.874 50.033 27.789 1.00 80.79 C ANISOU 1619 C ILE A 205 10622 8773 11303 -117 -2705 2433 C ATOM 1620 O ILE A 205 -239.628 49.141 28.194 1.00 85.79 O ANISOU 1620 O ILE A 205 11121 9464 12011 -74 -2721 2363 O ATOM 1621 CB ILE A 205 -239.678 52.348 27.170 1.00 67.72 C ANISOU 1621 CB ILE A 205 8901 6820 10009 -55 -3039 2802 C ATOM 1622 CG1 ILE A 205 -239.824 53.786 27.660 1.00 70.31 C ANISOU 1622 CG1 ILE A 205 9106 6937 10673 85 -3053 2881 C ATOM 1623 CG2 ILE A 205 -241.027 51.783 26.764 1.00 60.96 C ANISOU 1623 CG2 ILE A 205 7925 5984 9253 -66 -3300 2916 C ATOM 1624 CD1 ILE A 205 -240.266 54.745 26.580 1.00 66.11 C ANISOU 1624 CD1 ILE A 205 8651 6268 10200 13 -3362 3179 C ATOM 1625 N TYR A 206 -237.886 49.787 26.925 1.00 76.45 N ANISOU 1625 N TYR A 206 10323 8306 10417 -283 -2655 2430 N ATOM 1626 CA TYR A 206 -237.636 48.429 26.454 1.00 75.23 C ANISOU 1626 CA TYR A 206 10297 8308 9980 -409 -2606 2321 C ATOM 1627 C TYR A 206 -237.288 47.500 27.611 1.00 71.64 C ANISOU 1627 C TYR A 206 9721 7920 9578 -302 -2363 2083 C ATOM 1628 O TYR A 206 -237.763 46.360 27.666 1.00 65.83 O ANISOU 1628 O TYR A 206 8952 7264 8797 -323 -2380 2008 O ATOM 1629 CB TYR A 206 -236.522 48.436 25.407 1.00 74.21 C ANISOU 1629 CB TYR A 206 10451 8243 9502 -598 -2537 2330 C ATOM 1630 CG TYR A 206 -235.749 47.142 25.334 1.00 83.09 C ANISOU 1630 CG TYR A 206 11681 9505 10386 -675 -2334 2122 C ATOM 1631 CD1 TYR A 206 -236.284 46.021 24.712 1.00 81.96 C ANISOU 1631 CD1 TYR A 206 11615 9450 10076 -785 -2434 2095 C ATOM 1632 CD2 TYR A 206 -234.480 47.041 25.887 1.00 94.47 C ANISOU 1632 CD2 TYR A 206 13136 10973 11787 -638 -2050 1950 C ATOM 1633 CE1 TYR A 206 -235.576 44.835 24.648 1.00 87.41 C ANISOU 1633 CE1 TYR A 206 12398 10239 10576 -847 -2241 1894 C ATOM 1634 CE2 TYR A 206 -233.767 45.864 25.829 1.00 95.70 C ANISOU 1634 CE2 TYR A 206 13365 11229 11767 -693 -1868 1763 C ATOM 1635 CZ TYR A 206 -234.317 44.764 25.208 1.00 91.70 C ANISOU 1635 CZ TYR A 206 12938 10796 11107 -793 -1956 1731 C ATOM 1636 OH TYR A 206 -233.602 43.590 25.150 1.00 92.31 O ANISOU 1636 OH TYR A 206 13086 10950 11037 -841 -1767 1535 O ATOM 1637 N MET A 207 -236.461 47.971 28.547 1.00 78.36 N ANISOU 1637 N MET A 207 10513 8735 10524 -198 -2149 1971 N ATOM 1638 CA MET A 207 -236.161 47.177 29.734 1.00 73.22 C ANISOU 1638 CA MET A 207 9746 8138 9937 -98 -1946 1771 C ATOM 1639 C MET A 207 -237.418 46.916 30.549 1.00 70.89 C ANISOU 1639 C MET A 207 9231 7816 9887 20 -2012 1767 C ATOM 1640 O MET A 207 -237.642 45.796 31.026 1.00 66.89 O ANISOU 1640 O MET A 207 8667 7385 9362 31 -1949 1658 O ATOM 1641 CB MET A 207 -235.115 47.885 30.591 1.00 75.05 C ANISOU 1641 CB MET A 207 9954 8325 10236 -21 -1745 1675 C ATOM 1642 CG MET A 207 -233.705 47.760 30.066 1.00 81.02 C ANISOU 1642 CG MET A 207 10884 9137 10761 -129 -1605 1612 C ATOM 1643 SD MET A 207 -233.161 46.047 30.099 1.00 75.08 S ANISOU 1643 SD MET A 207 10179 8520 9828 -178 -1469 1434 S ATOM 1644 CE MET A 207 -233.256 45.710 31.856 1.00 59.79 C ANISOU 1644 CE MET A 207 8036 6577 8106 -9 -1346 1296 C ATOM 1645 N PHE A 208 -238.252 47.942 30.716 1.00 73.23 N ANISOU 1645 N PHE A 208 9396 7997 10432 106 -2132 1885 N ATOM 1646 CA PHE A 208 -239.446 47.799 31.539 1.00 67.24 C ANISOU 1646 CA PHE A 208 8402 7204 9943 224 -2161 1870 C ATOM 1647 C PHE A 208 -240.449 46.844 30.904 1.00 74.04 C ANISOU 1647 C PHE A 208 9231 8129 10771 148 -2346 1939 C ATOM 1648 O PHE A 208 -241.073 46.038 31.603 1.00 76.47 O ANISOU 1648 O PHE A 208 9398 8482 11176 193 -2293 1855 O ATOM 1649 CB PHE A 208 -240.078 49.169 31.774 1.00 63.80 C ANISOU 1649 CB PHE A 208 7823 6606 9812 337 -2241 1976 C ATOM 1650 CG PHE A 208 -241.337 49.123 32.582 1.00 68.40 C ANISOU 1650 CG PHE A 208 8143 7141 10706 460 -2251 1955 C ATOM 1651 CD1 PHE A 208 -241.285 49.024 33.963 1.00 73.27 C ANISOU 1651 CD1 PHE A 208 8635 7763 11441 567 -2015 1776 C ATOM 1652 CD2 PHE A 208 -242.573 49.186 31.964 1.00 71.64 C ANISOU 1652 CD2 PHE A 208 8428 7503 11291 458 -2496 2116 C ATOM 1653 CE1 PHE A 208 -242.448 48.983 34.712 1.00 79.94 C ANISOU 1653 CE1 PHE A 208 9237 8569 12568 668 -1991 1745 C ATOM 1654 CE2 PHE A 208 -243.739 49.146 32.707 1.00 84.60 C ANISOU 1654 CE2 PHE A 208 9799 9098 13248 571 -2486 2091 C ATOM 1655 CZ PHE A 208 -243.676 49.044 34.083 1.00 85.91 C ANISOU 1655 CZ PHE A 208 9845 9272 13524 675 -2216 1898 C ATOM 1656 N VAL A 209 -240.614 46.910 29.584 1.00 79.04 N ANISOU 1656 N VAL A 209 10005 8769 11257 16 -2566 2094 N ATOM 1657 CA VAL A 209 -241.606 46.069 28.924 1.00 75.27 C ANISOU 1657 CA VAL A 209 9505 8346 10747 -75 -2776 2169 C ATOM 1658 C VAL A 209 -241.083 44.650 28.750 1.00 79.43 C ANISOU 1658 C VAL A 209 10172 9006 11000 -185 -2671 2024 C ATOM 1659 O VAL A 209 -241.741 43.678 29.138 1.00 94.07 O ANISOU 1659 O VAL A 209 11918 10908 12917 -180 -2674 1958 O ATOM 1660 CB VAL A 209 -242.017 46.682 27.573 1.00 68.49 C ANISOU 1660 CB VAL A 209 8760 7445 9819 -195 -3079 2401 C ATOM 1661 CG1 VAL A 209 -242.964 45.745 26.842 1.00 61.15 C ANISOU 1661 CG1 VAL A 209 7832 6584 8819 -319 -3311 2471 C ATOM 1662 CG2 VAL A 209 -242.657 48.044 27.780 1.00 66.69 C ANISOU 1662 CG2 VAL A 209 8359 7055 9925 -69 -3205 2558 C ATOM 1663 N VAL A 210 -239.890 44.510 28.171 1.00 72.21 N ANISOU 1663 N VAL A 210 9494 8143 9798 -287 -2568 1966 N ATOM 1664 CA VAL A 210 -239.400 43.195 27.771 1.00 67.44 C ANISOU 1664 CA VAL A 210 9042 7644 8936 -407 -2489 1836 C ATOM 1665 C VAL A 210 -238.762 42.458 28.943 1.00 69.08 C ANISOU 1665 C VAL A 210 9174 7883 9189 -308 -2226 1636 C ATOM 1666 O VAL A 210 -238.982 41.256 29.125 1.00 71.43 O ANISOU 1666 O VAL A 210 9458 8232 9449 -337 -2195 1540 O ATOM 1667 CB VAL A 210 -238.422 43.338 26.592 1.00 62.78 C ANISOU 1667 CB VAL A 210 8733 7093 8029 -569 -2475 1852 C ATOM 1668 CG1 VAL A 210 -237.755 42.007 26.287 1.00 59.33 C ANISOU 1668 CG1 VAL A 210 8443 6745 7353 -671 -2332 1674 C ATOM 1669 CG2 VAL A 210 -239.147 43.866 25.366 1.00 55.07 C ANISOU 1669 CG2 VAL A 210 7863 6100 6961 -705 -2772 2065 C ATOM 1670 N HIS A 211 -237.959 43.149 29.751 1.00 72.04 N ANISOU 1670 N HIS A 211 9506 8222 9645 -200 -2048 1577 N ATOM 1671 CA HIS A 211 -237.178 42.499 30.794 1.00 70.73 C ANISOU 1671 CA HIS A 211 9299 8087 9487 -127 -1818 1404 C ATOM 1672 C HIS A 211 -237.749 42.719 32.190 1.00 75.75 C ANISOU 1672 C HIS A 211 9717 8687 10376 21 -1751 1371 C ATOM 1673 O HIS A 211 -237.047 42.489 33.180 1.00 72.93 O ANISOU 1673 O HIS A 211 9328 8344 10037 87 -1572 1252 O ATOM 1674 CB HIS A 211 -235.726 42.977 30.739 1.00 62.45 C ANISOU 1674 CB HIS A 211 8368 7039 8323 -136 -1653 1339 C ATOM 1675 CG HIS A 211 -235.032 42.649 29.455 1.00 68.33 C ANISOU 1675 CG HIS A 211 9330 7829 8804 -291 -1653 1334 C ATOM 1676 ND1 HIS A 211 -234.196 41.562 29.317 1.00 73.25 N ANISOU 1676 ND1 HIS A 211 10043 8507 9283 -344 -1507 1185 N ATOM 1677 CD2 HIS A 211 -235.053 43.263 28.248 1.00 77.33 C ANISOU 1677 CD2 HIS A 211 10622 8963 9795 -413 -1772 1455 C ATOM 1678 CE1 HIS A 211 -233.730 41.522 28.081 1.00 76.35 C ANISOU 1678 CE1 HIS A 211 10632 8931 9448 -492 -1511 1194 C ATOM 1679 NE2 HIS A 211 -234.234 42.543 27.412 1.00 76.43 N ANISOU 1679 NE2 HIS A 211 10695 8914 9433 -546 -1675 1364 N ATOM 1680 N PHE A 212 -239.004 43.148 32.297 1.00 85.88 N ANISOU 1680 N PHE A 212 10850 9924 11856 68 -1890 1472 N ATOM 1681 CA PHE A 212 -239.579 43.417 33.609 1.00 87.61 C ANISOU 1681 CA PHE A 212 10864 10107 12315 199 -1796 1426 C ATOM 1682 C PHE A 212 -241.052 43.028 33.652 1.00 87.36 C ANISOU 1682 C PHE A 212 10661 10073 12461 206 -1927 1491 C ATOM 1683 O PHE A 212 -241.481 42.303 34.555 1.00 82.10 O ANISOU 1683 O PHE A 212 9879 9439 11874 239 -1830 1411 O ATOM 1684 CB PHE A 212 -239.392 44.893 33.968 1.00 87.39 C ANISOU 1684 CB PHE A 212 10785 9983 12437 293 -1758 1462 C ATOM 1685 CG PHE A 212 -239.757 45.232 35.386 1.00 90.36 C ANISOU 1685 CG PHE A 212 10987 10322 13025 418 -1608 1372 C ATOM 1686 CD1 PHE A 212 -238.950 44.834 36.438 1.00 89.39 C ANISOU 1686 CD1 PHE A 212 10891 10248 12826 442 -1408 1226 C ATOM 1687 CD2 PHE A 212 -240.894 45.973 35.666 1.00 98.79 C ANISOU 1687 CD2 PHE A 212 11865 11302 14369 504 -1666 1433 C ATOM 1688 CE1 PHE A 212 -239.274 45.155 37.743 1.00 85.11 C ANISOU 1688 CE1 PHE A 212 10219 9681 12438 531 -1265 1138 C ATOM 1689 CE2 PHE A 212 -241.224 46.299 36.970 1.00 95.06 C ANISOU 1689 CE2 PHE A 212 11244 10796 14078 607 -1495 1327 C ATOM 1690 CZ PHE A 212 -240.412 45.889 38.009 1.00 84.22 C ANISOU 1690 CZ PHE A 212 9929 9485 12584 610 -1292 1178 C ATOM 1691 N ILE A 213 -241.833 43.502 32.681 1.00 86.15 N ANISOU 1691 N ILE A 213 10485 9876 12373 166 -2155 1646 N ATOM 1692 CA ILE A 213 -243.245 43.142 32.627 1.00 84.13 C ANISOU 1692 CA ILE A 213 10045 9614 12307 163 -2308 1722 C ATOM 1693 C ILE A 213 -243.419 41.734 32.072 1.00 82.01 C ANISOU 1693 C ILE A 213 9865 9436 11858 27 -2384 1695 C ATOM 1694 O ILE A 213 -244.121 40.902 32.658 1.00 80.10 O ANISOU 1694 O ILE A 213 9490 9226 11719 30 -2352 1647 O ATOM 1695 CB ILE A 213 -244.031 44.173 31.797 1.00 76.97 C ANISOU 1695 CB ILE A 213 9066 8615 11563 170 -2558 1915 C ATOM 1696 CG1 ILE A 213 -244.061 45.525 32.512 1.00 78.77 C ANISOU 1696 CG1 ILE A 213 9159 8723 12047 325 -2468 1925 C ATOM 1697 CG2 ILE A 213 -245.442 43.673 31.532 1.00 55.43 C ANISOU 1697 CG2 ILE A 213 6156 5891 9014 137 -2759 2007 C ATOM 1698 CD1 ILE A 213 -244.708 45.479 33.876 1.00 73.57 C ANISOU 1698 CD1 ILE A 213 8258 8044 11651 452 -2285 1812 C ATOM 1699 N ILE A 214 -242.778 41.450 30.935 1.00 84.14 N ANISOU 1699 N ILE A 214 10369 9744 11855 -104 -2475 1720 N ATOM 1700 CA ILE A 214 -242.923 40.134 30.306 1.00 81.65 C ANISOU 1700 CA ILE A 214 10164 9501 11359 -248 -2550 1680 C ATOM 1701 C ILE A 214 -242.456 39.001 31.211 1.00 87.45 C ANISOU 1701 C ILE A 214 10897 10279 12052 -226 -2334 1509 C ATOM 1702 O ILE A 214 -243.165 37.983 31.304 1.00 85.55 O ANISOU 1702 O ILE A 214 10593 10065 11848 -282 -2384 1486 O ATOM 1703 CB ILE A 214 -242.220 40.125 28.937 1.00 67.95 C ANISOU 1703 CB ILE A 214 8703 7795 9318 -400 -2647 1714 C ATOM 1704 CG1 ILE A 214 -242.988 41.000 27.948 1.00 64.84 C ANISOU 1704 CG1 ILE A 214 8312 7363 8962 -463 -2937 1921 C ATOM 1705 CG2 ILE A 214 -242.090 38.709 28.409 1.00 59.38 C ANISOU 1705 CG2 ILE A 214 7764 6775 8021 -543 -2650 1611 C ATOM 1706 CD1 ILE A 214 -244.437 40.613 27.814 1.00 80.52 C ANISOU 1706 CD1 ILE A 214 10120 9343 11129 -496 -3169 2020 C ATOM 1707 N PRO A 215 -241.299 39.080 31.885 1.00 87.21 N ANISOU 1707 N PRO A 215 10930 10253 11953 -157 -2109 1396 N ATOM 1708 CA PRO A 215 -240.939 37.990 32.806 1.00 87.80 C ANISOU 1708 CA PRO A 215 10987 10356 12016 -135 -1937 1261 C ATOM 1709 C PRO A 215 -241.969 37.764 33.898 1.00 89.99 C ANISOU 1709 C PRO A 215 11044 10629 12521 -69 -1905 1265 C ATOM 1710 O PRO A 215 -242.217 36.615 34.283 1.00 94.13 O ANISOU 1710 O PRO A 215 11547 11176 13041 -111 -1867 1209 O ATOM 1711 CB PRO A 215 -239.592 38.451 33.378 1.00 81.26 C ANISOU 1711 CB PRO A 215 10232 9522 11123 -59 -1741 1176 C ATOM 1712 CG PRO A 215 -239.032 39.336 32.334 1.00 81.31 C ANISOU 1712 CG PRO A 215 10374 9514 11007 -102 -1806 1236 C ATOM 1713 CD PRO A 215 -240.208 40.066 31.772 1.00 80.72 C ANISOU 1713 CD PRO A 215 10213 9407 11049 -116 -2018 1390 C ATOM 1714 N LEU A 216 -242.588 38.833 34.401 1.00 81.89 N ANISOU 1714 N LEU A 216 9850 9564 11702 29 -1909 1328 N ATOM 1715 CA LEU A 216 -243.590 38.680 35.450 1.00 79.62 C ANISOU 1715 CA LEU A 216 9341 9272 11638 86 -1844 1319 C ATOM 1716 C LEU A 216 -244.831 37.969 34.925 1.00 83.04 C ANISOU 1716 C LEU A 216 9669 9719 12165 -1 -2021 1392 C ATOM 1717 O LEU A 216 -245.361 37.061 35.576 1.00 87.65 O ANISOU 1717 O LEU A 216 10160 10329 12813 -29 -1956 1350 O ATOM 1718 CB LEU A 216 -243.958 40.046 36.025 1.00 76.85 C ANISOU 1718 CB LEU A 216 8834 8860 11505 212 -1793 1351 C ATOM 1719 CG LEU A 216 -245.061 40.032 37.084 1.00 72.79 C ANISOU 1719 CG LEU A 216 8074 8337 11245 272 -1698 1330 C ATOM 1720 CD1 LEU A 216 -244.530 39.523 38.416 1.00 64.66 C ANISOU 1720 CD1 LEU A 216 7069 7352 10146 292 -1452 1199 C ATOM 1721 CD2 LEU A 216 -245.673 41.413 37.232 1.00 76.08 C ANISOU 1721 CD2 LEU A 216 8318 8665 11923 385 -1712 1382 C ATOM 1722 N ILE A 217 -245.307 38.370 33.745 1.00 73.53 N ANISOU 1722 N ILE A 217 8479 8493 10965 -58 -2257 1511 N ATOM 1723 CA ILE A 217 -246.524 37.784 33.191 1.00 64.67 C ANISOU 1723 CA ILE A 217 7244 7380 9946 -152 -2463 1595 C ATOM 1724 C ILE A 217 -246.314 36.307 32.881 1.00 68.18 C ANISOU 1724 C ILE A 217 7833 7877 10197 -288 -2472 1520 C ATOM 1725 O ILE A 217 -247.188 35.470 33.143 1.00 75.46 O ANISOU 1725 O ILE A 217 8629 8812 11229 -345 -2508 1520 O ATOM 1726 CB ILE A 217 -246.970 38.569 31.943 1.00 68.17 C ANISOU 1726 CB ILE A 217 7706 7790 10408 -199 -2746 1756 C ATOM 1727 CG1 ILE A 217 -247.177 40.043 32.292 1.00 73.72 C ANISOU 1727 CG1 ILE A 217 8256 8411 11342 -51 -2734 1832 C ATOM 1728 CG2 ILE A 217 -248.245 37.979 31.364 1.00 64.03 C ANISOU 1728 CG2 ILE A 217 7053 7275 9999 -307 -2992 1852 C ATOM 1729 CD1 ILE A 217 -248.169 40.271 33.408 1.00 75.67 C ANISOU 1729 CD1 ILE A 217 8191 8622 11936 64 -2627 1815 C ATOM 1730 N VAL A 218 -245.151 35.962 32.326 1.00 74.35 N ANISOU 1730 N VAL A 218 8871 8676 10702 -345 -2427 1448 N ATOM 1731 CA VAL A 218 -244.878 34.572 31.967 1.00 72.71 C ANISOU 1731 CA VAL A 218 8813 8493 10322 -470 -2425 1359 C ATOM 1732 C VAL A 218 -244.833 33.698 33.214 1.00 70.82 C ANISOU 1732 C VAL A 218 8489 8254 10164 -426 -2232 1265 C ATOM 1733 O VAL A 218 -245.428 32.615 33.257 1.00 76.44 O ANISOU 1733 O VAL A 218 9169 8967 10907 -515 -2275 1246 O ATOM 1734 CB VAL A 218 -243.570 34.473 31.162 1.00 65.89 C ANISOU 1734 CB VAL A 218 8224 7638 9174 -523 -2376 1283 C ATOM 1735 CG1 VAL A 218 -243.172 33.023 30.988 1.00 56.48 C ANISOU 1735 CG1 VAL A 218 7171 6445 7842 -622 -2318 1157 C ATOM 1736 CG2 VAL A 218 -243.730 35.147 29.811 1.00 67.71 C ANISOU 1736 CG2 VAL A 218 8571 7876 9278 -619 -2591 1387 C ATOM 1737 N ILE A 219 -244.126 34.158 34.249 1.00 63.83 N ANISOU 1737 N ILE A 219 7577 7365 9310 -301 -2026 1213 N ATOM 1738 CA ILE A 219 -244.018 33.382 35.483 1.00 68.72 C ANISOU 1738 CA ILE A 219 8141 7988 9982 -271 -1850 1142 C ATOM 1739 C ILE A 219 -245.390 33.196 36.118 1.00 75.55 C ANISOU 1739 C ILE A 219 8776 8861 11070 -282 -1869 1196 C ATOM 1740 O ILE A 219 -245.750 32.093 36.548 1.00 88.39 O ANISOU 1740 O ILE A 219 10376 10489 12720 -352 -1836 1171 O ATOM 1741 CB ILE A 219 -243.033 34.051 36.457 1.00 58.28 C ANISOU 1741 CB ILE A 219 6838 6666 8640 -150 -1654 1087 C ATOM 1742 CG1 ILE A 219 -241.598 33.897 35.953 1.00 60.67 C ANISOU 1742 CG1 ILE A 219 7352 6959 8739 -155 -1607 1016 C ATOM 1743 CG2 ILE A 219 -243.181 33.467 37.853 1.00 52.14 C ANISOU 1743 CG2 ILE A 219 5975 5900 7937 -126 -1495 1049 C ATOM 1744 CD1 ILE A 219 -240.561 34.464 36.893 1.00 62.31 C ANISOU 1744 CD1 ILE A 219 7578 7167 8928 -52 -1437 963 C ATOM 1745 N PHE A 220 -246.181 34.270 36.182 1.00 71.72 N ANISOU 1745 N PHE A 220 8111 8370 10769 -216 -1918 1272 N ATOM 1746 CA PHE A 220 -247.484 34.183 36.836 1.00 72.41 C ANISOU 1746 CA PHE A 220 7945 8462 11105 -217 -1903 1313 C ATOM 1747 C PHE A 220 -248.435 33.279 36.063 1.00 76.41 C ANISOU 1747 C PHE A 220 8400 8972 11659 -356 -2104 1371 C ATOM 1748 O PHE A 220 -249.192 32.506 36.662 1.00 73.56 O ANISOU 1748 O PHE A 220 7908 8623 11417 -412 -2054 1366 O ATOM 1749 CB PHE A 220 -248.086 35.576 37.002 1.00 76.72 C ANISOU 1749 CB PHE A 220 8297 8979 11875 -102 -1910 1373 C ATOM 1750 CG PHE A 220 -247.919 36.150 38.379 1.00 92.19 C ANISOU 1750 CG PHE A 220 10166 10938 13923 9 -1649 1298 C ATOM 1751 CD1 PHE A 220 -246.682 36.598 38.811 1.00 97.22 C ANISOU 1751 CD1 PHE A 220 10967 11574 14396 76 -1510 1224 C ATOM 1752 CD2 PHE A 220 -248.999 36.250 39.240 1.00101.31 C ANISOU 1752 CD2 PHE A 220 11073 12095 15326 34 -1539 1295 C ATOM 1753 CE1 PHE A 220 -246.524 37.130 40.078 1.00101.33 C ANISOU 1753 CE1 PHE A 220 11427 12098 14975 157 -1283 1149 C ATOM 1754 CE2 PHE A 220 -248.849 36.783 40.508 1.00109.78 C ANISOU 1754 CE2 PHE A 220 12086 13171 16453 116 -1283 1208 C ATOM 1755 CZ PHE A 220 -247.609 37.225 40.926 1.00108.09 C ANISOU 1755 CZ PHE A 220 12060 12959 16052 174 -1164 1136 C ATOM 1756 N PHE A 221 -248.414 33.362 34.732 1.00 75.12 N ANISOU 1756 N PHE A 221 8347 8801 11393 -429 -2334 1426 N ATOM 1757 CA PHE A 221 -249.286 32.514 33.926 1.00 75.93 C ANISOU 1757 CA PHE A 221 8424 8908 11517 -583 -2551 1476 C ATOM 1758 C PHE A 221 -248.895 31.046 34.053 1.00 86.23 C ANISOU 1758 C PHE A 221 9879 10213 12672 -691 -2482 1379 C ATOM 1759 O PHE A 221 -249.730 30.194 34.380 1.00 98.59 O ANISOU 1759 O PHE A 221 11323 11776 14360 -775 -2500 1387 O ATOM 1760 CB PHE A 221 -249.248 32.955 32.463 1.00 75.85 C ANISOU 1760 CB PHE A 221 8545 8895 11381 -658 -2815 