HEADER CALCIUM-BINDING PROTEIN 11-JUL-11 3SUI TITLE CRYSTAL STRUCTURE OF CA2+-CALMODULIN IN COMPLEX WITH A TRPV1 C- TITLE 2 TERMINAL PEPTIDE COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CAM; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V COMPND 8 MEMBER 1; COMPND 9 CHAIN: B; COMPND 10 FRAGMENT: UNP RESIDUES 767-801; COMPND 11 SYNONYM: TRPV1, CAPSAICIN RECEPTOR, OSM-9-LIKE TRP CHANNEL 1, OTRPC1, COMPND 12 VANILLOID RECEPTOR 1, VANILLOID RECEPTOR TYPE 1-LIKE; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: CALM, CALM1, CALM2, CALM3, CALML2, CAM, CAM1, CAM2, CAM3, SOURCE 6 CAMB, CAMC, CAMIII; SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET21; SOURCE 12 MOL_ID: 2; SOURCE 13 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS; SOURCE 14 ORGANISM_COMMON: RAT; SOURCE 15 ORGANISM_TAXID: 10116; SOURCE 16 GENE: TRPV1, VR1, VR1L; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 19 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 21 EXPRESSION_SYSTEM_PLASMID: PMALC2 KEYWDS CALMODULIN, CALCIUM-CALMODULIN, TRPV1, TRPV1 C-TERMINUS, CALMODULIN KEYWDS 2 COMPLEX, THERMOSENSOR, TRP CHANNEL, EF HANDS, 1-10 MOTIF, CALCIUM KEYWDS 3 CHANNEL, CALMODULIN-BINDING, ION CHANNEL, CALCIUM BINDING PROTEIN, KEYWDS 4 CALCIUM-BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR S.-Y.LAU,R.GAUDET REVDAT 3 08-NOV-17 3SUI 1 REMARK REVDAT 2 14-NOV-12 3SUI 1 JRNL REVDAT 1 12-SEP-12 3SUI 0 JRNL AUTH S.Y.LAU,E.PROCKO,R.GAUDET JRNL TITL DISTINCT PROPERTIES OF CA2+-CALMODULIN BINDING TO N- AND JRNL TITL 2 C-TERMINAL REGULATORY REGIONS OF THE TRPV1 CHANNEL. JRNL REF J.GEN.PHYSIOL. V. 140 541 2012 JRNL REFN ISSN 0022-1295 JRNL PMID 23109716 JRNL DOI 10.1085/JGP.201210810 REMARK 2 REMARK 2 RESOLUTION. 1.95 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0102 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.95 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.10 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 98.7 REMARK 3 NUMBER OF REFLECTIONS : 13172 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.194 REMARK 3 R VALUE (WORKING SET) : 0.192 REMARK 3 FREE R VALUE : 0.248 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 690 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.95 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.00 REMARK 3 REFLECTION IN BIN (WORKING SET) : 885 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 93.11 REMARK 3 BIN R VALUE (WORKING SET) : 0.2570 REMARK 3 BIN FREE R VALUE SET COUNT : 47 REMARK 3 BIN FREE R VALUE : 0.3220 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1268 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 9 REMARK 3 SOLVENT ATOMS : 91 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.98 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.47000 REMARK 3 B22 (A**2) : 0.47000 REMARK 3 B33 (A**2) : -0.70000 REMARK 3 B12 (A**2) : 0.23000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.168 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.164 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.107 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.173 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.957 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.942 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1372 ; 0.017 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 1866 ; 1.519 ; 1.960 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 182 ; 4.707 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 81 ;36.926 ;26.296 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 256 ;16.447 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 8 ;19.427 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 202 ; 0.102 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1077 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 830 ; 0.972 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1341 ; 1.728 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 542 ; 2.525 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 513 ; 4.141 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 3 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 3 A 80 REMARK 3 RESIDUE RANGE : A 501 A 502 REMARK 3 ORIGIN FOR THE GROUP (A): -5.9420 -25.8990 -17.7520 REMARK 3 T TENSOR REMARK 3 T11: 0.3192 T22: 0.1938 REMARK 3 T33: 0.0356 T12: 0.0009 REMARK 3 T13: 0.0272 T23: -0.0085 REMARK 3 L TENSOR REMARK 3 L11: 2.3932 L22: 3.2130 REMARK 3 L33: 5.9637 L12: -1.1152 REMARK 3 L13: 1.2655 L23: -1.8376 REMARK 3 S TENSOR REMARK 3 S11: 0.1125 S12: 0.1300 S13: -0.0104 REMARK 3 S21: -0.2230 S22: -0.0082 S23: -0.0218 REMARK 3 S31: 0.2080 S32: -0.2905 S33: -0.1043 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 2 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 81 A 148 REMARK 3 RESIDUE RANGE : A 503 A 504 REMARK 3 ORIGIN FOR THE GROUP (A): -12.4150 -9.6580 -6.2110 REMARK 3 T TENSOR REMARK 3 T11: 0.3531 T22: 0.1727 REMARK 3 T33: 0.0478 T12: -0.0116 REMARK 3 T13: 0.0095 T23: 0.0079 REMARK 3 L TENSOR REMARK 3 L11: 3.2946 L22: 3.7392 REMARK 3 L33: 2.6175 L12: -1.8878 REMARK 3 L13: -0.4618 L23: 0.0066 REMARK 3 S TENSOR REMARK 3 S11: 0.0013 S12: 0.1104 S13: -0.0225 REMARK 3 S21: -0.1786 S22: -0.0292 S23: -0.1591 REMARK 3 S31: 0.1166 S32: 0.0833 S33: 0.0279 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 784 B 798 REMARK 3 ORIGIN FOR THE GROUP (A): -11.3290 -17.9790 -12.6830 REMARK 3 T TENSOR REMARK 3 T11: 0.3192 T22: 0.2687 REMARK 3 T33: 0.0575 T12: 0.0318 REMARK 3 T13: 0.0243 T23: -0.0702 REMARK 3 L TENSOR REMARK 3 L11: 11.4538 L22: 30.8631 REMARK 3 L33: 13.1870 L12: 0.7982 REMARK 3 L13: -1.6430 L23: 0.5393 REMARK 3 S TENSOR REMARK 3 S11: 0.1270 S12: 0.2760 S13: -0.1402 REMARK 3 S21: -0.8867 S22: -0.2584 S23: 0.2787 REMARK 3 S31: -0.0152 S32: -0.2764 S33: 0.1314 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING REMARK 3 POSITIONS REMARK 4 REMARK 4 3SUI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUL-11. REMARK 100 THE DEPOSITION ID IS D_1000066667. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 28-OCT-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6.0 REMARK 200 NUMBER OF CRYSTALS USED : NULL REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 24-ID-C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13862 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.950 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000 REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0 REMARK 200 DATA REDUNDANCY : 5.400 REMARK 200 R MERGE (I) : 0.05200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.98 REMARK 200 COMPLETENESS FOR SHELL (%) : 91.2 REMARK 200 DATA REDUNDANCY IN SHELL : 3.90 REMARK 200 R MERGE FOR SHELL (I) : 0.46900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: 3DVE REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.87 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES PH6.0, 2.2-2.8M AMMONIUM REMARK 280 SULFATE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -Y,X-Y,Z+1/3 REMARK 290 3555 -X+Y,-X,Z+2/3 REMARK 290 4555 -X,-Y,Z+1/2 REMARK 290 5555 Y,-X+Y,Z+5/6 REMARK 290 6555 X-Y,X,Z+1/6 REMARK 290 7555 Y,X,-Z+1/3 REMARK 290 8555 X-Y,-Y,-Z REMARK 290 9555 -X,-X+Y,-Z+2/3 REMARK 290 10555 -Y,-X,-Z+5/6 REMARK 290 11555 -X+Y,Y,-Z+1/2 REMARK 290 12555 X,X-Y,-Z+1/6 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 113.84433 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 227.68867 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 170.76650 REMARK 290 SMTRY1 5 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 5 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 284.61083 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 56.92217 REMARK 290 SMTRY1 7 -0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 7 0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 113.84433 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 9 -0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 9 -0.866025 0.500000 0.000000 0.00000 REMARK 290 SMTRY3 9 0.000000 0.000000 -1.000000 227.68867 REMARK 290 SMTRY1 10 0.500000 -0.866025 0.000000 0.00000 REMARK 290 SMTRY2 10 -0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 10 0.000000 0.000000 -1.000000 284.61083 REMARK 290 SMTRY1 11 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 11 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 11 0.000000 0.000000 -1.000000 170.76650 REMARK 290 SMTRY1 12 0.500000 0.866025 0.000000 0.00000 REMARK 290 SMTRY2 12 0.866025 -0.500000 0.000000 0.00000 REMARK 290 SMTRY3 12 0.000000 0.000000 -1.000000 56.92217 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 8590 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 MET A 0 REMARK 465 ALA A 1 REMARK 465 ASP A 2 REMARK 465 GLY B 765 REMARK 465 PRO B 766 REMARK 465 GLU B 767 REMARK 465 GLY B 768 REMARK 465 VAL B 769 REMARK 465 LYS B 770 REMARK 465 ARG B 771 REMARK 465 THR B 772 REMARK 465 LEU B 773 REMARK 465 SER B 774 REMARK 465 PHE B 775 REMARK 465 SER B 776 REMARK 465 LEU B 777 REMARK 465 ARG B 778 REMARK 465 SER B 779 REMARK 465 GLY B 780 REMARK 465 ARG B 781 REMARK 465 VAL B 782 REMARK 