HEADER MEMBRANE PROTEIN 23-JAN-18 6FK6 TITLE CRYSTAL STRUCTURE OF N2C/D282C STABILIZED OPSIN BOUND TO RS01 COMPND MOL_ID: 1; COMPND 2 MOLECULE: RHODOPSIN; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: 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_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293S GNTI-; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID 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 6FK6 1 COMPND REMARK HETNAM LINK REVDAT 3 2 1 SITE ATOM REVDAT 2 11-APR-18 6FK6 1 JRNL REVDAT 1 04-APR-18 6FK6 0 JRNL AUTH D.MATTLE,B.KUHN,J.AEBI,M.BEDOUCHA,D.KEKILLI,N.GROZINGER, JRNL AUTH 2 A.ALKER,M.G.RUDOLPH,G.SCHMID,G.F.X.SCHERTLER,M.HENNIG, JRNL AUTH 3 J.STANDFUSS,R.J.P.DAWSON JRNL TITL LIGAND CHANNEL IN PHARMACOLOGICALLY STABILIZED RHODOPSIN. JRNL REF PROC. NATL. ACAD. SCI. V. 115 3640 2018 JRNL REF 2 U.S.A. JRNL REFN ESSN 1091-6490 JRNL PMID 29555765 JRNL DOI 10.1073/PNAS.1718084115 REMARK 2 REMARK 2 RESOLUTION. 2.36 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.10_2155 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.36 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.79 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.330 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 3 NUMBER OF REFLECTIONS : 52046 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.216 REMARK 3 R VALUE (WORKING SET) : 0.216 REMARK 3 FREE R VALUE : 0.226 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.120 REMARK 3 FREE R VALUE TEST SET COUNT : 2664 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 47.8032 - 6.2930 1.00 2678 170 0.2154 0.2011 REMARK 3 2 6.2930 - 4.9967 1.00 2637 137 0.2011 0.2352 REMARK 3 3 4.9967 - 4.3655 1.00 2628 146 0.1789 0.1823 REMARK 3 4 4.3655 - 3.9666 1.00 2625 141 0.1783 0.2142 REMARK 3 5 3.9666 - 3.6824 1.00 2607 147 0.1901 0.1908 REMARK 3 6 3.6824 - 3.4654 1.00 2583 147 0.1919 0.2101 REMARK 3 7 3.4654 - 3.2919 1.00 2611 140 0.2070 0.2206 REMARK 3 8 3.2919 - 3.1486 1.00 2622 134 0.2181 0.2156 REMARK 3 9 3.1486 - 3.0274 1.00 2611 114 0.2264 0.2245 REMARK 3 10 3.0274 - 2.9230 1.00 2609 135 0.2336 0.2508 REMARK 3 11 2.9230 - 2.8316 1.00 2599 141 0.2464 0.2607 REMARK 3 12 2.8316 - 2.7506 1.00 2551 150 0.2667 0.3361 REMARK 3 13 2.7506 - 2.6782 1.00 2591 135 0.2990 0.3168 REMARK 3 14 2.6782 - 2.6129 1.00 2606 124 0.2980 0.3144 REMARK 3 15 2.6129 - 2.5535 1.00 2574 150 0.3228 0.3138 REMARK 3 16 2.5535 - 2.4992 0.99 2583 132 0.3336 0.3853 REMARK 3 17 2.4992 - 2.4492 0.99 2562 140 0.3734 0.3792 REMARK 3 18 2.4492 - 2.4030 0.99 2553 148 0.4026 0.4458 REMARK 3 19 2.4030 - 2.3600 0.98 2552 133 0.4100 0.4190 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) : 0.340 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.410 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 64.38 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 86.27 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 2882 REMARK 3 ANGLE : 0.772 3927 REMARK 3 CHIRALITY : 0.042 454 REMARK 3 PLANARITY : 0.005 461 REMARK 3 DIHEDRAL : 15.055 1686 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):-108.2461-171.1727 148.6078 REMARK 3 T TENSOR REMARK 3 T11: 0.5077 T22: 0.4183 REMARK 3 T33: 0.5142 T12: 0.0225 REMARK 3 T13: -0.0617 T23: 0.0682 REMARK 3 L TENSOR REMARK 3 L11: 2.2997 L22: 4.2627 REMARK 3 L33: 1.4077 L12: 1.4596 REMARK 3 L13: 0.1496 L23: 0.0507 REMARK 3 S TENSOR REMARK 3 S11: -0.1483 S12: 0.2565 S13: 0.0934 REMARK 3 S21: -0.4819 S22: 0.1850 S23: -0.0735 REMARK 3 S31: -0.0291 S32: -0.0506 S33: -0.0425 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 326 ) REMARK 3 ORIGIN FOR THE GROUP (A):-115.2970-176.8455 158.1323 REMARK 3 T TENSOR REMARK 3 T11: 0.5501 T22: 0.4490 REMARK 3 T33: 0.6909 T12: -0.0209 REMARK 3 T13: -0.1027 T23: -0.0088 REMARK 3 L TENSOR REMARK 3 L11: 4.4633 L22: 1.5139 REMARK 3 L33: 3.2224 L12: 0.0908 REMARK 3 L13: -0.0650 L23: 0.5636 REMARK 3 S TENSOR REMARK 3 S11: -0.0254 S12: 0.2129 S13: 0.4229 REMARK 3 S21: -0.0068 S22: -0.0308 S23: 0.3480 REMARK 3 S31: -0.2584 S32: -0.1557 S33: 0.0320 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 6FK6 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_1200008386. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 21-NOV-15 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 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) : 1.000020 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 52217 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.360 REMARK 200 RESOLUTION RANGE LOW (A) : 47.790 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 200 DATA REDUNDANCY : 11.43 REMARK 200 R MERGE (I) : 0.11400 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 15.3900 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.36 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 5.37000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 0.550 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: INHOUSE MODEL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULPHATE, SODIUM ACETATE, REMARK 280 D(+)-TREHALOSE, PH 6.0, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z REMARK 290 3555 -X+Y,-X,Z REMARK 290 4555 Y,X,-Z REMARK 290 5555 X-Y,-Y,-Z REMARK 290 6555 -X,-X+Y,-Z REMARK 290 7555 X+2/3,Y+1/3,Z+1/3 REMARK 290 8555 -Y+2/3,X-Y+1/3,Z+1/3 REMARK 290 9555 -X+Y+2/3,-X+1/3,Z+1/3 REMARK 290 10555 Y+2/3,X+1/3,-Z+1/3 REMARK 290 11555 X-Y+2/3,-Y+1/3,-Z+1/3 REMARK 290 12555 -X+2/3,-X+Y+1/3,-Z+1/3 REMARK 290 13555 X+1/3,Y+2/3,Z+2/3 REMARK 290 14555 -Y+1/3,X-Y+2/3,Z+2/3 REMARK 290 15555 -X+Y+1/3,-X+2/3,Z+2/3 REMARK 290 16555 Y+1/3,X+2/3,-Z+2/3 REMARK 290 17555 X-Y+1/3,-Y+2/3,-Z+2/3 REMARK 290 18555 -X+1/3,-X+Y+2/3,-Z+2/3 REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 7 1.000000 0.000000 0.000000 122.10450 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 70.49707 REMARK 290 SMTRY3 7 0.000000 0.000000 1.000000 37.25067 REMARK 290 SMTRY1 8 -0.500000 -0.866025 0.000000 122.10450 REMARK 290 SMTRY2 8 0.866025 -0.500000 0.000000 70.49707 REMARK 290 SMTRY3 8 0.000000 0.000000 1.000000 37.25067 REMARK 290 SMTRY1 9 -0.500000 0.866025 0.000000 122.10450 REMARK 290 SMTRY2 9 -0.866025 -0.500000 0.000000 70.49707 REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 37.25067 REMARK 290 SMTRY1 10 -0.500000 0.866025 0.000000 122.10450 REMARK 290 SMTRY2 10 0.866025 0.500000 0.000000 70.49707 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 37.25067 REMARK 290 SMTRY1 11 1.000000 0.000000 0.000000 122.10450 REMARK 290 SMTRY2 11 0.000000 -1.000000 0.000000 70.49707 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 37.25067 REMARK 290 SMTRY1 12 -0.500000 -0.866025 0.000000 122.10450 REMARK 290 SMTRY2 12 -0.866025 0.500000 0.000000 70.49707 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 37.25067 REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 140.99413 REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 74.50133 REMARK 290 SMTRY1 14 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 14 0.866025 -0.500000 0.000000 140.99413 REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 74.50133 REMARK 290 SMTRY1 15 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 15 -0.866025 -0.500000 0.000000 140.99413 REMARK 290 SMTRY3 15 0.000000 0.000000 1.000000 74.50133 REMARK 290 SMTRY1 16 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 16 0.866025 0.500000 0.000000 140.99413 REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 74.50133 REMARK 290 SMTRY1 17 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 17 0.000000 -1.000000 0.000000 140.99413 REMARK 290 SMTRY3 17 0.000000 0.000000 -1.000000 74.50133 REMARK 290 SMTRY1 18 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 18 -0.866025 0.500000 0.000000 140.99413 REMARK 290 SMTRY3 18 0.000000 0.000000 -1.000000 74.50133 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: 3370 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 375 REMARK 375 SPECIAL POSITION REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL REMARK 375 POSITIONS. REMARK 375 REMARK 375 ATOM RES CSSEQI REMARK 375 HOH A 517 LIES ON A SPECIAL POSITION. REMARK 375 HOH A 579 LIES ON A SPECIAL POSITION. REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O PHE A 88 O HOH A 501 2.08 REMARK 500 O MET A 163 O HOH A 502 2.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 GLN A 28 49.61 -92.98 REMARK 500 ASN A 145 43.77 -107.73 REMARK 500 SER A 176 -162.08 60.77 REMARK 500 PRO A 194 51.51 -94.58 REMARK 500 HIS A 195 102.38 -51.40 REMARK 500 PHE A 212 -52.44 -142.87 REMARK 500 GLN A 237 52.62 -140.75 REMARK 500 PHE A 287 -70.12 -57.49 REMARK 500 ILE A 307 -59.52 -124.12 REMARK 500 REMARK 500 REMARK: NULL DBREF 6FK6 A 1 326 UNP P02699 OPSD_BOVIN 1 326 SEQADV 6FK6 ACE A 0 UNP P02699 ACETYLATION SEQADV 6FK6 CYS A 2 UNP P02699 ASN 2 CONFLICT SEQADV 6FK6 CYS A 282 UNP P02699 ASP 282 CONFLICT SEQRES 1 A 327 ACE MET CYS GLY THR GLU GLY PRO ASN PHE TYR VAL PRO SEQRES 2 A 327 PHE SER ASN LYS THR GLY VAL VAL ARG SER PRO PHE GLU SEQRES 3 A 327 ALA PRO GLN TYR TYR LEU ALA GLU PRO TRP GLN PHE SER SEQRES 4 A 327 MET LEU ALA ALA TYR MET PHE LEU LEU ILE MET LEU GLY SEQRES 5 A 327 PHE PRO ILE ASN PHE LEU THR LEU TYR VAL THR VAL GLN SEQRES 6 A 327 HIS LYS LYS LEU ARG THR PRO LEU ASN TYR ILE LEU LEU SEQRES 7 A 327 ASN LEU ALA VAL ALA ASP LEU PHE MET VAL PHE GLY GLY SEQRES 8 A 327 PHE THR THR THR LEU TYR THR SER LEU HIS GLY TYR PHE SEQRES 9 A 327 VAL PHE GLY PRO THR GLY CYS ASN LEU GLU GLY PHE PHE SEQRES 10 A 327 ALA THR LEU GLY GLY GLU ILE ALA LEU TRP SER LEU VAL SEQRES 11 A 327 VAL LEU ALA ILE GLU ARG TYR VAL VAL VAL CYS LYS PRO SEQRES 12 A 327 MET SER ASN PHE ARG PHE GLY GLU ASN HIS ALA ILE MET SEQRES 13 A 327 GLY VAL ALA PHE THR TRP VAL MET ALA LEU ALA CYS ALA SEQRES 14 A 327 ALA PRO PRO LEU VAL GLY TRP SER ARG TYR ILE PRO GLU SEQRES 15 A 327 GLY MET GLN CYS SER CYS GLY ILE ASP TYR TYR THR PRO SEQRES 16 A 327 HIS GLU GLU THR ASN ASN GLU SER PHE VAL ILE TYR MET SEQRES 17 A 327 PHE VAL VAL HIS PHE ILE ILE PRO LEU ILE VAL ILE PHE SEQRES 18 A 327 PHE CYS TYR GLY GLN LEU VAL PHE THR VAL LYS GLU ALA SEQRES 19 A 327 ALA ALA GLN GLN GLN GLU SER ALA THR THR GLN LYS ALA SEQRES 20 A 327 GLU LYS GLU VAL THR ARG MET VAL ILE ILE MET VAL ILE SEQRES 21 A 327 ALA PHE LEU ILE CYS TRP LEU PRO TYR ALA GLY VAL ALA SEQRES 22 A 327 PHE TYR ILE PHE THR HIS GLN GLY SER CYS PHE GLY PRO SEQRES 23 A 327 ILE PHE MET THR ILE PRO ALA PHE PHE ALA LYS THR SER SEQRES 24 A 327 ALA VAL TYR ASN PRO VAL ILE TYR ILE MET MET ASN LYS SEQRES 25 A 327 GLN PHE ARG ASN CYS MET VAL THR THR LEU CYS CYS GLY SEQRES 26 A 327 LYS ASN HET ACE A 0 3 HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET MAN B 4 11 HET MAN B 5 11 HET PLM A 401 17 HET BOG A 407 20 HET BOG A 408 20 HET BOG A 409 20 HET BOG A 410 20 HET DOK A 411 27 HETNAM ACE ACETYL GROUP HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM PLM PALMITIC ACID HETNAM BOG OCTYL BETA-D-GLUCOPYRANOSIDE HETNAM DOK (2~{S})-2-(4-CHLOROPHENYL)-3-METHYL-1-SPIRO[1,3- HETNAM 2 DOK BENZODIOXOLE-2,4'-PIPERIDINE]-1'-YL-BUTAN-1-ONE FORMUL 1 ACE C2 H4 O FORMUL 2 NAG 2(C8 H15 N O6) FORMUL 2 BMA C6 H12 O6 FORMUL 2 MAN 2(C6 H12 O6) FORMUL 3 PLM C16 H32 O2 FORMUL 4 BOG 4(C14 H28 O6) FORMUL 8 DOK C22 H24 CL N O3 FORMUL 9 HOH *79(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 HIS A 278 1 39 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 CYS A 322 1 13 SHEET 1 AA1 2 THR A 4 GLY A 6 0 SHEET 2 AA1 2 PHE A 9 VAL A 11 -1 O VAL A 11 N THR A 4 SHEET 1 AA2 2 TYR A 178 GLU A 181 0 SHEET 2 AA2 2 SER A 186 ILE A 189 -1 O SER A 186 N GLU A 181 SSBOND 1 CYS A 2 CYS A 282 1555 1555 2.03 SSBOND 2 CYS A 110 CYS A 187 1555 1555 2.05 LINK C ACE A 0 N MET A 1 1555 1555 1.35 LINK ND2 ASN A 15 C1 NAG B 1 1555 1555 1.45 LINK SG CYS A 322 C1 PLM A 401 1555 1555 1.74 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.44 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45 LINK O3 BMA B 3 C1 MAN B 4 1555 1555 1.47 LINK O6 BMA B 3 C1 MAN B 5 1555 1555 1.44 CRYST1 244.209 244.209 111.752 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 0.004095 0.002364 0.000000 0.00000 SCALE2 0.000000 0.004728 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008948 0.00000 HETATM 1 C ACE A 0 -110.626-139.886 151.716 1.00 74.14 C HETATM 2 O ACE A 0 -111.712-139.773 151.143 1.00105.84 O HETATM 3 CH3 ACE A 0 -110.554-139.715 153.210 1.00 74.20 C ATOM 4 N MET A 1 -109.517-140.126 150.991 1.00107.89 N ANISOU 4 N MET A 1 14019 8885 18088 821 -1436 1532 N ATOM 5 CA MET A 1 -108.115-140.320 151.390 1.00 97.63 C ANISOU 5 CA MET A 1 12828 7736 16533 646 -1299 1415 C ATOM 6 C MET A 1 -107.962-141.355 152.497 1.00 95.00 C ANISOU 6 C MET A 1 12428 7664 16004 662 -1126 1139 C ATOM 7 O MET A 1 -107.479-141.056 153.589 1.00107.66 O ANISOU 7 O MET A 1 14044 9229 17632 636 -996 896 O ATOM 8 CB MET A 1 -107.480-138.997 151.822 1.00 99.58 C ANISOU 8 CB MET A 1 13147 7697 16993 588 -1261 1338 C ATOM 9 CG MET A 1 -107.409-137.958 150.719 1.00101.84 C ANISOU 9 CG MET A 1 13533 7719 17442 529 -1430 1631 C ATOM 10 SD MET A 1 -106.778-138.628 149.166 1.00106.55 S ANISOU 10 SD MET A 1 14271 8534 17679 339 -1540 1971 S ATOM 11 CE MET A 1 -105.167-139.235 149.662 1.00 97.63 C ANISOU 11 CE MET A 1 13188 7666 16242 141 -1336 1797 C ATOM 12 N CYS A 2 -108.393-142.577 152.198 1.00 81.42 N ANISOU 12 N CYS A 2 10653 6202 14082 694 -1142 1186 N ATOM 13 CA CYS A 2 -108.419-143.630 153.204 1.00 93.53 C ANISOU 13 CA CYS A 2 12122 7974 15442 720 -1000 954 C ATOM 14 C CYS A 2 -107.053-144.280 153.378 1.00 90.17 C ANISOU 14 C CYS A 2 11776 7766 14719 554 -930 903 C ATOM 15 O CYS A 2 -106.622-144.529 154.509 1.00100.37 O ANISOU 15 O CYS A 2 13065 9135 15936 527 -817 676 O ATOM 16 CB CYS A 2 -109.476-144.672 152.829 1.00101.94 C ANISOU 16 CB CYS A 2 13086 9204 16444 821 -1051 1025 C ATOM 17 SG CYS A 2 -111.183-144.090 153.056 1.00114.10 S ANISOU 17 SG CYS A 2 14453 10508 18391 1043 -1090 996 S ATOM 18 N GLY A 3 -106.359-144.557 152.281 1.00 77.60 N ANISOU 18 N GLY A 3 10255 6267 12963 434 -994 1109 N ATOM 19 CA GLY A 3 -105.064-145.197 152.384 1.00 80.13 C ANISOU 19 CA GLY A 3 10614 6781 13053 286 -919 1062 C ATOM 20 C GLY A 3 -103.982-144.455 151.636 1.00 75.63 C ANISOU 20 C GLY A 3 10138 6111 12489 124 -933 1203 C ATOM 21 O GLY A 3 -104.096-143.251 151.390 1.00 77.93 O ANISOU 21 O GLY A 3 10481 6146 12981 118 -990 1283 O ATOM 22 N THR A 4 -102.919-145.163 151.274 1.00 76.92 N ANISOU 22 N THR A 4 10315 6459 12452 -10 -873 1233 N ATOM 23 CA THR A 4 -101.839-144.601 150.478 1.00 67.54 C ANISOU 23 CA THR A 4 9205 5207 11252 -186 -850 1369 C ATOM 24 C THR A 4 -101.635-145.486 149.258 1.00 63.46 C ANISOU 24 C THR A 4 8736 4872 10505 -266 -826 1538 C ATOM 25 O THR A 4 -101.419-146.695 149.393 1.00 69.06 O ANISOU 25 O THR A 4 9383 5809 11048 -258 -761 1459 O ATOM 26 CB THR A 4 -100.552-144.486 151.298 1.00 78.54 C ANISOU 26 CB THR A 4 10551 6622 12670 -299 -767 1209 C ATOM 27 OG1 THR A 4 -100.781-143.615 152.413 1.00 69.31 O ANISOU 27 OG1 THR A 4 9374 5270 11691 -243 -792 1042 O ATOM 28 CG2 THR A 4 -99.433-143.915 150.444 1.00 77.21 C ANISOU 28 CG2 THR A 4 10439 6384 12513 -493 -719 1350 C ATOM 29 N GLU A 5 -101.727-144.887 148.076 1.00 71.80 N ANISOU 29 N GLU A 5 9918 5817 11547 -350 -880 1769 N ATOM 30 CA GLU A 5 -101.534-145.607 146.830 1.00 72.91 C ANISOU 30 CA GLU A 5 10152 6109 11443 -460 -846 1932 C ATOM 31 C GLU A 5 -100.074-145.568 146.409 1.00 82.71 C ANISOU 31 C GLU A 5 11422 7396 12608 -666 -684 1947 C ATOM 32 O GLU A 5 -99.338-144.622 146.707 1.00 83.64 O ANISOU 32 O GLU A 5 11536 7361 12885 -753 -650 1930 O ATOM 33 CB GLU A 5 -102.379-145.008 145.707 1.00 72.92 C ANISOU 33 CB GLU A 5 10308 5970 11431 -476 -1001 2194 C ATOM 34 CG GLU A 5 -103.872-145.041 145.921 1.00 81.41 C ANISOU 34 CG GLU A 5 11333 6985 12616 -279 -1177 2215 C ATOM 35 CD GLU A 5 -104.611-144.292 144.832 1.00 91.96 C ANISOU 35 CD GLU A 5 12813 8139 13989 -307 -1374 2498 C ATOM 36 OE1 GLU A 5 -104.413-143.065 144.713 1.00 90.28 O ANISOU 36 OE1 GLU A 5 12669 7679 13955 -355 -1429 2603 O ATOM 37 OE2 GLU A 5 -105.370-144.936 144.079 1.00102.53 O ANISOU 37 OE2 GLU A 5 14207 9575 15175 -293 -1489 2626 O ATOM 38 N GLY A 6 -99.671-146.606 145.692 1.00 81.29 N ANISOU 38 N GLY A 6 11266 7419 12200 -750 -573 1973 N ATOM 39 CA GLY A 6 -98.398-146.635 145.027 1.00 82.31 C ANISOU 39 CA GLY A 6 11431 7594 12249 -956 -391 2011 C ATOM 40 C GLY A 6 -98.446-147.653 143.913 1.00 76.74 C ANISOU 40 C GLY A 6 10828 7068 11262 -1035 -301 2091 C ATOM 41 O GLY A 6 -99.458-148.329 143.713 1.00 81.76 O ANISOU 41 O GLY A 6 11502 7791 11771 -928 -405 2116 O ATOM 42 N PRO A 7 -97.365-147.773 143.149 1.00 70.17 N ANISOU 42 N PRO A 7 10044 6287 10329 -1233 -95 2126 N ATOM 43 CA PRO A 7 -97.284-148.865 142.171 1.00 81.25 C ANISOU 43 CA PRO A 7 11540 7873 11459 -1318 42 2146 C ATOM 44 C PRO A 7 -97.240-150.205 142.891 1.00 79.70 C ANISOU 44 C PRO A 7 11155 7863 11265 -1178 93 1934 C ATOM 45 O PRO A 7 -96.343-150.465 143.694 1.00 85.01 O ANISOU 45 O PRO A 7 11626 8571 12102 -1159 193 1771 O ATOM 46 CB PRO A 7 -95.981-148.567 141.420 1.00 76.51 C ANISOU 46 CB PRO A 7 10990 7259 10822 -1563 299 2186 C ATOM 47 CG PRO A 7 -95.750-147.092 141.632 1.00 65.81 C ANISOU 47 CG PRO A 7 9666 5677 9661 -1629 222 2292 C ATOM 48 CD PRO A 7 -96.227-146.846 143.031 1.00 70.01 C ANISOU 48 CD PRO A 7 10020 6143 10439 -1410 34 2160 C ATOM 49 N ASN A 8 -98.255-151.029 142.636 1.00 71.79 N ANISOU 49 N ASN A 8 10218 6965 10095 -1081 -7 1948 N ATOM 50 CA ASN A 8 -98.376-152.407 143.117 1.00 66.40 C ANISOU 50 CA ASN A 8 9403 6457 9370 -963 32 1780 C ATOM 51 C ASN A 8 -98.790-152.518 144.579 1.00 66.19 C ANISOU 51 C ASN A 8 9186 6425 9538 -762 -104 1640 C ATOM 52 O ASN A 8 -98.585-153.578 145.185 1.00 64.78 O ANISOU 52 O ASN A 8 8869 6371 9372 -682 -57 1489 O ATOM 53 CB ASN A 8 -97.081-153.211 142.933 1.00 59.23 C ANISOU 53 CB ASN A 8 8393 5657 8454 -1063 298 1651 C ATOM 54 CG ASN A 8 -96.490-153.063 141.556 1.00 78.54 C ANISOU 54 CG ASN A 8 11021 8106 10715 -1291 502 1754 C ATOM 55 OD1 ASN A 8 -97.191-153.157 140.549 1.00 88.72 O ANISOU 55 OD1 ASN A 8 12543 9418 11750 -1364 459 1885 O ATOM 56 ND2 ASN A 8 -95.186-152.820 141.502 1.00 87.19 N ANISOU 56 ND2 ASN A 8 12016 9176 11935 -1419 724 1698 N ATOM 57 N PHE A 9 -99.358-151.480 145.188 1.00 67.29 N ANISOU 57 N PHE A 9 9322 6415 9831 -684 -264 1679 N ATOM 58 CA PHE A 9 -99.821-151.660 146.558 1.00 68.28 C ANISOU 58 CA PHE A 9 9297 6545 10099 -510 -364 1530 C ATOM 59 C PHE A 9 -100.871-150.621 146.910 1.00 63.47 C ANISOU 59 C PHE A 9 8730 5769 9617 -411 -537 1594 C ATOM 60 O PHE A 9 -100.984-149.572 146.272 1.00 77.28 O ANISOU 60 O PHE A 9 10595 7362 11408 -480 -590 1747 O ATOM 61 CB PHE A 9 -98.662-151.611 147.568 1.00 57.97 C ANISOU 61 CB PHE A 9 7834 5240 8954 -532 -285 1373 C ATOM 62 CG PHE A 9 -97.899-150.306 147.585 1.00 67.65 C ANISOU 62 CG PHE A 9 9075 6295 10334 -645 -263 1417 C ATOM 63 CD1 PHE A 9 -96.690-150.190 146.919 1.00 61.80 C ANISOU 63 CD1 PHE A 9 8325 5556 9599 -819 -99 1453 C ATOM 64 CD2 PHE A 9 -98.371-149.210 148.297 1.00 61.26 C ANISOU 64 CD2 PHE A 9 8279 5313 9682 -584 -387 1406 C ATOM 65 CE1 PHE A 9 -95.976-148.999 146.945 1.00 74.44 C ANISOU 65 CE1 PHE A 9 9933 6995 11355 -938 -77 1495 C ATOM 66 CE2 PHE A 9 -97.662-148.019 148.324 1.00 72.01 C ANISOU 66 CE2 PHE A 9 9661 6504 11197 -696 -371 1441 C ATOM 67 CZ PHE A 9 -96.461-147.918 147.646 1.00 71.25 C ANISOU 67 CZ PHE A 9 9556 6416 11099 -877 -223 1492 C ATOM 68 N TYR A 10 -101.634-150.943 147.953 1.00 75.48 N ANISOU 68 N TYR A 10 10153 7315 11211 -251 -615 1470 N ATOM 69 CA TYR A 10 -102.540-150.002 148.605 1.00 74.90 C ANISOU 69 CA TYR A 10 10066 7074 11318 -136 -735 1459 C ATOM 70 C TYR A 10 -102.431-150.254 150.106 1.00 74.51 C ANISOU 70 C TYR A 10 9895 7060 11357 -49 -709 1238 C ATOM 71 O TYR A 10 -102.965-151.243 150.616 1.00 74.14 O ANISOU 71 O TYR A 10 9785 7149 11236 41 -711 1147 O ATOM 72 CB TYR A 10 -103.974-150.168 148.117 1.00 69.12 C ANISOU 72 CB TYR A 10 9369 6331 10563 -31 -866 1566 C ATOM 73 CG TYR A 10 -104.972-149.348 148.903 1.00 77.12 C ANISOU 73 CG TYR A 10 10320 7174 11807 114 -961 1517 C ATOM 74 CD1 TYR A 10 -105.103-147.982 148.685 1.00 80.01 C ANISOU 74 CD1 TYR A 10 10741 7298 12361 106 -1035 1617 C ATOM 75 CD2 TYR A 10 -105.778-149.938 149.869 1.00 70.25 C ANISOU 75 CD2 TYR A 10 9339 6373 10981 254 -958 1365 C ATOM 76 CE1 TYR A 10 -106.014-147.225 149.408 1.00 78.08 C ANISOU 76 CE1 TYR A 10 10427 6876 12366 248 -1097 1552 C ATOM 77 CE2 TYR A 10 -106.685-149.194 150.592 1.00 72.99 C ANISOU 77 CE2 TYR A 10 9621 6559 11554 382 -1001 1297 C ATOM 78 CZ TYR A 10 -106.800-147.840 150.359 1.00 82.39 C ANISOU 78 CZ TYR A 10 10852 7500 12951 386 -1067 1382 C ATOM 79 OH TYR A 10 -107.707-147.102 151.085 1.00 88.25 O ANISOU 79 OH TYR A 10 11516 8060 13953 523 -1087 1292 O ATOM 80 N VAL A 11 -101.728-149.370 150.803 1.00 69.10 N ANISOU 80 N VAL A 11 9192 6250 10814 -95 -689 1156 N ATOM 81 CA VAL A 11 -101.621-149.444 152.258 1.00 67.55 C ANISOU 81 CA VAL A 11 8921 6063 10681 -42 -684 950 C ATOM 82 C VAL A 11 -102.873-148.811 152.853 1.00 75.79 C ANISOU 82 C VAL A 11 9974 6972 11852 93 -739 893 C ATOM 83 O VAL A 11 -103.116-147.616 152.639 1.00 70.69 O ANISOU 83 O VAL A 11 9374 6114 11370 97 -777 950 O ATOM 84 CB VAL A 11 -100.347-148.746 152.759 1.00 65.05 C ANISOU 84 CB VAL A 11 8590 5662 10465 -165 -657 877 C ATOM 85 CG1 VAL A 11 -100.322-148.695 154.288 1.00 61.96 C ANISOU 85 CG1 VAL A 11 8165 5258 10118 -129 -681 666 C ATOM 86 CG2 VAL A 11 -99.110-149.455 152.214 1.00 63.71 C ANISOU 86 CG2 VAL A 11 8366 5626 10215 -288 -582 917 C ATOM 87 N PRO A 12 -103.705-149.562 153.581 1.00 81.59 N ANISOU 87 N PRO A 12 10658 7807 12537 203 -733 782 N ATOM 88 CA PRO A 12 -104.928-148.967 154.138 1.00 72.10 C ANISOU 88 CA PRO A 12 9441 6469 11487 332 -747 711 C ATOM 89 C PRO A 12 -104.633-148.040 155.305 1.00 73.50 C ANISOU 89 C PRO A 12 9641 6494 11790 316 -706 527 C ATOM 90 O PRO A 12 -105.069-148.293 156.431 1.00 78.79 O ANISOU 90 O PRO A 12 10299 7197 12442 367 -650 344 O ATOM 91 CB PRO A 12 -105.742-150.189 154.581 1.00 67.20 C ANISOU 91 CB PRO A 12 8758 6027 10748 420 -721 638 C ATOM 92 CG PRO A 12 -104.711-151.216 154.888 1.00 69.02 C ANISOU 92 CG PRO A 12 8986 6449 10789 331 -691 587 C ATOM 93 CD PRO A 12 -103.582-150.993 153.912 1.00 63.68 C ANISOU 93 CD PRO A 12 8341 5766 10090 211 -702 718 C ATOM 94 N PHE A 13 -103.893-146.963 155.052 1.00 73.73 N ANISOU 94 N PHE A 13 9722 6355 11936 230 -727 569 N ATOM 95 CA PHE A 13 -103.542-146.021 156.104 1.00 70.31 C ANISOU 95 CA PHE A 13 9331 5760 11624 193 -697 390 C ATOM 96 C PHE A 13 -103.204-144.683 155.464 1.00 70.09 C ANISOU 96 C PHE A 13 9355 5486 11791 138 -738 499 C ATOM 97 O PHE A 13 -102.522-144.638 154.438 1.00 79.99 O ANISOU 97 O PHE A 13 10627 6757 13009 42 -770 682 O ATOM 98 CB PHE A 13 -102.368-146.534 156.948 1.00 72.70 C ANISOU 98 CB PHE A 13 9641 6197 11783 68 -687 261 C ATOM 99 CG PHE A 13 -102.106-145.713 158.177 1.00 74.29 C ANISOU 99 CG PHE A 13 9909 6257 12059 17 -670 48 C ATOM 100 CD1 PHE A 13 -102.818-145.936 159.346 1.00 64.45 C ANISOU 100 CD1 PHE A 13 8698 5033 10756 77 -611 -155 C ATOM 101 CD2 PHE A 13 -101.157-144.711 158.160 1.00 74.53 C ANISOU 101 CD2 PHE A 13 9981 6128 12208 -107 -704 45 C ATOM 102 CE1 PHE A 13 -102.583-145.173 160.476 1.00 72.09 C ANISOU 102 CE1 PHE A 13 9761 5868 11761 9 -586 -367 C ATOM 103 CE2 PHE A 13 -100.918-143.942 159.290 1.00 69.41 C ANISOU 103 CE2 PHE A 13 9413 5340 11619 -169 -699 -164 C ATOM 104 CZ PHE A 13 -101.629-144.173 160.446 1.00 69.44 C ANISOU 104 CZ PHE A 13 9472 5369 11543 -114 -639 -375 C ATOM 105 N SER A 14 -103.692-143.603 156.066 1.00 71.65 N ANISOU 105 N SER A 14 9583 5444 12196 192 -721 383 N ATOM 106 CA SER A 14 -103.489-142.277 155.498 1.00 63.94 C ANISOU 106 CA SER A 14 8661 4195 11440 152 -768 489 C ATOM 107 C SER A 14 -102.054-141.806 155.707 1.00 68.09 C ANISOU 107 C SER A 14 9239 4685 11949 -37 -768 453 C ATOM 108 O SER A 14 -101.436-142.070 156.738 1.00 78.04 O ANISOU 108 O SER A 14 10504 6028 13119 -108 -738 260 O ATOM 109 CB SER A 14 -104.455-141.269 156.118 1.00 70.85 C ANISOU 109 CB SER A 14 9539 4799 12581 276 -738 354 C ATOM 110 OG SER A 14 -104.044-139.942 155.820 1.00 69.25 O ANISOU 110 OG SER A 14 9405 4311 12597 212 -781 414 O ATOM 111 N ASN A 15 -101.532-141.072 154.720 1.00 71.19 N ANISOU 111 N ASN A 15 9674 4940 12436 -131 -814 649 N ATOM 112 CA ASN A 15 -100.154-140.594 154.753 1.00 70.54 C ANISOU 112 CA ASN A 15 9619 4814 12370 -325 -809 645 C ATOM 113 C ASN A 15 -100.054-139.103 155.075 1.00 68.55 C ANISOU 113 C ASN A 15 9442 4230 12375 -368 -830 587 C ATOM 114 O ASN A 15 -99.039-138.474 154.760 1.00 77.96 O ANISOU 114 O ASN A 15 10665 5323 13634 -535 -840 656 O ATOM 115 CB ASN A 15 -99.456-140.906 153.425 1.00 80.10 C ANISOU 115 CB ASN A 15 10830 6123 13480 -444 -807 894 C ATOM 116 CG ASN A 15 -97.932-140.898 153.540 1.00 75.60 C ANISOU 116 CG ASN A 15 10225 5610 12888 -645 -769 864 C ATOM 117 OD1 ASN A 15 -97.380-140.971 154.639 1.00 73.65 O ANISOU 117 OD1 ASN A 15 9939 5395 12651 -689 -775 662 O ATOM 118 ND2 ASN A 15 -97.246-140.811 152.407 1.00 84.14 N ANISOU 118 ND2 ASN A 15 11324 6703 13945 -780 -730 1065 N ATOM 119 N LYS A 16 -101.078-138.521 155.714 1.00 73.41 N ANISOU 119 N LYS A 16 10079 4658 13154 -225 -821 450 N ATOM 120 CA LYS A 16 -101.007-137.097 156.046 1.00 86.80 C ANISOU 120 CA LYS A 16 11851 6012 15118 -259 -831 374 C ATOM 121 C LYS A 16 -99.895-136.806 157.044 1.00 85.46 C ANISOU 121 C LYS A 16 11723 5830 14919 -428 -812 162 C ATOM 122 O LYS A 16 -99.347-135.697 157.057 1.00 91.12 O ANISOU 122 O LYS A 16 12504 6297 15820 -539 -836 154 O ATOM 123 CB LYS A 16 -102.348-136.597 156.586 1.00 91.56 C ANISOU 123 CB LYS A 16 12449 6412 15928 -61 -795 236 C ATOM 124 CG LYS A 16 -102.949-137.443 157.696 1.00103.59 C ANISOU 124 CG LYS A 16 13934 8117 17308 38 -698 -17 C ATOM 125 CD LYS A 16 -104.108-136.712 158.359 1.00102.66 C ANISOU 125 CD LYS A 16 13814 7743 17448 200 -615 -207 C ATOM 126 CE LYS A 16 -104.901-137.629 159.269 1.00105.99 C ANISOU 126 CE LYS A 16 14190 8356 17725 306 -494 -417 C ATOM 127 NZ LYS A 16 -105.731-138.582 158.484 1.00116.73 N ANISOU 127 NZ LYS A 16 15429 9902 19022 439 -530 -225 N ATOM 128 N THR A 17 -99.535-137.787 157.871 1.00 79.30 N ANISOU 128 N THR A 17 10909 5306 13914 -461 -789 2 N ATOM 129 CA THR A 17 -98.403-137.638 158.778 1.00 76.80 C ANISOU 129 CA THR A 17 10626 5007 13547 -642 -818 -172 C ATOM 130 C THR A 17 -97.064-137.919 158.107 1.00 77.42 C ANISOU 130 C THR A 17 10634 5207 13577 -822 -868 -7 C ATOM 131 O THR A 17 -96.022-137.579 158.674 1.00 86.28 O ANISOU 131 O THR A 17 11762 6291 14731 -994 -918 -109 O ATOM 132 CB THR A 17 -98.569-138.560 159.988 1.00 92.68 C ANISOU 132 CB THR A 17 12647 7227 15339 -618 -800 -399 C ATOM 133 OG1 THR A 17 -98.768-139.910 159.545 1.00 91.47 O ANISOU 133 OG1 THR A 17 12398 7370 14987 -542 -795 -277 O ATOM 134 CG2 THR A 17 -99.759-138.122 160.833 1.00 86.73 C ANISOU 134 CG2 THR A 17 11979 6322 14652 -483 -709 -619 C ATOM 135 N GLY A 18 -97.057-138.535 156.929 1.00 73.09 N ANISOU 135 N GLY A 18 10014 4800 12955 -796 -849 233 N ATOM 136 CA GLY A 18 -95.803-138.788 156.241 1.00 73.90 C ANISOU 136 CA GLY A 18 10040 5006 13031 -969 -849 376 C ATOM 137 C GLY A 18 -95.084-140.063 156.638 1.00 75.14 C ANISOU 137 C GLY A 18 10081 5459 13010 -1013 -859 314 C ATOM 138 O GLY A 18 -93.924-140.258 156.248 1.00 73.17 O ANISOU 138 O GLY A 18 9735 5281 12784 -1165 -851 389 O ATOM 139 N VAL A 19 -95.739-140.960 157.381 1.00 74.04 N ANISOU 139 N VAL A 19 9937 5484 12710 -887 -870 186 N ATOM 140 CA VAL A 19 -95.051-142.132 157.928 1.00 80.54 C ANISOU 140 CA VAL A 19 10662 6555 13384 -931 -911 118 C ATOM 141 C VAL A 19 -95.248-143.392 157.101 1.00 72.45 C ANISOU 141 C VAL A 19 9548 5767 12214 -847 -854 261 C ATOM 142 O VAL A 19 -94.553-144.391 157.349 1.00 81.81 O ANISOU 142 O VAL A 19 10627 7142 13317 -887 -883 239 O ATOM 143 CB VAL A 19 -95.488-142.411 159.383 1.00 70.42 C ANISOU 143 CB VAL A 19 9452 5316 11989 -887 -970 -118 C ATOM 144 CG1 VAL A 19 -95.284-141.167 160.245 1.00 65.44 C ANISOU 144 CG1 VAL A 19 8936 4444 11483 -987 -1017 -290 C ATOM 145 CG2 VAL A 19 -96.935-142.895 159.427 1.00 61.70 C ANISOU 145 CG2 VAL A 19 8399 4272 10773 -688 -899 -139 C ATOM 146 N VAL A 20 -96.163-143.387 156.133 1.00 81.45 N ANISOU 146 N VAL A 20 10729 6890 13330 -736 -790 406 N ATOM 147 CA VAL A 20 -96.431-144.594 155.361 1.00 75.56 C ANISOU 147 CA VAL A 20 9923 6361 12426 -663 -739 523 C ATOM 148 C VAL A 20 -95.232-144.933 154.484 1.00 77.21 C ANISOU 148 C VAL A 20 10036 6654 12645 -804 -678 646 C ATOM 149 O VAL A 20 -94.576-144.047 153.920 1.00 74.75 O ANISOU 149 O VAL A 20 9739 6202 12463 -935 -644 734 O ATOM 150 CB VAL A 20 -97.710-144.418 154.525 1.00 71.43 C ANISOU 150 CB VAL A 20 9478 5781 11882 -531 -716 655 C ATOM 151 CG1 VAL A 20 -97.957-145.645 153.661 1.00 60.67 C ANISOU 151 CG1 VAL A 20 8073 4635 10342 -482 -672 775 C ATOM 152 CG2 VAL A 20 -98.895-144.161 155.441 1.00 73.33 C ANISOU 152 CG2 VAL A 20 9770 5940 12152 -384 -747 511 C ATOM 153 N ARG A 21 -94.936-146.228 154.376 1.00 74.34 N ANISOU 153 N ARG A 21 9573 6511 12160 -782 -647 647 N ATOM 154 CA ARG A 21 -93.862-146.744 153.542 1.00 60.09 C ANISOU 154 CA ARG A 21 7656 4804 10373 -895 -550 738 C ATOM 155 C ARG A 21 -94.400-147.857 152.654 1.00 67.96 C ANISOU 155 C ARG A 21 8658 5972 11194 -810 -465 830 C ATOM 156 O ARG A 21 -95.414-148.488 152.964 1.00 69.95 O ANISOU 156 O ARG A 21 8952 6309 11319 -666 -512 793 O ATOM 157 CB ARG A 21 -92.701-147.274 154.395 1.00 70.28 C ANISOU 157 CB ARG A 21 8781 6173 11748 -972 -606 619 C ATOM 158 CG ARG A 21 -92.109-146.246 155.337 1.00 70.38 C ANISOU 158 CG ARG A 21 8794 6026 11920 -1079 -717 515 C ATOM 159 CD ARG A 21 -91.391-145.163 154.558 1.00 61.41 C ANISOU 159 CD ARG A 21 7654 4728 10952 -1237 -637 615 C ATOM 160 NE ARG A 21 -90.785-144.179 155.447 1.00 82.11 N ANISOU 160 NE ARG A 21 10273 7186 13739 -1355 -751 509 N ATOM 161 CZ ARG A 21 -91.333-143.006 155.756 1.00 75.39 C ANISOU 161 CZ ARG A 21 9574 6129 12940 -1357 -798 472 C ATOM 162 NH1 ARG A 21 -90.704-142.176 156.575 1.00 85.07 N ANISOU 162 NH1 ARG A 21 10802 7209 14312 -1482 -901 359 N ATOM 163 NH2 ARG A 21 -92.508-142.658 155.245 1.00 69.34 N ANISOU 163 NH2 ARG A 21 8955 5291 12101 -1236 -750 546 N ATOM 164 N SER A 22 -93.706-148.092 151.543 1.00 61.36 N ANISOU 164 N SER A 22 7783 5181 10349 -915 -325 940 N ATOM 165 CA SER A 22 -94.037-149.211 150.670 1.00 77.44 C ANISOU 165 CA SER A 22 9828 7382 12213 -866 -227 1006 C ATOM 166 C SER A 22 -94.041-150.516 151.459 1.00 69.02 C ANISOU 166 C SER A 22 8644 6482 11099 -761 -274 880 C ATOM 167 O SER A 22 -93.079-150.796 152.189 1.00 65.11 O ANISOU 167 O SER A 22 7996 6012 10732 -805 -307 784 O ATOM 168 CB SER A 22 -93.032-149.309 149.524 1.00 70.83 C ANISOU 168 CB SER A 22 8950 6569 11392 -1025 -34 1094 C ATOM 169 OG SER A 22 -93.152-150.552 148.853 1.00 74.10 O ANISOU 169 OG SER A 22 9351 7152 11653 -988 76 1105 O ATOM 170 N PRO A 23 -95.086-151.340 151.339 1.00 73.82 N ANISOU 170 N PRO A 23 9314 7196 11537 -631 -296 889 N ATOM 171 CA PRO A 23 -95.091-152.641 152.022 1.00 69.25 C ANISOU 171 CA PRO A 23 8636 6769 10909 -542 -336 788 C ATOM 172 C PRO A 23 -94.054-153.617 151.491 1.00 68.15 C ANISOU 172 C PRO A 23 8356 6730 10808 -601 -211 781 C ATOM 173 O PRO A 23 -93.946-154.726 152.026 1.00 69.16 O ANISOU 173 O PRO A 23 8388 6963 10928 -531 -250 708 O ATOM 174 CB PRO A 23 -96.516-153.159 151.773 1.00 61.99 C ANISOU 174 CB PRO A 23 7829 5916 9808 -411 -366 823 C ATOM 175 CG PRO A 23 -96.925-152.496 150.505 1.00 68.85 C ANISOU 175 CG PRO A 23 8827 6716 10616 -461 -301 973 C ATOM 176 CD PRO A 23 -96.298-151.132 150.530 1.00 67.57 C ANISOU 176 CD PRO A 23 8683 6385 10607 -570 -300 1005 C ATOM 177 N PHE A 24 -93.300-153.247 150.456 1.00 69.23 N ANISOU 177 N PHE A 24 8478 6828 10996 -730 -49 854 N ATOM 178 CA PHE A 24 -92.183-154.040 149.962 1.00 67.04 C ANISOU 178 CA PHE A 24 8041 6620 10814 -801 112 825 C ATOM 179 C PHE A 24 -90.840-153.576 150.513 1.00 66.93 C ANISOU 179 C PHE A 24 7830 6529 11071 -907 104 770 C ATOM 180 O PHE A 24 -89.817-154.188 150.195 1.00 78.96 O ANISOU 180 O PHE A 24 9170 8089 12741 -964 239 735 O ATOM 181 CB PHE A 24 -92.137-154.002 148.425 1.00 60.06 C ANISOU 181 CB PHE A 24 7265 5748 9807 -905 338 925 C ATOM 182 CG PHE A 24 -93.408-154.458 147.759 1.00 76.71 C ANISOU 182 CG PHE A 24 9571 7928 11648 -828 328 992 C ATOM 183 CD1 PHE A 24 -93.849-155.765 147.892 1.00 66.44 C ANISOU 183 CD1 PHE A 24 8239 6752 10253 -714 314 927 C ATOM 184 CD2 PHE A 24 -94.149-153.582 146.979 1.00 70.97 C ANISOU 184 CD2 PHE A 24 9058 7130 10777 -878 315 1131 C ATOM 185 CE1 PHE A 24 -95.015-156.186 147.273 1.00 64.05 C ANISOU 185 CE1 PHE A 24 8109 6511 9715 -658 289 987 C ATOM 186 CE2 PHE A 24 -95.318-154.002 146.357 1.00 74.34 C ANISOU 186 CE2 PHE A 24 9654 7617 10977 -817 271 1204 C ATOM 187 CZ PHE A 24 -95.747-155.303 146.506 1.00 72.52 C ANISOU 187 CZ PHE A 24 9383 7520 10653 -711 261 1126 C ATOM 188 N GLU A 25 -90.810-152.523 151.335 1.00 63.63 N ANISOU 188 N GLU A 25 7434 5998 10743 -938 -48 754 N ATOM 189 CA GLU A 25 -89.544-151.880 151.685 1.00 66.84 C ANISOU 189 CA GLU A 25 7675 6310 11410 -1075 -57 722 C ATOM 190 C GLU A 25 -89.311-151.685 153.177 1.00 71.46 C ANISOU 190 C GLU A 25 8189 6855 12108 -1055 -306 621 C ATOM 191 O GLU A 25 -88.159-151.655 153.620 1.00 77.36 O ANISOU 191 O GLU A 25 8735 7568 13088 -1146 -358 575 O ATOM 192 CB GLU A 25 -89.450-150.516 151.004 1.00 66.38 C ANISOU 192 CB GLU A 25 7732 6110 11380 -1210 31 816 C ATOM 193 CG GLU A 25 -89.570-150.555 149.489 1.00 88.61 C ANISOU 193 CG GLU A 25 10654 8949 14064 -1281 274 935 C ATOM 194 CD GLU A 25 -88.227-150.679 148.805 1.00119.61 C ANISOU 194 CD GLU A 25 14400 12875 18169 -1442 504 936 C ATOM 195 OE1 GLU A 25 -87.511-151.671 149.070 1.00122.92 O ANISOU 195 OE1 GLU A 25 14596 13380 18728 -1411 546 842 O ATOM 196 OE2 GLU A 25 -87.884-149.769 148.019 1.00138.85 O ANISOU 196 OE2 GLU A 25 16914 15216 20627 -1602 644 1031 O ATOM 197 N ALA A 26 -90.372-151.528 153.964 1.00 67.27 N ANISOU 197 N ALA A 26 7820 6321 11420 -952 -462 582 N ATOM 198 CA ALA A 26 -90.194-151.149 155.360 1.00 66.39 C ANISOU 198 CA ALA A 26 7701 6152 11370 -970 -684 479 C ATOM 199 C ALA A 26 -91.368-151.656 156.179 1.00 61.39 C ANISOU 199 C ALA A 26 7210 5590 10525 -829 -800 418 C ATOM 200 O ALA A 26 -92.462-151.852 155.640 1.00 70.23 O ANISOU 200 O ALA A 26 8455 6752 11478 -725 -716 464 O ATOM 201 CB ALA A 26 -90.058-149.621 155.509 1.00 57.79 C ANISOU 201 CB ALA A 26 6700 4882 10375 -1082 -716 474 C ATOM 202 N PRO A 27 -91.172-151.890 157.476 1.00 73.71 N ANISOU 202 N PRO A 27 8758 7164 12084 -836 -995 320 N ATOM 203 CA PRO A 27 -92.236-152.506 158.282 1.00 76.53 C ANISOU 203 CA PRO A 27 9248 7603 12228 -721 -1079 261 C ATOM 204 C PRO A 27 -93.427-151.577 158.482 1.00 71.93 C ANISOU 204 C PRO A 27 8873 6934 11525 -671 -1049 218 C ATOM 205 O PRO A 27 -93.280-150.364 158.650 1.00 78.55 O ANISOU 205 O PRO A 27 9774 7623 12449 -749 -1064 182 O ATOM 206 CB PRO A 27 -91.541-152.825 159.616 1.00 73.19 C ANISOU 206 CB PRO A 27 8779 7194 11838 -791 -1307 177 C ATOM 207 CG PRO A 27 -90.357-151.925 159.662 1.00 70.06 C ANISOU 207 CG PRO A 27 8274 6677 11668 -946 -1367 167 C ATOM 208 CD PRO A 27 -89.931-151.701 158.241 1.00 62.73 C ANISOU 208 CD PRO A 27 7225 5723 10885 -965 -1154 269 C ATOM 209 N GLN A 28 -94.620-152.170 158.475 1.00 71.95 N ANISOU 209 N GLN A 28 8968 7018 11352 -540 -1005 218 N ATOM 210 CA GLN A 28 -95.881-151.427 158.522 1.00 65.88 C ANISOU 210 CA GLN A 28 8357 6169 10507 -463 -950 187 C ATOM 211 C GLN A 28 -96.385-151.260 159.952 1.00 68.30 C ANISOU 211 C GLN A 28 8786 6453 10713 -461 -1040 31 C ATOM 212 O GLN A 28 -97.548-151.512 160.253 1.00 72.75 O ANISOU 212 O GLN A 28 9437 7051 11152 -360 -993 -14 O ATOM 213 CB GLN A 28 -96.917-152.134 157.661 1.00 67.51 C ANISOU 213 CB GLN A 28 8577 6468 10605 -333 -849 275 C ATOM 214 CG GLN A 28 -96.466-152.378 156.232 1.00 68.98 C ANISOU 214 CG GLN A 28 8684 6686 10838 -355 -746 418 C ATOM 215 CD GLN A 28 -96.473-151.116 155.402 1.00 70.59 C ANISOU 215 CD GLN A 28 8945 6737 11140 -406 -684 501 C ATOM 216 OE1 GLN A 28 -97.520-150.501 155.207 1.00 68.04 O ANISOU 216 OE1 GLN A 28 8725 6329 10798 -335 -675 527 O ATOM 217 NE2 GLN A 28 -95.304-150.718 154.911 1.00 68.39 N ANISOU 217 NE2 GLN A 28 8590 6408 10988 -535 -644 548 N ATOM 218 N TYR A 29 -95.510-150.804 160.851 1.00 69.76 N ANISOU 218 N TYR A 29 8982 6575 10947 -589 -1165 -59 N ATOM 219 CA TYR A 29 -95.863-150.745 162.265 1.00 74.30 C ANISOU 219 CA TYR A 29 9704 7143 11382 -624 -1255 -216 C ATOM 220 C TYR A 29 -96.816-149.603 162.610 1.00 79.32 C ANISOU 220 C TYR A 29 10499 7627 12012 -595 -1165 -335 C ATOM 221 O TYR A 29 -97.076-149.381 163.796 1.00 77.38 O ANISOU 221 O TYR A 29 10401 7351 11649 -649 -1207 -495 O ATOM 222 CB TYR A 29 -94.593-150.653 163.118 1.00 66.56 C ANISOU 222 CB TYR A 29 8699 6143 10446 -791 -1452 -270 C ATOM 223 CG TYR A 29 -93.778-151.930 163.106 1.00 71.13 C ANISOU 223 CG TYR A 29 9124 6867 11035 -805 -1570 -180 C ATOM 224 CD1 TYR A 29 -94.399-153.164 162.998 1.00 61.12 C ANISOU 224 CD1 TYR A 29 7843 5746 9633 -691 -1532 -128 C ATOM 225 CD2 TYR A 29 -92.389-151.900 163.187 1.00 64.38 C ANISOU 225 CD2 TYR A 29 8118 5986 10357 -930 -1721 -147 C ATOM 226 CE1 TYR A 29 -93.666-154.340 162.980 1.00 63.20 C ANISOU 226 CE1 TYR A 29 7961 6115 9936 -693 -1640 -47 C ATOM 227 CE2 TYR A 29 -91.646-153.076 163.170 1.00 58.05 C ANISOU 227 CE2 TYR A 29 7147 5292 9618 -927 -1830 -65 C ATOM 228 CZ TYR A 29 -92.294-154.289 163.064 1.00 63.44 C ANISOU 228 CZ TYR A 29 7833 6108 10164 -804 -1787 -16 C ATOM 229 OH TYR A 29 -91.580-155.463 163.041 1.00 70.81 O ANISOU 229 OH TYR A 29 8597 7123 11184 -790 -1894 62 O ATOM 230 N TYR A 30 -97.341-148.883 161.618 1.00 81.28 N ANISOU 230 N TYR A 30 10729 7767 12386 -518 -1043 -263 N ATOM 231 CA TYR A 30 -98.437-147.947 161.847 1.00 77.84 C ANISOU 231 CA TYR A 30 10412 7178 11984 -446 -944 -361 C ATOM 232 C TYR A 30 -99.797-148.587 161.609 1.00 80.83 C ANISOU 232 C TYR A 30 10793 7641 12280 -282 -837 -339 C ATOM 233 O TYR A 30 -100.813-148.037 162.047 1.00 88.36 O ANISOU 233 O TYR A 30 11827 8491 13255 -211 -747 -453 O ATOM 234 CB TYR A 30 -98.275-146.704 160.954 1.00 76.70 C ANISOU 234 CB TYR A 30 10251 6832 12059 -459 -904 -283 C ATOM 235 CG TYR A 30 -97.822-147.034 159.554 1.00 77.81 C ANISOU 235 CG TYR A 30 10267 7033 12264 -452 -885 -65 C ATOM 236 CD1 TYR A 30 -98.732-147.453 158.591 1.00 67.78 C ANISOU 236 CD1 TYR A 30 8969 5818 10966 -322 -809 65 C ATOM 237 CD2 TYR A 30 -96.482-146.950 159.200 1.00 70.53 C ANISOU 237 CD2 TYR A 30 9257 6115 11428 -590 -936 4 C ATOM 238 CE1 TYR A 30 -98.323-147.774 157.307 1.00 69.98 C ANISOU 238 CE1 TYR A 30 9173 6156 11262 -339 -779 252 C ATOM 239 CE2 TYR A 30 -96.061-147.272 157.921 1.00 69.21 C ANISOU 239 CE2 TYR A 30 8990 6005 11303 -600 -877 184 C ATOM 240 CZ TYR A 30 -96.985-147.683 156.978 1.00 70.72 C ANISOU 240 CZ TYR A 30 9192 6253 11425 -480 -795 304 C ATOM 241 OH TYR A 30 -96.562-147.998 155.706 1.00 73.52 O ANISOU 241 OH TYR A 30 9485 6665 11784 -515 -725 470 O ATOM 242 N LEU A 31 -99.832-149.735 160.925 1.00 73.07 N ANISOU 242 N LEU A 31 9711 6833 11220 -224 -838 -203 N ATOM 243 CA LEU A 31 -101.055-150.523 160.813 1.00 66.32 C ANISOU 243 CA LEU A 31 8850 6080 10268 -90 -762 -186 C ATOM 244 C LEU A 31 -101.351-151.298 162.085 1.00 67.36 C ANISOU 244 C LEU A 31 9059 6324 10210 -110 -772 -323 C ATOM 245 O LEU A 31 -102.520-151.546 162.399 1.00 78.90 O ANISOU 245 O LEU A 31 10555 7809 11614 -21 -675 -385 O ATOM 246 CB LEU A 31 -100.948-151.511 159.648 1.00 70.17 C ANISOU 246 CB LEU A 31 9227 6708 10727 -43 -763 -6 C ATOM 247 CG LEU A 31 -100.685-150.974 158.244 1.00 77.32 C ANISOU 247 CG LEU A 31 10080 7539 11760 -43 -741 158 C ATOM 248 CD1 LEU A 31 -100.604-152.134 157.274 1.00 66.42 C ANISOU 248 CD1 LEU A 31 8623 6321 10294 -15 -726 293 C ATOM 249 CD2 LEU A 31 -101.773-150.000 157.833 1.00 70.36 C ANISOU 249 CD2 LEU A 31 9241 6497 10997 47 -694 182 C ATOM 250 N ALA A 32 -100.311-151.705 162.808 1.00 73.11 N ANISOU 250 N ALA A 32 9813 7120 10847 -233 -894 -360 N ATOM 251 CA ALA A 32 -100.454-152.575 163.964 1.00 62.13 C ANISOU 251 CA ALA A 32 8514 5848 9244 -279 -940 -449 C ATOM 252 C ALA A 32 -99.147-152.558 164.735 1.00 65.47 C ANISOU 252 C ALA A 32 8974 6272 9628 -442 -1124 -486 C ATOM 253 O ALA A 32 -98.076-152.356 164.156 1.00 70.37 O ANISOU 253 O ALA A 32 9478 6863 10396 -494 -1212 -398 O ATOM 254 CB ALA A 32 -100.808-154.009 163.548 1.00 51.88 C ANISOU 254 CB ALA A 32 7134 4727 7852 -199 -935 -334 C ATOM 255 N GLU A 33 -99.252-152.762 166.049 1.00 63.79 N ANISOU 255 N GLU A 33 8928 6091 9218 -536 -1181 -615 N ATOM 256 CA GLU A 33 -98.079-152.843 166.904 1.00 62.60 C ANISOU 256 CA GLU A 33 8833 5948 9003 -707 -1403 -642 C ATOM 257 C GLU A 33 -97.233-154.061 166.534 1.00 74.04 C ANISOU 257 C GLU A 33 10121 7527 10485 -704 -1558 -474 C ATOM 258 O GLU A 33 -97.740-155.032 165.966 1.00 63.63 O ANISOU 258 O GLU A 33 8719 6316 9142 -588 -1486 -377 O ATOM 259 CB GLU A 33 -98.497-152.925 168.367 1.00 76.85 C ANISOU 259 CB GLU A 33 10889 7773 10536 -819 -1429 -803 C ATOM 260 CG GLU A 33 -99.366-151.767 168.833 1.00 82.87 C ANISOU 260 CG GLU A 33 11818 8397 11273 -824 -1240 -1007 C ATOM 261 CD GLU A 33 -98.620-150.452 168.817 1.00105.56 C ANISOU 261 CD GLU A 33 14709 11091 14308 -916 -1300 -1084 C ATOM 262 OE1 GLU A 33 -97.392-150.465 169.042 1.00112.09 O ANISOU 262 OE1 GLU A 33 15509 11919 15159 -1052 -1529 -1038 O ATOM 263 OE2 GLU A 33 -99.258-149.407 168.572 1.00125.25 O ANISOU 263 OE2 GLU A 33 17230 13430 16928 -853 -1125 -1186 O ATOM 264 N PRO A 34 -95.928-154.020 166.829 1.00 66.74 N ANISOU 264 N PRO A 34 9136 6580 9643 -832 -1775 -443 N ATOM 265 CA PRO A 34 -95.085-155.203 166.567 1.00 58.26 C ANISOU 265 CA PRO A 34 7888 5606 8643 -825 -1929 -294 C ATOM 266 C PRO A 34 -95.617-156.485 167.195 1.00 61.16 C ANISOU 266 C PRO A 34 8343 6103 8794 -800 -1984 -261 C ATOM 267 O PRO A 34 -95.607-157.537 166.539 1.00 59.01 O ANISOU 267 O PRO A 34 7925 5914 8583 -698 -1964 -140 O ATOM 268 CB PRO A 34 -93.726-154.791 167.149 1.00 59.64 C ANISOU 268 CB PRO A 34 8023 5711 8928 -995 -2184 -304 C ATOM 269 CG PRO A 34 -93.714-153.292 167.027 1.00 63.99 C ANISOU 269 CG PRO A 34 8632 6113 9566 -1051 -2097 -411 C ATOM 270 CD PRO A 34 -95.137-152.849 167.255 1.00 61.36 C ANISOU 270 CD PRO A 34 8503 5759 9050 -978 -1882 -533 C ATOM 271 N TRP A 35 -96.117-156.423 168.434 1.00 55.81 N ANISOU 271 N TRP A 35 7915 5436 7853 -898 -2033 -371 N ATOM 272 CA TRP A 35 -96.655-157.621 169.078 1.00 54.93 C ANISOU 272 CA TRP A 35 7915 5441 7515 -898 -2076 -331 C ATOM 273 C TRP A 35 -97.856-158.194 168.327 1.00 73.04 C ANISOU 273 C TRP A 35 10158 7808 9788 -725 -1828 -298 C ATOM 274 O TRP A 35 -98.106-159.403 168.406 1.00 65.19 O ANISOU 274 O TRP A 35 9153 6911 8705 -689 -1863 -208 O ATOM 275 CB TRP A 35 -97.023-157.335 170.540 1.00 66.10 C ANISOU 275 CB TRP A 35 9645 6850 8620 -1063 -2134 -471 C ATOM 276 CG TRP A 35 -98.282-156.526 170.768 1.00 82.58 C ANISOU 276 CG TRP A 35 11902 8896 10577 -1035 -1848 -650 C ATOM 277 CD1 TRP A 35 -98.355-155.183 170.984 1.00 80.14 C ANISOU 277 CD1 TRP A 35 11691 8458 10299 -1090 -1759 -815 C ATOM 278 CD2 TRP A 35 -99.632-157.016 170.836 1.00 85.06 C ANISOU 278 CD2 TRP A 35 12296 9282 10743 -948 -1613 -689 C ATOM 279 NE1 TRP A 35 -99.660-154.801 171.166 1.00 71.65 N ANISOU 279 NE1 TRP A 35 10736 7361 9125 -1029 -1477 -958 N ATOM 280 CE2 TRP A 35 -100.465-155.906 171.078 1.00 80.94 C ANISOU 280 CE2 TRP A 35 11895 8664 10195 -944 -1381 -883 C ATOM 281 CE3 TRP A 35 -100.217-158.281 170.705 1.00 80.00 C ANISOU 281 CE3 TRP A 35 11621 8763 10014 -875 -1574 -581 C ATOM 282 CZ2 TRP A 35 -101.851-156.020 171.193 1.00 73.96 C ANISOU 282 CZ2 TRP A 35 11075 7806 9219 -866 -1108 -973 C ATOM 283 CZ3 TRP A 35 -101.595-158.393 170.819 1.00 76.32 C ANISOU 283 CZ3 TRP A 35 11233 8332 9435 -810 -1309 -665 C ATOM 284 CH2 TRP A 35 -102.396-157.268 171.059 1.00 74.56 C ANISOU 284 CH2 TRP A 35 11106 8015 9207 -804 -1077 -859 C ATOM 285 N GLN A 36 -98.604-157.363 167.589 1.00 64.56 N ANISOU 285 N GLN A 36 9048 6677 8807 -624 -1596 -359 N ATOM 286 CA GLN A 36 -99.707-157.890 166.790 1.00 69.21 C ANISOU 286 CA GLN A 36 9565 7328 9405 -466 -1396 -311 C ATOM 287 C GLN A 36 -99.209-158.585 165.532 1.00 57.98 C ANISOU 287 C GLN A 36 7915 5950 8167 -366 -1413 -153 C ATOM 288 O GLN A 36 -99.844-159.538 165.064 1.00 62.73 O ANISOU 288 O GLN A 36 8466 6636 8733 -273 -1339 -83 O ATOM 289 CB GLN A 36 -100.692-156.767 166.441 1.00 50.00 C ANISOU 289 CB GLN A 36 7164 4803 7032 -392 -1176 -416 C ATOM 290 CG GLN A 36 -101.452-156.272 167.667 1.00 64.45 C ANISOU 290 CG GLN A 36 9219 6597 8672 -470 -1085 -599 C ATOM 291 CD GLN A 36 -102.074-154.890 167.495 1.00 80.73 C ANISOU 291 CD GLN A 36 11308 8508 10858 -423 -909 -732 C ATOM 292 OE1 GLN A 36 -101.723-154.129 166.589 1.00 78.70 O ANISOU 292 OE1 GLN A 36 10930 8153 10818 -369 -907 -682 O ATOM 293 NE2 GLN A 36 -102.995-154.556 168.390 1.00 81.19 N ANISOU 293 NE2 GLN A 36 11531 8533 10783 -453 -753 -905 N ATOM 294 N PHE A 37 -98.096-158.118 164.960 1.00 55.96 N ANISOU 294 N PHE A 37 7523 5631 8108 -395 -1491 -106 N ATOM 295 CA PHE A 37 -97.457-158.879 163.889 1.00 61.45 C ANISOU 295 CA PHE A 37 8012 6368 8969 -329 -1499 25 C ATOM 296 C PHE A 37 -96.937-160.213 164.409 1.00 66.64 C ANISOU 296 C PHE A 37 8632 7101 9587 -352 -1668 95 C ATOM 297 O PHE A 37 -97.000-161.229 163.707 1.00 56.47 O ANISOU 297 O PHE A 37 7232 5873 8351 -265 -1624 180 O ATOM 298 CB PHE A 37 -96.322-158.067 163.256 1.00 55.93 C ANISOU 298 CB PHE A 37 7174 5579 8499 -378 -1526 49 C ATOM 299 CG PHE A 37 -96.788-157.050 162.248 1.00 56.37 C ANISOU 299 CG PHE A 37 7216 5562 8638 -325 -1342 47 C ATOM 300 CD1 PHE A 37 -97.095-155.755 162.640 1.00 59.76 C ANISOU 300 CD1 PHE A 37 7764 5881 9063 -370 -1311 -49 C ATOM 301 CD2 PHE A 37 -96.918-157.387 160.906 1.00 56.20 C ANISOU 301 CD2 PHE A 37 7082 5573 8698 -239 -1208 143 C ATOM 302 CE1 PHE A 37 -97.524-154.818 161.718 1.00 66.28 C ANISOU 302 CE1 PHE A 37 8579 6618 9986 -320 -1169 -29 C ATOM 303 CE2 PHE A 37 -97.353-156.443 159.976 1.00 58.25 C ANISOU 303 CE2 PHE A 37 7355 5758 9019 -207 -1071 167 C ATOM 304 CZ PHE A 37 -97.652-155.160 160.389 1.00 59.32 C ANISOU 304 CZ PHE A 37 7594 5773 9173 -242 -1062 90 C ATOM 305 N SER A 38 -96.433-160.232 165.647 1.00 54.14 N ANISOU 305 N SER A 38 7155 5505 7910 -477 -1875 63 N ATOM 306 CA SER A 38 -95.984-161.488 166.239 1.00 60.88 C ANISOU 306 CA SER A 38 7995 6413 8725 -507 -2073 150 C ATOM 307 C SER A 38 -97.157-162.434 166.454 1.00 71.57 C ANISOU 307 C SER A 38 9467 7856 9870 -446 -1980 166 C ATOM 308 O SER A 38 -97.032-163.649 166.262 1.00 64.78 O ANISOU 308 O SER A 38 8526 7040 9048 -396 -2040 266 O ATOM 309 CB SER A 38 -95.259-161.223 167.559 1.00 57.05 C ANISOU 309 CB SER A 38 7637 5889 8151 -678 -2344 122 C ATOM 310 OG SER A 38 -94.219-160.275 167.398 1.00 66.26 O ANISOU 310 OG SER A 38 8692 6964 9518 -749 -2433 97 O ATOM 311 N MET A 39 -98.311-161.893 166.842 1.00 69.35 N ANISOU 311 N MET A 39 9367 7591 9393 -452 -1821 63 N ATOM 312 CA MET A 39 -99.497-162.725 167.009 1.00 62.23 C ANISOU 312 CA MET A 39 8558 6771 8314 -402 -1703 70 C ATOM 313 C MET A 39 -99.986-163.262 165.671 1.00 59.39 C ANISOU 313 C MET A 39 8029 6448 8089 -246 -1544 139 C ATOM 314 O MET A 39 -100.413-164.420 165.583 1.00 57.43 O ANISOU 314 O MET A 39 7770 6264 7787 -203 -1537 207 O ATOM 315 CB MET A 39 -100.589-161.940 167.723 1.00 61.62 C ANISOU 315 CB MET A 39 8683 6687 8041 -446 -1542 -75 C ATOM 316 CG MET A 39 -100.368-161.872 169.227 1.00 63.50 C ANISOU 316 CG MET A 39 9165 6924 8037 -626 -1685 -140 C ATOM 317 SD MET A 39 -100.105-163.529 169.889 1.00 84.88 S ANISOU 317 SD MET A 39 11938 9715 10598 -691 -1898 11 S ATOM 318 CE MET A 39 -100.277-163.215 171.637 1.00 90.54 C ANISOU 318 CE MET A 39 13020 10435 10944 -924 -1985 -94 C ATOM 319 N LEU A 40 -99.907-162.451 164.613 1.00 53.61 N ANISOU 319 N LEU A 40 7178 5669 7524 -176 -1427 127 N ATOM 320 CA LEU A 40 -100.110-162.992 163.272 1.00 54.01 C ANISOU 320 CA LEU A 40 7077 5750 7696 -60 -1317 204 C ATOM 321 C LEU A 40 -99.147-164.139 162.998 1.00 69.82 C ANISOU 321 C LEU A 40 8948 7771 9808 -51 -1436 300 C ATOM 322 O LEU A 40 -99.541-165.164 162.429 1.00 62.40 O ANISOU 322 O LEU A 40 7959 6881 8869 20 -1381 354 O ATOM 323 CB LEU A 40 -99.946-161.892 162.219 1.00 53.36 C ANISOU 323 CB LEU A 40 6911 5602 7763 -23 -1207 196 C ATOM 324 CG LEU A 40 -100.116-162.317 160.756 1.00 66.87 C ANISOU 324 CG LEU A 40 8502 7339 9566 68 -1091 274 C ATOM 325 CD1 LEU A 40 -101.452-163.029 160.526 1.00 61.80 C ANISOU 325 CD1 LEU A 40 7907 6768 8806 143 -999 287 C ATOM 326 CD2 LEU A 40 -99.992-161.104 159.849 1.00 61.83 C ANISOU 326 CD2 LEU A 40 7830 6625 9039 73 -998 277 C ATOM 327 N ALA A 41 -97.887-163.994 163.417 1.00 55.40 N ANISOU 327 N ALA A 41 7058 5895 8098 -125 -1607 316 N ATOM 328 CA ALA A 41 -96.920-165.069 163.236 1.00 54.75 C ANISOU 328 CA ALA A 41 6822 5805 8176 -110 -1732 401 C ATOM 329 C ALA A 41 -97.306-166.295 164.049 1.00 60.13 C ANISOU 329 C ALA A 41 7597 6530 8721 -118 -1852 455 C ATOM 330 O ALA A 41 -97.232-167.424 163.551 1.00 55.18 O ANISOU 330 O ALA A 41 6871 5913 8181 -48 -1844 519 O ATOM 331 CB ALA A 41 -95.521-164.585 163.623 1.00 52.96 C ANISOU 331 CB ALA A 41 6489 5501 8132 -196 -1916 409 C ATOM 332 N ALA A 42 -97.708-166.088 165.307 1.00 51.37 N ANISOU 332 N ALA A 42 6691 5438 7391 -216 -1955 424 N ATOM 333 CA ALA A 42 -98.118-167.201 166.153 1.00 54.51 C ANISOU 333 CA ALA A 42 7215 5873 7621 -253 -2067 486 C ATOM 334 C ALA A 42 -99.320-167.925 165.563 1.00 69.10 C ANISOU 334 C ALA A 42 9081 7787 9389 -160 -1868 494 C ATOM 335 O ALA A 42 -99.394-169.161 165.604 1.00 65.25 O ANISOU 335 O ALA A 42 8578 7309 8904 -136 -1931 578 O ATOM 336 CB ALA A 42 -98.425-166.696 167.562 1.00 50.97 C ANISOU 336 CB ALA A 42 7023 5438 6906 -402 -2164 432 C ATOM 337 N TYR A 43 -100.268-167.169 165.004 1.00 55.91 N ANISOU 337 N TYR A 43 7432 6144 7665 -109 -1644 412 N ATOM 338 CA TYR A 43 -101.400-167.776 164.314 1.00 59.81 C ANISOU 338 CA TYR A 43 7913 6695 8118 -22 -1470 421 C ATOM 339 C TYR A 43 -100.937-168.616 163.130 1.00 61.78 C ANISOU 339 C TYR A 43 7985 6934 8556 70 -1452 489 C ATOM 340 O TYR A 43 -101.407-169.745 162.945 1.00 63.98 O ANISOU 340 O TYR A 43 8261 7240 8808 105 -1435 537 O ATOM 341 CB TYR A 43 -102.371-166.676 163.872 1.00 52.17 C ANISOU 341 CB TYR A 43 6970 5736 7118 18 -1271 332 C ATOM 342 CG TYR A 43 -103.622-167.137 163.156 1.00 65.32 C ANISOU 342 CG TYR A 43 8610 7451 8757 99 -1111 339 C ATOM 343 CD1 TYR A 43 -104.361-168.217 163.617 1.00 60.94 C ANISOU 343 CD1 TYR A 43 8121 6951 8083 82 -1103 371 C ATOM 344 CD2 TYR A 43 -104.080-166.462 162.032 1.00 75.04 C ANISOU 344 CD2 TYR A 43 9758 8670 10084 178 -983 325 C ATOM 345 CE1 TYR A 43 -105.520-168.627 162.958 1.00 70.94 C ANISOU 345 CE1 TYR A 43 9349 8259 9345 145 -969 376 C ATOM 346 CE2 TYR A 43 -105.225-166.861 161.375 1.00 74.01 C ANISOU 346 CE2 TYR A 43 9600 8580 9940 240 -873 340 C ATOM 347 CZ TYR A 43 -105.941-167.940 161.840 1.00 77.19 C ANISOU 347 CZ TYR A 43 10048 9038 10241 225 -866 360 C ATOM 348 OH TYR A 43 -107.079-168.322 161.174 1.00 77.31 O ANISOU 348 OH TYR A 43 10021 9090 10264 277 -770 375 O ATOM 349 N MET A 44 -100.011-168.090 162.321 1.00 65.44 N ANISOU 349 N MET A 44 8305 7349 9209 99 -1440 485 N ATOM 350 CA MET A 44 -99.482-168.869 161.205 1.00 66.19 C ANISOU 350 CA MET A 44 8241 7426 9482 171 -1391 525 C ATOM 351 C MET A 44 -98.780-170.125 161.698 1.00 72.56 C ANISOU 351 C MET A 44 8992 8196 10382 168 -1556 595 C ATOM 352 O MET A 44 -98.896-171.191 161.087 1.00 58.79 O ANISOU 352 O MET A 44 7187 6447 8705 229 -1507 623 O ATOM 353 CB MET A 44 -98.513-168.028 160.373 1.00 57.39 C ANISOU 353 CB MET A 44 6990 6262 8553 175 -1333 503 C ATOM 354 CG MET A 44 -99.147-166.883 159.613 1.00 61.28 C ANISOU 354 CG MET A 44 7525 6768 8991 188 -1169 462 C ATOM 355 SD MET A 44 -100.484-167.419 158.541 1.00 70.92 S ANISOU 355 SD MET A 44 8791 8053 10102 261 -1002 473 S ATOM 356 CE MET A 44 -101.858-166.700 159.409 1.00 57.79 C ANISOU 356 CE MET A 44 7280 6421 8256 251 -991 434 C ATOM 357 N PHE A 45 -98.035-170.013 162.799 1.00 67.34 N ANISOU 357 N PHE A 45 8354 7495 9736 92 -1770 626 N ATOM 358 CA PHE A 45 -97.352-171.177 163.353 1.00 62.16 C ANISOU 358 CA PHE A 45 7646 6782 9189 85 -1976 716 C ATOM 359 C PHE A 45 -98.349-172.246 163.780 1.00 72.67 C ANISOU 359 C PHE A 45 9118 8151 10341 85 -1983 765 C ATOM 360 O PHE A 45 -98.131-173.441 163.544 1.00 57.36 O ANISOU 360 O PHE A 45 7102 6163 8528 136 -2032 828 O ATOM 361 CB PHE A 45 -96.480-170.741 164.529 1.00 54.55 C ANISOU 361 CB PHE A 45 6718 5773 8236 -22 -2242 752 C ATOM 362 CG PHE A 45 -95.639-171.839 165.125 1.00 59.60 C ANISOU 362 CG PHE A 45 7285 6330 9031 -34 -2510 870 C ATOM 363 CD1 PHE A 45 -94.579-172.391 164.423 1.00 62.44 C ANISOU 363 CD1 PHE A 45 7379 6596 9751 48 -2543 900 C ATOM 364 CD2 PHE A 45 -95.881-172.278 166.416 1.00 64.22 C ANISOU 364 CD2 PHE A 45 8071 6919 9410 -138 -2734 951 C ATOM 365 CE1 PHE A 45 -93.796-173.382 164.991 1.00 55.78 C ANISOU 365 CE1 PHE A 45 6445 5650 9099 48 -2811 1016 C ATOM 366 CE2 PHE A 45 -95.105-173.266 166.987 1.00 66.73 C ANISOU 366 CE2 PHE A 45 8332 7143 9880 -156 -3021 1084 C ATOM 367 CZ PHE A 45 -94.061-173.818 166.278 1.00 61.21 C ANISOU 367 CZ PHE A 45 7341 6337 9580 -53 -3071 1120 C ATOM 368 N LEU A 46 -99.455-171.833 164.404 1.00 74.04 N ANISOU 368 N LEU A 46 9493 8401 10239 25 -1918 731 N ATOM 369 CA LEU A 46 -100.487-172.788 164.797 1.00 67.29 C ANISOU 369 CA LEU A 46 8770 7587 9210 9 -1891 772 C ATOM 370 C LEU A 46 -101.036-173.525 163.582 1.00 70.92 C ANISOU 370 C LEU A 46 9128 8058 9762 115 -1721 764 C ATOM 371 O LEU A 46 -101.144-174.757 163.581 1.00 63.68 O ANISOU 371 O LEU A 46 8206 7109 8880 132 -1771 832 O ATOM 372 CB LEU A 46 -101.608-172.067 165.542 1.00 68.22 C ANISOU 372 CB LEU A 46 9089 7783 9051 -71 -1787 705 C ATOM 373 CG LEU A 46 -102.802-172.918 165.978 1.00 66.82 C ANISOU 373 CG LEU A 46 9048 7657 8685 -108 -1714 734 C ATOM 374 CD1 LEU A 46 -102.362-173.935 167.004 1.00 62.58 C ANISOU 374 CD1 LEU A 46 8624 7079 8077 -201 -1942 855 C ATOM 375 CD2 LEU A 46 -103.896-172.036 166.541 1.00 68.97 C ANISOU 375 CD2 LEU A 46 9468 7996 8742 -171 -1547 633 C ATOM 376 N LEU A 47 -101.358-172.780 162.523 1.00 58.93 N ANISOU 376 N LEU A 47 7536 6572 8283 176 -1532 687 N ATOM 377 CA LEU A 47 -101.894-173.392 161.313 1.00 58.47 C ANISOU 377 CA LEU A 47 7408 6528 8281 254 -1381 673 C ATOM 378 C LEU A 47 -100.884-174.326 160.661 1.00 70.00 C ANISOU 378 C LEU A 47 8720 7905 9970 310 -1421 701 C ATOM 379 O LEU A 47 -101.264-175.355 160.093 1.00 62.54 O ANISOU 379 O LEU A 47 7760 6947 9055 350 -1363 709 O ATOM 380 CB LEU A 47 -102.326-172.309 160.331 1.00 52.26 C ANISOU 380 CB LEU A 47 6590 5781 7483 289 -1210 604 C ATOM 381 CG LEU A 47 -103.495-171.448 160.799 1.00 69.43 C ANISOU 381 CG LEU A 47 8878 8017 9484 259 -1136 564 C ATOM 382 CD1 LEU A 47 -103.633-170.249 159.885 1.00 63.42 C ANISOU 382 CD1 LEU A 47 8073 7258 8766 294 -1021 518 C ATOM 383 CD2 LEU A 47 -104.767-172.273 160.816 1.00 62.73 C ANISOU 383 CD2 LEU A 47 8089 7218 8527 262 -1072 578 C ATOM 384 N ILE A 48 -99.597-173.978 160.713 1.00 63.29 N ANISOU 384 N ILE A 48 7751 6991 9307 313 -1508 705 N ATOM 385 CA ILE A 48 -98.572-174.847 160.141 1.00 62.63 C ANISOU 385 CA ILE A 48 7495 6808 9493 373 -1529 717 C ATOM 386 C ILE A 48 -98.471-176.138 160.942 1.00 68.51 C ANISOU 386 C ILE A 48 8262 7482 10286 371 -1713 808 C ATOM 387 O ILE A 48 -98.514-177.241 160.387 1.00 62.04 O ANISOU 387 O ILE A 48 7389 6604 9580 428 -1664 810 O ATOM 388 CB ILE A 48 -97.219-174.114 160.078 1.00 66.35 C ANISOU 388 CB ILE A 48 7804 7220 10187 368 -1581 702 C ATOM 389 CG1 ILE A 48 -97.276-172.940 159.094 1.00 68.48 C ANISOU 389 CG1 ILE A 48 8050 7540 10430 367 -1375 621 C ATOM 390 CG2 ILE A 48 -96.093-175.082 159.697 1.00 56.84 C ANISOU 390 CG2 ILE A 48 6391 5891 9317 431 -1618 714 C ATOM 391 CD1 ILE A 48 -96.169-171.920 159.308 1.00 66.29 C ANISOU 391 CD1 ILE A 48 7660 7221 10305 325 -1439 611 C ATOM 392 N MET A 49 -98.358-176.018 162.266 1.00 69.20 N ANISOU 392 N MET A 49 8452 7567 10276 293 -1932 887 N ATOM 393 CA MET A 49 -98.136-177.190 163.103 1.00 69.57 C ANISOU 393 CA MET A 49 8532 7528 10371 273 -2152 1004 C ATOM 394 C MET A 49 -99.333-178.139 163.102 1.00 78.11 C ANISOU 394 C MET A 49 9753 8640 11285 267 -2076 1030 C ATOM 395 O MET A 49 -99.167-179.340 163.340 1.00 71.52 O ANISOU 395 O MET A 49 8909 7708 10557 282 -2197 1116 O ATOM 396 CB MET A 49 -97.794-176.741 164.524 1.00 66.40 C ANISOU 396 CB MET A 49 8256 7129 9845 157 -2411 1086 C ATOM 397 CG MET A 49 -96.495-175.951 164.614 1.00 81.09 C ANISOU 397 CG MET A 49 9961 8935 11917 150 -2543 1078 C ATOM 398 SD MET A 49 -95.060-176.948 164.150 1.00 79.43 S ANISOU 398 SD MET A 49 9444 8542 12193 254 -2682 1138 S ATOM 399 CE MET A 49 -94.950-178.035 165.569 1.00 80.44 C ANISOU 399 CE MET A 49 9708 8579 12277 177 -3064 1333 C ATOM 400 N LEU A 50 -100.541-177.633 162.849 1.00 76.89 N ANISOU 400 N LEU A 50 9715 8606 10894 244 -1887 963 N ATOM 401 CA LEU A 50 -101.709-178.502 162.754 1.00 66.72 C ANISOU 401 CA LEU A 50 8529 7348 9473 232 -1800 979 C ATOM 402 C LEU A 50 -102.018-178.889 161.318 1.00 72.54 C ANISOU 402 C LEU A 50 9163 8081 10318 320 -1605 899 C ATOM 403 O LEU A 50 -102.383-180.044 161.047 1.00 79.77 O ANISOU 403 O LEU A 50 10088 8944 11276 336 -1593 923 O ATOM 404 CB LEU A 50 -102.929-177.823 163.373 1.00 65.49 C ANISOU 404 CB LEU A 50 8546 7314 9023 147 -1712 954 C ATOM 405 CG LEU A 50 -102.919-177.549 164.877 1.00 70.79 C ANISOU 405 CG LEU A 50 9393 8004 9500 23 -1864 1017 C ATOM 406 CD1 LEU A 50 -104.233-176.924 165.293 1.00 62.56 C ANISOU 406 CD1 LEU A 50 8496 7074 8201 -48 -1697 954 C ATOM 407 CD2 LEU A 50 -102.679-178.837 165.633 1.00 76.20 C ANISOU 407 CD2 LEU A 50 10156 8602 10193 -32 -2062 1157 C ATOM 408 N GLY A 51 -101.864-177.949 160.383 1.00 60.35 N ANISOU 408 N GLY A 51 7538 6583 8809 362 -1458 807 N ATOM 409 CA GLY A 51 -102.130-178.147 158.976 1.00 63.05 C ANISOU 409 CA GLY A 51 7818 6932 9207 417 -1274 727 C ATOM 410 C GLY A 51 -101.239-179.118 158.248 1.00 66.07 C ANISOU 410 C GLY A 51 8074 7194 9836 481 -1252 702 C ATOM 411 O GLY A 51 -101.732-179.966 157.507 1.00 75.69 O ANISOU 411 O GLY A 51 9310 8391 11060 498 -1157 664 O ATOM 412 N PHE A 52 -99.919-179.021 158.444 1.00 62.81 N ANISOU 412 N PHE A 52 7524 6693 9650 513 -1335 712 N ATOM 413 CA PHE A 52 -99.027-179.941 157.738 1.00 77.06 C ANISOU 413 CA PHE A 52 9176 8362 11741 584 -1285 669 C ATOM 414 C PHE A 52 -99.236-181.393 158.159 1.00 66.97 C ANISOU 414 C PHE A 52 7927 6975 10542 602 -1396 732 C ATOM 415 O PHE A 52 -99.449-182.241 157.273 1.00 70.93 O ANISOU 415 O PHE A 52 8416 7420 11115 638 -1260 659 O ATOM 416 CB PHE A 52 -97.563-179.513 157.893 1.00 66.97 C ANISOU 416 CB PHE A 52 7706 7001 10740 616 -1353 669 C ATOM 417 CG PHE A 52 -96.598-180.503 157.329 1.00 72.10 C ANISOU 417 CG PHE A 52 8168 7485 11741 697 -1305 622 C ATOM 418 CD1 PHE A 52 -96.452-180.632 155.961 1.00 78.03 C ANISOU 418 CD1 PHE A 52 8858 8220 12569 729 -1029 483 C ATOM 419 CD2 PHE A 52 -95.863-181.324 158.164 1.00 84.11 C ANISOU 419 CD2 PHE A 52 9582 8857 13518 735 -1535 717 C ATOM 420 CE1 PHE A 52 -95.569-181.554 155.431 1.00 80.63 C ANISOU 420 CE1 PHE A 52 9011 8384 13240 804 -944 411 C ATOM 421 CE2 PHE A 52 -94.977-182.247 157.637 1.00 82.76 C ANISOU 421 CE2 PHE A 52 9212 8509 13725 825 -1480 664 C ATOM 422 CZ PHE A 52 -94.831-182.362 156.273 1.00 79.51 C ANISOU 422 CZ PHE A 52 8731 8080 13401 863 -1166 499 C ATOM 423 N PRO A 53 -99.165-181.763 159.446 1.00 70.31 N ANISOU 423 N PRO A 53 8403 7355 10957 569 -1641 865 N ATOM 424 CA PRO A 53 -99.289-183.193 159.783 1.00 80.71 C ANISOU 424 CA PRO A 53 9746 8541 12380 584 -1753 940 C ATOM 425 C PRO A 53 -100.598-183.811 159.329 1.00 78.51 C ANISOU 425 C PRO A 53 9608 8313 11908 552 -1620 906 C ATOM 426 O PRO A 53 -100.594-184.897 158.738 1.00 75.78 O ANISOU 426 O PRO A 53 9227 7851 11715 597 -1563 868 O ATOM 427 CB PRO A 53 -99.157-183.203 161.313 1.00 72.46 C ANISOU 427 CB PRO A 53 8796 7479 11256 511 -2044 1106 C ATOM 428 CG PRO A 53 -98.464-181.952 161.655 1.00 73.45 C ANISOU 428 CG PRO A 53 8865 7669 11376 490 -2104 1098 C ATOM 429 CD PRO A 53 -98.952-180.947 160.654 1.00 70.83 C ANISOU 429 CD PRO A 53 8530 7474 10909 500 -1835 956 C ATOM 430 N ILE A 54 -101.721-183.136 159.577 1.00 69.18 N ANISOU 430 N ILE A 54 8575 7294 10417 475 -1566 910 N ATOM 431 CA ILE A 54 -103.021-183.692 159.217 1.00 73.41 C ANISOU 431 CA ILE A 54 9225 7882 10788 433 -1462 889 C ATOM 432 C ILE A 54 -103.115-183.929 157.714 1.00 77.30 C ANISOU 432 C ILE A 54 9658 8360 11353 482 -1262 751 C ATOM 433 O ILE A 54 -103.582-184.984 157.267 1.00 76.94 O ANISOU 433 O ILE A 54 9647 8246 11341 477 -1220 726 O ATOM 434 CB ILE A 54 -104.144-182.771 159.720 1.00 89.06 C ANISOU 434 CB ILE A 54 11331 10033 12474 351 -1422 904 C ATOM 435 CG1 ILE A 54 -104.100-182.684 161.247 1.00 96.98 C ANISOU 435 CG1 ILE A 54 12440 11042 13367 273 -1602 1028 C ATOM 436 CG2 ILE A 54 -105.495-183.280 159.252 1.00 96.94 C ANISOU 436 CG2 ILE A 54 12406 11084 13342 308 -1312 876 C ATOM 437 CD1 ILE A 54 -105.187-181.825 161.846 1.00101.16 C ANISOU 437 CD1 ILE A 54 13092 11719 13624 188 -1532 1022 C ATOM 438 N ASN A 55 -102.665-182.966 156.908 1.00 70.25 N ANISOU 438 N ASN A 55 8692 7526 10475 513 -1135 659 N ATOM 439 CA ASN A 55 -102.811-183.128 155.464 1.00 66.74 C ANISOU 439 CA ASN A 55 8237 7082 10041 528 -939 530 C ATOM 440 C ASN A 55 -101.755-184.062 154.885 1.00 76.54 C ANISOU 440 C ASN A 55 9364 8151 11568 596 -878 455 C ATOM 441 O ASN A 55 -102.042-184.823 153.954 1.00 71.37 O ANISOU 441 O ASN A 55 8746 7445 10929 592 -751 358 O ATOM 442 CB ASN A 55 -102.765-181.769 154.761 1.00 61.33 C ANISOU 442 CB ASN A 55 7543 6514 9245 517 -817 471 C ATOM 443 CG ASN A 55 -103.989-180.917 155.063 1.00 72.36 C ANISOU 443 CG ASN A 55 9045 8060 10388 461 -838 517 C ATOM 444 OD1 ASN A 55 -105.053-181.105 154.475 1.00 69.15 O ANISOU 444 OD1 ASN A 55 8718 7711 9847 421 -783 493 O ATOM 445 ND2 ASN A 55 -103.841-179.976 155.988 1.00 73.92 N ANISOU 445 ND2 ASN A 55 9236 8310 10538 453 -922 576 N ATOM 446 N PHE A 56 -100.530-184.023 155.412 1.00 66.16 N ANISOU 446 N PHE A 56 7903 6735 10498 655 -966 489 N ATOM 447 CA PHE A 56 -99.520-184.955 154.929 1.00 72.04 C ANISOU 447 CA PHE A 56 8505 7291 11577 733 -905 413 C ATOM 448 C PHE A 56 -99.862-186.385 155.328 1.00 77.80 C ANISOU 448 C PHE A 56 9278 7876 12405 747 -1013 464 C ATOM 449 O PHE A 56 -99.686-187.316 154.533 1.00 70.02 O ANISOU 449 O PHE A 56 8262 6758 11584 784 -883 353 O ATOM 450 CB PHE A 56 -98.140-184.564 155.454 1.00 65.06 C ANISOU 450 CB PHE A 56 7421 6322 10977 794 -1003 452 C ATOM 451 CG PHE A 56 -97.047-185.501 155.027 1.00 75.24 C ANISOU 451 CG PHE A 56 8517 7393 12677 889 -939 374 C ATOM 452 CD1 PHE A 56 -96.449-185.369 153.785 1.00 81.43 C ANISOU 452 CD1 PHE A 56 9200 8144 13594 915 -653 194 C ATOM 453 CD2 PHE A 56 -96.621-186.518 155.865 1.00 86.79 C ANISOU 453 CD2 PHE A 56 9900 8672 14403 945 -1159 480 C ATOM 454 CE1 PHE A 56 -95.445-186.232 153.388 1.00 90.71 C ANISOU 454 CE1 PHE A 56 10180 9105 15179 1006 -556 98 C ATOM 455 CE2 PHE A 56 -95.619-187.384 155.475 1.00 87.48 C ANISOU 455 CE2 PHE A 56 9783 8533 14922 1048 -1100 403 C ATOM 456 CZ PHE A 56 -95.029-187.240 154.235 1.00 91.39 C ANISOU 456 CZ PHE A 56 10160 8996 15569 1083 -783 200 C ATOM 457 N LEU A 57 -100.358-186.576 156.555 1.00 76.48 N ANISOU 457 N LEU A 57 9200 7726 12134 705 -1241 629 N ATOM 458 CA LEU A 57 -100.750-187.908 157.000 1.00 77.84 C ANISOU 458 CA LEU A 57 9437 7759 12379 698 -1357 703 C ATOM 459 C LEU A 57 -101.860-188.483 156.131 1.00 82.65 C ANISOU 459 C LEU A 57 10172 8401 12829 648 -1196 606 C ATOM 460 O LEU A 57 -101.918-189.701 155.929 1.00 79.70 O ANISOU 460 O LEU A 57 9810 7863 12610 665 -1197 585 O ATOM 461 CB LEU A 57 -101.181-187.864 158.466 1.00 76.36 C ANISOU 461 CB LEU A 57 9364 7615 12035 624 -1606 901 C ATOM 462 CG LEU A 57 -101.465-189.186 159.179 1.00100.50 C ANISOU 462 CG LEU A 57 12500 10515 15169 597 -1776 1031 C ATOM 463 CD1 LEU A 57 -100.255-190.114 159.125 1.00 98.64 C ANISOU 463 CD1 LEU A 57 12098 10019 15364 708 -1875 1043 C ATOM 464 CD2 LEU A 57 -101.879-188.920 160.620 1.00109.28 C ANISOU 464 CD2 LEU A 57 13760 11704 16059 492 -1992 1221 C ATOM 465 N THR A 58 -102.746-187.628 155.611 1.00 80.60 N ANISOU 465 N THR A 58 10005 8337 12281 582 -1074 551 N ATOM 466 CA THR A 58 -103.773-188.092 154.681 1.00 79.77 C ANISOU 466 CA THR A 58 10009 8268 12031 524 -941 455 C ATOM 467 C THR A 58 -103.145-188.700 153.434 1.00 82.29 C ANISOU 467 C THR A 58 10278 8458 12531 570 -758 278 C ATOM 468 O THR A 58 -103.551-189.773 152.977 1.00 80.97 O ANISOU 468 O THR A 58 10174 8184 12408 547 -715 213 O ATOM 469 CB THR A 58 -104.695-186.936 154.295 1.00 73.10 C ANISOU 469 CB THR A 58 9242 7642 10890 457 -867 436 C ATOM 470 OG1 THR A 58 -105.459-186.527 155.435 1.00 72.59 O ANISOU 470 OG1 THR A 58 9237 7681 10662 404 -999 573 O ATOM 471 CG2 THR A 58 -105.639-187.364 153.177 1.00 71.96 C ANISOU 471 CG2 THR A 58 9197 7528 10616 391 -751 333 C ATOM 472 N LEU A 59 -102.160-188.011 152.856 1.00 83.69 N ANISOU 472 N LEU A 59 10346 8640 12811 623 -631 187 N ATOM 473 CA LEU A 59 -101.465-188.556 151.697 1.00 84.17 C ANISOU 473 CA LEU A 59 10357 8572 13051 658 -415 -1 C ATOM 474 C LEU A 59 -100.670-189.796 152.074 1.00 90.96 C ANISOU 474 C LEU A 59 11097 9175 14289 750 -470 -6 C ATOM 475 O LEU A 59 -100.507-190.710 151.256 1.00 96.49 O ANISOU 475 O LEU A 59 11806 9726 15129 764 -313 -160 O ATOM 476 CB LEU A 59 -100.545-187.505 151.085 1.00 72.58 C ANISOU 476 CB LEU A 59 8790 7165 11624 682 -252 -86 C ATOM 477 CG LEU A 59 -101.172-186.165 150.689 1.00 84.63 C ANISOU 477 CG LEU A 59 10420 8919 12818 601 -206 -69 C ATOM 478 CD1 LEU A 59 -100.128-185.229 150.101 1.00 81.12 C ANISOU 478 CD1 LEU A 59 9871 8499 12452 618 -38 -147 C ATOM 479 CD2 LEU A 59 -102.305-186.384 149.705 1.00 82.28 C ANISOU 479 CD2 LEU A 59 10316 8700 12247 500 -114 -148 C ATOM 480 N TYR A 60 -100.181-189.855 153.313 1.00 83.97 N ANISOU 480 N TYR A 60 10111 8223 13573 806 -701 162 N ATOM 481 CA TYR A 60 -99.285-190.935 153.706 1.00 85.70 C ANISOU 481 CA TYR A 60 10184 8176 14203 906 -791 183 C ATOM 482 C TYR A 60 -100.046-192.232 153.954 1.00 90.86 C ANISOU 482 C TYR A 60 10958 8695 14869 877 -885 229 C ATOM 483 O TYR A 60 -99.628-193.300 153.495 1.00 87.33 O ANISOU 483 O TYR A 60 10452 8020 14710 939 -805 124 O ATOM 484 CB TYR A 60 -98.491-190.536 154.947 1.00 81.69 C ANISOU 484 CB TYR A 60 9541 7637 13863 958 -1050 368 C ATOM 485 CG TYR A 60 -97.433-191.546 155.309 1.00 80.80 C ANISOU 485 CG TYR A 60 9238 7232 14230 1074 -1168 402 C ATOM 486 CD1 TYR A 60 -96.244-191.614 154.597 1.00 91.85 C ANISOU 486 CD1 TYR A 60 10403 8485 16009 1180 -993 248 C ATOM 487 CD2 TYR A 60 -97.630-192.445 156.347 1.00 89.18 C ANISOU 487 CD2 TYR A 60 10349 8152 15384 1073 -1449 591 C ATOM 488 CE1 TYR A 60 -95.273-192.550 154.915 1.00100.79 C ANISOU 488 CE1 TYR A 60 11327 9326 17642 1301 -1104 276 C ATOM 489 CE2 TYR A 60 -96.668-193.382 156.676 1.00 92.71 C ANISOU 489 CE2 TYR A 60 10615 8307 16303 1185 -1589 641 C ATOM 490 CZ TYR A 60 -95.491-193.431 155.956 1.00 97.88 C ANISOU 490 CZ TYR A 60 11010 8810 17371 1308 -1419 480 C ATOM 491 OH TYR A 60 -94.530-194.362 156.282 1.00115.02 O ANISOU 491 OH TYR A 60 12967 10669 20067 1434 -1563 528 O ATOM 492 N VAL A 61 -101.169-192.162 154.674 1.00 89.92 N ANISOU 492 N VAL A 61 11007 8706 14454 778 -1038 377 N ATOM 493 CA VAL A 61 -101.927-193.372 154.959 1.00 84.22 C ANISOU 493 CA VAL A 61 10403 7859 13738 730 -1129 436 C ATOM 494 C VAL A 61 -102.570-193.945 153.705 1.00 89.82 C ANISOU 494 C VAL A 61 11211 8546 14372 682 -910 237 C ATOM 495 O VAL A 61 -102.875-195.142 153.664 1.00100.98 O ANISOU 495 O VAL A 61 12681 9779 15908 667 -937 225 O ATOM 496 CB VAL A 61 -102.990-193.110 156.040 1.00 88.03 C ANISOU 496 CB VAL A 61 11036 8495 13918 617 -1313 634 C ATOM 497 CG1 VAL A 61 -102.327-192.610 157.316 1.00 89.67 C ANISOU 497 CG1 VAL A 61 11185 8711 14175 642 -1542 825 C ATOM 498 CG2 VAL A 61 -104.041-192.126 155.533 1.00 78.33 C ANISOU 498 CG2 VAL A 61 9910 7535 12316 524 -1181 571 C ATOM 499 N THR A 62 -102.793-193.125 152.677 1.00 87.67 N ANISOU 499 N THR A 62 10976 8444 13891 642 -707 87 N ATOM 500 CA THR A 62 -103.312-193.656 151.422 1.00 91.71 C ANISOU 500 CA THR A 62 11602 8928 14316 579 -510 -111 C ATOM 501 C THR A 62 -102.272-194.528 150.726 1.00 86.81 C ANISOU 501 C THR A 62 10885 8051 14049 669 -342 -296 C ATOM 502 O THR A 62 -102.629-195.473 150.011 1.00 94.16 O ANISOU 502 O THR A 62 11916 8854 15008 626 -234 -440 O ATOM 503 CB THR A 62 -103.771-192.504 150.523 1.00 80.56 C ANISOU 503 CB THR A 62 10271 7758 12580 501 -365 -200 C ATOM 504 OG1 THR A 62 -104.832-191.794 151.175 1.00 78.15 O ANISOU 504 OG1 THR A 62 10041 7661 11993 425 -515 -39 O ATOM 505 CG2 THR A 62 -104.276-193.016 149.183 1.00 84.15 C ANISOU 505 CG2 THR A 62 10872 8189 12910 410 -182 -403 C ATOM 506 N VAL A 63 -100.987-194.250 150.954 1.00 75.53 N ANISOU 506 N VAL A 63 9254 6529 12915 792 -318 -300 N ATOM 507 CA VAL A 63 -99.926-195.062 150.367 1.00 85.22 C ANISOU 507 CA VAL A 63 10344 7490 14547 896 -143 -480 C ATOM 508 C VAL A 63 -99.847-196.431 151.041 1.00 94.32 C ANISOU 508 C VAL A 63 11458 8358 16022 959 -312 -400 C ATOM 509 O VAL A 63 -99.508-197.430 150.394 1.00 91.36 O ANISOU 509 O VAL A 63 11060 7743 15910 1003 -155 -579 O ATOM 510 CB VAL A 63 -98.585-194.306 150.449 1.00 81.83 C ANISOU 510 CB VAL A 63 9674 7046 14374 1005 -77 -497 C ATOM 511 CG1 VAL A 63 -97.449-195.154 149.906 1.00 74.24 C ANISOU 511 CG1 VAL A 63 8524 5788 13894 1124 119 -686 C ATOM 512 CG2 VAL A 63 -98.673-192.979 149.700 1.00 82.68 C ANISOU 512 CG2 VAL A 63 9840 7415 14161 928 108 -579 C ATOM 513 N GLN A 64 -100.176-196.511 152.330 1.00 94.81 N ANISOU 513 N GLN A 64 11532 8433 16061 953 -626 -134 N ATOM 514 CA GLN A 64 -100.001-197.739 153.096 1.00 99.14 C ANISOU 514 CA GLN A 64 12042 8700 16927 1010 -830 -10 C ATOM 515 C GLN A 64 -101.226-198.645 153.109 1.00 98.10 C ANISOU 515 C GLN A 64 12126 8529 16617 894 -883 18 C ATOM 516 O GLN A 64 -101.097-199.815 153.487 1.00 97.17 O ANISOU 516 O GLN A 64 11998 8137 16786 933 -1001 76 O ATOM 517 CB GLN A 64 -99.619-197.413 154.544 1.00106.36 C ANISOU 517 CB GLN A 64 12875 9623 17916 1046 -1163 281 C ATOM 518 CG GLN A 64 -98.187-196.959 154.726 1.00113.80 C ANISOU 518 CG GLN A 64 13548 10474 19215 1185 -1191 283 C ATOM 519 CD GLN A 64 -97.763-196.974 156.180 1.00115.55 C ANISOU 519 CD GLN A 64 13706 10626 19571 1212 -1575 579 C ATOM 520 OE1 GLN A 64 -98.599-197.035 157.083 1.00117.21 O ANISOU 520 OE1 GLN A 64 14102 10927 19504 1104 -1791 783 O ATOM 521 NE2 GLN A 64 -96.456-196.926 156.416 1.00111.34 N ANISOU 521 NE2 GLN A 64 12910 9926 19467 1345 -1663 603 N ATOM 522 N HIS A 65 -102.399-198.152 152.716 1.00 78.09 N ANISOU 522 N HIS A 65 9776 6245 13648 750 -814 -13 N ATOM 523 CA HIS A 65 -103.645-198.902 152.856 1.00 84.46 C ANISOU 523 CA HIS A 65 10772 7044 14275 620 -892 44 C ATOM 524 C HIS A 65 -104.328-198.998 151.499 1.00 94.45 C ANISOU 524 C HIS A 65 12171 8379 15338 523 -657 -201 C ATOM 525 O HIS A 65 -104.792-197.987 150.961 1.00 87.18 O ANISOU 525 O HIS A 65 11308 7719 14097 452 -563 -257 O ATOM 526 CB HIS A 65 -104.549-198.246 153.899 1.00 77.86 C ANISOU 526 CB HIS A 65 10023 6442 13117 517 -1087 283 C ATOM 527 CG HIS A 65 -103.937-198.198 155.265 1.00 84.70 C ANISOU 527 CG HIS A 65 10811 7240 14130 576 -1337 528 C ATOM 528 ND1 HIS A 65 -104.169-199.163 156.222 1.00 80.63 N ANISOU 528 ND1 HIS A 65 10361 6550 13724 539 -1552 723 N ATOM 529 CD2 HIS A 65 -103.080-197.311 155.826 1.00 90.80 C ANISOU 529 CD2 HIS A 65 11458 8088 14953 655 -1422 616 C ATOM 530 CE1 HIS A 65 -103.490-198.868 157.317 1.00 83.15 C ANISOU 530 CE1 HIS A 65 10613 6844 14134 587 -1770 926 C ATOM 531 NE2 HIS A 65 -102.822-197.749 157.103 1.00 87.39 N ANISOU 531 NE2 HIS A 65 11029 7533 14642 658 -1699 860 N ATOM 532 N LYS A 66 -104.407-200.220 150.961 1.00 94.77 N ANISOU 532 N LYS A 66 12272 8173 15562 510 -582 -340 N ATOM 533 CA LYS A 66 -104.895-200.407 149.598 1.00 93.76 C ANISOU 533 CA LYS A 66 12286 8074 15265 410 -355 -602 C ATOM 534 C LYS A 66 -106.359-200.004 149.450 1.00 87.87 C ANISOU 534 C LYS A 66 11713 7583 14093 229 -424 -544 C ATOM 535 O LYS A 66 -106.753-199.507 148.390 1.00 89.99 O ANISOU 535 O LYS A 66 12084 8004 14103 138 -278 -705 O ATOM 536 CB LYS A 66 -104.698-201.862 149.164 1.00 96.35 C ANISOU 536 CB LYS A 66 12653 8059 15896 426 -276 -762 C ATOM 537 CG LYS A 66 -104.965-202.116 147.684 1.00107.08 C ANISOU 537 CG LYS A 66 14169 9406 17110 325 -12 -1077 C ATOM 538 CD LYS A 66 -104.523-203.507 147.260 1.00122.31 C ANISOU 538 CD LYS A 66 16112 10959 19402 369 107 -1273 C ATOM 539 CE LYS A 66 -104.469-203.635 145.742 1.00127.15 C ANISOU 539 CE LYS A 66 16874 11550 19887 282 425 -1629 C ATOM 540 NZ LYS A 66 -103.420-202.760 145.137 1.00122.17 N ANISOU 540 NZ LYS A 66 16136 11004 19279 367 675 -1778 N ATOM 541 N LYS A 67 -107.176-200.201 150.490 1.00 75.29 N ANISOU 541 N LYS A 67 10149 6032 12425 165 -644 -313 N ATOM 542 CA LYS A 67 -108.606-199.966 150.355 1.00 87.54 C ANISOU 542 CA LYS A 67 11832 7787 13643 -7 -701 -267 C ATOM 543 C LYS A 67 -108.966-198.481 150.318 1.00 96.04 C ANISOU 543 C LYS A 67 12886 9191 14413 -32 -696 -210 C ATOM 544 O LYS A 67 -110.094-198.150 149.937 1.00 95.66 O ANISOU 544 O LYS A 67 12925 9317 14106 -165 -716 -214 O ATOM 545 CB LYS A 67 -109.371-200.663 151.487 1.00 97.29 C ANISOU 545 CB LYS A 67 13100 8956 14910 -81 -901 -47 C ATOM 546 CG LYS A 67 -109.073-202.155 151.620 1.00107.09 C ANISOU 546 CG LYS A 67 14371 9849 16469 -62 -938 -68 C ATOM 547 CD LYS A 67 -109.027-202.860 150.267 1.00118.00 C ANISOU 547 CD LYS A 67 15839 11078 17917 -97 -758 -360 C ATOM 548 CE LYS A 67 -110.282-203.682 150.006 1.00122.98 C ANISOU 548 CE LYS A 67 16621 11667 18438 -284 -810 -382 C ATOM 549 NZ LYS A 67 -110.164-204.527 148.780 1.00117.01 N ANISOU 549 NZ LYS A 67 15976 10712 17772 -327 -649 -673 N ATOM 550 N LEU A 68 -108.053-197.583 150.695 1.00 91.52 N ANISOU 550 N LEU A 68 12192 8693 13888 89 -682 -156 N ATOM 551 CA LEU A 68 -108.303-196.156 150.547 1.00 85.98 C ANISOU 551 CA LEU A 68 11473 8273 12922 72 -658 -127 C ATOM 552 C LEU A 68 -108.201-195.684 149.104 1.00 86.17 C ANISOU 552 C LEU A 68 11565 8377 12800 35 -471 -341 C ATOM 553 O LEU A 68 -108.826-194.676 148.757 1.00 81.48 O ANISOU 553 O LEU A 68 11010 8009 11941 -31 -474 -320 O ATOM 554 CB LEU A 68 -107.325-195.347 151.404 1.00 80.70 C ANISOU 554 CB LEU A 68 10663 7646 12354 200 -709 -7 C ATOM 555 CG LEU A 68 -107.413-195.507 152.926 1.00 78.79 C ANISOU 555 CG LEU A 68 10384 7379 12175 214 -916 232 C ATOM 556 CD1 LEU A 68 -106.358-194.654 153.617 1.00 66.17 C ANISOU 556 CD1 LEU A 68 8658 5820 10664 326 -969 321 C ATOM 557 CD2 LEU A 68 -108.807-195.158 153.425 1.00 76.21 C ANISOU 557 CD2 LEU A 68 10141 7242 11574 82 -998 355 C ATOM 558 N ARG A 69 -107.449-196.387 148.254 1.00 88.70 N ANISOU 558 N ARG A 69 11909 8508 13285 67 -304 -545 N ATOM 559 CA ARG A 69 -107.216-195.943 146.880 1.00 92.36 C ANISOU 559 CA ARG A 69 12464 9038 13591 16 -96 -758 C ATOM 560 C ARG A 69 -108.381-196.337 145.969 1.00 94.94 C ANISOU 560 C ARG A 69 12993 9413 13667 -165 -102 -859 C ATOM 561 O ARG A 69 -108.224-197.031 144.966 1.00102.23 O ANISOU 561 O ARG A 69 14042 10207 14594 -229 50 -1078 O ATOM 562 CB ARG A 69 -105.893-196.498 146.366 1.00 85.71 C ANISOU 562 CB ARG A 69 11559 7971 13036 117 122 -956 C ATOM 563 CG ARG A 69 -104.702-196.132 147.232 1.00 85.95 C ANISOU 563 CG ARG A 69 11363 7938 13355 292 103 -855 C ATOM 564 CD ARG A 69 -103.374-196.455 146.562 1.00 85.52 C ANISOU 564 CD ARG A 69 11211 7688 13592 389 360 -1072 C ATOM 565 NE ARG A 69 -103.218-197.885 146.314 1.00 97.32 N ANISOU 565 NE ARG A 69 12733 8889 15354 409 432 -1217 N ATOM 566 CZ ARG A 69 -102.728-198.746 147.200 1.00105.69 C ANISOU 566 CZ ARG A 69 13650 9706 16802 531 305 -1124 C ATOM 567 NH1 ARG A 69 -102.621-200.030 146.886 1.00 99.82 N ANISOU 567 NH1 ARG A 69 12942 8678 16308 545 382 -1270 N ATOM 568 NH2 ARG A 69 -102.348-198.319 148.398 1.00 97.93 N ANISOU 568 NH2 ARG A 69 12501 8754 15952 632 91 -882 N ATOM 569 N THR A 70 -109.560-195.845 146.319 1.00 88.15 N ANISOU 569 N THR A 70 12160 8741 12591 -256 -278 -702 N ATOM 570 CA THR A 70 -110.767-195.975 145.521 1.00 97.84 C ANISOU 570 CA THR A 70 13548 10057 13571 -435 -338 -755 C ATOM 571 C THR A 70 -111.070-194.665 144.799 1.00100.47 C ANISOU 571 C THR A 70 13934 10628 13611 -496 -331 -749 C ATOM 572 O THR A 70 -110.708-193.589 145.285 1.00 93.66 O ANISOU 572 O THR A 70 12958 9895 12732 -404 -341 -634 O ATOM 573 CB THR A 70 -111.960-196.359 146.399 1.00 94.19 C ANISOU 573 CB THR A 70 13052 9625 13110 -503 -545 -579 C ATOM 574 OG1 THR A 70 -112.147-195.364 147.413 1.00 98.18 O ANISOU 574 OG1 THR A 70 13422 10301 13582 -436 -643 -372 O ATOM 575 CG2 THR A 70 -111.719-197.704 147.060 1.00 93.02 C ANISOU 575 CG2 THR A 70 12883 9225 13235 -468 -566 -570 C ATOM 576 N PRO A 71 -111.726-194.724 143.634 1.00101.19 N ANISOU 576 N PRO A 71 14208 10770 13470 -660 -331 -865 N ATOM 577 CA PRO A 71 -111.960-193.489 142.858 1.00 89.88 C ANISOU 577 CA PRO A 71 12850 9543 11758 -729 -342 -848 C ATOM 578 C PRO A 71 -112.712-192.399 143.619 1.00 90.74 C ANISOU 578 C PRO A 71 12822 9848 11807 -696 -524 -617 C ATOM 579 O PRO A 71 -112.402-191.215 143.443 1.00 91.23 O ANISOU 579 O PRO A 71 12860 10042 11761 -657 -499 -565 O ATOM 580 CB PRO A 71 -112.761-193.993 141.649 1.00 93.08 C ANISOU 580 CB PRO A 71 13486 9942 11937 -938 -386 -981 C ATOM 581 CG PRO A 71 -112.362-195.426 141.502 1.00 85.25 C ANISOU 581 CG PRO A 71 12567 8708 11115 -951 -266 -1163 C ATOM 582 CD PRO A 71 -112.153-195.931 142.902 1.00 87.84 C ANISOU 582 CD PRO A 71 12686 8930 11760 -798 -316 -1031 C ATOM 583 N LEU A 72 -113.671-192.762 144.473 1.00 80.32 N ANISOU 583 N LEU A 72 11411 8539 10569 -713 -689 -484 N ATOM 584 CA LEU A 72 -114.413-191.786 145.258 1.00 77.68 C ANISOU 584 CA LEU A 72 10934 8371 10208 -681 -827 -288 C ATOM 585 C LEU A 72 -113.543-191.042 146.270 1.00 86.12 C ANISOU 585 C LEU A 72 11857 9473 11392 -512 -764 -191 C ATOM 586 O LEU A 72 -113.974-189.998 146.777 1.00 81.33 O ANISOU 586 O LEU A 72 11154 9011 10739 -479 -837 -60 O ATOM 587 CB LEU A 72 -115.580-192.472 145.978 1.00 83.82 C ANISOU 587 CB LEU A 72 11644 9133 11070 -751 -969 -189 C ATOM 588 CG LEU A 72 -116.798-191.607 146.313 1.00 94.49 C ANISOU 588 CG LEU A 72 12884 10657 12362 -794 -1119 -38 C ATOM 589 CD1 LEU A 72 -117.252-190.804 145.095 1.00 94.83 C ANISOU 589 CD1 LEU A 72 13012 10814 12204 -884 -1200 -66 C ATOM 590 CD2 LEU A 72 -117.933-192.477 146.834 1.00 90.95 C ANISOU 590 CD2 LEU A 72 12381 10168 12008 -896 -1224 23 C ATOM 591 N ASN A 73 -112.340-191.538 146.571 1.00 82.14 N ANISOU 591 N ASN A 73 11329 8828 11051 -408 -639 -256 N ATOM 592 CA ASN A 73 -111.437-190.875 147.503 1.00 77.72 C ANISOU 592 CA ASN A 73 10635 8286 10609 -262 -604 -169 C ATOM 593 C ASN A 73 -110.412-189.982 146.816 1.00 74.24 C ANISOU 593 C ASN A 73 10202 7888 10117 -208 -465 -248 C ATOM 594 O ASN A 73 -109.669-189.281 147.512 1.00 65.17 O ANISOU 594 O ASN A 73 8939 6768 9056 -98 -448 -177 O ATOM 595 CB ASN A 73 -110.694-191.907 148.367 1.00 77.83 C ANISOU 595 CB ASN A 73 10586 8110 10878 -175 -590 -158 C ATOM 596 CG ASN A 73 -111.588-192.563 149.397 1.00 79.43 C ANISOU 596 CG ASN A 73 10761 8285 11133 -219 -730 -22 C ATOM 597 OD1 ASN A 73 -112.673-192.072 149.696 1.00 82.56 O ANISOU 597 OD1 ASN A 73 11141 8825 11403 -287 -820 77 O ATOM 598 ND2 ASN A 73 -111.128-193.682 149.952 1.00 88.86 N ANISOU 598 ND2 ASN A 73 11945 9283 12532 -182 -744 -13 N ATOM 599 N TYR A 74 -110.340-189.997 145.480 1.00 68.48 N ANISOU 599 N TYR A 74 9618 7159 9241 -297 -365 -395 N ATOM 600 CA TYR A 74 -109.353-189.176 144.782 1.00 70.90 C ANISOU 600 CA TYR A 74 9948 7501 9488 -270 -204 -474 C ATOM 601 C TYR A 74 -109.527-187.699 145.116 1.00 79.25 C ANISOU 601 C TYR A 74 10935 8734 10443 -236 -281 -327 C ATOM 602 O TYR A 74 -108.542-186.984 145.330 1.00 73.80 O ANISOU 602 O TYR A 74 10161 8054 9827 -148 -187 -318 O ATOM 603 CB TYR A 74 -109.457-189.382 143.269 1.00 74.79 C ANISOU 603 CB TYR A 74 10658 7989 9769 -416 -95 -642 C ATOM 604 CG TYR A 74 -108.968-190.714 142.743 1.00 82.10 C ANISOU 604 CG TYR A 74 11672 8719 10802 -446 61 -847 C ATOM 605 CD1 TYR A 74 -108.707-191.779 143.595 1.00 91.46 C ANISOU 605 CD1 TYR A 74 12745 9734 12270 -351 47 -850 C ATOM 606 CD2 TYR A 74 -108.760-190.899 141.381 1.00 86.19 C ANISOU 606 CD2 TYR A 74 12403 9211 11133 -577 226 -1041 C ATOM 607 CE1 TYR A 74 -108.264-192.996 143.103 1.00 94.04 C ANISOU 607 CE1 TYR A 74 13147 9856 12730 -370 193 -1046 C ATOM 608 CE2 TYR A 74 -108.315-192.108 140.881 1.00 96.85 C ANISOU 608 CE2 TYR A 74 13842 10367 12589 -607 397 -1257 C ATOM 609 CZ TYR A 74 -108.069-193.153 141.746 1.00105.01 C ANISOU 609 CZ TYR A 74 14737 11219 13943 -493 379 -1261 C ATOM 610 OH TYR A 74 -107.626-194.360 141.252 1.00122.57 O ANISOU 610 OH TYR A 74 17040 13222 16308 -513 551 -1482 O ATOM 611 N ILE A 75 -110.775-187.224 145.168 1.00 70.19 N ANISOU 611 N ILE A 75 9806 7711 9153 -304 -452 -214 N ATOM 612 CA ILE A 75 -111.015-185.808 145.422 1.00 71.97 C ANISOU 612 CA ILE A 75 9967 8080 9300 -272 -523 -85 C ATOM 613 C ILE A 75 -110.569-185.426 146.830 1.00 74.70 C ANISOU 613 C ILE A 75 10138 8427 9819 -137 -541 18 C ATOM 614 O ILE A 75 -110.187-184.273 147.074 1.00 71.91 O ANISOU 614 O ILE A 75 9724 8147 9452 -80 -529 79 O ATOM 615 CB ILE A 75 -112.498-185.458 145.171 1.00 70.77 C ANISOU 615 CB ILE A 75 9844 8034 9012 -368 -707 9 C ATOM 616 CG1 ILE A 75 -112.674-183.945 145.060 1.00 74.72 C ANISOU 616 CG1 ILE A 75 10311 8655 9425 -347 -764 114 C ATOM 617 CG2 ILE A 75 -113.389-186.014 146.270 1.00 62.07 C ANISOU 617 CG2 ILE A 75 8625 6925 8035 -350 -821 96 C ATOM 618 CD1 ILE A 75 -111.939-183.347 143.889 1.00 65.03 C ANISOU 618 CD1 ILE A 75 9227 7442 8039 -401 -662 50 C ATOM 619 N LEU A 76 -110.586-186.377 147.772 1.00 69.90 N ANISOU 619 N LEU A 76 9464 7731 9365 -96 -576 40 N ATOM 620 CA LEU A 76 -110.109-186.092 149.123 1.00 68.44 C ANISOU 620 CA LEU A 76 9149 7538 9315 8 -609 139 C ATOM 621 C LEU A 76 -108.598-185.929 149.153 1.00 78.26 C ANISOU 621 C LEU A 76 10336 8705 10694 101 -498 84 C ATOM 622 O LEU A 76 -108.075-185.100 149.906 1.00 71.67 O ANISOU 622 O LEU A 76 9411 7911 9908 171 -520 157 O ATOM 623 CB LEU A 76 -110.537-187.203 150.082 1.00 71.47 C ANISOU 623 CB LEU A 76 9509 7838 9808 2 -689 195 C ATOM 624 CG LEU A 76 -112.042-187.328 150.320 1.00 76.78 C ANISOU 624 CG LEU A 76 10194 8588 10391 -89 -792 268 C ATOM 625 CD1 LEU A 76 -112.349-188.481 151.269 1.00 69.38 C ANISOU 625 CD1 LEU A 76 9247 7552 9561 -111 -848 326 C ATOM 626 CD2 LEU A 76 -112.614-186.015 150.844 1.00 61.77 C ANISOU 626 CD2 LEU A 76 8221 6837 8411 -71 -835 366 C ATOM 627 N LEU A 77 -107.878-186.735 148.368 1.00 76.51 N ANISOU 627 N LEU A 77 10157 8359 10553 97 -374 -54 N ATOM 628 CA LEU A 77 -106.440-186.535 148.240 1.00 75.06 C ANISOU 628 CA LEU A 77 9893 8098 10528 179 -240 -126 C ATOM 629 C LEU A 77 -106.145-185.192 147.593 1.00 76.26 C ANISOU 629 C LEU A 77 10063 8372 10542 159 -158 -134 C ATOM 630 O LEU A 77 -105.208-184.491 147.994 1.00 72.85 O ANISOU 630 O LEU A 77 9520 7941 10220 231 -121 -107 O ATOM 631 CB LEU A 77 -105.820-187.672 147.428 1.00 77.26 C ANISOU 631 CB LEU A 77 10214 8210 10933 172 -83 -300 C ATOM 632 CG LEU A 77 -105.877-189.068 148.053 1.00 83.82 C ANISOU 632 CG LEU A 77 11014 8870 11964 207 -154 -298 C ATOM 633 CD1 LEU A 77 -105.375-190.108 147.067 1.00 87.60 C ANISOU 633 CD1 LEU A 77 11554 9178 12552 189 28 -502 C ATOM 634 CD2 LEU A 77 -105.068-189.118 149.341 1.00 86.27 C ANISOU 634 CD2 LEU A 77 11155 9099 12525 329 -254 -182 C ATOM 635 N ASN A 78 -106.941-184.819 146.590 1.00 72.33 N ANISOU 635 N ASN A 78 9710 7969 9805 51 -147 -160 N ATOM 636 CA ASN A 78 -106.819-183.498 145.986 1.00 74.40 C ANISOU 636 CA ASN A 78 10013 8343 9914 15 -103 -134 C ATOM 637 C ASN A 78 -107.005-182.402 147.027 1.00 76.57 C ANISOU 637 C ASN A 78 10174 8707 10213 84 -229 17 C ATOM 638 O ASN A 78 -106.264-181.412 147.039 1.00 67.02 O ANISOU 638 O ASN A 78 8914 7526 9025 116 -170 36 O ATOM 639 CB ASN A 78 -107.840-183.353 144.860 1.00 76.57 C ANISOU 639 CB ASN A 78 10472 8696 9924 -124 -143 -147 C ATOM 640 CG ASN A 78 -107.555-182.172 143.968 1.00 73.61 C ANISOU 640 CG ASN A 78 10187 8401 9381 -186 -73 -137 C ATOM 641 OD1 ASN A 78 -106.429-181.989 143.502 1.00 73.64 O ANISOU 641 OD1 ASN A 78 10197 8362 9422 -185 121 -227 O ATOM 642 ND2 ASN A 78 -108.574-181.357 143.726 1.00 69.82 N ANISOU 642 ND2 ASN A 78 9767 8026 8734 -245 -230 -22 N ATOM 643 N LEU A 79 -107.986-182.572 147.916 1.00 65.49 N ANISOU 643 N LEU A 79 8733 