1555 C ATOM 1761 CG PHE A 221 -249.997 32.038 31.539 1.00 78.86 C ANISOU 1761 CG PHE A 221 8954 9283 11724 -844 -3057 1591 C ATOM 1762 CD1 PHE A 221 -251.356 32.202 31.331 1.00 76.54 C ANISOU 1762 CD1 PHE A 221 8415 8987 11680 -889 -3265 1713 C ATOM 1763 CD2 PHE A 221 -249.342 31.006 30.884 1.00 82.29 C ANISOU 1763 CD2 PHE A 221 9654 9721 11891 -977 -3075 1494 C ATOM 1764 CE1 PHE A 221 -252.047 31.356 30.485 1.00 85.51 C ANISOU 1764 CE1 PHE A 221 9579 10131 12780 -1077 -3506 1747 C ATOM 1765 CE2 PHE A 221 -250.027 30.157 30.041 1.00 88.33 C ANISOU 1765 CE2 PHE A 221 10462 10487 12611 -1163 -3296 1511 C ATOM 1766 CZ PHE A 221 -251.381 30.331 29.839 1.00 89.92 C ANISOU 1766 CZ PHE A 221 10427 10694 13043 -1220 -3523 1642 C ATOM 1767 N CYS A 222 -247.625 30.731 33.780 1.00 85.22 N ANISOU 1767 N CYS A 222 10006 10075 12298 -693 -2402 1286 N ATOM 1768 CA CYS A 222 -247.175 29.342 33.793 1.00 78.34 C ANISOU 1768 CA CYS A 222 9287 9176 11302 -787 -2347 1189 C ATOM 1769 C CYS A 222 -247.479 28.676 35.128 1.00 78.18 C ANISOU 1769 C CYS A 222 9139 9147 11420 -765 -2179 1172 C ATOM 1770 O CYS A 222 -248.120 27.620 35.181 1.00 86.76 O ANISOU 1770 O CYS A 222 10189 10210 12566 -880 -2226 1171 O ATOM 1771 CB CYS A 222 -245.681 29.275 33.487 1.00 69.43 C ANISOU 1771 CB CYS A 222 8407 8029 9943 -752 -2240 1087 C ATOM 1772 SG CYS A 222 -245.264 29.674 31.777 1.00 79.36 S ANISOU 1772 SG CYS A 222 9883 9298 10971 -845 -2418 1083 S ATOM 1773 N TYR A 223 -247.034 29.292 36.222 1.00 68.81 N ANISOU 1773 N TYR A 223 7891 7976 10276 -633 -1984 1162 N ATOM 1774 CA TYR A 223 -247.288 28.718 37.537 1.00 72.02 C ANISOU 1774 CA TYR A 223 8200 8383 10779 -629 -1816 1154 C ATOM 1775 C TYR A 223 -248.765 28.770 37.898 1.00 75.98 C ANISOU 1775 C TYR A 223 8443 8910 11516 -674 -1848 1229 C ATOM 1776 O TYR A 223 -249.254 27.894 38.620 1.00 82.22 O ANISOU 1776 O TYR A 223 9166 9694 12379 -749 -1770 1233 O ATOM 1777 CB TYR A 223 -246.448 29.437 38.589 1.00 75.31 C ANISOU 1777 CB TYR A 223 8635 8821 11160 -495 -1614 1122 C ATOM 1778 CG TYR A 223 -244.985 29.063 38.543 1.00 77.69 C ANISOU 1778 CG TYR A 223 9160 9089 11268 -464 -1552 1047 C ATOM 1779 CD1 TYR A 223 -244.592 27.748 38.335 1.00 84.02 C ANISOU 1779 CD1 TYR A 223 10095 9834 11994 -548 -1574 1005 C ATOM 1780 CD2 TYR A 223 -243.997 30.025 38.699 1.00 74.82 C ANISOU 1780 CD2 TYR A 223 8863 8741 10825 -351 -1472 1017 C ATOM 1781 CE1 TYR A 223 -243.257 27.398 38.292 1.00 85.46 C ANISOU 1781 CE1 TYR A 223 10453 9972 12046 -509 -1513 934 C ATOM 1782 CE2 TYR A 223 -242.659 29.685 38.655 1.00 87.18 C ANISOU 1782 CE2 TYR A 223 10603 10274 12248 -323 -1416 950 C ATOM 1783 CZ TYR A 223 -242.295 28.371 38.452 1.00 89.54 C ANISOU 1783 CZ TYR A 223 11013 10514 12492 -396 -1435 909 C ATOM 1784 OH TYR A 223 -240.963 28.026 38.408 1.00 92.59 O ANISOU 1784 OH TYR A 223 11546 10855 12779 -356 -1375 840 O ATOM 1785 N GLY A 224 -249.488 29.774 37.408 1.00 73.97 N ANISOU 1785 N GLY A 224 8031 8674 11398 -635 -1961 1294 N ATOM 1786 CA GLY A 224 -250.916 29.852 37.639 1.00 67.64 C ANISOU 1786 CA GLY A 224 6950 7887 10862 -674 -2005 1364 C ATOM 1787 C GLY A 224 -251.644 28.661 37.055 1.00 66.11 C ANISOU 1787 C GLY A 224 6743 7677 10698 -848 -2170 1391 C ATOM 1788 O GLY A 224 -252.393 27.973 37.755 1.00 70.76 O ANISOU 1788 O GLY A 224 7190 8271 11426 -922 -2090 1403 O ATOM 1789 N GLN A 225 -251.420 28.407 35.762 1.00 64.52 N ANISOU 1789 N GLN A 225 6702 7456 10356 -930 -2396 1396 N ATOM 1790 CA GLN A 225 -251.996 27.228 35.125 1.00 76.22 C ANISOU 1790 CA GLN A 225 8216 8912 11831 -1113 -2563 1399 C ATOM 1791 C GLN A 225 -251.467 25.946 35.750 1.00 86.69 C ANISOU 1791 C GLN A 225 9684 10197 13059 -1176 -2412 1318 C ATOM 1792 O GLN A 225 -252.190 24.945 35.826 1.00 94.83 O ANISOU 1792 O GLN A 225 10652 11201 14180 -1315 -2461 1330 O ATOM 1793 CB GLN A 225 -251.703 27.241 33.626 1.00 78.18 C ANISOU 1793 CB GLN A 225 8661 9150 11892 -1198 -2812 1397 C ATOM 1794 CG GLN A 225 -252.394 28.355 32.850 1.00 91.92 C ANISOU 1794 CG GLN A 225 10266 10920 13740 -1179 -3037 1515 C ATOM 1795 CD GLN A 225 -253.888 28.141 32.724 1.00107.16 C ANISOU 1795 CD GLN A 225 11921 12855 15939 -1282 -3222 1615 C ATOM 1796 OE1 GLN A 225 -254.676 28.779 33.421 1.00108.26 O ANISOU 1796 OE1 GLN A 225 11764 13006 16362 -1193 -3161 1684 O ATOM 1797 NE2 GLN A 225 -254.286 27.235 31.837 1.00116.64 N ANISOU 1797 NE2 GLN A 225 13212 14043 17063 -1475 -3444 1615 N ATOM 1798 N LEU A 226 -250.214 25.959 36.206 1.00 84.66 N ANISOU 1798 N LEU A 226 9610 9923 12633 -1080 -2240 1244 N ATOM 1799 CA LEU A 226 -249.629 24.761 36.799 1.00 78.23 C ANISOU 1799 CA LEU A 226 8933 9049 11741 -1128 -2115 1182 C ATOM 1800 C LEU A 226 -250.347 24.382 38.089 1.00 85.82 C ANISOU 1800 C LEU A 226 9715 10022 12869 -1154 -1965 1232 C ATOM 1801 O LEU A 226 -250.782 23.237 38.257 1.00 92.66 O ANISOU 1801 O LEU A 226 10583 10838 13785 -1286 -1981 1240 O ATOM 1802 CB LEU A 226 -248.138 24.980 37.049 1.00 69.66 C ANISOU 1802 CB LEU A 226 8047 7945 10477 -1007 -1977 1108 C ATOM 1803 CG LEU A 226 -247.285 23.776 37.451 1.00 63.25 C ANISOU 1803 CG LEU A 226 7408 7045 9578 -1038 -1884 1044 C ATOM 1804 CD1 LEU A 226 -245.903 23.904 36.839 1.00 60.69 C ANISOU 1804 CD1 LEU A 226 7299 6686 9074 -965 -1865 950 C ATOM 1805 CD2 LEU A 226 -247.182 23.658 38.962 1.00 50.50 C ANISOU 1805 CD2 LEU A 226 5723 5441 8024 -989 -1695 1085 C ATOM 1806 N VAL A 227 -250.482 25.336 39.015 1.00 81.05 N ANISOU 1806 N VAL A 227 8965 9481 12348 -1041 -1808 1263 N ATOM 1807 CA VAL A 227 -251.194 25.064 40.262 1.00 75.51 C ANISOU 1807 CA VAL A 227 8098 8806 11787 -1079 -1635 1303 C ATOM 1808 C VAL A 227 -252.647 24.716 39.976 1.00 81.81 C ANISOU 1808 C VAL A 227 8666 9612 12807 -1207 -1744 1365 C ATOM 1809 O VAL A 227 -253.248 23.877 40.658 1.00 87.82 O ANISOU 1809 O VAL A 227 9348 10363 13658 -1322 -1660 1394 O ATOM 1810 CB VAL A 227 -251.077 26.262 41.224 1.00 71.93 C ANISOU 1810 CB VAL A 227 7540 8419 11373 -938 -1437 1298 C ATOM 1811 CG1 VAL A 227 -251.807 25.973 42.529 1.00 62.23 C ANISOU 1811 CG1 VAL A 227 6160 7226 10259 -999 -1230 1325 C ATOM 1812 CG2 VAL A 227 -249.623 26.583 41.494 1.00 79.58 C ANISOU 1812 CG2 VAL A 227 8731 9379 12128 -827 -1352 1241 C ATOM 1813 N PHE A 228 -253.234 25.352 38.960 1.00 81.24 N ANISOU 1813 N PHE A 228 8480 9555 12831 -1200 -1944 1396 N ATOM 1814 CA PHE A 228 -254.602 25.026 38.574 1.00 83.23 C ANISOU 1814 CA PHE A 228 8501 9811 13311 -1329 -2092 1463 C ATOM 1815 C PHE A 228 -254.703 23.586 38.085 1.00 79.73 C ANISOU 1815 C PHE A 228 8189 9303 12802 -1516 -2220 1450 C ATOM 1816 O PHE A 228 -255.617 22.849 38.473 1.00 75.04 O ANISOU 1816 O PHE A 228 7442 8700 12372 -1648 -2204 1489 O ATOM 1817 CB PHE A 228 -255.086 25.998 37.498 1.00 80.19 C ANISOU 1817 CB PHE A 228 7999 9445 13023 -1287 -2327 1516 C ATOM 1818 CG PHE A 228 -256.459 25.688 36.977 1.00 91.71 C ANISOU 1818 CG PHE A 228 9216 10905 14726 -1423 -2531 1596 C ATOM 1819 CD1 PHE A 228 -257.585 26.110 37.663 1.00 88.40 C ANISOU 1819 CD1 PHE A 228 8445 10517 14628 -1404 -2439 1652 C ATOM 1820 CD2 PHE A 228 -256.624 24.976 35.800 1.00 99.28 C ANISOU 1820 CD2 PHE A 228 10292 11831 15600 -1579 -2813 1606 C ATOM 1821 CE1 PHE A 228 -258.850 25.828 37.186 1.00 87.64 C ANISOU 1821 CE1 PHE A 228 8094 10418 14786 -1531 -2636 1731 C ATOM 1822 CE2 PHE A 228 -257.887 24.689 35.318 1.00 98.98 C ANISOU 1822 CE2 PHE A 228 10025 11793 15789 -1719 -3027 1686 C ATOM 1823 CZ PHE A 228 -259.001 25.116 36.011 1.00 93.30 C ANISOU 1823 CZ PHE A 228 8931 11105 15413 -1692 -2946 1755 C ATOM 1824 N THR A 229 -253.767 23.168 37.229 1.00 81.48 N ANISOU 1824 N THR A 229 8693 9472 12793 -1534 -2335 1385 N ATOM 1825 CA THR A 229 -253.793 21.803 36.710 1.00 71.35 C ANISOU 1825 CA THR A 229 7558 8106 11447 -1709 -2450 1347 C ATOM 1826 C THR A 229 -253.557 20.785 37.820 1.00 64.41 C ANISOU 1826 C THR A 229 6731 7170 10573 -1755 -2253 1337 C ATOM 1827 O THR A 229 -254.226 19.745 37.873 1.00 72.61 O ANISOU 1827 O THR A 229 7727 8152 11708 -1920 -2301 1358 O ATOM 1828 CB THR A 229 -252.749 21.647 35.602 1.00 64.81 C ANISOU 1828 CB THR A 229 7029 7229 10367 -1705 -2569 1253 C ATOM 1829 OG1 THR A 229 -253.114 22.464 34.482 1.00 77.40 O ANISOU 1829 OG1 THR A 229 8589 8875 11945 -1714 -2790 1284 O ATOM 1830 CG2 THR A 229 -252.650 20.197 35.151 1.00 61.05 C ANISOU 1830 CG2 THR A 229 6730 6643 9824 -1874 -2647 1182 C ATOM 1831 N VAL A 230 -252.619 21.074 38.724 1.00 62.78 N ANISOU 1831 N VAL A 230 6618 6971 10264 -1621 -2042 1317 N ATOM 1832 CA VAL A 230 -252.319 20.150 39.814 1.00 69.68 C ANISOU 1832 CA VAL A 230 7562 7788 11124 -1666 -1872 1332 C ATOM 1833 C VAL A 230 -253.518 20.017 40.748 1.00 73.82 C ANISOU 1833 C VAL A 230 7838 8361 11848 -1760 -1761 1419 C ATOM 1834 O VAL A 230 -253.900 18.908 41.139 1.00 68.53 O ANISOU 1834 O VAL A 230 7176 7626 11236 -1910 -1739 1455 O ATOM 1835 CB VAL A 230 -251.058 20.607 40.570 1.00 61.76 C ANISOU 1835 CB VAL A 230 6705 6797 9966 -1507 -1699 1304 C ATOM 1836 CG1 VAL A 230 -250.842 19.761 41.812 1.00 59.08 C ANISOU 1836 CG1 VAL A 230 6421 6410 9617 -1561 -1539 1352 C ATOM 1837 CG2 VAL A 230 -249.842 20.537 39.661 1.00 55.16 C ANISOU 1837 CG2 VAL A 230 6110 5896 8954 -1436 -1788 1211 C ATOM 1838 N LYS A 231 -254.133 21.145 41.116 1.00 81.87 N ANISOU 1838 N LYS A 231 8630 9488 12990 -1678 -1679 1450 N ATOM 1839 CA LYS A 231 -255.290 21.095 42.006 1.00 85.72 C ANISOU 1839 CA LYS A 231 8858 10028 13685 -1765 -1537 1516 C ATOM 1840 C LYS A 231 -256.474 20.414 41.334 1.00 89.63 C ANISOU 1840 C LYS A 231 9186 10494 14377 -1942 -1716 1559 C ATOM 1841 O LYS A 231 -257.252 19.708 41.989 1.00 66.35 O ANISOU 1841 O LYS A 231 6111 7539 11562 -2087 -1621 1611 O ATOM 1842 CB LYS A 231 -255.676 22.503 42.459 1.00 81.77 C ANISOU 1842 CB LYS A 231 8139 9630 13300 -1625 -1402 1516 C ATOM 1843 CG LYS A 231 -254.701 23.127 43.435 1.00 75.35 C ANISOU 1843 CG LYS A 231 7457 8854 12317 -1488 -1178 1477 C ATOM 1844 CD LYS A 231 -255.203 24.461 43.950 1.00 69.10 C ANISOU 1844 CD LYS A 231 6438 8147 11668 -1369 -1021 1460 C ATOM 1845 CE LYS A 231 -254.342 24.932 45.102 1.00 65.87 C ANISOU 1845 CE LYS A 231 6166 7778 11084 -1279 -776 1416 C ATOM 1846 NZ LYS A 231 -254.351 23.941 46.214 1.00 71.99 N ANISOU 1846 NZ LYS A 231 7023 8554 11774 -1421 -602 1453 N ATOM 1847 N GLU A 232 -256.629 20.615 40.026 1.00 79.99 N ANISOU 1847 N GLU A 232 7967 9257 13168 -1949 -1982 1542 N ATOM 1848 CA GLU A 232 -257.727 19.984 39.304 1.00 79.02 C ANISOU 1848 CA GLU A 232 7696 9106 13221 -2131 -2194 1582 C ATOM 1849 C GLU A 232 -257.554 18.470 39.268 1.00 90.97 C ANISOU 1849 C GLU A 232 9397 10507 14660 -2309 -2232 1564 C ATOM 1850 O GLU A 232 -258.504 17.719 39.519 1.00 99.76 O ANISOU 1850 O GLU A 232 10357 11597 15950 -2483 -2240 1616 O ATOM 1851 CB GLU A 232 -257.813 20.557 37.891 1.00 85.06 C ANISOU 1851 CB GLU A 232 8472 9881 13965 -2110 -2490 1573 C ATOM 1852 CG GLU A 232 -259.186 20.476 37.258 1.00106.56 C ANISOU 1852 CG GLU A 232 10923 12620 16944 -2254 -2717 1645 C ATOM 1853 CD GLU A 232 -259.238 21.186 35.918 1.00123.46 C ANISOU 1853 CD GLU A 232 13085 14780 19043 -2229 -3023 1659 C ATOM 1854 OE1 GLU A 232 -258.160 21.464 35.350 1.00130.89 O ANISOU 1854 OE1 GLU A 232 14306 15707 19718 -2144 -3064 1595 O ATOM 1855 OE2 GLU A 232 -260.353 21.471 35.433 1.00124.50 O ANISOU 1855 OE2 GLU A 232 12952 14940 19412 -2302 -3226 1742 O ATOM 1856 N ALA A 233 -256.341 18.006 38.961 1.00 89.57 N ANISOU 1856 N ALA A 233 9543 10249 14243 -2267 -2249 1488 N ATOM 1857 CA ALA A 233 -256.084 16.570 38.924 1.00 84.32 C ANISOU 1857 CA ALA A 233 9068 9446 13524 -2417 -2280 1460 C ATOM 1858 C ALA A 233 -256.162 15.956 40.316 1.00 81.05 C ANISOU 1858 C ALA A 233 8624 9006 13165 -2468 -2046 1531 C ATOM 1859 O ALA A 233 -256.627 14.821 40.476 1.00 76.92 O ANISOU 1859 O ALA A 233 8110 8390 12728 -2650 -2070 1563 O ATOM 1860 CB ALA A 233 -254.718 16.299 38.293 1.00 78.50 C ANISOU 1860 CB ALA A 233 8661 8618 12546 -2337 -2328 1351 C ATOM 1861 N ALA A 234 -255.711 16.692 41.336 1.00 77.59 N ANISOU 1861 N ALA A 234 8166 8648 12669 -2325 -1824 1557 N ATOM 1862 CA ALA A 234 -255.786 16.189 42.704 1.00 77.30 C ANISOU 1862 CA ALA A 234 8118 8604 12648 -2389 -1599 1635 C ATOM 1863 C ALA A 234 -257.226 16.079 43.184 1.00 83.55 C ANISOU 1863 C ALA A 234 8612 9457 13676 -2543 -1524 1714 C ATOM 1864 O ALA A 234 -257.543 15.199 43.992 1.00 82.63 O ANISOU 1864 O ALA A 234 8501 9295 13601 -2694 -1408 1786 O ATOM 1865 CB ALA A 234 -254.980 17.087 43.644 1.00 64.38 C ANISOU 1865 CB ALA A 234 6537 7051 10872 -2213 -1390 1633 C ATOM 1866 N ALA A 235 -258.108 16.960 42.703 1.00 82.24 N ANISOU 1866 N ALA A 235 8178 9389 13680 -2512 -1590 1709 N ATOM 1867 CA ALA A 235 -259.516 16.872 43.072 1.00 75.61 C ANISOU 1867 CA ALA A 235 7015 8603 13111 -2655 -1526 1776 C ATOM 1868 C ALA A 235 -260.144 15.579 42.572 1.00 91.13 C ANISOU 1868 C ALA A 235 8979 10462 15185 -2891 -1696 1810 C ATOM 1869 O ALA A 235 -261.075 15.059 43.196 1.00109.27 O ANISOU 1869 O ALA A 235 11090 12767 17660 -3059 -1586 1880 O ATOM 1870 CB ALA A 235 -260.279 18.077 42.526 1.00 72.87 C ANISOU 1870 CB ALA A 235 6372 8356 12961 -2558 -1606 1768 C ATOM 1871 N GLN A 236 -259.649 15.046 41.455 1.00 92.21 N ANISOU 1871 N GLN A 236 9324 10496 15215 -2917 -1951 1751 N ATOM 1872 CA GLN A 236 -260.147 13.784 40.925 1.00 86.77 C ANISOU 1872 CA GLN A 236 8675 9685 14609 -3146 -2124 1760 C ATOM 1873 C GLN A 236 -259.589 12.570 41.653 1.00 80.10 C ANISOU 1873 C GLN A 236 8060 8703 13669 -3245 -2005 1786 C ATOM 1874 O GLN A 236 -260.035 11.450 41.387 1.00 77.52 O ANISOU 1874 O GLN A 236 7764 8256 13432 -3450 -2113 1802 O ATOM 1875 CB GLN A 236 -259.822 13.676 39.434 1.00 86.81 C ANISOU 1875 CB GLN A 236 8840 9627 14518 -3151 -2431 1667 C ATOM 1876 CG GLN A 236 -260.851 14.337 38.537 1.00 90.61 C ANISOU 1876 CG GLN A 236 9060 10196 15173 -3193 -2656 1684 C ATOM 1877 CD GLN A 236 -262.139 13.542 38.454 1.00 97.07 C ANISOU 1877 CD GLN A 236 9654 10982 16248 -3445 -2764 1747 C ATOM 1878 OE1 GLN A 236 -262.180 12.364 38.810 1.00103.90 O ANISOU 1878 OE1 GLN A 236 10621 11731 17124 -3610 -2717 1756 O ATOM 1879 NE2 GLN A 236 -263.200 14.184 37.980 1.00 97.58 N ANISOU 1879 NE2 GLN A 236 9403 11137 16537 -3479 -2919 1798 N ATOM 1880 N GLN A 237 -258.627 12.755 42.554 1.00 82.92 N ANISOU 1880 N GLN A 237 8582 9066 13856 -3113 -1802 1799 N ATOM 1881 CA GLN A 237 -258.043 11.650 43.305 1.00 80.61 C ANISOU 1881 CA GLN A 237 8511 8636 13480 -3196 -1706 1851 C ATOM 1882 C GLN A 237 -257.962 12.022 44.787 1.00 81.77 C ANISOU 1882 C GLN A 237 8616 8878 13576 -3161 -1415 1946 C ATOM 1883 O GLN A 237 -256.906 11.986 45.412 1.00 93.29 O ANISOU 1883 O GLN A 237 10291 10303 14853 -3061 -1320 1961 O ATOM 1884 CB GLN A 237 -256.664 11.275 42.759 1.00 82.39 C ANISOU 1884 CB GLN A 237 9066 8724 13514 -3080 -1809 1762 C ATOM 1885 CG GLN A 237 -256.656 10.761 41.326 1.00 95.03 C ANISOU 1885 CG GLN A 237 10766 10213 15128 -3143 -2070 1648 C ATOM 1886 CD GLN A 237 -255.342 10.097 40.961 1.00102.97 C ANISOU 1886 CD GLN A 237 12096 11044 15985 -3067 -2120 1558 C ATOM 1887 OE1 GLN A 237 -254.706 9.463 41.802 1.00100.30 O ANISOU 1887 OE1 GLN A 237 11899 10597 15613 -3058 -2007 1618 O ATOM 1888 NE2 GLN A 237 -254.925 10.242 39.705 1.00109.16 N ANISOU 1888 NE2 GLN A 237 12998 11795 16683 -3017 -2286 1416 N ATOM 1889 N GLN A 238 -259.105 12.389 45.371 1.00 75.41 N ANISOU 1889 N GLN A 238 7522 8196 12936 -3255 -1268 2007 N ATOM 1890 CA GLN A 238 -259.108 12.771 46.779 1.00 83.12 C ANISOU 1890 CA GLN A 238 8461 9274 13845 -3247 -967 2080 C ATOM 1891 C GLN A 238 -258.948 11.581 47.714 1.00 88.90 C ANISOU 1891 C GLN A 238 9367 9899 14513 -3428 -864 2200 C ATOM 1892 O GLN A 238 -258.720 11.787 48.910 1.00 83.30 O ANISOU 1892 O GLN A 238 8713 9260 13678 -3434 -632 2268 O ATOM 1893 CB GLN A 238 -260.387 13.528 47.127 1.00 92.52 C ANISOU 1893 CB GLN A 238 9282 10622 15250 -3294 -807 2092 C ATOM 1894 CG GLN A 238 -260.481 14.904 46.504 1.00101.01 C ANISOU 1894 CG GLN A 238 10181 11812 16387 -3088 -857 1998 C ATOM 1895 CD GLN A 238 -261.625 15.713 47.068 1.00110.71 C ANISOU 1895 CD GLN A 238 11043 13182 17839 -3105 -644 2006 C ATOM 1896 OE1 GLN A 238 -262.266 15.309 48.038 1.00110.34 O ANISOU 1896 OE1 GLN A 238 10891 13170 17863 -3268 -413 2071 O ATOM 1897 NE2 GLN A 238 -261.890 16.864 46.462 1.00119.25 N ANISOU 1897 NE2 GLN A 238 11926 14339 19045 -2941 -715 1940 N ATOM 1898 N GLU A 239 -259.052 10.352 47.204 1.00100.16 N ANISOU 1898 N GLU A 239 10893 11150 16014 -3585 -1037 2229 N ATOM 1899 CA GLU A 239 -258.830 9.168 48.024 1.00101.98 C ANISOU 1899 CA GLU A 239 11311 11243 16195 -3754 -972 2356 C ATOM 1900 C GLU A 239 -257.352 8.881 48.261 1.00105.52 C ANISOU 1900 C GLU A 239 12095 11572 16427 -3618 -1016 2366 C ATOM 1901 