465 SER B 783 REMARK 465 ALA B 799 REMARK 465 SER B 800 REMARK 465 THR B 801 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A 7 CG CD OE1 OE2 REMARK 470 LYS A 148 CG CD CE NZ REMARK 470 ASP B 798 CG OD1 OD2 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 OD1 ASN A 53 O HOH A 234 2.02 REMARK 500 OE2 GLU A 139 O HOH A 227 2.05 REMARK 500 OE2 GLU A 123 NH1 ARG A 126 2.09 REMARK 500 OD1 ASN A 53 O HOH A 235 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 TRP B 787 CB TRP B 787 CG 0.139 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 TRP B 787 CA - CB - CG ANGL. DEV. = 13.8 DEGREES REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 502 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 175 O REMARK 620 2 ASP A 56 OD2 159.3 REMARK 620 3 THR A 62 O 105.5 90.6 REMARK 620 4 ASP A 58 OD2 77.8 82.3 156.9 REMARK 620 5 ASN A 60 OD1 83.4 87.0 79.1 78.6 REMARK 620 6 GLU A 67 OE1 86.6 109.4 80.2 122.9 153.7 REMARK 620 7 GLU A 67 OE2 89.3 90.6 128.9 73.4 152.0 51.5 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 503 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HOH A 166 O REMARK 620 2 TYR A 99 O 101.4 REMARK 620 3 ASP A 93 OD2 166.2 90.4 REMARK 620 4 ASN A 97 OD1 84.5 82.0 90.2 REMARK 620 5 ASP A 95 OD1 81.4 156.5 84.9 75.1 REMARK 620 6 GLU A 104 OE2 89.8 77.1 99.9 156.7 126.4 REMARK 620 7 GLU A 104 OE1 82.8 129.6 95.2 147.7 73.8 52.6 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 504 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 129 OD2 REMARK 620 2 ASP A 133 OD2 92.5 REMARK 620 3 GLN A 135 O 86.7 79.7 REMARK 620 4 ASP A 131 OD1 81.8 78.2 154.5 REMARK 620 5 GLU A 140 OE1 110.0 149.5 81.2 124.1 REMARK 620 6 HOH A 159 O 165.7 80.0 103.8 84.7 81.6 REMARK 620 7 GLU A 140 OE2 85.7 155.2 124.7 77.1 51.1 96.0 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 501 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 THR A 26 O REMARK 620 2 ASP A 20 OD1 83.8 REMARK 620 3 HOH A 195 O 116.5 157.6 REMARK 620 4 GLU A 31 OE2 122.5 94.3 82.9 REMARK 620 5 ASP A 24 OD2 81.7 83.1 90.3 155.4 REMARK 620 6 GLU A 31 OE1 77.2 117.2 78.6 52.8 148.5 REMARK 620 7 ASP A 22 OD1 153.8 75.9 81.8 76.1 79.6 126.8 REMARK 620 N 1 2 3 4 5 6 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 501 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 502 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 503 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 504 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC5 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 149 DBREF 3SUI A 0 148 UNP P62158 CALM_HUMAN 1 149 DBREF 3SUI B 767 801 UNP O35433 TRPV1_RAT 767 801 SEQADV 3SUI GLY B 765 UNP O35433 EXPRESSION TAG SEQADV 3SUI PRO B 766 UNP O35433 EXPRESSION TAG SEQRES 1 A 149 MET ALA ASP GLN LEU THR GLU GLU GLN ILE ALA GLU PHE SEQRES 2 A 149 LYS GLU ALA PHE SER LEU PHE ASP LYS ASP GLY ASP GLY SEQRES 3 A 149 THR ILE THR THR LYS GLU LEU GLY THR VAL MET ARG SER SEQRES 4 A 149 LEU GLY GLN ASN PRO THR GLU ALA GLU LEU GLN ASP MET SEQRES 5 A 149 ILE ASN GLU VAL ASP ALA ASP GLY ASN GLY THR ILE ASP SEQRES 6 A 149 PHE PRO GLU PHE LEU THR MET MET ALA ARG LYS MET LYS SEQRES 7 A 149 ASP THR ASP SER GLU GLU GLU ILE ARG GLU ALA PHE ARG SEQRES 8 A 149 VAL PHE ASP LYS ASP GLY ASN GLY TYR ILE SER ALA ALA SEQRES 9 A 149 GLU LEU ARG HIS VAL MET THR ASN LEU GLY GLU LYS LEU SEQRES 10 A 149 THR ASP GLU GLU VAL ASP GLU MET ILE ARG GLU ALA ASP SEQRES 11 A 149 ILE ASP GLY ASP GLY GLN VAL ASN TYR GLU GLU PHE VAL SEQRES 12 A 149 GLN MET MET THR ALA LYS SEQRES 1 B 37 GLY PRO GLU GLY VAL LYS ARG THR LEU SER PHE SER LEU SEQRES 2 B 37 ARG SER GLY ARG VAL SER GLY ARG ASN TRP LYS ASN PHE SEQRES 3 B 37 ALA LEU VAL PRO LEU LEU ARG ASP ALA SER THR HET CA A 501 1 HET CA A 502 1 HET CA A 503 1 HET CA A 504 1 HET SO4 A 149 5 HETNAM CA CALCIUM ION HETNAM SO4 SULFATE ION FORMUL 3 CA 4(CA 2+) FORMUL 7 SO4 O4 S 2- FORMUL 8 HOH *91(H2 O) HELIX 1 1 THR A 5 ASP A 20 1 16 HELIX 2 2 THR A 28 LEU A 39 1 12 HELIX 3 3 THR A 44 GLU A 54 1 11 HELIX 4 4 ASP A 64 THR A 79 1 16 HELIX 5 5 SER A 81 ASP A 93 1 13 HELIX 6 6 SER A 101 GLY A 113 1 13 HELIX 7 7 THR A 117 ASP A 129 1 13 HELIX 8 8 TYR A 138 ALA A 147 1 10 HELIX 9 9 TRP B 787 VAL B 793 1 7 HELIX 10 10 PRO B 794 LEU B 796 5 3 SHEET 1 A 2 TYR A 99 ILE A 100 0 SHEET 2 A 2 VAL A 136 ASN A 137 -1 O VAL A 136 N ILE A 100 LINK CA CA A 502 O HOH A 175 1555 1555 2.14 LINK CA CA A 503 O HOH A 166 1555 1555 2.20 LINK O TYR A 99 CA CA A 503 1555 1555 2.21 LINK OD2 ASP A 129 CA CA A 504 1555 1555 2.24 LINK OD2 ASP A 56 CA CA A 502 1555 1555 