7340 8810 97 -387 115 N ATOM 644 CA LEU A 79 -108.187-181.626 149.010 1.00 63.98 C ANISOU 644 CA LEU A 79 8447 7219 8645 155 -483 234 C ATOM 645 C LEU A 79 -106.950-181.518 149.889 1.00 74.07 C ANISOU 645 C LEU A 79 9611 8434 10099 246 -455 241 C ATOM 646 O LEU A 79 -106.544-180.414 150.265 1.00 72.32 O ANISOU 646 O LEU A 79 9336 8259 9885 280 -461 287 O ATOM 647 CB LEU A 79 -109.387-182.052 149.850 1.00 56.86 C ANISOU 647 CB LEU A 79 7526 6347 7731 140 -611 312 C ATOM 648 CG LEU A 79 -109.619-181.230 151.115 1.00 72.27 C ANISOU 648 CG LEU A 79 9395 8357 9708 190 -680 411 C ATOM 649 CD1 LEU A 79 -109.932-179.766 150.779 1.00 65.77 C ANISOU 649 CD1 LEU A 79 8564 7624 8800 192 -686 447 C ATOM 650 CD2 LEU A 79 -110.727-181.855 151.947 1.00 59.83 C ANISOU 650 CD2 LEU A 79 7807 6795 8129 156 -760 469 C ATOM 651 N ALA A 80 -106.337-182.655 150.227 1.00 69.18 N ANISOU 651 N ALA A 80 8951 7694 9641 282 -440 201 N ATOM 652 CA ALA A 80 -105.158-182.635 151.085 1.00 67.05 C ANISOU 652 CA ALA A 80 8559 7347 9570 365 -457 224 C ATOM 653 C ALA A 80 -104.013-181.879 150.428 1.00 70.11 C ANISOU 653 C ALA A 80 8889 7725 10027 386 -322 156 C ATOM 654 O ALA A 80 -103.314-181.103 151.089 1.00 67.63 O ANISOU 654 O ALA A 80 8479 7421 9797 430 -362 207 O ATOM 655 CB ALA A 80 -104.731-184.061 151.425 1.00 57.31 C ANISOU 655 CB ALA A 80 7288 5958 8529 401 -479 199 C ATOM 656 N VAL A 81 -103.810-182.091 149.126 1.00 67.66 N ANISOU 656 N VAL A 81 8645 7393 9671 340 -155 38 N ATOM 657 CA VAL A 81 -102.763-181.369 148.410 1.00 75.09 C ANISOU 657 CA VAL A 81 9545 8327 10658 336 12 -33 C ATOM 658 C VAL A 81 -103.058-179.872 148.392 1.00 78.85 C ANISOU 658 C VAL A 81 10052 8931 10975 303 -27 52 C ATOM 659 O VAL A 81 -102.152-179.047 148.567 1.00 72.04 O ANISOU 659 O VAL A 81 9095 8065 10211 328 18 63 O ATOM 660 CB VAL A 81 -102.601-181.939 146.988 1.00 70.83 C ANISOU 660 CB VAL A 81 9117 7743 10053 262 222 -188 C ATOM 661 CG1 VAL A 81 -101.619-181.101 146.187 1.00 71.13 C ANISOU 661 CG1 VAL A 81 9138 7791 10098 227 425 -256 C ATOM 662 CG2 VAL A 81 -102.134-183.389 147.046 1.00 67.43 C ANISOU 662 CG2 VAL A 81 8629 7149 9843 312 284 -292 C ATOM 663 N ALA A 82 -104.326-179.496 148.194 1.00 70.27 N ANISOU 663 N ALA A 82 9085 7944 9671 248 -120 116 N ATOM 664 CA ALA A 82 -104.681-178.079 148.151 1.00 69.37 C ANISOU 664 CA ALA A 82 8997 7926 9434 225 -167 200 C ATOM 665 C ALA A 82 -104.345-177.388 149.464 1.00 71.76 C ANISOU 665 C ALA A 82 9177 8235 9853 299 -267 277 C ATOM 666 O ALA A 82 -103.818-176.269 149.472 1.00 71.21 O ANISOU 666 O ALA A 82 9074 8186 9799 299 -241 303 O ATOM 667 CB ALA A 82 -106.166-177.915 147.833 1.00 55.54 C ANISOU 667 CB ALA A 82 7356 6256 7491 169 -280 261 C ATOM 668 N ASP A 83 -104.653-178.040 150.587 1.00 65.41 N ANISOU 668 N ASP A 83 8322 7410 9119 344 -385 317 N ATOM 669 CA ASP A 83 -104.329-177.477 151.893 1.00 68.40 C ANISOU 669 CA ASP A 83 8619 7792 9576 391 -488 383 C ATOM 670 C ASP A 83 -102.825-177.336 152.085 1.00 75.24 C ANISOU 670 C ASP A 83 9368 8582 10637 428 -448 354 C ATOM 671 O ASP A 83 -102.369-176.404 152.757 1.00 73.89 O ANISOU 671 O ASP A 83 9144 8425 10506 439 -505 394 O ATOM 672 CB ASP A 83 -104.929-178.344 152.997 1.00 61.12 C ANISOU 672 CB ASP A 83 7703 6857 8664 404 -611 434 C ATOM 673 CG ASP A 83 -106.449-178.436 152.910 1.00 75.88 C ANISOU 673 CG ASP A 83 9653 8800 10376 362 -645 464 C ATOM 674 OD1 ASP A 83 -107.071-177.564 152.259 1.00 72.44 O ANISOU 674 OD1 ASP A 83 9254 8432 9836 338 -620 470 O ATOM 675 OD2 ASP A 83 -107.024-179.373 153.508 1.00 75.82 O ANISOU 675 OD2 ASP A 83 9664 8774 10368 350 -706 491 O ATOM 676 N LEU A 84 -102.042-178.250 151.506 1.00 68.21 N ANISOU 676 N LEU A 84 8426 7600 9890 444 -349 275 N ATOM 677 CA LEU A 84 -100.589-178.132 151.570 1.00 75.39 C ANISOU 677 CA LEU A 84 9186 8425 11036 480 -292 238 C ATOM 678 C LEU A 84 -100.091-176.945 150.751 1.00 74.50 C ANISOU 678 C LEU A 84 9069 8354 10884 435 -151 206 C ATOM 679 O LEU A 84 -99.108-176.299 151.132 1.00 67.52 O ANISOU 679 O LEU A 84 8061 7439 10156 450 -157 216 O ATOM 680 CB LEU A 84 -99.938-179.432 151.107 1.00 66.41 C ANISOU 680 CB LEU A 84 7978 7159 10095 515 -193 145 C ATOM 681 CG LEU A 84 -100.046-180.595 152.095 1.00 74.54 C ANISOU 681 CG LEU A 84 8969 8099 11252 569 -359 198 C ATOM 682 CD1 LEU A 84 -99.360-181.841 151.554 1.00 77.84 C ANISOU 682 CD1 LEU A 84 9305 8360 11909 614 -246 93 C ATOM 683 CD2 LEU A 84 -99.449-180.195 153.434 1.00 64.84 C ANISOU 683 CD2 LEU A 84 7636 6850 10152 605 -558 304 C ATOM 684 N PHE A 85 -100.753-176.644 149.629 1.00 71.13 N ANISOU 684 N PHE A 85 8784 7991 10250 367 -38 176 N ATOM 685 CA PHE A 85 -100.481-175.397 148.917 1.00 77.56 C ANISOU 685 CA PHE A 85 9636 8852 10979 306 64 183 C ATOM 686 C PHE A 85 -100.746-174.185 149.802 1.00 76.61 C ANISOU 686 C PHE A 85 9499 8782 10826 320 -83 283 C ATOM 687 O PHE A 85 -99.976-173.218 149.786 1.00 76.35 O ANISOU 687 O PHE A 85 9406 8738 10867 300 -39 293 O ATOM 688 CB PHE A 85 -101.326-175.315 147.647 1.00 78.55 C ANISOU 688 CB PHE A 85 9953 9038 10854 217 150 166 C ATOM 689 CG PHE A 85 -100.716-176.009 146.465 1.00 86.26 C ANISOU 689 CG PHE A 85 10977 9965 11834 157 377 39 C ATOM 690 CD1 PHE A 85 -100.673-177.390 146.397 1.00 91.25 C ANISOU 690 CD1 PHE A 85 11594 10526 12551 187 423 -55 C ATOM 691 CD2 PHE A 85 -100.195-175.276 145.412 1.00 89.65 C ANISOU 691 CD2 PHE A 85 11481 10407 12175 60 560 7 C ATOM 692 CE1 PHE A 85 -100.114-178.027 145.309 1.00 92.43 C ANISOU 692 CE1 PHE A 85 11795 10616 12707 128 661 -199 C ATOM 693 CE2 PHE A 85 -99.635-175.910 144.319 1.00 91.68 C ANISOU 693 CE2 PHE A 85 11802 10619 12414 -14 808 -130 C ATOM 694 CZ PHE A 85 -99.596-177.287 144.269 1.00 90.16 C ANISOU 694 CZ PHE A 85 11588 10353 12315 24 865 -244 C ATOM 695 N MET A 86 -101.831-174.213 150.580 1.00 77.21 N ANISOU 695 N MET A 86 9628 8907 10802 345 -242 348 N ATOM 696 CA MET A 86 -102.089-173.112 151.505 1.00 71.62 C ANISOU 696 CA MET A 86 8908 8231 10072 359 -359 417 C ATOM 697 C MET A 86 -101.066-173.091 152.634 1.00 74.90 C ANISOU 697 C MET A 86 9197 8592 10669 393 -441 421 C ATOM 698 O MET A 86 -100.630-172.016 153.062 1.00 68.76 O ANISOU 698 O MET A 86 8386 7812 9930 380 -476 442 O ATOM 699 CB MET A 86 -103.507-173.205 152.072 1.00 61.84 C ANISOU 699 CB MET A 86 7745 7051 8699 371 -471 465 C ATOM 700 CG MET A 86 -104.628-173.029 151.055 1.00 80.04 C ANISOU 700 CG MET A 86 10158 9408 10845 334 -446 485 C ATOM 701 SD MET A 86 -106.255-173.370 151.781 1.00 92.12 S ANISOU 701 SD MET A 86 11720 10991 12291 351 -564 529 S ATOM 702 CE MET A 86 -106.304-172.163 153.097 1.00 82.26 C ANISOU 702 CE MET A 86 10428 9745 11081 385 -626 558 C ATOM 703 N VAL A 87 -100.668-174.266 153.129 1.00 76.63 N ANISOU 703 N VAL A 87 9349 8756 11010 430 -493 407 N ATOM 704 CA VAL A 87 -99.728-174.327 154.246 1.00 68.90 C ANISOU 704 CA VAL A 87 8256 7716 10207 455 -623 434 C ATOM 705 C VAL A 87 -98.359-173.799 153.829 1.00 68.44 C ANISOU 705 C VAL A 87 8054 7598 10352 447 -540 395 C ATOM 706 O VAL A 87 -97.746-173.002 154.552 1.00 61.23 O ANISOU 706 O VAL A 87 7076 6671 9519 431 -638 425 O ATOM 707 CB VAL A 87 -99.637-175.761 154.802 1.00 68.31 C ANISOU 707 CB VAL A 87 8145 7575 10234 495 -718 449 C ATOM 708 CG1 VAL A 87 -98.317-175.962 155.538 1.00 55.11 C ANISOU 708 CG1 VAL A 87 6314 5803 8824 521 -837 472 C ATOM 709 CG2 VAL A 87 -100.800-176.040 155.746 1.00 62.44 C ANISOU 709 CG2 VAL A 87 7528 6886 9310 480 -849 514 C ATOM 710 N PHE A 88 -97.864-174.215 152.658 1.00 70.49 N ANISOU 710 N PHE A 88 8265 7820 10699 444 -347 320 N ATOM 711 CA PHE A 88 -96.531-173.837 152.197 1.00 75.37 C ANISOU 711 CA PHE A 88 8723 8372 11541 429 -223 269 C ATOM 712 C PHE A 88 -96.515-172.625 151.280 1.00 83.39 C ANISOU 712 C PHE A 88 9806 9439 12439 352 -64 257 C ATOM 713 O PHE A 88 -95.504-171.922 151.242 1.00 94.52 O ANISOU 713 O PHE A 88 11091 10809 14014 321 -11 246 O ATOM 714 CB PHE A 88 -95.857-175.007 151.471 1.00 65.09 C ANISOU 714 CB PHE A 88 7315 6977 10439 462 -61 173 C ATOM 715 CG PHE A 88 -95.529-176.159 152.370 1.00 75.43 C ANISOU 715 CG PHE A 88 8508 8189 11962 543 -225 195 C ATOM 716 CD1 PHE A 88 -94.470-176.081 153.259 1.00 83.94 C ANISOU 716 CD1 PHE A 88 9388 9183 13322 575 -378 238 C ATOM 717 CD2 PHE A 88 -96.280-177.320 152.332 1.00 76.69 C ANISOU 717 CD2 PHE A 88 8760 8332 12049 576 -248 186 C ATOM 718 CE1 PHE A 88 -94.168-177.139 154.097 1.00 85.34 C ANISOU 718 CE1 PHE A 88 9469 9256 13701 643 -566 285 C ATOM 719 CE2 PHE A 88 -95.986-178.378 153.160 1.00 75.71 C ANISOU 719 CE2 PHE A 88 8541 8100 12124 644 -412 225 C ATOM 720 CZ PHE A 88 -94.929-178.290 154.045 1.00 80.82 C ANISOU 720 CZ PHE A 88 9000 8660 13049 679 -578 282 C ATOM 721 N GLY A 89 -97.585-172.351 150.529 1.00 85.08 N ANISOU 721 N GLY A 89 10209 9731 12387 311 -1 269 N ATOM 722 CA GLY A 89 -97.591-171.154 149.702 1.00 75.02 C ANISOU 722 CA GLY A 89 9017 8491 10997 230 113 287 C ATOM 723 C GLY A 89 -97.999-169.907 150.454 1.00 79.58 C ANISOU 723 C GLY A 89 9632 9096 11507 224 -38 369 C ATOM 724 O GLY A 89 -97.634-168.797 150.056 1.00 87.58 O ANISOU 724 O GLY A 89 10658 10100 12520 162 28 392 O ATOM 725 N GLY A 90 -98.745-170.063 151.547 1.00 74.77 N ANISOU 725 N GLY A 90 9049 8514 10848 279 -224 408 N ATOM 726 CA GLY A 90 -99.299-168.923 152.249 1.00 65.74 C ANISOU 726 CA GLY A 90 7963 7390 9625 274 -341 461 C ATOM 727 C GLY A 90 -98.879-168.798 153.700 1.00 73.27 C ANISOU 727 C GLY A 90 8842 8317 10681 296 -506 467 C ATOM 728 O GLY A 90 -98.318-167.772 154.095 1.00 79.84 O ANISOU 728 O GLY A 90 9638 9115 11583 262 -543 472 O ATOM 729 N PHE A 91 -99.143-169.835 154.504 1.00 63.97 N ANISOU 729 N PHE A 91 7657 7147 9501 338 -614 469 N ATOM 730 CA PHE A 91 -98.927-169.734 155.946 1.00 64.93 C ANISOU 730 CA PHE A 91 7765 7252 9653 335 -796 489 C ATOM 731 C PHE A 91 -97.444-169.583 156.281 1.00 63.44 C ANISOU 731 C PHE A 91 7420 6989 9697 313 -859 483 C ATOM 732 O PHE A 91 -97.075-168.788 157.156 1.00 60.33 O ANISOU 732 O PHE A 91 7024 6574 9323 271 -982 492 O ATOM 733 CB PHE A 91 -99.509-170.957 156.672 1.00 57.88 C ANISOU 733 CB PHE A 91 6917 6376 8699 366 -897 512 C ATOM 734 CG PHE A 91 -100.980-171.204 156.416 1.00 68.73 C ANISOU 734 CG PHE A 91 8417 7820 9877 380 -844 518 C ATOM 735 CD1 PHE A 91 -101.812-170.201 155.946 1.00 64.85 C ANISOU 735 CD1 PHE A 91 7999 7369 9272 372 -770 513 C ATOM 736 CD2 PHE A 91 -101.529-172.455 156.662 1.00 64.41 C ANISOU 736 CD2 PHE A 91 7903 7284 9288 400 -881 535 C ATOM 737 CE1 PHE A 91 -103.162-170.447 155.714 1.00 62.50 C ANISOU 737 CE1 PHE A 91 7782 7126 8839 386 -741 524 C ATOM 738 CE2 PHE A 91 -102.877-172.708 156.436 1.00 69.12 C ANISOU 738 CE2 PHE A 91 8592 7940 9731 403 -838 541 C ATOM 739 CZ PHE A 91 -103.695-171.702 155.960 1.00 67.74 C ANISOU 739 CZ PHE A 91 8468 7810 9462 398 -771 534 C ATOM 740 N THR A 92 -96.577-170.349 155.606 1.00 56.82 N ANISOU 740 N THR A 92 6440 6099 9051 336 -775 459 N ATOM 741 CA THR A 92 -95.156-170.334 155.950 1.00 57.25 C ANISOU 741 CA THR A 92 6299 6067 9385 323 -846 456 C ATOM 742 C THR A 92 -94.484-169.048 155.477 1.00 63.88 C ANISOU 742 C THR A 92 7078 6889 10303 259 -750 435 C ATOM 743 O THR A 92 -93.695-168.447 156.219 1.00 61.97 O ANISOU 743 O THR A 92 6746 6602 10197 216 -887 449 O ATOM 744 CB THR A 92 -94.460-171.567 155.375 1.00 56.70 C ANISOU 744 CB THR A 92 6073 5927 9542 378 -761 422 C ATOM 745 OG1 THR A 92 -95.034-172.746 155.952 1.00 77.82 O ANISOU 745 OG1 THR A 92 8807 8597 12165 430 -885 456 O ATOM 746 CG2 THR A 92 -92.974-171.527 155.690 1.00 68.75 C ANISOU 746 CG2 THR A 92 7353 7351 11418 372 -833 420 C ATOM 747 N THR A 93 -94.830-168.578 154.274 1.00 62.44 N ANISOU 747 N THR A 93 6965 6740 10019 235 -532 410 N ATOM 748 CA THR A 93 -94.344-167.281 153.815 1.00 74.38 C ANISOU 748 CA THR A 93 8460 8233 11569 159 -439 408 C ATOM 749 C THR A 93 -94.835-166.157 154.719 1.00 69.51 C ANISOU 749 C THR A 93 7953 7627 10832 128 -594 440 C ATOM 750 O THR A 93 -94.077-165.238 155.044 1.00 63.84 O ANISOU 750 O THR A 93 7164 6857 10237 66 -641 439 O ATOM 751 CB THR A 93 -94.787-167.031 152.373 1.00 74.30 C ANISOU 751 CB THR A 93 8557 8257 11417 125 -202 399 C ATOM 752 OG1 THR A 93 -96.180-167.333 152.242 1.00 93.80 O ANISOU 752 OG1 THR A 93 11210 10797 13633 164 -231 423 O ATOM 753 CG2 THR A 93 -93.999-167.900 151.411 1.00 73.54 C ANISOU 753 CG2 THR A 93 8343 8129 11470 120 6 334 C ATOM 754 N THR A 94 -96.094-166.230 155.158 1.00 57.48 N ANISOU 754 N THR A 94 6594 6160 9086 166 -667 458 N ATOM 755 CA THR A 94 -96.653-165.163 155.984 1.00 60.07 C ANISOU 755 CA THR A 94 7034 6487 9303 141 -773 463 C ATOM 756 C THR A 94 -96.028-165.156 157.373 1.00 67.10 C ANISOU 756 C THR A 94 7880 7344 10270 109 -981 453 C ATOM 757 O THR A 94 -95.814-164.089 157.959 1.00 62.37 O ANISOU 757 O THR A 94 7316 6706 9677 50 -1054 435 O ATOM 758 CB THR A 94 -98.171-165.312 156.072 1.00 56.36 C ANISOU 758 CB THR A 94 6724 6080 8610 190 -768 472 C ATOM 759 OG1 THR A 94 -98.736-165.162 154.761 1.00 59.08 O ANISOU 759 OG1 THR A 94 7120 6446 8883 200 -616 496 O ATOM 760 CG2 THR A 94 -98.773-164.272 157.013 1.00 53.41 C ANISOU 760 CG2 THR A 94 6456 5690 8147 171 -850 451 C ATOM 761 N LEU A 95 -95.737-166.336 157.922 1.00 55.09 N ANISOU 761 N LEU A 95 6299 5828 8805 139 -1093 468 N ATOM 762 CA LEU A 95 -94.997-166.400 159.179 1.00 62.53 C ANISOU 762 CA LEU A 95 7198 6728 9832 91 -1326 481 C ATOM 763 C LEU A 95 -93.651-165.697 159.054 1.00 72.77 C ANISOU 763 C LEU A 95 8323 7949 11380 28 -1357 473 C ATOM 764 O LEU A 95 -93.203-165.017 159.986 1.00 66.09 O ANISOU 764 O LEU A 95 7492 7065 10553 -50 -1532 467 O ATOM 765 CB LEU A 95 -94.807-167.857 159.599 1.00 56.95 C ANISOU 765 CB LEU A 95 6434 6016 9188 136 -1447 525 C ATOM 766 CG LEU A 95 -93.835-168.167 160.738 1.00 65.36 C ANISOU 766 CG LEU A 95 7418 7018 10398 87 -1725 571 C ATOM 767 CD1 LEU A 95 -94.279-167.530 162.041 1.00 73.74 C ANISOU 767 CD1 LEU A 95 8680 8105 11234 -2 -1903 570 C ATOM 768 CD2 LEU A 95 -93.714-169.666 160.906 1.00 71.72 C ANISOU 768 CD2 LEU A 95 8160 7796 11295 149 -1818 629 C ATOM 769 N TYR A 96 -93.007-165.828 157.894 1.00 66.61 N ANISOU 769 N TYR A 96 7383 7141 10786 46 -1176 463 N ATOM 770 CA TYR A 96 -91.695-165.230 157.685 1.00 71.78 C ANISOU 770 CA TYR A 96 7840 7718 11715 -19 -1169 452 C ATOM 771 C TYR A 96 -91.787-163.721 157.468 1.00 71.22 C ANISOU 771 C TYR A 96 7853 7632 11577 -100 -1098 434 C ATOM 772 O TYR A 96 -91.007-162.963 158.052 1.00 63.28 O ANISOU 772 O TYR A 96 6775 6564 10704 -184 -1227 428 O ATOM 773 CB TYR A 96 -91.013-165.919 156.501 1.00 67.61 C ANISOU 773 CB TYR A 96 7121 7162 11404 17 -952 431 C ATOM 774 CG TYR A 96 -89.625-165.410 156.208 1.00 67.94 C ANISOU 774 CG TYR A 96 6920 7120 11772 -52 -902 413 C ATOM 775 CD1 TYR A 96 -88.533-165.850 156.944 1.00 73.05 C ANISOU 775 CD1 TYR A 96 7337 7690 12730 -57 -1103 429 C ATOM 776 CD2 TYR A 96 -89.408-164.483 155.200 1.00 62.91 C ANISOU 776 CD2 TYR A 96 6281 6476 11147 -123 -665 391 C ATOM 777 CE1 TYR A 96 -87.254-165.372 156.688 1.00 72.92 C ANISOU 777 CE1 TYR A 96 7063 7591 13054 -126 -1059 411 C ATOM 778 CE2 TYR A 96 -88.140-164.005 154.930 1.00 66.04 C ANISOU 778 CE2 TYR A 96 6445 6794 11853 -202 -597 373 C ATOM 779 CZ TYR A 96 -87.068-164.451 155.678 1.00 65.87 C ANISOU 779 CZ TYR A 96 6168 6697 12163 -200 -789 376 C ATOM 780 OH TYR A 96 -85.809-163.976 155.407 1.00 77.55 O ANISOU 780 OH TYR A 96 7385 8093 13987 -283 -720 356 O ATOM 781 N THR A 97 -92.752-163.264 156.667 1.00 61.91 N ANISOU 781 N THR A 97 6829 6494 10198 -81 -919 432 N ATOM 782 CA THR A 97 -92.886-161.833 156.408 1.00 63.85 C ANISOU 782 CA THR A 97 7161 6702 10399 -151 -857 430 C ATOM 783 C THR A 97 -93.415-161.087 157.627 1.00 64.18 C ANISOU 783 C THR A 97 7348 6726 10311 -178 -1038 404 C ATOM 784 O THR A 97 -92.957-159.977 157.922 1.00 66.96 O ANISOU 784 O THR A 97 7701 7005 10736 -263 -1085 384 O ATOM 785 CB THR A 97 -93.800-161.608 155.209 1.00 58.29 C ANISOU 785 CB THR A 97 6586 6034 9529 -123 -651 456 C ATOM 786 OG1 THR A 97 -95.049-162.273 155.435 1.00 61.64 O ANISOU 786 OG1 THR A 97 7146 6531 9743 -36 -686 460 O ATOM 787 CG2 THR A 97 -93.164-162.159 153.941 1.00 61.32 C ANISOU 787 CG2 THR A 97 6857 6423 10019 -137 -440 462 C ATOM 788 N SER A 98 -94.384-161.674 158.345 1.00 61.32 N ANISOU 788 N SER A 98 7118 6425 9757 -119 -1123 394 N ATOM 789 CA SER A 98 -94.938-161.015 159.527 1.00 63.98 C ANISOU 789 CA SER A 98 7614 6747 9949 -155 -1256 347 C ATOM 790 C SER A 98 -93.862-160.697 160.559 1.00 62.31 C ANISOU 790 C SER A 98 7346 6477 9854 -259 -1467 323 C ATOM 791 O SER A 98 -93.956-159.682 161.261 1.00 60.43 O ANISOU 791 O SER A 98 7221 6186 9555 -332 -1538 266 O ATOM 792 CB SER A 98 -96.039-161.874 160.161 1.00 63.57 C ANISOU 792 CB SER A 98 7695 6775 9685 -93 -1295 341 C ATOM 793 OG SER A 98 -95.537-163.116 160.633 1.00 74.89 O ANISOU 793 OG SER A 98 9052 8239 11162 -84 -1427 377 O ATOM 794 N LEU A 99 -92.835-161.543 160.670 1.00 63.96 N ANISOU 794 N LEU A 99 7377 6680 10246 -269 -1580 364 N ATOM 795 CA LEU A 99 -91.757-161.275 161.614 1.00 59.73 C ANISOU 795 CA LEU A 99 6764 6081 9851 -375 -1822 359 C ATOM 796 C LEU A 99 -90.824-160.177 161.128 1.00 66.67 C ANISOU 796 C LEU A 99 7510 6872 10949 -461 -1772 342 C ATOM 797 O LEU A 99 -89.986-159.706 161.903 1.00 65.57 O ANISOU 797 O LEU A 99 7321 6669 10924 -570 -1978 327 O ATOM 798 CB LEU A 99 -90.986-162.568 161.899 1.00 65.96 C ANISOU 798 CB LEU A 99 7382 6871 10808 -349 -1985 423 C ATOM 799 CG LEU A 99 -91.813-163.602 162.674 1.00 74.44 C ANISOU 799 CG LEU A 99 8614 8012 11656 -303 -2098 452 C ATOM 800 CD1 LEU A 99 -91.104-164.938 162.790 1.00 57.49 C ANISOU 800 CD1 LEU A 99 6292 5844 9708 -257 -2244 531 C ATOM 801 CD2 LEU A 99 -92.136-163.064 164.053 1.00 79.88 C ANISOU 801 CD2 LEU A 99 9531 8702 12117 -413 -2302 418 C ATOM 802 N HIS A 100 -90.953-159.762 159.869 1.00 62.78 N ANISOU 802 N HIS A 100 6974 6373 10508 -429 -1516 349 N ATOM 803 CA HIS A 100 -90.308-158.554 159.377 1.00 67.39 C ANISOU 803 CA HIS A 100 7491 6869 11245 -523 -1434 337 C ATOM 804 C HIS A 100 -91.209-157.330 159.439 1.00 69.16 C ANISOU 804 C HIS A 100 7937 7054 11287 -546 -1373 299 C ATOM 805 O HIS A 100 -90.697-156.206 159.478 1.00 67.02 O ANISOU 805 O HIS A 100 7656 6685 11123 -648 -1387 276 O ATOM 806 CB HIS A 100 -89.850-158.743 157.927 1.00 56.47 C ANISOU 806 CB HIS A 100 5949 5486 10021 -505 -1178 377 C ATOM 807 CG HIS A 100 -88.714-159.699 157.770 1.00 70.37 C ANISOU 807 CG HIS A 100 7435 7240 12061 -499 -1197 393 C ATOM 808 ND1 HIS A 100 -88.892-161.066 157.727 1.00 72.45 N ANISOU 808 ND1 HIS A 100 7646 7564 12319 -393 -1202 407 N ATOM 809 CD2 HIS A 100 -87.383-159.486 157.645 1.00 61.55 C ANISOU 809 CD2 HIS A 100 6065 6048 11274 -584 -1209 393 C ATOM 810 CE1 HIS A 100 -87.718-161.653 157.579 1.00 72.87 C ANISOU 810 CE1 HIS A 100 7421 7569 12696 -402 -1214 412 C ATOM 811 NE2 HIS A 100 -86.787-160.717 157.529 1.00 73.26 N ANISOU 811 NE2 HIS A 100 7333 7541 12961 -517 -1217 403 N ATOM 812 N GLY A 101 -92.529-157.515 159.449 1.00 60.87 N ANISOU 812 N GLY A 101 7071 6061 9995 -453 -1307 288 N ATOM 813 CA GLY A 101 -93.451-156.403 159.456 1.00 64.50 C ANISOU 813 CA GLY A 101 7714 6465 10328 -452 -1237 251 C ATOM 814 C GLY A 101 -93.840-155.893 158.092 1.00 67.37 C ANISOU 814 C GLY A 101 8088 6802 10709 -419 -1027 314 C ATOM 815 O GLY A 101 -94.494-154.845 158.007 1.00 70.06 O ANISOU 815 O GLY A 101 8555 7061 11004 -420 -982 300 O ATOM 816 N TYR A 102 -93.460-156.594 157.026 1.00 57.11 N ANISOU 816 N TYR A 102 6670 5556 9474 -397 -900 383 N ATOM 817 CA TYR A 102 -93.833-156.222 155.664 1.00 59.21 C ANISOU 817 CA TYR A 102 6978 5808 9710 -388 -707 458 C ATOM 818 C TYR A 102 -93.473-157.367 154.728 1.00 66.33 C ANISOU 818 C TYR A 102 7772 6797 10633 -361 -576 498 C ATOM 819 O TYR A 102 -92.819-158.336 155.120 1.00 67.90 O ANISOU 819 O TYR A 102 7830 7041 10926 -346 -631 468 O ATOM 820 CB TYR A 102 -93.152-154.931 155.211 1.00 60.61 C ANISOU 820 CB TYR A 102 7139 5861 10029 -506 -648 486 C ATOM 821 CG TYR A 102 -91.648-155.003 155.041 1.00 57.21 C ANISOU 821 CG TYR A 102 6501 5404 9833 -614 -620 484 C ATOM 822 CD1 TYR A 102 -90.798-154.962 156.141 1.00 54.46 C ANISOU 822 CD1 TYR A 102 6037 5020 9633 -672 -802 420 C ATOM 823 CD2 TYR A 102 -91.075-155.067 153.776 1.00 64.53 C ANISOU 823 CD2 TYR A 102 7349 6332 10838 -673 -411 546 C ATOM 824 CE1 TYR A 102 -89.415-155.003 155.983 1.00 64.88 C ANISOU 824 CE1 TYR A 102 7129 6304 11219 -771 -788 423 C ATOM 825 CE2 TYR A 102 -89.699-155.105 153.611 1.00 62.23 C ANISOU 825 CE2 TYR A 102 6839 6006 10799 -775 -354 534 C ATOM 826 CZ TYR A 102 -88.878-155.073 154.715 1.00 66.91 C ANISOU 826 CZ TYR A 102 7282 6560 11581 -816 -549 475 C ATOM 827 OH TYR A 102 -87.514-155.114 154.549 1.00 75.97 O ANISOU 827 OH TYR A 102 8176 7664 13025 -916 -504 466 O ATOM 828 N PHE A 103 -93.896-157.233 153.473 1.00 61.55 N ANISOU 828 N PHE A 103 7243 6202 9943 -364 -407 566 N ATOM 829 CA PHE A 103 -93.698-158.284 152.478 1.00 60.35 C ANISOU 829 CA PHE A 103 7036 6129 9767 -350 -250 586 C ATOM 830 C PHE A 103 -92.304-158.140 151.877 1.00 64.03 C ANISOU 830 C PHE A 103 7337 6550 10442 -462 -105 584 C ATOM 831 O PHE A 103 -92.088-157.405 150.911 1.00 67.88 O ANISOU 831 O PHE A 103 7879 6992 10922 -559 50 640 O ATOM 832 CB PHE A 103 -94.774-158.229 151.403 1.00 60.90 C ANISOU 832 CB PHE A 103 7283 6230 9626 -327 -150 660 C ATOM 833 CG PHE A 103 -94.849-159.477 150.586 1.00 62.58 C ANISOU 833 CG PHE A 103 7486 6536 9755 -300 -23 654 C ATOM 834 CD1 PHE A 103 -95.548-160.577 151.050 1.00 63.64 C ANISOU 834 CD1 PHE A 103 7629 6749 9801 -191 -105 618 C ATOM 835 CD2 PHE A 103 -94.184-159.572 149.376 1.00 69.19 C ANISOU 835 CD2 PHE A 103 8312 7373 10605 -396 193 674 C ATOM 836 CE1 PHE A 103 -95.601-161.743 150.313 1.00 67.77 C ANISOU 836 CE1 PHE A 103 8147 7341 10260 -171 10 600 C ATOM 837 CE2 PHE A 103 -94.234-160.741 148.633 1.00 74.93 C ANISOU 837 CE2 PHE A 103 9044 8174 11252 -380 327 642 C ATOM 838 CZ PHE A 103 -94.948-161.826 149.106 1.00 70.34 C ANISOU 838 CZ PHE A 103 8469 7662 10595 -263 227 604 C ATOM 839 N VAL A 104 -91.345-158.879 152.442 1.00 65.40 N ANISOU 839 N VAL A 104 7301 6730 10816 -455 -153 524 N ATOM 840 CA VAL A 104 -89.933-158.694 152.109 1.00 70.85 C ANISOU 840 CA VAL A 104 7777 7361 11781 -559 -39 506 C ATOM 841 C VAL A 104 -89.539-159.292 150.768 1.00 69.08 C ANISOU 841 C VAL A 104 7503 7167 11576 -596 256 502 C ATOM 842 O VAL A 104 -88.369-159.184 150.385 1.00 78.46 O ANISOU 842 O VAL A 104 8498 8305 13009 -688 406 476 O ATOM 843 CB VAL A 104 -89.006-159.289 153.192 1.00 78.76 C ANISOU 843 CB VAL A 104 8543 8342 13040 -537 -221 452 C ATOM 844 CG1 VAL A 104 -89.115-158.493 154.471 1.00 81.60 C ANISOU 844 CG1 VAL A 104 8957 8654 13393 -562 -492 446 C ATOM 845 CG2 VAL A 104 -89.340-160.762 153.434 1.00 75.41 C ANISOU 845 CG2 VAL A 104 8083 7991 12577 -410 -272 426 C ATOM 846 N PHE A 105 -90.465-159.911 150.036 1.00 64.34 N ANISOU 846 N PHE A 105 7071 6643 10733 -540 356 517 N ATOM 847 CA PHE A 105 -90.117-160.602 148.803 1.00 67.84 C ANISOU 847 CA PHE A 105 7495 7117 11163 -583 641 488 C ATOM 848 C PHE A 105 -90.382-159.774 147.552 1.00 74.66 C ANISOU 848 C PHE A 105 8563 7973 11832 -714 840 562 C ATOM 849 O PHE A 105 -90.155-160.267 146.443 1.00 74.52 O ANISOU 849 O PHE A 105 8585 7984 11745 -781 1100 536 O ATOM 850 CB PHE A 105 -90.870-161.934 148.722 1.00 70.70 C ANISOU 850 CB PHE A 105 7920 7562 11382 -463 628 449 C ATOM 851 CG PHE A 105 -90.489-162.911 149.798 1.00 73.90 C ANISOU 851 CG PHE A 105 8125 7962 11991 -351 461 388 C ATOM 852 CD1 PHE A 105 -89.174-163.323 149.944 1.00 82.91 C ANISOU 852 CD1 PHE A 105 8983 9043 13477 -367 528 325 C ATOM 853 CD2 PHE A 105 -91.446-163.429 150.655 1.00 64.54 C ANISOU 853 CD2 PHE A 105 7032 6825 10667 -237 235 403 C ATOM 854 CE1 PHE A 105 -88.817-164.227 150.931 1.00 80.14 C ANISOU 854 CE1 PHE A 105 8451 8670 13329 -266 336 294 C ATOM 855 CE2 PHE A 105 -91.097-164.336 151.641 1.00 66.22 C ANISOU 855 CE2 PHE A 105 7089 7026 11047 -152 67 369 C ATOM 856 CZ PHE A 105 -89.782-164.735 151.779 1.00 70.60 C ANISOU 856 CZ PHE A 105 7369 7510 11944 -164 100 323 C ATOM 857 N GLY A 106 -90.852-158.537 147.698 1.00 81.18 N ANISOU 857 N GLY A 106 9531 8749 12566 -759 727 653 N ATOM 858 CA GLY A 106 -91.046-157.658 146.567 1.00 72.81 C ANISOU 858 CA GLY A 106 8668 7657 11342 -896 878 752 C ATOM 859 C GLY A 106 -92.276-158.005 145.749 1.00 83.73 C ANISOU 859 C GLY A 106 10310 9107 12395 -869 885 817 C ATOM 860 O GLY A 106 -92.972-158.992 146.013 1.00 72.64 O ANISOU 860 O GLY A 106 8922 7781 10897 -745 799 772 O ATOM 861 N PRO A 107 -92.563-157.193 144.728 1.00 85.93 N ANISOU 861 N PRO A 107 10803 9350 12494 -999 973 935 N ATOM 862 CA PRO A 107 -93.774-157.430 143.921 1.00 81.35 C ANISOU 862 CA PRO A 107 10485 8826 11599 -991 932 1021 C ATOM 863 C PRO A 107 -93.780-158.764 143.191 1.00 79.56 C ANISOU 863 C PRO A 107 10292 8703 11233 -998 1104 938 C ATOM 864 O PRO A 107 -94.849-159.370 143.038 1.00 81.88 O ANISOU 864 O PRO A 107 10716 9062 11332 -921 989 956 O ATOM 865 CB PRO A 107 -93.779-156.246 142.940 1.00 79.69 C ANISOU 865 CB PRO A 107 10484 8536 11261 -1167 1002 1177 C ATOM 866 CG PRO A 107 -92.366-155.748 142.919 1.00 73.30 C ANISOU 866 CG PRO A 107 9517 7661 10674 -1299 1203 1136 C ATOM 867 CD PRO A 107 -91.817-156.000 144.288 1.00 75.50 C ANISOU 867 CD PRO A 107 9503 7928 11254 -1169 1088 1011 C ATOM 868 N THR A 108 -92.621-159.244 142.737 1.00 74.98 N ANISOU 868 N THR A 108 9591 8131 10767 -1090 1384 837 N ATOM 869 CA THR A 108 -92.566-160.548 142.081 1.00 76.28 C ANISOU 869 CA THR A 108 9779 8375 10830 -1092 1573 726 C ATOM 870 C THR A 108 -92.959-161.664 143.045 1.00 82.73 C ANISOU 870 C THR A 108 10445 9238 11749 -891 1405 629 C ATOM 871 O THR A 108 -93.765-162.539 142.706 1.00 87.90 O ANISOU 871 O THR A 108 11228 9960 12211 -844 1377 606 O ATOM 872 CB THR A 108 -91.167-160.794 141.510 1.00 78.76 C ANISOU 872 CB THR A 108 9947 8663 11316 -1220 1933 614 C ATOM 873 OG1 THR A 108 -90.906-159.852 140.464 1.00 87.51 O ANISOU 873 OG1 THR A 108 11250 9738 12261 -1438 2121 711 O ATOM 874 CG2 THR A 108 -91.059-162.205 140.946 1.00 83.92 C ANISOU 874 CG2 THR A 108 10596 9375 11915 -1203 2144 463 C ATOM 875 N GLY A 109 -92.408-161.644 144.260 1.00 76.73 N ANISOU 875 N GLY A 109 9429 8440 11286 -785 1277 580 N ATOM 876 CA GLY A 109 -92.820-162.621 145.256 1.00 67.56 C ANISOU 876 CA GLY A 109 8153 7314 10202 -610 1088 517 C ATOM 877 C GLY A 109 -94.274-162.463 145.653 1.00 74.20 C ANISOU 877 C GLY A 109 9168 8196 10827 -520 832 601 C ATOM 878 O GLY A 109 -94.913-163.421 146.100 1.00 76.09 O ANISOU 878 O GLY A 109 9401 8487 11025 -406 722 561 O ATOM 879 N CYS A 110 -94.816-161.255 145.485 1.00 70.37 N ANISOU 879 N CYS A 110 8833 7677 10228 -573 742 720 N ATOM 880 CA CYS A 110 -96.221-161.014 145.783 1.00 64.81 C ANISOU 880 CA CYS A 110 8273 6993 9358 -489 518 801 C ATOM 881 C CYS A 110 -97.121-161.775 144.821 1.00 68.14 C ANISOU 881 C CYS A 110 8878 7488 9522 -504 549 824 C ATOM 882 O CYS A 110 -98.159-162.314 145.224 1.00 63.09 O ANISOU 882 O CYS A 110 8271 6896 8806 -398 390 826 O ATOM 883 CB CYS A 110 -96.507-159.514 145.720 1.00 74.29 C ANISOU 883 CB CYS A 110 9577 8109 10541 -545 430 923 C ATOM 884 SG CYS A 110 -98.120-159.032 146.344 1.00 77.61 S ANISOU 884 SG CYS A 110 10098 8513 10878 -417 154 1001 S ATOM 885 N ASN A 111 -96.746-161.813 143.540 1.00 61.76 N ANISOU 885 N ASN A 111 8204 6690 8572 -652 755 840 N ATOM 886 CA ASN A 111 -97.502-162.588 142.563 1.00 68.75 C ANISOU 886 CA ASN A 111 9287 7644 9192 -697 790 848 C ATOM 887 C ASN A 111 -97.365-164.085 142.821 1.00 77.74 C ANISOU 887 C ASN A 111 10315 8839 10385 -613 858 697 C ATOM 888 O ASN A 111 -98.340-164.834 142.694 1.00 80.85 O ANISOU 888 O ASN A 111 10803 9286 10629 -565 754 694 O ATOM 889 CB ASN A 111 -97.036-162.239 141.148 1.00 73.53 C ANISOU 889 CB ASN A 111 10092 8242 9605 -908 1016 891 C ATOM 890 CG ASN A 111 -97.592-160.913 140.659 1.00 83.53 C ANISOU 890 CG ASN A 111 11555 9453 10729 -1001 887 1085 C ATOM 891 OD1 ASN A 111 -98.737-160.563 140.945 1.00 89.84 O ANISOU 891 OD1 ASN A 111 12419 10242 11472 -918 623 1191 O ATOM 892 ND2 ASN A 111 -96.786-160.173 139.907 1.00 82.37 N ANISOU 892 ND2 ASN A 111 11497 9258 10540 -1179 1078 1137 N ATOM 893 N LEU A 112 -96.162-164.534 143.186 1.00 81.02 N ANISOU 893 N LEU A 112 10517 9226 11039 -595 1022 575 N ATOM 894 CA LEU A 112 -95.937-165.945 143.487 1.00 76.95 C ANISOU 894 CA LEU A 112 9875 8733 10632 -504 1079 436 C ATOM 895 C LEU A 112 -96.716-166.382 144.723 1.00 72.85 C ANISOU 895 C LEU A 112 9268 8234 10179 -337 806 449 C ATOM 896 O LEU A 112 -97.489-167.346 144.671 1.00 70.92 O ANISOU 896 O LEU A 112 9090 8032 9825 -284 746 419 O ATOM 897 CB LEU A 112 -94.442-166.198 143.673 1.00 76.26 C ANISOU 897 CB LEU A 112 9542 8586 10849 -513 1285 322 C ATOM 898 CG LEU A 112 -93.633-166.489 142.412 1.00 83.06 C ANISOU 898 CG LEU A 112 10453 9432 11672 -660 1647 226 C ATOM 899 CD1 LEU A 112 -92.197-166.029 142.584 1.00 82.14 C ANISOU 899 CD1 LEU A 112 10093 9242 11873 -706 1828 174 C ATOM 900 CD2 LEU A 112 -93.675-167.976 142.114 1.00 77.85 C ANISOU 900 CD2 LEU A 112 9781 8781 11016 -610 1768 80 C ATOM 901 N GLU A 113 -96.523-165.684 145.847 1.00 69.45 N ANISOU 901 N GLU A 113 8703 7769 9918 -269 646 489 N ATOM 902 CA GLU A 113 -97.241-166.035 147.069 1.00 65.89 C ANISOU 902 CA GLU A 113 8193 7337 9505 -135 410 498 C ATOM 903 C GLU A 113 -98.742-165.855 146.889 1.00 75.51 C ANISOU 903 C GLU A 113 9594 8604 10492 -113 267 581 C ATOM 904 O GLU A 113 -99.534-166.664 147.383 1.00 72.96 O ANISOU 904 O GLU A 113 9273 8320 10126 -30 154 564 O ATOM 905 CB GLU A 113 -96.713-165.193 148.236 1.00 64.19 C ANISOU 905 CB GLU A 113 7839 7071 9479 -101 281 517 C ATOM 906 CG GLU A 113 -97.177-165.630 149.620 1.00 69.40 C ANISOU 906 CG GLU A 113 8431 7744 10192 13 68 505 C ATOM 907 CD GLU A 113 -98.500-165.014 150.033 1.00 83.82 C ANISOU 907 CD GLU A 113 10390 9596 11862 52 -85 570 C ATOM 908 OE1 GLU A 113 -98.791-163.875 149.614 1.00 85.72 O ANISOU 908 OE1 GLU A 113 10720 9807 12042 4 -82 635 O ATOM 909 OE2 GLU A 113 -99.252-165.675 150.779 1.00 98.84 O ANISOU 909 OE2 GLU A 113 12299 11536 13718 129 -202 558 O ATOM 910 N GLY A 114 -99.149-164.812 146.164 1.00 74.03 N ANISOU 910 N GLY A 114 9554 8404 10171 -193 265 678 N ATOM 911 CA GLY A 114 -100.563-164.621 145.893 1.00 59.31 C ANISOU 911 CA GLY A 114 7840 6569 8127 -174 116 768 C ATOM 912 C GLY A 114 -101.153-165.733 145.046 1.00 68.57 C ANISOU 912 C GLY A 114 9129 7805 9119 -205 154 742 C ATOM 913 O GLY A 114 -102.230-166.250 145.349 1.00 62.58 O ANISOU 913 O GLY A 114 8391 7085 8302 -137 12 756 O ATOM 914 N PHE A 115 -100.453-166.125 143.982 1.00 64.19 N ANISOU 914 N PHE A 115 8655 7257 8478 -320 358 693 N ATOM 915 CA PHE A 115 -100.973-167.156 143.087 1.00 69.06 C ANISOU 915 CA PHE A 115 9416 7924 8898 -375 407 652 C ATOM 916 C PHE A 115 -101.145-168.488 143.813 1.00 76.85 C ANISOU 916 C PHE A 115 10282 8934 9985 -262 374 545 C ATOM 917 O PHE A 115 -102.231-169.081 143.793 1.00 74.24 O ANISOU 917 O PHE A 115 10022 8643 9544 -234 241 563 O ATOM 918 CB PHE A 115 -100.045-167.309 141.876 1.00 65.51 C ANISOU 918 CB PHE A 115 9080 7468 8345 -532 683 588 C ATOM 919 CG PHE A 115 -100.388-168.464 140.981 1.00 85.44 C ANISOU 919 CG PHE A 115 11758 10032 10673 -604 775 502 C ATOM 920 CD1 PHE A 115 -101.394-168.351 140.034 1.00 90.19 C ANISOU 920 CD1 PHE A 115 12618 10674 10977 -714 669 592 C ATOM 921 CD2 PHE A 115 -99.692-169.659 141.075 1.00 87.51 C ANISOU 921 CD2 PHE A 115 11910 10277 11062 -567 956 329 C ATOM 922 CE1 PHE A 115 -101.709-169.415 139.209 1.00 90.29 C ANISOU 922 CE1 PHE A 115 12794 10720 10794 -799 744 502 C ATOM 923 CE2 PHE A 115 -100.004-170.723 140.253 1.00 84.25 C ANISOU 923 CE2 PHE A 115 11651 9885 10475 -638 1052 230 C ATOM 924 CZ PHE A 115 -101.011-170.601 139.320 1.00 82.32 C ANISOU 924 CZ PHE A 115 11682 9691 9905 -761 949 311 C ATOM 925 N PHE A 116 -100.085-168.971 144.470 1.00 65.54 N ANISOU 925 N PHE A 116 8659 7464 8780 -201 478 444 N ATOM 926 CA PHE A 116 -100.134-170.308 145.060 1.00 72.96 C ANISOU 926 CA PHE A 116 9497 8401 9822 -107 455 351 C ATOM 927 C PHE A 116 -101.070-170.371 146.259 1.00 71.45 C ANISOU 927 C PHE A 116 9247 8234 9666 6 212 411 C ATOM 928 O PHE A 116 -101.737-171.389 146.475 1.00 69.44 O ANISOU 928 O PHE A 116 9007 8000 9379 49 144 383 O ATOM 929 CB PHE A 116 -98.731-170.770 145.448 1.00 60.86 C ANISOU 929 CB PHE A 116 7762 6802 8560 -70 601 246 C ATOM 930 CG PHE A 116 -97.946-171.284 144.292 1.00 67.97 C ANISOU 930 CG PHE A 116 8702 7673 9449 -164 886 131 C ATOM 931 CD1 PHE A 116 -98.273-172.498 143.712 1.00 71.29 C ANISOU 931 CD1 PHE A 116 9211 8092 9783 -177 970 32 C ATOM 932 CD2 PHE A 116 -96.900-170.550 143.761 1.00 70.59 C ANISOU 932 CD2 PHE A 116 8995 7973 9854 -254 1089 110 C ATOM 933 CE1 PHE A 116 -97.561-172.979 142.631 1.00 76.91 C ANISOU 933 CE1 PHE A 116 9979 8768 10475 -274 1266 -101 C ATOM 934 CE2 PHE A 116 -96.183-171.027 142.680 1.00 77.57 C ANISOU 934 CE2 PHE A 116 9924 8828 10722 -355 1396 -15 C ATOM 935 CZ PHE A 116 -96.517-172.244 142.115 1.00 80.26 C ANISOU 935 CZ PHE A 116 10362 9166 10968 -364 1491 -129 C ATOM 936 N ALA A 117 -101.137-169.304 147.055 1.00 67.31 N ANISOU 936 N ALA A 117 8664 7701 9208 44 95 485 N ATOM 937 CA ALA A 117 -102.079-169.302 148.169 1.00 68.77 C ANISOU 937 CA ALA A 117 8816 7909 9405 133 -98 527 C ATOM 938 C ALA A 117 -103.517-169.233 147.669 1.00 69.02 C ANISOU 938 C ALA A 117 8980 7987 9259 118 -196 595 C ATOM 939 O ALA A 117 -104.405-169.887 148.229 1.00 67.22 O ANISOU 939 O ALA A 117 8737 7789 9015 172 -298 594 O ATOM 940 CB ALA A 117 -101.778-168.148 149.123 1.00 60.43 C ANISOU 940 CB ALA A 117 7682 6820 8458 165 -176 565 C ATOM 941 N THR A 118 -103.766-168.452 146.614 1.00 69.95 N ANISOU 941 N THR A 118 9224 8104 9249 36 -177 663 N ATOM 942 CA THR A 118 -105.101-168.414 146.028 1.00 73.71 C ANISOU 942 CA THR A 118 9818 8613 9575 12 -302 742 C ATOM 943 C THR A 118 -105.420-169.723 145.319 1.00 70.90 C ANISOU 943 C THR A 118 9547 8297 9094 -38 -266 684 C ATOM 944 O THR A 118 -106.559-170.198 145.361 1.00 66.84 O ANISOU 944 O THR A 118 9054 7815 8525 -20 -396 711 O ATOM 945 CB THR A 118 -105.222-167.236 145.059 1.00 65.02 C ANISOU 945 CB THR A 118 8848 7485 8369 -78 -322 853 C ATOM 946 OG1 THR A 118 -104.909-166.014 145.740 1.00 73.91 O ANISOU 946 OG1 THR A 118 9896 8554 9633 -32 -351 898 O ATOM 947 CG2 THR A 118 -106.641-167.142 144.498 1.00 55.59 C ANISOU 947 CG2 THR A 118 7755 6310 7056 -98 -502 956 C ATOM 948 N LEU A 119 -104.422-170.317 144.660 1.00 74.94 N ANISOU 948 N LEU A 119 10099 8798 9576 -104 -80 592 N ATOM 949 CA LEU A 119 -104.625-171.602 144.000 1.00 72.81 C ANISOU 949 CA LEU A 119 9918 8547 9201 -155 -20 507 C ATOM 950 C LEU A 119 -104.997-172.680 145.010 1.00 78.21 C ANISOU 950 C LEU A 119 10479 9230 10008 -50 -94 453 C ATOM 951 O LEU A 119 -105.929-173.461 144.784 1.00 68.04 O ANISOU 951 O LEU A 119 9255 7967 8629 -69 -178 448 O ATOM 952 CB LEU A 119 -103.369-172.002 143.231 1.00 69.40 C ANISOU 952 CB LEU A 119 9524 8082 8764 -233 238 390 C ATOM 953 CG LEU A 119 -103.485-173.211 142.302 1.00 77.49 C ANISOU 953 CG LEU A 119 10688 9108 9648 -318 347 278 C ATOM 954 CD1 LEU A 119 -104.282-172.855 141.055 1.00 66.93 C ANISOU 954 CD1 LEU A 119 9611 7815 8003 -474 289 349 C ATOM 955 CD2 LEU A 119 -102.111-173.761 141.932 1.00 73.95 C ANISOU 955 CD2 LEU A 119 10191 8600 9308 -346 638 121 C ATOM 956 N GLY A 120 -104.282-172.729 146.135 1.00 75.16 N ANISOU 956 N GLY A 120 9922 8810 9825 46 -79 423 N ATOM 957 CA GLY A 120 -104.578-173.732 147.146 1.00 67.52 C ANISOU 957 CA GLY A 120 8858 7834 8963 130 -158 393 C ATOM 958 C GLY A 120 -105.993-173.627 147.680 1.00 63.35 C ANISOU 958 C GLY A 120 8342 7354 8374 158 -334 471 C ATOM 959 O GLY A 120 -106.702-174.630 147.796 1.00 62.84 O ANISOU 959 O GLY A 120 8292 7300 8286 160 -387 452 O ATOM 960 N GLY A 121 -106.423-172.409 148.017 1.00 63.67 N ANISOU 960 N GLY A 121 8366 7413 8413 178 -416 554 N ATOM 961 CA GLY A 121 -107.769-172.236 148.537 1.00 63.16 C ANISOU 961 CA GLY A 121 8282 7381 8334 211 -555 616 C ATOM 962 C GLY A 121 -108.839-172.527 147.505 1.00 67.28 C ANISOU 962 C GLY A 121 8904 7934 8724 143 -629 655 C ATOM 963 O GLY A 121 -109.917-173.025 147.841 1.00 66.90 O ANISOU 963 O GLY A 121 8823 7910 8685 157 -723 673 O ATOM 964 N GLU A 122 -108.554-172.230 146.236 1.00 66.86 N ANISOU 964 N GLU A 122 8980 7878 8544 54 -591 671 N ATOM 965 CA GLU A 122 -109.515-172.500 145.173 1.00 69.23 C ANISOU 965 CA GLU A 122 9408 8206 8691 -37 -691 715 C ATOM 966 C GLU A 122 -109.663-173.996 144.918 1.00 78.25 C ANISOU 966 C GLU A 122 10595 9357 9778 -80 -659 622 C ATOM 967 O GLU A 122 -110.785-174.492 144.753 1.00 73.00 O ANISOU 967 O GLU A 122 9948 8716 9074 -111 -791 651 O ATOM 968 CB GLU A 122 -109.097-171.775 143.896 1.00 73.41 C ANISOU 968 CB GLU A 122 10105 8727 9060 -149 -656 763 C ATOM 969 CG GLU A 122 -109.547-170.325 143.823 1.00 83.68 C ANISOU 969 CG GLU A 122 11403 10008 10384 -138 -781 903 C ATOM 970 CD GLU A 122 -111.029-170.187 143.524 1.00 90.90 C ANISOU 970 CD GLU A 122 12326 10932 11277 -151 -1012 1012 C ATOM 971 OE1 GLU A 122 -111.772-169.673 144.387 1.00 93.54 O ANISOU 971 OE1 GLU A 122 12506 11249 11785 -47 -1112 1060 O ATOM 972 OE2 GLU A 122 -111.453-170.597 142.423 1.00 93.83 O ANISOU 972 OE2 GLU A 122 12859 11325 11468 -274 -1093 1043 O ATOM 973 N ILE A 123 -108.549-174.733 144.871 1.00 73.06 N ANISOU 973 N ILE A 123 9947 8666 9145 -83 -487 507 N ATOM 974 CA ILE A 123 -108.632-176.178 144.673 1.00 67.07 C ANISOU 974 CA ILE A 123 9228 7888 8367 -114 -445 406 C ATOM 975 C ILE A 123 -109.425-176.823 145.803 1.00 72.33 C ANISOU 975 C ILE A 123 9770 8558 9154 -38 -556 427 C ATOM 976 O ILE A 123 -110.235-177.729 145.573 1.00 59.08 O ANISOU 976 O ILE A 123 8136 6883 7431 -86 -625 407 O ATOM 977 CB ILE A 123 -107.226-176.795 144.539 1.00 66.74 C ANISOU 977 CB ILE A 123 9177 7783 8400 -106 -229 275 C ATOM 978 CG1 ILE A 123 -106.505-176.236 143.312 1.00 56.02 C ANISOU 978 CG1 ILE A 123 7962 6425 6899 -213 -78 241 C ATOM 979 CG2 ILE A 123 -107.313-178.318 144.423 1.00 61.15 C ANISOU 979 CG2 ILE A 123 8497 7023 7713 -123 -186 164 C ATOM 980 CD1 ILE A 123 -105.033-176.592 143.259 1.00 59.91 C ANISOU 980 CD1 ILE A 123 8392 6847 7524 -193 163 113 C ATOM 981 N ALA A 124 -109.222-176.354 147.037 1.00 59.61 N ANISOU 981 N ALA A 124 8017 6945 7687 64 -573 465 N ATOM 982 CA ALA A 124 -109.979-176.891 148.164 1.00 57.34 C ANISOU 982 CA ALA A 124 7633 6665 7488 115 -658 490 C ATOM 983 C ALA A 124 -111.468-176.611 148.009 1.00 69.38 C ANISOU 983 C ALA A 124 9153 8240 8969 83 -796 565 C ATOM 984 O ALA A 124 -112.299-177.513 148.167 1.00 74.31 O ANISOU 984 O ALA A 124 9764 8868 9601 54 -854 559 O ATOM 985 CB ALA A 124 -109.457-176.307 149.477 1.00 51.10 C ANISOU 985 CB ALA A 124 6730 5867 6819 204 -647 514 C ATOM 986 N LEU A 125 -111.819-175.359 147.699 1.00 76.84 N ANISOU 986 N LEU A 125 10095 9209 9893 87 -855 640 N ATOM 987 CA LEU A 125 -113.217-174.983 147.512 1.00 70.68 C ANISOU 987 CA LEU A 125 9277 8456 9122 69 -1003 721 C ATOM 988 C LEU A 125 -113.898-175.878 146.489 1.00 69.15 C ANISOU 988 C LEU A 125 9180 8274 8821 -39 -1091 715 C ATOM 989 O LEU A 125 -114.980-176.419 146.742 1.00 65.23 O ANISOU 989 O LEU A 125 8613 7792 8381 -57 -1184 734 O ATOM 990 CB LEU A 125 -113.308-173.519 147.080 1.00 62.94 C ANISOU 990 CB LEU A 125 8303 7469 8141 82 -1063 808 C ATOM 991 CG LEU A 125 -114.671-173.051 146.559 1.00 63.34 C ANISOU 991 CG LEU A 125 8322 7525 8220 55 -1248 910 C ATOM 992 CD1 LEU A 125 -115.729-173.082 147.658 1.00 57.29 C ANISOU 992 CD1 LEU A 125 7367 6764 7636 127 -1281 918 C ATOM 993 CD2 LEU A 125 -114.569-171.660 145.940 1.00 66.08 C ANISOU 993 CD2 LEU A 125 8713 7839 8557 56 -1318 1009 C ATOM 994 N TRP A 126 -113.276-176.047 145.325 1.00 60.38 N ANISOU 994 N TRP A 126 8237 7155 7551 -127 -1053 680 N ATOM 995 CA TRP A 126 -113.899-176.823 144.267 1.00 66.21 C ANISOU 995 CA TRP A 126 9106 7901 8150 -255 -1146 665 C ATOM 996 C TRP A 126 -113.801-178.322 144.501 1.00 75.65 C ANISOU 996 C TRP A 126 10314 9069 9362 -277 -1075 553 C ATOM 997 O TRP A 126 -114.593-179.076 143.927 1.00 76.42 O ANISOU 997 O TRP A 126 10479 9168 9390 -376 -1179 539 O ATOM 998 CB TRP A 126 -113.293-176.437 142.918 1.00 56.17 C ANISOU 998 CB TRP A 126 8047 6629 6666 -367 -1114 660 C ATOM 999 CG TRP A 126 -113.744-175.073 142.502 1.00 83.83 C ANISOU 999 CG TRP A 126 11564 10145 10140 -379 -1259 807 C ATOM 1000 CD1 TRP A 126 -113.023-173.918 142.558 1.00 84.25 C ANISOU 1000 CD1 TRP A 126 11617 10185 10210 -334 -1191 857 C ATOM 1001 CD2 TRP A 126 -115.040-174.715 142.010 1.00 85.22 C ANISOU 1001 CD2 TRP A 126 11742 10335 10304 -435 -1515 933 C ATOM 1002 NE1 TRP A 126 -113.783-172.864 142.112 1.00 86.18 N ANISOU 1002 NE1 TRP A 126 11876 10424 10446 -357 -1385 1009 N ATOM 1003 CE2 TRP A 126 -115.026-173.327 141.770 1.00 85.18 C ANISOU 1003 CE2 TRP A 126 11742 10311 10311 -414 -1594 1062 C ATOM 1004 CE3 TRP A 126 -116.207-175.435 141.738 1.00 82.18 C ANISOU 1004 CE3 TRP A 126 11343 9964 9919 -506 -1699 955 C ATOM 1005 CZ2 TRP A 126 -116.135-172.643 141.274 1.00 86.84 C ANISOU 1005 CZ2 TRP A 126 11938 10508 10549 -450 -1860 1218 C ATOM 1006 CZ3 TRP A 126 -117.308-174.755 141.242 1.00 86.53 C ANISOU 1006 CZ3 TRP A 126 11869 10512 10498 -547 -1965 1106 C ATOM 1007 CH2 TRP A 126 -117.263-173.373 141.016 1.00 85.14 C ANISOU 1007 CH2 TRP A 126 11692 10309 10348 -514 -2049 1240 C ATOM 1008 N SER A 127 -112.862-178.769 145.337 1.00 68.51 N ANISOU 1008 N SER A 127 9344 8125 8560 -193 -922 479 N ATOM 1009 CA SER A 127 -112.868-180.163 145.762 1.00 71.43 C ANISOU 1009 CA SER A 127 9699 8447 8995 -197 -882 399 C ATOM 1010 C SER A 127 -114.119-180.473 146.575 1.00 75.95 C ANISOU 1010 C SER A 127 10150 9042 9664 -188 -1006 466 C ATOM 1011 O SER A 127 -114.745-181.522 146.389 1.00 73.16 O ANISOU 1011 O SER A 127 9827 8665 9305 -260 -1057 433 O ATOM 1012 CB SER A 127 -111.605-180.478 146.562 1.00 60.46 C ANISOU 1012 CB SER A 127 8247 6998 7728 -102 -731 338 C ATOM 1013 OG SER A 127 -110.455-180.443 145.731 1.00 63.90 O ANISOU 1013 OG SER A 127 8776 7395 8108 -125 -585 249 O ATOM 1014 N LEU A 128 -114.502-179.567 147.480 1.00 70.15 N ANISOU 1014 N LEU A 128 9280 8348 9026 -109 -1039 549 N ATOM 1015 CA LEU A 128 -115.739-179.750 148.237 1.00 71.01 C ANISOU 1015 CA LEU A 128 9263 8482 9237 -109 -1121 604 C ATOM 1016 C LEU A 128 -116.955-179.712 147.321 1.00 74.25 C ANISOU 1016 C LEU A 128 9678 8920 