O GLU A 239 -257.027 8.070 49.135 1.00107.42 O ANISOU 1901 O GLU A 239 12504 11711 16599 -3728 -948 2498 O ATOM 1902 CB GLU A 239 -259.493 7.945 47.380 1.00 92.03 C ANISOU 1902 CB GLU A 239 10032 9813 15121 -3975 -1146 2378 C ATOM 1903 CG GLU A 239 -258.839 7.464 46.085 1.00 90.63 C ANISOU 1903 CG GLU A 239 10035 9466 14935 -3905 -1428 2258 C ATOM 1904 CD GLU A 239 -259.250 8.272 44.864 1.00 88.27 C ANISOU 1904 CD GLU A 239 9566 9265 14709 -3815 -1591 2121 C ATOM 1905 OE1 GLU A 239 -259.851 9.355 45.031 1.00 92.59 O ANISOU 1905 OE1 GLU A 239 9862 10008 15310 -3748 -1492 2117 O ATOM 1906 OE2 GLU A 239 -258.973 7.819 43.732 1.00 79.71 O ANISOU 1906 OE2 GLU A 239 8604 8055 13628 -3819 -1821 2017 O ATOM 1907 N SER A 240 -256.457 9.519 47.511 1.00104.50 N ANISOU 1907 N SER A 240 12059 11449 16198 -3390 -1132 2241 N ATOM 1908 CA SER A 240 -255.019 9.322 47.650 1.00103.13 C ANISOU 1908 CA SER A 240 12169 11165 15853 -3243 -1179 2236 C ATOM 1909 C SER A 240 -254.465 10.419 48.552 1.00 98.55 C ANISOU 1909 C SER A 240 11599 10753 15093 -3091 -1001 2255 C ATOM 1910 O SER A 240 -254.457 11.595 48.175 1.00104.12 O ANISOU 1910 O SER A 240 12186 11605 15768 -2934 -976 2152 O ATOM 1911 CB SER A 240 -254.338 9.336 46.284 1.00102.46 C ANISOU 1911 CB SER A 240 12183 10982 15765 -3101 -1392 2077 C ATOM 1912 OG SER A 240 -252.931 9.250 46.415 1.00101.45 O ANISOU 1912 OG SER A 240 12291 10757 15499 -2941 -1417 2059 O ATOM 1913 N ALA A 241 -254.003 10.032 49.744 1.00106.87 N ANISOU 1913 N ALA A 241 11575 11317 17715 -3909 2180 -1983 N ATOM 1914 CA ALA A 241 -253.464 11.015 50.677 1.00103.43 C ANISOU 1914 CA ALA A 241 11243 10960 17095 -3674 2138 -1776 C ATOM 1915 C ALA A 241 -252.163 11.623 50.166 1.00108.67 C ANISOU 1915 C ALA A 241 12082 11581 17627 -3396 1892 -1653 C ATOM 1916 O ALA A 241 -251.880 12.795 50.439 1.00108.99 O ANISOU 1916 O ALA A 241 12105 11776 17530 -3175 1749 -1589 O ATOM 1917 CB ALA A 241 -253.252 10.378 52.050 1.00 91.18 C ANISOU 1917 CB ALA A 241 9912 9236 15495 -3780 2410 -1536 C ATOM 1918 N THR A 242 -251.365 10.851 49.424 1.00102.08 N ANISOU 1918 N THR A 242 11408 10535 16844 -3412 1855 -1636 N ATOM 1919 CA THR A 242 -250.117 11.384 48.887 1.00 95.82 C ANISOU 1919 CA THR A 242 10762 9713 15931 -3172 1642 -1541 C ATOM 1920 C THR A 242 -250.379 12.373 47.758 1.00 95.81 C ANISOU 1920 C THR A 242 10566 9966 15873 -3073 1373 -1720 C ATOM 1921 O THR A 242 -249.668 13.376 47.629 1.00 95.35 O ANISOU 1921 O THR A 242 10562 9996 15672 -2849 1184 -1627 O ATOM 1922 CB THR A 242 -249.219 10.245 48.403 1.00 91.34 C ANISOU 1922 CB THR A 242 10395 8848 15461 -3223 1703 -1507 C ATOM 1923 OG1 THR A 242 -249.880 9.524 47.356 1.00 91.33 O ANISOU 1923 OG1 THR A 242 10257 8836 15609 -3436 1726 -1775 O ATOM 1924 CG2 THR A 242 -248.903 9.292 49.547 1.00 90.15 C ANISOU 1924 CG2 THR A 242 10456 8417 15378 -3296 1939 -1276 C ATOM 1925 N THR A 243 -251.389 12.102 46.926 1.00 97.26 N ANISOU 1925 N THR A 243 10522 10270 16162 -3248 1343 -1967 N ATOM 1926 CA THR A 243 -251.776 13.053 45.888 1.00 90.27 C ANISOU 1926 CA THR A 243 9432 9650 15215 -3165 1064 -2112 C ATOM 1927 C THR A 243 -252.152 14.400 46.494 1.00 89.52 C ANISOU 1927 C THR A 243 9210 9749 15055 -2970 953 -2043 C ATOM 1928 O THR A 243 -251.742 15.455 45.993 1.00 84.02 O ANISOU 1928 O THR A 243 8508 9168 14247 -2773 707 -1998 O ATOM 1929 CB THR A 243 -252.936 12.489 45.065 1.00 84.89 C ANISOU 1929 CB THR A 243 8499 9092 14663 -3409 1059 -2387 C ATOM 1930 OG1 THR A 243 -252.470 11.403 44.255 1.00 83.34 O ANISOU 1930 OG1 THR A 243 8423 8731 14510 -3571 1114 -2492 O ATOM 1931 CG2 THR A 243 -253.541 13.561 44.171 1.00 84.02 C ANISOU 1931 CG2 THR A 243 8140 9290 14493 -3317 752 -2503 C ATOM 1932 N GLN A 244 -252.927 14.384 47.581 1.00 90.77 N ANISOU 1932 N GLN A 244 9268 9935 15286 -3031 1144 -2042 N ATOM 1933 CA GLN A 244 -253.259 15.628 48.267 1.00 92.14 C ANISOU 1933 CA GLN A 244 9324 10269 15418 -2846 1081 -2006 C ATOM 1934 C GLN A 244 -252.027 16.234 48.924 1.00 93.80 C ANISOU 1934 C GLN A 244 9799 10380 15460 -2633 1051 -1774 C ATOM 1935 O GLN A 244 -251.875 17.461 48.959 1.00 95.03 O ANISOU 1935 O GLN A 244 9910 10645 15552 -2423 880 -1743 O ATOM 1936 CB GLN A 244 -254.354 15.381 49.304 1.00 93.37 C ANISOU 1936 CB GLN A 244 9309 10489 15679 -2995 1338 -2089 C ATOM 1937 CG GLN A 244 -255.569 14.659 48.753 1.00 84.37 C ANISOU 1937 CG GLN A 244 7898 9440 14720 -3244 1403 -2327 C ATOM 1938 CD GLN A 244 -256.139 15.339 47.525 1.00 90.24 C ANISOU 1938 CD GLN A 244 8370 10397 15520 -3167 1093 -2499 C ATOM 1939 OE1 GLN A 244 -256.425 14.689 46.519 1.00 92.30 O ANISOU 1939 OE1 GLN A 244 8549 10684 15838 -3328 1016 -2639 O ATOM 1940 NE2 GLN A 244 -256.310 16.656 47.601 1.00 90.52 N ANISOU 1940 NE2 GLN A 244 8268 10583 15541 -2924 906 -2488 N ATOM 1941 N LYS A 245 -251.137 15.389 49.451 1.00 98.65 N ANISOU 1941 N LYS A 245 10684 10779 16018 -2684 1209 -1607 N ATOM 1942 CA LYS A 245 -249.907 15.894 50.050 1.00 99.40 C ANISOU 1942 CA LYS A 245 11022 10795 15952 -2493 1165 -1387 C ATOM 1943 C LYS A 245 -248.982 16.474 48.989 1.00 83.89 C ANISOU 1943 C LYS A 245 9128 8837 13910 -2330 903 -1364 C ATOM 1944 O LYS A 245 -248.340 17.507 49.214 1.00 82.05 O ANISOU 1944 O LYS A 245 8963 8653 13559 -2136 772 -1265 O ATOM 1945 CB LYS A 245 -249.209 14.779 50.830 1.00112.97 C ANISOU 1945 CB LYS A 245 12992 12281 17650 -2584 1373 -1200 C ATOM 1946 CG LYS A 245 -248.504 15.246 52.096 1.00124.16 C ANISOU 1946 CG LYS A 245 14586 13687 18901 -2462 1426 -983 C ATOM 1947 CD LYS A 245 -248.010 14.063 52.916 1.00130.89 C ANISOU 1947 CD LYS A 245 15665 14320 19746 -2576 1625 -775 C ATOM 1948 CE LYS A 245 -247.481 14.504 54.271 1.00129.97 C ANISOU 1948 CE LYS A 245 15704 14244 19432 -2495 1682 -564 C ATOM 1949 NZ LYS A 245 -247.045 13.343 55.095 1.00127.97 N ANISOU 1949 NZ LYS A 245 15676 13782 19163 -2609 1852 -320 N ATOM 1950 N ALA A 246 -248.908 15.828 47.821 1.00 77.05 N ANISOU 1950 N ALA A 246 8247 7930 13100 -2427 836 -1468 N ATOM 1951 CA ALA A 246 -248.113 16.369 46.723 1.00 83.72 C ANISOU 1951 CA ALA A 246 9144 8817 13847 -2311 601 -1467 C ATOM 1952 C ALA A 246 -248.711 17.669 46.199 1.00 92.68 C ANISOU 1952 C ALA A 246 10091 10176 14948 -2198 362 -1535 C ATOM 1953 O ALA A 246 -247.976 18.601 45.854 1.00 90.45 O ANISOU 1953 O ALA A 246 9886 9933 14549 -2036 176 -1444 O ATOM 1954 CB ALA A 246 -247.996 15.341 45.599 1.00 70.16 C ANISOU 1954 CB ALA A 246 7440 7032 12186 -2474 610 -1603 C ATOM 1955 N GLU A 247 -250.041 17.749 46.130 1.00 95.14 N ANISOU 1955 N GLU A 247 10145 10626 15377 -2282 359 -1689 N ATOM 1956 CA GLU A 247 -250.682 18.988 45.700 1.00 86.48 C ANISOU 1956 CA GLU A 247 8846 9722 14292 -2150 119 -1739 C ATOM 1957 C GLU A 247 -250.395 20.123 46.676 1.00 80.74 C ANISOU 1957 C GLU A 247 8164 8986 13527 -1938 107 -1620 C ATOM 1958 O GLU A 247 -250.125 21.257 46.260 1.00 69.14 O ANISOU 1958 O GLU A 247 6688 7573 12007 -1766 -121 -1562 O ATOM 1959 CB GLU A 247 -252.189 18.769 45.542 1.00 82.13 C ANISOU 1959 CB GLU A 247 7976 9320 13909 -2278 136 -1940 C ATOM 1960 CG GLU A 247 -252.993 20.041 45.306 1.00 88.43 C ANISOU 1960 CG GLU A 247 8521 10298 14780 -2115 -97 -1989 C ATOM 1961 CD GLU A 247 -253.497 20.665 46.597 1.00103.20 C ANISOU 1961 CD GLU A 247 10287 12176 16749 -2006 49 -1999 C ATOM 1962 OE1 GLU A 247 -254.160 19.955 47.382 1.00112.91 O ANISOU 1962 OE1 GLU A 247 11424 13405 18071 -2158 312 -2095 O ATOM 1963 OE2 GLU A 247 -253.221 21.861 46.833 1.00 99.01 O ANISOU 1963 OE2 GLU A 247 9771 11647 16199 -1784 -84 -1920 O ATOM 1964 N LYS A 248 -250.439 19.837 47.980 1.00 83.65 N ANISOU 1964 N LYS A 248 8588 9284 13909 -1963 354 -1580 N ATOM 1965 CA LYS A 248 -250.202 20.880 48.975 1.00 87.06 C ANISOU 1965 CA LYS A 248 9060 9727 14293 -1790 367 -1505 C ATOM 1966 C LYS A 248 -248.774 21.409 48.899 1.00 95.50 C ANISOU 1966 C LYS A 248 10382 10704 15198 -1645 246 -1328 C ATOM 1967 O LYS A 248 -248.548 22.619 49.016 1.00 93.60 O ANISOU 1967 O LYS A 248 10138 10495 14929 -1472 107 -1295 O ATOM 1968 CB LYS A 248 -250.507 20.354 50.379 1.00 88.29 C ANISOU 1968 CB LYS A 248 9244 9853 14448 -1890 670 -1498 C ATOM 1969 CG LYS A 248 -251.992 20.303 50.731 1.00101.06 C ANISOU 1969 CG LYS A 248 10565 11605 16230 -1992 802 -1694 C ATOM 1970 CD LYS A 248 -252.223 19.677 52.105 1.00113.56 C ANISOU 1970 CD LYS A 248 12212 13166 17770 -2139 1130 -1669 C ATOM 1971 CE LYS A 248 -251.727 20.569 53.238 1.00119.94 C ANISOU 1971 CE LYS A 248 13133 13997 18441 -2001 1186 -1593 C ATOM 1972 NZ LYS A 248 -252.622 21.736 53.474 1.00125.21 N ANISOU 1972 NZ LYS A 248 13532 14814 19227 -1879 1152 -1785 N ATOM 1973 N GLU A 249 -247.794 20.524 48.696 1.00101.14 N ANISOU 1973 N GLU A 249 11308 11295 15827 -1713 301 -1224 N ATOM 1974 CA GLU A 249 -246.405 20.973 48.657 1.00101.10 C ANISOU 1974 CA GLU A 249 11519 11217 15678 -1587 202 -1069 C ATOM 1975 C GLU A 249 -246.065 21.677 47.348 1.00 91.30 C ANISOU 1975 C GLU A 249 10262 10033 14395 -1515 -60 -1077 C ATOM 1976 O GLU A 249 -245.208 22.567 47.336 1.00 91.67 O ANISOU 1976 O GLU A 249 10419 10067 14343 -1384 -182 -976 O ATOM 1977 CB GLU A 249 -245.456 19.795 48.895 1.00115.47 C ANISOU 1977 CB GLU A 249 13542 12880 17451 -1664 345 -959 C ATOM 1978 CG GLU A 249 -245.464 18.732 47.809 1.00136.00 C ANISOU 1978 CG GLU A 249 16134 15420 20119 -1802 353 -1043 C ATOM 1979 CD GLU A 249 -244.464 17.621 48.074 1.00149.33 C ANISOU 1979 CD GLU A 249 18017 16913 21808 -1842 491 -936 C ATOM 1980 OE1 GLU A 249 -243.611 17.790 48.971 1.00152.43 O ANISOU 1980 OE1 GLU A 249 18556 17241 22119 -1740 527 -768 O ATOM 1981 OE2 GLU A 249 -244.531 16.579 47.387 1.00152.66 O ANISOU 1981 OE2 GLU A 249 18438 17244 22323 -1973 558 -1026 O ATOM 1982 N VAL A 250 -246.716 21.303 46.244 1.00 85.30 N ANISOU 1982 N VAL A 250 9372 9347 13693 -1618 -149 -1194 N ATOM 1983 CA VAL A 250 -246.514 22.029 44.993 1.00 73.71 C ANISOU 1983 CA VAL A 250 7885 7969 12154 -1571 -412 -1188 C ATOM 1984 C VAL A 250 -247.077 23.440 45.107 1.00 79.55 C ANISOU 1984 C VAL A 250 8499 8787 12942 -1410 -592 -1169 C ATOM 1985 O VAL A 250 -246.471 24.408 44.630 1.00 81.50 O ANISOU 1985 O VAL A 250 8826 9036 13104 -1301 -783 -1067 O ATOM 1986 CB VAL A 250 -247.141 21.259 43.816 1.00 71.23 C ANISOU 1986 CB VAL A 250 7453 7745 11864 -1743 -470 -1329 C ATOM 1987 CG1 VAL A 250 -247.207 22.138 42.576 1.00 65.78 C ANISOU 1987 CG1 VAL A 250 6710 7197 11084 -1704 -770 -1312 C ATOM 1988 CG2 VAL A 250 -246.343 20.002 43.525 1.00 73.53 C ANISOU 1988 CG2 VAL A 250 7900 7925 12112 -1880 -316 -1355 C ATOM 1989 N THR A 251 -248.237 23.580 45.751 1.00 81.21 N ANISOU 1989 N THR A 251 8504 9047 13307 -1394 -523 -1272 N ATOM 1990 CA THR A 251 -248.821 24.900 45.954 1.00 78.65 C ANISOU 1990 CA THR A 251 8034 8767 13082 -1219 -671 -1281 C ATOM 1991 C THR A 251 -247.910 25.776 46.804 1.00 82.24 C ANISOU 1991 C THR A 251 8662 9117 13466 -1072 -643 -1170 C ATOM 1992 O THR A 251 -247.651 26.935 46.459 1.00 89.73 O ANISOU 1992 O THR A 251 9632 10044 14417 -930 -845 -1099 O ATOM 1993 CB THR A 251 -250.198 24.775 46.605 1.00 73.76 C ANISOU 1993 CB THR A 251 7144 8224 12659 -1240 -547 -1448 C ATOM 1994 OG1 THR A 251 -251.030 23.928 45.802 1.00 73.76 O ANISOU 1994 OG1 THR A 251 6970 8330 12724 -1400 -575 -1566 O ATOM 1995 CG2 THR A 251 -250.847 26.142 46.739 1.00 69.85 C ANISOU 1995 CG2 THR A 251 6465 7758 12316 -1038 -707 -1485 C ATOM 1996 N ARG A 252 -247.411 25.237 47.920 1.00 82.42 N ANISOU 1996 N ARG A 252 8817 9075 13425 -1115 -402 -1147 N ATOM 1997 CA ARG A 252 -246.553 26.027 48.798 1.00 88.25 C ANISOU 1997 CA ARG A 252 9711 9742 14078 -998 -373 -1061 C ATOM 1998 C ARG A 252 -245.262 26.434 48.097 1.00 84.89 C ANISOU 1998 C ARG A 252 9485 9258 13513 -951 -537 -915 C ATOM 1999 O ARG A 252 -244.742 27.532 48.331 1.00 88.31 O ANISOU 1999 O ARG A 252 9989 9647 13919 -831 -631 -861 O ATOM 2000 CB ARG A 252 -246.237 25.241 50.074 1.00 96.28 C ANISOU 2000 CB ARG A 252 10839 10728 15014 -1078 -104 -1039 C ATOM 2001 CG ARG A 252 -247.418 25.047 51.011 1.00119.54 C ANISOU 2001 CG ARG A 252 13610 13743 18065 -1132 96 -1179 C ATOM 2002 CD ARG A 252 -247.005 24.316 52.286 1.00133.01 C ANISOU 2002 CD ARG A 252 15468 15428 19641 -1229 348 -1112 C ATOM 2003 NE ARG A 252 -248.055 24.323 53.305 1.00146.67 N ANISOU 2003 NE ARG A 252 17049 17248 21431 -1289 558 -1248 N ATOM 2004 CZ ARG A 252 -248.941 23.347 53.480 1.00147.33 C ANISOU 2004 CZ ARG A 252 17020 17370 21586 -1457 740 -1319 C ATOM 2005 NH1 ARG A 252 -248.915 22.277 52.699 1.00149.89 N ANISOU 2005 NH1 ARG A 252 17370 17634 21946 -1575 730 -1274 N ATOM 2006 NH2 ARG A 252 -249.858 23.442 54.436 1.00143.02 N ANISOU 2006 NH2 ARG A 252 16333 16926 21081 -1522 947 -1453 N ATOM 2007 N MET A 253 -244.729 25.563 47.232 1.00 76.76 N ANISOU 2007 N MET A 253 8540 8225 12400 -1059 -558 -870 N ATOM 2008 CA MET A 253 -243.472 25.870 46.558 1.00 75.33 C ANISOU 2008 CA MET A 253 8534 8008 12079 -1039 -680 -752 C ATOM 2009 C MET A 253 -243.659 26.923 45.472 1.00 72.67 C ANISOU 2009 C MET A 253 8151 7717 11744 -982 -944 -719 C ATOM 2010 O MET A 253 -242.824 27.822 45.328 1.00 78.89 O ANISOU 2010 O MET A 253 9059 8461 12454 -912 -1055 -616 O ATOM 2011 CB MET A 253 -242.861 24.593 45.982 1.00 83.42 C ANISOU 2011 CB MET A 253 9649 9015 13033 -1173 -595 -748 C ATOM 2012 CG MET A 253 -241.890 23.914 46.935 1.00 94.78 C ANISOU 2012 CG MET A 253 11238 10357 14417 -1175 -414 -674 C ATOM 2013 SD MET A 253 -240.419 24.916 47.239 1.00106.96 S ANISOU 2013 SD MET A 253 12947 11866 15825 -1060 -502 -538 S ATOM 2014 CE MET A 253 -239.354 24.388 45.897 1.00107.77 C ANISOU 2014 CE MET A 253 13138 11970 15841 -1139 -562 -520 C ATOM 2015 N VAL A 254 -244.740 26.830 44.694 1.00 70.52 N ANISOU 2015 N VAL A 254 7704 7535 11555 -1020 -1056 -794 N ATOM 2016 CA VAL A 254 -245.028 27.866 43.706 1.00 71.76 C ANISOU 2016 CA VAL A 254 7809 7738 11719 -955 -1337 -730 C ATOM 2017 C VAL A 254 -245.227 29.211 44.394 1.00 71.72 C ANISOU 2017 C VAL A 254 7770 7645 11837 -769 -1413 -694 C ATOM 2018 O VAL A 254 -244.752 30.248 43.914 1.00 75.32 O ANISOU 2018 O VAL A 254 8314 8046 12257 -695 -1600 -570 O ATOM 2019 CB VAL A 254 -246.252 27.471 42.860 1.00 74.36 C ANISOU 2019 CB VAL A 254 7924 8203 12126 -1027 -1454 -823 C ATOM 2020 CG1 VAL A 254 -246.745 28.664 42.059 1.00 79.88 C ANISOU 2020 CG1 VAL A 254 8536 8941 12873 -920 -1768 -733 C ATOM 2021 CG2 VAL A 254 -245.902 26.319 41.932 1.00 72.18 C ANISOU 2021 CG2 VAL A 254 7713 8011 11702 -1226 -1419 -865 C ATOM 2022 N ILE A 255 -245.921 29.213 45.535 1.00 67.20 N ANISOU 2022 N ILE A 255 7072 7049 11413 -705 -1253 -811 N ATOM 2023 CA ILE A 255 -246.111 30.447 46.293 1.00 66.84 C ANISOU 2023 CA ILE A 255 6986 6909 11501 -533 -1283 -827 C ATOM 2024 C ILE A 255 -244.764 31.025 46.708 1.00 68.16 C ANISOU 2024 C ILE A 255 7395 6971 11534 -503 -1262 -720 C ATOM 2025 O ILE A 255 -244.497 32.218 46.525 1.00 71.23 O ANISOU 2025 O ILE A 255 7832 7262 11970 -395 -1420 -650 O ATOM 2026 CB ILE A 255 -247.016 30.195 47.513 1.00 68.52 C ANISOU 2026 CB ILE A 255 7031 7147 11857 -510 -1059 -1005 C ATOM 2027 CG1 ILE A 255 -248.454 29.926 47.063 1.00 66.95 C ANISOU 2027 CG1 ILE A 255 6540 7052 11845 -515 -1117 -1127 C ATOM 2028 CG2 ILE A 255 -246.954 31.373 48.479 1.00 65.19 C ANISOU 2028 CG2 ILE A 255 6611 6623 11534 -358 -1024 -1057 C ATOM 2029 CD1 ILE A 255 -249.382 29.535 48.190 1.00 68.20 C ANISOU 2029 CD1 ILE A 255 6514 7264 12133 -536 -864 -1318 C ATOM 2030 N ILE A 256 -243.890 30.179 47.259 1.00 69.05 N ANISOU 2030 N ILE A 256 7655 7093 11488 -600 -1075 -702 N ATOM 2031 CA ILE A 256 -242.579 30.638 47.712 1.00 67.34 C ANISOU 2031 CA ILE A 256 7642 6803 11140 -583 -1052 -614 C ATOM 2032 C ILE A 256 -241.796 31.260 46.562 1.00 65.15 C ANISOU 2032 C ILE A 256 7483 6494 10778 -592 -1262 -475 C ATOM 2033 O ILE A 256 -241.165 32.313 46.719 1.00 60.37 O ANISOU 2033 O ILE A 256 6975 5798 10164 -530 -1340 -415 O ATOM 2034 CB ILE A 256 -241.805 29.476 48.364 1.00 65.05 C ANISOU 2034 CB ILE A 256 7466 6542 10707 -683 -848 -596 C ATOM 2035 CG1 ILE A 256 -242.370 29.176 49.753 1.00 58.14 C ANISOU 2035 CG1 ILE A 256 6530 5689 9873 -677 -638 -696 C ATOM 2036 CG2 ILE A 256 -240.318 29.790 48.445 1.00 59.95 C ANISOU 2036 CG2 ILE A 256 7012 5855 9912 -687 -874 -487 C ATOM 2037 CD1 ILE A 256 -241.659 28.047 50.464 1.00 61.75 C ANISOU 2037 CD1 ILE A 256 7107 6160 10195 -767 -458 -639 C ATOM 2038 N MET A 257 -241.830 30.632 45.387 1.00 63.30 N ANISOU 2038 N MET A 257 7243 6337 10471 -690 -1348 -432 N ATOM 2039 CA MET A 257 -241.093 31.173 44.250 1.00 68.22 C ANISOU 2039 CA MET A 257 7985 6960 10974 -735 -1531 -297 C ATOM 2040 C MET A 257 -241.694 32.492 43.783 1.00 67.32 C ANISOU 2040 C MET A 257 7820 6781 10978 -628 -1766 -224 C ATOM 2041 O MET A 257 -240.967 33.463 43.538 1.00 75.36 