2.25 LINK O THR A 26 CA CA A 501 1555 1555 2.30 LINK OD2 ASP A 133 CA CA A 504 1555 1555 2.32 LINK OD2 ASP A 93 CA CA A 503 1555 1555 2.32 LINK O GLN A 135 CA CA A 504 1555 1555 2.35 LINK O THR A 62 CA CA A 502 1555 1555 2.35 LINK OD2 ASP A 58 CA CA A 502 1555 1555 2.35 LINK OD1 ASP A 20 CA CA A 501 1555 1555 2.37 LINK OD1 ASN A 60 CA CA A 502 1555 1555 2.37 LINK OD1 ASN A 97 CA CA A 503 1555 1555 2.37 LINK OE1 GLU A 67 CA CA A 502 1555 1555 2.38 LINK OD1 ASP A 95 CA CA A 503 1555 1555 2.38 LINK OD1 ASP A 131 CA CA A 504 1555 1555 2.38 LINK CA CA A 501 O HOH A 195 1555 1555 2.40 LINK OE2 GLU A 31 CA CA A 501 1555 1555 2.41 LINK OD2 ASP A 24 CA CA A 501 1555 1555 2.42 LINK OE2 GLU A 104 CA CA A 503 1555 1555 2.44 LINK OE1 GLU A 140 CA CA A 504 1555 1555 2.44 LINK CA CA A 504 O HOH A 159 1555 1555 2.46 LINK OE1 GLU A 31 CA CA A 501 1555 1555 2.48 LINK OE1 GLU A 104 CA CA A 503 1555 1555 2.49 LINK OD1 ASP A 22 CA CA A 501 1555 1555 2.51 LINK OE2 GLU A 140 CA CA A 504 1555 1555 2.60 LINK OE2 GLU A 67 CA CA A 502 1555 1555 2.66 SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26 SITE 2 AC1 6 GLU A 31 HOH A 195 SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62 SITE 2 AC2 6 GLU A 67 HOH A 175 SITE 1 AC3 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99 SITE 2 AC3 6 GLU A 104 HOH A 166 SITE 1 AC4 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135 SITE 2 AC4 6 GLU A 140 HOH A 159 SITE 1 AC5 3 GLN A 41 ASN A 42 ARG B 797 CRYST1 41.681 41.681 341.533 90.00 90.00 120.00 P 61 2 2 12 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 0.023992 0.013852 0.000000 0.00000 SCALE2 0.000000 0.027703 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002928 0.00000 ATOM 1 N GLN A 3 -15.861 -13.049 -33.630 1.00 73.96 N ANISOU 1 N GLN A 3 11283 10680 6140 2139 -339 1356 N ATOM 2 CA GLN A 3 -15.836 -11.951 -32.615 1.00 73.59 C ANISOU 2 CA GLN A 3 11281 10440 6238 2305 -241 1398 C ATOM 3 C GLN A 3 -14.980 -12.243 -31.352 1.00 70.15 C ANISOU 3 C GLN A 3 10832 9811 6012 2126 -111 1270 C ATOM 4 O GLN A 3 -15.186 -11.617 -30.305 1.00 70.46 O ANISOU 4 O GLN A 3 10869 9748 6156 2255 -74 1253 O ATOM 5 CB GLN A 3 -17.263 -11.572 -32.212 1.00 76.07 C ANISOU 5 CB GLN A 3 11390 10990 6524 2571 -353 1450 C ATOM 6 CG GLN A 3 -17.357 -10.243 -31.472 1.00 79.46 C ANISOU 6 CG GLN A 3 11970 11206 7016 2859 -275 1511 C ATOM 7 CD GLN A 3 -18.523 -10.184 -30.493 1.00 83.62 C ANISOU 7 CD GLN A 3 12234 11972 7567 3091 -309 1498 C ATOM 8 OE1 GLN A 3 -18.751 -11.115 -29.705 1.00 82.66 O ANISOU 8 OE1 GLN A 3 11849 12030 7527 2933 -302 1400 O ATOM 9 NE2 GLN A 3 -19.257 -9.071 -30.523 1.00 86.79 N ANISOU 9 NE2 GLN A 3 12712 12379 7884 3492 -333 1615 N ATOM 10 N LEU A 4 -14.034 -13.183 -31.436 1.00 66.49 N ANISOU 10 N LEU A 4 10375 9299 5588 1863 -50 1177 N ATOM 11 CA LEU A 4 -12.973 -13.294 -30.414 1.00 62.45 C ANISOU 11 CA LEU A 4 9895 8570 5261 1701 78 1092 C ATOM 12 C LEU A 4 -12.028 -12.081 -30.556 1.00 61.34 C ANISOU 12 C LEU A 4 10005 8131 5170 1725 180 1216 C ATOM 13 O LEU A 4 -11.617 -11.747 -31.673 1.00 62.59 O ANISOU 13 O LEU A 4 10304 8260 5217 1729 213 1345 O ATOM 14 CB LEU A 4 -12.219 -14.610 -30.581 1.00 61.26 C ANISOU 14 CB LEU A 4 9692 8468 5117 1461 113 983 C ATOM 15 CG LEU A 4 -11.034 -14.934 -29.665 1.00 60.43 C ANISOU 15 CG LEU A 4 9589 8188 5184 1284 233 904 C ATOM 16 CD1 LEU A 4 -11.440 -15.230 -28.246 1.00 59.80 C ANISOU 16 CD1 LEU A 4 9364 8117 5240 1257 207 794 C ATOM 17 CD2 LEU A 4 -10.291 -16.130 -30.248 1.00 60.10 C ANISOU 17 CD2 LEU A 4 9549 8208 5078 1137 273 834 C ATOM 18 N THR A 5 -11.725 -11.386 -29.460 1.00 58.01 N ANISOU 18 N THR A 5 9660 7485 4897 1738 213 1192 N ATOM 19 CA THR A 5 -10.900 -10.170 -29.558 1.00 57.16 C ANISOU 19 CA THR A 5 9817 7057 4844 1722 260 1325 C ATOM 20 C THR A 5 -9.457 -10.457 -29.149 1.00 55.20 C ANISOU 20 C THR A 5 9572 6656 4745 1429 353 1310 C ATOM 21 O THR A 5 -9.180 -11.441 -28.448 1.00 52.26 O ANISOU 21 O THR A 5 9027 6375 4453 1299 376 1166 O ATOM 22 CB THR A 5 -11.414 -9.027 -28.659 1.00 59.06 C ANISOU 22 CB THR A 5 10230 7077 5133 1933 199 1320 C ATOM 23 OG1 THR A 5 -11.280 -9.417 -27.278 1.00 54.30 O ANISOU 23 OG1 THR A 5 9540 6437 4655 1868 205 1153 O ATOM 24 CG2 THR A 5 -12.881 -8.656 -28.990 1.00 59.40 C ANISOU 24 CG2 THR A 5 10241 7304 5025 2287 116 1358 C ATOM 25 N GLU A 6 -8.550 -9.579 -29.558 1.00 55.14 N ANISOU 25 N GLU A 6 9753 6422 4777 1322 398 1482 N ATOM 26 CA GLU A 6 -7.156 -9.657 -29.126 1.00 54.19 C ANISOU 26 CA GLU A 6 9611 6164 4814 1036 468 1515 C ATOM 27 C GLU A 6 -7.012 -9.650 -27.611 