9615 -201 -1285 652 C ATOM 1017 O LEU A 128 -117.939-180.430 147.546 1.00 73.87 O ANISOU 1017 O LEU A 128 9561 8872 9635 -253 -1354 663 O ATOM 1018 CB LEU A 128 -115.863-178.685 149.321 1.00 66.35 C ANISOU 1018 CB LEU A 128 8540 7920 8750 -12 -1091 659 C ATOM 1019 CG LEU A 128 -114.794-178.671 150.409 1.00 73.64 C ANISOU 1019 CG LEU A 128 9450 8820 9709 64 -970 628 C ATOM 1020 CD1 LEU A 128 -115.241-177.790 151.568 1.00 76.81 C ANISOU 1020 CD1 LEU A 128 9738 9250 10196 124 -946 667 C ATOM 1021 CD2 LEU A 128 -114.506-180.084 150.879 1.00 76.24 C ANISOU 1021 CD2 LEU A 128 9812 9101 10053 36 -932 586 C ATOM 1022 N VAL A 129 -116.910-178.873 146.285 1.00 70.59 N ANISOU 1022 N VAL A 129 9295 8473 9052 -233 -1365 693 N ATOM 1023 CA VAL A 129 -118.001-178.832 145.317 1.00 72.04 C ANISOU 1023 CA VAL A 129 9506 8674 9193 -337 -1566 755 C ATOM 1024 C VAL A 129 -118.057-180.132 144.525 1.00 74.73 C ANISOU 1024 C VAL A 129 9998 8991 9404 -470 -1596 674 C ATOM 1025 O VAL A 129 -119.131-180.716 144.341 1.00 78.66 O ANISOU 1025 O VAL A 129 10453 9491 9945 -553 -1740 695 O ATOM 1026 CB VAL A 129 -117.849-177.610 144.392 1.00 66.11 C ANISOU 1026 CB VAL A 129 8841 7934 8344 -354 -1660 838 C ATOM 1027 CG1 VAL A 129 -118.909-177.635 143.299 1.00 60.19 C ANISOU 1027 CG1 VAL A 129 8151 7193 7526 -483 -1911 917 C ATOM 1028 CG2 VAL A 129 -117.932-176.314 145.197 1.00 66.79 C ANISOU 1028 CG2 VAL A 129 8765 8020 8593 -222 -1643 914 C ATOM 1029 N VAL A 130 -116.905-180.612 144.055 1.00 74.31 N ANISOU 1029 N VAL A 130 10115 8905 9213 -496 -1452 568 N ATOM 1030 CA VAL A 130 -116.878-181.833 143.253 1.00 78.83 C ANISOU 1030 CA VAL A 130 10854 9437 9661 -626 -1451 462 C ATOM 1031 C VAL A 130 -117.287-183.038 144.092 1.00 80.27 C ANISOU 1031 C VAL A 130 10938 9574 9987 -617 -1428 416 C ATOM 1032 O VAL A 130 -118.045-183.901 143.633 1.00 74.55 O ANISOU 1032 O VAL A 130 10265 8827 9232 -736 -1536 387 O ATOM 1033 CB VAL A 130 -115.490-182.019 142.616 1.00 77.88 C ANISOU 1033 CB VAL A 130 10916 9276 9401 -643 -1254 339 C ATOM 1034 CG1 VAL A 130 -115.295-183.465 142.156 1.00 75.58 C ANISOU 1034 CG1 VAL A 130 10759 8907 9052 -737 -1181 188 C ATOM 1035 CG2 VAL A 130 -115.331-181.076 141.443 1.00 65.44 C ANISOU 1035 CG2 VAL A 130 9509 7741 7614 -732 -1306 382 C ATOM 1036 N LEU A 131 -116.803-183.116 145.334 1.00 68.44 N ANISOU 1036 N LEU A 131 9310 8056 8639 -491 -1301 417 N ATOM 1037 CA LEU A 131 -117.193-184.224 146.201 1.00 71.04 C ANISOU 1037 CA LEU A 131 9560 8336 9096 -494 -1284 399 C ATOM 1038 C LEU A 131 -118.703-184.252 146.413 1.00 80.09 C ANISOU 1038 C LEU A 131 10579 9524 10327 -557 -1441 483 C ATOM 1039 O LEU A 131 -119.314-185.328 146.432 1.00 84.20 O ANISOU 1039 O LEU A 131 11101 10001 10889 -646 -1487 455 O ATOM 1040 CB LEU A 131 -116.459-184.129 147.539 1.00 62.10 C ANISOU 1040 CB LEU A 131 8326 7184 8085 -364 -1154 417 C ATOM 1041 CG LEU A 131 -116.810-185.210 148.561 1.00 73.08 C ANISOU 1041 CG LEU A 131 9654 8520 9595 -374 -1137 426 C ATOM 1042 CD1 LEU A 131 -116.549-186.593 147.990 1.00 66.41 C ANISOU 1042 CD1 LEU A 131 8932 7565 8735 -451 -1120 327 C ATOM 1043 CD2 LEU A 131 -116.029-185.009 149.842 1.00 75.89 C ANISOU 1043 CD2 LEU A 131 9945 8859 10031 -264 -1040 460 C ATOM 1044 N ALA A 132 -119.324-183.079 146.561 1.00 74.67 N ANISOU 1044 N ALA A 132 9767 8909 9695 -513 -1521 582 N ATOM 1045 CA ALA A 132 -120.776-183.023 146.697 1.00 66.32 C ANISOU 1045 CA ALA A 132 8551 7883 8766 -566 -1667 658 C ATOM 1046 C ALA A 132 -121.467-183.519 145.435 1.00 77.23 C ANISOU 1046 C ALA A 132 10030 9255 10059 -722 -1863 652 C ATOM 1047 O ALA A 132 -122.469-184.241 145.507 1.00 78.69 O ANISOU 1047 O ALA A 132 10130 9426 10341 -813 -1961 663 O ATOM 1048 CB ALA A 132 -121.221-181.596 147.025 1.00 68.20 C ANISOU 1048 CB ALA A 132 8628 8172 9111 -474 -1707 754 C ATOM 1049 N ILE A 133 -120.945-183.141 144.267 1.00 73.98 N ANISOU 1049 N ILE A 133 9808 8849 9451 -772 -1923 633 N ATOM 1050 CA ILE A 133 -121.530-183.581 143.006 1.00 71.43 C ANISOU 1050 CA ILE A 133 9630 8518 8991 -946 -2123 623 C ATOM 1051 C ILE A 133 -121.393-185.089 142.848 1.00 82.37 C ANISOU 1051 C ILE A 133 11140 9835 10324 -1050 -2065 493 C ATOM 1052 O ILE A 133 -122.342-185.772 142.442 1.00 88.70 O ANISOU 1052 O ILE A 133 11941 10619 11143 -1188 -2233 493 O ATOM 1053 CB ILE A 133 -120.883-182.828 141.830 1.00 73.84 C ANISOU 1053 CB ILE A 133 10156 8844 9055 -995 -2166 629 C ATOM 1054 CG1 ILE A 133 -121.189-181.331 141.913 1.00 78.39 C ANISOU 1054 CG1 ILE A 133 10606 9467 9710 -907 -2271 780 C ATOM 1055 CG2 ILE A 133 -121.359-183.398 140.500 1.00 70.95 C ANISOU 1055 CG2 ILE A 133 10005 8466 8485 -1206 -2361 599 C ATOM 1056 CD1 ILE A 133 -120.583-180.524 140.789 1.00 64.83 C ANISOU 1056 CD1 ILE A 133 9114 7765 7754 -968 -2322 814 C ATOM 1057 N GLU A 134 -120.218-185.635 143.170 1.00 79.54 N ANISOU 1057 N GLU A 134 10877 9420 9926 -987 -1837 381 N ATOM 1058 CA GLU A 134 -120.004-187.070 143.012 1.00 75.28 C ANISOU 1058 CA GLU A 134 10457 8782 9363 -1071 -1770 249 C ATOM 1059 C GLU A 134 -120.940-187.867 143.910 1.00 78.81 C ANISOU 1059 C GLU A 134 10734 9199 10012 -1093 -1819 289 C ATOM 1060 O GLU A 134 -121.584-188.823 143.460 1.00 73.39 O ANISOU 1060 O GLU A 134 10109 8460 9317 -1238 -1922 240 O ATOM 1061 CB GLU A 134 -118.544-187.414 143.304 1.00 72.03 C ANISOU 1061 CB GLU A 134 10129 8297 8941 -969 -1519 139 C ATOM 1062 CG GLU A 134 -117.571-186.782 142.329 1.00 76.18 C ANISOU 1062 CG GLU A 134 10835 8840 9269 -977 -1430 73 C ATOM 1063 CD GLU A 134 -116.123-187.088 142.655 1.00 81.05 C ANISOU 1063 CD GLU A 134 11483 9377 9936 -867 -1177 -37 C ATOM 1064 OE1 GLU A 134 -115.853-187.620 143.754 1.00 88.09 O ANISOU 1064 OE1 GLU A 134 12243 10207 11020 -763 -1103 -28 O ATOM 1065 OE2 GLU A 134 -115.257-186.792 141.805 1.00 72.85 O ANISOU 1065 OE2 GLU A 134 10599 8330 8749 -893 -1056 -125 O ATOM 1066 N ARG A 135 -121.033-187.484 145.186 1.00 74.11 N ANISOU 1066 N ARG A 135 9937 8634 9589 -968 -1740 375 N ATOM 1067 CA ARG A 135 -121.934-188.176 146.101 1.00 68.80 C ANISOU 1067 CA ARG A 135 9106 7938 9097 -1003 -1757 422 C ATOM 1068 C ARG A 135 -123.389-188.056 145.663 1.00 81.00 C ANISOU 1068 C ARG A 135 10532 9529 10715 -1124 -1973 491 C ATOM 1069 O ARG A 135 -124.173-188.994 145.854 1.00 79.35 O ANISOU 1069 O ARG A 135 10267 9274 10609 -1234 -2027 486 O ATOM 1070 CB ARG A 135 -121.753-187.623 147.515 1.00 66.69 C ANISOU 1070 CB ARG A 135 8674 7706 8958 -863 -1620 498 C ATOM 1071 CG ARG A 135 -120.397-187.963 148.137 1.00 66.85 C ANISOU 1071 CG ARG A 135 8787 7661 8952 -761 -1442 448 C ATOM 1072 CD ARG A 135 -120.139-187.152 149.398 1.00 65.96 C ANISOU 1072 CD ARG A 135 8548 7601 8911 -635 -1338 525 C ATOM 1073 NE ARG A 135 -119.019-187.695 150.160 1.00 74.72 N ANISOU 1073 NE ARG A 135 9726 8633 10032 -564 -1215 502 N ATOM 1074 CZ ARG A 135 -118.510-187.128 151.248 1.00 71.68 C ANISOU 1074 CZ ARG A 135 9287 8275 9675 -467 -1130 555 C ATOM 1075 NH1 ARG A 135 -119.015-185.990 151.700 1.00 76.60 N ANISOU 1075 NH1 ARG A 135 9793 8998 10314 -424 -1121 612 N ATOM 1076 NH2 ARG A 135 -117.493-187.698 151.877 1.00 82.61 N ANISOU 1076 NH2 ARG A 135 10735 9573 11080 -416 -1064 547 N ATOM 1077 N TYR A 136 -123.764-186.924 145.061 1.00 77.52 N ANISOU 1077 N TYR A 136 10045 9167 10243 -1112 -2112 562 N ATOM 1078 CA TYR A 136 -125.119-186.775 144.545 1.00 83.99 C ANISOU 1078 CA TYR A 136 10737 10016 11158 -1226 -2359 639 C ATOM 1079 C TYR A 136 -125.379-187.737 143.396 1.00 88.55 C ANISOU 1079 C TYR A 136 11510 10542 11594 -1422 -2525 564 C ATOM 1080 O TYR A 136 -126.474-188.297 143.287 1.00 90.83 O ANISOU 1080 O TYR A 136 11692 10814 12006 -1551 -2688 591 O ATOM 1081 CB TYR A 136 -125.351-185.331 144.095 1.00 72.09 C ANISOU 1081 CB TYR A 136 9159 8579 9654 -1164 -2494 744 C ATOM 1082 CG TYR A 136 -126.574-185.151 143.223 1.00 74.22 C ANISOU 1082 CG TYR A 136 9351 8862 9988 -1297 -2814 829 C ATOM 1083 CD1 TYR A 136 -127.846-185.096 143.776 1.00 81.15 C ANISOU 1083 CD1 TYR A 136 9921 9746 11164 -1308 -2909 910 C ATOM 1084 CD2 TYR A 136 -126.455-185.026 141.842 1.00 79.97 C ANISOU 1084 CD2 TYR A 136 10313 9591 10480 -1422 -3023 831 C ATOM 1085 CE1 TYR A 136 -128.964-184.931 142.979 1.00 82.77 C ANISOU 1085 CE1 TYR A 136 10026 9953 11470 -1429 -3232 999 C ATOM 1086 CE2 TYR A 136 -127.570-184.860 141.040 1.00 85.85 C ANISOU 1086 CE2 TYR A 136 10997 10342 11280 -1557 -3362 927 C ATOM 1087 CZ TYR A 136 -128.820-184.811 141.613 1.00 91.51 C ANISOU 1087 CZ TYR A 136 11377 11059 12333 -1553 -3478 1015 C ATOM 1088 OH TYR A 136 -129.929-184.646 140.813 1.00100.39 O ANISOU 1088 OH TYR A 136 12414 12179 13552 -1686 -3844 1121 O ATOM 1089 N VAL A 137 -124.389-187.922 142.520 1.00 84.77 N ANISOU 1089 N VAL A 137 11316 10033 10859 -1458 -2479 461 N ATOM 1090 CA VAL A 137 -124.558-188.805 141.369 1.00 91.34 C ANISOU 1090 CA VAL A 137 12381 10811 11515 -1659 -2616 362 C ATOM 1091 C VAL A 137 -124.672-190.258 141.816 1.00 95.55 C ANISOU 1091 C VAL A 137 12924 11238 12144 -1728 -2530 263 C ATOM 1092 O VAL A 137 -125.520-191.010 141.320 1.00 98.77 O ANISOU 1092 O VAL A 137 13360 11604 12563 -1907 -2708 238 O ATOM 1093 CB VAL A 137 -123.394-188.605 140.378 1.00 79.56 C ANISOU 1093 CB VAL A 137 11199 9309 9722 -1680 -2525 256 C ATOM 1094 CG1 VAL A 137 -123.464-189.623 139.255 1.00 81.71 C ANISOU 1094 CG1 VAL A 137 11749 9510 9789 -1897 -2610 113 C ATOM 1095 CG2 VAL A 137 -123.402-187.191 139.817 1.00 71.88 C ANISOU 1095 CG2 VAL A 137 10241 8431 8640 -1651 -2651 375 C ATOM 1096 N VAL A 138 -123.829-190.672 142.765 1.00 86.69 N ANISOU 1096 N VAL A 138 11780 10059 11101 -1597 -2275 215 N ATOM 1097 CA VAL A 138 -123.801-192.070 143.188 1.00 84.15 C ANISOU 1097 CA VAL A 138 11494 9608 10871 -1656 -2189 128 C ATOM 1098 C VAL A 138 -125.082-192.445 143.929 1.00 90.41 C ANISOU 1098 C VAL A 138 12052 10407 11893 -1725 -2290 229 C ATOM 1099 O VAL A 138 -125.606-193.554 143.766 1.00 95.02 O ANISOU 1099 O VAL A 138 12677 10897 12528 -1874 -2357 175 O ATOM 1100 CB VAL A 138 -122.548-192.333 144.044 1.00 76.98 C ANISOU 1100 CB VAL A 138 10612 8630 10009 -1491 -1925 82 C ATOM 1101 CG1 VAL A 138 -122.595-193.722 144.667 1.00 83.47 C ANISOU 1101 CG1 VAL A 138 11439 9304 10971 -1538 -1855 36 C ATOM 1102 CG2 VAL A 138 -121.290-192.169 143.202 1.00 66.88 C ANISOU 1102 CG2 VAL A 138 9558 7318 8535 -1451 -1805 -49 C ATOM 1103 N VAL A 139 -125.614-191.534 144.738 1.00 90.05 N ANISOU 1103 N VAL A 139 11757 10461 11997 -1629 -2288 367 N ATOM 1104 CA VAL A 139 -126.767-191.847 145.580 1.00 87.51 C ANISOU 1104 CA VAL A 139 11189 10146 11917 -1685 -2319 454 C ATOM 1105 C VAL A 139 -128.081-191.590 144.853 1.00 88.11 C ANISOU 1105 C VAL A 139 11130 10270 12077 -1826 -2593 514 C ATOM 1106 O VAL A 139 -128.945-192.468 144.784 1.00 94.91 O ANISOU 1106 O VAL A 139 11931 11077 13055 -1986 -2699 508 O ATOM 1107 CB VAL A 139 -126.691-191.052 146.899 1.00 77.15 C ANISOU 1107 CB VAL A 139 9674 8902 10736 -1521 -2141 550 C ATOM 1108 CG1 VAL A 139 -127.950-191.274 147.728 1.00 81.61 C ANISOU 1108 CG1 VAL A 139 9977 9483 11550 -1595 -2141 632 C ATOM 1109 CG2 VAL A 139 -125.458-191.461 147.679 1.00 67.63 C ANISOU 1109 CG2 VAL A 139 8599 7634 9465 -1411 -1915 507 C ATOM 1110 N CYS A 140 -128.263-190.388 144.307 1.00 87.46 N ANISOU 1110 N CYS A 140 10992 10280 11960 -1774 -2731 583 N ATOM 1111 CA CYS A 140 -129.527-190.028 143.677 1.00 88.61 C ANISOU 1111 CA CYS A 140 10973 10464 12231 -1891 -3026 669 C ATOM 1112 C CYS A 140 -129.694-190.625 142.288 1.00 94.57 C ANISOU 1112 C CYS A 140 11965 11176 12791 -2095 -3283 604 C ATOM 1113 O CYS A 140 -130.807-190.582 141.751 1.00104.89 O ANISOU 1113 O CYS A 140 13145 12494 14212 -2233 -3570 674 O ATOM 1114 CB CYS A 140 -129.659-188.505 143.599 1.00 94.62 C ANISOU 1114 CB CYS A 140 11591 11314 13046 -1758 -3102 783 C ATOM 1115 SG CYS A 140 -129.552-187.692 145.211 1.00 94.81 S ANISOU 1115 SG CYS A 140 11344 11386 13294 -1534 -2804 841 S ATOM 1116 N LYS A 141 -128.624-191.172 141.702 1.00 94.39 N ANISOU 1116 N LYS A 141 12278 11099 12488 -2125 -3185 467 N ATOM 1117 CA LYS A 141 -128.625-191.827 140.395 1.00 98.65 C ANISOU 1117 CA LYS A 141 13107 11585 12789 -2333 -3372 363 C ATOM 1118 C LYS A 141 -129.426-191.043 139.359 1.00106.04 C ANISOU 1118 C LYS A 141 14039 12591 13661 -2452 -3734 468 C ATOM 1119 O LYS A 141 -130.461-191.527 138.883 1.00112.51 O ANISOU 1119 O LYS A 141 14807 13386 14556 -2644 -4008 492 O ATOM 1120 CB LYS A 141 -129.177-193.250 140.521 1.00 90.55 C ANISOU 1120 CB LYS A 141 12087 10449 11869 -2499 -3399 280 C ATOM 1121 CG LYS A 141 -128.359-194.150 141.442 1.00 91.97 C ANISOU 1121 CG LYS A 141 12313 10528 12103 -2405 -3078 184 C ATOM 1122 CD LYS A 141 -129.017-195.510 141.626 1.00103.76 C ANISOU 1122 CD LYS A 141 13789 11899 13736 -2575 -3120 128 C ATOM 1123 CE LYS A 141 -128.259-196.365 142.635 1.00109.21 C ANISOU 1123 CE LYS A 141 14508 12474 14515 -2477 -2828 71 C ATOM 1124 NZ LYS A 141 -128.976-197.640 142.928 1.00118.56 N ANISOU 1124 NZ LYS A 141 15650 13530 15866 -2643 -2867 46 N ATOM 1125 N PRO A 142 -128.994-189.833 138.986 1.00111.59 N ANISOU 1125 N PRO A 142 14793 13371 14235 -2353 -3768 546 N ATOM 1126 CA PRO A 142 -129.733-189.070 137.970 1.00112.10 C ANISOU 1126 CA PRO A 142 14875 13486 14233 -2473 -4147 672 C ATOM 1127 C PRO A 142 -129.452-189.514 136.545 1.00109.83 C ANISOU 1127 C PRO A 142 15003 13172 13557 -2705 -4320 573 C ATOM 1128 O PRO A 142 -130.165-189.080 135.631 1.00108.90 O ANISOU 1128 O PRO A 142 14936 13081 13359 -2859 -4691 681 O ATOM 1129 CB PRO A 142 -129.251-187.635 138.203 1.00109.75 C ANISOU 1129 CB PRO A 142 14498 13260 13942 -2271 -4076 788 C ATOM 1130 CG PRO A 142 -127.854-187.805 138.684 1.00103.38 C ANISOU 1130 CG PRO A 142 13851 12439 12987 -2131 -3683 656 C ATOM 1131 CD PRO A 142 -127.827-189.086 139.489 1.00107.84 C ANISOU 1131 CD PRO A 142 14357 12932 13686 -2136 -3482 536 C ATOM 1132 N MET A 143 -128.439-190.348 136.327 1.00111.83 N ANISOU 1132 N MET A 143 15555 13363 13571 -2742 -4065 371 N ATOM 1133 CA MET A 143 -128.152-190.933 135.025 1.00116.35 C ANISOU 1133 CA MET A 143 16546 13894 13768 -2981 -4167 228 C ATOM 1134 C MET A 143 -128.406-192.433 135.109 1.00124.65 C ANISOU 1134 C MET A 143 17658 14830 14875 -3121 -4123 62 C ATOM 1135 O MET A 143 -127.859-193.111 135.985 1.00124.43 O ANISOU 1135 O MET A 143 17554 14729 14993 -2993 -3814 -38 O ATOM 1136 CB MET A 143 -126.711-190.637 134.600 1.00112.12 C ANISOU 1136 CB MET A 143 16321 13362 12917 -2917 -3875 104 C ATOM 1137 CG MET A 143 -126.344-189.159 134.696 1.00122.96 C ANISOU 1137 CG MET A 143 17613 14835 14271 -2755 -3864 268 C ATOM 1138 SD MET A 143 -124.644-188.769 134.227 1.00127.04 S ANISOU 1138 SD MET A 143 18461 15356 14451 -2689 -3503 129 S ATOM 1139 CE MET A 143 -124.698-189.116 132.467 1.00138.55 C ANISOU 1139 CE MET A 143 20423 16802 15419 -3040 -3706 22 C ATOM 1140 N SER A 144 -129.238-192.944 134.198 1.00129.03 N ANISOU 1140 N SER A 144 18354 15355 15315 -3392 -4452 41 N ATOM 1141 CA SER A 144 -129.794-194.283 134.370 1.00139.05 C ANISOU 1141 CA SER A 144 19600 16513 16721 -3537 -4484 -73 C ATOM 1142 C SER A 144 -128.752-195.373 134.144 1.00145.79 C ANISOU 1142 C SER A 144 20782 17237 17375 -3579 -4170 -345 C ATOM 1143 O SER A 144 -128.731-196.375 134.870 1.00149.57 O ANISOU 1143 O SER A 144 21161 17602 18065 -3544 -3997 -434 O ATOM 1144 CB SER A 144 -130.985-194.472 133.431 1.00144.81 C ANISOU 1144 CB SER A 144 20387 17245 17389 -3830 -4955 -16 C ATOM 1145 OG SER A 144 -130.662-194.056 132.117 1.00149.34 O ANISOU 1145 OG SER A 144 21356 17856 17530 -4002 -5127 -51 O ATOM 1146 N ASN A 145 -127.888-195.211 133.146 1.00145.52 N ANISOU 1146 N ASN A 145 21137 17203 16950 -3658 -4084 -480 N ATOM 1147 CA ASN A 145 -126.901-196.226 132.787 1.00145.42 C ANISOU 1147 CA ASN A 145 21448 17052 16752 -3713 -3779 -765 C ATOM 1148 C ASN A 145 -125.488-195.810 133.186 1.00139.76 C ANISOU 1148 C ASN A 145 20765 16337 16001 -3467 -3364 -835 C ATOM 1149 O ASN A 145 -124.537-195.990 132.423 1.00143.05 O ANISOU 1149 O ASN A 145 21516 16704 16131 -3527 -3152 -1033 O ATOM 1150 CB ASN A 145 -126.953-196.528 131.291 1.00149.55 C ANISOU 1150 CB ASN A 145 22426 17550 16845 -4028 -3948 -921 C ATOM 1151 CG ASN A 145 -128.289-197.097 130.854 1.00153.37 C ANISOU 1151 CG ASN A 145 22906 18007 17360 -4300 -4370 -882 C ATOM 1152 OD1 ASN A 145 -128.942-197.828 131.600 1.00150.07 O ANISOU 1152 OD1 ASN A 145 22230 17514 17276 -4285 -4414 -859 O ATOM 1153 ND2 ASN A 145 -128.703-196.764 129.636 1.00157.48 N ANISOU 1153 ND2 ASN A 145 23673 18600 17562 -4501 -4626 -842 N ATOM 1154 N PHE A 146 -125.325-195.267 134.390 1.00128.02 N ANISOU 1154 N PHE A 146 18930 14901 14811 -3198 -3233 -682 N ATOM 1155 CA PHE A 146 -124.071-194.648 134.797 1.00114.10 C ANISOU 1155 CA PHE A 146 17155 13164 13033 -2965 -2904 -701 C ATOM 1156 C PHE A 146 -123.409-195.416 135.934 1.00106.48 C ANISOU 1156 C PHE A 146 16029 12077 12352 -2770 -2598 -776 C ATOM 1157 O PHE A 146 -124.078-195.867 136.869 1.00100.74 O ANISOU 1157 O PHE A 146 15047 11316 11912 -2724 -2659 -685 O ATOM 1158 CB PHE A 146 -124.293-193.197 135.225 1.00111.67 C ANISOU 1158 CB PHE A 146 16610 13019 12802 -2811 -3010 -454 C ATOM 1159 CG PHE A 146 -123.020-192.437 135.455 1.00107.61 C ANISOU 1159 CG PHE A 146 16120 12540 12226 -2612 -2714 -470 C ATOM 1160 CD1 PHE A 146 -122.327-191.891 134.390 1.00109.45 C ANISOU 1160 CD1 PHE A 146 16656 12813 12116 -2698 -2656 -540 C ATOM 1161 CD2 PHE A 146 -122.515-192.273 136.734 1.00104.10 C ANISOU 1161 CD2 PHE A 146 15407 12090 12058 -2357 -2496 -413 C ATOM 1162 CE1 PHE A 146 -121.153-191.191 134.594 1.00108.01 C ANISOU 1162 CE1 PHE A 146 16481 12660 11900 -2527 -2377 -556 C ATOM 1163 CE2 PHE A 146 -121.341-191.574 136.945 1.00105.82 C ANISOU 1163 CE2 PHE A 146 15636 12335 12234 -2186 -2245 -428 C ATOM 1164 CZ PHE A 146 -120.659-191.033 135.873 1.00105.36 C ANISOU 1164 CZ PHE A 146 15854 12313 11865 -2267 -2181 -500 C ATOM 1165 N ARG A 147 -122.085-195.539 135.847 1.00105.56 N ANISOU 1165 N ARG A 147 16059 11890 12159 -2663 -2272 -935 N ATOM 1166 CA ARG A 147 -121.261-196.130 136.898 1.00109.17 C ANISOU 1166 CA ARG A 147 16370 12225 12885 -2456 -1989 -989 C ATOM 1167 C ARG A 147 -120.028-195.257 137.078 1.00106.34 C ANISOU 1167 C ARG A 147 15994 11921 12491 -2259 -1741 -986 C ATOM 1168 O ARG A 147 -119.264-195.063 136.128 1.00109.54 O ANISOU 1168 O ARG A 147 16648 12319 12652 -2320 -1598 -1134 O ATOM 1169 CB ARG A 147 -120.860-197.566 136.547 1.00119.32 C ANISOU 1169 CB ARG A 147 17858 13292 14187 -2551 -1835 -1242 C ATOM 1170 CG ARG A 147 -119.739-198.134 137.402 1.00130.11 C ANISOU 1170 CG ARG A 147 19127 14503 15806 -2336 -1527 -1321 C ATOM 1171 CD ARG A 147 -120.227-198.543 138.781 1.00139.07 C ANISOU 1171 CD ARG A 147 19970 15595 17274 -2222 -1589 -1153 C ATOM 1172 NE ARG A 147 -119.169-199.180 139.560 1.00145.16 N ANISOU 1172 NE ARG A 147 20675 16193 18285 -2038 -1341 -1217 N ATOM 1173 CZ ARG A 147 -118.475-198.574 140.518 1.00146.20 C ANISOU 1173 CZ ARG A 147 20612 16372 18565 -1815 -1228 -1091 C ATOM 1174 NH1 ARG A 147 -118.735-197.310 140.828 1.00147.61 N ANISOU 1174 NH1 ARG A 147 20649 16763 18674 -1745 -1315 -910 N ATOM 1175 NH2 ARG A 147 -117.527-199.233 141.172 1.00144.18 N ANISOU 1175 NH2 ARG A 147 20304 15939 18540 -1665 -1043 -1144 N ATOM 1176 N PHE A 148 -119.836-194.736 138.288 1.00100.75 N ANISOU 1176 N PHE A 148 15000 11263 12020 -2040 -1683 -825 N ATOM 1177 CA PHE A 148 -118.745-193.806 138.567 1.00 97.86 C ANISOU 1177 CA PHE A 148 14577 10956 11647 -1853 -1486 -794 C ATOM 1178 C PHE A 148 -117.436-194.573 138.727 1.00 97.24 C ANISOU 1178 C PHE A 148 14560 10708 11678 -1747 -1175 -980 C ATOM 1179 O PHE A 148 -117.296-195.385 139.647 1.00 96.22 O ANISOU 1179 O PHE A 148 14295 10453 11810 -1649 -1113 -978 O ATOM 1180 CB PHE A 148 -119.057-192.995 139.823 1.00 93.57 C ANISOU 1180 CB PHE A 148 13721 10519 11312 -1677 -1550 -565 C ATOM 1181 CG PHE A 148 -117.960-192.049 140.230 1.00 90.33 C ANISOU 1181 CG PHE A 148 13236 10162 10923 -1487 -1366 -526 C ATOM 1182 CD1 PHE A 148 -117.779-190.844 139.567 1.00 87.52 C ANISOU 1182 CD1 PHE A 148 12953 9934 10369 -1500 -1396 -474 C ATOM 1183 CD2 PHE A 148 -117.118-192.359 141.285 1.00 90.54 C ANISOU 1183 CD2 PHE A 148 13122 10105 11174 -1307 -1186 -529 C ATOM 1184 CE1 PHE A 148 -116.775-189.974 139.941 1.00 82.45 C ANISOU 1184 CE1 PHE A 148 12236 9332 9757 -1338 -1229 -440 C ATOM 1185 CE2 PHE A 148 -116.108-191.489 141.666 1.00 97.83 C ANISOU 1185 CE2 PHE A 148 13967 11074 12129 -1145 -1039 -493 C ATOM 1186 CZ PHE A 148 -115.938-190.296 140.993 1.00 87.17 C ANISOU 1186 CZ PHE A 148 12684 9851 10587 -1161 -1051 -454 C ATOM 1187 N GLY A 149 -116.472-194.301 137.846 1.00 92.24 N ANISOU 1187 N GLY A 149 14123 10063 10862 -1767 -978 -1134 N ATOM 1188 CA GLY A 149 -115.224-195.042 137.852 1.00 81.40 C ANISOU 1188 CA GLY A 149 12799 8510 9617 -1676 -668 -1338 C ATOM 1189 C GLY A 149 -113.965-194.202 137.918 1.00 94.24 C ANISOU 1189 C GLY A 149 14372 10175 11262 -1523 -433 -1352 C ATOM 1190 O GLY A 149 -114.017-193.008 138.230 1.00 88.13 O ANISOU 1190 O GLY A 149 13481 9564 10441 -1449 -512 -1172 O ATOM 1191 N GLU A 150 -112.823-194.827 137.613 1.00105.69 N ANISOU 1191 N GLU A 150 15895 11460 12803 -1476 -136 -1573 N ATOM 1192 CA GLU A 150 -111.536-194.147 137.734 1.00 95.04 C ANISOU 1192 CA GLU A 150 14456 10119 11537 -1324 111 -1601 C ATOM 1193 C GLU A 150 -111.451-192.938 136.810 1.00 97.67 C ANISOU 1193 C GLU A 150 14949 10630 11531 -1432 134 -1577 C ATOM 1194 O GLU A 150 -110.980-191.870 137.217 1.00 93.09 O ANISOU 1194 O GLU A 150 14226 10158 10986 -1314 159 -1442 O ATOM 1195 CB GLU A 150 -110.399-195.128 137.438 1.00 97.48 C ANISOU 1195 CB GLU A 150 14813 10196 12030 -1276 435 -1870 C ATOM 1196 CG GLU A 150 -109.009-194.512 137.492 1.00112.97 C ANISOU 1196 CG GLU A 150 16661 12144 14119 -1130 714 -1924 C ATOM 1197 CD GLU A 150 -107.923-195.467 137.028 1.00129.47 C ANISOU 1197 CD GLU A 150 18799 13994 16400 -1100 1061 -2221 C ATOM 1198 OE1 GLU A 150 -108.256-196.598 136.614 1.00142.03 O ANISOU 1198 OE1 GLU A 150 20542 15425 17999 -1199 1091 -2396 O ATOM 1199 OE2 GLU A 150 -106.734-195.083 137.077 1.00127.54 O ANISOU 1199 OE2 GLU A 150 18430 13709 16321 -978 1310 -2285 O ATOM 1200 N ASN A 151 -111.899-193.085 135.561 1.00100.31 N ANISOU 1200 N ASN A 151 15597 10990 11527 -1671 116 -1702 N ATOM 1201 CA ASN A 151 -111.797-191.983 134.609 1.00 99.08 C ANISOU 1201 CA ASN A 151 15639 10988 11020 -1803 133 -1673 C ATOM 1202 C ASN A 151 -112.660-190.799 135.031 1.00102.63 C ANISOU 1202 C ASN A 151 15959 11632 11405 -1776 -188 -1369 C ATOM 1203 O ASN A 151 -112.276-189.641 134.827 1.00103.46 O ANISOU 1203 O ASN A 151 16070 11851 11388 -1758 -153 -1269 O ATOM 1204 CB ASN A 151 -112.184-192.460 133.210 1.00103.09 C ANISOU 1204 CB ASN A 151 16544 11476 11150 -2094 140 -1859 C ATOM 1205 CG ASN A 151 -111.307-193.593 132.720 1.00121.12 C ANISOU 1205 CG ASN A 151 18974 13553 13495 -2129 500 -2194 C ATOM 1206 OD1 ASN A 151 -111.764-194.727 132.573 1.00132.90 O ANISOU 1206 OD1 ASN A 151 20563 14912 15022 -2216 458 -2335 O ATOM 1207 ND2 ASN A 151 -110.038-193.291 132.461 1.00119.66 N ANISOU 1207 ND2 ASN A 151 18794 13327 13344 -2063 866 -2332 N ATOM 1208 N HIS A 152 -113.825-191.067 135.627 1.00 97.18 N ANISOU 1208 N HIS A 152 15140 10969 10817 -1774 -488 -1223 N ATOM 1209 CA HIS A 152 -114.696-189.979 136.061 1.00 87.89 C ANISOU 1209 CA HIS A 152 13810 9954 9629 -1738 -777 -950 C ATOM 1210 C HIS A 152 -114.077-189.197 137.213 1.00 93.15 C ANISOU 1210 C HIS A 152 14186 10661 10547 -1492 -692 -815 C ATOM 1211 O HIS A 152 -114.183-187.966 137.261 1.00 85.54 O ANISOU 1211 O HIS A 152 13164 9823 9516 -1456 -784 -651 O ATOM 1212 CB HIS A 152 -116.065-190.524 136.467 1.00 80.99 C ANISOU 1212 CB HIS A 152 12837 9084 8850 -1795 -1077 -849 C ATOM 1213 CG HIS A 152 -116.781-191.245 135.367 1.00 97.07 C ANISOU 1213 CG HIS A 152 15152 11087 10643 -2055 -1217 -963 C ATOM 1214 ND1 HIS A 152 -116.787-192.620 135.259 1.00 93.69 N ANISOU 1214 ND1 HIS A 152 14817 10502 10279 -2127 -1135 -1157 N ATOM 1215 CD2 HIS A 152 -117.516-190.782 134.329 1.00 93.28 C ANISOU 1215 CD2 HIS A 152 14887 10699 9856 -2270 -1453 -908 C ATOM 1216 CE1 HIS A 152 -117.494-192.972 134.200 1.00 99.91 C ANISOU 1216 CE1 HIS A 152 15871 11292 10797 -2383 -1305 -1231 C ATOM 1217 NE2 HIS A 152 -117.948-191.876 133.619 1.00103.20 N ANISOU 1217 NE2 HIS A 152 16370 11864 10979 -2477 -1510 -1076 N ATOM 1218 N ALA A 153 -113.430-189.893 138.153 1.00 91.29 N ANISOU 1218 N ALA A 153 13773 10308 10605 -1327 -533 -875 N ATOM 1219 CA ALA A 153 -112.826-189.211 139.293 1.00 87.91 C ANISOU 1219 CA ALA A 153 13083 9910 10406 -1110 -474 -750 C ATOM 1220 C ALA A 153 -111.637-188.359 138.865 1.00 84.45 C ANISOU 1220 C ALA A 153 12690 9501 9896 -1067 -253 -799 C ATOM 1221 O ALA A 153 -111.413-187.275 139.417 1.00 76.72 O ANISOU 1221 O ALA A 153 11565 8613 8972 -958 -282 -653 O ATOM 1222 CB ALA A 153 -112.405-190.230 140.351 1.00 87.64 C ANISOU 1222 CB ALA A 153 12879 9729 10691 -969 -389 -792 C ATOM 1223 N ILE A 154 -110.855-188.842 137.896 1.00 84.05 N ANISOU 1223 N ILE A 154 12838 9364 9733 -1158 -11 -1015 N ATOM 1224 CA ILE A 154 -109.767-188.038 137.344 1.00 85.50 C ANISOU 1224 CA ILE A 154 13085 9578 9824 -1156 225 -1074 C ATOM 1225 C ILE A 154 -110.327-186.793 136.672 1.00 89.09 C ANISOU 1225 C ILE A 154 13680 10198 9972 -1281 66 -924 C ATOM 1226 O ILE A 154 -109.795-185.688 136.828 1.00 91.28 O ANISOU 1226 O ILE A 154 13881 10549 10254 -1213 117 -823 O ATOM 1227 CB ILE A 154 -108.923-188.884 136.371 1.00 85.49 C ANISOU 1227 CB ILE A 154 13287 9443 9753 -1257 543 -1362 C ATOM 1228 CG1 ILE A 154 -108.268-190.055 137.112 1.00 90.50 C ANISOU 1228 CG1 ILE A 154 13740 9882 10764 -1101 696 -1495 C ATOM 1229 CG2 ILE A 154 -107.879-188.026 135.668 1.00 87.08 C ANISOU 1229 CG2 ILE A 154 13580 9686 9821 -1298 809 -1428 C ATOM 1230 CD1 ILE A 154 -107.803-191.178 136.202 1.00 92.82 C ANISOU 1230 CD1 ILE A 154 14236 10008 11024 -1210 960 -1796 C ATOM 1231 N MET A 155 -111.419-186.956 135.924 1.00 90.95 N ANISOU 1231 N MET A 155 14120 10484 9952 -1469 -152 -898 N ATOM 1232 CA MET A 155 -112.097-185.821 135.310 1.00 94.43 C ANISOU 1232 CA MET A 155 14688 11065 10127 -1590 -373 -722 C ATOM 1233 C MET A 155 -112.490-184.781 136.354 1.00 92.56 C ANISOU 1233 C MET A 155 14169 10914 10084 -1418 -561 -477 C ATOM 1234 O MET A 155 -112.290-183.579 136.149 1.00 88.92 O ANISOU 1234 O MET A 155 13725 10532 9529 -1416 -585 -353 O ATOM 1235 CB MET A 155 -113.324-186.326 134.550 1.00112.84 C ANISOU 1235 CB MET A 155 17227 13416 12231 -1801 -641 -715 C ATOM 1236 CG MET A 155 -113.752-185.495 133.359 1.00131.82 C ANISOU 1236 CG MET A 155 19917 15917 14252 -2020 -806 -623 C ATOM 1237 SD MET A 155 -114.918-186.440 132.355 1.00149.51 S ANISOU 1237 SD MET A 155 22449 18140 16219 -2303 -1068 -695 S ATOM 1238 CE MET A 155 -115.505-185.192 131.212 1.00157.16 C ANISOU 1238 CE MET A 155 23691 19234 16788 -2525 -1361 -490 C ATOM 1239 N GLY A 156 -113.011-185.227 137.500 1.00 83.39 N ANISOU 1239 N GLY A 156 12758 9730 9199 -1278 -675 -413 N ATOM 1240 CA GLY A 156 -113.411-184.290 138.538 1.00 83.18 C ANISOU 1240 CA GLY A 156 12474 9776 9353 -1124 -823 -209 C ATOM 1241 C GLY A 156 -112.239-183.551 139.153 1.00 89.31 C ANISOU 1241 C GLY A 156 13114 10552 10268 -964 -623 -196 C ATOM 1242 O GLY A 156 -112.345-182.365 139.474 1.00 92.28 O ANISOU 1242 O GLY A 156 13395 11002 10666 -900 -708 -43 O ATOM 1243 N VAL A 157 -111.111-184.241 139.342 1.00 85.71 N ANISOU 1243 N VAL A 157 12634 9998 9934 -898 -363 -356 N ATOM 1244 CA VAL A 157 -109.930-183.599 139.917 1.00 79.47 C ANISOU 1244 CA VAL A 157 11698 9195 9302 -756 -182 -350 C ATOM 1245 C VAL A 157 -109.378-182.546 138.963 1.00 78.89 C ANISOU 1245 C VAL A 157 11779 9181 9017 -848 -78 -341 C ATOM 1246 O VAL A 157 -109.131-181.399 139.356 1.00 76.23 O ANISOU 1246 O VAL A 157 11337 8900 8725 -774 -106 -213 O ATOM 1247 CB VAL A 157 -108.861-184.648 140.278 1.00 78.05 C ANISOU 1247 CB VAL A 157 11438 8875 9342 -668 52 -522 C ATOM 1248 CG1 VAL A 157 -107.531-183.971 140.581 1.00 76.36 C ANISOU 1248 CG1 VAL A 157 11098 8642 9272 -560 250 -538 C ATOM 1249 CG2 VAL A 157 -109.308-185.485 141.464 1.00 70.26 C ANISOU 1249 CG2 VAL A 157 10273 7828 8593 -556 -71 -477 C ATOM 1250 N ALA A 158 -109.175-182.922 137.695 1.00 77.50 N ANISOU 1250 N ALA A 158 11869 8983 8594 -1025 51 -479 N ATOM 1251 CA ALA A 158 -108.729-181.962 136.691 1.00 80.62 C ANISOU 1251 CA ALA A 158 12461 9435 8736 -1156 150 -461 C ATOM 1252 C ALA A 158 -109.662-180.761 136.609 1.00 84.52 C ANISOU 1252 C ALA A 158 12980 10038 9096 -1194 -144 -222 C ATOM 1253 O ALA A 158 -109.213-179.644 136.327 1.00 91.06 O ANISOU 1253 O ALA A 158 13849 10909 9842 -1216 -99 -132 O ATOM 1254 CB ALA A 158 -108.628-182.649 135.327 1.00 74.59 C ANISOU 1254 CB ALA A 158 12031 8639 7672 -1380 297 -644 C ATOM 1255 N PHE A 159 -110.954-180.969 136.872 1.00 83.49 N ANISOU 1255 N PHE A 159 12806 9940 8975 -1200 -445 -114 N ATOM 1256 CA PHE A 159 -111.907-179.868 136.845 1.00 80.38 C ANISOU 1256 CA PHE A 159 12394 9626 8522 -1216 -739 113 C ATOM 1257 C PHE A 159 -111.585-178.831 137.912 1.00 85.14 C ANISOU 1257 C PHE A 159 12739 10246 9364 -1024 -734 237 C ATOM 1258 O PHE A 159 -111.690-177.626 137.661 1.00 86.06 O ANISOU 1258 O PHE A 159 12886 10401 9412 -1042 -832 386 O ATOM 1259 CB PHE A 159 -113.324-180.410 137.024 1.00 76.95 C ANISOU 1259 CB PHE A 159 11906 9206 8125 -1245 -1035 183 C ATOM 1260 CG PHE A 159 -114.375-179.343 137.137 1.00 76.20 C ANISOU 1260 CG PHE A 159 11721 9170 8061 -1230 -1345 413 C ATOM 1261 CD1 PHE A 159 -114.891-178.737 136.004 1.00 77.02 C ANISOU 1261 CD1 PHE A 159 12051 9308 7905 -1407 -1549 526 C ATOM 1262 CD2 PHE A 159 -114.855-178.953 138.379 1.00 72.92 C ANISOU 1262 CD2 PHE A 159 11001 8763 7941 -1044 -1434 516 C ATOM 1263 CE1 PHE A 159 -115.858-177.754 136.109 1.00 74.72 C ANISOU 1263 CE1 PHE A 159 11652 9044 7693 -1379 -1851 746 C ATOM 1264 CE2 PHE A 159 -115.821-177.973 138.486 1.00 77.80 C ANISOU 1264 CE2 PHE A 159 11514 9414 8633 -1019 -1695 709 C ATOM 1265 CZ PHE A 159 -116.323-177.374 137.350 1.00 77.63 C ANISOU 1265 CZ PHE A 159 11689 9411 8396 -1176 -1911 828 C ATOM 1266 N THR A 160 -111.197-179.276 139.111 1.00 77.06 N ANISOU 1266 N THR A 160 11476 9185 8618 -848 -634 183 N ATOM 1267 CA THR A 160 -110.858-178.326 140.168 1.00 78.26 C ANISOU 1267 CA THR A 160 11406 9350 8979 -682 -628 283 C ATOM 1268 C THR A 160 -109.641-177.489 139.790 1.00 80.73 C ANISOU 1268 C THR A 160 11776 9656 9243 -693 -427 265 C ATOM 1269 O THR A 160 -109.610-176.278 140.040 1.00 72.46 O ANISOU 1269 O THR A 160 10665 8634 8233 -646 -491 394 O ATOM 1270 CB THR A 160 -110.610-179.058 141.489 1.00 74.54 C ANISOU 1270 CB THR A 160 10711 8836 8776 -524 -565 225 C ATOM 1271 OG1 THR A 160 -109.437-179.874 141.378 1.00 82.93 O ANISOU 1271 OG1 THR A 160 11795 9823 9891 -514 -320 58 O ATOM 1272 CG2 THR A 160 -111.807-179.937 141.854 1.00 69.29 C ANISOU 1272 CG2 THR A 160 9996 8172 8159 -533 -739 242 C ATOM 1273 N TRP A 161 -108.627-178.116 139.184 1.00 78.20 N ANISOU 1273 N TRP A 161 11567 9289 8857 -759 -170 98 N ATOM 1274 CA ATRP A 161 -107.435-177.383 138.765 0.60 79.41 C ANISOU 1274 CA ATRP A 161 11765 9431 8975 -789 55 67 C ATOM 1275 CA BTRP A 161 -107.443-177.361 138.790 0.40 79.01 C ANISOU 1275 CA BTRP A 161 11710 9381 8929 -786 51 71 C ATOM 1276 C TRP A 161 -107.776-176.329 137.720 1.00 85.08 C ANISOU 1276 C TRP A 161 12709 10203 9414 -948 -34 193 C ATOM 1277 O TRP A 161 -107.224-175.222 137.730 1.00 88.24 O ANISOU 1277 O TRP A 161 13087 10611 9830 -939 19 278 O ATOM 1278 CB ATRP A 161 -106.384-178.345 138.205 0.60 75.66 C ANISOU 1278 CB ATRP A 161 11369 8885 8493 -846 370 -157 C ATOM 1279 CB BTRP A 161 -106.342-178.313 138.319 0.40 76.45 C ANISOU 1279 CB BTRP A 161 11443 8983 8621 -828 370 -152 C ATOM 1280 CG ATRP A 161 -105.943-179.423 139.150 0.60 76.04 C ANISOU 1280 CG ATRP A 161 11204 8849 8838 -694 454 -276 C ATOM 1281 CG BTRP A 161 -105.669-179.015 139.463 0.40 75.82 C ANISOU 1281 CG BTRP A 161 11098 8827 8884 -646 463 -237 C ATOM 1282 CD1ATRP A 161 -106.273-179.549 140.470 0.60 73.20 C ANISOU 1282 CD1ATRP A 161 10611 8483 8720 -528 293 -194 C ATOM 1283 CD1BTRP A 161 -106.148-180.085 140.162 0.40 75.69 C ANISOU 1283 CD1BTRP A 161 10980 8766 9014 -561 367 -276 C ATOM 1284 CD2ATRP A 161 -105.086-180.532 138.843 0.60 77.93 C ANISOU 1284 CD2ATRP A 161 11455 8986 9170 -702 719 -493 C ATOM 1285 CD2BTRP A 161 -104.401-178.687 140.053 0.40 79.78 C ANISOU 1285 CD2BTRP A 161 11404 9279 9631 -536 645 -276 C ATOM 1286 NE1ATRP A 161 -105.674-180.667 141.002 0.60 77.44 N ANISOU 1286 NE1ATRP A 161 11023 8918 9481 -437 412 -324 N ATOM 1287 NE1BTRP A 161 -105.258-180.446 141.146 0.40 76.95 N ANISOU 1287 NE1BTRP A 161 10908 8847 9481 -407 464 -325 N ATOM 1288 CE2ATRP A 161 -104.941-181.287 140.024 0.60 79.14 C ANISOU 1288 CE2ATRP A 161 11369 9064 9635 -530 671 -510 C ATOM 1289 CE2BTRP A 161 -104.177-179.604 141.099 0.40 79.47 C ANISOU 1289 CE2BTRP A 161 11157 9163 9875 -387 626 -328 C ATOM 1290 CE3ATRP A 161 -104.428-180.958 137.685 0.60 79.40 C ANISOU 1290 CE3ATRP A 161 11836 9124 9207 -845 1002 -680 C ATOM 1291 CE3BTRP A 161 -103.435-177.710 139.795 0.40 77.83 C ANISOU 1291 CE3BTRP A 161 11134 9037 9400 -561 810 -263 C ATOM 1292 CZ2ATRP A 161 -104.166-182.443 140.080 0.60 78.15 C ANISOU 1292 CZ2ATRP A 161 11175 8806 9713 -479 869 -693 C ATOM 1293 CZ2BTRP A 161 -103.027-179.574 141.885 0.40 73.16 C ANISOU 1293 CZ2BTRP A 161 10129 8293 9375 -260 739 -363 C ATOM 1294 CZ3ATRP A 161 -103.658-182.106 137.743 0.60 78.17 C ANISOU 1294 CZ3ATRP A 161 11602 8838 9260 -791 1234 -888 C ATOM 1295 CZ3BTRP A 161 -102.295-177.682 140.578 0.40 72.11 C ANISOU 1295 CZ3BTRP A 161 10166 8246 8985 -434 941 -311 C ATOM 1296 CH2ATRP A 161 -103.535-182.836 138.932 0.60 79.88 C ANISOU 1296 CH2ATRP A 161 11559 8969 9822 -601 1154 -887 C ATOM 1297 CH2BTRP A 161 -102.100-178.608 141.609 0.40 70.63 C ANISOU 1297 CH2BTRP A 161 9773 7983 9079 -284 892 -357 C ATOM 1298 N VAL A 162 -108.679-176.663 136.797 1.00 87.96 N ANISOU 1298 N VAL A 162 13303 10597 9519 -1109 -187 215 N ATOM 1299 CA VAL A 162 -109.095-175.700 135.782 1.00 84.79 C ANISOU 1299 CA VAL A 162 13141 10239 8838 -1277 -328 364 C ATOM 1300 C VAL A 162 -109.838-174.538 136.430 1.00 86.62 C ANISOU 1300 C VAL A 162 13209 10490 9212 -1166 -603 592 C ATOM 1301 O VAL A 162 -109.563-173.367 136.143 1.00 87.01 O ANISOU 1301 O VAL A 162 13317 10539 9203 -1201 -618 720 O ATOM 1302 CB VAL A 162 -109.949-176.392 134.705 1.00 83.04 C ANISOU 1302 CB VAL A 162 13201 10038 8312 -1482 -476 341 C ATOM 1303 CG1 VAL A 162 -110.592-175.363 133.786 1.00 81.90 C ANISOU 1303 CG1 VAL A 162 13286 9932 7902 -1648 -724 550 C ATOM 1304 CG2 VAL A 162 -109.100-177.368 133.904 1.00 80.77 C ANISOU 1304 CG2 VAL A 162 13127 9717 7845 -1622 -154 97 C ATOM 1305 N MET A 163 -110.782-174.843 137.326 1.00 80.33 N ANISOU 1305 N MET A 163 12203 9699 8620 -1034 -806 640 N ATOM 1306 CA MET A 163 -111.505-173.784 138.025 1.00 84.22 C ANISOU 1306 CA MET A 163 12514 10196 9292 -914 -1031 825 C ATOM 1307 C MET A 163 -110.571-172.966 138.909 1.00 83.07 C ANISOU 1307 C MET A 163 12190 10024 9349 -768 -870 829 C ATOM 1308 O MET A 163 -110.733-171.747 139.033 1.00 86.94 O ANISOU 1308 O MET A 163 12638 10498 9896 -732 -977 975 O ATOM 1309 CB MET A 163 -112.643-174.373 138.859 1.00 77.90 C ANISOU 1309 CB MET A 163 11512 9403 8682 -810 -1220 843 C ATOM 1310 CG MET A 163 -113.766-174.989 138.047 1.00 84.27 C ANISOU 1310 CG MET A 163 12458 10230 9331 -954 -1453 878 C ATOM 1311 SD MET A 163 -114.472-173.832 136.860 1.00 93.43 S ANISOU 1311 SD MET A 163 13821 11394 10284 -1110 -1750 1103 S ATOM 1312 CE MET A 163 -115.044-172.534 137.953 1.00 89.27 C ANISOU 1312 CE MET A 163 12982 10834 10103 -899 -1901 1275 C ATOM 1313 N ALA A 164 -109.592-173.616 139.536 1.00 76.00 N ANISOU 1313 N ALA A 164 11183 9110 8582 -686 -629 673 N ATOM 1314 CA ALA A 164 -108.649-172.877 140.367 1.00 73.93 C ANISOU 1314 CA ALA A 164 10756 8822 8513 -566 -494 672 C ATOM 1315 C ALA A 164 -107.769-171.966 139.523 1.00 81.83 C ANISOU 1315 C ALA A 164 11907 9809 9376 -676 -357 706 C ATOM 1316 O ALA A 164 -107.467-170.836 139.925 1.00 78.10 O ANISOU 1316 O ALA A 164 11351 9313 9009 -620 -372 799 O ATOM 1317 CB ALA A 164 -107.793-173.842 141.175 1.00 68.48 C ANISOU 1317 CB ALA A 164 9914 8104 8002 -465 -303 511 C ATOM 1318 N LEU A 165 -107.348-172.440 138.349 1.00 81.55 N ANISOU 1318 N LEU A 165 12104 9780 9100 -846 -209 625 N ATOM 1319 CA LEU A 165 -106.491-171.625 137.495 1.00 80.85 C ANISOU 1319 CA LEU A 165 12181 9680 8857 -981 -43 652 C ATOM 1320 C LEU A 165 -107.248-170.432 136.934 1.00 87.98 C ANISOU 1320 C LEU A 165 13231 10588 9610 -1068 -285 875 C ATOM 1321 O LEU A 165 -106.696-169.330 136.836 1.00 89.56 O ANISOU 1321 O LEU A 165 13448 10759 9822 -1093 -232 968 O ATOM 1322 CB LEU A 165 -105.903-172.469 136.366 1.00 83.01 C ANISOU 1322 CB LEU A 165 12692 9959 8891 -1161 204 492 C ATOM 1323 CG LEU A 165 -104.718-173.359 136.750 1.00 87.00 C ANISOU 1323 CG LEU A 165 13049 10421 9586 -1089 529 268 C ATOM 1324 CD1 LEU A 165 -104.308-174.284 135.608 1.00 90.11 C ANISOU 1324 CD1 LEU A 165 13685 10805 9749 -1267 780 83 C ATOM 1325 CD2 LEU A 165 -103.542-172.507 137.205 1.00 80.14 C ANISOU 1325 CD2 LEU A 165 12014 9517 8916 -1027 713 274 C ATOM 1326 N ALA A 166 -108.515-170.619 136.574 1.00 88.22 N ANISOU 1326 N ALA A 166 13356 10643 9523 -1115 -568 974 N ATOM 1327 CA ALA A 166 -109.254-169.509 135.987 1.00 89.27 C ANISOU 1327 CA ALA A 166 13623 10759 9537 -1198 -832 1204 C ATOM 1328 C ALA A 166 -109.623-168.437 137.011 1.00 91.29 C ANISOU 1328 C ALA A 166 13628 10966 10090 -1013 -990 1338 C ATOM 1329 O ALA A 166 -110.152-167.390 136.621 1.00 90.46 O ANISOU 1329 O ALA A 166 13599 10818 9954 -1055 -1203 1535 O ATOM 1330 CB ALA A 166 -110.500-170.029 135.271 1.00 78.15 C ANISOU 1330 CB ALA A 166 12374 9379 7941 -1312 -1117 1276 C ATOM 1331 N CYS A 167 -109.353-168.662 138.298 1.00 89.85 N ANISOU 1331 N CYS A 167 13166 10779 10194 -818 -893 1236 N ATOM 1332 CA CYS A 167 -109.401-167.606 139.302 1.00 89.07 C ANISOU 1332 CA CYS A 167 12856 10627 10360 -660 -958 1316 C ATOM 1333 C CYS A 167 -108.027-167.038 139.630 1.00 87.96 C ANISOU 1333 C CYS A 167 12666 10455 10300 -642 -711 1256 C ATOM 1334 O CYS A 167 -107.872-165.815 139.723 1.00 86.90 O ANISOU 1334 O CYS A 167 12519 10259 10241 -629 -757 1372 O ATOM 1335 CB CYS A 167 -110.044-168.115 140.595 1.00 83.62 C ANISOU 1335 CB CYS A 167 11904 9949 9918 -476 -1026 1251 C ATOM 1336 SG CYS A 167 -109.614-167.135 142.074 1.00 87.15 S ANISOU 1336 SG CYS A 167 12099 10341 10675 -290 -969 1244 S ATOM 1337 N ALA A 168 -107.026-167.904 139.796 1.00 69.57 N ANISOU 1337 N ALA A 168 10299 8154 7981 -642 -458 1080 N ATOM 1338 CA ALA A 168 -105.716-167.482 140.278 1.00 75.22 C ANISOU 1338 CA ALA A 168 10903 8835 8841 -606 -237 1010 C ATOM 1339 C ALA A 168 -104.827-166.910 139.184 1.00 79.87 C ANISOU 1339 C ALA A 168 11687 9406 9256 -784 -58 1037 C ATOM 1340 O ALA A 168 -103.921-166.131 139.491 1.00 78.96 O ANISOU 1340 O ALA A 168 11488 9245 9268 -773 65 1042 O ATOM 1341 CB ALA A 168 -105.005-168.658 140.946 1.00 69.33 C ANISOU 1341 CB ALA A 168 10004 8108 8232 -524 -60 820 C ATOM 1342 N ALA A 169 -105.063-167.272 137.928 1.00 79.81 N ANISOU 1342 N ALA A 169 11944 9429 8950 -963 -37 1052 N ATOM 1343 CA ALA A 169 -104.188-166.876 136.828 1.00 78.76 C ANISOU 1343 CA ALA A 169 12032 9286 8607 -1165 182 1056 C ATOM 1344 C ALA A 169 -104.518-165.524 136.189 1.00 82.98 C ANISOU 1344 C ALA A 169 12749 9776 9003 -1282 24 1286 C ATOM 1345 O ALA A 169 -103.587-164.842 135.744 1.00 84.15 O ANISOU 1345 O ALA A 169 12983 9892 9100 -1400 219 1309 O ATOM 1346 CB ALA A 169 -104.185-167.958 135.743 1.00 68.42 C ANISOU 1346 CB ALA A 169 10965 8026 7006 -1335 319 939 C ATOM 1347 N PRO A 170 -105.782-165.105 136.073 1.00 88.26 N ANISOU 1347 N PRO A 170 13483 10432 9621 -1266 -319 1464 N ATOM 1348 CA PRO A 170 -106.069-163.793 135.449 1.00 90.80 C ANISOU 1348 CA PRO A 170 13978 10683 9839 -1374 -491 1702 C ATOM 1349 C PRO A 170 -105.321-162.643 136.110 1.00 86.08 C ANISOU 1349 C PRO A 170 13225 10001 9480 -1298 -405 1748 C ATOM 1350 O PRO A 170 -104.785-161.780 135.397 1.00 78.69 O ANISOU 1350 O PRO A 170 12471 9014 8415 -1458 -333 1863 O ATOM 1351 CB PRO A 170 -107.590-163.652 135.608 1.00 90.14 C ANISOU 1351 CB PRO A 170 13858 10580 9813 -1287 -891 1854 C ATOM 1352 CG PRO A 170 -108.074-165.047 135.544 1.00 88.26 C ANISOU 1352 CG PRO A 170 13621 10431 9483 -1282 -898 1713 C ATOM 1353 CD PRO A 170 -107.026-165.886 136.239 1.00 83.60 C ANISOU 1353 CD PRO A 170 12859 9882 9024 -1194 -565 1466 C ATOM 1354 N PRO A 171 -105.243-162.575 137.449 1.00 80.20 N ANISOU 1354 N PRO A 171 12169 9235 9069 -1077 -410 1666 N ATOM 1355 CA PRO A 171 -104.467-161.479 138.062 1.00 71.75 C ANISOU 1355 CA PRO A 171 10970 8079 8214 -1027 -327 1695 C ATOM 1356 C PRO A 171 -103.007-161.454 137.646 1.00 79.47 C ANISOU 1356 C PRO A 171 11996 9062 9136 -1164 12 1603 C ATOM 1357 O PRO A 171 -102.358-160.411 137.782 1.00 94.95 O ANISOU 1357 O PRO A 171 13927 10942 11207 -1196 74 1668 O ATOM 1358 CB PRO A 171 -104.615-161.740 139.567 1.00 78.45 C ANISOU 1358 CB PRO A 171 11504 8929 9373 -791 -368 1576 C ATOM 1359 CG PRO A 171 -105.885-162.474 139.678 1.00 79.34 C ANISOU 1359 CG PRO A 171 11600 9092 9455 -711 -576 1584 C ATOM 1360 CD PRO A 171 -105.905-163.380 138.495 1.00 71.15 C ANISOU 1360 CD PRO A 171 10791 8130 8111 -879 -510 1559 C ATOM 1361 N LEU A 172 -102.468-162.567 137.148 1.00 81.84 N ANISOU 1361 N LEU A 172 12358 9444 9294 -1248 244 1444 N ATOM 1362 CA LEU A 172 -101.106-162.572 136.633 1.00 78.83 C ANISOU 1362 CA LEU A 172 12021 9062 8871 -1393 598 1347 C ATOM 1363 C LEU A 172 -100.989-161.853 135.297 1.00 89.21 C ANISOU 1363 C LEU A 172 13672 10352 9873 -1654 656 1497 C ATOM 1364 O LEU A 172 -99.883-161.450 134.922 1.00 97.33 O ANISOU 1364 O LEU A 172 14732 11353 10896 -1788 937 1466 O ATOM 1365 CB LEU A 172 -100.603-164.010 136.474 1.00 82.04 C ANISOU 1365 CB LEU A 172 12388 9540 9242 -1400 845 1117 C ATOM 1366 CG LEU A 172 -99.735-164.669 137.548 1.00 80.88 C ANISOU 1366 CG LEU A 172 11910 9391 9431 -1233 1006 923 C ATOM 1367 CD1 LEU A 172 -100.200-164.297 138.933 1.00 81.07 C ANISOU 1367 CD1 LEU A 172 11688 9387 9728 -1014 752 971 C ATOM 1368 CD2 LEU A 172 -99.751-166.184 137.375 1.00 71.60 C ANISOU 1368 CD2 LEU A 172 10729 8269 8206 -1211 1129 736 C ATOM 1369 N VAL A 173 -102.093-161.679 134.570 1.00 93.78 N ANISOU 