O ANISOU 2041 O MET A 257 8969 7711 11952 -608 -1877 -105 O ATOM 2042 CB MET A 257 -241.069 30.158 43.111 1.00 73.70 C ANISOU 2042 CB MET A 257 8678 7779 11547 -885 -1551 -301 C ATOM 2043 CG MET A 257 -240.329 28.893 43.460 1.00 77.71 C ANISOU 2043 CG MET A 257 9252 8305 11969 -979 -1331 -359 C ATOM 2044 SD MET A 257 -240.539 27.621 42.211 1.00 88.18 S ANISOU 2044 SD MET A 257 10540 9758 13208 -1157 -1320 -436 S ATOM 2045 CE MET A 257 -239.488 26.344 42.894 1.00 95.67 C ANISOU 2045 CE MET A 257 11584 10641 14126 -1207 -1053 -484 C ATOM 2046 N VAL A 258 -243.022 32.546 43.660 1.00 62.19 N ANISOU 2046 N VAL A 258 6971 6163 10497 -558 -1848 -290 N ATOM 2047 CA VAL A 258 -243.687 33.768 43.214 1.00 66.78 C ANISOU 2047 CA VAL A 258 7475 6664 11236 -427 -2095 -211 C ATOM 2048 C VAL A 258 -243.453 34.899 44.208 1.00 78.98 C ANISOU 2048 C VAL A 258 9061 8020 12927 -280 -2059 -229 C ATOM 2049 O VAL A 258 -243.228 36.051 43.818 1.00 84.63 O ANISOU 2049 O VAL A 258 9853 8600 13704 -208 -2243 -100 O ATOM 2050 CB VAL A 258 -245.188 33.504 42.995 1.00 73.09 C ANISOU 2050 CB VAL A 258 8005 7550 12216 -370 -2177 -307 C ATOM 2051 CG1 VAL A 258 -245.936 34.811 42.798 1.00 84.64 C ANISOU 2051 CG1 VAL A 258 9352 8892 13915 -180 -2418 -242 C ATOM 2052 CG2 VAL A 258 -245.391 32.587 41.802 1.00 66.41 C ANISOU 2052 CG2 VAL A 258 7132 6891 11211 -532 -2271 -279 C ATOM 2053 N ILE A 259 -243.502 34.591 45.505 1.00 81.25 N ANISOU 2053 N ILE A 259 9308 8295 13268 -249 -1818 -391 N ATOM 2054 CA ILE A 259 -243.206 35.602 46.514 1.00 78.73 C ANISOU 2054 CA ILE A 259 9038 7821 13056 -140 -1755 -449 C ATOM 2055 C ILE A 259 -241.746 36.028 46.428 1.00 83.24 C ANISOU 2055 C ILE A 259 9854 8322 13451 -213 -1770 -325 C ATOM 2056 O ILE A 259 -241.425 37.218 46.541 1.00 65.34 O ANISOU 2056 O ILE A 259 7662 5889 11275 -141 -1860 -285 O ATOM 2057 CB ILE A 259 -243.566 35.078 47.916 1.00 74.24 C ANISOU 2057 CB ILE A 259 8380 7304 12524 -131 -1482 -652 C ATOM 2058 CG1 ILE A 259 -245.072 34.830 48.023 1.00 69.63 C ANISOU 2058 CG1 ILE A 259 7523 6781 12150 -59 -1460 -796 C ATOM 2059 CG2 ILE A 259 -243.112 36.052 48.989 1.00 70.89 C ANISOU 2059 CG2 ILE A 259 8029 6752 12153 -56 -1396 -738 C ATOM 2060 CD1 ILE A 259 -245.918 35.978 47.526 1.00 72.38 C ANISOU 2060 CD1 ILE A 259 7720 7008 12772 117 -1684 -792 C ATOM 2061 N ALA A 260 -240.839 35.071 46.215 1.00100.65 N ANISOU 2061 N ALA A 260 12176 10642 15423 -360 -1678 -273 N ATOM 2062 CA ALA A 260 -239.423 35.408 46.103 1.00 95.65 C ANISOU 2062 CA ALA A 260 11745 9971 14628 -441 -1684 -170 C ATOM 2063 C ALA A 260 -239.159 36.274 44.880 1.00 90.02 C ANISOU 2063 C ALA A 260 11121 9186 13896 -467 -1917 7 C ATOM 2064 O ALA A 260 -238.299 37.162 44.912 1.00 94.24 O ANISOU 2064 O ALA A 260 11794 9609 14404 -487 -1961 81 O ATOM 2065 CB ALA A 260 -238.580 34.136 46.047 1.00 82.96 C ANISOU 2065 CB ALA A 260 10206 8502 12814 -575 -1543 -162 C ATOM 2066 N PHE A 261 -239.884 36.025 43.789 1.00 74.90 N ANISOU 2066 N PHE A 261 9134 7344 11982 -486 -2070 81 N ATOM 2067 CA PHE A 261 -239.721 36.846 42.596 1.00 65.34 C ANISOU 2067 CA PHE A 261 8016 6082 10728 -523 -2311 281 C ATOM 2068 C PHE A 261 -240.239 38.259 42.826 1.00 85.37 C ANISOU 2068 C PHE A 261 10531 8391 13513 -360 -2467 333 C ATOM 2069 O PHE A 261 -239.642 39.230 42.347 1.00 97.94 O ANISOU 2069 O PHE A 261 12274 9850 15088 -389 -2600 498 O ATOM 2070 CB PHE A 261 -240.433 36.193 41.412 1.00 63.66 C ANISOU 2070 CB PHE A 261 7721 6036 10432 -593 -2450 340 C ATOM 2071 CG PHE A 261 -240.247 36.924 40.117 1.00 65.47 C ANISOU 2071 CG PHE A 261 8064 6259 10554 -667 -2705 571 C ATOM 2072 CD1 PHE A 261 -239.100 36.744 39.362 1.00 71.52 C ANISOU 2072 CD1 PHE A 261 9012 7115 11048 -863 -2685 673 C ATOM 2073 CD2 PHE A 261 -241.223 37.786 39.648 1.00 75.82 C ANISOU 2073 CD2 PHE A 261 9292 7478 12036 -543 -2967 693 C ATOM 2074 CE1 PHE A 261 -238.928 37.415 38.167 1.00 83.09 C ANISOU 2074 CE1 PHE A 261 10599 8595 12378 -962 -2908 900 C ATOM 2075 CE2 PHE A 261 -241.058 38.459 38.455 1.00 87.18 C ANISOU 2075 CE2 PHE A 261 10855 8913 13355 -621 -3220 947 C ATOM 2076 CZ PHE A 261 -239.909 38.273 37.712 1.00 87.87 C ANISOU 2076 CZ PHE A 261 11147 9106 13135 -845 -3185 1054 C ATOM 2077 N LEU A 262 -241.346 38.396 43.560 1.00 90.11 N ANISOU 2077 N LEU A 262 10941 8934 14364 -191 -2439 187 N ATOM 2078 CA LEU A 262 -241.897 39.722 43.823 1.00 91.39 C ANISOU 2078 CA LEU A 262 11055 8854 14816 -10 -2572 200 C ATOM 2079 C LEU A 262 -241.018 40.520 44.777 1.00 93.67 C ANISOU 2079 C LEU A 262 11479 8964 15147 2 -2445 131 C ATOM 2080 O LEU A 262 -240.940 41.749 44.663 1.00 99.58 O ANISOU 2080 O LEU A 262 12297 9472 16066 81 -2581 215 O ATOM 2081 CB LEU A 262 -243.315 39.600 44.379 1.00 87.74 C ANISOU 2081 CB LEU A 262 10317 8397 14622 163 -2546 18 C ATOM 2082 CG LEU A 262 -244.380 39.103 43.402 1.00 74.36 C ANISOU 2082 CG LEU A 262 8444 6846 12962 182 -2732 84 C ATOM 2083 CD1 LEU A 262 -245.666 38.784 44.143 1.00 72.12 C ANISOU 2083 CD1 LEU A 262 7867 6610 12925 317 -2631 -149 C ATOM 2084 CD2 LEU A 262 -244.628 40.129 42.306 1.00 73.79 C ANISOU 2084 CD2 LEU A 262 8406 6639 12991 258 -3077 335 C ATOM 2085 N ILE A 263 -240.359 39.847 45.725 1.00 93.31 N ANISOU 2085 N ILE A 263 11473 9026 14955 -79 -2196 -19 N ATOM 2086 CA ILE A 263 -239.450 40.537 46.637 1.00 87.11 C ANISOU 2086 CA ILE A 263 10814 8116 14168 -97 -2082 -97 C ATOM 2087 C ILE A 263 -238.317 41.195 45.867 1.00 87.13 C ANISOU 2087 C ILE A 263 11028 8027 14050 -219 -2203 103 C ATOM 2088 O ILE A 263 -237.809 42.250 46.266 1.00 91.02 O ANISOU 2088 O ILE A 263 11620 8322 14641 -210 -2212 88 O ATOM 2089 CB ILE A 263 -238.928 39.556 47.705 1.00 82.63 C ANISOU 2089 CB ILE A 263 10248 7727 13421 -177 -1825 -255 C ATOM 2090 CG1 ILE A 263 -240.060 39.176 48.661 1.00 86.29 C ANISOU 2090 CG1 ILE A 263 10518 8243 14025 -68 -1681 -468 C ATOM 2091 CG2 ILE A 263 -237.758 40.151 48.478 1.00 62.21 C ANISOU 2091 CG2 ILE A 263 7808 5071 10756 -244 -1737 -305 C ATOM 2092 CD1 ILE A 263 -239.638 38.233 49.757 1.00 84.79 C ANISOU 2092 CD1 ILE A 263 10341 8222 13652 -150 -1440 -591 C ATOM 2093 N CYS A 264 -237.909 40.597 44.749 1.00 85.85 N ANISOU 2093 N CYS A 264 10937 8008 13676 -354 -2285 277 N ATOM 2094 CA CYS A 264 -236.927 41.225 43.875 1.00 90.90 C ANISOU 2094 CA CYS A 264 11768 8581 14189 -493 -2401 481 C ATOM 2095 C CYS A 264 -237.575 42.167 42.867 1.00100.28 C ANISOU 2095 C CYS A 264 12983 9601 15515 -434 -2672 693 C ATOM 2096 O CYS A 264 -236.906 43.078 42.369 1.00102.96 O ANISOU 2096 O CYS A 264 13493 9791 15836 -519 -2777 863 O ATOM 2097 CB CYS A 264 -236.117 40.143 43.155 1.00 88.11 C ANISOU 2097 CB CYS A 264 11477 8475 13526 -684 -2337 545 C ATOM 2098 SG CYS A 264 -234.769 40.749 42.123 1.00 94.44 S ANISOU 2098 SG CYS A 264 12501 9260 14120 -907 -2415 759 S ATOM 2099 N TRP A 265 -238.865 41.984 42.582 1.00103.56 N ANISOU 2099 N TRP A 265 13231 10037 16079 -293 -2794 693 N ATOM 2100 CA TRP A 265 -239.564 42.736 41.544 1.00102.54 C ANISOU 2100 CA TRP A 265 13104 9787 16070 -225 -3091 924 C ATOM 2101 C TRP A 265 -240.179 44.027 42.077 1.00102.24 C ANISOU 2101 C TRP A 265 13016 9413 16419 -8 -3193 905 C ATOM 2102 O TRP A 265 -240.006 45.095 41.479 1.00 99.99 O ANISOU 2102 O TRP A 265 12866 8899 16228 -2 -3391 1129 O ATOM 2103 CB TRP A 265 -240.651 41.854 40.919 1.00101.84 C ANISOU 2103 CB TRP A 265 12830 9913 15950 -186 -3194 926 C ATOM 2104 CG TRP A 265 -241.337 42.445 39.723 1.00111.06 C ANISOU 2104 CG TRP A 265 13992 11031 17173 -142 -3532 1191 C ATOM 2105 CD1 TRP A 265 -240.980 42.293 38.414 1.00110.11 C ANISOU 2105 CD1 TRP A 265 14009 11059 16768 -328 -3700 1436 C ATOM 2106 CD2 TRP A 265 -242.510 43.269 39.726 1.00116.21 C ANISOU 2106 CD2 TRP A 265 14486 11487 18182 101 -3752 1241 C ATOM 2107 NE1 TRP A 265 -241.854 42.975 37.602 1.00109.33 N ANISOU 2107 NE1 TRP A 265 13862 10875 16802 -222 -4032 1663 N ATOM 2108 CE2 TRP A 265 -242.803 43.582 38.383 1.00114.38 C ANISOU 2108 CE2 TRP A 265 14311 11291 17856 56 -4077 1553 C ATOM 2109 CE3 TRP A 265 -243.338 43.774 40.733 1.00109.70 C ANISOU 2109 CE3 TRP A 265 13467 10464 17749 352 -3703 1044 C ATOM 2110 CZ2 TRP A 265 -243.887 44.380 38.022 1.00109.02 C ANISOU 2110 CZ2 TRP A 265 13496 10443 17482 274 -4380 1698 C ATOM 2111 CZ3 TRP A 265 -244.415 44.563 40.372 1.00103.96 C ANISOU 2111 CZ3 TRP A 265 12589 9562 17348 573 -3978 1155 C ATOM 2112 CH2 TRP A 265 -244.679 44.859 39.029 1.00105.44 C ANISOU 2112 CH2 TRP A 265 12833 9776 17454 543 -4326 1492 C ATOM 2113 N LEU A 266 -240.895 43.939 43.197 1.00104.84 N ANISOU 2113 N LEU A 266 13155 9700 16979 163 -3048 636 N ATOM 2114 CA LEU A 266 -241.625 45.094 43.714 1.00107.56 C ANISOU 2114 CA LEU A 266 13406 9730 17732 393 -3125 564 C ATOM 2115 C LEU A 266 -240.754 46.304 44.047 1.00114.49 C ANISOU 2115 C LEU A 266 14484 10299 18717 365 -3115 598 C ATOM 2116 O LEU A 266 -241.226 47.434 43.827 1.00124.02 O ANISOU 2116 O LEU A 266 15690 11189 20245 520 -3300 698 O ATOM 2117 CB LEU A 266 -242.442 44.668 44.940 1.00101.78 C ANISOU 2117 CB LEU A 266 12433 9062 17177 536 -2908 219 C ATOM 2118 CG LEU A 266 -243.706 43.856 44.651 1.00 94.03 C ANISOU 2118 CG LEU A 266 11187 8277 16262 633 -2965 168 C ATOM 2119 CD1 LEU A 266 -244.296 43.299 45.936 1.00 85.51 C ANISOU 2119 CD1 LEU A 266 9906 7304 15279 702 -2684 -178 C ATOM 2120 CD2 LEU A 266 -244.727 44.714 43.924 1.00 92.19 C ANISOU 2120 CD2 LEU A 266 10821 7850 16359 840 -3274 317 C ATOM 2121 N PRO A 267 -239.533 46.169 44.588 1.00104.13 N ANISOU 2121 N PRO A 267 13333 9044 17187 185 -2916 515 N ATOM 2122 CA PRO A 267 -238.709 47.371 44.808 1.00 95.10 C ANISOU 2122 CA PRO A 267 12379 7601 16153 132 -2923 553 C ATOM 2123 C PRO A 267 -238.520 48.222 43.565 1.00102.85 C ANISOU 2123 C PRO A 267 13532 8375 17171 82 -3197 914 C ATOM 2124 O PRO A 267 -238.570 49.456 43.654 1.00107.42 O ANISOU 2124 O PRO A 267 14186 8584 18044 167 -3293 964 O ATOM 2125 CB PRO A 267 -237.381 46.786 45.302 1.00 83.91 C ANISOU 2125 CB PRO A 267 11085 6390 14407 -96 -2702 456 C ATOM 2126 CG PRO A 267 -237.776 45.560 46.006 1.00 91.37 C ANISOU 2126 CG PRO A 267 11859 7627 15231 -61 -2518 241 C ATOM 2127 CD PRO A 267 -238.916 44.983 45.210 1.00 96.21 C ANISOU 2127 CD PRO A 267 12320 8349 15886 45 -2665 347 C ATOM 2128 N TYR A 268 -238.301 47.602 42.404 1.00 98.08 N ANISOU 2128 N TYR A 268 13001 7994 16272 -66 -3320 1165 N ATOM 2129 CA TYR A 268 -238.202 48.382 41.176 1.00 98.98 C ANISOU 2129 CA TYR A 268 13284 7942 16381 -131 -3594 1538 C ATOM 2130 C TYR A 268 -239.541 49.008 40.817 1.00 99.88 C ANISOU 2130 C TYR A 268 13263 7837 16850 134 -3865 1662 C ATOM 2131 O TYR A 268 -239.589 50.136 40.317 1.00 99.04 O ANISOU 2131 O TYR A 268 13284 7402 16945 179 -4079 1909 O ATOM 2132 CB TYR A 268 -237.693 47.506 40.033 1.00 99.55 C ANISOU 2132 CB TYR A 268 13453 8352 16021 -369 -3644 1743 C ATOM 2133 CG TYR A 268 -236.274 47.030 40.224 1.00 94.75 C ANISOU 2133 CG TYR A 268 12982 7924 15096 -631 -3408 1661 C ATOM 2134 CD1 TYR A 268 -236.007 45.816 40.843 1.00101.68 C ANISOU 2134 CD1 TYR A 268 13744 9096 15794 -669 -3171 1409 C ATOM 2135 CD2 TYR A 268 -235.201 47.795 39.788 1.00 84.41 C ANISOU 2135 CD2 TYR A 268 11907 6482 13683 -840 -3425 1843 C ATOM 2136 CE1 TYR A 268 -234.711 45.375 41.019 1.00102.44 C ANISOU 2136 CE1 TYR A 268 13937 9351 15633 -883 -2975 1338 C ATOM 2137 CE2 TYR A 268 -233.900 47.364 39.960 1.00 96.45 C ANISOU 2137 CE2 TYR A 268 13520 8185 14940 -1074 -3212 1752 C ATOM 2138 CZ TYR A 268 -233.661 46.153 40.576 1.00105.88 C ANISOU 2138 CZ TYR A 268 14578 9673 15976 -1081 -2996 1499 C ATOM 2139 OH TYR A 268 -232.368 45.719 40.750 1.00106.46 O ANISOU 2139 OH TYR A 268 14714 9921 15815 -1289 -2803 1413 O ATOM 2140 N ALA A 269 -240.640 48.292 41.071 1.00107.51 N ANISOU 2140 N ALA A 269 13963 8972 17913 310 -3862 1498 N ATOM 2141 CA ALA A 269 -241.964 48.851 40.822 1.00107.57 C ANISOU 2141 CA ALA A 269 13785 8790 18297 588 -4114 1575 C ATOM 2142 C ALA A 269 -242.274 49.984 41.791 1.00105.83 C ANISOU 2142 C ALA A 269 13506 8153 18552 812 -4063 1393 C ATOM 2143 O ALA A 269 -242.919 50.971 41.416 1.00103.88 O ANISOU 2143 O ALA A 269 13229 7579 18663 1009 -4316 1565 O ATOM 2144 CB ALA A 269 -243.023 47.754 40.919 1.00106.32 C ANISOU 2144 CB ALA A 269 13332 8941 18124 694 -4088 1402 C ATOM 2145 N GLY A 270 -241.830 49.860 43.043 1.00105.88 N ANISOU 2145 N GLY A 270 13492 8164 18575 787 -3742 1041 N ATOM 2146 CA GLY A 270 -241.986 50.958 43.981 1.00114.02 C ANISOU 2146 CA GLY A 270 14493 8807 20023 956 -3661 830 C ATOM 2147 C GLY A 270 -241.145 52.162 43.603 1.00123.96 C ANISOU 2147 C GLY A 270 16033 9692 21375 863 -3774 1056 C ATOM 2148 O GLY A 270 -241.596 53.306 43.708 1.00137.32 O ANISOU 2148 O GLY A 270 17712 10956 23506 1056 -3896 1074 O ATOM 2149 N VAL A 271 -239.909 51.921 43.159 1.00120.39 N ANISOU 2149 N VAL A 271 15831 9383 20530 561 -3726 1222 N ATOM 2150 CA VAL A 271 -239.074 53.007 42.656 1.00110.30 C ANISOU 2150 CA VAL A 271 14833 7778 19299 423 -3838 1477 C ATOM 2151 C VAL A 271 -239.625 53.531 41.335 1.00109.23 C ANISOU 2151 C VAL A 271 14768 7472 19262 493 -4213 1925 C ATOM 2152 O VAL A 271 -239.577 54.737 41.063 1.00114.85 O ANISOU 2152 O VAL A 271 15626 7746 20266 543 -4376 2125 O ATOM 2153 CB VAL A 271 -237.612 52.537 42.528 1.00102.59 C ANISOU 2153 CB VAL A 271 14068 7047 17865 69 -3670 1514 C ATOM 2154 CG1 VAL A 271 -236.820 53.457 41.612 1.00104.42 C ANISOU 2154 CG1 VAL A 271 14591 7031 18052 -128 -3829 1877 C ATOM 2155 CG2 VAL A 271 -236.964 52.481 43.899 1.00 88.31 C ANISOU 2155 CG2 VAL A 271 12232 5265 16055 11 -3353 1113 C ATOM 2156 N ALA A 272 -240.170 52.642 40.502 1.00107.30 N ANISOU 2156 N ALA A 272 14424 7563 18780 492 -4364 2093 N ATOM 2157 CA ALA A 272 -240.840 53.083 39.282 1.00119.15 C ANISOU 2157 CA ALA A 272 15958 8948 20364 578 -4751 2513 C ATOM 2158 C ALA A 272 -241.976 54.044 39.604 1.00129.33 C ANISOU 2158 C ALA A 272 17072 9816 22251 948 -4932 2489 C ATOM 2159 O ALA A 272 -242.018 55.170 39.097 1.00126.67 O ANISOU 2159 O ALA A 272 16859 9188 22084 989 -5104 2742 O ATOM 2160 CB ALA A 272 -241.373 51.881 38.501 1.00123.44 C ANISOU 2160 CB ALA A 272 16367 9962 20574 533 -4859 2604 C ATOM 2161 N PHE A 273 -242.908 53.610 40.461 1.00136.08 N ANISOU 2161 N PHE A 273 17604 10757 23343 1190 -4809 2125 N ATOM 2162 CA PHE A 273 -244.069 54.431 40.796 1.00142.49 C ANISOU 2162 CA PHE A 273 18184 11243 24715 1551 -4936 2034 C ATOM 2163 C PHE A 273 -243.663 55.747 41.447 1.00147.14 C ANISOU 2163 C PHE A 273 18887 11456 25564 1579 -4772 1896 C ATOM 2164 O PHE A 273 -244.378 56.748 41.318 1.00160.09 O ANISOU 2164 O PHE A 273 20437 12846 27544 1791 -4894 1952 O ATOM 2165 CB PHE A 273 -245.012 53.651 41.713 1.00137.96 C ANISOU 2165 CB PHE A 273 17242 10866 24311 1754 -4760 1611 C ATOM 2166 CG PHE A 273 -246.271 54.396 42.071 1.00142.86 C ANISOU 2166 CG PHE A 273 17566 11252 25463 2108 -4835 1456 C ATOM 2167 CD1 PHE A 273 -247.263 54.598 41.126 1.00142.16 C ANISOU 2167 CD1 PHE A 273 17323 11200 25492 2273 -5166 1727 C ATOM 2168 CD2 PHE A 273 -246.468 54.880 43.356 1.00144.17 C ANISOU 2168 CD2 PHE A 273 17595 11235 25947 2245 -4541 1012 C ATOM 2169 CE1 PHE A 273 -248.424 55.279 41.450 1.00141.34 C ANISOU 2169 CE1 PHE A 273 16926 10932 25843 2580 -5204 1564 C ATOM 2170 CE2 PHE A 273 -247.629 55.561 43.687 1.00144.31 C ANISOU 2170 CE2 PHE A 273 17325 11094 26411 2543 -4563 837 C ATOM 2171 CZ PHE A 273 -248.608 55.760 42.731 1.00142.29 C ANISOU 2171 CZ PHE A 273 16909 10857 26296 2718 -4896 1115 C ATOM 2172 N TYR A 274 -242.529 55.766 42.153 1.00140.68 N ANISOU 2172 N TYR A 274 18259 10595 24598 1366 -4501 1708 N ATOM 2173 CA TYR A 274 -242.006 57.015 42.690 1.00137.58 C ANISOU 2173 CA TYR A 274 18007 9863 24404 1343 -4352 1596 C ATOM 2174 C TYR A 274 -241.275 57.823 41.625 1.00136.01 C ANISOU 2174 C TYR A 274 18119 9514 24045 1149 -4525 2037 C ATOM 2175 O TYR A 274 -241.174 59.050 41.746 1.00116.70 O ANISOU 2175 O TYR A 274 15766 6729 21847 1196 -4505 2053 O ATOM 2176 CB TYR A 274 -241.068 56.738 43.866 1.00132.78 C ANISOU 2176 CB TYR A 274 17470 9297 23683 1171 -4004 1212 C ATOM 2177 CG TYR A 274 -240.983 57.873 44.863 1.00135.70 C ANISOU 2177 CG TYR A 274 17836 9351 24371 1249 -3795 896 C ATOM 2178 CD1 TYR A 274 -241.759 57.867 46.014 1.00134.40 C ANISOU 2178 CD1 TYR A 274 17407 9159 24499 1467 -3600 442 C ATOM 2179 CD2 TYR A 274 -240.133 58.952 44.653 1.00141.70 C ANISOU 2179 CD2 TYR A 274 18857 9847 25134 1090 -3779 1038 C ATOM 2180 CE1 TYR A 274 -241.689 58.900 46.931 1.00138.70 C ANISOU 2180 CE1 TYR A 274 17951 9431 25319 1523 -3400 131 C ATOM 2181 CE2 TYR A 274 -240.056 59.992 45.564 1.00147.30 C ANISOU 2181 CE2 TYR A 274 19568 10259 26139 1152 -3587 735 C ATOM 2182 CZ TYR A 274 -240.837 59.960 46.701 1.00148.07 C ANISOU 2182 CZ TYR A 274 19405 