1.00 51.81 C ANISOU 27 C GLU A 6 9301 5709 4674 971 403 1355 C ATOM 28 O GLU A 6 -6.157 -10.342 -27.083 1.00 49.96 O ANISOU 28 O GLU A 6 8921 5512 4549 772 447 1293 O ATOM 29 CB GLU A 6 -6.363 -8.479 -29.665 1.00 57.14 C ANISOU 29 CB GLU A 6 10200 6288 5221 915 487 1764 C ATOM 30 CG GLU A 6 -5.985 -8.576 -31.105 1.00 59.43 C ANISOU 30 CG GLU A 6 10475 6738 5369 891 604 1966 C ATOM 31 CD GLU A 6 -5.129 -7.401 -31.507 1.00 63.28 C ANISOU 31 CD GLU A 6 11156 6974 5915 717 626 2251 C ATOM 32 OE1 GLU A 6 -5.595 -6.568 -32.319 1.00 66.28 O ANISOU 32 OE1 GLU A 6 11747 7264 6171 850 600 2418 O ATOM 33 OE2 GLU A 6 -4.004 -7.309 -30.973 1.00 64.54 O ANISOU 33 OE2 GLU A 6 11251 7024 6246 436 653 2319 O ATOM 34 N GLU A 7 -7.850 -8.851 -26.951 1.00 51.70 N ANISOU 34 N GLU A 7 9459 5533 4650 1173 300 1296 N ATOM 35 CA GLU A 7 -7.931 -8.746 -25.510 1.00 51.25 C ANISOU 35 CA GLU A 7 9449 5338 4685 1195 231 1132 C ATOM 36 C GLU A 7 -8.284 -10.080 -24.877 1.00 48.06 C ANISOU 36 C GLU A 7 8758 5218 4286 1194 269 953 C ATOM 37 O GLU A 7 -7.636 -10.495 -23.899 1.00 46.49 O ANISOU 37 O GLU A 7 8502 4965 4197 1037 263 852 O ATOM 38 CB GLU A 7 -8.965 -7.683 -25.104 1.00 53.99 C ANISOU 38 CB GLU A 7 10048 5515 4949 1521 138 1105 C ATOM 39 N GLN A 8 -9.327 -10.744 -25.385 1.00 46.14 N ANISOU 39 N GLN A 8 8341 5269 3921 1355 285 924 N ATOM 40 CA GLN A 8 -9.718 -12.031 -24.803 1.00 43.50 C ANISOU 40 CA GLN A 8 7749 5186 3592 1318 300 781 C ATOM 41 C GLN A 8 -8.581 -13.041 -24.916 1.00 40.33 C ANISOU 41 C GLN A 8 7230 4825 3271 1046 364 753 C ATOM 42 O GLN A 8 -8.358 -13.816 -23.998 1.00 36.53 O ANISOU 42 O GLN A 8 6634 4384 2861 953 368 637 O ATOM 43 CB GLN A 8 -10.993 -12.578 -25.431 1.00 44.78 C ANISOU 43 CB GLN A 8 7740 5655 3617 1474 269 785 C ATOM 44 CG GLN A 8 -12.222 -11.834 -24.981 1.00 49.40 C ANISOU 44 CG GLN A 8 8345 6295 4130 1782 220 794 C ATOM 45 CD GLN A 8 -13.445 -12.099 -25.863 1.00 56.18 C ANISOU 45 CD GLN A 8 9034 7463 4847 1939 163 864 C ATOM 46 OE1 GLN A 8 -13.361 -12.131 -27.093 1.00 54.67 O ANISOU 46 OE1 GLN A 8 8878 7316 4577 1903 139 951 O ATOM 47 NE2 GLN A 8 -14.597 -12.275 -25.224 1.00 58.85 N ANISOU 47 NE2 GLN A 8 9179 8040 5142 2120 136 843 N ATOM 48 N ILE A 9 -7.861 -13.003 -26.038 1.00 39.25 N ANISOU 48 N ILE A 9 7126 4682 3104 950 422 875 N ATOM 49 CA ILE A 9 -6.749 -13.955 -26.299 1.00 38.52 C ANISOU 49 CA ILE A 9 6919 4664 3053 756 508 871 C ATOM 50 C ILE A 9 -5.592 -13.753 -25.324 1.00 38.55 C ANISOU 50 C ILE A 9 6921 4497 3230 575 520 868 C ATOM 51 O ILE A 9 -5.111 -14.709 -24.718 1.00 38.22 O ANISOU 51 O ILE A 9 6744 4526 3250 481 541 770 O ATOM 52 CB ILE A 9 -6.195 -13.824 -27.766 1.00 39.02 C ANISOU 52 CB ILE A 9 7028 4787 3010 739 598 1037 C ATOM 53 CG1 ILE A 9 -7.303 -14.198 -28.744 1.00 38.77 C ANISOU 53 CG1 ILE A 9 7001 4947 2784 905 555 1019 C ATOM 54 CG2 ILE A 9 -4.957 -14.755 -27.957 1.00 38.18 C ANISOU 54 CG2 ILE A 9 6799 4775 2932 597 715 1044 C ATOM 55 CD1 ILE A 9 -7.069 -13.660 -30.177 1.00 37.97 C ANISOU 55 CD1 ILE A 9 7019 4875 2532 961 618 1204 C ATOM 56 N ALA A 10 -5.161 -12.511 -25.167 1.00 40.78 N ANISOU 56 N ALA A 10 7368 4540 3585 519 482 979 N ATOM 57 CA ALA A 10 -4.151 -12.171 -24.170 1.00 41.98 C ANISOU 57 CA ALA A 10 7545 4505 3902 323 433 979 C ATOM 58 C ALA A 10 -4.546 -12.628 -22.758 1.00 41.10 C ANISOU 58 C ALA A 10 7404 4380 3832 370 359 774 C ATOM 59 O ALA A 10 -3.688 -13.111 -21.989 1.00 39.95 O ANISOU 59 O ALA A 10 7161 4226 3792 210 346 727 O ATOM 60 CB ALA A 10 -3.922 -10.674 -24.168 1.00 44.33 C ANISOU 60 CB ALA A 10 8101 4493 4250 267 344 1112 C ATOM 61 N GLU A 11 -5.819 -12.437 -22.400 1.00 40.60 N ANISOU 61 N GLU A 11 7415 4334 3676 599 314 675 N ATOM 62 CA GLU A 11 -6.316 -12.894 -21.096 1.00 40.22 C ANISOU 62 CA GLU A 11 7326 4325 3630 677 273 505 C ATOM 63 C GLU A 11 -6.206 -14.405 -20.925 1.00 37.48 C ANISOU 63 C GLU A 11 6733 4215 3293 593 332 426 C ATOM 64 O GLU A 11 -5.768 -14.888 -19.867 1.00 35.06 O ANISOU 64 O GLU A 11 6380 3890 3052 511 308 337 O ATOM 65 CB GLU A 11 -7.772 -12.467 -20.902 1.00 42.02 C ANISOU 65 CB GLU A 11 7621 4613 3733 975 250 458 C ATOM 66 CG GLU A 11 -7.952 -10.976 -20.807 1.00 46.39 C ANISOU 66 CG GLU A 11 8484 4886 4257 1124 174 500 C ATOM 67 CD GLU A 11 -9.416 -10.566 -21.014 1.00 54.75 C ANISOU 67 CD GLU A 11 9569 6069 5165 1477 180 504 C ATOM 68 OE1 GLU A 11 -9.667 -9.345 -21.113 1.00 58.62 O ANISOU 68 OE1 GLU A 11 10340 6328 5604 1658 121 550 O ATOM 69 OE2 GLU A 11 -10.303 -11.465 -21.068 1.00 54.92 O ANISOU 69 OE2 GLU A 11 9330 6416 5119 1568 231 473 O ATOM 70 N