1369 N VAL A 173 14503 10935 10194 -1740 393 1668 N ATOM 1370 CA VAL A 173 -101.998-161.285 133.167 1.00 93.90 C ANISOU 1370 CA VAL A 173 14901 10945 9831 -2027 453 1797 C ATOM 1371 C VAL A 173 -102.920-160.124 132.810 1.00 92.44 C ANISOU 1371 C VAL A 173 14887 10673 9562 -2078 88 2099 C ATOM 1372 O VAL A 173 -103.115-159.829 131.626 1.00105.48 O ANISOU 1372 O VAL A 173 16897 12318 10861 -2322 37 2252 O ATOM 1373 CB VAL A 173 -102.282-162.488 132.248 1.00 96.86 C ANISOU 1373 CB VAL A 173 15519 11418 9866 -2173 534 1686 C ATOM 1374 CG1 VAL A 173 -101.118-163.470 132.276 1.00 94.50 C ANISOU 1374 CG1 VAL A 173 15117 11170 9620 -2190 975 1398 C ATOM 1375 CG2 VAL A 173 -103.580-163.173 132.657 1.00 94.05 C ANISOU 1375 CG2 VAL A 173 15086 11100 9548 -2017 200 1696 C ATOM 1376 N GLY A 174 -103.499-159.456 133.807 1.00 82.34 N ANISOU 1376 N GLY A 174 13368 9316 8601 -1859 -169 2188 N ATOM 1377 CA GLY A 174 -104.190-158.216 133.505 1.00 84.21 C ANISOU 1377 CA GLY A 174 13733 9430 8832 -1898 -477 2471 C ATOM 1378 C GLY A 174 -105.623-158.034 133.964 1.00 93.66 C ANISOU 1378 C GLY A 174 14819 10576 10191 -1719 -894 2599 C ATOM 1379 O GLY A 174 -106.167-156.935 133.824 1.00100.68 O ANISOU 1379 O GLY A 174 15765 11332 11156 -1720 -1154 2830 O ATOM 1380 N TRP A 175 -106.264-159.075 134.491 1.00 95.70 N ANISOU 1380 N TRP A 175 14916 10924 10523 -1571 -964 2459 N ATOM 1381 CA TRP A 175 -107.613-158.950 135.037 1.00 90.62 C ANISOU 1381 CA TRP A 175 14114 10233 10085 -1389 -1321 2553 C ATOM 1382 C TRP A 175 -107.492-159.021 136.554 1.00 90.05 C ANISOU 1382 C TRP A 175 13669 10154 10394 -1126 -1235 2383 C ATOM 1383 O TRP A 175 -107.130-160.067 137.104 1.00 82.90 O ANISOU 1383 O TRP A 175 12627 9353 9518 -1054 -1048 2167 O ATOM 1384 CB TRP A 175 -108.548-160.027 134.484 1.00 88.46 C ANISOU 1384 CB TRP A 175 13946 10056 9607 -1441 -1491 2543 C ATOM 1385 CG TRP A 175 -110.010-159.669 134.616 1.00 92.21 C ANISOU 1385 CG TRP A 175 14333 10456 10246 -1332 -1909 2721 C ATOM 1386 CD1 TRP A 175 -110.528-158.424 134.825 1.00 87.21 C ANISOU 1386 CD1 TRP A 175 13626 9665 9846 -1248 -2149 2922 C ATOM 1387 CD2 TRP A 175 -111.130-160.565 134.562 1.00 95.84 C ANISOU 1387 CD2 TRP A 175 14745 10980 10689 -1292 -2131 2706 C ATOM 1388 NE1 TRP A 175 -111.899-158.487 134.900 1.00 87.30 N ANISOU 1388 NE1 TRP A 175 13528 9636 10007 -1150 -2499 3032 N ATOM 1389 CE2 TRP A 175 -112.294-159.789 134.742 1.00 93.08 C ANISOU 1389 CE2 TRP A 175 14273 10509 10586 -1181 -2498 2906 C ATOM 1390 CE3 TRP A 175 -111.262-161.945 134.378 1.00 93.86 C ANISOU 1390 CE3 TRP A 175 14535 10865 10263 -1340 -2052 2540 C ATOM 1391 CZ2 TRP A 175 -113.571-160.347 134.743 1.00 93.65 C ANISOU 1391 CZ2 TRP A 175 14245 10600 10740 -1124 -2786 2948 C ATOM 1392 CZ3 TRP A 175 -112.533-162.498 134.381 1.00 93.06 C ANISOU 1392 CZ3 TRP A 175 14356 10782 10219 -1292 -2345 2584 C ATOM 1393 CH2 TRP A 175 -113.669-161.699 134.562 1.00 97.32 C ANISOU 1393 CH2 TRP A 175 14757 11209 11013 -1187 -2707 2787 C ATOM 1394 N SER A 176 -107.791-157.902 137.220 1.00 91.02 N ANISOU 1394 N SER A 176 13644 10140 10800 -995 -1375 2482 N ATOM 1395 CA SER A 176 -107.472-157.686 138.629 1.00 84.43 C ANISOU 1395 CA SER A 176 12511 9274 10294 -791 -1266 2331 C ATOM 1396 C SER A 176 -105.961-157.758 138.829 1.00 84.79 C ANISOU 1396 C SER A 176 12539 9358 10320 -857 -931 2186 C ATOM 1397 O SER A 176 -105.197-157.631 137.865 1.00 74.98 O ANISOU 1397 O SER A 176 11507 8125 8855 -1058 -785 2236 O ATOM 1398 CB SER A 176 -108.195-158.690 139.530 1.00 78.14 C ANISOU 1398 CB SER A 176 11496 8565 9628 -614 -1308 2179 C ATOM 1399 OG SER A 176 -108.064-158.340 140.899 1.00 89.26 O ANISOU 1399 OG SER A 176 12651 9926 11336 -431 -1249 2063 O ATOM 1400 N ARG A 177 -105.517-157.949 140.068 1.00 75.81 N ANISOU 1400 N ARG A 177 11152 8236 9416 -703 -809 2010 N ATOM 1401 CA ARG A 177 -104.090-157.942 140.354 1.00 70.95 C ANISOU 1401 CA ARG A 177 10475 7637 8847 -754 -531 1883 C ATOM 1402 C ARG A 177 -103.849-158.488 141.750 1.00 69.61 C ANISOU 1402 C ARG A 177 10037 7510 8900 -577 -466 1689 C ATOM 1403 O ARG A 177 -104.763-158.585 142.573 1.00 70.08 O ANISOU 1403 O ARG A 177 9970 7563 9094 -421 -622 1666 O ATOM 1404 CB ARG A 177 -103.491-156.533 140.241 1.00 71.96 C ANISOU 1404 CB ARG A 177 10650 7623 9068 -829 -510 1999 C ATOM 1405 CG ARG A 177 -104.108-155.551 141.227 1.00 75.55 C ANISOU 1405 CG ARG A 177 10956 7944 9804 -665 -696 2040 C ATOM 1406 CD ARG A 177 -103.411-154.204 141.210 1.00 81.46 C ANISOU 1406 CD ARG A 177 11741 8539 10673 -738 -658 2129 C ATOM 1407 NE ARG A 177 -103.974-153.276 142.189 1.00 80.46 N ANISOU 1407 NE ARG A 177 11476 8268 10829 -580 -813 2137 N ATOM 1408 CZ ARG A 177 -103.437-152.096 142.481 1.00 80.17 C ANISOU 1408 CZ ARG A 177 11425 8076 10960 -606 -794 2176 C ATOM 1409 NH1 ARG A 177 -102.324-151.713 141.870 1.00 67.18 N ANISOU 1409 NH1 ARG A 177 9883 6408 9233 -788 -631 2222 N ATOM 1410 NH2 ARG A 177 -104.004-151.302 143.381 1.00 78.66 N ANISOU 1410 NH2 ARG A 177 11117 7744 11027 -459 -921 2157 N ATOM 1411 N TYR A 178 -102.589-158.819 142.001 1.00 65.25 N ANISOU 1411 N TYR A 178 9403 6995 8395 -616 -234 1556 N ATOM 1412 CA TYR A 178 -102.119-159.311 143.285 1.00 62.96 C ANISOU 1412 CA TYR A 178 8879 6736 8308 -483 -175 1387 C ATOM 1413 C TYR A 178 -101.370-158.185 143.992 1.00 68.38 C ANISOU 1413 C TYR A 178 9464 7316 9203 -474 -150 1385 C ATOM 1414 O TYR A 178 -100.433-157.607 143.425 1.00 68.79 O ANISOU 1414 O TYR A 178 9570 7320 9247 -609 -12 1423 O ATOM 1415 CB TYR A 178 -101.215-160.525 143.076 1.00 69.19 C ANISOU 1415 CB TYR A 178 9623 7622 9045 -529 41 1243 C ATOM 1416 CG TYR A 178 -101.945-161.823 142.845 1.00 73.54 C ANISOU 1416 CG TYR A 178 10211 8271 9459 -491 6 1187 C ATOM 1417 CD1 TYR A 178 -102.936-162.260 143.719 1.00 75.68 C ANISOU 1417 CD1 TYR A 178 10385 8570 9801 -341 -167 1162 C ATOM 1418 CD2 TYR A 178 -101.643-162.614 141.753 1.00 75.40 C ANISOU 1418 CD2 TYR A 178 10588 8566 9495 -617 162 1150 C ATOM 1419 CE1 TYR A 178 -103.595-163.454 143.516 1.00 68.67 C ANISOU 1419 CE1 TYR A 178 9526 7763 8802 -318 -200 1113 C ATOM 1420 CE2 TYR A 178 -102.301-163.801 141.534 1.00 70.72 C ANISOU 1420 CE2 TYR A 178 10038 8049 8782 -593 126 1090 C ATOM 1421 CZ TYR A 178 -103.272-164.218 142.414 1.00 73.55 C ANISOU 1421 CZ TYR A 178 10287 8431 9227 -443 -63 1078 C ATOM 1422 OH TYR A 178 -103.910-165.408 142.172 1.00 78.01 O ANISOU 1422 OH TYR A 178 10895 9064 9680 -433 -96 1021 O ATOM 1423 N ILE A 179 -101.788-157.874 145.216 1.00 63.42 N ANISOU 1423 N ILE A 179 8698 6646 8752 -331 -273 1334 N ATOM 1424 CA ILE A 179 -101.147-156.847 146.038 1.00 64.51 C ANISOU 1424 CA ILE A 179 8744 6679 9090 -320 -271 1306 C ATOM 1425 C ILE A 179 -101.117-157.320 147.481 1.00 66.66 C ANISOU 1425 C ILE A 179 8845 6986 9496 -192 -310 1155 C ATOM 1426 O ILE A 179 -101.891-158.202 147.880 1.00 71.22 O ANISOU 1426 O ILE A 179 9391 7646 10026 -96 -372 1105 O ATOM 1427 CB ILE A 179 -101.876-155.484 145.958 1.00 67.71 C ANISOU 1427 CB ILE A 179 9228 6933 9565 -305 -415 1436 C ATOM 1428 CG1 ILE A 179 -103.324-155.597 146.461 1.00 68.60 C ANISOU 1428 CG1 ILE A 179 9313 7040 9714 -154 -589 1442 C ATOM 1429 CG2 ILE A 179 -101.801-154.894 144.549 1.00 65.12 C ANISOU 1429 CG2 ILE A 179 9094 6548 9099 -458 -399 1615 C ATOM 1430 CD1 ILE A 179 -104.052-154.253 146.601 1.00 70.00 C ANISOU 1430 CD1 ILE A 179 9516 7039 10043 -103 -729 1540 C ATOM 1431 N PRO A 180 -100.220-156.755 148.289 1.00 64.69 N ANISOU 1431 N PRO A 180 8497 6675 9407 -207 -283 1086 N ATOM 1432 CA PRO A 180 -100.309-156.973 149.736 1.00 59.08 C ANISOU 1432 CA PRO A 180 7671 5977 8800 -105 -360 961 C ATOM 1433 C PRO A 180 -101.673-156.538 150.252 1.00 62.26 C ANISOU 1433 C PRO A 180 8112 6331 9210 4 -487 972 C ATOM 1434 O PRO A 180 -102.270-155.577 149.762 1.00 63.01 O ANISOU 1434 O PRO A 180 8287 6322 9333 3 -539 1071 O ATOM 1435 CB PRO A 180 -99.178-156.102 150.295 1.00 57.26 C ANISOU 1435 CB PRO A 180 7371 5653 8731 -175 -338 918 C ATOM 1436 CG PRO A 180 -98.179-156.056 149.182 1.00 59.01 C ANISOU 1436 CG PRO A 180 7603 5873 8944 -309 -189 978 C ATOM 1437 CD PRO A 180 -98.993-156.024 147.912 1.00 63.95 C ANISOU 1437 CD PRO A 180 8393 6510 9397 -338 -171 1109 C ATOM 1438 N GLU A 181 -102.178-157.277 151.233 1.00 62.26 N ANISOU 1438 N GLU A 181 8053 6403 9202 96 -531 874 N ATOM 1439 CA GLU A 181 -103.495-157.027 151.790 1.00 63.91 C ANISOU 1439 CA GLU A 181 8272 6579 9433 200 -611 858 C ATOM 1440 C GLU A 181 -103.409-157.076 153.308 1.00 64.30 C ANISOU 1440 C GLU A 181 8267 6630 9534 241 -626 713 C ATOM 1441 O GLU A 181 -102.466-157.631 153.880 1.00 59.37 O ANISOU 1441 O GLU A 181 7596 6063 8897 199 -612 644 O ATOM 1442 CB GLU A 181 -104.526-158.047 151.271 1.00 65.30 C ANISOU 1442 CB GLU A 181 8459 6856 9494 253 -638 901 C ATOM 1443 CG GLU A 181 -104.160-159.491 151.578 1.00 75.01 C ANISOU 1443 CG GLU A 181 9642 8225 10633 253 -597 828 C ATOM 1444 CD GLU A 181 -105.027-160.489 150.827 1.00 95.98 C ANISOU 1444 CD GLU A 181 12327 10969 13170 274 -617 879 C ATOM 1445 OE1 GLU A 181 -106.078-160.086 150.278 1.00103.86 O ANISOU 1445 OE1 GLU A 181 13365 11930 14166 302 -689 964 O ATOM 1446 OE2 GLU A 181 -104.655-161.681 150.786 1.00 90.61 O ANISOU 1446 OE2 GLU A 181 11627 10385 12417 260 -573 836 O ATOM 1447 N GLY A 182 -104.410-156.481 153.954 1.00 64.54 N ANISOU 1447 N GLY A 182 8306 6588 9627 316 -656 668 N ATOM 1448 CA GLY A 182 -104.454-156.495 155.406 1.00 55.97 C ANISOU 1448 CA GLY A 182 7210 5504 8552 336 -652 520 C ATOM 1449 C GLY A 182 -103.231-155.823 155.991 1.00 75.35 C ANISOU 1449 C GLY A 182 9675 7890 11064 249 -662 456 C ATOM 1450 O GLY A 182 -102.913-154.665 155.684 1.00 64.26 O ANISOU 1450 O GLY A 182 8294 6351 9769 214 -662 484 O ATOM 1451 N MET A 183 -102.520-156.566 156.837 1.00 57.95 N ANISOU 1451 N MET A 183 7452 5771 8795 205 -687 381 N ATOM 1452 CA MET A 183 -101.319-156.027 157.457 1.00 63.46 C ANISOU 1452 CA MET A 183 8146 6412 9555 110 -732 322 C ATOM 1453 C MET A 183 -100.128-156.014 156.516 1.00 63.06 C ANISOU 1453 C MET A 183 8024 6357 9578 36 -717 409 C ATOM 1454 O MET A 183 -99.011-155.755 156.996 1.00 68.49 O ANISOU 1454 O MET A 183 8670 7011 10342 -51 -766 368 O ATOM 1455 CB MET A 183 -100.990-156.809 158.729 1.00 73.91 C ANISOU 1455 CB MET A 183 9480 7815 10788 78 -802 227 C ATOM 1456 CG MET A 183 -102.052-156.699 159.821 1.00 71.06 C ANISOU 1456 CG MET A 183 9215 7448 10337 114 -784 114 C ATOM 1457 SD MET A 183 -101.641-157.683 161.289 1.00 87.41 S ANISOU 1457 SD MET A 183 11345 9617 12249 42 -883 31 S ATOM 1458 CE MET A 183 -103.003-157.270 162.375 1.00 99.94 C ANISOU 1458 CE MET A 183 13070 11175 13729 65 -787 -114 C ATOM 1459 N GLN A 184 -100.371-156.297 155.234 1.00 52.54 N ANISOU 1459 N GLN A 184 6683 5057 8223 57 -652 520 N ATOM 1460 CA GLN A 184 -99.404-156.136 154.155 1.00 62.95 C ANISOU 1460 CA GLN A 184 7962 6358 9597 -26 -586 605 C ATOM 1461 C GLN A 184 -98.291-157.173 154.203 1.00 67.61 C ANISOU 1461 C GLN A 184 8439 7038 10212 -69 -567 579 C ATOM 1462 O GLN A 184 -97.225-156.975 153.605 1.00 73.24 O ANISOU 1462 O GLN A 184 9083 7723 11021 -157 -498 610 O ATOM 1463 CB GLN A 184 -98.800-154.724 154.158 1.00 66.18 C ANISOU 1463 CB GLN A 184 8389 6617 10139 -109 -588 613 C ATOM 1464 CG GLN A 184 -99.834-153.599 154.148 1.00 56.44 C ANISOU 1464 CG GLN A 184 7256 5254 8937 -60 -613 634 C ATOM 1465 CD GLN A 184 -100.685-153.591 152.892 1.00 67.86 C ANISOU 1465 CD GLN A 184 8764 6698 10322 -22 -585 775 C ATOM 1466 OE1 GLN A 184 -100.197-153.308 151.796 1.00 66.32 O ANISOU 1466 OE1 GLN A 184 8600 6476 10124 -105 -532 889 O ATOM 1467 NE2 GLN A 184 -101.968-153.907 153.046 1.00 68.74 N ANISOU 1467 NE2 GLN A 184 8897 6838 10383 90 -623 770 N ATOM 1468 N CYS A 185 -98.512-158.271 154.919 1.00 60.63 N ANISOU 1468 N CYS A 185 7524 6247 9263 -13 -623 525 N ATOM 1469 CA CYS A 185 -97.532-159.339 155.021 1.00 68.57 C ANISOU 1469 CA CYS A 185 8409 7317 10326 -34 -628 506 C ATOM 1470 C CYS A 185 -97.841-160.513 154.109 1.00 73.10 C ANISOU 1470 C CYS A 185 8972 7981 10822 11 -537 544 C ATOM 1471 O CYS A 185 -96.971-161.365 153.896 1.00 76.95 O ANISOU 1471 O CYS A 185 9347 8497 11392 -4 -498 531 O ATOM 1472 CB CYS A 185 -97.432-159.826 156.469 1.00 59.54 C ANISOU 1472 CB CYS A 185 7250 6199 9172 -20 -777 434 C ATOM 1473 SG CYS A 185 -96.569-158.680 157.552 1.00 82.65 S ANISOU 1473 SG CYS A 185 10169 9023 12212 -118 -901 371 S ATOM 1474 N SER A 186 -99.050-160.584 153.571 1.00 80.84 N ANISOU 1474 N SER A 186 10058 8993 11664 64 -509 585 N ATOM 1475 CA SER A 186 -99.387-161.588 152.578 1.00 76.73 C ANISOU 1475 CA SER A 186 9555 8548 11050 84 -426 620 C ATOM 1476 C SER A 186 -100.114-160.915 151.427 1.00 73.88 C ANISOU 1476 C SER A 186 9311 8164 10597 61 -373 708 C ATOM 1477 O SER A 186 -100.556-159.768 151.522 1.00 76.71 O ANISOU 1477 O SER A 186 9726 8445 10975 60 -419 745 O ATOM 1478 CB SER A 186 -100.227-162.723 153.177 1.00 62.19 C ANISOU 1478 CB SER A 186 7723 6785 9119 164 -492 589 C ATOM 1479 OG SER A 186 -101.362-162.210 153.839 1.00 80.53 O ANISOU 1479 OG SER A 186 10116 9098 11382 214 -566 584 O ATOM 1480 N CYS A 187 -100.228-161.644 150.324 1.00 66.11 N ANISOU 1480 N CYS A 187 8371 7235 9513 37 -286 742 N ATOM 1481 CA CYS A 187 -100.659-161.082 149.052 1.00 64.47 C ANISOU 1481 CA CYS A 187 8294 7006 9197 -26 -240 842 C ATOM 1482 C CYS A 187 -101.890-161.829 148.553 1.00 75.67 C ANISOU 1482 C CYS A 187 9799 8493 10461 17 -292 878 C ATOM 1483 O CYS A 187 -102.019-163.041 148.766 1.00 75.50 O ANISOU 1483 O CYS A 187 9737 8545 10404 57 -283 815 O ATOM 1484 CB CYS A 187 -99.518-161.155 148.024 1.00 63.16 C ANISOU 1484 CB CYS A 187 8134 6836 9028 -145 -63 848 C ATOM 1485 SG CYS A 187 -98.225-159.905 148.196 1.00 78.74 S ANISOU 1485 SG CYS A 187 10033 8703 11180 -239 4 855 S ATOM 1486 N GLY A 188 -102.786-161.106 147.887 1.00 66.99 N ANISOU 1486 N GLY A 188 8813 7355 9287 2 -364 987 N ATOM 1487 CA GLY A 188 -103.994-161.712 147.376 1.00 61.64 C ANISOU 1487 CA GLY A 188 8207 6731 8483 30 -446 1035 C ATOM 1488 C GLY A 188 -104.673-160.842 146.338 1.00 70.73 C ANISOU 1488 C GLY A 188 9496 7822 9555 -28 -531 1186 C ATOM 1489 O GLY A 188 -104.143-159.812 145.911 1.00 74.28 O ANISOU 1489 O GLY A 188 10007 8189 10029 -101 -503 1260 O ATOM 1490 N ILE A 189 -105.868-161.285 145.931 1.00 77.30 N ANISOU 1490 N ILE A 189 10378 8691 10304 -2 -651 1243 N ATOM 1491 CA ILE A 189 -106.644-160.563 144.928 1.00 74.81 C ANISOU 1491 CA ILE A 189 10193 8314 9918 -56 -788 1409 C ATOM 1492 C ILE A 189 -106.995-159.182 145.455 1.00 68.84 C ANISOU 1492 C ILE A 189 9383 7420 9355 14 -885 1475 C ATOM 1493 O ILE A 189 -107.329-159.011 146.635 1.00 77.22 O ANISOU 1493 O ILE A 189 10302 8453 10586 136 -900 1388 O ATOM 1494 CB ILE A 189 -107.922-161.341 144.562 1.00 77.27 C ANISOU 1494 CB ILE A 189 10525 8685 10149 -30 -933 1450 C ATOM 1495 CG1 ILE A 189 -107.610-162.806 144.240 1.00 94.09 C ANISOU 1495 CG1 ILE A 189 12694 10939 12117 -84 -828 1349 C ATOM 1496 CG2 ILE A 189 -108.661-160.657 143.408 1.00 74.41 C ANISOU 1496 CG2 ILE A 189 10313 8257 9702 -109 -1112 1644 C ATOM 1497 CD1 ILE A 189 -107.262-163.067 142.810 1.00 99.60 C ANISOU 1497 CD1 ILE A 189 13605 11668 12571 -252 -781 1408 C ATOM 1498 N ASP A 190 -106.941-158.187 144.576 1.00 64.79 N ANISOU 1498 N ASP A 190 8998 6808 8812 -72 -947 1629 N ATOM 1499 CA ASP A 190 -107.233-156.807 144.960 1.00 72.34 C ANISOU 1499 CA ASP A 190 9916 7598 9971 -12 -1042 1702 C ATOM 1500 C ASP A 190 -108.744-156.599 144.947 1.00 71.18 C ANISOU 1500 C ASP A 190 9719 7390 9936 90 -1255 1792 C ATOM 1501 O ASP A 190 -109.348-156.297 143.917 1.00 71.69 O ANISOU 1501 O ASP A 190 9899 7403 9936 30 -1420 1971 O ATOM 1502 CB ASP A 190 -106.518-155.834 144.032 1.00 73.87 C ANISOU 1502 CB ASP A 190 10270 7694 10102 -155 -1024 1844 C ATOM 1503 CG ASP A 190 -106.789-154.377 144.377 1.00 73.35 C ANISOU 1503 CG ASP A 190 10176 7429 10265 -99 -1128 1927 C ATOM 1504 OD1 ASP A 190 -107.288-154.092 145.489 1.00 79.18 O ANISOU 1504 OD1 ASP A 190 10756 8107 11220 51 -1158 1827 O ATOM 1505 OD2 ASP A 190 -106.485-153.508 143.531 1.00 66.88 O ANISOU 1505 OD2 ASP A 190 9504 6501 9405 -214 -1168 2089 O ATOM 1506 N TYR A 191 -109.365-156.769 146.115 1.00 70.95 N ANISOU 1506 N TYR A 191 9513 7362 10084 238 -1253 1667 N ATOM 1507 CA TYR A 191 -110.738-156.342 146.348 1.00 73.27 C ANISOU 1507 CA TYR A 191 9699 7558 10582 358 -1415 1721 C ATOM 1508 C TYR A 191 -110.810-154.973 147.007 1.00 77.32 C ANISOU 1508 C TYR A 191 10141 7878 11360 443 -1422 1712 C ATOM 1509 O TYR A 191 -111.894-154.557 147.420 1.00 85.09 O ANISOU 1509 O TYR A 191 10996 8759 12577 566 -1512 1714 O ATOM 1510 CB TYR A 191 -111.479-157.360 147.223 1.00 71.55 C ANISOU 1510 CB TYR A 191 9329 7448 10408 457 -1377 1580 C ATOM 1511 CG TYR A 191 -111.383-158.762 146.708 1.00 77.45 C ANISOU 1511 CG TYR A 191 10138 8372 10919 381 -1357 1562 C ATOM 1512 CD1 TYR A 191 -110.583-159.704 147.346 1.00 67.44 C ANISOU 1512 CD1 TYR A 191 8853 7228 9545 366 -1188 1408 C ATOM 1513 CD2 TYR A 191 -112.073-159.142 145.567 1.00 94.08 C ANISOU 1513 CD2 TYR A 191 12328 10505 12914 315 -1521 1703 C ATOM 1514 CE1 TYR A 191 -110.487-160.987 146.865 1.00 87.97 C ANISOU 1514 CE1 TYR A 191 11507 9962 11955 301 -1162 1383 C ATOM 1515 CE2 TYR A 191 -111.987-160.419 145.076 1.00 98.41 C ANISOU 1515 CE2 TYR A 191 12948 11199 13243 235 -1495 1670 C ATOM 1516 CZ TYR A 191 -111.193-161.339 145.725 1.00100.23 C ANISOU 1516 CZ TYR A 191 13151 11539 13392 234 -1304 1505 C ATOM 1517 OH TYR A 191 -111.114-162.616 145.225 1.00 97.54 O ANISOU 1517 OH TYR A 191 12881 11320 12861 161 -1274 1464 O ATOM 1518 N TYR A 192 -109.680-154.272 147.121 1.00 83.85 N ANISOU 1518 N TYR A 192 11039 8643 12177 378 -1321 1692 N ATOM 1519 CA TYR A 192 -109.582-153.093 147.966 1.00 85.09 C ANISOU 1519 CA TYR A 192 11131 8625 12576 450 -1289 1627 C ATOM 1520 C TYR A 192 -109.494-151.784 147.195 1.00 85.22 C ANISOU 1520 C TYR A 192 11246 8438 12698 403 -1401 1809 C ATOM 1521 O TYR A 192 -109.765-150.732 147.779 1.00 84.96 O ANISOU 1521 O TYR A 192 11147 8214 12919 487 -1419 1779 O ATOM 1522 CB TYR A 192 -108.361-153.216 148.887 1.00 84.10 C ANISOU 1522 CB TYR A 192 10993 8560 12400 411 -1105 1449 C ATOM 1523 CG TYR A 192 -108.219-154.612 149.452 1.00 90.85 C ANISOU 1523 CG TYR A 192 11792 9619 13107 421 -1011 1311 C ATOM 1524 CD1 TYR A 192 -108.921-154.996 150.584 1.00 86.25 C ANISOU 1524 CD1 TYR A 192 11093 9069 12608 530 -976 1165 C ATOM 1525 CD2 TYR A 192 -107.406-155.555 148.836 1.00 90.02 C ANISOU 1525 CD2 TYR A 192 11755 9663 12786 317 -949 1326 C ATOM 1526 CE1 TYR A 192 -108.809-156.277 151.098 1.00 80.68 C ANISOU 1526 CE1 TYR A 192 10351 8538 11767 529 -906 1060 C ATOM 1527 CE2 TYR A 192 -107.290-156.830 149.339 1.00 93.25 C ANISOU 1527 CE2 TYR A 192 12109 10231 13088 333 -880 1211 C ATOM 1528 CZ TYR A 192 -107.993-157.188 150.469 1.00 87.76 C ANISOU 1528 CZ TYR A 192 11309 9564 12471 436 -871 1089 C ATOM 1529 OH TYR A 192 -107.877-158.464 150.972 1.00 85.94 O ANISOU 1529 OH TYR A 192 11040 9480 12133 441 -815 993 O ATOM 1530 N THR A 193 -109.121-151.822 145.915 1.00 81.60 N ANISOU 1530 N THR A 193 10954 8003 12045 260 -1469 1993 N ATOM 1531 CA THR A 193 -109.046-150.669 145.034 1.00 78.20 C ANISOU 1531 CA THR A 193 10657 7386 11668 182 -1595 2207 C ATOM 1532 C THR A 193 -109.777-150.975 143.735 1.00 82.24 C ANISOU 1532 C THR A 193 11296 7922 12029 111 -1802 2433 C ATOM 1533 O THR A 193 -109.839-152.132 143.309 1.00 84.39 O ANISOU 1533 O THR A 193 11613 8386 12064 53 -1782 2412 O ATOM 1534 CB THR A 193 -107.592-150.278 144.713 1.00 76.54 C ANISOU 1534 CB THR A 193 10582 7174 11325 16 -1445 2220 C ATOM 1535 OG1 THR A 193 -107.129-151.007 143.567 1.00 71.14 O ANISOU 1535 OG1 THR A 193 10068 6636 10325 -153 -1412 2321 O ATOM 1536 CG2 THR A 193 -106.676-150.569 145.889 1.00 67.92 C ANISOU 1536 CG2 THR A 193 9375 6163 10269 43 -1234 1976 C ATOM 1537 N PRO A 194 -110.331-149.952 143.078 1.00 79.57 N ANISOU 1537 N PRO A 194 11028 7379 11825 103 -2018 2655 N ATOM 1538 CA PRO A 194 -111.006-150.178 141.794 1.00 88.40 C ANISOU 1538 CA PRO A 194 12299 8508 12782 7 -2261 2898 C ATOM 1539 C PRO A 194 -110.090-149.937 140.606 1.00 99.73 C ANISOU 1539 C PRO A 194 14029 9954 13910 -236 -2242 3072 C ATOM 1540 O PRO A 194 -110.448-149.187 139.693 1.00116.40 O ANISOU 1540 O PRO A 194 16299 11913 16015 -321 -2470 3334 O ATOM 1541 CB PRO A 194 -112.142-149.154 141.832 1.00 99.12 C ANISOU 1541 CB PRO A 194 13549 9608 14502 144 -2527 3050 C ATOM 1542 CG PRO A 194 -111.512-147.982 142.543 1.00 77.24 C ANISOU 1542 CG PRO A 194 10735 6644 11968 193 -2405 2982 C ATOM 1543 CD PRO A 194 -110.555-148.583 143.576 1.00 82.94 C ANISOU 1543 CD PRO A 194 11378 7537 12599 204 -2084 2688 C ATOM 1544 N HIS A 195 -108.910-150.562 140.612 1.00 99.68 N ANISOU 1544 N HIS A 195 14096 10118 13662 -355 -1969 2932 N ATOM 1545 CA HIS A 195 -107.883-150.350 139.594 1.00 96.31 C ANISOU 1545 CA HIS A 195 13930 9710 12955 -598 -1865 3051 C ATOM 1546 C HIS A 195 -108.441-150.508 138.182 1.00 99.40 C ANISOU 1546 C HIS A 195 14583 10113 13071 -762 -2082 3301 C ATOM 1547 O HIS A 195 -108.641-151.632 137.708 1.00111.70 O ANISOU 1547 O HIS A 195 16214 11854 14373 -826 -2069 3257 O ATOM 1548 CB HIS A 195 -106.720-151.326 139.815 1.00 97.07 C ANISOU 1548 CB HIS A 195 14012 10014 12855 -675 -1539 2831 C ATOM 1549 CG HIS A 195 -105.389-150.811 139.354 1.00100.46 C ANISOU 1549 CG HIS A 195 14585 10417 13168 -869 -1329 2861 C ATOM 1550 ND1 HIS A 195 -104.759-149.737 139.948 1.00107.78 N ANISOU 1550 ND1 HIS A 195 15438 11187 14327 -851 -1261 2846 N ATOM 1551 CD2 HIS A 195 -104.561-151.232 138.367 1.00 99.14 C ANISOU 1551 CD2 HIS A 195 14626 10356 12688 -1094 -1152 2893 C ATOM 1552 CE1 HIS A 195 -103.605-149.515 139.343 1.00105.18 C ANISOU 1552 CE1 HIS A 195 15250 10870 13845 -1058 -1062 2880 C ATOM 1553 NE2 HIS A 195 -103.461-150.407 138.379 1.00101.19 N ANISOU 1553 NE2 HIS A 195 14915 10524 13009 -1207 -978 2905 N ATOM 1554 N GLU A 196 -108.689-149.384 137.503 1.00 96.43 N ANISOU 1554 N GLU A 196 14365 9532 12741 -843 -2294 3568 N ATOM 1555 CA GLU A 196 -109.295-149.435 136.175 1.00103.20 C ANISOU 1555 CA GLU A 196 15494 10378 13338 -1012 -2559 3839 C ATOM 1556 C GLU A 196 -108.362-150.055 135.144 1.00101.69 C ANISOU 1556 C GLU A 196 15608 10357 12671 -1296 -2353 3849 C ATOM 1557 O GLU A 196 -108.830-150.638 134.159 1.00106.76 O ANISOU 1557 O GLU A 196 16472 11088 13006 -1442 -2504 3970 O ATOM 1558 CB GLU A 196 -109.712-148.033 135.720 1.00115.12 C ANISOU 1558 CB GLU A 196 17056 11671 15015 -1017 -2784 4051 C ATOM 1559 CG GLU A 196 -110.926-147.465 136.437 1.00128.43 C ANISOU 1559 CG GLU A 196 18437 13218 17144 -746 -3004 4021 C ATOM 1560 CD GLU A 196 -110.581-146.884 137.792 1.00143.27 C ANISOU 1560 CD GLU A 196 20082 14947 19406 -558 -2852 3867 C ATOM 1561 OE1 GLU A 196 -109.376-146.725 138.081 1.00142.73 O ANISOU 1561 OE1 GLU A 196 20098 14853 19281 -654 -2620 3822 O ATOM 1562 OE2 GLU A 196 -111.513-146.589 138.570 1.00152.53 O ANISOU 1562 OE2 GLU A 196 20986 16026 20944 -327 -2955 3780 O ATOM 1563 N GLU A 197 -107.047-149.935 135.343 1.00100.30 N ANISOU 1563 N GLU A 197 15450 10223 12436 -1388 -2007 3716 N ATOM 1564 CA GLU A 197 -106.101-150.487 134.382 1.00107.75 C ANISOU 1564 CA GLU A 197 16663 11313 12963 -1660 -1757 3702 C ATOM 1565 C GLU A 197 -106.210-152.001 134.273 1.00110.20 C ANISOU 1565 C GLU A 197 16960 11862 13048 -1661 -1640 3507 C ATOM 1566 O GLU A 197 -105.811-152.568 133.250 1.00124.15 O ANISOU 1566 O GLU A 197 19002 13744 14426 -1896 -1513 3526 O ATOM 1567 CB GLU A 197 -104.672-150.090 134.762 1.00111.93 C ANISOU 1567 CB GLU A 197 17136 11833 13560 -1729 -1396 3570 C ATOM 1568 CG GLU A 197 -104.398-148.588 134.750 1.00125.01 C ANISOU 1568 CG GLU A 197 18848 13246 15402 -1779 -1474 3762 C ATOM 1569 CD GLU A 197 -104.742-147.904 136.064 1.00130.76 C ANISOU 1569 CD GLU A 197 19261 13822 16600 -1506 -1576 3677 C ATOM 1570 OE1 GLU A 197 -105.733-148.300 136.713 1.00121.82 O ANISOU 1570 OE1 GLU A 197 17933 12707 15645 -1282 -1750 3601 O ATOM 1571 OE2 GLU A 197 -104.010-146.970 136.455 1.00142.89 O ANISOU 1571 OE2 GLU A 197 20750 15217 18326 -1529 -1467 3675 O ATOM 1572 N THR A 198 -106.745-152.667 135.297 1.00 94.32 N ANISOU 1572 N THR A 198 14651 9919 11266 -1416 -1668 3318 N ATOM 1573 CA THR A 198 -106.913-154.115 135.286 1.00 99.97 C ANISOU 1573 CA THR A 198 15334 10840 11812 -1399 -1575 3134 C ATOM 1574 C THR A 198 -108.374-154.543 135.388 1.00105.92 C ANISOU 1574 C THR A 198 16001 11600 12644 -1265 -1908 3193 C ATOM 1575 O THR A 198 -108.644-155.739 135.553 1.00104.38 O ANISOU 1575 O THR A 198 15735 11558 12368 -1219 -1856 3033 O ATOM 1576 CB THR A 198 -106.106-154.759 136.421 1.00 92.71 C ANISOU 1576 CB THR A 198 14139 10020 11065 -1256 -1268 2833 C ATOM 1577 OG1 THR A 198 -106.371-154.077 137.653 1.00 90.55 O ANISOU 1577 OG1 THR A 198 13590 9633 11182 -1031 -1346 2788 O ATOM 1578 CG2 THR A 198 -104.614-154.702 136.120 1.00 81.52 C ANISOU 1578 CG2 THR A 198 12810 8641 9525 -1425 -912 2747 C ATOM 1579 N ASN A 199 -109.315-153.604 135.294 1.00108.13 N ANISOU 1579 N ASN A 199 16270 11705 13108 -1201 -2247 3420 N ATOM 1580 CA ASN A 199 -110.752-153.884 135.358 1.00102.14 C ANISOU 1580 CA ASN A 199 15398 10925 12486 -1075 -2587 3500 C ATOM 1581 C ASN A 199 -111.106-154.700 136.602 1.00 94.85 C ANISOU 1581 C ASN A 199 14135 10097 11806 -837 -2481 3241 C ATOM 1582 O ASN A 199 -111.668-155.794 136.528 1.00 95.17 O ANISOU 1582 O ASN A 199 14144 10272 11744 -826 -2528 3159 O ATOM 1583 CB ASN A 199 -111.226-154.590 134.086 1.00 96.91 C ANISOU 1583 CB ASN A 199 15028 10360 11435 -1287 -2770 3631 C ATOM 1584 CG ASN A 199 -111.143-153.703 132.864 1.00104.04 C ANISOU 1584 CG ASN A 199 16256 11162 12112 -1514 -2936 3901 C ATOM 1585 OD1 ASN A 199 -111.926-152.767 132.708 1.00121.17 O ANISOU 1585 OD1 ASN A 199 18327 13202 14508 -1435 -3198 4028 O ATOM 1586 ND2 ASN A 199 -110.200-154.001 131.980 1.00 97.30 N ANISOU 1586 ND2 ASN A 199 15730 10403 10835 -1782 -2718 3900 N ATOM 1587 N ASN A 200 -110.764-154.136 137.764 1.00 89.70 N ANISOU 1587 N ASN A 200 13244 9366 11470 -662 -2336 3114 N ATOM 1588 CA ASN A 200 -111.000-154.832 139.027 1.00 85.50 C ANISOU 1588 CA ASN A 200 12418 8919 11150 -457 -2211 2868 C ATOM 1589 C ASN A 200 -112.486-155.063 139.274 1.00 83.72 C ANISOU 1589 C ASN A 200 12017 8660 11132 -311 -2479 2914 C ATOM 1590 O ASN A 200 -112.877-156.112 139.801 1.00 84.17 O ANISOU 1590 O ASN A 200 11930 8850 11199 -231 -2420 2754 O ATOM 1591 CB ASN A 200 -110.390-154.043 140.185 1.00 80.19 C ANISOU 1591 CB ASN A 200 11564 8147 10759 -324 -2038 2742 C ATOM 1592 CG ASN A 200 -108.891-154.235 140.301 1.00 90.46 C ANISOU 1592 CG ASN A 200 12931 9534 11905 -429 -1722 2605 C ATOM 1593 OD1 ASN A 200 -108.225-154.627 139.343 1.00 89.57 O ANISOU 1593 OD1 ASN A 200 13034 9508 11491 -621 -1622 2646 O ATOM 1594 ND2 ASN A 200 -108.352-153.958 141.483 1.00 89.97 N ANISOU 1594 ND2 ASN A 200 12684 9443 12058 -311 -1560 2434 N ATOM 1595 N GLU A 201 -113.324-154.088 138.912 1.00 89.67 N ANISOU 1595 N GLU A 201 12765 9225 12080 -277 -2775 3137 N ATOM 1596 CA GLU A 201 -114.755-154.175 139.194 1.00 88.07 C ANISOU 1596 CA GLU A 201 12345 8960 12159 -123 -3031 3184 C ATOM 1597 C GLU A 201 -115.356-155.446 138.610 1.00 86.75 C ANISOU 1597 C GLU A 201 12233 8964 11763 -208 -3145 3183 C ATOM 1598 O GLU A 201 -116.035-156.206 139.311 1.00 86.94 O ANISOU 1598 O GLU A 201 12032 9066 11936 -81 -3124 3039 O ATOM 1599 CB GLU A 201 -115.461-152.935 138.640 1.00 99.92 C ANISOU 1599 CB GLU A 201 13860 10228 13877 -108 -3346 3443 C ATOM 1600 CG GLU A 201 -116.955-152.862 138.910 1.00117.97 C ANISOU 1600 CG GLU A 201 15853 12467 16503 52 -3543 3422 C ATOM 1601 CD GLU A 201 -117.585-151.612 138.319 1.00139.52 C ANISOU 1601 CD GLU A 201 18562 15024 19426 51 -3762 3578 C ATOM 1602 OE1 GLU A 201 -116.835-150.754 137.807 1.00144.06 O ANISOU 1602 OE1 GLU A 201 19341 15511 19884 -56 -3748 3693 O ATOM 1603 OE2 GLU A 201 -118.827-151.488 138.361 1.00149.98 O ANISOU 1603 OE2 GLU A 201 19661 16293 21032 150 -3947 3590 O ATOM 1604 N SER A 202 -115.098-155.701 137.327 1.00 87.00 N ANISOU 1604 N SER A 202 12584 9055 11418 -439 -3255 3334 N ATOM 1605 CA SER A 202 -115.693-156.853 136.666 1.00 88.52 C ANISOU 1605 CA SER A 202 12868 9392 11374 -547 -3394 3342 C ATOM 1606 C SER A 202 -115.153-158.166 137.221 1.00 94.80 C ANISOU 1606 C SER A 202 13607 10393 12019 -534 -3076 3056 C ATOM 1607 O SER A 202 -115.880-159.164 137.255 1.00 94.92 O ANISOU 1607 O SER A 202 13540 10506 12017 -520 -3159 2989 O ATOM 1608 CB SER A 202 -115.451-156.768 135.160 1.00 86.73 C ANISOU 1608 CB SER A 202 13042 9176 10737 -826 -3560 3556 C ATOM 1609 OG SER A 202 -114.066-156.804 134.877 1.00 94.95 O ANISOU 1609 OG SER A 202 14310 10292 11473 -975 -3232 3468 O ATOM 1610 N PHE A 203 -113.893-158.189 137.664 1.00 84.78 N ANISOU 1610 N PHE A 203 12369 9180 10664 -542 -2727 2892 N ATOM 1611 CA PHE A 203 -113.344-159.406 138.248 1.00 82.06 C ANISOU 1611 CA PHE A 203 11953 9004 10223 -516 -2442 2632 C ATOM 1612 C PHE A 203 -113.976-159.717 139.599 1.00 85.17 C ANISOU 1612 C PHE A 203 12008 9404 10948 -288 -2406 2481 C ATOM 1613 O PHE A 203 -114.180-160.890 139.928 1.00 79.81 O ANISOU 1613 O PHE A 203 11254 8851 10219 -265 -2328 2334 O ATOM 1614 CB PHE A 203 -111.823-159.293 138.386 1.00 84.09 C ANISOU 1614 CB PHE A 203 12300 9298 10352 -579 -2104 2511 C ATOM 1615 CG PHE A 203 -111.157-160.594 138.755 1.00 81.53 C ANISOU 1615 CG PHE A 203 11940 9133 9905 -583 -1833 2271 C ATOM 1616 CD1 PHE A 203 -110.875-161.542 137.784 1.00 74.29 C ANISOU 1616 CD1 PHE A 203 11248 8324 8654 -762 -1766 2235 C ATOM 1617 CD2 PHE A 203 -110.824-160.873 140.070 1.00 74.17 C ANISOU 1617 CD2 PHE A 203 10761 8227 9191 -415 -1654 2082 C ATOM 1618 CE1 PHE A 203 -110.274-162.739 138.114 1.00 70.68 C ANISOU 1618 CE1 PHE A 203 10746 7984 8124 -754 -1522 2015 C ATOM 1619 CE2 PHE A 203 -110.215-162.072 140.407 1.00 73.85 C ANISOU 1619 CE2 PHE A 203 10686 8310 9063 -416 -1437 1885 C ATOM 1620 CZ PHE A 203 -109.943-163.006 139.428 1.00 74.18 C ANISOU 1620 CZ PHE A 203 10928 8444 8813 -576 -1369 1850 C ATOM 1621 N VAL A 204 -114.289-158.687 140.391 1.00 85.43 N ANISOU 1621 N VAL A 204 11848 9295 11315 -128 -2447 2508 N ATOM 1622 CA VAL A 204 -114.973-158.902 141.664 1.00 91.37 C ANISOU 1622 CA VAL A 204 12298 10043 12375 71 -2400 2364 C ATOM 1623 C VAL A 204 -116.361-159.484 141.426 1.00 89.94 C ANISOU 1623 C VAL A 204 12005 9879 12289 99 -2642 2430 C ATOM 1624 O VAL A 204 -116.799-160.393 142.141 1.00 74.39 O ANISOU 1624 O VAL A 204 9871 8003 10391 173 -2559 2282 O ATOM 1625 CB VAL A 204 -115.032-157.587 142.467 1.00 84.75 C ANISOU 1625 CB VAL A 204 11304 9026 11871 218 -2384 2373 C ATOM 1626 CG1 VAL A 204 -115.891-157.745 143.724 1.00 75.86 C ANISOU 1626 CG1 VAL A 204 9881 7882 11061 408 -2333 2228 C ATOM 1627 CG2 VAL A 204 -113.631-157.125 142.830 1.00 77.92 C ANISOU 1627 CG2 VAL A 204 10527 8156 10923 184 -2136 2281 C ATOM 1628 N ILE A 205 -117.076-158.963 140.424 1.00 81.23 N ANISOU 1628 N ILE A 205 10987 8679 11198 31 -2960 2663 N ATOM 1629 CA ILE A 205 -118.364-159.536 140.036 1.00 82.69 C ANISOU 1629 CA ILE A 205 11078 8879 11461 26 -3234 2749 C ATOM 1630 C ILE A 205 -118.189-160.992 139.628 1.00 90.01 C ANISOU 1630 C ILE A 205 12141 10001 12059 -110 -3165 2644 C ATOM 1631 O ILE A 205 -118.946-161.874 140.050 1.00 82.29 O ANISOU 1631 O ILE A 205 10992 9093 11181 -58 -3186 2553 O ATOM 1632 CB ILE A 205 -118.994-158.715 138.896 1.00 88.18 C ANISOU 1632 CB ILE A 205 11893 9432 12178 -60 -3624 3046 C ATOM 1633 CG1 ILE A 205 -119.139-157.248 139.302 1.00 87.94 C ANISOU 1633 CG1 ILE A 205 11724 9180 12507 83 -3683 3144 C ATOM 1634 CG2 ILE A 205 -120.339-159.301 138.484 1.00 80.60 C ANISOU 1634 CG2 ILE A 205 10813 8489 11321 -76 -3926 3126 C ATOM 1635 CD1 ILE A 205 -119.616-156.368 138.171 1.00 84.43 C ANISOU 1635 CD1 ILE A 205 11393 8643 12045 -28 -3940 3333 C ATOM 1636 N TYR A 206 -117.182-161.261 138.795 1.00 87.91 N ANISOU 1636 N TYR A 206 12185 9812 11403 -292 -3065 2650 N ATOM 1637 CA TYR A 206 -116.947-162.622 138.325 1.00 86.38 C ANISOU 1637 CA TYR A 206 12146 9780 10893 -431 -2981 2537 C ATOM 1638 C TYR A 206 -116.578-163.550 139.479 1.00 83.71 C ANISOU 1638 C TYR A 206 11628 9545 10634 -315 -2682 2280 C ATOM 1639 O TYR A 206 -117.046-164.693 139.541 1.00 82.63 O ANISOU 1639 O TYR A 206 11447 9499 10447 -336 -2692 2188 O ATOM 1640 CB TYR A 206 -115.862-162.625 137.249 1.00 84.02 C ANISOU 1640 CB TYR A 206 12211 9527 10187 -647 -2877 2570 C ATOM 1641 CG TYR A 206 -115.112-163.930 137.151 1.00 89.90 C ANISOU 1641 CG TYR A 206 13073 10421 10664 -739 -2611 2359 C ATOM 1642 CD1 TYR A 206 -115.694-165.044 136.561 1.00 84.79 C ANISOU 1642 CD1 TYR A 206 12526 9858 9831 -853 -2726 2327 C ATOM 1643 CD2 TYR A 206 -113.821-164.048 137.647 1.00 93.32 C ANISOU 1643 CD2 TYR A 206 13508 10895 11056 -712 -2254 2191 C ATOM 1644 CE1 TYR A 206 -115.010-166.242 136.471 1.00 89.50 C ANISOU 1644 CE1 TYR A 206 13227 10565 10213 -930 -2475 2124 C ATOM 1645 CE2 TYR A 206 -113.129-165.242 137.562 1.00 95.01 C ANISOU 1645 CE2 TYR A 206 13804 11219 11076 -781 -2014 1998 C ATOM 1646 CZ TYR A 206 -113.730-166.336 136.971 1.00 93.04 C ANISOU 1646 CZ TYR A 206 13660 11042 10650 -886 -2117 1961 C ATOM 1647 OH TYR A 206 -113.055-167.532 136.878 1.00 92.94 O ANISOU 1647 OH TYR A 206 13729 11115 10471 -949 -1873 1760 O ATOM 1648 N MET A 207 -115.726-163.084 140.396 1.00 81.87 N ANISOU 1648 N MET A 207 11300 9290 10519 -205 -2430 2169 N ATOM 1649 CA MET A 207 -115.434-163.865 141.596 1.00 78.98 C ANISOU 1649 CA MET A 207 10758 9002 10251 -91 -2189 1952 C ATOM 1650 C MET A 207 -116.698-164.130 142.398 1.00 80.21 C ANISOU 1650 C MET A 207 10646 9143 10685 41 -2293 1927 C ATOM 1651 O MET A 207 -116.914-165.244 142.892 1.00 82.89 O ANISOU 1651 O MET A 207 10906 9575 11013 56 -2206 1798 O ATOM 1652 CB MET A 207 -114.411-163.138 142.468 1.00 78.04 C ANISOU 1652 CB MET A 207 10578 8839 10236 -2 -1961 1865 C ATOM 1653 CG MET A 207 -113.000-163.234 141.950 1.00 84.00 C ANISOU 1653 CG MET A 207 11535 9638 10745 -123 -1767 1820 C ATOM 1654 SD MET A 207 -112.523-164.958 141.735 1.00 85.71 S ANISOU 1654 SD MET A 207 11836 10004 10727 -210 -1603 1652 S ATOM 1655 CE MET A 207 -112.503-165.511 143.436 1.00 66.95 C ANISOU 1655 CE MET A 207 9193 7661 8586 -30 -1454 1473 C ATOM 1656 N PHE A 208 -117.548-163.115 142.528 1.00 78.78 N ANISOU 1656 N PHE A 208 10321 8836 10776 133 -2472 2049 N ATOM 1657 CA PHE A 208 -118.747-163.239 143.342 1.00 76.92 C ANISOU 1657 CA PHE A 208 9799 8570 10858 265 -2533 2013 C ATOM 1658 C PHE A 208 -119.715-164.254 142.756 1.00 83.80 C ANISOU 1658 C PHE A 208 10652 9510 11679 184 -2727 2056 C ATOM 1659 O PHE A 208 -120.272-165.079 143.487 1.00 79.59 O ANISOU 1659 O PHE A 208 9945 9038 11257 235 -2648 1940 O ATOM 1660 CB PHE A 208 -119.420-161.878 143.472 1.00 81.39 C ANISOU 1660 CB PHE A 208 10212 8957 11757 380 -2685 2137 C ATOM 1661 CG PHE A 208 -120.732-161.929 144.178 1.00 74.39 C ANISOU 1661 CG PHE A 208 9013 8019 11235 510 -2747 2107 C ATOM 1662 CD1 PHE A 208 -120.791-162.209 145.532 1.00 79.69 C ANISOU 1662 CD1 PHE A 208 9499 8724 12055 622 -2485 1908 C ATOM 1663 CD2 PHE A 208 -121.912-161.698 143.492 1.00 73.57 C ANISOU 1663 CD2 PHE A 208 8798 7827 11329 508 -3070 2281 C ATOM 1664 CE1 PHE A 208 -122.004-162.259 146.188 1.00 85.41 C ANISOU 1664 CE1 PHE A 208 9934 9401 13119 728 -2500 1867 C ATOM 1665 CE2 PHE A 208 -123.127-161.745 144.143 1.00 87.13 C ANISOU 1665 CE2 PHE A 208 10190 9488 13426 628 -3107 2244 C ATOM 1666 CZ PHE A 208 -123.171-162.028 145.495 1.00 87.32 C ANISOU 1666 CZ PHE A 208 10032 9551 13593 736 -2800 2029 C ATOM 1667 N VAL A 209 -119.933-164.209 141.443 1.00 84.37 N ANISOU 1667 N VAL A 209 10913 9570 11576 40 -2988 2226 N ATOM 1668 CA VAL A 209 -120.924-165.088 140.834 1.00 83.07 C ANISOU 1668 CA VAL A 209 10734 9455 11376 -54 -3221 2281 C ATOM 1669 C VAL A 209 -120.394-166.514 140.748 1.00 93.65 C ANISOU 1669 C VAL A 209 12219 10946 12419 -164 -3050 2121 C ATOM 1670 O VAL A 209 -121.031-167.461 141.233 1.00 84.71 O ANISOU 1670 O VAL A 209 10935 9871 11381 -143 -3030 2027 O ATOM 1671 CB VAL A 209 -121.338-164.555 139.452 1.00 82.52 C ANISOU 1671 CB VAL A 209 10847 9315 11193 -193 -3589 2525 C ATOM 1672 CG1 VAL A 209 -122.280-165.531 138.780 1.00 83.27 C ANISOU 1672 CG1 VAL A 209 10957 9468 11212 -320 -3845 2573 C ATOM 1673 CG2 VAL A 209 -121.980-163.172 139.571 1.00 83.24 C ANISOU 1673 CG2 VAL A 209 10757 9225 11647 -66 -3791 2698 C ATOM 1674 N VAL A 210 -119.214-166.684 140.153 1.00 89.85 N ANISOU 1674 N VAL A 210 12022 10517 11599 -281 -2908 2082 N ATOM 1675 CA VAL A 210 -118.714-168.013 139.804 1.00 78.05 C ANISOU 1675 CA VAL A 210 10700 9138 9816 -408 -2776 1944 C ATOM 1676 C VAL A 210 -118.053-168.714 140.986 1.00 85.00 C ANISOU 1676 C VAL A 210 11457 10077 10762 -299 -2452 1733 C ATOM 1677 O VAL A 210 -118.254-169.913 141.183 1.00 91.08 O ANISOU 1677 O VAL A 210 12204 10912 11489 -329 -2397 1621 O ATOM 1678 CB VAL A 210 -117.737-167.886 138.618 1.00 79.00 C ANISOU 1678 CB VAL A 210 11176 9277 9561 -589 -2738 1982 C ATOM 1679 CG1 VAL A 210 -117.040-169.209 138.350 1.00 84.56 C ANISOU 1679 CG1 VAL A 210 12048 10080 10001 -699 -2529 1799 C ATOM 1680 CG2 VAL A 210 -118.464-167.413 137.359 1.00 67.97 C ANISOU 1680 CG2 VAL A 210 9958 7834 8032 -744 -3098 2202 C ATOM 1681 N HIS A 211 -117.268-168.003 141.801 1.00 80.45 N ANISOU 1681 N HIS A 211 10804 9468 10294 -181 -2253 1682 N ATOM 1682 CA HIS A 211 -116.463-168.635 142.839 1.00 71.47 C ANISOU 1682 CA HIS A 211 9595 8382 9178 -105 -1970 1501 C ATOM 1683 C HIS A 211 -117.030-168.431 144.235 1.00 72.22 C ANISOU 1683 C HIS A 211 9419 8454 9569 58 -1912 1448 C ATOM 1684 O HIS A 211 -116.334-168.683 145.224 1.00 77.32 O ANISOU 1684 O HIS A 211 10009 9124 10246 127 -1701 1323 O ATOM 1685 CB HIS A 211 -115.029-168.118 142.772 1.00 70.70 C ANISOU 1685 CB HIS A 211 9626 8274 8963 -118 -1773 1460 C ATOM 1686 CG HIS A 211 -114.373-168.381 141.460 1.00 76.25 C ANISOU 1686 CG HIS A 211 10605 9005 9364 -292 -1759 1481 C ATOM 1687 ND1 HIS A 211 -113.634-169.518 141.218 1.00 70.89 N ANISOU 1687 ND1 HIS A 211 10038 8387 8509 -367 -1582 1339 N ATOM 1688 CD2 HIS A 211 -114.379-167.677 140.304 1.00 82.84 C ANISOU 1688 CD2 HIS A 211 11637 9804 10034 -416 -1894 1625 C ATOM 1689 CE1 HIS A 211 -113.197-169.492 139.973 1.00 66.16 C ANISOU 1689 CE1 HIS A 211 9695 7796 7646 -533 -1578 1373 C ATOM 1690 NE2 HIS A 211 -113.636-168.389 139.395 1.00 72.32 N ANISOU 1690 NE2 HIS A 211 10546 8525 8407 -576 -1771 1554 N ATOM 1691 N PHE A 212 -118.280-167.994 144.339 1.00 72.97 N ANISOU 1691 N PHE A 212 9345 8497 9883 112 -2094 1537 N ATOM 1692 CA PHE A 212 -118.858-167.739 145.650 1.00 80.72 C ANISOU 1692 CA PHE A 212 10073 9448 11147 254 -2002 1471 C ATOM 1693 C PHE A 212 -120.329-168.137 145.690 1.00 79.36 C ANISOU 1693 C PHE A 212 9710 9270 11175 264 -2162 1512 C ATOM 1694 O PHE A 212 -120.743-168.893 146.573 1.00 74.65 O ANISOU 1694 O PHE A 212 8976 8718 10669 296 -2044 1409 O ATOM 1695 CB PHE A 212 -118.678-166.267 146.017 1.00 77.30 C ANISOU 1695 CB PHE A 212 9576 8907 10890 358 -1983 1516 C ATOM 1696 CG PHE A 212 -118.996-165.960 147.444 1.00 71.93 C ANISOU 1696 CG PHE A 212 8686 8195 10449 491 -1818 1405 C ATOM 1697 CD1 PHE A 212 -118.210-166.469 148.464 1.00 69.96 C ANISOU 1697 CD1 PHE A 212 8457 8010 10113 509 -1584 1255 C ATOM 1698 CD2 PHE A 212 -120.081-165.164 147.769 1.00 72.71 C ANISOU 1698 CD2 PHE A 212 8571 8190 10864 590 -1898 1448 C ATOM 1699 CE1 PHE A 212 -118.502-166.188 149.787 1.00 66.65 C ANISOU 1699 CE1 PHE A 212 7887 7566 9871 603 -1428 1148 C ATOM 1700 CE2 PHE A 212 -120.377-164.879 149.085 1.00 70.59 C ANISOU 1700 CE2 PHE A 212 8131 7891 10801 696 -1707 1321 C ATOM 1701 CZ PHE A 212 -119.586-165.392 150.096 1.00 64.44 C ANISOU 1701 CZ PHE A 212 7412 7189 9883 692 -1471 1170 C ATOM 1702 N ILE A 213 -121.123-167.639 144.739 1.00 73.32 N ANISOU 1702 N ILE A 213 8931 8442 10486 226 -2440 1672 N ATOM 1703 CA ILE A 213 -122.544-167.976 144.701 1.00 80.33 C ANISOU 1703 CA ILE A 213 9606 9311 11605 229 -2624 1725 C ATOM 1704 C ILE A 213 -122.739-169.404 144.201 1.00 86.70 C ANISOU 1704 C ILE A 213 10511 10220 12212 88 -2683 1688 C ATOM 1705 O ILE A 213 -123.408-170.221 144.846 1.00 80.88 O ANISOU 1705 O ILE A 213 9607 9520 11603 97 -2622 1609 O ATOM 1706 CB ILE A 213 -123.314-166.964 143.830 1.00 78.92 C ANISOU 1706 CB ILE A 213 9372 9015 11598 233 -2947 1928 C ATOM 1707 CG1 ILE A 213 -123.330-165.576 144.480 1.00 87.15 C ANISOU 1707 CG1 ILE A 213 10259 9925 12930 396 -2880 1948 C ATOM 1708 CG2 ILE A 213 -124.736-167.439 143.579 1.00 73.41 C ANISOU 1708 CG2 ILE A 213 8465 8302 11126 205 -3188 1999 C ATOM 1709 CD1 ILE A 213 -123.979-165.547 145.847 1.00 87.21 C ANISOU 1709 CD1 ILE A 213 9961 9907 13267 539 -2676 1811 C ATOM 1710 N ILE A 214 -122.146-169.724 143.048 1.00 85.16 N ANISOU 1710 N ILE A 214 10600 10061 11695 -58 -2786 1736 N ATOM 1711 CA ILE A 214 -122.356-171.040 142.441 1.00 82.08 C ANISOU 1711 CA ILE A 214 10332 9747 11108 -209 -2861 1695 C ATOM 1712 C ILE A 214 -121.886-172.184 143.332 1.00 80.01 C ANISOU 1712 C ILE A 214 10051 9557 10792 -191 -2586 1510 C ATOM 1713 O ILE A 214 -122.628-173.171 143.470 1.00 83.23 O ANISOU 1713 O ILE A 214 10370 9994 11258 -243 -2633 1470 O ATOM 1714 CB ILE A 214 -121.715-171.077 141.037 1.00 77.72 C ANISOU 1714 CB ILE A 214 10124 9213 10194 -380 -2982 1760 C ATOM 1715 CG1 ILE A 214 -122.545-170.254 140.050 1.00 82.48 C ANISOU 1715 CG1 ILE A 214 10748 9745 10847 -446 -3354 1977 C ATOM 1716 CG2 ILE A 214 -121.558-172.507 140.546 1.00 78.89 C ANISOU 1716 CG2 ILE A 214 10447 9437 10091 -532 -2951 1651 C ATOM 1717 CD1 ILE A 214 -121.929-170.153 138.671 1.00 86.87 C ANISOU 1717 CD1 ILE A 214 11678 10314 11015 -638 -3473 2059 C ATOM 1718 N PRO A 215 -120.698-172.137 143.957 1.00 77.53 N ANISOU 1718 N PRO A 215 9813 9263 10384 -128 -2317 1404 N ATOM 1719 CA PRO A 215 -120.323-173.247 144.853 1.00 77.18 C ANISOU 1719 CA PRO A 215 9740 9269 10318 -110 -2097 1253 C ATOM 1720 C PRO A 215 -121.327-173.493 145.968 1.00 76.66 C ANISOU 1720 C PRO A 215 9408 9200 10519 -36 -2057 1225 C ATOM 1721 O PRO A 215 -121.578-174.652 146.325 1.00 77.24 O ANISOU 1721 O PRO A 215 9457 9308 10581 -85 -2000 1152 O ATOM 1722 CB PRO A 215 -118.959-172.805 145.398 1.00 70.43 C ANISOU 1722 CB PRO A 215 8963 8412 9386 -35 -1867 1182 C ATOM 1723 CG PRO A 215 -118.397-171.951 144.318 1.00 73.09 C ANISOU 1723 CG PRO A 215 9476 8723 9573 -88 -1950 1267 C ATOM 1724 CD PRO A 215 -119.579-171.189 143.786 1.00 72.86 C ANISOU 1724 CD PRO A 215 9356 8646 9683 -94 -2217 1421 C ATOM 1725 N LEU A 216 -121.925-172.435 146.521 1.00 78.44 N ANISOU 1725 N LEU A 216 9434 9375 10993 74 -2073 1276 N ATOM 1726 CA LEU A 216 -122.903-172.619 147.590 1.00 84.34 C ANISOU 1726 CA LEU A 216 9925 10117 12003 135 -1994 1233 C ATOM 1727 C LEU A 216 -124.165-173.305 147.078 1.00 85.94 C ANISOU 1727 C LEU A 216 10003 10323 12326 47 -2193 1289 C ATOM 1728 O LEU A 216 -124.715-174.187 147.748 1.00 72.72 O ANISOU 1728 O LEU A 216 8212 8680 10739 19 -2101 1224 O ATOM 1729 CB LEU A 216 -123.250-171.274 148.223 1.00 81.61 C ANISOU 1729 CB LEU A 216 9395 9696 11916 271 -1947 1255 C ATOM 1730 CG LEU A 216 -124.300-171.333 149.335 1.00 81.93 C ANISOU 1730 CG LEU A 216 9160 9722 12249 332 -1822 1194 C ATOM 1731 CD1 LEU A 216 -123.684-171.829 150.628 1.00 87.85 C ANISOU 1731 CD1 LEU A 216 9955 10523 12901 348 -1528 1055 C ATOM 1732 CD2 LEU A 216 -124.947-169.977 149.530 1.00 88.69 C ANISOU 1732 CD2 LEU A 216 9809 10470 13420 454 -1856 1238 C ATOM 1733 N ILE A 217 -124.635-172.915 145.893 1.00 79.29 N ANISOU 1733 N ILE A 217 9191 9446 11487 -11 -2480 1418 N ATOM 1734 CA ILE A 217 -125.859-173.492 145.347 1.00 81.65 C ANISOU 1734 CA ILE A 217 9364 9742 11920 -106 -2720 1486 C ATOM 1735 C ILE A 217 -125.658-174.969 145.031 1.00 86.13 C ANISOU 1735 C ILE A 217 10097 10377 12254 -253 -2706 1409 C ATOM 1736 O ILE A 217 -126.504-175.812 145.357 1.00 81.57 O ANISOU 1736 O ILE A 217 9367 9811 11813 -307 -2721 1379 O ATOM 1737 CB ILE A 217 -126.310-172.707 144.103 1.00 84.54 C ANISOU 1737 CB ILE A 217 9765 10047 12309 -152 -3071 1661 C ATOM 1738 CG1 ILE A 217 -126.530-171.233 144.446 1.00 76.99 C ANISOU 1738 CG1 ILE A 217 8630 8992 11630 5 -3087 1740 C ATOM 1739 CG2 ILE A 217 -127.583-173.303 143.530 1.00 87.03 C ANISOU 1739 CG2 ILE A 217 9939 10353 12775 -262 -3359 1739 C ATOM 1740 CD1 ILE A 217 -126.908-170.389 143.250 1.00 82.26 C ANISOU 1740 CD1 ILE A 217 9347 9580 12329 -37 -3453 1940 C ATOM 1741 N VAL A 218 -124.530-175.306 144.402 1.00 87.00 N ANISOU 1741 N VAL A 218 10512 10518 12025 -322 -2662 1368 N ATOM 1742 CA VAL A 218 -124.265-176.695 144.030 1.00 82.87 C ANISOU 1742 CA VAL A 218 10164 10034 11288 -459 -2638 1278 C ATOM 1743 C VAL A 218 -124.164-177.571 145.272 1.00 79.03 C ANISOU 1743 C VAL A 218 9575 9568 10885 -413 -2386 1159 C ATOM 1744 O VAL A 218 -124.739-178.666 145.330 1.00 82.29 O ANISOU 1744 O VAL A 218 9951 9987 11327 -506 -2416 1120 O ATOM 1745 CB VAL A 218 -122.989-176.790 143.174 1.00 80.51 C ANISOU 1745 CB VAL A 218 10197 9750 10641 -526 -2584 1236 C ATOM 1746 CG1 VAL A 218 -122.562-178.241 143.023 1.00 79.11 C ANISOU 1746 CG1 VAL A 218 10182 9591 10286 -632 -2482 1104 C ATOM 1747 CG2 VAL A 218 -123.218-176.161 141.812 1.00 68.75 C ANISOU 1747 CG2 VAL A 218 8863 8245 9013 -633 -2862 1363 C ATOM 1748 N ILE A 219 -123.427-177.106 146.283 1.00 70.52 N ANISOU 1748 N ILE A 219 8465 8493 9837 -284 -2148 1107 N ATOM 1749 CA ILE A 219 -123.290-177.883 147.511 1.00 78.88 C ANISOU 1749 CA ILE A 219 9455 9566 10949 -254 -1924 1014 C ATOM 1750 C ILE A 219 -124.648-178.070 148.176 1.00 84.09 C ANISOU 1750 C ILE A 219 9848 10223 11879 -261 -1940 1035 C ATOM 1751 O ILE A 219 -124.972-179.160 148.665 1.00 83.92 O ANISOU 1751 O ILE A 219 9796 10210 11880 -331 -1867 987 O ATOM 1752 CB ILE A 219 -122.272-177.215 148.455 1.00 74.41 C ANISOU 1752 CB ILE A 219 8914 9002 10358 -129 -1704 968 C ATOM 1753 CG1 ILE A 219 -120.852-177.441 147.929 1.00 83.84 C ANISOU 1753 CG1 ILE A 219 10354 10197 11304 -144 -1644 920 C ATOM 1754 CG2 ILE A 219 -122.417-177.749 149.873 1.00 64.88 C ANISOU 1754 CG2 ILE A 219 7603 7806 9243 -101 -1507 905 C ATOM 1755 CD1 ILE A 219 -119.769-176.915 148.840 1.00 83.60 C ANISOU 1755 CD1 ILE A 219 10348 10164 11251 -39 -1453 874 C ATOM 1756 N PHE A 220 -125.476-177.023 148.176 1.00 79.15 N ANISOU 1756 N PHE A 220 9017 9572 11485 -195 -2032 1109 N ATOM 1757 CA PHE A 220 -126.781-177.118 148.820 1.00 74.93 C ANISOU 1757 CA PHE A 220 8189 9024 11257 -195 -2017 1118 C ATOM 1758 C PHE A 220 -127.729-178.020 148.040 1.00 82.47 C ANISOU 1758 C PHE A 220 9087 9978 12270 -340 -2242 1162 C ATOM 1759 O PHE A 220 -128.459-178.819 148.636 1.00 77.77 O ANISOU 1759 O PHE A 220 8345 9390 11814 -401 -2165 1127 O ATOM 1760 CB PHE A 220 -127.385-175.727 148.998 1.00 80.79 C ANISOU 1760 CB PHE A 220 8705 9713 12277 -72 -2050 1174 C ATOM 1761 CG PHE A 220 -127.203-175.168 150.378 1.00 97.41 C ANISOU 1761 CG PHE A 220 10710 11813 14490 42 -1748 1087 C ATOM 1762 CD1 PHE A 220 -125.977-174.670 150.784 1.00105.94 C ANISOU 1762 CD1 PHE A 220 11977 12903 15374 114 -1597 1037 C ATOM 1763 CD2 PHE A 220 -128.261-175.142 151.271 1.00105.24 C ANISOU 1763 CD2 PHE A 220 11424 12787 15777 61 -1607 1046 C ATOM 1764 CE1 PHE A 220 -125.810-174.157 152.056 1.00110.25 C ANISOU 1764 CE1 PHE A 220 12458 13441 15991 197 -1336 951 C ATOM 1765 CE2 PHE A 220 -128.098-174.628 152.543 1.00112.12 C ANISOU 1765 CE2 PHE A 220 12237 13652 16711 143 -1311 949 C ATOM 1766 CZ PHE A 220 -126.873-174.133 152.935 1.00114.83 C ANISOU 1766 CZ PHE A 220 12792 14006 16832 207 -1188 902 C ATOM 1767 N PHE A 221 -127.734-177.911 146.709 1.00 81.20 N ANISOU 1767 N PHE A 221 9054 9806 11992 -414 -2525 1241 N ATOM 1768 CA PHE A 221 -128.623-178.743 145.903 1.00 84.48 C ANISOU 1768 CA PHE A 221 9439 10217 12443 -572 -2776 1283 C ATOM 1769 C PHE A 221 -128.260-180.217 146.032 1.00 92.71 C ANISOU 1769 C PHE A 221 10646 11282 13296 -690 -2666 1180 C ATOM 1770 O PHE A 221 -129.112-181.056 146.348 1.00 95.42 O ANISOU 1770 O PHE A 221 10841 11620 13794 -778 -2676 1163 O ATOM 1771 CB PHE A 221 -128.573-178.306 144.439 1.00 80.02 C ANISOU 1771 CB PHE A 221 9044 9635 11723 -650 -3103 1387 C ATOM 1772 CG PHE A 221 -129.342-179.209 143.509 1.00 84.91 C ANISOU 1772 CG PHE A 221 9702 10251 12309 -843 -3387 1421 C ATOM 1773 CD1 PHE A 221 -130.690-178.992 143.267 1.00 90.40 C ANISOU 1773 CD1 PHE A 221 10118 10910 13321 -883 -3656 1530 C ATOM 1774 CD2 PHE A 221 -128.717-180.274 142.877 1.00 90.21 C ANISOU 1774 CD2 PHE A 221 10680 10944 12650 -988 -3388 1336 C ATOM 1775 CE1 PHE A 221 -131.399-179.822 142.415 1.00 88.89 C ANISOU 1775 CE1 PHE A 221 9963 10713 13100 -1077 -3943 1562 C ATOM 1776 CE2 PHE A 221 -129.423-181.107 142.027 1.00 92.86 C ANISOU 1776 CE2 PHE A 221 11072 11270 12942 -1181 -3652 1352 C ATOM 1777 CZ PHE A 221 -130.762-180.881 141.796 1.00 87.54 C ANISOU 1777 CZ PHE A 221 10128 10567 12564 -1233 -3941 1469 C ATOM 1778 N CYS A 222 -126.990-180.547 145.788 1.00 86.05 N ANISOU 1778 N CYS A 222 10100 10453 12142 -695 -2557 1109 N ATOM 1779 CA CYS A 222 -126.557-181.942 145.803 1.00 82.65 C ANISOU 1779 CA CYS A 222 9842 10016 11546 -799 -2467 1009 C ATOM 1780 C CYS A 222 -126.828-182.599 147.150 1.00 84.48 C ANISOU 1780 C CYS A 222 9920 10244 11934 -775 -2243 960 C ATOM 1781 O CYS A 222 -127.408-183.689 147.215 1.00 90.19 O ANISOU 1781 O CYS A 222 10612 10946 12711 -894 -2270 935 O ATOM 1782 CB CYS A 222 -125.073-182.024 145.444 1.00 66.21 C ANISOU 1782 CB CYS A 222 8056 7932 9167 -773 -2345 934 C ATOM 1783 SG CYS A 222 -124.727-181.669 143.699 1.00 83.75 S ANISOU 1783 SG CYS A 222 10547 10155 11118 -883 -2581 965 S ATOM 1784 N TYR A 223 -126.427-181.946 148.242 1.00 82.56 N ANISOU 1784 N TYR A 223 9596 10018 11756 -637 -2023 949 N ATOM 1785 CA TYR A 223 -126.629-182.549 149.555 1.00 84.58 C ANISOU 1785 CA TYR A 223 9750 10273 12113 -636 -1802 909 C ATOM 1786 C TYR A 223 -128.089-182.503 149.979 1.00 82.97 C ANISOU 1786 C TYR A 223 9244 10071 12209 -678 -1822 949 C ATOM 1787 O TYR A 223 -128.543-183.383 150.718 1.00 78.86 O ANISOU 1787 O TYR A 223 8655 9542 11765 -758 -1702 925 O ATOM 1788 CB TYR A 223 -125.735-181.864 150.585 1.00 71.96 C ANISOU 1788 CB TYR A 223 8190 8692 10461 -500 -1573 880 C ATOM 1789 CG TYR A 223 -124.304-182.310 150.454 1.00 81.05 C ANISOU 1789 CG TYR A 223 9605 9828 11363 -481 -1510 828 C ATOM 1790 CD1 TYR A 223 -124.000-183.651 150.267 1.00 82.87 C ANISOU 1790 CD1 TYR A 223 9978 10017 11493 -578 -1514 786 C ATOM 1791 CD2 TYR A 223 -123.261-181.400 150.486 1.00 76.43 C ANISOU 1791 CD2 TYR A 223 9113 9253 10673 -367 -1448 819 C ATOM 1792 CE1 TYR A 223 -122.701-184.079 150.134 1.00 81.88 C ANISOU 1792 CE1 TYR A 223 10061 9856 11193 -550 -1449 731 C ATOM 1793 CE2 TYR A 223 -121.950-181.821 150.354 1.00 72.15 C ANISOU 1793 CE2 TYR A 223 8778 8688 9949 -350 -1386 768 C ATOM 1794 CZ TYR A 223 -121.679-183.163 150.173 1.00 81.92 C ANISOU 1794 CZ TYR A 223 10135 9879 11113 -435 -1385 723 C ATOM 1795 OH TYR A 223 -120.380-183.595 150.035 1.00 80.09 O ANISOU 1795 OH TYR A 223 10076 9603 10750 -406 -1315 665 O ATOM 1796 N GLY A 224 -128.835-181.495 149.524 1.00 77.72 N ANISOU 1796 N GLY A 224 8389 9405 11738 -631 -1972 1015 N ATOM 1797 CA GLY A 224 -130.266-181.492 149.766 1.00 73.19 C ANISOU 1797 CA GLY A 224 7493 8818 11499 -677 -2018 1052 C ATOM 1798 C GLY A 224 -130.952-182.675 149.114 1.00 84.88 C ANISOU 1798 C GLY A 224 8967 10282 13003 -858 -2206 1066 C ATOM 1799 O GLY A 224 -131.723-183.394 149.754 1.00 89.76 O ANISOU 1799 O GLY A 224 9421 10891 13792 -944 -2105 1048 O ATOM 1800 N GLN A 225 -130.669-182.898 147.828 1.00 83.94 N ANISOU 1800 N GLN A 225 9044 10153 12698 -933 -2473 1093 N ATOM 1801 CA GLN A 225 -131.256-184.032 147.121 1.00 88.23 C ANISOU 1801 CA GLN A 225 9622 10672 13229 -1123 -2672 1092 C ATOM 1802 C GLN A 225 -130.785-185.353 147.713 1.00 85.06 C ANISOU 1802 C GLN A 225 9377 10252 12689 -1203 -2473 1001 C ATOM 1803 O GLN A 225 -131.568-186.304 147.834 1.00 85.00 O ANISOU 1803 O GLN A 225 9271 10216 12810 -1343 -2506 994 O ATOM 1804 CB GLN A 225 -130.910-183.958 145.635 1.00 77.29 C ANISOU 1804 CB GLN A 225 8478 9280 11608 -1200 -2972 1121 C ATOM 1805 CG GLN A 225 -131.645-182.865 144.887 1.00 83.98 C ANISOU 1805 CG GLN A 225 9164 10122 12622 -1177 -3267 1247 C ATOM 1806 CD GLN A 225 -133.127-183.148 144.770 1.00 86.56 C ANISOU 1806 CD GLN A 225 9176 10421 13290 -1285 -3482 1314 C ATOM 1807 OE1 GLN A 225 -133.536-184.294 144.590 1.00100.80 O ANISOU 1807 OE1 GLN A 225 11007 12209 15082 -1451 -3549 1273 O ATOM 1808 NE2 GLN A 225 -133.941-182.105 144.877 1.00 94.83 N ANISOU 1808 NE2 GLN A 225 9910 11448 14674 -1191 -3592 1414 N ATOM 1809 N LEU A 226 -129.505-185.431 148.082 1.00 78.14 N ANISOU 1809 N LEU A 226 8738 9380 11573 -1120 -2278 940 N ATOM 1810 CA LEU A 226 -128.970-186.655 148.670 1.00 84.35 C ANISOU 1810 CA LEU A 226 9676 10125 12247 -1179 -2107 870 C ATOM 1811 C LEU A 226 -129.700-187.007 149.960 1.00 88.28 C ANISOU 1811 C LEU A 226 9963 10623 12956 -1207 -1911 886 C ATOM 1812 O LEU A 226 -130.111-188.156 150.162 1.00 85.23 O ANISOU 1812 O LEU A 226 9580 10189 12614 -1344 -1896 871 O ATOM 1813 CB LEU A 226 -127.469-186.495 148.919 1.00 71.22 C ANISOU 1813 CB LEU A 226 8253 8460 10348 -1061 -1945 818 C ATOM 1814 CG LEU A 226 -126.667-187.724 149.355 1.00 76.75 C ANISOU 1814 CG LEU A 226 9147 9091 10922 -1102 -1808 753 C ATOM 1815 CD1 LEU A 226 -125.241-187.602 148.850 1.00 74.55 C ANISOU 1815 CD1 LEU A 226 9117 8793 10417 -1020 -1774 692 C ATOM 1816 CD2 LEU A 226 -126.682-187.895 150.870 1.00 75.14 C ANISOU 1816 CD2 LEU A 226 8855 8889 10806 -1066 -1578 777 C ATOM 1817 N VAL A 227 -129.862-186.029 150.853 1.00 72.83 N ANISOU 1817 N VAL A 227 7836 8712 11126 -1088 -1744 908 N ATOM 1818 CA VAL A 227 -130.601-186.277 152.086 1.00 76.71 C ANISOU 1818 CA VAL A 227 8134 9209 11804 -1130 -1523 913 C ATOM 1819 C VAL A 227 -132.032-186.679 151.767 1.00 88.17 C ANISOU 1819 C VAL A 227 9321 10643 13535 -1267 -1651 946 C ATOM 1820 O VAL A 227 -132.584-187.601 152.377 1.00 84.44 O ANISOU 1820 O VAL A 227 8783 10145 13154 -1397 -1538 943 O ATOM 1821 CB VAL A 227 -130.547-185.042 153.005 1.00 71.81 C ANISOU 1821 CB VAL A 227 7385 8634 11266 -984 -1317 907 C ATOM 1822 CG1 VAL A 227 -131.507-185.207 154.172 1.00 71.99 C ANISOU 1822 CG1 VAL A 227 7183 8665 11504 -1050 -1078 900 C ATOM 1823 CG2 VAL A 227 -129.132-184.828 153.514 1.00 78.90 C ANISOU 1823 CG2 VAL A 227 8543 9542 11892 -881 -1179 875 C ATOM 1824 N PHE A 228 -132.645-186.014 150.786 1.00 81.47 N ANISOU 1824 N PHE A 228 8322 9800 12831 -1252 -1906 989 N ATOM 1825 CA PHE A 228 -134.013-186.346 150.401 1.00 84.69 C ANISOU 1825 CA PHE A 228 8455 10185 13539 -1384 -2077 1031 C ATOM 1826 C PHE A 228 -134.115-187.792 149.930 1.00 90.29 C ANISOU 1826 C PHE A 228 9310 10845 14148 -1580 -2199 1011 C ATOM 1827 O PHE A 228 -135.004-188.537 150.358 1.00 87.95 O ANISOU 1827 O PHE A 228 8838 10523 14056 -1718 -2145 1017 O ATOM 1828 CB PHE A 228 -134.494-185.389 149.311 1.00 76.78 C ANISOU 1828 CB PHE A 228 7316 9183 12674 -1336 -2396 1101 C ATOM 1829 CG PHE A 228 -135.884-185.677 148.828 1.00 88.44 C ANISOU 1829 CG PHE A 228 8492 10629 14484 -1472 -2631 1158 C ATOM 1830 CD1 PHE A 228 -136.981-185.161 149.496 1.00 98.62 C ANISOU 1830 CD1 PHE A 228 9368 11910 16196 -1438 -2524 1182 C ATOM 1831 CD2 PHE A 228 -136.096-186.464 147.707 1.00 96.39 C ANISOU 1831 CD2 PHE A 228 9624 11606 15393 -1641 -2956 1179 C ATOM 1832 CE1 PHE A 228 -138.264-185.425 149.058 1.00 96.39 C ANISOU 1832 CE1 PHE A 228 8770 11589 16264 -1563 -2750 1238 C ATOM 1833 CE2 PHE A 228 -137.378-186.734 147.265 1.00 95.72 C ANISOU 1833 CE2 PHE A 228 9255 11489 15627 -1779 -3202 1237 C ATOM 1834 CZ PHE A 228 -138.462-186.213 147.941 1.00 92.34 C ANISOU 1834 CZ PHE A 228 8384 11051 15650 -1736 -3107 1274 C ATOM 1835 N THR A 229 -133.207-188.206 149.043 1.00 87.71 N ANISOU 1835 N THR A 229 9309 10498 13518 -1603 -2349 979 N ATOM 1836 CA THR A 229 -133.222-189.578 148.544 1.00 87.59 C ANISOU 1836 CA THR A 229 9466 10416 13399 -1785 -2457 937 C ATOM 1837 C THR A 229 -133.011-190.582 149.671 1.00 85.61 C ANISOU 1837 C THR A 229 9272 10121 13136 -1839 -2183 905 C ATOM 1838 O THR A 229 -133.681-191.621 149.723 1.00 91.63 O ANISOU 1838 O THR A 229 9981 10824 14010 -2012 -2216 903 O ATOM 1839 CB THR A 229 -132.152-189.756 147.465 1.00 82.81 C ANISOU 1839 CB THR A 229 9218 9789 12459 -1781 -2600 880 C ATOM 1840 OG1 THR A 229 -132.479-188.955 146.324 1.00 85.78 O ANISOU 1840 OG1 THR A 229 9569 10197 12826 -1786 -2895 928 O ATOM 1841 CG2 THR A 229 -132.054-191.213 147.040 1.00 81.80 C ANISOU 1841 CG2 THR A 229 9293 9569 12220 -1959 -2663 807 C ATOM 1842 N VAL A 230 -132.089-190.287 150.587 1.00 83.29 N ANISOU 1842 N VAL A 230 9091 9848 12708 -1704 -1927 891 N ATOM 1843 CA VAL A 230 -131.781-191.234 151.655 1.00 79.88 C ANISOU 1843 CA VAL A 230 8758 9364 12230 -1760 -1696 884 C ATOM 1844 C VAL A 230 -132.951-191.345 152.627 1.00 78.33 C ANISOU 1844 C VAL A 230 8280 9185 12299 -1855 -1533 928 C ATOM 1845 O VAL A 230 -133.346-192.449 153.019 1.00 83.51 O ANISOU 1845 O VAL A 230 8945 9774 13011 -2015 -1474 940 O ATOM 1846 CB VAL A 230 -130.480-190.831 152.369 1.00 75.72 C ANISOU 1846 CB VAL A 230 8428 8854 11490 -1601 -1504 870 C ATOM 1847 CG1 VAL A 230 -130.291-191.653 153.629 1.00 70.40 C ANISOU 1847 CG1 VAL A 230 7829 8131 10789 -1664 -1278 895 C ATOM 1848 CG2 VAL A 230 -129.296-191.018 151.435 1.00 68.91 C ANISOU 1848 CG2 VAL A 230 7846 7948 10389 -1541 -1629 812 C ATOM 1849 N LYS A 231 -133.521-190.206 153.032 1.00 80.84 N ANISOU 1849 N LYS A 231 8340 9579 12795 -1763 -1442 949 N ATOM 1850 CA LYS A 231 -134.721-190.231 153.865 1.00 77.93 C ANISOU 1850 CA LYS A 231 7665 9225 12719 -1857 -1266 972 C ATOM 1851 C LYS A 231 -135.843-190.995 153.175 1.00 85.36 C ANISOU 1851 C LYS A 231 8421 10118 13895 -2044 -1471 993 C ATOM 1852 O LYS A 231 -136.612-191.715 153.825 1.00 85.19 O ANISOU 1852 O LYS A 231 8261 10067 14041 -2200 -1327 1009 O ATOM 1853 CB LYS A 231 -135.178-188.806 154.185 1.00 78.25 C ANISOU 1853 CB LYS A 231 7438 9335 12960 -1712 -1166 969 C ATOM 1854 CG LYS A 231 -134.167-187.935 154.926 1.00 88.78 C ANISOU 1854 CG LYS A 231 8930 10715 14089 -1538 -957 939 C ATOM 1855 CD LYS A 231 -134.394-187.934 156.423 1.00 94.92 C ANISOU 1855 CD LYS A 231 9654 11514 14896 -1578 -579 919 C ATOM 1856 CE LYS A 231 -133.526-186.892 157.101 1.00 95.95 C ANISOU 1856 CE LYS A 231 9908 11692 14858 -1410 -403 881 C ATOM 1857 NZ LYS A 231 -133.561-187.037 158.579 1.00103.00 N ANISOU 1857 NZ LYS A 231 10850 12605 15681 -1482 -44 858 N ATOM 1858 N GLU A 232 -135.945-190.851 151.854 1.00 83.21 N ANISOU 1858 N GLU A 232 8156 9835 13626 -2047 -1814 997 N ATOM 1859 CA GLU A 232 -137.017-191.493 151.101 1.00 79.77 C ANISOU 1859 CA GLU A 232 7545 9354 13411 -2232 -2065 1019 C ATOM 1860 C GLU A 232 -136.855-193.006 151.096 1.00 96.82 C ANISOU 1860 C GLU A 232 9917 11422 15448 -2420 -2068 993 C ATOM 1861 O GLU A 232 -137.824-193.745 151.301 1.00 98.54 O ANISOU 1861 O GLU A 232 9949 11596 15896 -2603 -2065 1012 O ATOM 1862 CB GLU A 232 -137.028-190.947 149.674 1.00 90.27 C ANISOU 1862 CB GLU A 232 8904 10693 14702 -2202 -2452 1035 C ATOM 1863 CG GLU A 232 -138.322-191.123 148.917 1.00 98.96 C ANISOU 1863 CG GLU A 232 9724 11767 16110 -2358 -2757 1083 C ATOM 1864 CD GLU A 232 -138.246-190.504 147.536 1.00124.33 C ANISOU 1864 CD GLU A 232 13016 14991 19233 -2333 -3156 1117 C ATOM 1865 OE1 GLU A 232 -137.115-190.330 147.033 1.00141.97 O ANISOU 1865 OE1 GLU A 232 15598 17238 21105 -2251 -3190 1081 O ATOM 1866 OE2 GLU A 232 -139.308-190.181 146.962 1.00123.24 O ANISOU 1866 OE2 GLU A 232 12591 14845 19390 -2403 -3436 1187 O ATOM 1867 N ALA A 233 -135.634-193.486 150.858 1.00 86.32 N ANISOU 1867 N ALA A 233 8965 10051 13783 -2378 -2070 946 N ATOM 1868 CA ALA A 233 -135.410-194.926 150.818 1.00 81.75 C ANISOU 1868 CA ALA A 233 8601 9356 13105 -2540 -2079 914 C ATOM 1869 C ALA A 233 -135.563-195.546 152.203 1.00 83.81 C ANISOU 1869 C ALA A 233 8825 9582 13435 -2610 -1768 954 C ATOM 1870 O ALA A 233 -136.126-196.638 152.341 1.00 84.57 O ANISOU 1870 O ALA A 233 8903 9588 13641 -2807 -1771 966 O ATOM 1871 CB ALA A 233 -134.029-195.224 150.236 1.00 68.87 C ANISOU 1871 CB ALA A 233 7357 7671 11138 -2457 -2135 844 C ATOM 1872 N ALA A 234 -135.081-194.859 153.242 1.00 82.42 N ANISOU 1872 N ALA A 234 8654 9472 13188 -2469 -1503 978 N ATOM 1873 CA ALA A 234 -135.221-195.384 154.596 1.00 86.32 C ANISOU 1873 CA ALA A 234 9148 9942 13708 -2555 -1205 1027 C ATOM 1874 C ALA A 234 -136.680-195.451 155.031 1.00 91.96 C ANISOU 1874 C ALA A 234 9508 10679 14756 -2714 -1102 1060 C ATOM 1875 O ALA A 234 -137.050-196.344 155.801 1.00 89.15 O ANISOU 1875 O ALA A 234 9160 10261 14451 -2886 -933 1101 O ATOM 1876 CB ALA A 234 -134.410-194.541 155.581 1.00 66.17 C ANISOU 1876 CB ALA A 234 6690 7463 10986 -2384 -962 1037 C ATOM 1877 N ALA A 235 -137.521-194.528 154.553 1.00 85.40 N ANISOU 1877 N ALA A 235 8354 9923 14173 -2666 -1201 1050 N ATOM 1878 CA ALA A 235 -138.938-194.580 154.898 1.00 92.14 C ANISOU 1878 CA ALA A 235 8821 10786 15404 -2814 -1110 1074 C ATOM 1879 C ALA A 235 -139.596-195.845 154.364 1.00 93.71 C ANISOU 1879 C ALA A 235 8993 10883 15731 -3056 -1293 1089 C ATOM 1880 O ALA A 235 -140.566-196.335 154.951 1.00 95.05 O ANISOU 1880 O ALA A 235 8935 11028 16154 -3235 -1137 1118 O ATOM 1881 CB ALA A 235 -139.662-193.342 154.366 1.00 76.30 C ANISOU 1881 CB ALA A 235 6461 8852 13678 -2696 -1237 1066 C ATOM 1882 N GLN A 236 -139.087-196.381 153.258 1.00 95.58 N ANISOU 1882 N GLN A 236 9462 11054 15799 -3076 -1608 1062 N ATOM 1883 CA GLN A 236 -139.593-197.619 152.685 1.00 89.98 C ANISOU 1883 CA GLN A 236 8783 10230 15175 -3310 -1801 1057 C ATOM 1884 C GLN A 236 -139.037-198.864 153.365 1.00 86.97 C ANISOU 1884 C GLN A 236 8691 9731 14622 -3426 -1630 1069 C ATOM 1885 O GLN A 236 -139.417-199.975 152.979 1.00 94.07 O ANISOU 1885 O GLN A 236 9638 10511 15592 -3630 -1764 1062 O ATOM 1886 CB GLN A 236 -139.273-197.670 151.188 1.00 95.15 C ANISOU 1886 CB GLN A 236 9600 10856 15698 -3300 -2201 1003 C ATOM 1887 CG GLN A 236 -140.313-197.010 150.308 1.00 97.28 C ANISOU 1887 CG GLN A 236 9544 11178 16239 -3336 -2496 1022 C ATOM 1888 CD GLN A 236 -141.590-197.819 150.237 1.00115.56 C ANISOU 1888 CD GLN A 236 11589 13426 18892 -3596 -2597 1048 C ATOM 1889 OE1 GLN A 236 -142.604-197.454 150.829 1.00121.42 O ANISOU 1889 OE1 GLN A 236 11932 14209 19993 -3636 -2467 1097 O ATOM 1890 NE2 GLN A 236 -141.546-198.929 149.510 1.00112.97 N ANISOU 1890 NE2 GLN A 236 11472 12985 18466 -3782 -2818 1005 N ATOM 1891 N GLN A 237 -138.151-198.714 154.349 1.00 83.78 N ANISOU 1891 N GLN A 237 8486 9344 14004 -3309 -1362 1094 N ATOM 1892 CA GLN A 237 -137.527-199.848 155.031 1.00 90.09 C ANISOU 1892 CA GLN A 237 9578 10016 14637 -3403 -1225 1130 C ATOM 1893 C GLN A 237 -137.404-199.559 156.523 1.00 87.22 C ANISOU 1893 C GLN A 237 9218 9707 14215 -3383 -860 1204 C ATOM 1894 O GLN A 237 -136.333-199.682 157.119 1.00 83.55 O ANISOU 1894 O GLN A 237 9041 9210 13493 -3292 -755 1233 O ATOM 1895 CB GLN A 237 -136.154-200.171 154.442 1.00100.45 C ANISOU 1895 CB GLN A 237 11267 11246 15654 -3274 -1371 1078 C ATOM 1896 CG GLN A 237 -136.172-200.576 152.977 1.00121.65 C ANISOU 1896 CG GLN A 237 14026 13862 18335 -3322 -1703 986 C ATOM 1897 CD GLN A 237 -134.859-201.184 152.522 1.00129.97 C ANISOU 1897 CD GLN A 237 15460 14791 19133 -3240 -1778 918 C ATOM 1898 OE1 GLN A 237 -134.164-201.843 153.296 1.00122.85 O ANISOU 1898 OE1 GLN A 237 14758 13784 18138 -3232 -1627 961 O ATOM 1899 NE2 GLN A 237 -134.515-200.967 151.258 1.00139.24 N ANISOU 1899 NE2 GLN A 237 16736 15967 20202 -3185 -2011 815 N ATOM 1900 N GLN A 238 -138.516-199.182 157.150 1.00 85.68 N ANISOU 1900 N GLN A 238 8700 9588 14265 -3481 -660 1231 N ATOM 1901 CA GLN A 238 -138.483-198.808 158.558 1.00 92.36 C ANISOU 1901 CA GLN A 238 9552 10499 15041 -3482 -285 1280 C ATOM 1902 C GLN A 238 -138.349-200.002 159.496 1.00 97.20 C ANISOU 1902 C GLN A 238 10393 10995 15542 -3686 -111 1375 C ATOM 1903 O GLN A 238 -138.139-199.802 160.698 1.00108.27 O ANISOU 1903 O GLN A 238 11898 12439 16802 -3706 184 1429 O ATOM 1904 CB GLN A 238 -139.734-198.005 158.912 1.00 95.17 C ANISOU 1904 CB GLN A 238 9478 10964 15720 -3524 -89 1257 C ATOM 1905 CG GLN A 238 -139.702-196.570 158.413 1.00104.84 C ANISOU 1905 CG GLN A 238 10510 12307 17019 -3284 -167 1186 C ATOM 1906 CD GLN A 238 -140.842-195.746 158.972 1.00110.18 C ANISOU 1906 CD GLN A 238 10767 13067 18028 -3304 90 1157 C ATOM 1907 OE1 GLN A 238 -141.898-196.278 159.316 1.00111.32 O ANISOU 1907 OE1 GLN A 238 10671 13182 18443 -3514 231 1176 O ATOM 1908 NE2 GLN A 238 -140.631-194.442 159.073 1.00114.64 N ANISOU 1908 NE2 GLN A 238 11234 13726 18597 -3089 166 1103 N ATOM 1909 N GLU A 239 -138.459-201.227 158.986 1.00 92.06 N ANISOU 1909 N GLU A 239 9844 10192 14943 -3847 -293 1400 N ATOM 1910 CA GLU A 239 -138.247-202.413 159.807 1.00 90.99 C ANISOU 1910 CA GLU A 239 9957 9914 14703 -4035 -169 1507 C ATOM 1911 C GLU A 239 -136.770-202.708 160.048 1.00 90.03 C ANISOU 1911 C GLU A 239 10247 9705 14254 -3897 -230 1548 C ATOM 1912 O GLU A 239 -136.451-203.592 160.849 1.00108.00 O ANISOU 1912 O GLU A 239 12760 11857 16419 -4028 -134 1661 O ATOM 1913 CB GLU A 239 -138.921-203.631 159.159 1.00 95.61 C ANISOU 1913 CB GLU A 239 10493 10342 15493 -4263 -347 1512 C ATOM 1914 CG GLU A 239 -138.319-204.068 157.818 1.00 91.23 C ANISOU 1914 CG GLU A 239 10093 9679 14890 -4177 -715 1425 C ATOM 1915 CD GLU A 239 -138.727-203.183 156.641 1.00 99.92 C ANISOU 1915 CD GLU A 239 10948 10898 16119 -4062 -940 1311 C ATOM 1916 OE1 GLU A 239 -139.314-202.100 156.863 1.00109.38 O ANISOU 1916 OE1 GLU A 239 11857 12260 17443 -3989 -826 1302 O ATOM 1917 OE2 GLU A 239 -138.457-203.579 155.486 1.00 87.60 O ANISOU 1917 OE2 GLU A 239 9496 9255 14532 -4050 -1235 1230 O ATOM 1918 N SER A 240 -135.865-201.991 159.389 1.00 90.40 N ANISOU 1918 N SER A 240 10379 9806 14162 -3644 -390 1469 N ATOM 1919 CA SER A 240 -134.429-202.199 159.543 1.00 98.16 C ANISOU 1919 CA SER A 240 11709 10707 14882 -3494 -459 1496 C ATOM 1920 C SER A 240 -133.871-201.120 160.467 1.00 97.10 C ANISOU 1920 C SER A 240 11622 10714 14556 -3344 -265 1524 C ATOM 1921 O SER A 240 -133.794-199.947 160.087 1.00 97.45 O ANISOU 1921 O SER A 240 11526 10904 14595 -3166 -277 1439 O ATOM 1922 CB SER A 240 -133.731-202.176 158.185 1.00 94.18 C ANISOU 1922 CB SER A 240 11284 10154 14347 -3331 -746 1378 C ATOM 1923 OG SER A 240 -132.329-202.299 158.340 1.00101.46 O ANISOU 1923 OG SER A 240 12497 10996 15057 -3171 -790 1393 O ATOM 1924 N ALA A 241 -133.473-201.522 161.678 1.00109.71 N ANISOU 1924 N ALA A 241 12420 11420 17846 -4563 681 -1026 N ATOM 1925 CA ALA A 241 -132.926-200.566 162.636 1.00105.72 C ANISOU 1925 CA ALA A 241 12010 11083 17076 -4288 729 -754 C ATOM 1926 C ALA A 241 -131.605-199.976 162.158 1.00113.62 C ANISOU 1926 C ALA A 241 13208 12038 17924 -3908 558 -775 C ATOM 1927 O ALA A 241 -131.270-198.840 162.516 1.00109.75 O ANISOU 1927 O ALA A 241 12706 11801 17193 -3646 528 -687 O ATOM 1928 CB ALA A 241 -132.741-201.232 163.999 1.00 97.34 C ANISOU 1928 CB ALA A 241 11146 9787 16052 -4423 936 -381 C ATOM 1929 N THR A 242 -130.848-200.725 161.352 1.00114.37 N ANISOU 1929 N THR A 242 13476 11818 18162 -3879 450 -906 N ATOM 1930 CA THR A 242 -129.577-200.222 160.838 1.00104.91 C ANISOU 1930 CA THR A 242 12445 10594 16822 -3536 295 -939 C ATOM 1931 C THR A 242 -129.782-199.237 159.695 1.00100.78 C ANISOU 1931 C THR A 242 11714 10428 16151 -3382 120 -1210 C ATOM 1932 O THR A 242 -129.022-198.273 159.562 1.00 96.63 O ANISOU 1932 O THR A 242 11242 10054 15417 -3089 26 -1168 O ATOM 1933 CB THR A 242 -128.690-201.383 160.383 1.00104.29 C ANISOU 1933 CB THR A 242 12607 10070 16947 -3542 250 -999 C ATOM 1934 OG1 THR A 242 -129.420-202.220 159.478 1.00106.25 O ANISOU 1934 OG1 THR A 242 12731 10208 17430 -3807 220 -1298 O ATOM 1935 CG2 THR A 242 -128.232-202.208 161.579 1.00109.18 C ANISOU 1935 CG2 THR A 242 13479 10327 17676 -3601 400 -657 C ATOM 1936 N THR A 243 -130.793-199.469 158.853 1.00 99.63 N ANISOU 1936 N THR A 243 11325 10422 16107 -3583 70 -1480 N ATOM 1937 CA THR A 243 -131.138-198.498 157.818 1.00 94.32 C ANISOU 1937 CA THR A 243 10424 10137 15275 -3443 -96 -1699 C ATOM 1938 C THR A 243 -131.459-197.141 158.433 1.00 85.01 C ANISOU 1938 C THR A 243 9120 9295 13885 -3259 -74 -1541 C ATOM 1939 O THR A 243 -130.959-196.106 157.979 1.00 89.80 O ANISOU 1939 O THR A 243 9724 10090 14305 -2984 -200 -1550 O ATOM 1940 CB THR A 243 -132.315-199.013 156.985 1.00 97.71 C ANISOU 1940 CB THR A 243 10580 10702 15845 -3718 -140 -1997 C ATOM 1941 OG1 THR A 243 -131.855-200.021 156.077 1.00 99.85 O ANISOU 1941 OG1 THR A 243 10956 10717 16266 -3809 -220 -2233 O ATOM 1942 CG2 THR A 243 -132.957-197.884 156.196 1.00103.57 C ANISOU 1942 CG2 THR A 243 11032 11921 16401 -3580 -287 -2148 C ATOM 1943 N GLN A 244 -132.272-197.132 159.490 1.00 84.09 N ANISOU 1943 N GLN A 244 8902 9247 13801 -3411 95 -1394 N ATOM 1944 CA GLN A 244 -132.557-195.882 160.183 1.00 92.75 C ANISOU 1944 CA GLN A 244 9888 10640 14712 -3230 136 -1264 C ATOM 1945 C GLN A 244 -131.306-195.321 160.848 1.00 98.90 C ANISOU 1945 C GLN A 244 10935 11307 15335 -2962 144 -1046 C ATOM 1946 O GLN A 244 -131.129-194.100 160.908 1.00 95.46 O ANISOU 1946 O GLN A 244 10454 11086 14731 -2716 86 -1019 O ATOM 1947 CB GLN A 244 -133.664-196.098 161.210 1.00 83.89 C ANISOU 1947 CB GLN A 244 8595 9629 13649 -3466 337 -1168 C ATOM 1948 CG GLN A 244 -134.850-196.882 160.673 1.00 83.63 C ANISOU 1948 CG GLN A 244 8309 9661 13807 -3797 356 -1372 C ATOM 1949 CD GLN A 244 -135.420-196.300 159.391 1.00 91.95 C ANISOU 1949 CD GLN A 244 9094 11020 14822 -3713 159 -1655 C ATOM 1950 OE1 GLN A 244 -135.720-197.032 158.444 1.00 89.70 O ANISOU 1950 OE1 GLN A 244 8723 10691 14667 -3894 71 -1884 O ATOM 1951 NE2 GLN A 244 -135.578-194.979 159.354 1.00 86.90 N ANISOU 1951 NE2 GLN A 244 8319 10694 14005 -3437 86 -1644 N ATOM 1952 N LYS A 245 -130.427-196.194 161.344 1.00101.19 N ANISOU 1952 N LYS A 245 11500 11257 15690 -3003 209 -893 N ATOM 1953 CA LYS A 245 -129.182-195.729 161.948 1.00 97.04 C ANISOU 1953 CA LYS A 245 11216 10643 15012 -2754 202 -699 C ATOM 1954 C LYS A 245 -128.278-195.083 160.903 1.00 90.77 C ANISOU 1954 C LYS A 245 10480 9890 14118 -2500 10 -826 C ATOM 1955 O LYS A 245 -127.663-194.041 161.159 1.00 81.89 O ANISOU 1955 O LYS A 245 9406 8887 12820 -2265 -31 -745 O ATOM 1956 CB LYS A 245 -128.476-196.895 162.637 1.00106.96 C ANISOU 1956 CB LYS A 245 12735 11532 16374 -2847 298 -504 C ATOM 1957 CG LYS A 245 -127.658-196.516 163.859 1.00110.55 C ANISOU 1957 CG LYS A 245 13370 11974 16658 -2687 375 -227 C ATOM 1958 CD LYS A 245 -127.153-197.758 164.585 1.00120.19 C ANISOU 1958 CD LYS A 245 14825 12847 17996 -2799 476 2 C ATOM 1959 CE LYS A 245 -128.306-198.686 164.962 1.00131.46 C ANISOU 1959 CE LYS A 245 16158 14183 19607 -3147 634 56 C ATOM 1960 NZ LYS A 245 -127.839-199.960 165.582 1.00134.94 N ANISOU 1960 NZ LYS A 245 16841 14230 20200 -3266 726 301 N ATOM 1961 N ALA A 246 -128.205-195.680 159.710 1.00 85.30 N ANISOU 1961 N ALA A 246 9770 9111 13529 -2556 -105 -1035 N ATOM 1962 CA ALA A 246 -127.406-195.104 158.631 1.00 80.88 C ANISOU 1962 CA ALA A 246 9242 8635 12855 -2339 -280 -1160 C ATOM 1963 C ALA A 246 -128.005-193.795 158.130 1.00 99.06 C ANISOU 1963 C ALA A 246 11325 11299 15015 -2211 -375 -1230 C ATOM 1964 O ALA A 246 -127.273-192.838 157.849 1.00 98.05 O ANISOU 1964 O ALA A 246 11253 11270 14733 -1979 -466 -1187 O ATOM 1965 CB ALA A 246 -127.274-196.107 157.484 1.00 68.38 C ANISOU 1965 CB ALA A 246 7670 6910 11403 -2446 -369 -1397 C ATOM 1966 N GLU A 247 -129.332-193.734 158.002 1.00 97.78 N ANISOU 1966 N GLU A 247 10906 11333 14912 -2359 -356 -1333 N ATOM 1967 CA GLU A 247 -129.971-192.492 157.581 1.00 87.27 C ANISOU 1967 CA GLU A 247 9355 10338 13465 -2214 -448 -1381 C ATOM 1968 C GLU A 247 -129.676-191.363 158.561 1.00 77.74 C ANISOU 1968 C GLU A 247 8205 9193 12139 -2014 -385 -1190 C ATOM 1969 O GLU A 247 -129.380-190.236 158.147 1.00 76.98 O ANISOU 1969 O GLU A 247 8088 9235 11925 -1789 -492 -1175 O ATOM 1970 CB GLU A 247 -131.479-192.705 157.428 1.00 88.74 C ANISOU 1970 CB GLU A 247 9235 10733 13748 -2412 -422 -1519 C ATOM 1971 CG GLU A 247 -132.266-191.436 157.154 1.00 95.80 C ANISOU 1971 CG GLU A 247 9877 11976 14546 -2244 -504 -1548 C ATOM 1972 CD GLU A 247 -132.782-190.791 158.424 1.00103.71 C ANISOU 1972 CD GLU A 247 10809 13061 15536 -2201 -352 -1412 C ATOM 1973 OE1 GLU A 247 -133.397-191.506 159.243 1.00116.45 O ANISOU 1973 OE1 GLU A 247 12365 14633 17247 -2429 -186 -1388 O ATOM 1974 OE2 GLU A 247 -132.555-189.575 158.609 1.00 95.43 O ANISOU 1974 OE2 GLU A 247 9764 12115 14380 -1947 -392 -1332 O ATOM 1975 N LYS A 248 -129.739-191.648 159.866 1.00 73.69 N ANISOU 1975 N LYS A 248 7767 8577 11653 -2099 -210 -1043 N ATOM 1976 CA LYS A 248 -129.487-190.609 160.859 1.00 79.13 C ANISOU 1976 CA LYS A 248 8501 9345 12221 -1924 -142 -900 C ATOM 1977 C LYS A 248 -128.054-190.093 160.773 1.00 81.30 C ANISOU 1977 C LYS A 248 9010 9501 12381 -1708 -223 -815 C ATOM 1978 O LYS A 248 -127.811-188.892 160.935 1.00 78.71 O ANISOU 1978 O LYS A 248 8674 9281 11952 -1510 -260 -781 O ATOM 1979 CB LYS A 248 -129.791-191.130 162.267 1.00 85.86 C ANISOU 1979 CB LYS A 248 9389 10143 13091 -2076 66 -759 C ATOM 1980 CG LYS A 248 -131.274-191.128 162.632 1.00105.72 C ANISOU 1980 CG LYS A 248 11622 12880 15669 -2237 176 -822 C ATOM 1981 CD LYS A 248 -131.498-191.380 164.123 1.00126.31 C ANISOU 1981 CD LYS A 248 14262 15499 18232 -2350 394 -656 C ATOM 1982 CE LYS A 248 -130.930-190.248 164.976 1.00139.82 C ANISOU 1982 CE LYS A 248 16053 17307 19766 -2110 424 -571 C ATOM 1983 NZ LYS A 248 -131.187-190.448 166.433 1.00146.60 N ANISOU 1983 NZ LYS A 248 16921 18244 20536 -2215 637 -424 N ATOM 1984 N GLU A 249 -127.091-190.979 160.506 1.00 83.08 N ANISOU 1984 N GLU A 249 9435 9498 12632 -1743 -250 -790 N ATOM 1985 CA GLU A 249 -125.701-190.534 160.480 1.00 89.06 C ANISOU 1985 CA GLU A 249 10395 10167 13278 -1549 -317 -711 C ATOM 1986 C GLU A 249 -125.339-189.857 159.161 1.00 86.06 C ANISOU 1986 C GLU A 249 9971 9893 12836 -1409 -490 -819 C ATOM 1987 O GLU A 249 -124.490-188.957 159.147 1.00 77.48 O ANISOU 1987 O GLU A 249 8971 8832 11638 -1232 -544 -755 O ATOM 1988 CB GLU A 249 -124.756-191.705 160.775 1.00 95.84 C ANISOU 1988 CB GLU A 249 11473 10755 14186 -1606 -277 -633 C ATOM 1989 CG GLU A 249 -124.678-192.772 159.703 1.00123.95 C ANISOU 1989 CG GLU A 249 15049 14175 17870 -1708 -348 -782 C ATOM 1990 CD GLU A 249 -123.880-193.985 160.151 1.00143.24 C ANISOU 1990 CD GLU A 249 17706 16312 20408 -1758 -290 -694 C ATOM 1991 OE1 GLU A 249 -123.859-194.267 161.369 1.00147.60 O ANISOU 1991 OE1 GLU A 249 18347 16770 20963 -1803 -164 -500 O ATOM 1992 OE2 GLU A 249 -123.270-194.652 159.288 1.00149.22 O ANISOU 1992 OE2 GLU A 249 18536 16931 21229 -1740 -370 -816 O ATOM 1993 N VAL A 250 -125.973-190.250 158.054 1.00 73.95 N ANISOU 1993 N VAL A 250 8297 8440 11361 -1495 -576 -980 N ATOM 1994 CA VAL A 250 -125.794-189.516 156.802 1.00 77.35 C ANISOU 1994 CA VAL A 250 8655 9038 11698 -1364 -740 -1060 C ATOM 1995 C VAL A 250 -126.331-188.096 156.943 1.00 83.92 C ANISOU 1995 C VAL A 250 9357 10062 12466 -1215 -771 -997 C ATOM 1996 O VAL A 250 -125.660-187.122 156.579 1.00 85.00 O ANISOU 1996 O VAL A 250 9551 10242 12503 -1041 -853 -930 O ATOM 1997 CB VAL A 250 -126.468-190.256 155.633 1.00 79.43 C ANISOU 1997 CB VAL A 250 8768 9395 12016 -1498 -828 -1263 C ATOM 1998 CG1 VAL A 250 -126.530-189.354 154.407 1.00 76.16 C ANISOU 1998 CG1 VAL A 250 8233 9233 11470 -1359 -997 -1314 C ATOM 1999 CG2 VAL A 250 -125.718-191.532 155.309 1.00 79.38 C ANISOU 1999 CG2 VAL A 250 8914 9171 12074 -1598 -821 -1355 C ATOM 2000 N THR A 251 -127.547-187.958 157.478 1.00 73.71 N ANISOU 2000 N THR A 251 7883 8879 11245 -1282 -700 -1019 N ATOM 2001 CA THR A 251 -128.122-186.635 157.694 1.00 69.09 C ANISOU 2001 CA THR A 251 7164 8457 10631 -1120 -720 -978 C ATOM 2002 C THR A 251 -127.251-185.812 158.630 1.00 73.94 C ANISOU 2002 C THR A 251 7950 8959 11183 -976 -657 -846 C ATOM 2003 O THR A 251 -126.978-184.635 158.371 1.00 76.15 O ANISOU 2003 O THR A 251 8235 9281 11417 -792 -735 -800 O ATOM 2004 CB THR A 251 -129.534-186.764 158.265 1.00 62.95 C ANISOU 2004 CB THR A 251 6154 7820 9945 -1226 -624 -1040 C ATOM 2005 OG1 THR A 251 -130.342-187.549 157.381 1.00 75.19 O ANISOU 2005 OG1 THR A 251 7526 9487 11558 -1384 -689 -1185 O ATOM 2006 CG2 THR A 251 -130.166-185.386 158.453 1.00 62.77 C ANISOU 2006 CG2 THR A 251 5974 7962 9914 -1025 -650 -1023 C ATOM 2007 N ARG A 252 -126.816-186.420 159.735 1.00 72.95 N ANISOU 2007 N ARG A 252 7965 8694 11059 -1063 -519 -782 N ATOM 2008 CA ARG A 252 -126.000-185.708 160.711 1.00 71.97 C ANISOU 2008 CA ARG A 252 7989 8497 10858 -946 -458 -682 C ATOM 2009 C ARG A 252 -124.684-185.240 160.096 1.00 80.24 C ANISOU 2009 C ARG A 252 9201 9460 11826 -819 -570 -635 C ATOM 2010 O ARG A 252 -124.198-184.145 160.409 1.00 73.57 O ANISOU 2010 O ARG A 252 8408 8612 10933 -679 -584 -590 O ATOM 2011 CB ARG A 252 -125.758-186.604 161.926 1.00 81.91 C ANISOU 2011 CB ARG A 252 9363 9653 12105 -1073 -303 -605 C ATOM 2012 CG ARG A 252 -124.591-186.196 162.807 1.00102.31 C ANISOU 2012 CG ARG A 252 12137 12157 14578 -974 -266 -504 C ATOM 2013 CD ARG A 252 -124.467-187.127 164.008 1.00129.21 C ANISOU 2013 CD ARG A 252 15640 15501 17954 -1096 -120 -399 C ATOM 2014 NE ARG A 252 -123.172-187.014 164.676 1.00141.20 N ANISOU 2014 NE ARG A 252 17352 16945 19355 -1010 -117 -300 N ATOM 2015 CZ ARG A 252 -122.183-187.894 164.547 1.00140.96 C ANISOU 2015 CZ ARG A 252 17484 16758 19314 -1025 -150 -221 C ATOM 2016 NH1 ARG A 252 -121.037-187.712 165.190 1.00136.40 N ANISOU 2016 NH1 ARG A 252 17051 16156 18619 -933 -155 -137 N ATOM 2017 NH2 ARG A 252 -122.340-188.963 163.779 1.00141.77 N ANISOU 2017 NH2 ARG A 252 17597 16737 19533 -1127 -180 -244 N ATOM 2018 N MET A 253 -124.109-186.044 159.195 1.00 69.31 N ANISOU 2018 N MET A 253 7888 8013 10435 -873 -646 -661 N ATOM 2019 CA MET A 253 -122.844-185.673 158.566 1.00 61.93 C ANISOU 2019 CA MET A 253 7086 7032 9411 -768 -740 -622 C ATOM 2020 C MET A 253 -123.035-184.583 157.520 1.00 75.72 C ANISOU 2020 C MET A 253 8738 8911 11123 -651 -869 -625 C ATOM 2021 O MET A 253 -122.191-183.690 157.390 1.00 74.34 O ANISOU 2021 O MET A 253 8648 8713 10884 -539 -915 -550 O ATOM 2022 CB MET A 253 -122.185-186.899 157.934 1.00 64.68 C ANISOU 2022 CB MET A 253 7525 7290 9760 -849 -771 -673 C ATOM 2023 CG MET A 253 -121.291-187.680 158.884 1.00 84.68 C ANISOU 2023 CG MET A 253 10235 9648 12293 -878 -681 -602 C ATOM 2024 SD MET A 253 -119.937-186.662 159.522 1.00106.51 S ANISOU 2024 SD MET A 253 13138 12398 14932 -724 -685 -488 S ATOM 2025 CE MET A 253 -119.310-187.692 160.847 1.00112.98 C ANISOU 2025 CE MET A 253 14112 13066 15750 -768 -572 -391 C ATOM 2026 N VAL A 254 -124.121-184.651 156.746 1.00 68.90 N ANISOU 2026 N VAL A 254 7691 8188 10299 -680 -934 -700 N ATOM 2027 CA VAL A 254 -124.397-183.594 155.776 1.00 66.47 C ANISOU 2027 CA VAL A 254 7282 8022 9951 -551 -1065 -667 C ATOM 2028 C VAL A 254 -124.599-182.265 156.494 1.00 74.13 C ANISOU 2028 C VAL A 254 8241 8963 10963 -407 -1036 -584 C ATOM 2029 O VAL A 254 -124.092-181.223 156.061 1.00 75.16 O ANISOU 2029 O VAL A 254 8420 9079 11059 -279 -1113 -489 O ATOM 2030 CB VAL A 254 -125.608-183.964 154.900 1.00 66.23 C ANISOU 2030 CB VAL A 254 7031 8187 9947 -605 -1145 -771 C ATOM 2031 CG1 VAL A 254 -126.107-182.744 154.136 1.00 65.53 C ANISOU 2031 CG1 VAL A 254 6813 8256 9828 -439 -1275 -698 C ATOM 2032 CG2 VAL A 254 -125.240-185.078 153.934 1.00 65.23 C ANISOU 2032 CG2 VAL A 254 6925 8098 9763 -724 -1206 -879 C ATOM 2033 N ILE A 255 -125.324-182.285 157.614 1.00 72.50 N ANISOU 2033 N ILE A 255 7970 8742 10836 -431 -917 -624 N ATOM 2034 CA ILE A 255 -125.516-181.070 158.401 1.00 71.98 C ANISOU 2034 CA ILE A 255 7890 8641 10818 -292 -873 -593 C ATOM 2035 C ILE A 255 -124.174-180.511 158.852 1.00 79.52 C ANISOU 2035 C ILE A 255 9056 9441 11718 -239 -854 -519 C ATOM 2036 O ILE A 255 -123.931-179.302 158.781 1.00 73.58 O ANISOU 2036 O ILE A 255 8330 8632 10995 -105 -900 -470 O ATOM 2037 CB ILE A 255 -126.441-181.346 159.600 1.00 67.49 C ANISOU 2037 CB ILE A 255 7214 8119 10309 -350 -723 -670 C ATOM 2038 CG1 ILE A 255 -127.873-181.627 159.131 1.00 74.71 C ANISOU 2038 CG1 ILE A 255 7871 9219 11296 -384 -749 -752 C ATOM 2039 CG2 ILE A 255 -126.406-180.185 160.585 1.00 67.68 C ANISOU 2039 CG2 ILE A 255 7259 8093 10365 -212 -654 -677 C ATOM 2040 CD1 ILE A 255 -128.852-181.863 160.265 1.00 76.80 C ANISOU 2040 CD1 ILE A 255 7996 9569 11614 -453 -590 -828 C ATOM 2041 N ILE A 256 -123.279-181.384 159.320 1.00 72.98 N ANISOU 2041 N ILE A 256 8374 8534 10820 -345 -791 -511 N ATOM 2042 CA ILE A 256 -121.962-180.943 159.771 1.00 64.04 C ANISOU 2042 CA ILE A 256 7419 7289 9622 -308 -778 -455 C ATOM 2043 C ILE A 256 -121.200-180.280 158.629 1.00 72.29 C ANISOU 2043 C ILE A 256 8515 8320 10631 -241 -905 -383 C ATOM 2044 O ILE A 256 -120.569-179.231 158.806 1.00 68.89 O ANISOU 2044 O ILE A 256 8157 7813 10205 -166 -920 -335 O ATOM 2045 CB ILE A 256 -121.176-182.128 160.361 1.00 73.91 C ANISOU 2045 CB ILE A 256 8796 8484 10804 -416 -707 -447 C ATOM 2046 CG1 ILE A 256 -121.729-182.514 161.736 1.00 69.70 C ANISOU 2046 CG1 ILE A 256 8243 7962 10277 -474 -565 -469 C ATOM 2047 CG2 ILE A 256 -119.683-181.815 160.448 1.00 64.68 C ANISOU 2047 CG2 ILE A 256 7783 7242 9549 -379 -735 -393 C ATOM 2048 CD1 ILE A 256 -121.089-183.759 162.309 1.00 68.36 C ANISOU 2048 CD1 ILE A 256 8194 7729 10052 -573 -500 -420 C ATOM 2049 N MET A 257 -121.256-180.874 157.439 1.00 68.03 N ANISOU 2049 N MET A 257 7933 7863 10050 -278 -993 -379 N ATOM 2050 CA MET A 257 -120.468-180.363 156.325 1.00 66.90 C ANISOU 2050 CA MET A 257 7836 7749 9833 -235 -1101 -297 C ATOM 2051 C MET A 257 -121.038-179.061 155.789 1.00 77.40 C ANISOU 2051 C MET A 257 9088 9105 11216 -113 -1182 -210 C ATOM 2052 O MET A 257 -120.284-178.143 155.448 1.00 70.34 O ANISOU 2052 O MET A 257 8272 8152 10301 -60 -1227 -101 O ATOM 2053 CB MET A 257 -120.397-181.412 155.225 1.00 58.27 C ANISOU 2053 CB MET A 257 6708 6773 8659 -309 -1165 -346 C ATOM 2054 CG MET A 257 -119.558-182.617 155.621 1.00 73.08 C ANISOU 2054 CG MET A 257 8692 8576 10497 -399 -1099 -412 C ATOM 2055 SD MET A 257 -119.892-184.014 154.544 1.00 91.07 S ANISOU 2055 SD MET A 257 10900 10956 12747 -497 -1151 -547 S ATOM 2056 CE MET A 257 -119.954-183.149 152.998 1.00 90.68 C ANISOU 2056 CE MET A 257 10757 11117 12579 -426 -1298 -490 C ATOM 2057 N VAL A 258 -122.365-178.963 155.706 1.00 68.85 N ANISOU 2057 N VAL A 258 7843 8105 10212 -66 -1204 -248 N ATOM 2058 CA VAL A 258 -122.984-177.729 155.240 1.00 65.56 C ANISOU 2058 CA VAL A 258 7342 7701 9868 85 -1289 -155 C ATOM 2059 C VAL A 258 -122.715-176.594 156.223 1.00 73.72 C ANISOU 2059 C VAL A 258 8458 8541 11013 176 -1224 -134 C ATOM 2060 O VAL A 258 -122.422-175.462 155.819 1.00 69.95 O ANISOU 2060 O VAL A 258 8026 7967 10584 276 -1289 -11 O ATOM 2061 CB VAL A 258 -124.490-177.948 155.007 1.00 73.24 C ANISOU 2061 CB VAL A 258 8093 8834 10902 125 -1326 -223 C ATOM 2062 CG1 VAL A 258 -125.172-176.629 154.708 1.00 72.71 C ANISOU 2062 CG1 VAL A 258 7931 8757 10937 321 -1410 -124 C ATOM 2063 CG2 VAL A 258 -124.708-178.940 153.871 1.00 76.63 C ANISOU 2063 CG2 VAL A 258 8434 9466 11215 31 -1415 -260 C ATOM 2064 N ILE A 259 -122.799-176.876 157.527 1.00 73.74 N ANISOU 2064 N ILE A 259 8481 8481 11055 134 -1093 -253 N ATOM 2065 CA ILE A 259 -122.535-175.843 158.525 1.00 74.83 C ANISOU 2065 CA ILE A 259 8689 8458 11284 210 -1025 -284 C ATOM 2066 C ILE A 259 -121.075-175.405 158.466 1.00 79.08 C ANISOU 2066 C ILE A 259 9410 8868 11770 169 -1039 -209 C ATOM 2067 O ILE A 259 -120.767-174.211 158.578 1.00 71.28 O ANISOU 2067 O ILE A 259 8479 7725 10878 246 -1056 -171 O ATOM 2068 CB ILE A 259 -122.930-176.337 159.931 1.00 80.82 C ANISOU 2068 CB ILE A 259 9419 9243 12047 161 -877 -433 C ATOM 2069 CG1 ILE A 259 -124.456-176.416 160.069 1.00 86.20 C ANISOU 2069 CG1 ILE A 259 9890 10049 12814 221 -851 -513 C ATOM 2070 CG2 ILE A 259 -122.341-175.425 161.013 1.00 74.93 C ANISOU 2070 CG2 ILE A 259 8772 8356 11341 205 -803 -499 C ATOM 2071 CD1 ILE A 259 -124.921-176.895 161.434 1.00 89.30 C ANISOU 2071 CD1 ILE A 259 10233 10506 13191 158 -690 -645 C ATOM 2072 N ALA A 260 -120.156-176.355 158.280 1.00 70.98 N ANISOU 2072 N ALA A 260 8468 7895 10605 45 -1031 -195 N ATOM 2073 CA ALA A 260 -118.745-175.998 158.149 1.00 70.50 C ANISOU 2073 CA ALA A 260 8548 7756 10482 -2 -1047 -130 C ATOM 2074 C ALA A 260 -118.511-175.112 156.934 1.00 78.62 C ANISOU 2074 C ALA A 260 9586 8758 11529 45 -1156 29 C ATOM 2075 O ALA A 260 -117.748-174.141 157.000 1.00 82.90 O ANISOU 2075 O ALA A 260 10216 9165 12116 46 -1161 93 O ATOM 2076 CB ALA A 260 -117.887-177.260 158.059 1.00 57.10 C ANISOU 2076 CB ALA