10343 26513 1368 -3400 278 C ATOM 2183 OH TYR A 274 -240.764 60.992 47.610 1.00156.82 O ANISOU 2183 OH TYR A 274 20518 11169 27898 1414 -3201 -44 O ATOM 2184 N ILE A 275 -240.749 57.162 40.590 1.00150.69 N ANISOU 2184 N ILE A 275 20145 11619 25490 917 -4677 2386 N ATOM 2185 CA ILE A 275 -240.171 57.893 39.468 1.00161.06 C ANISOU 2185 CA ILE A 275 21739 12829 26627 726 -4853 2829 C ATOM 2186 C ILE A 275 -241.235 58.199 38.417 1.00181.97 C ANISOU 2186 C ILE A 275 24303 15456 29382 912 -5209 3181 C ATOM 2187 O ILE A 275 -241.163 59.236 37.746 1.00190.01 O ANISOU 2187 O ILE A 275 25484 16240 30470 893 -5357 3483 O ATOM 2188 CB ILE A 275 -238.987 57.107 38.872 1.00150.78 C ANISOU 2188 CB ILE A 275 20673 11816 24799 343 -4811 3013 C ATOM 2189 CG1 ILE A 275 -237.810 57.075 39.856 1.00151.46 C ANISOU 2189 CG1 ILE A 275 20869 11877 24804 136 -4475 2701 C ATOM 2190 CG2 ILE A 275 -238.530 57.715 37.547 1.00139.26 C ANISOU 2190 CG2 ILE A 275 19481 10327 23104 132 -5015 3502 C ATOM 2191 CD1 ILE A 275 -236.574 56.374 39.321 1.00150.37 C ANISOU 2191 CD1 ILE A 275 20946 12011 24176 -251 -4406 2853 C ATOM 2192 N PHE A 276 -242.234 57.323 38.264 1.00190.93 N ANISOU 2192 N PHE A 276 25180 16833 30532 1090 -5351 3146 N ATOM 2193 CA PHE A 276 -243.338 57.592 37.347 1.00200.58 C ANISOU 2193 CA PHE A 276 26274 18061 31876 1286 -5695 3439 C ATOM 2194 C PHE A 276 -244.068 58.869 37.743 1.00201.47 C ANISOU 2194 C PHE A 276 26270 17767 32511 1580 -5726 3361 C ATOM 2195 O PHE A 276 -244.216 59.794 36.937 1.00209.48 O ANISOU 2195 O PHE A 276 27411 18583 33600 1606 -5947 3709 O ATOM 2196 CB PHE A 276 -244.298 56.400 37.321 1.00200.42 C ANISOU 2196 CB PHE A 276 25950 18377 31825 1432 -5796 3324 C ATOM 2197 CG PHE A 276 -245.410 56.538 36.320 1.00202.00 C ANISOU 2197 CG PHE A 276 26002 18657 32092 1599 -6165 3621 C ATOM 2198 CD1 PHE A 276 -245.233 56.130 35.010 1.00199.58 C ANISOU 2198 CD1 PHE A 276 25853 18624 31355 1388 -6425 4035 C ATOM 2199 CD2 PHE A 276 -246.629 57.084 36.687 1.00201.55 C ANISOU 2199 CD2 PHE A 276 25643 18421 32515 1956 -6246 3476 C ATOM 2200 CE1 PHE A 276 -246.246 56.261 34.086 1.00200.34 C ANISOU 2200 CE1 PHE A 276 25815 18820 31486 1526 -6772 4306 C ATOM 2201 CE2 PHE A 276 -247.647 57.220 35.768 1.00200.34 C ANISOU 2201 CE2 PHE A 276 25343 18350 32425 2108 -6593 3748 C ATOM 2202 CZ PHE A 276 -247.456 56.807 34.465 1.00200.58 C ANISOU 2202 CZ PHE A 276 25539 18661 32011 1892 -6863 4168 C ATOM 2203 N THR A 277 -244.547 58.927 38.982 1.00190.71 N ANISOU 2203 N THR A 277 24667 16282 31514 1802 -5501 2901 N ATOM 2204 CA THR A 277 -244.998 60.179 39.573 1.00180.16 C ANISOU 2204 CA THR A 277 23254 14532 30667 2037 -5440 2742 C ATOM 2205 C THR A 277 -243.782 60.875 40.184 1.00179.17 C ANISOU 2205 C THR A 277 23400 14161 30514 1832 -5170 2613 C ATOM 2206 O THR A 277 -242.639 60.462 39.969 1.00170.69 O ANISOU 2206 O THR A 277 22575 13237 29041 1513 -5080 2715 O ATOM 2207 CB THR A 277 -246.101 59.929 40.601 1.00163.17 C ANISOU 2207 CB THR A 277 20705 12391 28899 2347 -5308 2288 C ATOM 2208 OG1 THR A 277 -245.571 59.201 41.717 1.00147.46 O ANISOU 2208 OG1 THR A 277 18680 10551 26799 2240 -4965 1864 O ATOM 2209 CG2 THR A 277 -247.241 59.135 39.977 1.00160.56 C ANISOU 2209 CG2 THR A 277 20095 12349 28562 2512 -5565 2405 C ATOM 2210 N HIS A 278 -244.016 61.951 40.941 1.00189.43 N ANISOU 2210 N HIS A 278 24650 15087 32240 2005 -5036 2378 N ATOM 2211 CA HIS A 278 -242.971 62.643 41.692 1.00195.07 C ANISOU 2211 CA HIS A 278 25578 15561 32980 1833 -4755 2171 C ATOM 2212 C HIS A 278 -241.710 62.901 40.876 1.00209.29 C ANISOU 2212 C HIS A 278 27762 17342 34416 1484 -4800 2542 C ATOM 2213 O HIS A 278 -240.598 62.680 41.366 1.00208.72 O ANISOU 2213 O HIS A 278 27853 17343 34109 1219 -4561 2380 O ATOM 2214 CB HIS A 278 -242.617 61.842 42.955 1.00182.86 C ANISOU 2214 CB HIS A 278 23919 14219 31341 1764 -4418 1668 C ATOM 2215 CG HIS A 278 -243.644 61.938 44.040 1.00180.79 C ANISOU 2215 CG HIS A 278 23324 13885 31483 2063 -4264 1207 C ATOM 2216 ND1 HIS A 278 -244.970 61.618 43.843 1.00183.73 N ANISOU 2216 ND1 HIS A 278 23380 14350 32079 2352 -4429 1201 N ATOM 2217 CD2 HIS A 278 -243.539 62.331 45.332 1.00180.12 C ANISOU 2217 CD2 HIS A 278 23167 13663 31607 2101 -3951 725 C ATOM 2218 CE1 HIS A 278 -245.637 61.807 44.967 1.00185.20 C ANISOU 2218 CE1 HIS A 278 23308 14457 32601 2555 -4211 731 C ATOM 2219 NE2 HIS A 278 -244.792 62.240 45.886 1.00183.17 N ANISOU 2219 NE2 HIS A 278 23201 14065 32333 2406 -3919 435 N ATOM 2220 N GLN A 279 -241.865 63.370 39.637 1.00208.35 N ANISOU 2220 N GLN A 279 27782 17140 34240 1468 -5098 3034 N ATOM 2221 CA GLN A 279 -240.725 63.478 38.729 1.00200.78 C ANISOU 2221 CA GLN A 279 27173 16235 32878 1110 -5150 3414 C ATOM 2222 C GLN A 279 -240.050 64.837 38.877 1.00184.47 C ANISOU 2222 C GLN A 279 25349 13731 31009 1019 -5039 3458 C ATOM 2223 O GLN A 279 -239.574 65.413 37.895 1.00182.16 O ANISOU 2223 O GLN A 279 25316 13329 30566 843 -5183 3878 O ATOM 2224 CB GLN A 279 -241.150 63.279 37.270 1.00216.33 C ANISOU 2224 CB GLN A 279 29202 18372 34622 1087 -5517 3937 C ATOM 2225 CG GLN A 279 -242.160 62.158 37.007 1.00224.20 C ANISOU 2225 CG GLN A 279 29918 19730 35536 1255 -5698 3927 C ATOM 2226 CD GLN A 279 -243.505 62.702 36.594 1.00238.58 C ANISOU 2226 CD GLN A 279 31535 21394 37720 1599 -5986 4083 C ATOM 2227 OE1 GLN A 279 -244.121 63.469 37.330 1.00243.38 O ANISOU 2227 OE1 GLN A 279 31982 21677 38813 1875 -5916 3844 O ATOM 2228 NE2 GLN A 279 -243.958 62.332 35.402 1.00244.51 N ANISOU 2228 NE2 GLN A 279 32291 22378 38233 1574 -6310 4479 N ATOM 2229 N GLY A 280 -239.995 65.354 40.098 1.00172.95 N ANISOU 2229 N GLY A 280 23814 12026 29873 1119 -4776 3018 N ATOM 2230 CA GLY A 280 -239.573 66.719 40.316 1.00167.63 C ANISOU 2230 CA GLY A 280 23330 10887 29474 1089 -4679 3016 C ATOM 2231 C GLY A 280 -238.524 66.927 41.389 1.00162.51 C ANISOU 2231 C GLY A 280 22791 10158 28798 876 -4319 2618 C ATOM 2232 O GLY A 280 -238.193 68.073 41.721 1.00147.40 O ANISOU 2232 O GLY A 280 21020 7842 27145 852 -4205 2543 O ATOM 2233 N SER A 281 -237.988 65.843 41.943 1.00151.70 N ANISOU 2233 N SER A 281 21358 9163 27117 712 -4141 2360 N ATOM 2234 CA SER A 281 -236.988 65.950 42.993 1.00152.21 C ANISOU 2234 CA SER A 281 21506 9205 27122 498 -3812 1968 C ATOM 2235 C SER A 281 -235.764 65.104 42.672 1.00140.70 C ANISOU 2235 C SER A 281 20209 8101 25150 117 -3735 2073 C ATOM 2236 O SER A 281 -235.797 64.195 41.837 1.00135.91 O ANISOU 2236 O SER A 281 19596 7817 24224 48 -3899 2354 O ATOM 2237 CB SER A 281 -237.555 65.548 44.363 1.00158.69 C ANISOU 2237 CB SER A 281 22049 10109 28139 697 -3604 1410 C ATOM 2238 OG SER A 281 -238.344 66.590 44.913 1.00166.69 O ANISOU 2238 OG SER A 281 22956 10732 29645 969 -3569 1203 O ATOM 2239 N CYS A 282 -234.670 65.424 43.359 1.00140.77 N ANISOU 2239 N CYS A 282 20352 8049 25084 -140 -3478 1827 N ATOM 2240 CA CYS A 282 -233.427 64.686 43.192 1.00137.70 C ANISOU 2240 CA CYS A 282 20091 7986 24242 -511 -3371 1866 C ATOM 2241 C CYS A 282 -233.466 63.411 44.023 1.00138.05 C ANISOU 2241 C CYS A 282 19927 8418 24108 -487 -3249 1520 C ATOM 2242 O CYS A 282 -233.729 63.456 45.228 1.00134.26 O ANISOU 2242 O CYS A 282 19299 7891 23823 -361 -3070 1074 O ATOM 2243 CB CYS A 282 -232.229 65.541 43.616 1.00143.50 C ANISOU 2243 CB CYS A 282 21031 8516 24977 -807 -3150 1725 C ATOM 2244 SG CYS A 282 -232.151 67.201 42.899 1.00163.69 S ANISOU 2244 SG CYS A 282 23846 10529 27819 -839 -3231 2048 S ATOM 2245 N PHE A 283 -233.211 62.275 43.380 1.00143.43 N ANISOU 2245 N PHE A 283 20603 9480 24413 -615 -3339 1721 N ATOM 2246 CA PHE A 283 -233.041 61.027 44.108 1.00155.84 C ANISOU 2246 CA PHE A 283 22019 11419 25774 -649 -3212 1426 C ATOM 2247 C PHE A 283 -231.604 60.965 44.604 1.00163.55 C ANISOU 2247 C PHE A 283 23118 12515 26510 -1003 -2990 1245 C ATOM 2248 O PHE A 283 -230.663 61.002 43.803 1.00172.94 O ANISOU 2248 O PHE A 283 24489 13785 27434 -1295 -3011 1516 O ATOM 2249 CB PHE A 283 -233.374 59.830 43.221 1.00166.19 C ANISOU 2249 CB PHE A 283 23275 13072 26799 -641 -3395 1702 C ATOM 2250 CG PHE A 283 -234.652 59.985 42.454 1.00178.72 C ANISOU 2250 CG PHE A 283 24772 14557 28575 -354 -3662 1971 C ATOM 2251 CD1 PHE A 283 -235.873 59.925 43.102 1.00184.83 C ANISOU 2251 CD1 PHE A 283 25294 15254 29678 -3 -3680 1732 C ATOM 2252 CD2 PHE A 283 -234.633 60.200 41.087 1.00183.79 C ANISOU 2252 CD2 PHE A 283 25573 15201 29058 -448 -3893 2455 C ATOM 2253 CE1 PHE A 283 -237.051 60.077 42.401 1.00190.86 C ANISOU 2253 CE1 PHE A 283 25946 15941 30631 260 -3936 1969 C ATOM 2254 CE2 PHE A 283 -235.809 60.353 40.381 1.00189.27 C ANISOU 2254 CE2 PHE A 283 26175 15823 29918 -190 -4163 2705 C ATOM 2255 CZ PHE A 283 -237.018 60.292 41.040 1.00192.81 C ANISOU 2255 CZ PHE A 283 26352 16192 30716 169 -4190 2462 C ATOM 2256 N GLY A 284 -231.435 60.901 45.923 1.00168.85 N ANISOU 2256 N GLY A 284 23679 13208 27269 -988 -2778 781 N ATOM 2257 CA GLY A 284 -230.130 60.937 46.534 1.00173.16 C ANISOU 2257 CA GLY A 284 24308 13856 27627 -1306 -2578 560 C ATOM 2258 C GLY A 284 -229.209 59.850 46.023 1.00171.49 C ANISOU 2258 C GLY A 284 24132 14041 26985 -1575 -2587 715 C ATOM 2259 O GLY A 284 -229.622 58.946 45.288 1.00161.53 O ANISOU 2259 O GLY A 284 22826 12996 25552 -1510 -2732 954 O ATOM 2260 N PRO A 285 -227.925 59.912 46.418 1.00181.21 N ANISOU 2260 N PRO A 285 25433 15386 28034 -1892 -2429 563 N ATOM 2261 CA PRO A 285 -226.951 58.921 45.933 1.00170.31 C ANISOU 2261 CA PRO A 285 24070 14388 26251 -2165 -2423 694 C ATOM 2262 C PRO A 285 -227.267 57.492 46.356 1.00160.08 C ANISOU 2262 C PRO A 285 22588 13466 24769 -2053 -2422 549 C ATOM 2263 O PRO A 285 -226.351 56.667 46.427 1.00157.44 O ANISOU 2263 O PRO A 285 22195 13554 24073 -2240 -2309 490 O ATOM 2264 CB PRO A 285 -225.628 59.402 46.555 1.00175.88 C ANISOU 2264 CB PRO A 285 24829 15115 26881 -2482 -2238 461 C ATOM 2265 CG PRO A 285 -226.037 60.308 47.711 1.00184.88 C ANISOU 2265 CG PRO A 285 25932 15963 28353 -2339 -2129 92 C ATOM 2266 CD PRO A 285 -227.287 60.970 47.219 1.00190.94 C ANISOU 2266 CD PRO A 285 26734 16388 29427 -2033 -2258 285 C ATOM 2267 N ILE A 286 -228.542 57.179 46.611 1.00158.16 N ANISOU 2267 N ILE A 286 22206 13195 24693 -1717 -2484 483 N ATOM 2268 CA ILE A 286 -228.940 55.915 47.226 1.00152.47 C ANISOU 2268 CA ILE A 286 21264 12912 23755 -1563 -2388 277 C ATOM 2269 C ILE A 286 -230.312 55.450 46.737 1.00153.78 C ANISOU 2269 C ILE A 286 21323 13083 24025 -1262 -2533 426 C ATOM 2270 O ILE A 286 -230.450 54.326 46.238 1.00149.14 O ANISOU 2270 O ILE A 286 20654 12863 23150 -1245 -2557 553 O ATOM 2271 CB ILE A 286 -228.926 56.037 48.763 1.00145.92 C ANISOU 2271 CB ILE A 286 20315 12104 23024 -1506 -2201 -195 C ATOM 2272 CG1 ILE A 286 -227.501 55.896 49.311 1.00145.59 C ANISOU 2272 CG1 ILE A 286 20298 12309 22712 -1809 -2050 -365 C ATOM 2273 CG2 ILE A 286 -229.874 55.029 49.412 1.00131.01 C ANISOU 2273 CG2 ILE A 286 18207 10499 21070 -1254 -2138 -383 C ATOM 2274 CD1 ILE A 286 -227.408 55.933 50.829 1.00142.65 C ANISOU 2274 CD1 ILE A 286 19811 12032 22357 -1790 -1878 -822 C ATOM 2275 N PHE A 287 -231.327 56.315 46.871 1.00161.28 N ANISOU 2275 N PHE A 287 22258 13617 25404 -1025 -2632 400 N ATOM 2276 CA PHE A 287 -232.733 55.922 46.769 1.00163.47 C ANISOU 2276 CA PHE A 287 22361 13902 25849 -701 -2736 417 C ATOM 2277 C PHE A 287 -233.032 55.001 45.587 1.00166.41 C ANISOU 2277 C PHE A 287 22716 14561 25949 -696 -2894 765 C ATOM 2278 O PHE A 287 -233.504 53.874 45.770 1.00171.08 O ANISOU 2278 O PHE A 287 23132 15513 26356 -596 -2839 668 O ATOM 2279 CB PHE A 287 -233.623 57.167 46.693 1.00164.65 C ANISOU 2279 CB PHE A 287 22528 13526 26507 -474 -2869 455 C ATOM 2280 CG PHE A 287 -235.040 56.870 46.278 1.00163.86 C ANISOU 2280 CG PHE A 287 22252 13406 26600 -154 -3041 568 C ATOM 2281 CD1 PHE A 287 -235.952 56.350 47.185 1.00164.39 C ANISOU 2281 CD1 PHE A 287 22067 13593 26802 78 -2930 229 C ATOM 2282 CD2 PHE A 287 -235.457 57.111 44.980 1.00168.09 C ANISOU 2282 CD2 PHE A 287 22860 13867 27139 -102 -3299 1006 C ATOM 2283 CE1 PHE A 287 -237.249 56.076 46.799 1.00169.70 C ANISOU 2283 CE1 PHE A 287 22551 14264 27663 360 -3085 317 C ATOM 2284 CE2 PHE A 287 -236.749 56.839 44.591 1.00174.69 C ANISOU 2284 CE2 PHE A 287 23514 14710 28152 184 -3479 1106 C ATOM 2285 CZ PHE A 287 -237.647 56.321 45.501 1.00176.70 C ANISOU 2285 CZ PHE A 287 23505 15036 28596 419 -3379 757 C ATOM 2286 N MET A 288 -232.766 55.467 44.366 1.00161.38 N ANISOU 2286 N MET A 288 22269 13771 25275 -821 -3087 1169 N ATOM 2287 CA MET A 288 -233.094 54.699 43.170 1.00154.10 C ANISOU 2287 CA MET A 288 21347 13110 24095 -833 -3255 1500 C ATOM 2288 C MET A 288 -232.296 53.407 43.043 1.00144.68 C ANISOU 2288 C MET A 288 20116 12439 22416 -1037 -3104 1452 C ATOM 2289 O MET A 288 -232.671 52.546 42.239 1.00138.23 O ANISOU 2289 O MET A 288 19247 11900 21373 -1026 -3196 1625 O ATOM 2290 CB MET A 288 -232.872 55.565 41.932 1.00158.42 C ANISOU 2290 CB MET A 288 22136 13382 24673 -968 -3483 1948 C ATOM 2291 CG MET A 288 -231.546 56.291 41.955 1.00155.13 C ANISOU 2291 CG MET A 288 21941 12813 24189 -1286 -3374 1979 C ATOM 2292 SD MET A 288 -231.566 57.816 41.003 1.00161.54 S ANISOU 2292 SD MET A 288 22965 13266 25147 -1321 -3522 2350 S ATOM 2293 CE MET A 288 -229.986 58.515 41.477 1.00163.11 C ANISOU 2293 CE MET A 288 23329 13389 25257 -1675 -3267 2196 C ATOM 2294 N THR A 289 -231.216 53.250 43.810 1.00137.44 N ANISOU 2294 N THR A 289 19214 11661 21348 -1220 -2882 1215 N ATOM 2295 CA THR A 289 -230.367 52.067 43.760 1.00113.73 C ANISOU 2295 CA THR A 289 16161 9121 17930 -1400 -2735 1156 C ATOM 2296 C THR A 289 -230.597 51.136 44.945 1.00106.33 C ANISOU 2296 C THR A 289 15015 8446 16940 -1264 -2557 806 C ATOM 2297 O THR A 289 -229.758 50.270 45.219 1.00107.41 O ANISOU 2297 O THR A 289 15105 8915 16792 -1401 -2410 699 O ATOM 2298 CB THR A 289 -228.894 52.473 43.692 1.00101.96 C ANISOU 2298 CB THR A 289 14818 7642 16279 -1723 -2630 1171 C ATOM 2299 OG1 THR A 289 -228.540 53.170 44.891 1.00104.21 O ANISOU 2299 OG1 THR A 289 15092 7736 16765 -1726 -2505 876 O ATOM 2300 CG2 THR A 289 -228.648 53.383 42.496 1.00106.72 C ANISOU 2300 CG2 THR A 289 15650 7992 16908 -1896 -2791 1543 C ATOM 2301 N ILE A 290 -231.703 51.309 45.662 1.00 99.10 N ANISOU 2301 N ILE A 290 13970 7384 16299 -1000 -2564 628 N ATOM 2302 CA ILE A 290 -232.078 50.413 46.754 1.00 85.52 C ANISOU 2302 CA ILE A 290 12058 5916 14521 -873 -2398 323 C ATOM 2303 C ILE A 290 -232.564 49.080 46.189 1.00 86.11 C ANISOU 2303 C ILE A 290 12019 6329 14371 -819 -2423 426 C ATOM 2304 O ILE A 290 -232.185 48.028 46.725 1.00 87.28 O ANISOU 2304 O ILE A 290 12081 6796 14287 -865 -2270 283 O ATOM 2305 CB ILE A 290 -233.134 51.057 47.670 1.00 80.04 C ANISOU 2305 CB ILE A 290 11252 4965 14194 -629 -2374 80 C ATOM 2306 CG1 ILE A 290 -232.539 52.248 48.423 1.00 82.37 C ANISOU 2306 CG1 ILE A 290 11649 4962 14686 -711 -2297 -109 C ATOM 2307 CG2 ILE A 290 -233.686 50.039 48.658 1.00 78.42 C ANISOU 2307 CG2 ILE A 290 10848 5052 13897 -509 -2210 -192 C ATOM 2308 CD1 ILE A 290 -233.530 52.945 49.337 1.00 84.92 C ANISOU 2308 CD1 ILE A 290 11860 5015 15390 -481 -2247 -393 C ATOM 2309 N PRO A 291 -233.398 49.048 45.135 1.00 88.78 N ANISOU 2309 N PRO A 291 12348 6613 14769 -725 -2615 670 N ATOM 2310 CA PRO A 291 -233.719 47.743 44.530 1.00 88.52 C ANISOU 2310 CA PRO A 291 12221 6924 14490 -726 -2628 752 C ATOM 2311 C PRO A 291 -232.490 46.971 44.087 1.00 88.52 C ANISOU 2311 C PRO A 291 12301 7211 14122 -976 -2533 819 C ATOM 2312 O PRO A 291 -232.446 45.745 44.239 1.00 85.20 O ANISOU 2312 O PRO A 291 11775 7092 13506 -982 -2423 726 O ATOM 2313 CB PRO A 291 -234.614 48.120 43.343 1.00 86.26 C ANISOU 2313 CB PRO A 291 11956 6502 14317 -638 -2889 1038 C ATOM 2314 CG PRO A 291 -235.258 49.370 43.759 1.00 88.33 C ANISOU 2314 CG PRO A 291 12216 6361 14986 -457 -2983 1004 C ATOM 2315 CD PRO A 291 -234.223 50.120 44.544 1.00 89.58 C ANISOU 2315 CD PRO A 291 12497 6350 15190 -585 -2836 855 C ATOM 2316 N ALA A 292 -231.483 47.662 43.547 1.00 94.81 N ANISOU 2316 N ALA A 292 13275 7911 14839 -1185 -2564 972 N ATOM 2317 CA ALA A 292 -230.242 46.993 43.173 1.00 86.91 C ANISOU 2317 CA ALA A 292 12325 7183 13515 -1427 -2451 1000 C ATOM 2318 C ALA A 292 -229.521 46.446 44.398 1.00 86.49 C ANISOU 2318 C ALA A 292 12176 7297 13389 -1444 -2242 719 C ATOM 2319 O ALA A 292 -228.947 45.352 44.351 1.00 66.18 O ANISOU 2319 O ALA A 292 9536 5023 10586 -1520 -2134 671 O ATOM 2320 CB ALA A 292 -229.339 47.956 42.403 1.00 75.18 C ANISOU 2320 CB ALA A 292 11041 5545 11981 -1665 -2512 1208 C ATOM 2321 N PHE A 293 -229.554 47.187 45.507 1.00 83.97 N ANISOU 2321 N PHE A 293 11846 6789 13270 -1373 -2189 528 N ATOM 2322 CA PHE A 293 -228.853 46.756 46.712 1.00 90.02 C ANISOU 2322 