PHE A 12 -6.607 -15.144 -21.963 1.00 35.48 N ANISOU 70 N PHE A 12 6357 4163 2961 619 390 458 N ATOM 71 CA PHE A 12 -6.484 -16.607 -21.934 1.00 34.51 C ANISOU 71 CA PHE A 12 6064 4214 2832 537 424 385 C ATOM 72 C PHE A 12 -5.020 -16.998 -21.853 1.00 33.28 C ANISOU 72 C PHE A 12 5865 4003 2777 369 470 409 C ATOM 73 O PHE A 12 -4.659 -17.937 -21.156 1.00 31.09 O ANISOU 73 O PHE A 12 5500 3770 2544 305 469 329 O ATOM 74 CB PHE A 12 -7.129 -17.253 -23.169 1.00 34.42 C ANISOU 74 CB PHE A 12 5998 4385 2696 588 439 409 C ATOM 75 CG PHE A 12 -8.639 -17.367 -23.094 1.00 36.45 C ANISOU 75 CG PHE A 12 6192 4796 2863 715 372 379 C ATOM 76 CD1 PHE A 12 -9.432 -16.762 -24.063 1.00 42.23 C ANISOU 76 CD1 PHE A 12 6959 5599 3486 848 343 460 C ATOM 77 CD2 PHE A 12 -9.259 -18.143 -22.095 1.00 37.92 C ANISOU 77 CD2 PHE A 12 6257 5088 3064 694 338 298 C ATOM 78 CE1 PHE A 12 -10.828 -16.882 -24.037 1.00 44.07 C ANISOU 78 CE1 PHE A 12 7080 6028 3637 965 272 463 C ATOM 79 CE2 PHE A 12 -10.657 -18.283 -22.059 1.00 39.60 C ANISOU 79 CE2 PHE A 12 6349 5501 3195 790 283 315 C ATOM 80 CZ PHE A 12 -11.448 -17.640 -23.037 1.00 39.83 C ANISOU 80 CZ PHE A 12 6385 5623 3126 929 245 399 C ATOM 81 N LYS A 13 -4.177 -16.253 -22.557 1.00 34.86 N ANISOU 81 N LYS A 13 6115 4119 3011 301 510 545 N ATOM 82 CA LYS A 13 -2.738 -16.530 -22.564 1.00 35.45 C ANISOU 82 CA LYS A 13 6092 4195 3180 148 567 619 C ATOM 83 C LYS A 13 -2.109 -16.358 -21.157 1.00 35.07 C ANISOU 83 C LYS A 13 6033 4021 3272 26 478 565 C ATOM 84 O LYS A 13 -1.278 -17.190 -20.719 1.00 33.71 O ANISOU 84 O LYS A 13 5723 3924 3160 -48 498 543 O ATOM 85 CB LYS A 13 -2.097 -15.619 -23.591 1.00 37.96 C ANISOU 85 CB LYS A 13 6451 4473 3501 85 628 822 C ATOM 86 CG LYS A 13 -0.821 -16.089 -24.205 1.00 39.68 C ANISOU 86 CG LYS A 13 6510 4827 3740 -2 753 954 C ATOM 87 CD LYS A 13 -0.396 -15.099 -25.322 1.00 43.97 C ANISOU 87 CD LYS A 13 7098 5356 4254 -56 829 1195 C ATOM 88 CE LYS A 13 1.063 -15.357 -25.688 1.00 48.66 C ANISOU 88 CE LYS A 13 7481 6105 4901 -174 960 1380 C ATOM 89 NZ LYS A 13 1.553 -14.730 -26.946 1.00 52.82 N ANISOU 89 NZ LYS A 13 7995 6718 5355 -203 1095 1646 N ATOM 90 N GLU A 14 -2.473 -15.276 -20.461 1.00 35.14 N ANISOU 90 N GLU A 14 6208 3831 3312 28 368 544 N ATOM 91 CA AGLU A 14 -2.079 -15.031 -19.073 0.50 35.75 C ANISOU 91 CA AGLU A 14 6344 3766 3475 -55 247 462 C ATOM 92 CA BGLU A 14 -1.958 -15.107 -19.110 0.50 36.06 C ANISOU 92 CA BGLU A 14 6362 3817 3522 -72 254 470 C ATOM 93 C GLU A 14 -2.497 -16.204 -18.186 1.00 33.25 C ANISOU 93 C GLU A 14 5929 3582 3121 21 254 307 C ATOM 94 O GLU A 14 -1.735 -16.667 -17.352 1.00 33.25 O ANISOU 94 O GLU A 14 5860 3581 3191 -79 209 271 O ATOM 95 CB AGLU A 14 -2.770 -13.760 -18.557 0.50 37.86 C ANISOU 95 CB AGLU A 14 6882 3795 3706 36 132 420 C ATOM 96 CB BGLU A 14 -2.195 -13.698 -18.528 0.50 38.96 C ANISOU 96 CB BGLU A 14 6998 3903 3901 -69 113 461 C ATOM 97 CG AGLU A 14 -2.235 -13.216 -17.226 0.50 40.19 C ANISOU 97 CG AGLU A 14 7330 3875 4065 -63 -31 344 C ATOM 98 CG BGLU A 14 -1.058 -12.659 -18.826 0.50 44.21 C ANISOU 98 CG BGLU A 14 7743 4366 4688 -316 29 636 C ATOM 99 CD AGLU A 14 -2.660 -11.761 -16.977 0.50 46.43 C ANISOU 99 CD AGLU A 14 8471 4357 4814 16 -161 333 C ATOM 100 CD BGLU A 14 0.171 -12.869 -17.931 0.50 48.38 C ANISOU 100 CD BGLU A 14 8168 4863 5350 -554 -78 645 C ATOM 101 OE1AGLU A 14 -2.842 -11.014 -17.967 0.50 52.25 O ANISOU 101 OE1AGLU A 14 9309 5005 5540 34 -138 458 O ATOM 102 OE1BGLU A 14 0.154 -12.404 -16.765 0.50 49.66 O ANISOU 102 OE1BGLU A 14 8519 4828 5520 -580 -251 528 O ATOM 103 OE2AGLU A 14 -2.807 -11.357 -15.798 0.50 51.46 O ANISOU 103 OE2AGLU A 14 9317 4826 5411 79 -290 199 O ATOM 104 OE2BGLU A 14 1.155 -13.502 -18.383 0.50 49.20 O ANISOU 104 OE2BGLU A 14 8005 5155 5532 -694 5 769 O ATOM 105 N ALA A 15 -3.752 -16.641 -18.365 1.00 31.27 N ANISOU 105 N ALA A 15 5673 3452 2757 189 298 238 N ATOM 106 CA ALA A 15 -4.322 -17.753 -17.546 1.00 31.99 C ANISOU 106 CA ALA A 15 5675 3675 2803 241 304 125 C ATOM 107 C ALA A 15 -3.599 -19.067 -17.832 1.00 30.70 C ANISOU 107 C ALA A 15 5365 3627 2673 150 356 128 C ATOM 108 O ALA A 15 -3.301 -19.840 -16.903 1.00 31.80 O ANISOU 108 O ALA A 15 5458 3787 2839 113 330 65 O ATOM 109 CB ALA A 15 -5.834 -17.915 -17.764 1.00 30.65 C ANISOU 109 CB ALA A 15 5486 3644 2515 402 328 98 C ATOM 110 N PHE A 16 -3.307 -19.325 -19.101 1.00 29.86 N ANISOU 110 N PHE A 16 5213 3588 2542 144 430 200 N ATOM 111 CA PHE A 16 -2.552 -20.515 -19.463 1.00 30.13 C ANISOU 111 CA PHE A 16 5154 3715 2578 116 488 199 C ATOM 112 C PHE A 16 -1.181 -20.520 -18.793 1.00 31.10 C ANISOU 112 C PHE A 16 5196 3801 2820 21 477 239 C ATOM 113 O PHE A 16 -0.744 -21.535 -18.240 1.00 30.45 O ANISOU 113 O PHE A 16 5054 3761 2753 24 473 189 O ATOM 114 CB PHE A 16 -2.362 -20.609 -20.986 1.00 29.47 C ANISOU 114 CB PHE A 16 5071 3712 2414 166 581 278 C ATOM 115 CG PHE A 16 -1.693 -21.869 -21.432 1.00 29.78 C ANISOU 115 CG PHE A 16 5067 3841 2405 210 649 257 C ATOM 116 CD1 PHE A 16 -2.466 -22.997 -21.748 1.00 29.89 C ANISOU 116 CD1 PHE A 16 5156 3894 2305 271 619 154 C ATOM 117 CD2 PHE A 16 -0.303 -21.925 -21.610 1.00 30.29 C ANISOU 117 CD2 PHE A 16 5026 3957 2525 203 735 354 C ATOM 118 CE1 PHE A 16 -1.878 -24.195 -22.171 1.00 30.98 C ANISOU 118 CE1 PHE A 16 5332 4068 2371 348 663 113 C ATOM 119 CE2 PHE A 16 0.322 -23.130 -22.039 1.00 34.92 C ANISOU 119 CE2 PHE A 16 5596 4636 3036 319 813 329 C ATOM 120 CZ PHE A 16 -0.468 -24.261 -22.343 1.00 31.17 C ANISOU 120 CZ PHE A 16 5265 4147 2430 408 775 195 C ATOM 121 N SER A 17 -0.510 -19.376 -18.856 1.00 32.17 N ANISOU 121 N SER A 17 5332 3852 3037 -74 455 345 N ATOM 122 CA SER A 17 0.845 -19.262 -18.340 1.00 35.04 C ANISOU 122 CA SER A 17 5579 4210 3525 -206 420 424 C ATOM 123 C SER A 17 0.916 -19.381 -16.789 1.00 34.53 C ANISOU 123 C SER A 17 5548 4062 3511 -254 282 317 C ATOM 124 O SER A 17 1.922 -19.810 -16.241 1.00 34.50 O ANISOU 124 O SER A 17 5418 4108 3582 -322 244 347 O ATOM 125 CB SER A 17 1.478 -17.987 -18.925 1.00 38.02 C ANISOU 125 CB SER A 17 5954 4515 3976 -345 411 600 C ATOM 126 OG SER A 17 2.039 -17.235 -17.891 1.00 44.24 O ANISOU 126 OG SER A 17 6778 5154 4879 -514 250 613 O ATOM 127 N LEU A 18 -0.162 -19.017 -16.102 1.00 34.11 N ANISOU 127 N LEU A 18 5656 3909 3396 -190 214 202 N ATOM 128 CA LEU A 18 -0.295 -19.257 -14.649 1.00 33.71 C ANISOU 128 CA LEU A 18 5665 3810 3334 -182 110 90 C ATOM 129 C LEU A 18 -0.060 -20.735 -14.366 1.00 32.52 C ANISOU 129 C LEU A 18 5394 3794 3169 -144 156 55 C ATOM 130 O LEU A 18 0.612 -21.073 -13.383 1.00 31.75 O ANISOU 130 O LEU A 18 5264 3690 3110 -189 74 34 O ATOM 131 CB LEU A 18 -1.704 -18.878 -14.148 1.00 33.74 C ANISOU 131 CB LEU A 18 5829 3769 3221 -41 97 -11 C ATOM 132 CG LEU A 18 -2.159 -19.441 -12.791 1.00 37.87 C ANISOU 132 CG LEU A 18 6394 4324 3672 27 55 -116 C ATOM 133 CD1 LEU A 18 -1.349 -18.809 -11.707 1.00 41.34 C ANISOU 133 CD1 LEU A 18 6943 4619 4145 -50 -97 -153 C ATOM 134 CD2 LEU A 18 -3.655 -19.282 -12.516 1.00 40.97 C ANISOU 134 CD2 LEU A 18 6861 4777 3928 202 103 -169 C ATOM 135 N PHE A 19 -0.676 -21.617 -15.166 1.00 29.85 N ANISOU 135 N PHE A 19 5025 3557 2761 -58 261 44 N ATOM 136 CA PHE A 19 -0.512 -23.044 -14.959 1.00 29.97 C ANISOU 136 CA PHE A 19 4991 3646 2750 -17 287 9 C ATOM 137 C PHE A 19 0.832 -23.551 -15.516 1.00 31.77 C ANISOU 137 C PHE A 19 5094 3942 3035 -10 340 87 C ATOM 138 O PHE A 19 1.497 -24.358 -14.873 1.00 30.84 O ANISOU 138 O PHE A 19 4927 3851 2941 14 311 79 O ATOM 139 CB PHE A 19 -1.625 -23.866 -15.621 1.00 28.16 C ANISOU 139 CB PHE A 19 4812 3470 2419 45 339 -32 C ATOM 140 CG PHE A 19 -2.959 -23.722 -14.965 1.00 28.75 C ANISOU 140 CG PHE A 19 4939 3555 2429 54 303 -78 C ATOM 141 CD1 PHE A 19 -3.293 -24.510 -13.838 1.00 30.97 C ANISOU 141 CD1 PHE A 19 5234 3852 2680 41 265 -112 C ATOM 142 CD2 PHE A 19 -3.846 -22.772 -15.406 1.00 29.80 C ANISOU 142 CD2 PHE A 19 5098 3703 2522 95 316 -65 C ATOM 143 CE1 PHE A 19 -4.563 -24.356 -13.194 1.00 29.18 C ANISOU 143 CE1 PHE A 19 5016 3695 2377 65 260 -119 C ATOM 144 CE2 PHE A 19 -5.096 -22.606 -14.794 1.00 30.98 C ANISOU 144 CE2 PHE A 19 5256 3917 2597 147 303 -84 C ATOM 145 CZ PHE A 19 -5.452 -23.420 -13.693 1.00 30.84 C ANISOU 145 CZ PHE A 19 5221 3952 2545 129 285 -104 C ATOM 146 N ASP A 20 1.191 -23.092 -16.708 1.00 31.81 N ANISOU 146 N ASP A 20 5047 3995 3045 -2 427 176 N ATOM 147 CA ASP A 20 2.371 -23.574 -17.419 1.00 35.55 C ANISOU 147 CA ASP A 20 5381 4591 3534 58 524 275 C ATOM 148 C ASP A 20 3.614 -22.889 -16.868 1.00 38.67 C ANISOU 148 C ASP A 20 5602 5023 4068 -67 467 399 C ATOM 149 O ASP A 20 4.261 -22.079 -17.560 1.00 39.82 O ANISOU 149 O ASP A 20 5632 5229 4268 -147 517 552 O ATOM 150 CB ASP A 20 2.244 -23.306 -18.943 1.00 35.40 C ANISOU 150 CB ASP A 20 5375 4642 3435 125 654 347 C ATOM 151 CG ASP A 20 3.421 -23.849 -19.728 1.00 38.16 C ANISOU 151 CG ASP A 20 5584 5160 3757 247 793 458 C ATOM 152 OD1 ASP A 20 4.140 -24.715 -19.181 1.00 35.26 O ANISOU 152 OD1 ASP A 20 5138 4848 3409 329 789 446 O ATOM 153 OD2 ASP A 20 3.619 -23.423 -20.889 1.00 36.72 O ANISOU 153 OD2 ASP A 20 5371 5068 3513 289 914 567 O ATOM 