A 260 6910 6146 8639 -114 -1028 -149 C ATOM 2077 N PHE A 261 -119.167-175.427 155.816 1.00 65.09 N ANISOU 2077 N PHE A 261 7776 7181 9773 75 -1244 100 N ATOM 2078 CA PHE A 261 -119.027-174.597 154.626 1.00 65.63 C ANISOU 2078 CA PHE A 261 7844 7261 9830 126 -1352 287 C ATOM 2079 C PHE A 261 -119.609-173.205 154.852 1.00 77.72 C ANISOU 2079 C PHE A 261 9367 8611 11553 265 -1376 362 C ATOM 2080 O PHE A 261 -119.050-172.211 154.375 1.00 68.06 O ANISOU 2080 O PHE A 261 8221 7266 10372 284 -1421 525 O ATOM 2081 CB PHE A 261 -119.694-175.277 153.431 1.00 62.16 C ANISOU 2081 CB PHE A 261 7283 7055 9279 135 -1449 325 C ATOM 2082 CG PHE A 261 -119.546-174.519 152.145 1.00 76.24 C ANISOU 2082 CG PHE A 261 9060 8909 11000 185 -1566 544 C ATOM 2083 CD1 PHE A 261 -118.433-174.702 151.342 1.00 83.14 C ANISOU 2083 CD1 PHE A 261 10004 9882 11703 90 -1586 634 C ATOM 2084 CD2 PHE A 261 -120.522-173.625 151.739 1.00 71.61 C ANISOU 2084 CD2 PHE A 261 8387 8305 10514 335 -1654 670 C ATOM 2085 CE1 PHE A 261 -118.296-174.004 150.157 1.00 84.63 C ANISOU 2085 CE1 PHE A 261 10184 10165 11806 122 -1685 862 C ATOM 2086 CE2 PHE A 261 -120.388-172.925 150.557 1.00 84.99 C ANISOU 2086 CE2 PHE A 261 10082 10071 12137 386 -1766 914 C ATOM 2087 CZ PHE A 261 -119.276-173.115 149.765 1.00 85.14 C ANISOU 2087 CZ PHE A 261 10179 10203 11968 269 -1778 1018 C ATOM 2088 N LEU A 262 -120.720-173.111 155.588 1.00 74.95 N ANISOU 2088 N LEU A 262 8918 8231 11330 362 -1339 243 N ATOM 2089 CA LEU A 262 -121.320-171.806 155.844 1.00 81.55 C ANISOU 2089 CA LEU A 262 9733 8879 12373 524 -1359 281 C ATOM 2090 C LEU A 262 -120.486-170.979 156.817 1.00 80.01 C ANISOU 2090 C LEU A 262 9679 8434 12287 497 -1276 215 C ATOM 2091 O LEU A 262 -120.507-169.745 156.750 1.00 75.82 O ANISOU 2091 O LEU A 262 9193 7682 11932 597 -1308 295 O ATOM 2092 CB LEU A 262 -122.746-171.972 156.374 1.00 78.09 C ANISOU 2092 CB LEU A 262 9122 8518 12032 640 -1332 142 C ATOM 2093 CG LEU A 262 -123.799-172.436 155.362 1.00 83.40 C ANISOU 2093 CG LEU A 262 9615 9422 12652 705 -1441 208 C ATOM 2094 CD1 LEU A 262 -125.108-172.781 156.057 1.00 85.98 C ANISOU 2094 CD1 LEU A 262 9752 9857 13059 773 -1384 31 C ATOM 2095 CD2 LEU A 262 -124.024-171.373 154.296 1.00 79.80 C ANISOU 2095 CD2 LEU A 262 9142 8914 12265 863 -1584 440 C ATOM 2096 N ILE A 263 -119.751-171.631 157.723 1.00 76.95 N ANISOU 2096 N ILE A 263 9360 8073 11806 365 -1175 69 N ATOM 2097 CA ILE A 263 -118.914-170.901 158.675 1.00 81.67 C ANISOU 2097 CA ILE A 263 10073 8478 12479 322 -1103 -24 C ATOM 2098 C ILE A 263 -117.807-170.143 157.950 1.00 81.66 C ANISOU 2098 C ILE A 263 10192 8343 12493 253 -1159 146 C ATOM 2099 O ILE A 263 -117.416-169.042 158.366 1.00 72.77 O ANISOU 2099 O ILE A 263 9144 6980 11524 259 -1140 124 O ATOM 2100 CB ILE A 263 -118.346-171.873 159.731 1.00 83.39 C ANISOU 2100 CB ILE A 263 10324 8811 12551 200 -1001 -189 C ATOM 2101 CG1 ILE A 263 -119.431-172.267 160.735 1.00 83.28 C ANISOU 2101 CG1 ILE A 263 10204 8876 12561 262 -914 -363 C ATOM 2102 CG2 ILE A 263 -117.154-171.264 160.456 1.00 75.89 C ANISOU 2102 CG2 ILE A 263 9493 7731 11611 114 -956 -261 C ATOM 2103 CD1 ILE A 263 -118.982-173.293 161.741 1.00 86.22 C ANISOU 2103 CD1 ILE A 263 10606 9380 12775 150 -818 -477 C ATOM 2104 N CYS A 264 -117.294-170.709 156.854 1.00 74.55 N ANISOU 2104 N CYS A 264 9299 7593 11432 175 -1222 307 N ATOM 2105 CA CYS A 264 -116.314-170.034 156.017 1.00 78.62 C ANISOU 2105 CA CYS A 264 9904 8032 11935 97 -1270 502 C ATOM 2106 C CYS A 264 -116.950-169.087 155.000 1.00 85.08 C ANISOU 2106 C CYS A 264 10705 8752 12870 216 -1370 736 C ATOM 2107 O CYS A 264 -116.367-168.040 154.691 1.00 84.06 O ANISOU 2107 O CYS A 264 10668 8423 12848 183 -1389 890 O ATOM 2108 CB CYS A 264 -115.467-171.084 155.293 1.00 77.39 C ANISOU 2108 CB CYS A 264 9749 8122 11534 -31 -1283 556 C ATOM 2109 SG CYS A 264 -114.255-170.435 154.127 1.00 97.80 S ANISOU 2109 SG CYS A 264 12407 10711 14042 -150 -1328 807 S ATOM 2110 N TRP A 265 -118.155-169.404 154.516 1.00 77.25 N ANISOU 2110 N TRP A 265 9592 7890 11871 354 -1436 771 N ATOM 2111 CA TRP A 265 -118.769-168.654 153.426 1.00 65.91 C ANISOU 2111 CA TRP A 265 8118 6428 10497 483 -1555 1025 C ATOM 2112 C TRP A 265 -119.425-167.371 153.923 1.00 81.86 C ANISOU 2112 C TRP A 265 10154 8130 12818 655 -1563 1038 C ATOM 2113 O TRP A 265 -119.271-166.312 153.307 1.00 77.71 O ANISOU 2113 O TRP A 265 9700 7410 12417 708 -1627 1277 O ATOM 2114 CB TRP A 265 -119.785-169.551 152.717 1.00 67.10 C ANISOU 2114 CB TRP A 265 8105 6883 10505 559 -1634 1031 C ATOM 2115 CG TRP A 265 -120.376-169.001 151.452 1.00 66.49 C ANISOU 2115 CG TRP A 265 7965 6887 10412 687 -1777 1305 C ATOM 2116 CD1 TRP A 265 -119.917-169.192 150.180 1.00 72.65 C ANISOU 2116 CD1 TRP A 265 8749 7879 10977 619 -1860 1522 C ATOM 2117 CD2 TRP A 265 -121.570-168.211 151.333 1.00 63.85 C ANISOU 2117 CD2 TRP A 265 7535 6460 10263 918 -1861 1393 C ATOM 2118 NE1 TRP A 265 -120.738-168.551 149.276 1.00 75.40 N ANISOU 2118 NE1 TRP A 265 9019 8279 11350 789 -1996 1762 N ATOM 2119 CE2 TRP A 265 -121.759-167.944 149.959 1.00 65.16 C ANISOU 2119 CE2 TRP A 265 7659 6788 10310 983 -2004 1692 C ATOM 2120 CE3 TRP A 265 -122.489-167.694 152.253 1.00 70.64 C ANISOU 2120 CE3 TRP A 265 8331 7137 11372 1089 -1829 1245 C ATOM 2121 CZ2 TRP A 265 -122.826-167.186 149.488 1.00 68.17 C ANISOU 2121 CZ2 TRP A 265 7940 7140 10820 1222 -2128 1865 C ATOM 2122 CZ3 TRP A 265 -123.549-166.940 151.777 1.00 72.18 C ANISOU 2122 CZ3 TRP A 265 8420 7294 11711 1332 -1944 1394 C ATOM 2123 CH2 TRP A 265 -123.707-166.694 150.409 1.00 76.30 C ANISOU 2123 CH2 TRP A 265 8906 7967 12118 1402 -2098 1711 C ATOM 2124 N LEU A 266 -120.172-167.452 155.026 1.00 80.12 N ANISOU 2124 N LEU A 266 9865 7855 12721 748 -1494 786 N ATOM 2125 CA LEU A 266 -120.961-166.310 155.487 1.00 83.11 C ANISOU 2125 CA LEU A 266 10225 7961 13392 950 -1501 753 C ATOM 2126 C LEU A 266 -120.140-165.079 155.867 1.00 86.73 C ANISOU 2126 C LEU A 266 10852 8036 14066 913 -1466 780 C ATOM 2127 O LEU A 266 -120.611-163.959 155.595 1.00 75.20 O ANISOU 2127 O LEU A 266 9412 6308 12853 1083 -1527 911 O ATOM 2128 CB LEU A 266 -121.847-166.744 156.662 1.00 84.32 C ANISOU 2128 CB LEU A 266 10256 8187 13595 1030 -1410 441 C ATOM 2129 CG LEU A 266 -123.063-167.595 156.283 1.00 87.67 C ANISOU 2129 CG LEU A 266 10476 8915 13920 1126 -1457 422 C ATOM 2130 CD1 LEU A 266 -123.747-168.165 157.520 1.00 77.19 C ANISOU 2130 CD1 LEU A 266 9035 7693 12601 1138 -1334 118 C ATOM 2131 CD2 LEU A 266 -124.048-166.787 155.443 1.00 76.21 C ANISOU 2131 CD2 LEU A 266 8921 7412 12621 1369 -1591 612 C ATOM 2132 N PRO A 267 -118.964-165.185 156.505 1.00 81.09 N ANISOU 2132 N PRO A 267 10253 7265 13294 708 -1375 655 N ATOM 2133 CA PRO A 267 -118.184-163.962 156.770 1.00 65.00 C ANISOU 2133 CA PRO A 267 8365 4857 11477 647 -1350 681 C ATOM 2134 C PRO A 267 -117.942-163.110 155.531 1.00 71.07 C ANISOU 2134 C PRO A 267 9214 5452 12337 660 -1450 1058 C ATOM 2135 O PRO A 267 -118.114-161.885 155.592 1.00 70.96 O ANISOU 2135 O PRO A 267 9275 5062 12624 759 -1469 1126 O ATOM 2136 CB PRO A 267 -116.883-164.513 157.365 1.00 77.76 C ANISOU 2136 CB PRO A 267 10051 6574 12920 394 -1263 532 C ATOM 2137 CG PRO A 267 -117.310-165.759 158.057 1.00 70.28 C ANISOU 2137 CG PRO A 267 8996 5930 11777 402 -1206 308 C ATOM 2138 CD PRO A 267 -118.367-166.358 157.172 1.00 75.73 C ANISOU 2138 CD PRO A 267 9563 6829 12382 538 -1288 454 C ATOM 2139 N TYR A 268 -117.580-163.719 154.397 1.00 71.70 N ANISOU 2139 N TYR A 268 9279 5797 12168 569 -1513 1307 N ATOM 2140 CA TYR A 268 -117.450-162.947 153.162 1.00 75.79 C ANISOU 2140 CA TYR A 268 9859 6208 12732 589 -1611 1703 C ATOM 2141 C TYR A 268 -118.764-162.274 152.790 1.00 81.40 C ANISOU 2141 C TYR A 268 10503 6780 13643 883 -1714 1848 C ATOM 2142 O TYR A 268 -118.781-161.095 152.421 1.00 83.33 O ANISOU 2142 O TYR A 268 10844 6689 14131 963 -1764 2085 O ATOM 2143 CB TYR A 268 -116.975-163.844 152.017 1.00 78.91 C ANISOU 2143 CB TYR A 268 10213 6995 12775 463 -1659 1905 C ATOM 2144 CG TYR A 268 -115.571-164.366 152.196 1.00 87.29 C ANISOU 2144 CG TYR A 268 11337 8177 13654 189 -1568 1818 C ATOM 2145 CD1 TYR A 268 -115.345-165.624 152.736 1.00 81.62 C ANISOU 2145 CD1 TYR A 268 10549 7734 12728 113 -1508 1550 C ATOM 2146 CD2 TYR A 268 -114.472-163.599 151.828 1.00 83.00 C ANISOU 2146 CD2 TYR A 268 10913 7468 13156 9 -1543 2013 C ATOM 2147 CE1 TYR A 268 -114.064-166.106 152.903 1.00 88.49 C ANISOU 2147 CE1 TYR A 268 11460 8723 13439 -106 -1436 1473 C ATOM 2148 CE2 TYR A 268 -113.189-164.074 151.987 1.00 81.92 C ANISOU 2148 CE2 TYR A 268 10801 7473 12850 -233 -1463 1923 C ATOM 2149 CZ TYR A 268 -112.989-165.329 152.525 1.00 84.00 C ANISOU 2149 CZ TYR A 268 10988 8022 12907 -274 -1415 1649 C ATOM 2150 OH TYR A 268 -111.710-165.812 152.691 1.00 79.87 O ANISOU 2150 OH TYR A 268 10475 7649 12223 -484 -1345 1559 O ATOM 2151 N ALA A 269 -119.878-163.000 152.904 1.00 81.62 N ANISOU 2151 N ALA A 269 10363 7059 13591 1049 -1748 1711 N ATOM 2152 CA ALA A 269 -121.175-162.420 152.570 1.00 81.31 C ANISOU 2152 CA ALA A 269 10221 6940 13733 1349 -1854 1827 C ATOM 2153 C ALA A 269 -121.521-161.272 153.507 1.00 76.31 C ANISOU 2153 C ALA A 269 9644 5855 13494 1508 -1808 1678 C ATOM 2154 O ALA A 269 -122.030-160.235 153.068 1.00 79.93 O ANISOU 2154 O ALA A 269 10127 6040 14201 1717 -1897 1899 O ATOM 2155 CB ALA A 269 -122.258-163.499 152.615 1.00 84.99 C ANISOU 2155 CB ALA A 269 10469 7792 14030 1457 -1882 1657 C ATOM 2156 N GLY A 270 -121.248-161.436 154.802 1.00 83.71 N ANISOU 2156 N GLY A 270 10601 6711 14493 1422 -1671 1301 N ATOM 2157 CA GLY A 270 -121.512-160.359 155.743 1.00 85.16 C ANISOU 2157 CA GLY A 270 10836 6480 15040 1559 -1615 1101 C ATOM 2158 C GLY A 270 -120.648-159.137 155.495 1.00 95.45 C ANISOU 2158 C GLY A 270 12346 7329 16591 1478 -1624 1292 C ATOM 2159 O GLY A 270 -121.140-158.006 155.494 1.00 96.45 O ANISOU 2159 O GLY A 270 12517 7063 17067 1684 -1666 1362 O ATOM 2160 N VAL A 271 -119.348-159.344 155.278 1.00 92.30 N ANISOU 2160 N VAL A 271 12071 6967 16032 1175 -1582 1380 N ATOM 2161 CA VAL A 271 -118.467-158.202 155.050 1.00101.59 C ANISOU 2161 CA VAL A 271 13437 7717 17445 1049 -1577 1563 C ATOM 2162 C VAL A 271 -118.784-157.542 153.713 1.00 95.30 C ANISOU 2162 C VAL A 271 12686 6791 16734 1175 -1710 2059 C ATOM 2163 O VAL A 271 -118.835-156.310 153.613 1.00 93.21 O ANISOU 2163 O VAL A 271 12540 6049 16825 1266 -1738 2215 O ATOM 2164 CB VAL A 271 -116.989-158.621 155.145 1.00 95.72 C ANISOU 2164 CB VAL A 271 12781 7096 16492 685 -1495 1527 C ATOM 2165 CG1 VAL A 271 -116.091-157.517 154.595 1.00 81.94 C ANISOU 2165 CG1 VAL A 271 11213 4974 14949 521 -1502 1812 C ATOM 2166 CG2 VAL A 271 -116.631-158.920 156.590 1.00 76.90 C ANISOU 2166 CG2 VAL A 271 10382 4728 14107 583 -1372 1050 C ATOM 2167 N ALA A 272 -119.011-158.343 152.669 1.00 86.67 N ANISOU 2167 N ALA A 272 11498 6117 15317 1187 -1798 2317 N ATOM 2168 CA ALA A 272 -119.387-157.763 151.383 1.00 88.33 C ANISOU 2168 CA ALA A 272 11730 6273 15558 1327 -1938 2803 C ATOM 2169 C ALA A 272 -120.712-157.022 151.487 1.00104.69 C ANISOU 2169 C ALA A 272 13735 8097 17947 1709 -2028 2829 C ATOM 2170 O ALA A 272 -120.892-155.967 150.867 1.00103.02 O ANISOU 2170 O ALA A 272 13617 7547 17978 1849 -2115 3183 O ATOM 2171 CB ALA A 272 -119.461-158.846 150.307 1.00 88.36 C ANISOU 2171 CB ALA A 272 11614 6838 15122 1278 -2017 3005 C ATOM 2172 N PHE A 273 -121.649-157.551 152.277 1.00108.91 N ANISOU 2172 N PHE A 273 14100 8791 18488 1887 -2004 2466 N ATOM 2173 CA PHE A 273 -122.907-156.843 152.490 1.00105.78 C ANISOU 2173 CA PHE A 273 13611 8172 18408 2264 -2075 2434 C ATOM 2174 C PHE A 273 -122.676-155.523 153.214 1.00108.17 C ANISOU 2174 C PHE A 273 14079 7843 19180 2329 -2014 2329 C ATOM 2175 O PHE A 273 -123.285-154.507 152.865 1.00104.50 O ANISOU 2175 O PHE A 273 13648 7085 18971 2580 -2082 2521 O ATOM 2176 CB PHE A 273 -123.890-157.717 153.268 1.00106.40 C ANISOU 2176 CB PHE A 273 13461 8584 18385 2400 -2033 2034 C ATOM 2177 CG PHE A 273 -125.218-157.059 153.511 1.00113.55 C ANISOU 2177 CG PHE A 273 14226 9322 19594 2798 -2097 1964 C ATOM 2178 CD1 PHE A 273 -126.084-156.812 152.459 1.00122.90 C ANISOU 2178 CD1 PHE A 273 15301 10603 20791 3067 -2274 2317 C ATOM 2179 CD2 PHE A 273 -125.602-156.688 154.790 1.00119.86 C ANISOU 2179 CD2 PHE A 273 14989 9897 20655 2915 -1983 1536 C ATOM 2180 CE1 PHE A 273 -127.308-156.203 152.676 1.00122.28 C ANISOU 2180 CE1 PHE A 273 15073 10385 21001 3459 -2341 2251 C ATOM 2181 CE2 PHE A 273 -126.825-156.081 155.014 1.00122.69 C ANISOU 2181 CE2 PHE A 273 15200 10118 21300 3299 -2035 1449 C ATOM 2182 CZ PHE A 273 -127.679-155.838 153.955 1.00116.99 C ANISOU 2182 CZ PHE A 273 14363 9480 20608 3579 -2216 1809 C ATOM 2183 N TYR A 274 -121.791-155.515 154.214 1.00110.55 N ANISOU 2183 N TYR A 274 14483 7992 19528 2083 -1864 1994 N ATOM 2184 CA TYR A 274 -121.492-154.277 154.928 1.00116.66 C ANISOU 2184 CA TYR A 274 15415 8210 20701 2092 -1786 1831 C ATOM 2185 C TYR A 274 -120.781-153.277 154.024 1.00120.30 C ANISOU 2185 C TYR A 274 16088 8403 21217 1960 -1799 2242 C ATOM 2186 O TYR A 274 -121.098-152.083 154.041 1.00122.90 O ANISOU 2186 O TYR A 274 16521 8379 21796 2106 -1780 2281 O ATOM 2187 CB TYR A 274 -120.645-154.579 156.167 1.00119.21 C ANISOU 2187 CB TYR A 274 15782 8497 21017 1834 -1636 1376 C ATOM 2188 CG TYR A 274 -120.670-153.491 157.218 1.00122.18 C ANISOU 2188 CG TYR A 274 16243 8490 21690 1880 -1519 1013 C ATOM 2189 CD1 TYR A 274 -121.462-153.616 158.352 1.00128.51 C ANISOU 2189 CD1 TYR A 274 16908 9341 22578 2068 -1449 550 C ATOM 2190 CD2 TYR A 274 -119.900-152.344 157.080 1.00126.23 C ANISOU 2190 CD2 TYR A 274 16967 8625 22370 1723 -1468 1121 C ATOM 2191 CE1 TYR A 274 -121.489-152.625 159.319 1.00135.41 C ANISOU 2191 CE1 TYR A 274 17852 9913 23684 2107 -1339 197 C ATOM 2192 CE2 TYR A 274 -119.921-151.348 158.040 1.00135.49 C ANISOU 2192 CE2 TYR A 274 18217 9464 23798 1758 -1365 770 C ATOM 2193 CZ TYR A 274 -120.717-151.493 159.156 1.00135.74 C ANISOU 2193 CZ TYR A 274 18110 9567 23899 1954 -1303 304 C ATOM 2194 OH TYR A 274 -120.735-150.502 160.111 1.00140.46 O ANISOU 2194 OH TYR A 274 18779 9859 24730 1988 -1202 -60 O ATOM 2195 N ILE A 275 -119.817-153.749 153.226 1.00125.24 N ANISOU 2195 N ILE A 275 16779 9196 21611 1683 -1828 2553 N ATOM 2196 CA ILE A 275 -119.091-152.863 152.321 1.00130.07 C ANISOU 2196 CA ILE A 275 17579 9602 22241 1527 -1828 2962 C ATOM 2197 C ILE A 275 -120.038-152.220 151.317 1.00141.14 C ANISOU 2197 C ILE A 275 18976 10971 23680 1830 -1947 3355 C ATOM 2198 O ILE A 275 -119.858-151.055 150.939 1.00148.75 O ANISOU 2198 O ILE A 275 20110 11592 24816 1836 -1926 3576 O ATOM 2199 CB ILE A 275 -117.951-153.629 151.623 1.00125.88 C ANISOU 2199 CB ILE A 275 17073 9350 21404 1184 -1835 3215 C ATOM 2200 CG1 ILE A 275 -116.806-153.886 152.605 1.00129.15 C ANISOU 2200 CG1 ILE A 275 17543 9689 21837 854 -1702 2857 C ATOM 2201 CG2 ILE A 275 -117.446-152.877 150.401 1.00122.88 C ANISOU 2201 CG2 ILE A 275 16835 8891 20963 1074 -1861 3732 C ATOM 2202 CD1 ILE A 275 -115.577-154.491 151.963 1.00128.13 C ANISOU 2202 CD1 ILE A 275 17444 9840 21398 498 -1678 3071 C ATOM 2203 N PHE A 276 -121.069-152.944 150.885 1.00138.60 N ANISOU 2203 N PHE A 276 18458 11004 23201 2087 -2074 3439 N ATOM 2204 CA PHE A 276 -122.000-152.401 149.906 1.00145.67 C ANISOU 2204 CA PHE A 276 19324 11933 24091 2387 -2203 3808 C ATOM 2205 C PHE A 276 -123.229-151.755 150.535 1.00143.74 C ANISOU 2205 C PHE A 276 19005 11477 24134 2769 -2212 3568 C ATOM 2206 O PHE A 276 -123.939-151.016 149.843 1.00131.08 O ANISOU 2206 O PHE A 276 17420 9785 22598 3031 -2303 3854 O ATOM 2207 CB PHE A 276 -122.435-153.494 148.924 1.00148.90 C ANISOU 2207 CB PHE A 276 19545 12899 24133 2450 -2356 4070 C ATOM 2208 CG PHE A 276 -121.390-153.838 147.894 1.00153.72 C ANISOU 2208 CG PHE A 276 20240 13735 24434 2147 -2377 4456 C ATOM 2209 CD1 PHE A 276 -121.209-153.034 146.779 1.00158.99 C ANISOU 2209 CD1 PHE A 276 21034 14343 25031 2148 -2423 4931 C ATOM 2210 CD2 PHE A 276 -120.597-154.967 148.035 1.00143.70 C ANISOU 2210 CD2 PHE A 276 18919 12749 22931 1868 -2348 4346 C ATOM 2211 CE1 PHE A 276 -120.252-153.346 145.829 1.00158.67 C ANISOU 2211 CE1 PHE A 276 21054 14553 24680 1864 -2427 5275 C ATOM 2212 CE2 PHE A 276 -119.640-155.285 147.088 1.00141.62 C ANISOU 2212 CE2 PHE A 276 18718 12726 22367 1595 -2358 4687 C ATOM 2213 CZ PHE A 276 -119.468-154.473 145.984 1.00151.84 C ANISOU 2213 CZ PHE A 276 20124 13991 23579 1587 -2391 5145 C ATOM 2214 N THR A 277 -123.500-152.004 151.817 1.00147.53 N ANISOU 2214 N THR A 277 19397 11890 24767 2813 -2118 3054 N ATOM 2215 CA THR A 277 -124.613-151.339 152.490 1.00141.19 C ANISOU 2215 CA THR A 277 18519 10891 24238 3162 -2103 2789 C ATOM 2216 C THR A 277 -124.206-149.974 153.037 1.00141.45 C ANISOU 2216 C THR A 277 18779 10364 24600 3134 -1990 2672 C ATOM 2217 O THR A 277 -124.908-148.983 152.817 1.00155.45 O ANISOU 2217 O THR A 277 20601 11878 26586 3416 -2029 2787 O ATOM 2218 CB THR A 277 -125.168-152.226 153.615 1.00141.53 C ANISOU 2218 CB THR A 277 18342 11163 24271 3233 -2045 2282 C ATOM 2219 OG1 THR A 277 -126.100-153.166 153.067 1.00150.55 O ANISOU 2219 OG1 THR A 277 19230 12767 25203 3424 -2177 2392 O ATOM 2220 CG2 THR A 277 -125.859-151.397 154.684 1.00138.98 C ANISOU 2220 CG2 THR A 277 17999 10549 24259 3467 -1950 1882 C ATOM 2221 N HIS A 278 -123.074-149.901 153.739 1.00141.43 N ANISOU 2221 N HIS A 278 18916 10176 24647 2798 -1858 2439 N ATOM 2222 CA HIS A 278 -122.600-148.617 154.244 1.00141.92 C ANISOU 2222 CA HIS A 278 19192 9716 25013 2729 -1754 2314 C ATOM 2223 C HIS A 278 -121.836-147.860 153.163 1.00163.96 C ANISOU 2223 C HIS A 278 22209 12276 27812 2563 -1784 2815 C ATOM 2224 O HIS A 278 -122.274-146.795 152.709 1.00190.41 O ANISOU 2224 O HIS A 278 25675 15307 31366 2767 -1825 3046 O ATOM 2225 CB HIS A 278 -121.740-148.828 155.493 1.00143.53 C ANISOU 2225 CB HIS A 278 19430 9853 25252 2441 -1604 1822 C ATOM 2226 CG HIS A 278 -122.526-149.212 156.710 1.00153.81 C ANISOU 2226 CG HIS A 278 20548 11280 26610 2627 -1544 1290 C ATOM 2227 ND1 HIS A 278 -123.316-150.341 156.762 1.00159.92 N ANISOU 2227 ND1 HIS A 278 21080 12488 27193 2785 -1599 1206 N ATOM 2228 CD2 HIS A 278 -122.647-148.614 157.919 1.00156.18 C ANISOU 2228 CD2 HIS A 278 20866 11350 27126 2673 -1428 811 C ATOM 2229 CE1 HIS A 278 -123.889-150.422 157.950 1.00161.95 C ANISOU 2229 CE1 HIS A 278 21212 12781 27542 2917 -1511 709 C ATOM 2230 NE2 HIS A 278 -123.500-149.386 158.671 1.00160.00 N ANISOU 2230 NE2 HIS A 278 21116 12147 27530 2856 -1408 459 N ATOM 2231 N GLN A 279 -120.692-148.401 152.739 1.00163.07 N ANISOU 2231 N GLN A 279 22156 12328 27476 2193 -1762 2991 N ATOM 2232 CA GLN A 279 -119.955-147.900 151.574 1.00171.07 C ANISOU 2232 CA GLN A 279 23341 13244 28413 2009 -1791 3512 C ATOM 2233 C GLN A 279 -119.622-146.417 151.711 1.00174.99 C ANISOU 2233 C GLN A 279 24078 13162 29246 1974 -1717 3550 C ATOM 2234 O GLN A 279 -119.699-145.650 150.750 1.00179.07 O ANISOU 2234 O GLN A 279 24729 13497 29813 2046 -1774 3997 O ATOM 2235 CB GLN A 279 -120.741-148.160 150.284 1.00182.25 C ANISOU 2235 CB GLN A 279 24671 14955 29623 2251 -1954 3997 C ATOM 2236 CG GLN A 279 -119.876-148.310 149.037 1.00191.26 C ANISOU 2236 CG GLN A 279 25899 16282 30491 1991 -1989 4509 C ATOM 2237 CD GLN A 279 -120.684-148.673 147.805 1.00198.34 C ANISOU 2237 CD GLN A 279 26681 17552 31126 2232 -2159 4943 C ATOM 2238 OE1 GLN A 279 -121.914-148.632 147.821 1.00201.06 O ANISOU 2238 OE1 GLN A 279 26902 17957 31535 2611 -2258 4900 O ATOM 2239 NE2 GLN A 279 -119.993-149.034 146.729 1.00200.41 N ANISOU 2239 NE2 GLN A 279 26970 18105 31073 2009 -2193 5350 N ATOM 2240 N GLY A 280 -119.252-146.009 152.918 1.00172.88 N ANISOU 2240 N GLY A 280 23869 12611 29206 1860 -1593 3075 N ATOM 2241 CA GLY A 280 -118.991-144.604 153.161 1.00170.76 C ANISOU 2241 CA GLY A 280 23823 11774 29282 1834 -1524 3047 C ATOM 2242 C GLY A 280 -117.840-144.335 154.105 1.00162.78 C ANISOU 2242 C GLY A 280 22915 10557 28378 1460 -1378 2670 C ATOM 2243 O GLY A 280 -117.537-143.176 154.403 1.00157.35 O ANISOU 2243 O GLY A 280 22415 9386 27986 1397 -1313 2594 O ATOM 2244 N SER A 281 -117.184-145.390 154.583 1.00155.58 N ANISOU 2244 N SER A 281 21881 10005 27227 1209 -1332 2429 N ATOM 2245 CA SER A 281 -116.081-145.246 155.519 1.00158.87 C ANISOU 2245 CA SER A 281 22361 10303 27698 853 -1205 2046 C ATOM 2246 C SER A 281 -114.881-146.050 155.040 1.00148.61 C ANISOU 2246 C SER A 281 21041 9321 26102 462 -1183 2231 C ATOM 2247 O SER A 281 -114.996-146.950 154.204 1.00157.42 O ANISOU 2247 O SER A 281 22054 10816 26942 487 -1262 2549 O ATOM 2248 CB SER A 281 -116.474-145.690 156.935 1.00166.49 C ANISOU 2248 CB SER A 281 23182 11391 28687 951 -1152 1422 C ATOM 2249 OG SER A 281 -117.184-144.666 157.612 1.00180.16 O ANISOU 2249 OG SER A 281 24974 12736 30743 1194 -1122 1149 O ATOM 2250 N CYS A 282 -113.720-145.702 155.582 1.00137.43 N ANISOU 2250 N CYS A 282 19716 7757 24743 98 -1076 2016 N ATOM 2251 CA CYS A 282 -112.504-146.444 155.306 1.00136.09 C ANISOU 2251 CA CYS A 282 19507 7894 24307 -289 -1038 2110 C ATOM 2252 C CYS A 282 -112.508-147.744 156.093 1.00135.52 C ANISOU 2252 C CYS A 282 19235 8254 24002 -298 -1041 1740 C ATOM 2253 O CYS A 282 -112.863-147.771 157.275 1.00134.24 O ANISOU 2253 O CYS A 282 19013 8060 23932 -195 -1003 1247 O ATOM 2254 CB CYS A 282 -111.278-145.611 155.672 1.00139.27 C ANISOU 2254 CB CYS A 282 20055 8006 24855 -676 -925 1976 C ATOM 2255 SG CYS A 282 -111.325-143.900 155.071 1.00151.55 S ANISOU 2255 SG CYS A 282 21880 8931 26773 -663 -902 2292 S ATOM 2256 N PHE A 283 -112.129-148.828 155.430 1.00140.39 N ANISOU 2256 N PHE A 283 19749 9285 24308 -416 -1084 1982 N ATOM 2257 CA PHE A 283 -112.012-150.130 156.068 1.00139.24 C ANISOU 2257 CA PHE A 283 19431 9548 23926 -457 -1091 1683 C ATOM 2258 C PHE A 283 -110.540-150.389 156.354 1.00140.10 C ANISOU 2258 C PHE A 283 19541 9783 23908 -888 -1010 1555 C ATOM 2259 O PHE A 283 -109.732-150.484 155.424 1.00145.78 O ANISOU 2259 O PHE A 283 20289 10612 24490 -1126 -1007 1922 O ATOM 2260 CB PHE A 283 -112.601-151.228 155.184 1.00144.46 C ANISOU 2260 CB PHE A 283 19967 10592 24327 -291 -1204 2005 C ATOM 2261 CG PHE A 283 -113.932-150.871 154.597 1.00153.22 C ANISOU 2261 CG PHE A 283 21073 11604 25538 99 -1299 2246 C ATOM 2262 CD1 PHE A 283 -115.068-150.856 155.387 1.00156.70 C ANISOU 2262 CD1 PHE A 283 21434 11986 26119 425 -1314 1922 C ATOM 2263 CD2 PHE A 283 -114.047-150.537 153.258 1.00157.58 C ANISOU 2263 CD2 PHE A 283 21690 12154 26029 142 -1369 2793 C ATOM 2264 CE1 PHE A 283 -116.296-150.521 154.853 1.00160.20 C ANISOU 2264 CE1 PHE A 283 21851 12362 26657 791 -1405 2133 C ATOM 2265 CE2 PHE A 283 -115.273-150.201 152.717 1.00159.49 C ANISOU 2265 CE2 PHE A 283 21916 12334 26350 512 -1468 3013 C ATOM 2266 CZ PHE A 283 -116.398-150.193 153.516 1.00160.20 C ANISOU 2266 CZ PHE A 283 21916 12358 26596 839 -1489 2679 C ATOM 2267 N GLY A 284 -110.196-150.491 157.635 1.00140.07 N ANISOU 2267 N GLY A 284 19491 9793 23935 -986 -944 1034 N ATOM 2268 CA GLY A 284 -108.838-150.761 158.035 1.00135.66 C ANISOU 2268 CA GLY A 284 18903 9390 23251 -1375 -877 855 C ATOM 2269 C GLY A 284 -108.331-152.077 157.488 1.00127.96 C ANISOU 2269 C GLY A 284 17800 8870 21950 -1504 -923 1044 C ATOM 2270 O GLY A 284 -109.086-152.882 156.924 1.00115.06 O ANISOU 2270 O GLY A 284 16095 7447 20175 -1286 -1010 1258 O ATOM 2271 N PRO A 285 -107.026-152.328 157.657 1.00129.87 N ANISOU 2271 N PRO A 285 17999 9283 22064 -1868 -870 953 N ATOM 2272 CA PRO A 285 -106.431-153.580 157.164 1.00125.36 C ANISOU 2272 CA PRO A 285 17297 9162 21174 -2011 -911 1111 C ATOM 2273 C PRO A 285 -107.110-154.808 157.735 1.00133.42 C ANISOU 2273 C PRO A 285 18185 10631 21877 -1754 -936 852 C ATOM 2274 O PRO A 285 -107.087-155.892 157.141 1.00137.24 O ANISOU 2274 O PRO A 285 18574 11585 21985 -1708 -961 1019 O ATOM 2275 CB PRO A 285 -104.975-153.486 157.640 1.00121.83 C ANISOU 2275 CB PRO A 285 16802 8809 20676 -2413 -835 897 C ATOM 2276 CG PRO A 285 -104.979-152.452 158.734 1.00131.27 C ANISOU 2276 CG PRO A 285 18079 9678 22120 -2430 -764 484 C ATOM 2277 CD PRO A 285 -106.044-151.476 158.347 1.00129.11 C ANISOU 2277 CD PRO A 285 17958 8996 22101 -2162 -774 674 C ATOM 2278 N ILE A 286 -107.736-154.631 158.893 1.00136.70 N ANISOU 2278 N ILE A 286 18593 10895 22451 -1589 -923 437 N ATOM 2279 CA ILE A 286 -108.293-155.754 159.631 1.00137.51 C ANISOU 2279 CA ILE A 286 18569 11415 22265 -1392 -926 151 C ATOM 2280 C ILE A 286 -109.671-156.134 159.100 1.00132.79 C ANISOU 2280 C ILE A 286 17948 10873 21632 -1040 -991 347 C ATOM 2281 O ILE A 286 -109.937-157.310 158.825 1.00127.09 O ANISOU 2281 O ILE A 286 17124 10598 20565 -945 -1014 415 O ATOM 2282 CB ILE A 286 -108.328-155.429 161.134 1.00144.45 C ANISOU 2282 CB ILE A 286 19429 12175 23281 -1388 -873 -389 C ATOM 2283 CG1 ILE A 286 -106.902-155.334 161.677 1.00150.55 C ANISOU 2283 CG1 ILE A 286 20173 13047 23983 -1747 -822 -608 C ATOM 2284 CG2 ILE A 286 -109.130-156.466 161.883 1.00139.10 C ANISOU 2284 CG2 ILE A 286 18634 11874 22345 -1150 -869 -637 C ATOM 2285 CD1 ILE A 286 -106.830-154.936 163.134 1.00152.65 C ANISOU 2285 CD1 ILE A 286 20415 13217 24367 -1777 -776 -1152 C ATOM 2286 N PHE A 287 -110.550-155.150 158.907 1.00128.00 N ANISOU 2286 N PHE A 287 17431 9815 21391 -842 -1025 447 N ATOM 2287 CA PHE A 287 -111.968-155.419 158.675 1.00122.91 C ANISOU 2287 CA PHE A 287 16733 9215 20753 -477 -1087 528 C ATOM 2288 C PHE A 287 -112.257-156.318 157.475 1.00121.52 C ANISOU 2288 C PHE A 287 16491 9422 20260 -401 -1159 925 C ATOM 2289 O PHE A 287 -112.700-157.458 157.649 1.00122.08 O ANISOU 2289 O PHE A 287 16437 9917 20032 -294 -1165 813 O ATOM 2290 CB PHE A 287 -112.749-154.115 158.513 1.00125.33 C ANISOU 2290 CB PHE A 287 17146 8943 21531 -275 -1124 627 C ATOM 2291 CG PHE A 287 -114.169-154.329 158.082 1.00116.40 C ANISOU 2291 CG PHE A 287 15942 7875 20410 103 -1205 778 C ATOM 2292 CD1 PHE A 287 -114.601-153.920 156.833 1.00123.68 C ANISOU 2292 CD1 PHE A 287 16916 8664 21413 231 -1301 1269 C ATOM 2293 CD2 PHE A 287 -115.064-154.981 158.916 1.00117.19 C ANISOU 2293 CD2 PHE A 287 15903 8223 20400 321 -1183 436 C ATOM 2294 CE1 PHE A 287 -115.905-154.133 156.432 1.00134.44 C ANISOU 2294 CE1 PHE A 287 18186 10115 22781 581 -1391 1400 C ATOM 2295 CE2 PHE A 287 -116.367-155.199 158.522 1.00123.12 C ANISOU 2295 CE2 PHE A 287 16557 9066 21156 652 -1255 559 C ATOM 2296 CZ PHE A 287 -116.790-154.775 157.278 1.00134.51 C ANISOU 2296 CZ PHE A 287 18042 10366 22699 788 -1366 1032 C ATOM 2297 N MET A 288 -112.044-155.818 156.255 1.00114.42 N ANISOU 2297 N MET A 288 15673 8381 19419 -458 -1214 1385 N ATOM 2298 CA MET A 288 -112.365-156.593 155.057 1.00106.37 C ANISOU 2298 CA MET A 288 14587 7736 18094 -377 -1291 1754 C ATOM 2299 C MET A 288 -111.461-157.806 154.865 1.00103.66 C ANISOU 2299 C MET A 288 14155 7916 17317 -591 -1254 1722 C ATOM 2300 O MET A 288 -111.674-158.568 153.915 1.00 89.35 O ANISOU 2300 O MET A 288 12273 6458 15220 -538 -1310 1966 O ATOM 2301 CB MET A 288 -112.304-155.695 153.822 1.00118.12 C ANISOU 2301 CB MET A 288 16186 8960 19733 -396 -1354 2270 C ATOM 2302 CG MET A 288 -111.153-154.715 153.826 1.00130.94 C ANISOU 2302 CG MET A 288 17950 10221 21582 -708 -1288 2359 C ATOM 2303 SD MET A 288 -111.384-153.464 152.557 1.00142.22 S ANISOU 2303 SD MET A 288 19530 11260 23247 -658 -1349 2951 S ATOM 2304 CE MET A 288 -109.932-152.443 152.836 1.00148.74 C ANISOU 2304 CE MET A 288 20492 11801 24221 -1069 -1201 2883 C ATOM 2305 N THR A 289 -110.465-158.001 155.727 1.00 97.58 N ANISOU 2305 N THR A 289 13376 7211 16490 -819 -1168 1418 N ATOM 2306 CA THR A 289 -109.651-159.208 155.741 1.00 84.71 C ANISOU 2306 CA THR A 289 11646 6069 14471 -976 -1133 1325 C ATOM 2307 C THR A 289 -110.037-160.154 156.873 1.00 87.08 C ANISOU 2307 C THR A 289 11849 6613 14626 -861 -1104 924 C ATOM 2308 O THR A 289 -109.422-161.217 157.011 1.00 85.83 O ANISOU 2308 O THR A 289 11609 6840 14164 -958 -1079 824 O ATOM 2309 CB THR A 289 -108.159-158.844 155.838 1.00 94.69 C ANISOU 2309 CB THR A 289 12942 7302 15733 -1322 -1065 1303 C ATOM 2310 OG1 THR A 289 -107.904-158.165 157.075 1.00109.79 O ANISOU 2310 OG1 THR A 289 14895 8923 17896 -1399 -1011 942 O ATOM 2311 CG2 THR A 289 -107.742-157.936 154.672 1.00 90.52 C ANISOU 2311 CG2 THR A 289 12508 6553 15332 -1470 -1079 1741 C ATOM 2312 N ILE A 290 -111.045-159.795 157.678 1.00 81.22 N ANISOU 2312 N ILE A 290 11108 5659 14092 -651 -1103 703 N ATOM 2313 CA ILE A 290 -111.516-160.702 158.728 1.00 78.20 C ANISOU 2313 CA ILE A 290 10628 5532 13554 -539 -1067 359 C ATOM 2314 C ILE A 290 -112.037-162.019 158.165 1.00 74.64 C ANISOU 2314 C ILE A 290 10074 5495 12792 -428 -1106 476 C ATOM 2315 O ILE A 290 -111.713-163.075 158.731 1.00 73.13 O ANISOU 2315 O ILE A 290 9813 5619 12353 -480 -1067 291 O ATOM 2316 CB ILE A 290 -112.559-159.991 159.615 1.00 84.51 C ANISOU 2316 CB ILE A 290 11433 6039 14638 -328 -1050 110 C ATOM 2317 CG1 ILE A 290 -111.876-159.005 160.564 1.00 95.91 C ANISOU 2317 CG1 ILE A 290 12954 7169 16321 -476 -987 -172 C ATOM 2318 CG2 ILE A 290 -113.376-161.006 160.408 1.00 78.26 C ANISOU 2318 CG2 ILE A 290 10520 5558 13658 -167 -1020 -139 C ATOM 2319 CD1 ILE A 290 -112.840-158.171 161.385 1.00104.44 C ANISOU 2319 CD1 ILE A 290 14044 7924 17714 -267 -964 -440 C ATOM 2320 N PRO A 291 -112.839-162.046 157.090 1.00 78.79 N ANISOU 2320 N PRO A 291 10580 6041 13314 -275 -1184 768 N ATOM 2321 CA PRO A 291 -113.225-163.358 156.533 1.00 65.06 C ANISOU 2321 CA PRO A 291 8736 4715 11269 -211 -1220 842 C ATOM 2322 C PRO A 291 -112.029-164.196 156.112 1.00 64.32 C ANISOU 2322 C PRO A 291 8629 4925 10886 -424 -1200 900 C ATOM 2323 O PRO A 291 -111.992-165.400 156.390 1.00 65.84 O ANISOU 2323 O PRO A 291 8745 5425 10846 -424 -1180 760 O ATOM 2324 CB PRO A 291 -114.123-162.985 155.342 1.00 65.76 C ANISOU 2324 CB PRO A 291 8813 4752 11422 -43 -1322 1170 C ATOM 2325 CG PRO A 291 -114.654-161.657 155.682 1.00 79.56 C ANISOU 2325 CG PRO A 291 10632 6057 13541 84 -1332 1170 C ATOM 2326 CD PRO A 291 -113.540-160.945 156.400 1.00 70.01 C ANISOU 2326 CD PRO A 291 9530 4593 12479 -129 -1252 1020 C ATOM 2327 N ALA A 292 -111.037-163.586 155.458 1.00 73.37 N ANISOU 2327 N ALA A 292 9842 5986 12050 -607 -1198 1104 N ATOM 2328 CA ALA A 292 -109.846-164.331 155.061 1.00 75.53 C ANISOU 2328 CA ALA A 292 10080 6566 12053 -805 -1170 1140 C ATOM 2329 C ALA A 292 -109.088-164.848 156.277 1.00 81.55 C ANISOU 2329 C ALA A 292 10814 7432 12740 -909 -1100 808 C ATOM 2330 O ALA A 292 -108.619-165.992 156.285 1.00 77.43 O ANISOU 2330 O ALA A 292 10220 7238 11962 -943 -1086 732 O ATOM 2331 CB ALA A 292 -108.943-163.454 154.197 1.00 79.69 C ANISOU 2331 CB ALA A 292 10672 6975 12632 -1000 -1167 1420 C ATOM 2332 N PHE A 293 -108.981-164.023 157.322 1.00 83.07 N ANISOU 2332 N PHE A 293 11058 7351 13154 -947 -1059 600 N ATOM 2333 CA PHE A 293 -108.279-164.420 158.540 1.00 79.47 C ANISOU 2333 CA PHE A 293 10567 7012 12616 -1040 -1002 280 C ATOM 2334 C PHE A 293 -108.823-165.735 159.095 1.00 76.77 C ANISOU 2334 C PHE A 293 10148 6961 12062 -898 -997 122 C ATOM 2335 O PHE A 293 -108.060-166.667 159.375 1.00 79.97 O ANISOU 2335 O PHE A 293 10498 7644 12243 -971 -979 35 O ATOM 2336 CB PHE A 293 -108.381-163.299 159.578 1.00 75.47 C ANISOU 2336 CB PHE A 293 10121 6166 12390 -1061 -967 50 C ATOM 2337 CG PHE A 293 -107.528-163.511 160.801 1.00 86.13 C ANISOU 2337 CG PHE A 293 11431 7644 13649 -1190 -918 -273 C ATOM 2338 CD1 PHE A 293 -106.248-162.983 160.873 1.00 83.76 C ANISOU 2338 CD1 PHE A 293 11136 7311 13377 -1441 -897 -313 C ATOM 2339 CD2 PHE A 293 -108.016-164.224 161.886 1.00 90.25 C ANISOU 2339 CD2 PHE A 293 11900 8341 14050 -1066 -893 -531 C ATOM 2340 CE1 PHE A 293 -105.469-163.173 162.000 1.00 81.86 C ANISOU 2340 CE1 PHE A 293 10839 7226 13037 -1553 -868 -617 C ATOM 2341 CE2 PHE A 293 -107.241-164.416 163.012 1.00 97.59 C ANISOU 2341 CE2 PHE A 293 12788 9425 14869 -1173 -860 -809 C ATOM 2342 CZ PHE A 293 -105.967-163.887 163.069 1.00 89.25 C ANISOU 2342 CZ PHE A 293 11727 8348 13834 -1409 -854 -859 C ATOM 2343 N PHE A 294 -110.142-165.838 159.252 1.00 76.33 N ANISOU 2343 N PHE A 294 10079 6841 12081 -693 -1011 94 N ATOM 2344 CA PHE A 294 -110.706-167.059 159.820 1.00 77.01 C ANISOU 2344 CA PHE A 294 10093 7180 11987 -584 -993 -46 C ATOM 2345 C PHE A 294 -110.866-168.181 158.799 1.00 70.10 C ANISOU 2345 C PHE A 294 9165 6564 10905 -547 -1036 133 C ATOM 2346 O PHE A 294 -110.877-169.354 159.191 1.00 68.97 O ANISOU 2346 O PHE A 294 8973 6650 10583 -525 -1015 33 O ATOM 2347 CB PHE A 294 -112.048-166.760 160.492 1.00 71.68 C ANISOU 2347 CB PHE A 294 9398 6371 11467 -398 -976 -184 C ATOM 2348 CG PHE A 294 -111.919-165.957 161.759 1.00 81.12 C ANISOU 2348 CG PHE A 294 10622 7391 12808 -421 -916 -460 C ATOM 2349 CD1 PHE A 294 -111.477-166.553 162.933 1.00 83.72 C ANISOU 2349 CD1 PHE A 294 10919 7914 12975 -477 -860 -701 C ATOM 2350 CD2 PHE A 294 -112.220-164.605 161.775 1.00 94.60 C ANISOU 2350 CD2 PHE A 294 12388 8742 14814 -382 -921 -482 C ATOM 2351 CE1 PHE A 294 -111.344-165.815 164.096 1.00 94.31 C ANISOU 2351 CE1 PHE A 294 12275 9139 14420 -504 -808 -981 C ATOM 2352 CE2 PHE A 294 -112.089-163.864 162.934 1.00 95.92 C ANISOU 2352 CE2 PHE A 294 12576 8748 15120 -407 -865 -780 C ATOM 2353 CZ PHE A 294 -111.651-164.470 164.095 1.00 96.88 C ANISOU 2353 CZ PHE A 294 12653 9107 15048 -473 -809 -1042 C ATOM 2354 N ALA A 295 -110.972-167.862 157.504 1.00 65.98 N ANISOU 2354 N ALA A 295 8654 6017 10399 -545 -1094 394 N ATOM 2355 CA ALA A 295 -111.067-168.918 156.496 1.00 64.14 C ANISOU 2355 CA ALA A 295 8361 6058 9951 -522 -1136 529 C ATOM 2356 C ALA A 295 -109.783-169.733 156.377 1.00 74.14 C ANISOU 2356 C ALA A 295 9606 7563 11001 -663 -1110 497 C ATOM 2357 O ALA A 295 -109.815-170.829 155.811 1.00 61.47 O ANISOU 2357 O ALA A 295 7947 6197 9213 -635 -1128 519 O ATOM 2358 CB ALA A 295 -111.418-168.328 155.129 1.00 57.34 C ANISOU 2358 CB ALA A 295 7507 5157 9121 -491 -1208 822 C ATOM 2359 N LYS A 296 -108.658-169.218 156.882 1.00 72.89 N ANISOU 2359 N LYS A 296 9478 7347 10869 -810 -1069 430 N ATOM 2360 CA LYS A 296 -107.408-169.965 156.820 1.00 61.32 C ANISOU 2360 CA LYS A 296 7966 6127 9205 -926 -1047 387 C ATOM 2361 C LYS A 296 -107.506-171.276 157.588 1.00 72.48 C ANISOU 2361 C LYS A 296 9338 7722 10479 -841 -1031 205 C ATOM 2362 O LYS A 296 -106.942-172.292 157.160 1.00 56.51 O ANISOU 2362 O LYS A 296 7264 5930 8276 -848 -1035 211 O ATOM 2363 CB LYS A 296 -106.251-169.127 157.367 1.00 60.32 C ANISOU 2363 CB LYS A 296 7857 5913 9148 -1103 -1010 317 C ATOM 2364 CG LYS A 296 -105.879-167.894 156.539 1.00 62.65 C ANISOU 2364 CG LYS A 296 8196 6033 9575 -1240 -1014 526 C ATOM 2365 CD LYS A 296 -104.790-167.086 157.247 1.00 75.67 C ANISOU 2365 CD LYS A 296 9853 7577 11322 -1438 -972 405 C ATOM 2366 CE LYS A 296 -104.536-165.737 156.581 1.00 83.73 C ANISOU 2366 CE LYS A 296 10941 8335 12539 -1590 -964 610 C ATOM 2367 NZ LYS A 296 -103.904-165.870 155.243 1.00106.70 N ANISOU 2367 NZ LYS A 296 13808 11440 15292 -1702 -963 881 N ATOM 2368 N THR A 297 -108.214-171.277 158.722 1.00 57.88 N ANISOU 2368 N THR A 297 7508 5771 8713 -758 -1006 46 N ATOM 2369 CA THR A 297 -108.342-172.484 159.534 1.00 69.17 C ANISOU 2369 CA THR A 297 8909 7356 10016 -688 -983 -93 C ATOM 2370 C THR A 297 -109.043-173.624 158.811 1.00 69.83 C ANISOU 2370 C THR A 297 8959 7564 10008 -595 -1006 -23 C ATOM 2371 O THR A 297 -109.042-174.746 159.327 1.00 67.46 O ANISOU 2371 O THR A 297 8643 7382 9607 -552 -987 -105 O ATOM 2372 CB THR A 297 -109.095-172.189 160.830 1.00 67.26 C ANISOU 2372 CB THR A 297 8686 7004 9867 -624 -942 -258 C ATOM 2373 OG1 THR A 297 -110.429-171.771 160.524 1.00 71.88 O ANISOU 2373 OG1 THR A 297 9273 7444 10594 -519 -951 -209 O ATOM 2374 CG2 THR A 297 -108.392-171.089 161.606 1.00 52.27 C ANISOU 2374 CG2 THR A 297 6815 4988 8058 -724 -920 -380 C ATOM 2375 N SER A 298 -109.641-173.378 157.643 1.00 67.40 N ANISOU 2375 N SER A 298 8640 7235 9734 -566 -1051 127 N ATOM 2376 CA SER A 298 -110.239-174.477 156.893 1.00 63.40 C ANISOU 2376 CA SER A 298 8087 6873 9128 -500 -1080 160 C ATOM 2377 C SER A 298 -109.199-175.497 156.453 1.00 74.66 C ANISOU 2377 C SER A 298 9486 8503 10379 -545 -1080 141 C ATOM 2378 O SER A 298 -109.555-176.643 156.164 1.00 65.63 O ANISOU 2378 O SER A 298 8312 7464 9162 -493 -1089 98 O ATOM 2379 CB SER A 298 -110.998-173.948 155.674 1.00 55.60 C ANISOU 2379 CB SER A 298 7075 5870 8179 -463 -1143 326 C ATOM 2380 OG SER A 298 -110.105-173.386 154.726 1.00 74.00 O ANISOU 2380 OG SER A 298 9413 8256 10446 -554 -1165 477 O ATOM 2381 N ALA A 299 -107.921-175.107 156.397 1.00 59.00 N ANISOU 2381 N ALA A 299 7503 6575 8341 -641 -1067 158 N ATOM 2382 CA ALA A 299 -106.867-176.063 156.091 1.00 61.26 C ANISOU 2382 CA ALA A 299 7742 7066 8467 -661 -1062 114 C ATOM 2383 C ALA A 299 -106.710-177.102 157.191 1.00 66.02 C ANISOU 2383 C ALA A 299 8353 7694 9038 -595 -1037 -29 C ATOM 2384 O ALA A 299 -106.108-178.155 156.955 1.00 58.88 O ANISOU 2384 O ALA A 299 7414 6931 8028 -559 -1039 -77 O ATOM 2385 CB ALA A 299 -105.540-175.336 155.868 1.00 53.44 C ANISOU 2385 CB ALA A 299 6725 6148 7433 -789 -1048 158 C ATOM 2386 N VAL A 300 -107.239-176.827 158.378 1.00 64.10 N ANISOU 2386 N VAL A 300 8152 7322 8882 -570 -1012 -94 N ATOM 2387 CA VAL A 300 -107.180-177.745 159.506 1.00 58.04 C ANISOU 2387 CA VAL A 300 7399 6585 8070 -510 -985 -191 C ATOM 2388 C VAL A 300 -108.496-178.500 159.691 1.00 75.76 C ANISOU 2388 C VAL A 300 9662 8763 10362 -434 -969 -200 C ATOM 2389 O VAL A 300 -108.501-179.724 159.827 1.00 67.79 O ANISOU 2389 O VAL A 300 8656 7799 9302 -383 -961 -223 O ATOM 2390 CB VAL A 300 -106.783-176.986 160.792 1.00 63.56 C ANISOU 2390 CB VAL A 300 8116 7246 8789 -551 -960 -273 C ATOM 2391 CG1 VAL A 300 -106.846-177.921 161.995 1.00 60.81 C ANISOU 2391 CG1 VAL A 300 7784 6955 8368 -481 -934 -340 C ATOM 2392 CG2 VAL A 300 -105.389-176.373 160.648 1.00 66.77 C ANISOU 2392 CG2 VAL A 300 8483 7741 9146 -651 -976 -284 C ATOM 2393 N TYR A 301 -109.635-177.797 159.691 1.00 69.32 N ANISOU 2393 N TYR A 301 8851 7831 9657 -424 -962 -184 N ATOM 2394 CA TYR A 301 -110.883-178.469 160.043 1.00 67.58 C ANISOU 2394 CA TYR A 301 8624 7572 9483 -370 -934 -210 C ATOM 2395 C TYR A 301 -111.549-179.185 158.871 1.00 72.65 C ANISOU 2395 C TYR A 301 9225 8252 10127 -351 -972 -170 C ATOM 2396 O TYR A 301 -112.344-180.103 159.107 1.00 68.31 O ANISOU 2396 O TYR A 301 8662 7695 9597 -332 -946 -205 O ATOM 2397 CB TYR A 301 -111.881-177.498 160.705 1.00 60.79 C ANISOU 2397 CB TYR A 301 7757 6601 8739 -348 -902 -244 C ATOM 2398 CG TYR A 301 -112.425-176.360 159.863 1.00 64.13 C ANISOU 2398 CG TYR A 301 8158 6933 9276 -333 -946 -178 C ATOM 2399 CD1 TYR A 301 -113.341-176.589 158.843 1.00 68.23 C ANISOU 2399 CD1 TYR A 301 8624 7475 9827 -294 -991 -110 C ATOM 2400 CD2 TYR A 301 -112.067-175.043 160.135 1.00 67.32 C ANISOU 2400 CD2 TYR A 301 8592 7220 9766 -356 -945 -186 C ATOM 2401 CE1 TYR A 301 -113.847-175.540 158.088 1.00 74.60 C ANISOU 2401 CE1 TYR A 301 9408 8207 10729 -258 -1043 -17 C ATOM 2402 CE2 TYR A 301 -112.571-173.996 159.395 1.00 68.64 C ANISOU 2402 CE2 TYR A 301 8753 7267 10062 -327 -987 -96 C ATOM 2403 CZ TYR A 301 -113.457-174.247 158.372 1.00 73.77 C ANISOU 2403 CZ TYR A 301 9350 7957 10724 -268 -1039 4 C ATOM 2404 OH TYR A 301 -113.954-173.196 157.637 1.00 74.95 O ANISOU 2404 OH TYR A 301 9491 7996 10992 -219 -1094 125 O ATOM 2405 N ASN A 302 -111.246-178.812 157.622 1.00 66.00 N ANISOU 2405 N ASN A 302 8356 7467 9255 -370 -1028 -102 N ATOM 2406 CA ASN A 302 -111.777-179.587 156.499 1.00 58.88 C ANISOU 2406 CA ASN A 302 7404 6651 8316 -358 -1070 -97 C ATOM 2407 C ASN A 302 -111.239-181.016 156.483 1.00 70.69 C ANISOU 2407 C ASN A 302 8908 8208 9742 -351 -1056 -180 C ATOM 2408 O ASN A 302 -112.048-181.951 156.352 1.00 67.92 O ANISOU 2408 O ASN A 302 8537 7843 9426 -343 -1053 -237 O ATOM 2409 CB ASN A 302 -111.519-178.856 155.176 1.00 54.89 C ANISOU 2409 CB ASN A 302 6864 6237 7756 -380 -1133 6 C ATOM 2410 CG ASN A 302 -112.610-177.857 154.840 1.00 75.59 C ANISOU 2410 CG ASN A 302 9456 8793 10472 -347 -1172 99 C ATOM 2411 OD1 ASN A 302 -113.739-177.969 155.319 1.00 77.17 O ANISOU 2411 OD1 ASN A 302 9628 8927 10767 -300 -1162 54 O ATOM 2412 ND2 ASN A 302 -112.279-176.871 154.012 1.00 71.33 N ANISOU 2412 ND2 ASN A 302 8916 8277 9910 -367 -1216 241 N ATOM 2413 N PRO A 303 -109.931-181.272 156.606 1.00 70.92 N ANISOU 2413 N PRO A 303 8960 8297 9690 -353 -1048 -197 N ATOM 2414 CA PRO A 303 -109.496-182.677 156.693 1.00 61.16 C ANISOU 2414 CA PRO A 303 7736 7079 8422 -312 -1035 -278 C ATOM 2415 C PRO A 303 -110.010-183.388 157.934 1.00 68.54 C ANISOU 2415 C PRO A 303 8724 7889 9428 -288 -985 -295 C ATOM 2416 O PRO A 303 -110.230-184.603 157.891 1.00 73.04 O ANISOU 2416 O PRO A 303 9311 8409 10031 -265 -975 -343 O ATOM 2417 CB PRO A 303 -107.961-182.582 156.679 1.00 67.68 C ANISOU 2417 CB PRO A 303 8552 8013 9150 -302 -1039 -283 C ATOM 2418 CG PRO A 303 -107.647-181.183 157.063 1.00 72.12 C ANISOU 2418 CG PRO A 303 9117 8571 9714 -361 -1035 -213 C ATOM 2419 CD PRO A 303 -108.778-180.353 156.535 1.00 66.83 C ANISOU 2419 CD PRO A 303 8440 7840 9113 -392 -1054 -149 C ATOM 2420 N VAL A 304 -110.225-182.667 159.037 1.00 63.29 N ANISOU 2420 N VAL A 304 8088 7172 8789 -298 -950 -259 N ATOM 2421 CA VAL A 304 -110.819-183.285 160.222 1.00 65.13 C ANISOU 2421 CA VAL A 304 8362 7324 9059 -287 -891 -256 C ATOM 2422 C VAL A 304 -112.225-183.796 159.914 1.00 76.26 C ANISOU 2422 C VAL A 304 9743 8670 10563 -318 -872 -273 C ATOM 2423 O VAL A 304 -112.596-184.909 160.307 1.00 80.30 O ANISOU 2423 O VAL A 304 10283 9114 11114 -326 -833 -275 O ATOM 2424 CB VAL A 304 -110.822-182.292 161.399 1.00 65.82 C ANISOU 2424 CB VAL A 304 8465 7412 9131 -297 -854 -247 C ATOM 2425 CG1 VAL A 304 -111.704-182.802 162.523 1.00 71.92 C ANISOU 2425 CG1 VAL A 304 9259 8142 9925 -300 -781 -237 C ATOM 2426 CG2 VAL A 304 -109.405-182.054 161.903 1.00 68.77 C ANISOU 2426 CG2 VAL A 304 8857 7868 9405 -281 -872 -250 C ATOM 2427 N ILE A 305 -113.016-183.005 159.185 1.00 68.43 N ANISOU 2427 N ILE A 305 8688 7699 9615 -337 -902 -277 N ATOM 2428 CA ILE A 305 -114.411-183.357 158.932 1.00 72.57 C ANISOU 2428 CA ILE A 305 9150 8200 10224 -368 -891 -304 C ATOM 2429 C ILE A 305 -114.531-184.383 157.810 1.00 70.89 C ANISOU 2429 C ILE A 305 8907 8014 10016 -393 -935 -365 C ATOM 2430 O ILE A 305 -115.308-185.336 157.914 1.00 77.21 O ANISOU 2430 O ILE A 305 