CA PHE A 293 12532 7727 13944 -1405 -2015 274 C ATOM 2323 C PHE A 293 -229.422 45.454 47.262 1.00 79.84 C ANISOU 2323 C PHE A 293 11083 6696 12558 -1261 -1927 152 C ATOM 2324 O PHE A 293 -228.686 44.661 47.861 1.00 85.94 O ANISOU 2324 O PHE A 293 11792 7708 13152 -1320 -1807 43 O ATOM 2325 CB PHE A 293 -228.917 47.857 47.771 1.00 99.96 C ANISOU 2325 CB PHE A 293 13817 8733 15432 -1364 -1980 72 C ATOM 2326 CG PHE A 293 -227.989 47.644 48.934 1.00106.80 C ANISOU 2326 CG PHE A 293 14634 9775 16171 -1459 -1831 -166 C ATOM 2327 CD1 PHE A 293 -226.640 47.940 48.823 1.00103.34 C ANISOU 2327 CD1 PHE A 293 14263 9393 15607 -1695 -1800 -152 C ATOM 2328 CD2 PHE A 293 -228.468 47.165 50.144 1.00110.09 C ANISOU 2328 CD2 PHE A 293 14932 10314 16584 -1327 -1728 -402 C ATOM 2329 CE1 PHE A 293 -225.781 47.753 49.893 1.00103.88 C ANISOU 2329 CE1 PHE A 293 14268 9644 15557 -1781 -1692 -366 C ATOM 2330 CE2 PHE A 293 -227.614 46.978 51.220 1.00111.22 C ANISOU 2330 CE2 PHE A 293 15036 10641 16582 -1423 -1618 -600 C ATOM 2331 CZ PHE A 293 -226.269 47.273 51.093 1.00108.25 C ANISOU 2331 CZ PHE A 293 14715 10325 16090 -1643 -1612 -581 C ATOM 2332 N PHE A 294 -230.718 45.210 47.064 1.00 70.72 N ANISOU 2332 N PHE A 294 9854 5492 11526 -1077 -1992 180 N ATOM 2333 CA PHE A 294 -231.355 43.996 47.554 1.00 71.04 C ANISOU 2333 CA PHE A 294 9746 5753 11494 -957 -1902 72 C ATOM 2334 C PHE A 294 -231.554 42.936 46.478 1.00 73.92 C ANISOU 2334 C PHE A 294 10078 6306 11701 -983 -1946 232 C ATOM 2335 O PHE A 294 -231.700 41.756 46.816 1.00 72.09 O ANISOU 2335 O PHE A 294 9746 6287 11359 -946 -1844 155 O ATOM 2336 CB PHE A 294 -232.707 44.331 48.195 1.00 86.19 C ANISOU 2336 CB PHE A 294 11563 7526 13661 -744 -1908 -64 C ATOM 2337 CG PHE A 294 -232.592 45.102 49.480 1.00101.06 C ANISOU 2337 CG PHE A 294 13443 9285 15669 -715 -1807 -305 C ATOM 2338 CD1 PHE A 294 -231.520 44.896 50.337 1.00 95.88 C ANISOU 2338 CD1 PHE A 294 12814 8783 14833 -843 -1682 -433 C ATOM 2339 CD2 PHE A 294 -233.551 46.038 49.830 1.00107.82 C ANISOU 2339 CD2 PHE A 294 14259 9880 16828 -560 -1841 -417 C ATOM 2340 CE1 PHE A 294 -231.413 45.606 51.522 1.00101.38 C ANISOU 2340 CE1 PHE A 294 13512 9395 15613 -840 -1592 -675 C ATOM 2341 CE2 PHE A 294 -233.449 46.751 51.012 1.00106.18 C ANISOU 2341 CE2 PHE A 294 14048 9564 16731 -548 -1728 -679 C ATOM 2342 CZ PHE A 294 -232.378 46.535 51.858 1.00105.90 C ANISOU 2342 CZ PHE A 294 14054 9705 16477 -701 -1603 -811 C ATOM 2343 N ALA A 295 -231.562 43.320 45.199 1.00 80.73 N ANISOU 2343 N ALA A 295 11032 7100 12544 -1058 -2092 451 N ATOM 2344 CA ALA A 295 -231.647 42.327 44.134 1.00 78.92 C ANISOU 2344 CA ALA A 295 10781 7077 12129 -1123 -2123 576 C ATOM 2345 C ALA A 295 -230.375 41.499 44.015 1.00 89.14 C ANISOU 2345 C ALA A 295 12089 8602 13179 -1292 -1988 550 C ATOM 2346 O ALA A 295 -230.411 40.417 43.418 1.00 80.27 O ANISOU 2346 O ALA A 295 10912 7676 11909 -1328 -1952 569 O ATOM 2347 CB ALA A 295 -231.950 43.003 42.797 1.00 74.20 C ANISOU 2347 CB ALA A 295 10291 6371 11533 -1186 -2323 827 C ATOM 2348 N LYS A 296 -229.254 41.983 44.555 1.00 92.29 N ANISOU 2348 N LYS A 296 12541 8978 13548 -1398 -1914 490 N ATOM 2349 CA LYS A 296 -228.032 41.186 44.545 1.00 75.54 C ANISOU 2349 CA LYS A 296 10391 7080 11233 -1533 -1788 444 C ATOM 2350 C LYS A 296 -228.209 39.904 45.343 1.00 72.59 C ANISOU 2350 C LYS A 296 9879 6879 10821 -1416 -1669 303 C ATOM 2351 O LYS A 296 -227.667 38.855 44.978 1.00 77.65 O ANISOU 2351 O LYS A 296 10467 7709 11330 -1471 -1590 297 O ATOM 2352 CB LYS A 296 -226.865 41.987 45.112 1.00 66.25 C ANISOU 2352 CB LYS A 296 9265 5851 10055 -1658 -1742 384 C ATOM 2353 CG LYS A 296 -226.492 43.226 44.341 1.00 62.87 C ANISOU 2353 CG LYS A 296 8988 5244 9657 -1817 -1833 531 C ATOM 2354 CD LYS A 296 -225.170 43.755 44.860 1.00 66.70 C ANISOU 2354 CD LYS A 296 9492 5743 10109 -1982 -1756 444 C ATOM 2355 CE LYS A 296 -224.989 45.214 44.535 1.00 69.18 C ANISOU 2355 CE LYS A 296 9964 5787 10536 -2110 -1838 545 C ATOM 2356 NZ LYS A 296 -225.100 45.474 43.074 1.00 67.52 N ANISOU 2356 NZ LYS A 296 9878 5534 10243 -2240 -1930 799 N ATOM 2357 N THR A 297 -228.965 39.973 46.442 1.00 65.18 N ANISOU 2357 N THR A 297 8886 5871 10008 -1260 -1647 186 N ATOM 2358 CA THR A 297 -229.178 38.816 47.301 1.00 65.53 C ANISOU 2358 CA THR A 297 8821 6064 10013 -1163 -1534 76 C ATOM 2359 C THR A 297 -229.838 37.653 46.572 1.00 70.56 C ANISOU 2359 C THR A 297 9395 6806 10609 -1126 -1520 124 C ATOM 2360 O THR A 297 -229.813 36.529 47.087 1.00 55.35 O ANISOU 2360 O THR A 297 7392 5003 8635 -1080 -1416 63 O ATOM 2361 CB THR A 297 -230.023 39.214 48.512 1.00 59.34 C ANISOU 2361 CB THR A 297 7998 5189 9358 -1028 -1506 -57 C ATOM 2362 OG1 THR A 297 -229.815 40.601 48.799 1.00 72.17 O ANISOU 2362 OG1 THR A 297 9701 6632 11089 -1057 -1561 -95 O ATOM 2363 CG2 THR A 297 -229.620 38.401 49.728 1.00 59.00 C ANISOU 2363 CG2 THR A 297 7894 5305 9219 -1003 -1382 -167 C ATOM 2364 N SER A 298 -230.423 37.888 45.393 1.00 76.72 N ANISOU 2364 N SER A 298 10209 7539 11403 -1153 -1628 236 N ATOM 2365 CA SER A 298 -230.923 36.782 44.587 1.00 70.13 C ANISOU 2365 CA SER A 298 9316 6827 10501 -1160 -1616 262 C ATOM 2366 C SER A 298 -229.817 35.811 44.202 1.00 72.76 C ANISOU 2366 C SER A 298 9637 7327 10679 -1274 -1507 246 C ATOM 2367 O SER A 298 -230.110 34.666 43.847 1.00 84.72 O ANISOU 2367 O SER A 298 11088 8945 12158 -1268 -1444 210 O ATOM 2368 CB SER A 298 -231.613 37.309 43.328 1.00 72.10 C ANISOU 2368 CB SER A 298 9615 7027 10754 -1200 -1779 398 C ATOM 2369 OG SER A 298 -230.699 38.004 42.498 1.00 80.36 O ANISOU 2369 OG SER A 298 10782 8063 11688 -1363 -1836 519 O ATOM 2370 N ALA A 299 -228.553 36.236 44.263 1.00 66.47 N ANISOU 2370 N ALA A 299 8888 6555 9813 -1378 -1476 254 N ATOM 2371 CA ALA A 299 -227.457 35.301 44.049 1.00 58.27 C ANISOU 2371 CA ALA A 299 7798 5672 8669 -1458 -1359 209 C ATOM 2372 C ALA A 299 -227.329 34.302 45.189 1.00 65.24 C ANISOU 2372 C ALA A 299 8584 6607 9597 -1337 -1254 115 C ATOM 2373 O ALA A 299 -226.631 33.293 45.038 1.00 82.35 O ANISOU 2373 O ALA A 299 10684 8881 11726 -1356 -1160 75 O ATOM 2374 CB ALA A 299 -226.142 36.058 43.867 1.00 58.46 C ANISOU 2374 CB ALA A 299 7868 5719 8623 -1607 -1353 230 C ATOM 2375 N VAL A 300 -227.990 34.552 46.316 1.00 61.52 N ANISOU 2375 N VAL A 300 8104 6062 9208 -1216 -1265 80 N ATOM 2376 CA VAL A 300 -227.929 33.685 47.482 1.00 61.30 C ANISOU 2376 CA VAL A 300 8009 6087 9194 -1117 -1177 22 C ATOM 2377 C VAL A 300 -229.243 32.934 47.693 1.00 75.54 C ANISOU 2377 C VAL A 300 9772 7864 11065 -1019 -1139 2 C ATOM 2378 O VAL A 300 -229.244 31.719 47.882 1.00 88.24 O ANISOU 2378 O VAL A 300 11328 9525 12674 -985 -1051 -7 O ATOM 2379 CB VAL A 300 -227.534 34.485 48.744 1.00 63.18 C ANISOU 2379 CB VAL A 300 8267 6309 9431 -1093 -1192 -23 C ATOM 2380 CG1 VAL A 300 -227.670 33.625 49.987 1.00 59.50 C ANISOU 2380 CG1 VAL A 300 7749 5910 8947 -999 -1117 -56 C ATOM 2381 CG2 VAL A 300 -226.111 35.006 48.611 1.00 70.81 C ANISOU 2381 CG2 VAL A 300 9242 7331 10333 -1206 -1213 -20 C ATOM 2382 N TYR A 301 -230.379 33.641 47.652 1.00 75.58 N ANISOU 2382 N TYR A 301 9792 7778 11148 -975 -1203 -6 N ATOM 2383 CA TYR A 301 -231.637 32.981 47.989 1.00 73.88 C ANISOU 2383 CA TYR A 301 9511 7553 11008 -891 -1154 -48 C ATOM 2384 C TYR A 301 -232.266 32.236 46.816 1.00 75.55 C ANISOU 2384 C TYR A 301 9683 7791 11230 -925 -1168 -28 C ATOM 2385 O TYR A 301 -233.085 31.339 47.048 1.00 81.10 O ANISOU 2385 O TYR A 301 10319 8512 11983 -887 -1095 -71 O ATOM 2386 CB TYR A 301 -232.645 33.980 48.584 1.00 72.98 C ANISOU 2386 CB TYR A 301 9386 7341 11004 -810 -1199 -104 C ATOM 2387 CG TYR A 301 -233.132 35.104 47.683 1.00 71.90 C ANISOU 2387 CG TYR A 301 9275 7091 10951 -810 -1348 -57 C ATOM 2388 CD1 TYR A 301 -234.017 34.860 46.639 1.00 72.75 C ANISOU 2388 CD1 TYR A 301 9339 7200 11103 -808 -1428 -11 C ATOM 2389 CD2 TYR A 301 -232.752 36.419 47.920 1.00 70.57 C ANISOU 2389 CD2 TYR A 301 9178 6807 10829 -813 -1419 -56 C ATOM 2390 CE1 TYR A 301 -234.473 35.885 45.833 1.00 75.32 C ANISOU 2390 CE1 TYR A 301 9692 7423 11504 -798 -1594 68 C ATOM 2391 CE2 TYR A 301 -233.207 37.452 47.121 1.00 71.68 C ANISOU 2391 CE2 TYR A 301 9356 6809 11071 -803 -1568 17 C ATOM 2392 CZ TYR A 301 -234.066 37.179 46.079 1.00 77.29 C ANISOU 2392 CZ TYR A 301 10023 7530 11814 -789 -1665 95 C ATOM 2393 OH TYR A 301 -234.520 38.205 45.280 1.00 87.83 O ANISOU 2393 OH TYR A 301 11398 8728 13245 -772 -1843 204 O ATOM 2394 N ASN A 302 -231.916 32.575 45.568 1.00 71.78 N ANISOU 2394 N ASN A 302 9249 7330 10694 -1019 -1255 31 N ATOM 2395 CA ASN A 302 -232.427 31.789 44.444 1.00 71.35 C ANISOU 2395 CA ASN A 302 9159 7339 10610 -1080 -1263 29 C ATOM 2396 C ASN A 302 -231.896 30.361 44.453 1.00 71.13 C ANISOU 2396 C ASN A 302 9091 7382 10554 -1109 -1115 -32 C ATOM 2397 O ASN A 302 -232.698 29.429 44.268 1.00 74.78 O ANISOU 2397 O ASN A 302 9492 7859 11064 -1105 -1062 -86 O ATOM 2398 CB ASN A 302 -232.128 32.494 43.117 1.00 71.73 C ANISOU 2398 CB ASN A 302 9279 7416 10558 -1200 -1387 113 C ATOM 2399 CG ASN A 302 -233.191 33.507 42.740 1.00 77.45 C ANISOU 2399 CG ASN A 302 10014 8062 11352 -1158 -1562 188 C ATOM 2400 OD1 ASN A 302 -234.333 33.427 43.195 1.00 66.21 O ANISOU 2400 OD1 ASN A 302 8505 6595 10057 -1049 -1581 144 O ATOM 2401 ND2 ASN A 302 -232.823 34.462 41.893 1.00 93.10 N ANISOU 2401 ND2 ASN A 302 12093 10021 13258 -1248 -1691 310 N ATOM 2402 N PRO A 303 -230.594 30.103 44.643 1.00 71.41 N ANISOU 2402 N PRO A 303 9145 7452 10537 -1138 -1044 -32 N ATOM 2403 CA PRO A 303 -230.163 28.701 44.755 1.00 64.54 C ANISOU 2403 CA PRO A 303 8220 6607 9695 -1128 -907 -89 C ATOM 2404 C PRO A 303 -230.690 28.013 46.002 1.00 66.98 C ANISOU 2404 C PRO A 303 8495 6859 10095 -1018 -830 -91 C ATOM 2405 O PRO A 303 -230.815 26.783 46.007 1.00 75.36 O ANISOU 2405 O PRO A 303 9517 7898 11218 -1008 -727 -127 O ATOM 2406 CB PRO A 303 -228.631 28.798 44.763 1.00 65.35 C ANISOU 2406 CB PRO A 303 8325 6759 9745 -1162 -875 -82 C ATOM 2407 CG PRO A 303 -228.340 30.174 45.227 1.00 63.34 C ANISOU 2407 CG PRO A 303 8128 6490 9450 -1164 -975 -24 C ATOM 2408 CD PRO A 303 -229.441 31.023 44.671 1.00 66.96 C ANISOU 2408 CD PRO A 303 8635 6902 9905 -1188 -1085 11 C ATOM 2409 N VAL A 304 -231.010 28.762 47.059 1.00 56.59 N ANISOU 2409 N VAL A 304 7200 5515 8788 -949 -867 -61 N ATOM 2410 CA VAL A 304 -231.579 28.138 48.251 1.00 60.41 C ANISOU 2410 CA VAL A 304 7662 5971 9320 -874 -782 -60 C ATOM 2411 C VAL A 304 -232.999 27.659 47.975 1.00 74.27 C ANISOU 2411 C VAL A 304 9367 7698 11155 -881 -747 -110 C ATOM 2412 O VAL A 304 -233.410 26.587 48.437 1.00 79.92 O ANISOU 2412 O VAL A 304 10056 8388 11923 -871 -636 -115 O ATOM 2413 CB VAL A 304 -231.526 29.112 49.442 1.00 61.69 C ANISOU 2413 CB VAL A 304 7857 6139 9443 -824 -815 -49 C ATOM 2414 CG1 VAL A 304 -232.331 28.572 50.615 1.00 51.57 C ANISOU 2414 CG1 VAL A 304 6559 4856 8180 -777 -718 -57 C ATOM 2415 CG2 VAL A 304 -230.084 29.355 49.860 1.00 77.22 C ANISOU 2415 CG2 VAL A 304 9852 8155 11331 -828 -840 -8 C ATOM 2416 N ILE A 305 -233.761 28.430 47.201 1.00 75.56 N ANISOU 2416 N ILE A 305 9510 7864 11337 -903 -848 -138 N ATOM 2417 CA ILE A 305 -235.160 28.095 46.955 1.00 67.33 C ANISOU 2417 CA ILE A 305 8386 6816 10380 -906 -839 -196 C ATOM 2418 C ILE A 305 -235.292 27.063 45.839 1.00 66.86 C ANISOU 2418 C ILE A 305 8295 6785 10323 -998 -809 -239 C ATOM 2419 O ILE A 305 -236.051 26.095 45.962 1.00 86.79 O ANISOU 2419 O ILE A 305 10759 9296 12923 -1021 -714 -296 O ATOM 2420 CB ILE A 305 -235.950 29.379 46.646 1.00 69.50 C ANISOU 2420 CB ILE A 305 8632 7076 10698 -869 -985 -200 C ATOM 2421 CG1 ILE A 305 -236.055 30.242 47.903 1.00 65.70 C ANISOU 2421 CG1 ILE A 305 8159 6550 10252 -780 -967 -217 C ATOM 2422 CG2 ILE A 305 -237.331 29.055 46.099 1.00 75.97 C ANISOU 2422 CG2 ILE A 305 9336 7919 11610 -881 -1015 -262 C ATOM 2423 CD1 ILE A 305 -236.746 31.556 47.676 1.00 54.77 C ANISOU 2423 CD1 ILE A 305 6744 5105 8959 -718 -1105 -230 C ATOM 2424 N TYR A 306 -234.558 27.242 44.744 1.00 57.97 N ANISOU 2424 N TYR A 306 7211 5705 9111 -1071 -876 -227 N ATOM 2425 CA TYR A 306 -234.712 26.393 43.571 1.00 67.61 C ANISOU 2425 CA TYR A 306 8402 6978 10307 -1182 -853 -301 C ATOM 2426 C TYR A 306 -233.813 25.162 43.583 1.00 75.77 C ANISOU 2426 C TYR A 306 9445 7981 11362 -1210 -696 -352 C ATOM 2427 O TYR A 306 -234.045 24.243 42.790 1.00 83.77 O ANISOU 2427 O TYR A 306 10425 9012 12393 -1300 -633 -455 O ATOM 2428 CB TYR A 306 -234.440 27.202 42.298 1.00 70.14 C ANISOU 2428 CB TYR A 306 8766 7388 10497 -1275 -996 -270 C ATOM 2429 CG TYR A 306 -235.541 28.178 41.947 1.00 83.07 C ANISOU 2429 CG TYR A 306 10375 9045 12144 -1256 -1176 -220 C ATOM 2430 CD1 TYR A 306 -235.580 29.449 42.510 1.00 86.86 C ANISOU 2430 CD1 TYR A 306 10888 9457 12659 -1162 -1281 -127 C ATOM 2431 CD2 TYR A 306 -236.542 27.828 41.052 1.00 87.09 C ANISOU 2431 CD2 TYR A 306 10812 9635 12645 -1331 -1249 -273 C ATOM 2432 CE1 TYR A 306 -236.588 30.341 42.189 1.00 84.91 C ANISOU 2432 CE1 TYR A 306 10600 9197 12467 -1118 -1454 -78 C ATOM 2433 CE2 TYR A 306 -237.551 28.712 40.726 1.00 88.02 C ANISOU 2433 CE2 TYR A 306 10879 9772 12794 -1293 -1439 -213 C ATOM 2434 CZ TYR A 306 -237.571 29.965 41.296 1.00 86.54 C ANISOU 2434 CZ TYR A 306 10721 9490 12669 -1175 -1542 -110 C ATOM 2435 OH TYR A 306 -238.579 30.841 40.967 1.00 94.26 O ANISOU 2435 OH TYR A 306 11635 10457 13722 -1113 -1740 -48 O ATOM 2436 N ILE A 307 -232.804 25.109 44.451 1.00 69.05 N ANISOU 2436 N ILE A 307 8630 7083 10523 -1134 -638 -293 N ATOM 2437 CA ILE A 307 -231.849 24.006 44.407 1.00 66.13 C ANISOU 2437 CA ILE A 307 8251 6669 10205 -1135 -512 -330 C ATOM 2438 C ILE A 307 -231.748 23.321 45.764 1.00 67.63 C ANISOU 2438 C ILE A 307 8444 6757 10495 -1028 -425 -258 C ATOM 2439 O ILE A 307 -231.946 22.106 45.869 1.00 75.70 O ANISOU 2439 O ILE A 307 9446 7683 11633 -1029 -309 -290 O ATOM 2440 CB ILE A 307 -230.467 24.488 43.932 1.00 66.09 C ANISOU 2440 CB ILE A 307 8265 6730 10115 -1159 -538 -324 C ATOM 2441 CG1 ILE A 307 -230.568 25.078 42.525 1.00 73.39 C ANISOU 2441 CG1 ILE A 307 9208 7767 10910 -1299 -612 -378 C ATOM 2442 CG2 ILE A 307 -229.467 23.344 43.958 1.00 53.21 C ANISOU 2442 CG2 ILE A 307 6591 5043 8583 -1129 -407 -376 C ATOM 2443 CD1 ILE A 307 -229.341 25.843 42.096 1.00 70.89 C ANISOU 2443 CD1 ILE A 307 8921 7533 10483 -1354 -644 -353 C ATOM 2444 N MET A 308 -231.430 24.085 46.812 1.00 73.88 N ANISOU 2444 N MET A 308 9269 7566 11235 -949 -481 -156 N ATOM 2445 CA MET A 308 -231.276 23.483 48.133 1.00 82.44 C ANISOU 2445 CA MET A 308 10371 8587 12365 -865 -416 -62 C ATOM 2446 C MET A 308 -232.588 22.938 48.683 1.00 84.83 C ANISOU 2446 C MET A 308 10669 8834 12728 -879 -337 -62 C ATOM 2447 O MET A 308 -232.559 22.067 49.558 1.00 93.42 O ANISOU 2447 O MET A 308 11780 9846 13867 -845 -251 19 O ATOM 2448 CB MET A 308 -230.679 24.489 49.119 1.00100.42 C ANISOU 2448 CB MET A 308 12685 10932 14539 -806 -498 21 C ATOM 2449 CG MET A 308 -229.159 24.559 49.084 1.00118.42 C ANISOU 2449 CG MET A 308 14952 13249 16794 -774 -536 56 C ATOM 2450 SD MET A 308 -228.451 25.043 50.671 1.00134.36 S ANISOU 2450 SD MET A 308 17001 15333 18717 -698 -598 174 S ATOM 2451 CE MET A 308 -228.978 23.680 51.710 1.00137.72 C ANISOU 2451 CE MET A 308 17452 15670 19204 -641 -501 289 C ATOM 2452 N MET A 309 -233.730 23.423 48.200 1.00 88.21 N ANISOU 2452 N MET A 309 11061 9300 13156 -934 -369 -143 N ATOM 2453 CA MET A 309 -235.013 22.851 48.583 1.00 83.08 C ANISOU 2453 CA MET A 309 10372 8613 12581 -970 -280 -175 C ATOM 2454 C MET A 309 -235.503 21.796 47.601 1.00 88.70 C ANISOU 2454 C MET A 309 11036 9270 13396 -1063 -209 -276 C ATOM 2455 O MET A 309 -236.520 21.146 47.870 1.00 96.26 O ANISOU 2455 O MET A 309 11953 10185 14436 -1117 -115 -313 O ATOM 2456 CB MET A 309 -236.063 23.954 48.737 1.00 83.12 C ANISOU 2456 CB MET A 309 10327 8692 12561 -963 -351 -222 C ATOM 2457 CG MET A 309 -235.828 24.827 49.958 1.00 90.14 C ANISOU 2457 CG MET A 309 11259 9617 13372 -890 -369 -162 C ATOM 2458 SD MET A 309 -237.157 25.993 50.303 1.00 96.96 S ANISOU 2458 SD MET A 309 12040 10532 14268 -863 -409 -255 S ATOM 2459 CE MET A 309 -236.699 26.520 51.953 1.00 98.50 C ANISOU 2459 CE MET A 309 12307 10766 14352 -814 -354 -208 C ATOM 2460 N ASN A 310 -234.812 21.615 46.477 1.00 95.43 N ANISOU 2460 N ASN A 310 11888 10133 14239 -1101 -238 -341 N ATOM 2461 CA ASN A 310 -235.052 20.458 45.628 1.00 89.61 C ANISOU 2461 CA ASN A 310 11116 9331 13600 -1197 -143 -461 C ATOM 2462 C ASN A 310 -234.661 19.196 46.386 1.00 83.67 C ANISOU 2462 C ASN A 310 10399 8405 12987 -1160 5 -403 C ATOM 2463 O ASN A 310 -233.591 19.133 46.999 1.00 82.89 O ANISOU 2463 O ASN A 310 10346 8259 12889 -1059 6 -291 O ATOM 2464 CB ASN A 310 -234.252 20.587 44.328 1.00 90.05 C ANISOU 2464 CB ASN A 310 11170 9457 13589 -1254 -188 -556 C ATOM 2465 CG ASN A 310 -234.644 19.556 43.284 1.00 94.81 C ANISOU 2465 CG ASN A 310 11728 10033 14262 -1385 -100 -734 C ATOM 2466 OD1 ASN A 310 -234.779 18.368 43.580 1.00110.04 O ANISOU 2466 OD1 ASN A 310 13652 11809 16350 -1398 42 -776 O ATOM 2467 ND2 ASN A 310 -234.822 20.010 42.048 1.00 87.40 N ANISOU 2467 ND2 ASN A 310 10767 9242 13199 -1496 -187 -839 N ATOM 2468 N LYS A 311 -235.540 18.193 46.356 1.00 96.61 N ANISOU 2468 N LYS A 311 12012 9943 14751 -1245 122 -470 N ATOM 2469 CA LYS A 311 -235.333 17.003 47.176 1.00107.72 C ANISOU 2469 CA LYS A 311 13470 11151 16307 -1217 262 -379 C ATOM 2470 C LYS A 311 -234.067 16.256 46.767 1.00100.78 C ANISOU 2470 C LYS A 311 12611 10144 15538 -1158 306 -394 C ATOM 2471 O LYS A 311 -233.381 15.671 47.614 1.00 90.81 O ANISOU 2471 O LYS A 311 11400 8739 14365 -1057 347 -241 O ATOM 2472 CB LYS A 311 -236.556 16.091 47.082 1.00115.35 C ANISOU 2472 CB LYS A 311 14401 12025 17401 -1354 388 -471 C ATOM 2473 CG LYS A 311 -236.704 15.117 48.236 1.00120.72 C ANISOU 2473 CG LYS A 311 15154 12514 18202 -1348 524 -317 C ATOM 2474 CD LYS A 311 -238.036 14.384 48.161 1.00124.67 C ANISOU 2474 CD LYS A 311 15607 12948 18814 -1515 653 -419 C ATOM 2475 CE LYS A 311 -238.259 13.505 49.382 1.00120.63 C ANISOU 2475 CE LYS A 311 15185 12255 18394 -1537 795 -234 C ATOM 2476 NZ LYS A 311 -239.577 12.814 49.332 1.00117.88 N ANISOU 2476 NZ LYS A 311 14783 11848 18157 -1728 938 -340 N ATOM 2477 N GLN A 312 -233.736 16.275 45.475 1.00100.99 N ANISOU 2477 N GLN A 312 12589 10228 15555 -1220 296 -579 N ATOM 2478 CA GLN A 312 -232.562 15.553 44.995 1.00106.17 C ANISOU 2478 CA GLN A 312 13234 10770 16336 -1171 366 -647 C ATOM 2479 C GLN A 312 -231.275 16.244 45.432 1.00102.44 C ANISOU 2479 C GLN A 312 12767 10368 15788 -1027 272 -518 C ATOM 2480 O GLN A 312 -230.399 15.623 46.046 1.00101.02 O ANISOU 2480 O GLN A 312 12592 10044 15747 -902 306 -414 O ATOM 2481 CB GLN A 312 -232.612 15.430 43.470 1.00118.22 C ANISOU 2481 CB GLN A 312 14703 12381 17834 -1311 398 -910 C ATOM 2482 CG GLN A 312 -233.959 15.011 42.907 1.00130.43 C ANISOU 2482 CG GLN A 312 16222 13937 19398 -1482 445 -1062 C ATOM 2483 CD GLN A 312 -234.010 15.130 41.395 1.00139.83 C ANISOU 2483 CD GLN A 312 17364 15288 20478 -1639 433 -1307 C ATOM 2484 OE1 GLN A 312 -232.984 15.039 40.720 1.00134.52 O ANISOU 2484 OE1 GLN A 312 16680 14640 19791 -1637 473 -1413 O ATOM 2485 NE2 GLN A 312 -235.205 15.345 40.858 1.00149.36 N ANISOU 2485 NE2 GLN A 312 18532 16625 21593 -1784 375 -1400 N ATOM 2486 N PHE A 313 -231.149 17.539 45.122 1.00 97.18 N ANISOU 2486 N PHE A 313 12095 9916 14913 -1047 143 -517 N ATOM 2487 CA PHE A 313 -229.911 18.266 45.396 1.00 89.38 C ANISOU 2487 CA PHE A 313 11100 9013 13846 -947 58 -430 C ATOM 2488 C PHE A 313 -229.552 18.236 46.877 1.00 86.30 C ANISOU 2488 C PHE A 313 10748 8559 13482 -808 19 -209 C ATOM 2489 O PHE A 313 -228.370 18.173 47.234 1.00 86.48 O ANISOU 2489 O PHE A 313 10742 8571 13547 -700 -10 -137 O ATOM 2490 CB PHE A 313 -230.035 19.713 44.919 1.00 87.23 C ANISOU 2490 CB PHE A 313 10839 8952 13354 -1013 -73 -443 C ATOM 2491 CG PHE A 313 -229.935 19.880 43.429 1.00 92.44 C ANISOU 2491 CG PHE A 313 11468 9720 13935 -1148 -64 -622 C ATOM 2492 CD1 PHE A 313 -228.700 20.037 42.821 1.00 96.18 C ANISOU 2492 CD1 PHE A 313 11903 10262 14377 -1158 -45 -690 C ATOM 2493 CD2 PHE A 313 -231.073 19.900 42.639 1.00 90.91 C ANISOU 2493 CD2 PHE A 313 11275 9584 13683 -1279 -78 -725 C ATOM 2494 CE1 PHE A 313 -228.600 20.200 41.451 1.00 91.75 C ANISOU 2494 CE1 PHE A 313 11327 9829 13704 -1312 -23 -854 C ATOM 2495 CE2 PHE A 313 -230.980 20.062 41.267 1.00 91.00 C ANISOU 2495 CE2 PHE A 313 11270 9726 13578 -1424 -83 -876 C ATOM 2496 CZ PHE A 313 -229.742 20.213 40.673 1.00 89.59 C ANISOU 2496 CZ PHE A 313 11075 9620 13345 -1449 -48 -939 C ATOM 2497 N ARG A 314 -230.558 18.286 47.753 1.00 85.37 N ANISOU 2497 N ARG A 314 10687 8421 13329 -818 18 -104 N ATOM 2498 CA ARG A 314 -230.293 18.354 49.187 1.00 89.53 C ANISOU 2498 CA ARG A 314 11267 8932 13817 -718 -24 108 C ATOM 2499 C ARG A 314 -229.563 17.107 49.673 1.00 97.00 C ANISOU 2499 C ARG A 314 12218 9686 14950 -618 34 222 C ATOM 2500 O ARG A 314 -228.531 17.200 50.348 1.00 84.68 O ANISOU 2500 O ARG A 314 10651 8147 13377 -500 -46 360 O ATOM 2501 CB ARG A 314 -231.605 18.542 49.948 1.00 87.02 C ANISOU 2501 CB ARG A 314 11001 8636 13427 -780 3 163 C ATOM 2502 CG ARG A 314 -231.461 19.225 51.298 1.00 87.01 C ANISOU 2502 CG ARG A 314 11055 8734 13271 -723 -68 327 C ATOM 2503 CD ARG A 314 -232.733 19.100 52.132 1.00 91.60 C ANISOU 2503 CD ARG A 314 11679 9314 13809 -794 14 373 C ATOM 2504 NE ARG A 314 -233.943 19.366 51.357 1.00 97.88 N ANISOU 2504 NE ARG A 314 12417 10141 14634 -895 55 201 N ATOM 2505 CZ ARG A 314 -234.790 18.427 50.944 1.00108.84 C ANISOU 2505 CZ ARG A 314 13781 11417 16157 -985 172 133 C ATOM 2506 NH1 ARG A 314 -234.563 17.153 51.234 1.00120.90 N ANISOU 2506 NH1 ARG A 314 15356 12761 17820 -986 274 225 N ATOM 2507 NH2 ARG A 314 -235.865 18.760 50.242 1.00104.60 N ANISOU 2507 NH2 ARG A 314 13167 10944 15634 -1074 179 -26 N ATOM 2508 N ASN A 315 -230.081 15.925 49.328 1.00106.85 N ANISOU 2508 N ASN A 315 13473 10737 16389 -662 166 167 N ATOM 2509 CA ASN A 315 -229.462 14.685 49.787 1.00108.64 C ANISOU 2509 CA ASN A 315 13714 10726 16840 -557 222 291 C ATOM 2510 C ASN A 315 -228.075 14.499 49.183 1.00100.01 C ANISOU 2510 C ASN A 315 12520 9603 15875 -443 198 214 C ATOM 2511 O ASN A 315 -227.168 13.972 49.837 1.00108.59 O ANISOU 2511 O ASN A 315 13591 10579 17091 -291 155 376 O ATOM 2512 CB ASN A 315 -230.359 13.497 49.444 1.00118.94 C ANISOU 2512 CB ASN A 315 15047 11801 18345 -652 385 214 C ATOM 2513 CG ASN A 315 -231.785 13.691 49.922 1.00128.36 C ANISOU 2513 CG ASN A 315 16303 13046 19421 -790 429 247 C ATOM 2514 OD1 ASN A 315 -232.159 14.777 50.364 1.00133.89 O ANISOU 2514 OD1 ASN A 315 17014 13961 19897 -811 344 288 O ATOM 2515 ND2 ASN A 315 -232.591 12.640 49.825 1.00127.55 N ANISOU 2515 ND2 ASN A 315 16231 12743 19491 -890 572 210 N ATOM 2516 N CYS A 316 -227.892 14.930 47.935 1.00 88.89 N ANISOU 2516 N CYS A 316 11035 8306 14431 -518 223 -30 N ATOM 2517 CA CYS A 316 -226.592 14.799 47.288 1.00 89.30 C ANISOU 2517 CA CYS A 316 10973 8361 14595 -436 230 -143 C ATOM 2518 C CYS A 316 -225.575 15.774 47.863 1.00 95.18 C ANISOU 2518 C CYS A 316 11674 9292 15197 -341 78 -19 C ATOM 2519 O CYS A 316 -224.386 15.447 47.946 1.00106.92 O ANISOU 2519 O CYS A 316 13059 10739 16828 -209 56 -2 O ATOM 2520 CB CYS A 316 -226.734 15.000 45.783 1.00 89.72 C ANISOU 2520 CB CYS A 316 10971 8512 14605 -585 314 -440 C ATOM 2521 SG CYS A 316 -227.828 13.794 44.986 1.00 77.10 S ANISOU 2521 SG CYS A 316 9399 6714 13182 -721 496 -644 S ATOM 2522 N MET A 317 -226.011 16.967 48.265 1.00 87.97 N ANISOU 2522 N MET A 317 10824 8578 14024 -406 -28 52 N ATOM 2523 CA MET A 317 -225.083 17.891 48.909 1.00 93.32 C ANISOU 2523 CA MET A 317 11468 9423 14566 -335 -171 162 C ATOM 2524 C MET A 317 -224.679 17.387 50.288 1.00 91.25 C ANISOU 2524 C MET A 317 11229 9085 14359 -189 -249 414 C ATOM 2525 O MET A 317 -223.521 17.539 50.697 1.00 89.23 O ANISOU 2525 O MET A 317 10886 8896 14122 -80 -350 489 O ATOM 2526 CB MET A 317 -225.695 19.288 49.003 1.00105.88 C ANISOU 2526 CB MET A 317 13127 11210 15892 -443 -254 157 C ATOM 2527 CG MET A 317 -225.687 20.034 47.682 1.00114.81 C ANISOU 2527 CG MET A 317 14226 12461 16937 -570 -237 -39 C ATOM 2528 SD MET A 317 -226.798 21.452 47.627 1.00113.08 S ANISOU 2528 SD MET A 317 14101 12381 16485 -690 -321 -43 S ATOM 2529 CE MET A 317 -226.984 21.620 45.853 1.00108.59 C ANISOU 2529 CE MET A 317 13505 11873 15882 -843 -269 -251 C ATOM 2530 N VAL A 318 -225.616 16.776 51.016 1.00 89.88 N ANISOU 2530 N VAL A 318 11165 8784 14201 -198 -210 553 N ATOM 2531 CA VAL A 318 -225.275 16.170 52.300 1.00 93.84 C ANISOU 2531 CA VAL A 318 11710 9202 14741 -78 -282 824 C ATOM 2532 C VAL A 318 -224.302 15.018 52.097 1.00104.63 C ANISOU 2532 C VAL A 318 12981 10359 16416 80 -266 860 C ATOM 2533 O VAL A 318 -223.347 14.845 52.865 1.00115.74 O ANISOU 2533 O VAL A 318 14337 11775 17864 227 -396 1046 O ATOM 2534 CB VAL A 318 -226.549 15.709 53.033 1.00 89.01 C ANISOU 2534 CB VAL A 318 11246 8494 14079 -157 -210 957 C ATOM 2535 CG1 VAL A 318 -226.185 14.929 54.288 1.00 89.31 C ANISOU 2535 CG1 VAL A 318 11350 8425 14158 -49 -279 1267 C ATOM 2536 CG2 VAL A 318 -227.422 16.904 53.378 1.00 83.51 C ANISOU 2536 CG2 VAL A 318 10615 8017 13100 -283 -234 916 C ATOM 2537 N THR A 319 -224.526 14.215 51.055 1.00100.35 N ANISOU 2537 N THR A 319 12399 9625 16104 54 -112 672 N ATOM 2538 CA THR A 319 -223.630 13.102 50.765 1.00 98.16 C ANISOU 2538 CA THR A 319 12014 9114 16168 210 -69 656 C ATOM 2539 C THR A 319 -222.236 13.594 50.397 1.00 93.29 C ANISOU 2539 C THR A 319 11213 8649 15586 313 -150 559 C ATOM 2540 O THR A 319 -221.230 12.978 50.772 1.00 91.97 O ANISOU 2540 O THR A 319 10933 8369 15641 505 -217 667 O ATOM 2541 CB THR A 319 -224.215 12.249 49.639 1.00 97.36 C ANISOU 2541 CB THR A 319 11906 8801 16283 123 136 408 C ATOM 2542 OG1 THR A 319 -225.449 11.660 50.072 1.00101.19 O ANISOU 2542 OG1 THR A 319 12546 9123 16780 30 213 514 O ATOM 2543 CG2 THR A 319 -223.249 11.152 49.236 1.00 97.57 C ANISOU 2543 CG2 THR A 319 11801 8574 16696 288 204 332 C ATOM 2544 N THR A 320 -222.153 14.713 49.678 1.00 89.99 N ANISOU 2544 N THR A 320 10752 8484 14957 187 -149 365 N ATOM 2545 CA THR A 320 -220.861 15.195 49.204 1.00 91.47 C ANISOU 2545 CA THR A 320 10756 8825 15174 242 -191 238 C ATOM 2546 C THR A 320 -220.055 15.836 50.328 1.00106.07 C ANISOU 2546 C THR A 320 12561 10844 16898 344 -399 456 C ATOM 2547 O THR A 320 -218.860 15.556 50.485 1.00112.67 O ANISOU 2547 O THR A 320 13222 11682 17906 498 -469 480 O ATOM 2548 CB THR A 320 -221.066 16.182 48.054 1.00 78.50 C ANISOU 2548 CB THR A 320 9107 7389 13331 45 -120 -14 C ATOM 2549 OG1 THR A 320 -221.640 15.496 46.936 1.00 82.22 O ANISOU 2549 OG1 THR A 320 9588 7728 13924 -49 65 -240 O ATOM 2550 CG2 THR A 320 -219.737 16.799 47.636 1.00 70.34 C ANISOU 2550 CG2 THR A 320 7893 6543 12291 64 -155 -132 C ATOM 2551 N LEU A 321 -220.690 16.698 51.120 1.00108.01 N ANISOU 2551 N LEU A 321 12947 11241 16850 256 -500 597 N ATOM 2552 CA LEU A 321 -220.002 17.440 52.176 1.00106.80 C ANISOU 2552 CA LEU A 321 12764 11288 16525 308 -695 766 C ATOM 2553 C LEU A 321 -219.382 16.521 53.223 1.00113.61 C ANISOU 2553 C LEU A 321 13584 12040 17543 508 -822 1031 C ATOM 2554 O LEU A 321 -220.086 15.873 53.993 1.00120.01 O ANISOU 2554 O LEU A 321 14538 12709 18349 534 -830 1242 O ATOM 2555 CB LEU A 321 -220.967 18.419 52.851 1.00 96.16 C ANISOU 2555 CB LEU A 321 11592 10090 14854 169 -745 840 C ATOM 2556 CG LEU A 321 -221.453 19.582 51.983 1.00 81.19 C ANISOU 2556 CG LEU A 321 9730 8331 12785 -9 -685 626 C ATOM 2557 CD1 LEU A 321 -222.397 20.479 52.767 1.00 73.45 C ANISOU 2557 CD1 LEU A 321 8903 7463 11542 -110 -735 697 C ATOM 2558 CD2 LEU A 321 -220.271 20.373 51.444 1.00 74.89 C ANISOU 2558 CD2 LEU A 321 8783 7707 11967 -31 -737 492 C ATOM 2559 N CYS A 322 -221.286 13.926 53.493 1.00150.79 N ATOM 2560 CA CYS A 322 -220.976 12.782 54.314 1.00154.12 C ATOM 2561 O CYS A 322 -218.953 10.238 54.950 1.00143.27 O ATOM 2562 CB CYS A 322 -221.944 12.598 55.482 1.00161.18 C ATOM 2563 SG CYS A 322 -221.314 13.227 57.011 1.00160.21 S ATOM 2564 N CYS A 323 -218.544 13.694 52.245 1.00111.62 N ANISOU 2564 N CYS A 323 13114 11168 18127 843 -635 975 N ATOM 2565 CA CYS A 323 -217.462 12.720 52.255 1.00115.17 C ANISOU 2565 CA CYS A 323 13370 11430 18960 1084 -675 1017 C ATOM 2566 C CYS A 323 -217.900 11.415 51.599 1.00106.66 C ANISOU 2566 C CYS A 323 12315 9969 18240 1135 -478 915 C ATOM 2567 O CYS A 323 -217.232 10.911 50.696 1.00106.83 O ANISOU 2567 O CYS A 323 12149 9874 18566 1218 -358 669 O ATOM 2568 CB CYS A 323 -216.987 12.464 53.686 1.00124.44 C ANISOU 2568 CB CYS A 323 14554 12608 20121 1256 -927 1408 C ATOM 2569 SG CYS A 323 -216.460 13.954 54.562 1.00129.30 S ANISOU 2569 SG CYS A 323 15141 13678 20308 1180 -1165 1510 S ATOM 2570 N GLY A 324 -219.030 10.875 52.048 1.00102.05 N ANISOU 2570 N GLY A 324 11956 9194 17624 1068 -430 1082 N ATOM 2571 CA GLY A 324 -219.523 9.627 51.502 1.00102.08 C ANISOU 2571 CA GLY A 324 12002 8814 17968 1090 -242 992 C ATOM 2572 C GLY A 324 -220.860 9.185 52.060 1.00111.35 C ANISOU 2572 C GLY A 324 13434 9824 19051 965 -186 1181 C ATOM 2573 O GLY A 324 -221.772 8.848 51.300 1.00113.87 O ANISOU 2573 O GLY A 324 13830 10014 19420 809 13 972 O ATOM 2574 N LYS A 325 -220.991 9.180 53.386 1.00123.79 N ANISOU 2574 N LYS A 325 15137 11421 20478 1013 -357 1568 N ATOM 2575 CA LYS A 325 -222.218 8.732 54.031 1.00142.01 C ANISOU 2575 CA LYS A 325 17685 13583 22690 883 -296 1773 C ATOM 2576 C LYS A 325 -223.260 9.845 54.043 1.00149.79 C ANISOU 2576 C LYS A 325 18786 14875 23252 636 -252 1673 C ATOM 2577 O LYS A 325 -223.200 10.764 53.219 1.00150.45 O ANISOU 2577 O LYS A 325 18779 15191 23194 548 -216 1389 O ATOM 2578 CB LYS A 325 -221.925 8.259 55.458 1.00152.73 C ANISOU 2578 CB LYS A 325 19141 14857 24033 1015 -491 2241 C ATOM 2579 CG LYS A 325 -222.861 7.170 55.975 1.00155.62 C ANISOU 2579 CG LYS A 325 19719 14883 24525 952 -392 2478 C ATOM 2580 CD LYS A 325 -223.162 7.362 57.452 1.00153.81 C ANISOU 2580 CD LYS A 325 19674 14795 23970 904 -552 2901 C ATOM 2581 CE LYS A 325 -224.205 6.369 57.945 1.00151.60 C ANISOU 2581 CE LYS A 325 19623 14210 23769 783 -423 3128 C ATOM 2582 NZ LYS A 325 -223.748 4.961 57.799 1.00153.24 N ANISOU 2582 NZ LYS A 325 19820 13926 24480 968 -404 3271 N ATOM 2583 N ASN A 326 -224.224 9.754 54.971 1.00162.63 N ANISOU 2583 N ASN A 326 20609 16494 24688 521 -250 1909 N ATOM 2584 CA ASN A 326 -225.234 10.761 55.286 1.00177.71 C ANISOU 2584 CA ASN A 326 22628 18683 26210 313 -226 1871 C ATOM 2585 C ASN A 326 -226.191 10.189 56.326 1.00192.28 C ANISOU 2585 C ASN A 326 24677 20416 27965 212 -182 2153 C ATOM 2586 O ASN A 326 -226.483 8.986 56.304 1.00200.45 O ANISOU 2586 O ASN A 326 25781 21107 29274 223 -80 2254 O ATOM 2587 CB ASN A 326 -226.012 11.200 54.041 1.00179.51 C ANISOU 2587 CB ASN A 326 22815 18970 26419 149 -59 1496 C ATOM 2588 CG ASN A 326 -226.982 10.144 53.554 1.00183.61 C ANISOU 2588 CG ASN A 326 23406 19192 27165 43 143 1412 C ATOM 2589 OD1 ASN A 326 -228.159 10.152 53.914 1.00184.29 O ANISOU 2589 OD1 ASN A 326 23612 19293 27117 -124 229 1453 O ATOM 2590 ND2 ASN A 326 -226.493 9.227 52.728 1.00186.10 N ANISOU 2590 ND2 ASN A 326 23636 19239 27836 129 231 1269 N ATOM 2591 N PRO A 327 -226.693 11.004 57.254 1.00193.92 N ANISOU 2591 N PRO A 327 24985 20896 27800 98 -242 2276 N ATOM 2592 CA PRO A 327 -227.688 10.501 58.211 1.00193.52 C ANISOU 2592 CA PRO A 327 25125 20772 27630 -40 -162 2516 C ATOM 2593 C PRO A 327 -229.015 10.227 57.517 1.00190.56 C ANISOU 2593 C PRO A 327 24786 20278 27338 -233 75 2294 C ATOM 2594 O PRO A 327 -229.587 11.106 56.868 1.00190.93 O ANISOU 2594 O PRO A 327 24766 20520 27260 -338 136 2006 O ATOM 2595 CB PRO A 327 -227.805 11.635 59.237 1.00192.06 C ANISOU 2595 CB PRO A 327 24999 20968 27008 -119 -272 2611 C ATOM 2596 CG PRO A 327 -227.380 12.856 58.496 1.00188.46 C ANISOU 2596 CG PRO A 327 24390 20757 26458 -93 -332 2309 C ATOM 2597 CD PRO A 327 -226.326 12.406 57.522 1.00190.83 C ANISOU 2597 CD PRO A 327 24536 20886 27084 84 -375 2200 C ATOM 2598 N LEU A 328 -229.497 8.996 57.654 1.00185.80 N ANISOU 2598 N LEU A 328 24287 19347 26960 -281 199 2437 N ATOM 2599 CA LEU A 328 -230.739 8.578 57.012 1.00169.20 C ANISOU 2599 CA LEU A 328 22208 17107 24973 -477 426 2230 C ATOM 2600 C LEU A 328 -231.910 8.654 57.987 1.00160.24 C ANISOU 2600 C LEU A 328 21218 16079 23589 -692 527 2381 C ATOM 2601 O LEU A 328 -232.181 7.705 58.724 1.00155.97 O ANISOU 2601 O LEU A 328 20825 15319 23117 -752 589 2663 O ATOM 2602 CB LEU A 328 -230.604 7.157 56.457 1.00161.98 C ANISOU 2602 CB LEU A 328 21308 15742 24495 -431 536 2237 C ATOM 2603 CG LEU A 328 -231.791 6.624 55.652 1.00153.00 C ANISOU 2603 CG LEU A 328 20172 14441 23521 -640 770 1979 C ATOM 2604 CD1 LEU A 328 -232.096 7.550 54.485 1.00152.24 C ANISOU 2604 CD1 LEU A 328 19918 14594 23331 -703 796 1564 C ATOM 2605 CD2 LEU A 328 -231.522 5.209 55.164 1.00142.80 C ANISOU 2605 CD2 LEU A 328 18899 12677 22683 -584 874 1979 C TER 2606 LEU A 328 HETATM 2607 C1 PLM A 401 -221.265 14.944 56.801 1.00131.64 C HETATM 2608 O2 PLM A 401 -222.021 15.601 56.082 1.00114.00 O HETATM 2609 C2 PLM A 401 -219.899 15.409 57.209 1.00120.87 C HETATM 2610 C3 PLM A 401 -219.751 16.913 57.114 1.00115.36 C HETATM 2611 C4 PLM A 401 -218.446 17.397 57.709 1.00105.68 C HETATM 2612 C5 PLM A 401 -218.474 18.896 57.925 1.00 96.39 C HETATM 2613 C6 PLM A 401 -219.511 19.275 58.961 1.00 85.20 C HETATM 2614 C7 PLM A 401 -219.261 20.658 59.527 1.00 76.47 C HETATM 2615 C8 PLM A 401 -219.584 21.744 58.523 1.00 77.94 C HETATM 2616 C9 PLM A 401 -219.379 23.119 59.127 1.00 78.30 C HETATM 2617 CA PLM A 401 -219.908 24.208 58.217 1.00 80.29 C HETATM 2618 CB PLM A 401 -219.998 25.535 58.941 1.00 78.02 C HETATM 2619 CC PLM A 401 -218.796 26.409 58.650 1.00 75.37 C HETATM 2620 CD PLM A 401 -218.940 27.768 59.301 1.00 80.40 C HETATM 2621 CE PLM A 401 -217.916 28.751 58.775 1.00 75.32 C HETATM 2622 CF PLM A 401 -218.418 30.174 58.905 1.00 73.32 C HETATM 2623 CG PLM A 401 -217.475 31.163 58.270 1.00 67.19 C HETATM 2624 C1 NAG A 402 -216.206 69.908 41.057 1.00 76.71 C HETATM 2625 C2 NAG A 402 -215.713 69.425 39.740 1.00 71.83 C HETATM 2626 C3 NAG A 402 -214.217 69.680 39.618 1.00 73.85 C HETATM 2627 C4 NAG A 402 -213.736 70.929 40.364 1.00 89.28 C HETATM 2628 C5 NAG A 402 -214.735 71.657 41.287 1.00 85.02 C HETATM 2629 C6 NAG A 402 -214.726 73.156 41.084 1.00 67.89 C HETATM 2630 C7 NAG A 402 -216.374 67.473 38.400 1.00 67.20 C HETATM 2631 C8 NAG A 402 -216.649 66.000 38.414 1.00 76.14 C HETATM 2632 N2 NAG A 402 -216.009 68.011 39.569 1.00 68.70 N HETATM 2633 O3 NAG A 402 -213.914 69.841 38.237 1.00 61.06 O HETATM 2634 O4 NAG A 402 -212.592 70.592 41.143 1.00103.50 O HETATM 2635 O5 NAG A 402 -216.092 71.237 41.108 1.00 75.06 O HETATM 2636 O6 NAG A 402 -215.445 73.531 39.916 1.00 62.32 O HETATM 2637 O7 NAG A 402 -216.470 68.143 37.377 1.00 67.59 O HETATM 2638 C1 NAG A 403 -211.657 73.196 39.120 1.00 77.31 C HETATM 2639 C2 NAG A 403 -210.472 72.712 39.916 1.00 52.84 C HETATM 2640 C3 NAG A 403 -209.207 72.898 39.093 1.00 59.52 C HETATM 2641 C4 NAG A 403 -209.345 72.154 37.769 1.00 73.97 C HETATM 2642 C5 NAG A 403 -210.651 72.516 37.052 1.00 48.43 C HETATM 2643 C6 NAG A 403 -210.946 71.597 35.890 1.00 54.80 C HETATM 2644 C7 NAG A 403 -210.638 72.762 42.358 1.00 77.27 C HETATM 2645 C8 NAG A 403 -210.500 73.590 43.601 1.00 94.10 C HETATM 2646 N2 NAG A 403 -210.373 73.383 41.203 1.00 67.65 N HETATM 2647 O3 NAG A 403 -208.084 72.412 39.818 1.00 93.52 O HETATM 2648 O4 NAG A 403 -208.253 72.459 36.909 1.00 99.96 O HETATM 2649 O5 NAG A 403 -211.779 72.421 37.940 1.00 56.43 O HETATM 2650 O6 NAG A 403 -211.387 72.319 34.748 1.00 77.06 O HETATM 2651 O7 NAG A 403 -210.968 71.580 42.398 1.00 74.48 O HETATM 2652 C1 BMA A 404 -206.953 75.334 37.410 1.00133.02 C HETATM 2653 C2 BMA A 404 -206.047 74.351 38.157 1.00127.06 C HETATM 2654 C3 BMA A 404 -204.853 75.079 38.768 1.00146.35 C HETATM 2655 C4 BMA A 404 -204.641 76.506 38.187 1.00159.84 C HETATM 2656 C5 BMA A 404 -204.985 76.586 36.661 1.00149.71 C HETATM 2657 C6 BMA A 404 -203.912 75.963 35.786 1.00133.01 C HETATM 2658 O2 BMA A 404 -205.514 73.381 37.270 1.00113.61 O HETATM 2659 O3 BMA A 404 -203.655 74.306 38.643 1.00144.99 O HETATM 2660 O4 BMA A 404 -205.385 77.477 38.932 1.00163.27 O HETATM 2661 O5 BMA A 404 -206.273 75.961 36.341 1.00143.64 O HETATM 2662 O6 BMA A 404 -204.352 74.669 35.385 1.00114.80 O HETATM 2663 C1 MAN A 405 -205.458 75.041 32.219 1.00112.42 C HETATM 2664 C2 MAN A 405 -204.254 76.008 32.259 1.00109.04 C HETATM 2665 C3 MAN A 405 -204.718 77.414 32.655 1.00118.09 C HETATM 2666 C4 MAN A 405 -206.195 77.629 32.318 1.00114.77 C HETATM 2667 C5 MAN A 405 -207.047 76.664 33.168 1.00120.40 C HETATM 2668 C6 MAN A 405 -208.485 76.521 32.681 1.00108.62 C HETATM 2669 O2 MAN A 405 -203.623 76.144 30.981 1.00109.30 O HETATM 2670 O3 MAN A 405 -203.922 78.429 32.058 1.00122.85 O HETATM 2671 O4 MAN A 405 -206.558 78.969 32.607 1.00100.46 O HETATM 2672 O5 MAN A 405 -206.439 75.330 33.200 1.00122.31 O HETATM 2673 O6 MAN A 405 -209.227 75.809 33.671 1.00 88.50 O HETATM 2674 C1 MAN A 406 -204.190 74.281 42.607 1.00143.39 C HETATM 2675 C2 MAN A 406 -205.240 75.394 42.310 1.00143.72 C HETATM 2676 C3 MAN A 406 -204.566 76.753 42.040 1.00146.97 C HETATM 2677 C4 MAN A 406 -203.057 76.707 42.306 1.00146.04 C HETATM 2678 C5 MAN A 406 -202.466 75.615 41.419 1.00135.83 C HETATM 2679 C6 MAN A 406 -200.946 75.525 41.486 1.00114.86 C HETATM 2680 O2 MAN A 406 -206.137 75.610 43.414 1.00140.32 O HETATM 2681 O3 MAN A 406 -205.177 77.807 42.776 1.00144.66 O HETATM 2682 O4 MAN A 406 -202.473 77.953 41.962 1.00144.80 O HETATM 2683 O5 MAN A 406 -203.020 74.309 41.786 1.00140.26 O HETATM 2684 O6 MAN A 406 -200.502 74.759 40.369 1.00101.51 O HETATM 2685 C1 BOG A 407 -205.575 53.177 49.336 1.00121.16 C HETATM 2686 O1 BOG A 407 -205.713 51.937 48.647 1.00116.30 O HETATM 2687 C2 BOG A 407 -204.506 54.031 48.662 1.00122.85 C HETATM 2688 O2 BOG A 407 -203.231 53.381 48.748 1.00124.79 O HETATM 2689 C3 BOG A 407 -204.434 55.407 49.310 1.00126.27 C HETATM 2690 O3 BOG A 407 -203.521 56.230 48.576 1.00130.48 O HETATM 2691 C4 BOG A 407 -205.814 56.052 49.314 1.00127.98 C HETATM 2692 O4 BOG A 407 -205.754 57.290 50.034 1.00127.10 O HETATM 2693 C5 BOG A 407 -206.843 55.124 49.957 1.00127.74 C HETATM 2694 O5 BOG A 407 -206.841 53.840 49.328 1.00127.75 O HETATM 2695 C6 BOG A 407 -208.260 55.695 49.894 1.00119.47 C HETATM 2696 O6 BOG A 407 -208.894 55.315 48.665 1.00110.09 O HETATM 2697 C1' BOG A 407 -206.599 51.055 49.334 1.00102.23 C HETATM 2698 C2' BOG A 407 -206.710 49.753 48.551 1.00 91.49 C HETATM 2699 C3' BOG A 407 -207.521 48.710 49.310 1.00 88.24 C HETATM 2700 C4' BOG A 407 -207.699 47.448 48.474 1.00 89.33 C HETATM 2701 C5' BOG A 407 -208.365 46.346 49.288 1.00 85.85 C HETATM 2702 C6' BOG A 407 -208.605 45.109 48.432 1.00 80.43 C HETATM 2703 C7' BOG A 407 -209.234 43.985 49.246 1.00 85.15 C HETATM 2704 C8' BOG A 407 -209.531 42.794 48.361 1.00 90.77 C HETATM 2705 C1 BOG A 408 -229.235 44.692 38.302 1.00119.49 C HETATM 2706 O1 BOG A 408 -229.921 43.666 39.015 1.00120.03 O HETATM 2707 C2 BOG A 408 -229.677 46.062 38.799 1.00118.28 C HETATM 2708 O2 BOG A 408 -231.085 46.222 38.595 1.00120.80 O HETATM 2709 C3 BOG A 408 -228.936 47.164 38.060 1.00108.69 C HETATM 2710 O3 BOG A 408 -229.216 48.420 38.689 1.00 97.15 O HETATM 2711 C4 BOG A 408 -227.432 46.923 38.077 1.00115.67 C HETATM 2712 O4 BOG A 408 -226.835 47.793 37.111 1.00122.28 O HETATM 2713 C5 BOG A 408 -227.062 45.485 37.723 1.00110.21 C HETATM 2714 O5 BOG A 408 -227.825 44.540 38.475 1.00115.41 O HETATM 2715 C6 BOG A 408 -225.578 45.245 37.976 1.00102.10 C HETATM 2716 O6 BOG A 408 -225.281 45.527 39.349 1.00103.69 O HETATM 2717 C1' BOG A 408 -230.014 42.466 38.250 1.00113.91 C HETATM 2718 C2' BOG A 408 -230.541 41.350 39.141 1.00106.36 C HETATM 2719 C3' BOG A 408 -231.593 40.513 38.424 1.00102.11 C HETATM 2720 C4' BOG A 408 -232.021 39.351 39.310 1.00103.97 C HETATM 2721 C5' BOG A 408 -233.297 38.690 38.805 1.00100.02 C HETATM 2722 C6' BOG A 408 -233.691 37.542 39.727 1.00 94.59 C HETATM 2723 C7' BOG A 408 -235.127 37.699 40.213 1.00 95.95 C HETATM 2724 C8' BOG A 408 -235.416 36.774 41.375 1.00 97.80 C HETATM 2725 C1 BOG A 409 -225.162 50.719 45.737 1.00115.11 C HETATM 2726 O1 BOG A 409 -226.278 51.575 45.960 1.00 90.98 O HETATM 2727 C2 BOG A 409 -225.532 49.652 44.710 1.00122.69 C HETATM 2728 O2 BOG A 409 -226.639 48.866 45.176 1.00123.11 O HETATM 2729 C3 BOG A 409 -224.340 48.751 44.426 1.00115.26 C HETATM 2730 O3 BOG A 409 -224.624 47.965 43.265 1.00110.19 O HETATM 2731 C4 BOG A 409 -223.096 49.567 44.120 1.00113.33 C HETATM 2732 C5 BOG A 409 -222.862 50.724 45.082 1.00116.39 C HETATM 2733 O5 BOG A 409 -224.051 51.491 45.277 1.00118.68 O HETATM 2734 C6 BOG A 409 -221.771 51.627 44.518 1.00114.21 C HETATM 2735 O6 BOG A 409 -221.174 50.990 43.381 1.00114.82 O HETATM 2736 C1' BOG A 409 -226.001 52.539 46.969 1.00 80.39 C HETATM 2737 C2' BOG A 409 -227.269 52.732 47.784 1.00 82.04 C HETATM 2738 C3' BOG A 409 -227.692 51.434 48.459 1.00 91.49 C HETATM 2739 C4' BOG A 409 -228.693 51.758 49.560 1.00101.07 C HETATM 2740 C5' BOG A 409 -228.990 50.577 50.474 1.00 99.35 C HETATM 2741 C6' BOG A 409 -229.665 51.057 51.754 1.00 83.29 C HETATM 2742 C7' BOG A 409 -229.777 49.925 52.768 1.00 78.58 C HETATM 2743 C8' BOG A 409 -230.097 50.452 54.150 1.00 72.69 C HETATM 2744 C1 BOG A 410 -254.341 27.332 47.692 1.00119.95 C HETATM 2745 O1 BOG A 410 -253.290 28.247 47.384 1.00114.80 O HETATM 2746 C2 BOG A 410 -254.125 26.763 49.099 1.00114.20 C HETATM 2747 O2 BOG A 410 -253.144 25.718 49.029 1.00110.23 O HETATM 2748 C3 BOG A 410 -255.385 26.192 49.746 1.00118.50 C HETATM 2749 O3 BOG A 410 -255.153 26.070 51.157 1.00110.24 O HETATM 2750 C4 BOG A 410 -256.604 27.068 49.468 1.00131.26 C HETATM 2751 O4 BOG A 410 -257.796 26.445 49.965 1.00131.11 O HETATM 2752 C5 BOG A 410 -256.725 27.300 47.966 1.00134.85 C HETATM 2753 O5 BOG A 410 -255.580 28.026 47.531 1.00129.24 O HETATM 2754 C6 BOG A 410 -257.979 28.088 47.590 1.00131.65 C HETATM 2755 O6 BOG A 410 -257.945 28.455 46.203 1.00126.95 O HETATM 2756 C1' BOG A 410 -253.518 28.910 46.140 1.00 99.71 C HETATM 2757 C2' BOG A 410 -252.296 29.745 45.782 1.00 83.25 C HETATM 2758 C3' BOG A 410 -252.217 29.974 44.280 1.00 65.44 C HETATM 2759 C4' BOG A 410 -250.792 30.332 43.890 1.00 66.33 C HETATM 2760 C5' BOG A 410 -250.744 30.802 42.445 1.00 73.80 C HETATM 2761 C6' BOG A 410 -249.368 31.358 42.113 1.00 73.56 C HETATM 2762 C7' BOG A 410 -249.496 32.390 41.004 1.00 73.21 C HETATM 2763 C8' BOG A 410 -248.516 32.104 39.891 1.00 77.15 C HETATM 2764 C1 BOG A 411 -203.155 46.221 48.457 1.00126.01 C HETATM 2765 O1 BOG A 411 -202.956 44.867 48.044 1.00118.98 O HETATM 2766 C2 BOG A 411 -202.041 46.637 49.418 1.00128.69 C HETATM 2767 O2 BOG A 411 -202.056 45.802 50.585 1.00133.07 O HETATM 2768 C3 BOG A 411 -202.192 48.106 49.802 1.00124.97 C HETATM 2769 O3 BOG A 411 -201.100 48.525 50.630 1.00124.39 O HETATM 2770 C4 BOG A 411 -202.236 48.953 48.537 1.00123.44 C HETATM 2771 O4 BOG A 411 -202.471 50.324 48.875 1.00118.99 O HETATM 2772 C5 BOG A 411 -203.350 48.472 47.615 1.00128.86 C HETATM 2773 O5 BOG A 411 -203.185 47.081 47.311 1.00128.33 O HETATM 2774 C6 BOG A 411 -203.383 49.282 46.319 1.00127.80 C HETATM 2775 O6 BOG A 411 -203.708 50.654 46.585 1.00127.74 O HETATM 2776 C1' BOG A 411 -203.889 44.463 47.041 1.00107.88 C HETATM 2777 C2' BOG A 411 -203.870 42.944 46.906 1.00103.05 C HETATM 2778 C3' BOG A 411 -205.164 42.358 47.455 1.00 96.06 C HETATM 2779 C4' BOG A 411 -204.960 40.955 48.010 1.00 91.52 C HETATM 2780 C5' BOG A 411 -205.943 40.716 49.148 1.00 90.99 C HETATM 2781 C6' BOG A 411 -206.205 39.232 49.361 1.00 91.63 C HETATM 2782 C7' BOG A 411 -207.341 39.045 50.359 1.00 91.41 C HETATM 2783 C8' BOG A 411 -207.783 37.600 50.422 1.00 88.12 C HETATM 2784 C10 DLH A 412 -233.947 47.313 36.380 1.00134.68 C HETATM 2785 C11 DLH A 412 -235.738 45.768 35.591 1.00131.45 C HETATM 2786 C15 DLH A 412 -235.977 41.938 38.307 1.00109.20 C HETATM 2787 C17 DLH A 412 -235.511 42.344 36.017 1.00113.51 C HETATM 2788 C18 DLH A 412 -234.010 43.162 37.729 1.00113.20 C HETATM 2789 C19 DLH A 412 -236.337 41.791 36.981 1.00108.32 C HETATM 2790 C20 DLH A 412 -234.832 42.611 38.708 1.00109.66 C HETATM 2791 C21 DLH A 412 -237.763 50.239 37.409 1.00131.53 C HETATM 2792 C22 DLH A 412 -237.692 51.257 34.720 1.00125.55 C HETATM 2793 C23 DLH A 412 -238.378 51.919 35.746 1.00126.16 C HETATM 2794 C24 DLH A 412 -238.406 51.427 37.039 1.00130.39 C HETATM 2795 C1 DLH A 412 -235.876 48.206 35.160 1.00131.86 C HETATM 2796 C12 DLH A 412 -233.508 43.601 35.299 1.00125.98 C HETATM 2797 C14 DLH A 412 -234.354 43.022 36.388 1.00118.35 C HETATM 2798 C3 DLH A 412 -233.272 45.102 35.471 1.00134.23 C HETATM 2799 C6 DLH A 412 -237.060 50.098 35.083 1.00127.92 C HETATM 2800 C7 DLH A 412 -237.096 49.601 36.401 1.00128.22 C HETATM 2801 C8 DLH A 412 -234.370 48.303 35.290 1.00132.79 C HETATM 2802 C9 DLH A 412 -236.270 46.837 34.624 1.00133.71 C HETATM 2803 N2 DLH A 412 -234.306 45.932 36.002 1.00134.56 N HETATM 2804 O13 DLH A 412 -232.196 45.597 35.156 1.00140.37 O HETATM 2805 O4 DLH A 412 -236.392 48.435 36.468 1.00126.67 O HETATM 2806 O5 DLH A 412 -236.325 49.250 34.299 1.00130.57 O HETATM 2807 CL DLH A 412 -237.002 41.251 39.508 1.00107.39 CL HETATM 2808 O HOH A1000 -227.063 46.674 34.783 1.00 65.97 O HETATM 2809 O HOH A1001 -230.086 46.687 35.056 1.00 62.48 O CONECT 1 2 3 4 CONECT 2 1 CONECT 3 1 CONECT 4 1 CONECT 17 2244 CONECT 884 1474 CONECT 1474 884 CONECT 2244 17 CONECT 2563 2607 CONECT 2607 2563 2608 2609 CONECT 2608 2607 CONECT 2609 2607 2610 CONECT 2610 2609 2611 CONECT 2611 2610 2612 CONECT 2612 2611 2613 CONECT 2613 2612 2614 CONECT 2614 2613 2615 CONECT 2615 2614 2616 CONECT 2616 2615 2617 CONECT 2617 2616 2618 CONECT 2618 2617 2619 CONECT 2619 2618 2620 CONECT 2620 2619 2621 CONECT 2621 2620 2622 CONECT 2622 2621 2623 CONECT 2623 2622 CONECT 2624 2625 2635 CONECT 2625 2624 2626 2632 CONECT 2626 2625 2627 2633 CONECT 2627 2626 2628 2634 CONECT 2628 2627 2629 2635 CONECT 2629 2628 2636 CONECT 2630 2631 2632 2637 CONECT 2631 2630 CONECT 2632 2625 2630 CONECT 2633 2626 CONECT 2634 2627 CONECT 2635 2624 2628 CONECT 2636 2629 CONECT 2637 2630 CONECT 2638 2639 2649 CONECT 2639 2638 2640 2646 CONECT 2640 2639 2641 2647 CONECT 2641 2640 2642 2648 CONECT 2642 2641 2643 2649 CONECT 2643 2642 2650 CONECT 2644 2645 2646 2651 CONECT 2645 2644 CONECT 2646 2639 2644 CONECT 2647 2640 CONECT 2648 2641 CONECT 2649 2638 2642 CONECT 2650 2643 CONECT 2651 2644 CONECT 2652 2653 2661 CONECT 2653 2652 2654 2658 CONECT 2654 2653 2655 2659 CONECT 2655 2654 2656 2660 CONECT 2656 2655 2657 2661 CONECT 2657 2656 2662 CONECT 2658 2653 CONECT 2659 2654 CONECT 2660 2655 CONECT 2661 2652 2656 CONECT 2662 2657 CONECT 2663 2664 2672 CONECT 2664 2663 2665 2669 CONECT 2665 2664 2666 2670 CONECT 2666 2665 2667 2671 CONECT 2667 2666 2668 2672 CONECT 2668 2667 2673 CONECT 2669 2664 CONECT 2670 2665 CONECT 2671 2666 CONECT 2672 2663 2667 CONECT 2673 2668 CONECT 2674 2675 2683 CONECT 2675 2674 2676 2680 CONECT 2676 2675 2677 2681 CONECT 2677 2676 2678 2682 CONECT 2678 2677 2679 2683 CONECT 2679 2678 2684 CONECT 2680 2675 CONECT 2681 2676 CONECT 2682 2677 CONECT 2683 2674 2678 CONECT 2684 2679 CONECT 2685 2686 2687 2694 CONECT 2686 2685 2697 CONECT 2687 2685 2688 2689 CONECT 2688 2687 CONECT 2689 2687 2690 2691 CONECT 2690 2689 CONECT 2691 2689 2692 2693 CONECT 2692 2691 CONECT 2693 2691 2694 2695 CONECT 2694 2685 2693 CONECT 2695 2693 2696 CONECT 2696 2695 CONECT 2697 2686 2698 CONECT 2698 2697 2699 CONECT 2699 2698 2700 CONECT 2700 2699 2701 CONECT 2701 2700 2702 CONECT 2702 2701 2703 CONECT 2703 2702 2704 CONECT 2704 2703 CONECT 2705 2706 2707 2714 CONECT 2706 2705 2717 CONECT 2707 2705 2708 2709 CONECT 2708 2707 CONECT 2709 2707 2710 2711 CONECT 2710 2709 CONECT 2711 2709 2712 2713 CONECT 2712 2711 CONECT 2713 2711 2714 2715 CONECT 2714 2705 2713 CONECT 2715 2713 2716 CONECT 2716 2715 CONECT 2717 2706 2718 CONECT 2718 2717 2719 CONECT 2719 2718 2720 CONECT 2720 2719 2721 CONECT 2721 2720 2722 CONECT 2722 2721 2723 CONECT 2723 2722 2724 CONECT 2724 2723 CONECT 2725 2726 2727 2733 CONECT 2726 2725 2736 CONECT 2727 2725 2728 2729 CONECT 2728 2727 CONECT 2729 2727 2730 2731 CONECT 2730 2729 CONECT 2731 2729 2732 CONECT 2732 2731 2733 2734 CONECT 2733 2725 2732 CONECT 2734 2732 2735 CONECT 2735 2734 CONECT 2736 2726 2737 CONECT 2737 2736 2738 CONECT 2738 2737 2739 CONECT 2739 2738 2740 CONECT 2740 2739 2741 CONECT 2741 2740 2742 CONECT 2742 2741 2743 CONECT 2743 2742 CONECT 2744 2745 2746 2753 CONECT 2745 2744 2756 CONECT 2746 2744 2747 2748 CONECT 2747 2746 CONECT 2748 2746 2749 2750 CONECT 2749 2748 CONECT 2750 2748 2751 2752 CONECT 2751 2750 CONECT 2752 2750 2753 2754 CONECT 2753 2744 2752 CONECT 2754 2752 2755 CONECT 2755 2754 CONECT 2756 2745 2757 CONECT 2757 2756 2758 CONECT 2758 2757 2759 CONECT 2759 2758 2760 CONECT 2760 2759 2761 CONECT 2761 2760 2762 CONECT 2762 2761 2763 CONECT 2763 2762 CONECT 2764 2765 2766 2773 CONECT 2765 2764 2776 CONECT 2766 2764 2767 2768 CONECT 2767 2766 CONECT 2768 2766 2769 2770 CONECT 2769 2768 CONECT 2770 2768 2771 2772 CONECT 2771 2770 CONECT 2772 2770 2773 2774 CONECT 2773 2764 2772 CONECT 2774 2772 2775 CONECT 2775 2774 CONECT 2776 2765 2777 CONECT 2777 2776 2778 CONECT 2778 2777 2779 CONECT 2779 2778 2780 CONECT 2780 2779 2781 CONECT 2781 2780 2782 CONECT 2782 2781 2783 CONECT 2783 2782 CONECT 2784 2801 2803 CONECT 2785 2802 2803 CONECT 2786 2789 2790 2807 CONECT 2787 2789 2797 CONECT 2788 2790 2797 CONECT 2789 2786 2787 CONECT 2790 2786 2788 CONECT 2791 2794 2800 CONECT 2792 2793 2799 CONECT 2793 2792 2794 CONECT 2794 2791 2793 CONECT 2795 2801 2802 2805 2806 CONECT 2796 2797 2798 CONECT 2797 2787 2788 2796 CONECT 2798 2796 2803 2804 CONECT 2799 2792 2800 2806 CONECT 2800 2791 2799 2805 CONECT 2801 2784 2795 CONECT 2802 2785 2795 CONECT 2803 2784 2785 2798 CONECT 2804 2798 CONECT 2805 2795 2800 CONECT 2806 2795 2799 CONECT 2807 2786 MASTER 333 0 13 16 4 0 0 6 2808 1 210 26 END