9689 8759 10889 -440 -905 -412 O ATOM 2431 CB ILE A 305 -115.229-182.092 158.617 1.00 69.40 C ANISOU 2431 CB ILE A 305 8676 7823 9870 -351 -919 -283 C ATOM 2432 CG1 ILE A 305 -115.325-181.198 159.854 1.00 71.33 C ANISOU 2432 CG1 ILE A 305 8943 8017 10140 -328 -858 -275 C ATOM 2433 CG2 ILE A 305 -116.617-182.472 158.100 1.00 68.22 C ANISOU 2433 CG2 ILE A 305 8425 7703 9794 -375 -932 -321 C ATOM 2434 CD1 ILE A 305 -116.011-179.879 159.590 1.00 74.08 C ANISOU 2434 CD1 ILE A 305 9232 8347 10567 -284 -887 -260 C ATOM 2435 N TYR A 306 -113.787-184.202 156.719 1.00 65.01 N ANISOU 2435 N TYR A 306 8147 7363 9193 -373 -1002 -377 N ATOM 2436 CA TYR A 306 -113.944-185.045 155.543 1.00 63.78 C ANISOU 2436 CA TYR A 306 7941 7272 9018 -394 -1050 -471 C ATOM 2437 C TYR A 306 -113.069-186.293 155.553 1.00 69.85 C ANISOU 2437 C TYR A 306 8769 7988 9782 -374 -1032 -552 C ATOM 2438 O TYR A 306 -113.304-187.202 154.746 1.00 73.33 O ANISOU 2438 O TYR A 306 9177 8442 10242 -396 -1056 -674 O ATOM 2439 CB TYR A 306 -113.628-184.248 154.278 1.00 62.89 C ANISOU 2439 CB TYR A 306 7769 7330 8796 -381 -1127 -445 C ATOM 2440 CG TYR A 306 -114.687-183.248 153.920 1.00 73.18 C ANISOU 2440 CG TYR A 306 8997 8686 10123 -383 -1170 -373 C ATOM 2441 CD1 TYR A 306 -114.717-181.987 154.507 1.00 70.22 C ANISOU 2441 CD1 TYR A 306 8644 8251 9784 -353 -1158 -256 C ATOM 2442 CD2 TYR A 306 -115.666-183.563 152.993 1.00 69.60 C ANISOU 2442 CD2 TYR A 306 8441 8340 9662 -405 -1230 -433 C ATOM 2443 CE1 TYR A 306 -115.693-181.074 154.174 1.00 70.69 C ANISOU 2443 CE1 TYR A 306 8633 8335 9890 -324 -1204 -186 C ATOM 2444 CE2 TYR A 306 -116.642-182.659 152.654 1.00 76.34 C ANISOU 2444 CE2 TYR A 306 9210 9258 10537 -380 -1284 -355 C ATOM 2445 CZ TYR A 306 -116.654-181.424 153.245 1.00 79.25 C ANISOU 2445 CZ TYR A 306 9610 9543 10959 -328 -1270 -224 C ATOM 2446 OH TYR A 306 -117.643-180.552 152.879 1.00 75.74 O ANISOU 2446 OH TYR A 306 9077 9144 10557 -275 -1330 -146 O ATOM 2447 N ILE A 307 -112.063-186.363 156.427 1.00 72.47 N ANISOU 2447 N ILE A 307 9179 8266 10093 -323 -996 -500 N ATOM 2448 CA ILE A 307 -111.110-187.471 156.414 1.00 74.71 C ANISOU 2448 CA ILE A 307 9509 8503 10375 -265 -991 -564 C ATOM 2449 C ILE A 307 -111.062-188.155 157.773 1.00 72.20 C ANISOU 2449 C ILE A 307 9281 8020 10130 -240 -932 -494 C ATOM 2450 O ILE A 307 -111.337-189.355 157.882 1.00 71.01 O ANISOU 2450 O ILE A 307 9174 7723 10084 -244 -908 -534 O ATOM 2451 CB ILE A 307 -109.713-186.987 155.972 1.00 72.59 C ANISOU 2451 CB ILE A 307 9219 8383 9979 -205 -1022 -564 C ATOM 2452 CG1 ILE A 307 -109.762-186.520 154.519 1.00 68.04 C ANISOU 2452 CG1 ILE A 307 8554 7986 9310 -238 -1074 -619 C ATOM 2453 CG2 ILE A 307 -108.679-188.095 156.137 1.00 64.37 C ANISOU 2453 CG2 ILE A 307 8214 7297 8948 -109 -1016 -627 C ATOM 2454 CD1 ILE A 307 -108.627-185.611 154.102 1.00 70.60 C ANISOU 2454 CD1 ILE A 307 8841 8486 9499 -228 -1091 -567 C ATOM 2455 N MET A 308 -110.710-187.404 158.821 1.00 65.92 N ANISOU 2455 N MET A 308 8516 7251 9280 -221 -907 -388 N ATOM 2456 CA MET A 308 -110.601-188.006 160.150 1.00 80.39 C ANISOU 2456 CA MET A 308 10428 8980 11135 -192 -855 -299 C ATOM 2457 C MET A 308 -111.936-188.512 160.677 1.00 80.20 C ANISOU 2457 C MET A 308 10424 8834 11216 -277 -790 -264 C ATOM 2458 O MET A 308 -111.949-189.375 161.560 1.00 87.33 O ANISOU 2458 O MET A 308 11400 9622 12157 -267 -742 -179 O ATOM 2459 CB MET A 308 -109.997-187.013 161.141 1.00 76.20 C ANISOU 2459 CB MET A 308 9905 8550 10496 -167 -847 -224 C ATOM 2460 CG MET A 308 -108.482-187.045 161.175 1.00107.50 C ANISOU 2460 CG MET A 308 13869 12608 14367 -75 -892 -226 C ATOM 2461 SD MET A 308 -107.831-186.652 162.807 1.00138.66 S ANISOU 2461 SD MET A 308 17849 16636 18201 -35 -875 -132 S ATOM 2462 CE MET A 308 -108.471-188.029 163.764 1.00143.00 C ANISOU 2462 CE MET A 308 18494 17028 18811 -7 -819 -13 C ATOM 2463 N MET A 309 -113.053-187.998 160.170 1.00 82.34 N ANISOU 2463 N MET A 309 10620 9135 11529 -359 -788 -312 N ATOM 2464 CA MET A 309 -114.354-188.531 160.544 1.00 89.27 C ANISOU 2464 CA MET A 309 11482 9925 12513 -455 -723 -301 C ATOM 2465 C MET A 309 -114.839-189.611 159.590 1.00 86.94 C ANISOU 2465 C MET A 309 11166 9534 12334 -516 -742 -409 C ATOM 2466 O MET A 309 -115.836-190.278 159.885 1.00 97.21 O ANISOU 2466 O MET A 309 12455 10736 13745 -620 -684 -406 O ATOM 2467 CB MET A 309 -115.381-187.402 160.632 1.00 77.91 C ANISOU 2467 CB MET A 309 9949 8586 11067 -500 -708 -307 C ATOM 2468 CG MET A 309 -115.082-186.446 161.760 1.00 89.69 C ANISOU 2468 CG MET A 309 11464 10140 12472 -458 -668 -235 C ATOM 2469 SD MET A 309 -116.446-185.350 162.174 1.00108.16 S ANISOU 2469 SD MET A 309 13696 12554 14845 -494 -619 -258 S ATOM 2470 CE MET A 309 -115.908-184.837 163.803 1.00118.81 C ANISOU 2470 CE MET A 309 15109 13952 16082 -458 -545 -199 C ATOM 2471 N ASN A 310 -114.165-189.789 158.458 1.00 81.59 N ANISOU 2471 N ASN A 310 10471 8897 11631 -467 -817 -517 N ATOM 2472 CA ASN A 310 -114.399-190.951 157.616 1.00 84.73 C ANISOU 2472 CA ASN A 310 10862 9194 12136 -510 -835 -658 C ATOM 2473 C ASN A 310 -113.930-192.204 158.346 1.00 82.35 C ANISOU 2473 C ASN A 310 10685 8661 11945 -481 -785 -608 C ATOM 2474 O ASN A 310 -112.813-192.245 158.870 1.00 87.90 O ANISOU 2474 O ASN A 310 11460 9349 12588 -360 -790 -525 O ATOM 2475 CB ASN A 310 -113.657-190.789 156.292 1.00 94.28 C ANISOU 2475 CB ASN A 310 12021 10545 13256 -447 -918 -795 C ATOM 2476 CG ASN A 310 -114.060-191.820 155.268 1.00104.10 C ANISOU 2476 CG ASN A 310 13225 11737 14590 -504 -946 -997 C ATOM 2477 OD1 ASN A 310 -113.778-193.010 155.417 1.00105.02 O ANISOU 2477 OD1 ASN A 310 13418 11651 14835 -491 -919 -1062 O ATOM 2478 ND2 ASN A 310 -114.719-191.367 154.209 1.00103.62 N ANISOU 2478 ND2 ASN A 310 13044 11860 14467 -563 -1004 -1103 N ATOM 2479 N LYS A 311 -114.786-193.228 158.387 1.00 93.47 N ANISOU 2479 N LYS A 311 12109 9884 13520 -594 -741 -649 N ATOM 2480 CA LYS A 311 -114.479-194.411 159.186 1.00109.13 C ANISOU 2480 CA LYS A 311 14226 11603 15636 -578 -685 -552 C ATOM 2481 C LYS A 311 -113.252-195.151 158.660 1.00100.24 C ANISOU 2481 C LYS A 311 13164 10376 14546 -428 -738 -644 C ATOM 2482 O LYS A 311 -112.476-195.700 159.452 1.00 88.83 O ANISOU 2482 O LYS A 311 11829 8790 13131 -317 -720 -507 O ATOM 2483 CB LYS A 311 -115.693-195.338 159.229 1.00123.64 C ANISOU 2483 CB LYS A 311 16060 13245 17671 -764 -621 -588 C ATOM 2484 CG LYS A 311 -115.761-196.239 160.453 1.00130.33 C ANISOU 2484 CG LYS A 311 17042 13842 18637 -800 -528 -377 C ATOM 2485 CD LYS A 311 -117.102-196.955 160.511 1.00134.27 C ANISOU 2485 CD LYS A 311 17510 14187 19321 -1032 -450 -401 C ATOM 2486 CE LYS A 311 -117.223-197.835 161.743 1.00130.09 C ANISOU 2486 CE LYS A 311 17117 13410 18902 -1093 -344 -149 C ATOM 2487 NZ LYS A 311 -118.535-198.541 161.790 1.00124.55 N ANISOU 2487 NZ LYS A 311 16373 12557 18392 -1354 -254 -169 N ATOM 2488 N GLN A 312 -113.052-195.162 157.340 1.00107.25 N ANISOU 2488 N GLN A 312 13973 11360 15416 -410 -804 -874 N ATOM 2489 CA GLN A 312 -111.904-195.853 156.759 1.00118.46 C ANISOU 2489 CA GLN A 312 15428 12717 16865 -258 -846 -1004 C ATOM 2490 C GLN A 312 -110.598-195.173 157.149 1.00115.48 C ANISOU 2490 C GLN A 312 15058 12503 16316 -85 -875 -892 C ATOM 2491 O GLN A 312 -109.699-195.805 157.715 1.00114.31 O ANISOU 2491 O GLN A 312 14992 12223 16218 60 -874 -817 O ATOM 2492 CB GLN A 312 -112.039-195.899 155.237 1.00135.34 C ANISOU 2492 CB GLN A 312 17455 14995 18973 -291 -904 -1291 C ATOM 2493 CG GLN A 312 -113.450-196.123 154.733 1.00150.82 C ANISOU 2493 CG GLN A 312 19347 16931 21027 -491 -898 -1417 C ATOM 2494 CD GLN A 312 -113.610-195.722 153.279 1.00161.41 C ANISOU 2494 CD GLN A 312 20546 18547 22237 -520 -972 -1652 C ATOM 2495 OE1 GLN A 312 -112.643-195.706 152.518 1.00160.14 O ANISOU 2495 OE1 GLN A 312 20356 18524 21968 -400 -1014 -1780 O ATOM 2496 NE2 GLN A 312 -114.835-195.385 152.889 1.00167.28 N ANISOU 2496 NE2 GLN A 312 21184 19405 22971 -676 -990 -1704 N ATOM 2497 N PHE A 313 -110.472-193.878 156.837 1.00105.38 N ANISOU 2497 N PHE A 313 13685 11510 14843 -97 -906 -877 N ATOM 2498 CA PHE A 313 -109.225-193.163 157.095 1.00 93.14 C ANISOU 2498 CA PHE A 313 12118 10137 13133 33 -934 -801 C ATOM 2499 C PHE A 313 -108.837-193.231 158.567 1.00 91.07 C ANISOU 2499 C PHE A 313 11948 9784 12871 99 -903 -584 C ATOM 2500 O PHE A 313 -107.653-193.374 158.896 1.00 87.63 O ANISOU 2500 O PHE A 313 11525 9390 12382 249 -930 -544 O ATOM 2501 CB PHE A 313 -109.346-191.705 156.640 1.00 90.88 C ANISOU 2501 CB PHE A 313 11735 10121 12676 -32 -960 -787 C ATOM 2502 CG PHE A 313 -109.116-191.497 155.163 1.00 86.91 C ANISOU 2502 CG PHE A 313 11130 9807 12085 -37 -1008 -963 C ATOM 2503 CD1 PHE A 313 -107.829-191.345 154.662 1.00 87.50 C ANISOU 2503 CD1 PHE A 313 11155 10049 12043 68 -1033 -1023 C ATOM 2504 CD2 PHE A 313 -110.189-191.433 154.280 1.00 81.94 C ANISOU 2504 CD2 PHE A 313 10438 9228 11469 -150 -1027 -1067 C ATOM 2505 CE1 PHE A 313 -107.613-191.150 153.305 1.00 86.82 C ANISOU 2505 CE1 PHE A 313 10967 10178 11844 55 -1066 -1175 C ATOM 2506 CE2 PHE A 313 -109.984-191.237 152.926 1.00 75.89 C ANISOU 2506 CE2 PHE A 313 9572 8678 10583 -154 -1074 -1217 C ATOM 2507 CZ PHE A 313 -108.693-191.096 152.436 1.00 76.42 C ANISOU 2507 CZ PHE A 313 9600 8914 10523 -55 -1088 -1267 C ATOM 2508 N ARG A 314 -109.820-193.141 159.465 1.00 87.91 N ANISOU 2508 N ARG A 314 11595 9292 12513 -8 -848 -445 N ATOM 2509 CA ARG A 314 -109.519-193.067 160.892 1.00 92.29 C ANISOU 2509 CA ARG A 314 12223 9828 13015 41 -816 -232 C ATOM 2510 C ARG A 314 -108.779-194.314 161.365 1.00 94.67 C ANISOU 2510 C ARG A 314 12624 9932 13415 181 -822 -153 C ATOM 2511 O ARG A 314 -107.717-194.220 161.993 1.00 92.41 O ANISOU 2511 O ARG A 314 12350 9732 13029 325 -856 -56 O ATOM 2512 CB ARG A 314 -110.813-192.868 161.684 1.00 91.07 C ANISOU 2512 CB ARG A 314 12089 9625 12890 -110 -740 -119 C ATOM 2513 CG ARG A 314 -110.639-192.175 163.022 1.00 89.95 C ANISOU 2513 CG ARG A 314 11969 9608 12602 -92 -708 55 C ATOM 2514 CD ARG A 314 -111.865-192.365 163.915 1.00102.42 C ANISOU 2514 CD ARG A 314 13578 11115 14223 -226 -611 177 C ATOM 2515 NE ARG A 314 -113.134-192.221 163.201 1.00105.17 N ANISOU 2515 NE ARG A 314 13851 11437 14672 -376 -580 61 N ATOM 2516 CZ ARG A 314 -113.911-193.240 162.839 1.00120.12 C ANISOU 2516 CZ ARG A 314 15764 13134 16743 -478 -543 29 C ATOM 2517 NH1 ARG A 314 -113.549-194.485 163.121 1.00130.53 N ANISOU 2517 NH1 ARG A 314 17195 14221 18180 -444 -527 115 N ATOM 2518 NH2 ARG A 314 -115.048-193.015 162.195 1.00120.32 N ANISOU 2518 NH2 ARG A 314 15690 13188 16838 -614 -528 -90 N ATOM 2519 N ASN A 315 -109.318-195.495 161.051 1.00101.43 N ANISOU 2519 N ASN A 315 13546 10515 14478 145 -795 -200 N ATOM 2520 CA ASN A 315 -108.688-196.740 161.480 1.00 98.68 C ANISOU 2520 CA ASN A 315 13309 9916 14269 288 -801 -111 C ATOM 2521 C ASN A 315 -107.341-196.957 160.803 1.00 91.41 C ANISOU 2521 C ASN A 315 12344 9061 13328 499 -877 -252 C ATOM 2522 O ASN A 315 -106.420-197.504 161.420 1.00101.99 O ANISOU 2522 O ASN A 315 13737 10330 14683 687 -907 -131 O ATOM 2523 CB ASN A 315 -109.617-197.920 161.198 1.00104.61 C ANISOU 2523 CB ASN A 315 14139 10326 15283 174 -750 -159 C ATOM 2524 CG ASN A 315 -111.003-197.719 161.780 1.00108.45 C ANISOU 2524 CG ASN A 315 14636 10779 15790 -55 -664 -42 C ATOM 2525 OD1 ASN A 315 -111.324-196.646 162.292 1.00120.51 O ANISOU 2525 OD1 ASN A 315 16103 12548 17137 -118 -644 43 O ATOM 2526 ND2 ASN A 315 -111.836-198.748 161.695 1.00 95.48 N ANISOU 2526 ND2 ASN A 315 13059 8839 14382 -187 -609 -53 N ATOM 2527 N CYS A 316 -107.206-196.540 159.543 1.00 81.20 N ANISOU 2527 N CYS A 316 10939 7925 11988 478 -909 -501 N ATOM 2528 CA CYS A 316 -105.915-196.652 158.872 1.00 80.69 C ANISOU 2528 CA CYS A 316 10801 7983 11872 667 -967 -649 C ATOM 2529 C CYS A 316 -104.897-195.687 159.465 1.00 86.02 C ANISOU 2529 C CYS A 316 11409 8948 12329 760 -1003 -530 C ATOM 2530 O CYS A 316 -103.708-196.013 159.554 1.00 88.48 O ANISOU 2530 O CYS A 316 11686 9314 12617 959 -1046 -541 O ATOM 2531 CB CYS A 316 -106.082-196.415 157.373 1.00 78.42 C ANISOU 2531 CB CYS A 316 10403 7838 11553 599 -981 -933 C ATOM 2532 SG CYS A 316 -107.029-197.703 156.529 1.00 89.65 S ANISOU 2532 SG CYS A 316 11878 8948 13238 515 -957 -1161 S ATOM 2533 N MET A 317 -105.341-194.498 159.880 1.00 88.99 N ANISOU 2533 N MET A 317 11751 9508 12552 621 -987 -433 N ATOM 2534 CA MET A 317 -104.433-193.557 160.528 1.00 93.33 C ANISOU 2534 CA MET A 317 12239 10313 12909 678 -1018 -336 C ATOM 2535 C MET A 317 -103.962-194.089 161.875 1.00 92.60 C ANISOU 2535 C MET A 317 12225 10147 12813 808 -1031 -125 C ATOM 2536 O MET A 317 -102.779-193.972 162.216 1.00 83.24 O ANISOU 2536 O MET A 317 10978 9126 11524 958 -1086 -97 O ATOM 2537 CB MET A 317 -105.111-192.197 160.688 1.00100.43 C ANISOU 2537 CB MET A 317 13099 11375 13685 497 -994 -299 C ATOM 2538 CG MET A 317 -104.571-191.126 159.753 1.00110.96 C ANISOU 2538 CG MET A 317 14307 12963 14890 455 -1022 -423 C ATOM 2539 SD MET A 317 -105.741-189.806 159.380 1.00111.12 S ANISOU 2539 SD MET A 317 14298 13057 14865 246 -994 -425 S ATOM 2540 CE MET A 317 -106.300-190.318 157.761 1.00 91.01 C ANISOU 2540 CE MET A 317 11708 10479 12391 202 -1003 -608 C ATOM 2541 N VAL A 318 -104.874-194.677 162.652 1.00 97.16 N ANISOU 2541 N VAL A 318 12926 10502 13489 747 -982 33 N ATOM 2542 CA VAL A 318 -104.493-195.270 163.930 1.00100.75 C ANISOU 2542 CA VAL A 318 13467 10886 13928 871 -993 272 C ATOM 2543 C VAL A 318 -103.491-196.396 163.714 1.00102.75 C ANISOU 2543 C VAL A 318 13740 10997 14302 1114 -1051 261 C ATOM 2544 O VAL A 318 -102.492-196.508 164.435 1.00106.36 O ANISOU 2544 O VAL A 318 14179 11569 14665 1297 -1111 386 O ATOM 2545 CB VAL A 318 -105.742-195.764 164.682 1.00101.62 C ANISOU 2545 CB VAL A 318 13704 10776 14131 734 -911 452 C ATOM 2546 CG1 VAL A 318 -105.340-196.522 165.928 1.00102.45 C ANISOU 2546 CG1 VAL A 318 13911 10795 14220 870 -922 732 C ATOM 2547 CG2 VAL A 318 -106.638-194.591 165.035 1.00 95.42 C ANISOU 2547 CG2 VAL A 318 12874 10172 13208 534 -856 458 C ATOM 2548 N THR A 319 -103.738-197.239 162.709 1.00102.14 N ANISOU 2548 N THR A 319 13692 10681 14437 1128 -1037 93 N ATOM 2549 CA THR A 319 -102.819-198.330 162.410 1.00 99.26 C ANISOU 2549 CA THR A 319 13342 10150 14222 1377 -1087 37 C ATOM 2550 C THR A 319 -101.452-197.803 161.991 1.00 91.88 C ANISOU 2550 C THR A 319 12241 9537 13131 1545 -1158 -99 C ATOM 2551 O THR A 319 -100.417-198.355 162.384 1.00 86.47 O ANISOU 2551 O THR A 319 11537 8857 12462 1795 -1220 -31 O ATOM 2552 CB THR A 319 -103.414-199.217 161.317 1.00 96.28 C ANISOU 2552 CB THR A 319 13010 9476 14096 1330 -1053 -184 C ATOM 2553 OG1 THR A 319 -104.573-199.889 161.828 1.00115.36 O ANISOU 2553 OG1 THR A 319 15581 11562 16691 1184 -987 -34 O ATOM 2554 CG2 THR A 319 -102.407-200.237 160.865 1.00 90.87 C ANISOU 2554 CG2 THR A 319 12318 8640 13570 1602 -1102 -310 C ATOM 2555 N THR A 320 -101.427-196.732 161.197 1.00 89.24 N ANISOU 2555 N THR A 320 11777 9483 12647 1412 -1150 -278 N ATOM 2556 CA THR A 320 -100.158-196.173 160.742 1.00 85.61 C ANISOU 2556 CA THR A 320 11142 9350 12034 1528 -1200 -408 C ATOM 2557 C THR A 320 -99.410-195.496 161.885 1.00 91.62 C ANISOU 2557 C THR A 320 11849 10359 12602 1585 -1249 -223 C ATOM 2558 O THR A 320 -98.192-195.667 162.028 1.00 96.67 O ANISOU 2558 O THR A 320 12382 11164 13185 1789 -1312 -238 O ATOM 2559 CB THR A 320 -100.411-195.196 159.592 1.00 86.35 C ANISOU 2559 CB THR A 320 11126 9661 12020 1343 -1170 -608 C ATOM 2560 OG1 THR A 320 -100.824-195.931 158.432 1.00 77.49 O ANISOU 2560 OG1 THR A 320 10015 8381 11045 1339 -1144 -825 O ATOM 2561 CG2 THR A 320 -99.161-194.383 159.264 1.00 84.47 C ANISOU 2561 CG2 THR A 320 10702 9802 11591 1398 -1204 -694 C ATOM 2562 N LEU A 321 -100.119-194.744 162.719 1.00 90.12 N ANISOU 2562 N LEU A 321 11717 10216 12309 1412 -1223 -67 N ATOM 2563 CA LEU A 321 -99.482-194.045 163.826 1.00 98.84 C ANISOU 2563 CA LEU A 321 12765 11578 13214 1440 -1269 74 C ATOM 2564 C LEU A 321 -98.985-195.019 164.891 1.00108.35 C ANISOU 2564 C LEU A 321 14035 12692 14441 1666 -1325 288 C ATOM 2565 O LEU A 321 -97.924-194.811 165.480 1.00105.89 O ANISOU 2565 O LEU A 321 13619 12632 13984 1806 -1402 340 O ATOM 2566 CB LEU A 321 -100.443-193.026 164.443 1.00 98.81 C ANISOU 2566 CB LEU A 321 12807 11634 13102 1205 -1217 154 C ATOM 2567 CG LEU A 321 -100.762-191.829 163.542 1.00 96.30 C ANISOU 2567 CG LEU A 321 12406 11453 12731 1004 -1182 -19 C ATOM 2568 CD1 LEU A 321 -101.766-190.897 164.204 1.00 92.85 C ANISOU 2568 CD1 LEU A 321 12020 11033 12224 807 -1132 53 C ATOM 2569 CD2 LEU A 321 -99.488-191.080 163.157 1.00 85.44 C ANISOU 2569 CD2 LEU A 321 10858 10387 11221 1039 -1233 -138 C ATOM 2570 N CYS A 322 -99.742-196.087 165.129 1.00119.18 N ANISOU 2570 N CYS A 322 15574 13711 15997 1698 -1290 421 N ATOM 2571 CA CYS A 322 -99.352-197.068 166.117 1.00127.06 C ANISOU 2571 CA CYS A 322 16659 14581 17036 1913 -1340 671 C ATOM 2572 C CYS A 322 -98.518-198.240 165.597 1.00126.88 C ANISOU 2572 C CYS A 322 16629 14370 17210 2201 -1397 615 C ATOM 2573 O CYS A 322 -98.509-199.353 166.131 1.00139.51 O ANISOU 2573 O CYS A 322 18356 15691 18962 2372 -1419 816 O ATOM 2574 CB CYS A 322 -100.476-197.619 167.001 1.00134.02 C ANISOU 2574 CB CYS A 322 17734 15199 17989 1812 -1276 936 C ATOM 2575 SG CYS A 322 -101.660-196.440 167.596 1.00136.91 S ANISOU 2575 SG CYS A 322 18118 15728 18174 1491 -1186 983 S ATOM 2576 N CYS A 323 -97.802-197.965 164.511 1.00115.37 N ANISOU 2576 N CYS A 323 15014 13071 15751 2256 -1416 332 N ATOM 2577 CA CYS A 323 -96.820-198.891 163.945 1.00116.05 C ANISOU 2577 CA CYS A 323 15034 13075 15986 2552 -1472 211 C ATOM 2578 C CYS A 323 -97.407-200.248 163.564 1.00109.30 C ANISOU 2578 C CYS A 323 14350 11719 15459 2637 -1437 202 C ATOM 2579 O CYS A 323 -96.777-201.282 163.777 1.00113.60 O ANISOU 2579 O CYS A 323 14929 12068 16166 2927 -1494 274 O ATOM 2580 CB CYS A 323 -95.665-199.101 164.927 1.00128.48 C ANISOU 2580 CB CYS A 323 16529 14838 17449 2829 -1583 399 C ATOM 2581 SG CYS A 323 -95.056-197.591 165.699 1.00134.24 S ANISOU 2581 SG CYS A 323 17079 16128 17800 2707 -1634 446 S ATOM 2582 N GLY A 324 -98.614-200.242 163.003 1.00103.80 N ANISOU 2582 N GLY A 324 13756 10810 14873 2385 -1347 108 N ATOM 2583 CA GLY A 324 -99.229-201.450 162.500 1.00 92.31 C ANISOU 2583 CA GLY A 324 12446 8888 13741 2411 -1305 35 C ATOM 2584 C GLY A 324 -100.101-202.195 163.485 1.00108.40 C ANISOU 2584 C GLY A 324 14704 10550 15932 2351 -1270 353 C ATOM 2585 O GLY A 324 -100.795-203.137 163.082 1.00118.90 O ANISOU 2585 O GLY A 324 16166 11462 17548 2302 -1220 294 O ATOM 2586 N LYS A 325 -100.093-201.807 164.757 1.00120.63 N ANISOU 2586 N LYS A 325 16291 12247 17295 2339 -1290 681 N ATOM 2587 CA LYS A 325 -100.878-202.464 165.789 1.00134.55 C ANISOU 2587 CA LYS A 325 18253 13713 19157 2275 -1248 1028 C ATOM 2588 C LYS A 325 -102.060-201.589 166.189 1.00142.45 C ANISOU 2588 C LYS A 325 19278 14851 19996 1934 -1158 1103 C ATOM 2589 O LYS A 325 -101.993-200.358 166.120 1.00138.88 O ANISOU 2589 O LYS A 325 18691 14784 19292 1817 -1161 992 O ATOM 2590 CB LYS A 325 -100.019-202.772 167.021 1.00134.81 C ANISOU 2590 CB LYS A 325 18311 13834 19076 2534 -1337 1373 C ATOM 2591 CG LYS A 325 -98.947-203.833 166.803 1.00142.62 C ANISOU 2591 CG LYS A 325 19301 14614 20273 2912 -1429 1367 C ATOM 2592 CD LYS A 325 -99.539-205.236 166.798 1.00148.06 C ANISOU 2592 CD LYS A 325 20216 14694 21348 2954 -1384 1502 C ATOM 2593 CE LYS A 325 -98.453-206.305 166.834 1.00155.85 C ANISOU 2593 CE LYS A 325 21221 15449 22546 3375 -1486 1568 C ATOM 2594 NZ LYS A 325 -97.595-206.285 165.617 1.00158.79 N ANISOU 2594 NZ LYS A 325 21414 15926 22994 3557 -1528 1132 N ATOM 2595 N ASN A 326 -103.140-202.244 166.609 1.00155.35 N ANISOU 2595 N ASN A 326 21080 16154 21792 1775 -1074 1290 N ATOM 2596 CA ASN A 326 -104.365-201.572 167.042 1.00157.73 C ANISOU 2596 CA ASN A 326 21403 16553 21973 1460 -974 1372 C ATOM 2597 C ASN A 326 -104.898-200.628 165.968 1.00156.26 C ANISOU 2597 C ASN A 326 21089 16547 21737 1256 -940 1028 C ATOM 2598 O ASN A 326 -106.099-200.368 165.898 1.00157.05 O ANISOU 2598 O ASN A 326 21208 16602 21863 995 -852 1006 O ATOM 2599 CB ASN A 326 -104.128-200.807 168.347 1.00156.73 C ANISOU 2599 CB ASN A 326 21246 16785 21518 1469 -992 1636 C ATOM 2600 CG ASN A 326 -105.410-200.253 168.940 1.00155.26 C ANISOU 2600 CG ASN A 326 21090 16679 21221 1172 -877 1742 C ATOM 2601 OD1 ASN A 326 -105.900-199.205 168.519 1.00150.24 O ANISOU 2601 OD1 ASN A 326 20347 16264 20473 996 -843 1532 O ATOM 2602 ND2 ASN A 326 -105.957-200.954 169.927 1.00158.15 N ANISOU 2602 ND2 ASN A 326 21598 16873 21620 1121 -815 2079 N TER 2603 ASN A 326 HETATM 2604 C1 NAG B 1 -95.802-140.784 152.491 1.00 60.72 C HETATM 2605 C2 NAG B 1 -95.103-141.441 151.289 1.00 60.16 C HETATM 2606 C3 NAG B 1 -93.587-141.218 151.345 1.00 59.67 C HETATM 2607 C4 NAG B 1 -93.213-139.777 151.666 1.00 67.26 C HETATM 2608 C5 NAG B 1 -94.020-139.250 152.846 1.00 70.82 C HETATM 2609 C6 NAG B 1 -93.826-137.768 153.067 1.00 69.66 C HETATM 2610 C7 NAG B 1 -95.739-143.534 150.156 1.00 65.27 C HETATM 2611 C8 NAG B 1 -95.949-145.010 150.321 1.00 56.73 C HETATM 2612 N2 NAG B 1 -95.383-142.868 151.258 1.00 56.32 N HETATM 2613 O3 NAG B 1 -93.015-141.583 150.093 1.00 59.26 O HETATM 2614 O4 NAG B 1 -91.841-139.771 152.039 1.00 70.74 O HETATM 2615 O5 NAG B 1 -95.415-139.438 152.588 1.00 62.48 O HETATM 2616 O6 NAG B 1 -94.107-137.055 151.870 1.00 66.50 O HETATM 2617 O7 NAG B 1 -95.897-142.971 149.078 1.00 62.43 O HETATM 2618 C1 NAG B 2 -91.023-138.862 151.282 1.00 63.00 C HETATM 2619 C2 NAG B 2 -89.799-138.620 152.153 1.00 57.72 C HETATM 2620 C3 NAG B 2 -88.815-137.693 151.445 1.00 63.69 C HETATM 2621 C4 NAG B 2 -88.451-138.272 150.080 1.00 61.03 C HETATM 2622 C5 NAG B 2 -89.734-138.502 149.286 1.00 56.72 C HETATM 2623 C6 NAG B 2 -89.499-139.129 147.931 1.00 57.78 C HETATM 2624 C7 NAG B 2 -90.158-138.789 154.580 1.00 72.53 C HETATM 2625 C8 NAG B 2 -90.587-138.064 155.823 1.00 65.53 C HETATM 2626 N2 NAG B 2 -90.177-138.075 153.448 1.00 69.97 N HETATM 2627 O3 NAG B 2 -87.692-137.563 152.310 1.00 66.18 O HETATM 2628 O4 NAG B 2 -87.616-137.442 149.272 1.00 66.39 O HETATM 2629 O5 NAG B 2 -90.615-139.375 150.009 1.00 60.37 O HETATM 2630 O6 NAG B 2 -90.658-139.051 147.112 1.00 60.42 O HETATM 2631 O7 NAG B 2 -89.808-139.965 154.601 1.00 84.57 O HETATM 2632 C1 BMA B 3 -86.456-136.829 149.895 1.00 96.69 C HETATM 2633 C2 BMA B 3 -85.411-137.930 150.262 1.00122.41 C HETATM 2634 C3 BMA B 3 -84.060-137.247 150.344 1.00131.73 C HETATM 2635 C4 BMA B 3 -83.615-136.812 148.941 1.00128.71 C HETATM 2636 C5 BMA B 3 -84.768-136.103 148.171 1.00115.10 C HETATM 2637 C6 BMA B 3 -85.280-136.874 146.960 1.00115.50 C HETATM 2638 O2 BMA B 3 -85.344-138.961 149.283 1.00138.57 O HETATM 2639 O3 BMA B 3 -83.057-138.074 150.964 1.00138.67 O HETATM 2640 O4 BMA B 3 -82.513-135.925 149.038 1.00139.18 O HETATM 2641 O5 BMA B 3 -85.888-135.776 149.041 1.00108.41 O HETATM 2642 O6 BMA B 3 -84.388-136.654 145.899 1.00115.57 O HETATM 2643 C1 MAN B 4 -82.717-137.756 152.356 1.00143.05 C HETATM 2644 C2 MAN B 4 -83.815-136.800 153.074 1.00140.27 C HETATM 2645 C3 MAN B 4 -83.407-135.307 153.220 1.00140.12 C HETATM 2646 C4 MAN B 4 -81.894-135.116 153.360 1.00148.05 C HETATM 2647 C5 MAN B 4 -81.222-135.820 152.197 1.00144.99 C HETATM 2648 C6 MAN B 4 -79.742-135.535 152.094 1.00136.35 C HETATM 2649 O2 MAN B 4 -84.127-137.257 154.393 1.00140.91 O HETATM 2650 O3 MAN B 4 -84.092-134.685 154.308 1.00127.96 O HETATM 2651 O4 MAN B 4 -81.571-133.735 153.321 1.00152.08 O HETATM 2652 O5 MAN B 4 -81.368-137.226 152.413 1.00146.64 O HETATM 2653 O6 MAN B 4 -79.243-136.240 150.962 1.00132.38 O HETATM 2654 C1 MAN B 5 -84.578-135.300 145.455 1.00134.66 C HETATM 2655 C2 MAN B 5 -85.094-135.390 143.998 1.00146.51 C HETATM 2656 C3 MAN B 5 -84.959-134.065 143.227 1.00155.46 C HETATM 2657 C4 MAN B 5 -83.708-133.213 143.603 1.00156.98 C HETATM 2658 C5 MAN B 5 -83.354-133.257 145.113 1.00149.44 C HETATM 2659 C6 MAN B 5 -84.211-132.373 146.057 1.00144.90 C HETATM 2660 O2 MAN B 5 -86.497-135.677 143.985 1.00146.76 O HETATM 2661 O3 MAN B 5 -86.147-133.277 143.326 1.00156.41 O HETATM 2662 O4 MAN B 5 -82.588-133.665 142.853 1.00163.09 O HETATM 2663 O5 MAN B 5 -83.363-134.613 145.583 1.00143.52 O HETATM 2664 O6 MAN B 5 -85.538-132.219 145.552 1.00135.74 O HETATM 2665 C1 PLM A 401 -100.857-195.219 168.537 1.00142.52 C ANISOU 2665 C1 PLM A 401 18693 16914 18545 1501 -1251 1016 C HETATM 2666 O2 PLM A 401 -101.211-194.044 168.621 1.00152.55 O ANISOU 2666 O2 PLM A 401 19898 18390 19673 1315 -1217 913 O HETATM 2667 C2 PLM A 401 -99.707-195.779 169.325 1.00136.70 C ANISOU 2667 C2 PLM A 401 17925 16302 17712 1767 -1358 1190 C HETATM 2668 C3 PLM A 401 -98.526-194.827 169.313 1.00125.31 C ANISOU 2668 C3 PLM A 401 16280 15269 16064 1823 -1446 1035 C HETATM 2669 C4 PLM A 401 -98.488-193.935 170.534 1.00116.24 C ANISOU 2669 C4 PLM A 401 15086 14453 14628 1734 -1466 1128 C HETATM 2670 C5 PLM A 401 -98.541-192.470 170.155 1.00112.58 C ANISOU 2670 C5 PLM A 401 14502 14218 14057 1512 -1437 878 C HETATM 2671 C6 PLM A 401 -98.794-191.623 171.384 1.00110.33 C ANISOU 2671 C6 PLM A 401 14202 14195 13522 1392 -1430 939 C HETATM 2672 C7 PLM A 401 -98.116-190.270 171.319 1.00104.91 C ANISOU 2672 C7 PLM A 401 13343 13833 12684 1279 -1469 709 C HETATM 2673 C8 PLM A 401 -98.908-189.269 170.502 1.00102.04 C ANISOU 2673 C8 PLM A 401 12987 13364 12421 1037 -1376 511 C HETATM 2674 C9 PLM A 401 -98.679-187.854 170.993 1.00 96.11 C ANISOU 2674 C9 PLM A 401 12129 12888 11500 875 -1384 352 C HETATM 2675 CA PLM A 401 -99.192-186.828 170.002 1.00 99.78 C ANISOU 2675 CA PLM A 401 12579 13241 12090 673 -1316 160 C HETATM 2676 CB PLM A 401 -99.324-185.459 170.636 1.00105.26 C ANISOU 2676 CB PLM A 401 13220 14108 12665 496 -1298 20 C HETATM 2677 CC PLM A 401 -98.053-184.646 170.490 1.00107.55 C ANISOU 2677 CC PLM A 401 13339 14652 12874 453 -1373 -142 C HETATM 2678 CD PLM A 401 -98.172-183.341 171.245 1.00104.88 C ANISOU 2678 CD PLM A 401 12956 14462 12430 276 -1359 -298 C HETATM 2679 CE PLM A 401 -97.152-182.315 170.798 1.00 97.37 C ANISOU 2679 CE PLM A 401 11850 13667 11478 150 -1402 -491 C HETATM 2680 CF PLM A 401 -97.555-180.942 171.295 1.00 91.32 C ANISOU 2680 CF PLM A 401 11080 12916 10700 -56 -1361 -671 C HETATM 2681 CG PLM A 401 -96.525-179.886 170.994 1.00 82.36 C ANISOU 2681 CG PLM A 401 9794 11928 9572 -214 -1401 -861 C HETATM 2682 C1 BOG A 407 -108.437-166.508 150.588 1.00 81.64 C HETATM 2683 O1 BOG A 407 -109.029-167.416 151.506 1.00 83.56 O HETATM 2684 C2 BOG A 407 -108.776-165.078 150.992 1.00 77.50 C HETATM 2685 O2 BOG A 407 -110.199-164.911 150.918 1.00 67.82 O HETATM 2686 C3 BOG A 407 -108.044-164.072 150.109 1.00 79.67 C HETATM 2687 O3 BOG A 407 -108.277-162.739 150.579 1.00 88.52 O HETATM 2688 C4 BOG A 407 -106.550-164.365 150.149 1.00 77.07 C HETATM 2689 O4 BOG A 407 -105.870-163.534 149.204 1.00 74.77 O HETATM 2690 C5 BOG A 407 -106.282-165.822 149.784 1.00 80.84 C HETATM 2691 O5 BOG A 407 -107.027-166.720 150.607 1.00 73.43 O HETATM 2692 C6 BOG A 407 -104.805-166.171 149.940 1.00 74.49 C HETATM 2693 O6 BOG A 407 -104.421-166.091 151.320 1.00 79.83 O HETATM 2694 C1' BOG A 407 -108.947-168.748 151.013 1.00 83.77 C HETATM 2695 C2' BOG A 407 -109.907-169.619 151.809 1.00 88.23 C HETATM 2696 C3' BOG A 407 -110.051-170.993 151.168 1.00 88.95 C HETATM 2697 C4' BOG A 407 -111.227-171.748 151.774 1.00 90.49 C HETATM 2698 C5' BOG A 407 -111.376-173.115 151.116 1.00 90.67 C HETATM 2699 C6' BOG A 407 -112.487-173.923 151.773 1.00 89.54 C HETATM 2700 C7' BOG A 407 -113.841-173.258 151.569 1.00 90.15 C HETATM 2701 C8' BOG A 407 -114.940-174.084 152.197 1.00 83.86 C HETATM 2702 C1 BOG A 408 -85.335-158.127 161.158 1.00118.62 C HETATM 2703 O1 BOG A 408 -85.311-159.432 160.583 1.00106.59 O HETATM 2704 C2 BOG A 408 -83.995-157.459 160.872 1.00124.09 C HETATM 2705 O2 BOG A 408 -82.944-158.198 161.501 1.00127.68 O HETATM 2706 C3 BOG A 408 -83.978-156.028 161.376 1.00125.16 C HETATM 2707 O3 BOG A 408 -82.751-155.400 160.994 1.00129.05 O HETATM 2708 C4 BOG A 408 -85.142-155.271 160.764 1.00127.27 C HETATM 2709 O4 BOG A 408 -85.188-153.965 161.347 1.00126.54 O HETATM 2710 C5 BOG A 408 -86.456-156.000 161.031 1.00129.27 C HETATM 2711 O5 BOG A 408 -86.413-157.367 160.604 1.00127.35 O HETATM 2712 C6 BOG A 408 -87.614-155.297 160.329 1.00113.53 C HETATM 2713 O6 BOG A 408 -88.814-155.499 161.082 1.00102.19 O HETATM 2714 C1' BOG A 408 -86.280-160.314 161.142 1.00 92.78 C HETATM 2715 C2' BOG A 408 -86.025-161.713 160.598 1.00 83.92 C HETATM 2716 C3' BOG A 408 -87.125-162.669 161.042 1.00 87.39 C HETATM 2717 C4' BOG A 408 -86.898-164.073 160.493 1.00 81.20 C HETATM 2718 C5' BOG A 408 -87.891-165.042 161.122 1.00 82.65 C HETATM 2719 C6' BOG A 408 -87.680-166.475 160.646 1.00 87.52 C HETATM 2720 C7' BOG A 408 -88.669-167.392 161.356 1.00 94.11 C HETATM 2721 C8' BOG A 408 -88.607-168.815 160.848 1.00 92.99 C HETATM 2722 C1 BOG A 409 -104.511-159.837 158.035 1.00 94.17 C HETATM 2723 O1 BOG A 409 -105.272-158.683 158.376 1.00 89.83 O HETATM 2724 C2 BOG A 409 -105.311-160.742 157.103 1.00103.35 C HETATM 2725 O2 BOG A 409 -106.541-161.119 157.730 1.00104.72 O HETATM 2726 C3 BOG A 409 -104.519-161.989 156.763 1.00101.47 C HETATM 2727 O3 BOG A 409 -105.220-162.726 155.756 1.00 95.94 O HETATM 2728 C4 BOG A 409 -103.156-161.575 156.233 1.00 94.15 C HETATM 2729 O4 BOG A 409 -102.356-162.749 156.051 1.00 89.67 O HETATM 2730 C5 BOG A 409 -102.442-160.597 157.168 1.00 87.42 C HETATM 2731 O5 BOG A 409 -103.263-159.464 157.452 1.00 86.12 O HETATM 2732 C6 BOG A 409 -101.115-160.112 156.584 1.00 74.97 C HETATM 2733 O6 BOG A 409 -101.283-159.605 155.252 1.00 68.26 O HETATM 2734 C1' BOG A 409 -105.308-158.539 159.794 1.00 94.38 C HETATM 2735 C2' BOG A 409 -106.746-158.787 160.228 1.00102.57 C HETATM 2736 C3' BOG A 409 -106.858-159.415 161.610 1.00105.70 C HETATM 2737 C4' BOG A 409 -108.244-160.033 161.767 1.00107.86 C HETATM 2738 C5' BOG A 409 -108.359-160.826 163.062 1.00101.52 C HETATM 2739 C6' BOG A 409 -108.545-159.899 164.255 1.00102.58 C HETATM 2740 C7' BOG A 409 -108.621-160.709 165.540 1.00101.30 C HETATM 2741 C8' BOG A 409 -109.654-161.806 165.420 1.00101.18 C HETATM 2742 C1 BOG A 410 -133.919-183.824 159.395 1.00129.00 C HETATM 2743 O1 BOG A 410 -132.726-183.095 159.127 1.00117.94 O HETATM 2744 C2 BOG A 410 -133.903-184.382 160.815 1.00126.77 C HETATM 2745 O2 BOG A 410 -132.857-185.349 160.954 1.00116.55 O HETATM 2746 C3 BOG A 410 -135.231-185.044 161.150 1.00138.47 C HETATM 2747 O3 BOG A 410 -135.244-185.408 162.535 1.00138.31 O HETATM 2748 C4 BOG A 410 -136.385-184.094 160.857 1.00145.16 C HETATM 2749 O4 BOG A 410 -137.624-184.793 161.017 1.00148.53 O HETATM 2750 C5 BOG A 410 -136.297-183.548 159.436 1.00144.13 C HETATM 2751 O5 BOG A 410 -135.026-182.942 159.204 1.00139.94 O HETATM 2752 C6 BOG A 410 -137.381-182.509 159.186 1.00144.74 C HETATM 2753 O6 BOG A 410 -137.187-181.926 157.893 1.00143.88 O HETATM 2754 C1' BOG A 410 -132.795-182.522 157.825 1.00104.01 C HETATM 2755 C2' BOG A 410 -131.562-181.668 157.576 1.00 96.34 C HETATM 2756 C3' BOG A 410 -131.220-181.695 156.095 1.00 88.44 C HETATM 2757 C4' BOG A 410 -130.105-180.709 155.779 1.00 84.65 C HETATM 2758 C5' BOG A 410 -129.621-180.923 154.351 1.00 86.39 C HETATM 2759 C6' BOG A 410 -128.765-179.752 153.892 1.00 90.45 C HETATM 2760 C7' BOG A 410 -128.295-179.967 152.463 1.00 93.80 C HETATM 2761 C8' BOG A 410 -127.743-178.681 151.899 1.00 92.28 C HETATM 2762 C11 DOK A 411 -116.997-161.916 147.785 1.00 81.61 C HETATM 2763 C15 DOK A 411 -118.550-160.262 147.185 1.00 83.69 C HETATM 2764 C16 DOK A 411 -117.871-160.044 145.998 1.00 85.93 C HETATM 2765 C17 DOK A 411 -116.716-160.765 145.657 1.00 92.68 C HETATM 2766 C18 DOK A 411 -112.110-167.281 147.332 1.00 80.53 C HETATM 2767 C19 DOK A 411 -113.026-167.811 149.607 1.00 64.38 C HETATM 2768 C20 DOK A 411 -114.266-168.536 147.660 1.00 65.10 C HETATM 2769 C21 DOK A 411 -110.763-168.044 147.498 1.00 84.94 C HETATM 2770 C22 DOK A 411 -113.983-168.373 150.433 1.00 56.56 C HETATM 2771 C23 DOK A 411 -115.234-169.107 148.482 1.00 61.54 C HETATM 2772 C24 DOK A 411 -110.957-169.568 147.469 1.00 84.09 C HETATM 2773 C25 DOK A 411 -109.781-167.648 146.388 1.00 82.39 C HETATM 2774 C26 DOK A 411 -115.070-169.013 149.849 1.00 74.45 C HETATM 2775 C1 DOK A 411 -112.761-163.465 147.759 1.00 73.14 C HETATM 2776 C2 DOK A 411 -113.989-162.989 148.536 1.00 77.73 C HETATM 2777 C3 DOK A 411 -115.241-163.300 147.727 1.00 82.17 C HETATM 2778 C4 DOK A 411 -115.343-164.790 147.384 1.00 74.38 C HETATM 2779 C5 DOK A 411 -114.086-165.178 146.585 1.00 70.03 C HETATM 2780 N6 DOK A 411 -112.887-164.882 147.378 1.00 78.86 N HETATM 2781 C7 DOK A 411 -111.926-165.827 147.757 1.00 83.22 C HETATM 2782 O8 DOK A 411 -110.952-165.482 148.429 1.00 79.05 O HETATM 2783 C9 DOK A 411 -113.159-167.892 148.222 1.00 67.73 C HETATM 2784 O10 DOK A 411 -116.368-162.896 148.499 1.00 84.07 O HETATM 2785 C12 DOK A 411 -116.307-161.696 146.581 1.00 85.24 C HETATM 2786 O13 DOK A 411 -115.228-162.536 146.519 1.00 76.87 O HETATM 2787 C14 DOK A 411 -118.125-161.217 148.121 1.00 80.44 C HETATM 2788 CL DOK A 411 -116.262-169.719 150.883 1.00 86.32 CL HETATM 2789 O HOH A 501 -94.302-170.735 152.464 1.00137.12 O HETATM 2790 O HOH A 502 -112.049-170.646 137.765 1.00134.28 O HETATM 2791 O HOH A 503 -103.274-165.841 147.274 1.00136.95 O HETATM 2792 O HOH A 504 -107.417-160.662 148.563 1.00 74.04 O HETATM 2793 O HOH A 505 -100.669-140.569 158.241 1.00 73.67 O HETATM 2794 O HOH A 506 -107.285-146.644 138.983 1.00112.04 O HETATM 2795 O HOH A 507 -104.063-162.834 152.749 1.00 96.81 O HETATM 2796 O HOH A 508 -105.545-166.158 153.576 1.00106.22 O HETATM 2797 O HOH A 509 -112.874-186.795 141.568 1.00 79.05 O HETATM 2798 O HOH A 510 -133.279-186.372 145.770 1.00 93.86 O HETATM 2799 O HOH A 511 -106.475-164.003 146.924 1.00 64.41 O HETATM 2800 O HOH A 512 -100.809-153.498 149.462 1.00 59.33 O HETATM 2801 O HOH A 513 -92.328-150.407 146.580 1.00 73.71 O HETATM 2802 O HOH A 514 -88.786-159.175 163.975 1.00 70.49 O HETATM 2803 O HOH A 515 -113.040-191.570 152.428 1.00138.24 O HETATM 2804 O HOH A 516 -107.936-167.261 153.705 1.00 88.49 O HETATM 2805 O HOH A 517 -110.745-140.994 149.003 0.50106.48 O HETATM 2806 O HOH A 518 -100.943-159.163 140.129 1.00 78.84 O HETATM 2807 O HOH A 519 -83.207-159.487 163.652 1.00 85.97 O HETATM 2808 O HOH A 520 -98.199-155.994 144.528 1.00110.95 O HETATM 2809 O HOH A 521 -101.320-161.336 145.826 1.00165.79 O HETATM 2810 O HOH A 522 -118.101-178.259 154.107 1.00 66.42 O HETATM 2811 O HOH A 523 -103.051-158.160 136.550 1.00 89.65 O HETATM 2812 O HOH A 524 -111.500-161.133 153.830 1.00 87.47 O HETATM 2813 O HOH A 525 -89.719-139.714 144.806 1.00 64.62 O HETATM 2814 O HOH A 526 -106.239-161.718 153.609 1.00116.32 O HETATM 2815 O HOH A 527 -96.487-144.638 147.172 1.00 59.12 O HETATM 2816 O HOH A 528 -102.220-164.574 151.325 1.00 81.18 O HETATM 2817 O HOH A 529 -101.519-148.942 142.120 1.00 69.42 O HETATM 2818 O HOH A 530 -104.037-153.696 150.730 1.00 65.63 O HETATM 2819 O HOH A 531 -92.675-157.915 162.988 1.00 70.25 O HETATM 2820 O HOH A 532 -109.371-164.234 146.520 1.00 87.76 O HETATM 2821 O HOH A 533 -113.477-170.562 158.085 1.00 84.53 O HETATM 2822 O HOH A 534 -96.977-164.408 152.831 1.00 70.42 O HETATM 2823 O HOH A 535 -114.996-174.367 155.398 1.00130.66 O HETATM 2824 O HOH A 536 -100.962-133.998 158.463 1.00112.16 O HETATM 2825 O HOH A 537 -102.737-148.821 144.313 1.00 80.72 O HETATM 2826 O HOH A 538 -139.008-202.694 152.957 1.00 83.15 O HETATM 2827 O HOH A 539 -95.376-154.427 170.157 1.00 68.05 O HETATM 2828 O HOH A 540 -110.563-157.277 141.316 1.00 83.48 O HETATM 2829 O HOH A 541 -114.450-166.645 156.509 1.00 71.81 O HETATM 2830 O HOH A 542 -98.559-140.138 150.055 1.00 59.77 O HETATM 2831 O HOH A 543 -114.810-168.136 158.710 1.00 70.68 O HETATM 2832 O HOH A 544 -101.587-166.855 154.059 1.00 85.27 O HETATM 2833 O HOH A 545 -102.754-141.096 145.828 1.00 66.57 O HETATM 2834 O HOH A 546 -112.997-188.519 143.965 1.00 78.53 O HETATM 2835 O HOH A 547 -92.573-135.890 149.824 1.00 65.23 O HETATM 2836 O HOH A 548 -137.961-193.765 158.420 1.00 95.05 O HETATM 2837 O HOH A 549 -91.404-148.226 158.591 1.00 79.50 O HETATM 2838 O HOH A 550 -93.131-158.115 168.903 1.00 66.50 O HETATM 2839 O HOH A 551 -109.686-176.355 152.936 1.00 72.14 O HETATM 2840 O HOH A 552 -118.452-181.462 150.167 1.00 62.48 O HETATM 2841 O HOH A 553 -114.887-195.353 144.643 1.00 95.99 O HETATM 2842 O HOH A 554 -141.233-198.876 156.120 1.00 77.27 O HETATM 2843 O HOH A 555 -92.942-145.520 159.489 1.00 79.74 O HETATM 2844 O HOH A 556 -105.993-154.443 152.591 1.00 81.39 O HETATM 2845 O HOH A 557 -90.430-135.153 153.328 1.00 72.13 O HETATM 2846 O HOH A 558 -116.274-176.611 154.657 1.00 73.01 O HETATM 2847 O HOH A 559 -92.821-148.718 161.056 1.00 89.65 O HETATM 2848 O HOH A 560 -92.200-136.514 147.301 1.00 69.50 O HETATM 2849 O HOH A 561 -134.906-193.039 147.398 1.00 90.25 O HETATM 2850 O HOH A 562 -87.574-138.286 144.969 1.00 77.30 O HETATM 2851 O HOH A 563 -101.368-141.872 147.842 1.00 62.23 O HETATM 2852 O HOH A 564 -100.441-199.061 158.529 1.00103.16 O HETATM 2853 O HOH A 565 -131.364-204.788 159.978 1.00 86.50 O HETATM 2854 O HOH A 566 -92.680-158.174 165.436 1.00 66.01 O HETATM 2855 O HOH A 567 -112.505-151.435 137.279 1.00 94.97 O HETATM 2856 O HOH A 568 -136.900-187.613 159.506 1.00106.31 O HETATM 2857 O HOH A 569 -138.771-185.716 158.079 1.00134.67 O HETATM 2858 O HOH A 570 -96.523-196.785 167.714 1.00131.49 O HETATM 2859 O HOH A 571 -103.727-196.407 137.418 1.00124.22 O HETATM 2860 O HOH A 572 -114.106-153.363 135.194 1.00 93.26 O HETATM 2861 O HOH A 573 -116.818-187.000 155.210 1.00 93.44 O HETATM 2862 O HOH A 574 -85.494-161.997 152.559 1.00 88.53 O HETATM 2863 O HOH A 575 -110.158-151.969 160.797 1.00 92.31 O HETATM 2864 O HOH A 576 -118.718-185.916 157.190 1.00102.88 O HETATM 2865 O HOH A 577 -102.300-140.402 160.188 1.00100.23 O HETATM 2866 O HOH A 578 -90.843-147.768 147.046 1.00 73.77 O HETATM 2867 O HOH A 579 -91.038-157.682 167.628 0.50110.49 O CONECT 1 2 3 4 CONECT 2 1 CONECT 3 1 CONECT 4 1 CONECT 17 2255 CONECT 118 2604 CONECT 884 1485 CONECT 1485 884 CONECT 2255 17 CONECT 2575 2665 CONECT 2604 118 2605 2615 CONECT 2605 2604 2606 2612 CONECT 2606 2605 2607 2613 CONECT 2607 2606 2608 2614 CONECT 2608 2607 2609 2615 CONECT 2609 2608 2616 CONECT 2610 2611 2612 2617 CONECT 2611 2610 CONECT 2612 2605 2610 CONECT 2613 2606 CONECT 2614 2607 2618 CONECT 2615 2604 2608 CONECT 2616 2609 CONECT 2617 2610 CONECT 2618 2614 2619 2629 CONECT 2619 2618 2620 2626 CONECT 2620 2619 2621 2627 CONECT 2621 2620 2622 2628 CONECT 2622 2621 2623 2629 CONECT 2623 2622 2630 CONECT 2624 2625 2626 2631 CONECT 2625 2624 CONECT 2626 2619 2624 CONECT 2627 2620 CONECT 2628 2621 2632 CONECT 2629 2618 2622 CONECT 2630 2623 CONECT 2631 2624 CONECT 2632 2628 2633 2641 CONECT 2633 2632 2634 2638 CONECT 2634 2633 2635 2639 CONECT 2635 2634 2636 2640 CONECT 2636 2635 2637 2641 CONECT 2637 2636 2642 CONECT 2638 2633 CONECT 2639 2634 2643 CONECT 2640 2635 CONECT 2641 2632 2636 CONECT 2642 2637 2654 CONECT 2643 2639 2644 2652 CONECT 2644 2643 2645 2649 CONECT 2645 2644 2646 2650 CONECT 2646 2645 2647 2651 CONECT 2647 2646 2648 2652 CONECT 2648 2647 2653 CONECT 2649 2644 CONECT 2650 2645 CONECT 2651 2646 CONECT 2652 2643 2647 CONECT 2653 2648 CONECT 2654 2642 2655 2663 CONECT 2655 2654 2656 2660 CONECT 2656 2655 2657 2661 CONECT 2657 2656 2658 2662 CONECT 2658 2657 2659 2663 CONECT 2659 2658 2664 CONECT 2660 2655 CONECT 2661 2656 CONECT 2662 2657 CONECT 2663 2654 2658 CONECT 2664 2659 CONECT 2665 2575 2666 2667 CONECT 2666 2665 CONECT 2667 2665 2668 CONECT 2668 2667 2669 CONECT 2669 2668 2670 CONECT 2670 2669 2671 CONECT 2671 2670 2672 CONECT 2672 2671 2673 CONECT 2673 2672 2674 CONECT 2674 2673 2675 CONECT 2675 2674 2676 CONECT 2676 2675 2677 CONECT 2677 2676 2678 CONECT 2678 2677 2679 CONECT 2679 2678 2680 CONECT 2680 2679 2681 CONECT 2681 2680 CONECT 2682 2683 2684 2691 CONECT 2683 2682 2694 CONECT 2684 2682 2685 2686 CONECT 2685 2684 CONECT 2686 2684 2687 2688 CONECT 2687 2686 CONECT 2688 2686 2689 2690 CONECT 2689 2688 CONECT 2690 2688 2691 2692 CONECT 2691 2682 2690 CONECT 2692 2690 2693 CONECT 2693 2692 CONECT 2694 2683 2695 CONECT 2695 2694 2696 CONECT 2696 2695 2697 CONECT 2697 2696 2698 CONECT 2698 2697 2699 CONECT 2699 2698 2700 CONECT 2700 2699 2701 CONECT 2701 2700 CONECT 2702 2703 2704 2711 CONECT 2703 2702 2714 CONECT 2704 2702 2705 2706 CONECT 2705 2704 CONECT 2706 2704 2707 2708 CONECT 2707 2706 CONECT 2708 2706 2709 2710 CONECT 2709 2708 CONECT 2710 2708 2711 2712 CONECT 2711 2702 2710 CONECT 2712 2710 2713 CONECT 2713 2712 CONECT 2714 2703 2715 CONECT 2715 2714 2716 CONECT 2716 2715 2717 CONECT 2717 2716 2718 CONECT 2718 2717 2719 CONECT 2719 2718 2720 CONECT 2720 2719 2721 CONECT 2721 2720 CONECT 2722 2723 2724 2731 CONECT 2723 2722 2734 CONECT 2724 2722 2725 2726 CONECT 2725 2724 CONECT 2726 2724 2727 2728 CONECT 2727 2726 CONECT 2728 2726 2729 2730 CONECT 2729 2728 CONECT 2730 2728 2731 2732 CONECT 2731 2722 2730 CONECT 2732 2730 2733 CONECT 2733 2732 CONECT 2734 2723 2735 CONECT 2735 2734 2736 CONECT 2736 2735 2737 CONECT 2737 2736 2738 CONECT 2738 2737 2739 CONECT 2739 2738 2740 CONECT 2740 2739 2741 CONECT 2741 2740 CONECT 2742 2743 2744 2751 CONECT 2743 2742 2754 CONECT 2744 2742 2745 2746 CONECT 2745 2744 CONECT 2746 2744 2747 2748 CONECT 2747 2746 CONECT 2748 2746 2749 2750 CONECT 2749 2748 CONECT 2750 2748 2751 2752 CONECT 2751 2742 2750 CONECT 2752 2750 2753 CONECT 2753 2752 CONECT 2754 2743 2755 CONECT 2755 2754 2756 CONECT 2756 2755 2757 CONECT 2757 2756 2758 CONECT 2758 2757 2759 CONECT 2759 2758 2760 CONECT 2760 2759 2761 CONECT 2761 2760 CONECT 2762 2784 2785 2787 CONECT 2763 2764 2787 CONECT 2764 2763 2765 CONECT 2765 2764 2785 CONECT 2766 2769 2781 2783 CONECT 2767 2770 2783 CONECT 2768 2771 2783 CONECT 2769 2766 2772 2773 CONECT 2770 2767 2774 CONECT 2771 2768 2774 CONECT 2772 2769 CONECT 2773 2769 CONECT 2774 2770 2771 2788 CONECT 2775 2776 2780 CONECT 2776 2775 2777 CONECT 2777 2776 2778 2784 2786 CONECT 2778 2777 2779 CONECT 2779 2778 2780 CONECT 2780 2775 2779 2781 CONECT 2781 2766 2780 2782 CONECT 2782 2781 CONECT 2783 2766 2767 2768 CONECT 2784 2762 2777 CONECT 2785 2762 2765 2786 CONECT 2786 2777 2785 CONECT 2787 2762 2763 CONECT 2788 2774 MASTER 343 0 12 16 4 0 0 6 2855 1 195 26 END