154 N LYS A 21 3.939 -23.230 -15.616 1.00 40.37 N ANISOU 154 N LYS A 21 5795 5209 4334 -102 348 349 N ATOM 155 CA LYS A 21 5.019 -22.557 -14.892 1.00 43.75 C ANISOU 155 CA LYS A 21 6075 5656 4892 -260 227 450 C ATOM 156 C LYS A 21 6.432 -22.772 -15.463 1.00 46.59 C ANISOU 156 C LYS A 21 6147 6232 5323 -248 307 640 C ATOM 157 O LYS A 21 7.307 -21.929 -15.268 1.00 49.37 O ANISOU 157 O LYS A 21 6333 6627 5798 -442 218 789 O ATOM 158 CB LYS A 21 4.944 -22.893 -13.409 1.00 43.96 C ANISOU 158 CB LYS A 21 6175 5608 4921 -280 68 342 C ATOM 159 CG LYS A 21 3.819 -22.082 -12.708 1.00 45.34 C ANISOU 159 CG LYS A 21 6589 5593 5046 -341 -35 216 C ATOM 160 CD LYS A 21 3.607 -22.471 -11.244 1.00 49.08 C ANISOU 160 CD LYS A 21 7167 6013 5469 -320 -164 107 C ATOM 161 CE LYS A 21 2.172 -22.174 -10.820 1.00 46.77 C ANISOU 161 CE LYS A 21 7097 5617 5058 -255 -159 -18 C ATOM 162 NZ LYS A 21 1.922 -20.701 -10.850 1.00 52.78 N ANISOU 162 NZ LYS A 21 7990 6234 5831 -334 -238 -29 N ATOM 163 N ASP A 22 6.662 -23.860 -16.188 1.00 46.30 N ANISOU 163 N ASP A 22 6054 6337 5201 -20 470 651 N ATOM 164 CA ASP A 22 7.962 -24.019 -16.861 1.00 47.87 C ANISOU 164 CA ASP A 22 5961 6794 5434 55 594 855 C ATOM 165 C ASP A 22 7.970 -23.495 -18.303 1.00 48.59 C ANISOU 165 C ASP A 22 6007 6983 5470 79 777 983 C ATOM 166 O ASP A 22 9.005 -23.482 -18.961 1.00 50.94 O ANISOU 166 O ASP A 22 6043 7530 5780 138 912 1189 O ATOM 167 CB ASP A 22 8.484 -25.467 -16.754 1.00 48.14 C ANISOU 167 CB ASP A 22 5947 6953 5391 345 668 822 C ATOM 168 CG ASP A 22 7.590 -26.475 -17.476 1.00 47.29 C ANISOU 168 CG ASP A 22 6116 6751 5102 586 782 659 C ATOM 169 OD1 ASP A 22 6.609 -26.070 -18.133 1.00 42.15 O ANISOU 169 OD1 ASP A 22 5642 5987 4385 530 814 589 O ATOM 170 OD2 ASP A 22 7.852 -27.694 -17.392 1.00 47.05 O ANISOU 170 OD2 ASP A 22 6148 6744 4987 831 819 601 O ATOM 171 N GLY A 23 6.816 -23.069 -18.803 1.00 46.29 N ANISOU 171 N GLY A 23 5957 6526 5106 49 788 881 N ATOM 172 CA GLY A 23 6.761 -22.381 -20.094 1.00 46.84 C ANISOU 172 CA GLY A 23 6013 6665 5121 39 930 1014 C ATOM 173 C GLY A 23 6.992 -23.282 -21.296 1.00 47.52 C ANISOU 173 C GLY A 23 6089 6939 5029 334 1152 1041 C ATOM 174 O GLY A 23 7.377 -22.811 -22.376 1.00 49.74 O ANISOU 174 O GLY A 23 6272 7372 5253 362 1309 1218 O ATOM 175 N ASP A 24 6.791 -24.588 -21.114 1.00 46.22 N ANISOU 175 N ASP A 24 6049 6755 4759 566 1164 875 N ATOM 176 CA ASP A 24 6.993 -25.514 -22.228 1.00 46.26 C ANISOU 176 CA ASP A 24 6125 6894 4558 887 1351 864 C ATOM 177 C ASP A 24 5.776 -25.636 -23.118 1.00 44.16 C ANISOU 177 C ASP A 24 6168 6493 4120 949 1361 719 C ATOM 178 O ASP A 24 5.789 -26.418 -24.065 1.00 45.48 O ANISOU 178 O ASP A 24 6478 6722 4080 1215 1480 670 O ATOM 179 CB ASP A 24 7.484 -26.895 -21.766 1.00 46.84 C ANISOU 179 CB ASP A 24 6228 6997 4573 1145 1357 771 C ATOM 180 CG ASP A 24 6.390 -27.731 -21.066 1.00 44.56 C ANISOU 180 CG ASP A 24 6252 6429 4249 1134 1188 519 C ATOM 181 OD1 ASP A 24 6.668 -28.915 -20.824 1.00 44.30 O ANISOU 181 OD1 ASP A 24 6324 6368 4140 1354 1186 437 O ATOM 182 OD2 ASP A 24 5.274 -27.232 -20.750 1.00 40.41 O ANISOU 182 OD2 ASP A 24 5864 5724 3766 918 1062 423 O ATOM 183 N GLY A 25 4.734 -24.865 -22.835 1.00 40.86 N ANISOU 183 N GLY A 25 5860 5897 3766 727 1229 653 N ATOM 184 CA GLY A 25 3.565 -24.834 -23.730 1.00 39.37 C ANISOU 184 CA GLY A 25 5914 5621 3421 765 1222 553 C ATOM 185 C GLY A 25 2.578 -25.971 -23.489 1.00 37.55 C ANISOU 185 C GLY A 25 5938 5237 3094 834 1103 327 C ATOM 186 O GLY A 25 1.630 -26.138 -24.252 1.00 35.84 O ANISOU 186 O GLY A 25 5918 4965 2734 867 1069 241 O ATOM 187 N THR A 26 2.762 -26.729 -22.392 1.00 37.10 N ANISOU 187 N THR A 26 5875 5105 3117 826 1017 247 N ATOM 188 CA THR A 26 1.789 -27.751 -22.012 1.00 36.13 C ANISOU 188 CA THR A 26 5982 4815 2930 822 881 69 C ATOM 189 C THR A 26 1.491 -27.648 -20.526 1.00 33.64 C ANISOU 189 C THR A 26 5600 4408 2773 645 752 39 C ATOM 190 O THR A 26 2.351 -27.207 -19.740 1.00 35.13 O ANISOU 190 O THR A 26 5600 4652 3095 598 759 123 O ATOM 191 CB THR A 26 2.269 -29.190 -22.337 1.00 38.50 C ANISOU 191 CB THR A 26 6460 5083 3087 1068 911 -15 C ATOM 192 OG1 THR A 26 3.225 -29.585 -21.348 1.00 44.75 O ANISOU 192 OG1 THR A 26 7116 5901 3986 1124 917 27 O ATOM 193 CG2 THR A 26 2.930 -29.275 -23.697 1.00 41.88 C ANISOU 193 CG2 THR A 26 6927 5652 3335 1322 1084 37 C ATOM 194 N ILE A 27 0.281 -28.037 -20.123 1.00 30.29 N ANISOU 194 N ILE A 27 5319 3865 2325 539 626 -64 N ATOM 195 CA ILE A 27 -0.079 -28.088 -18.710 1.00 28.63 C ANISOU 195 CA ILE A 27 5071 3588 2219 407 522 -88 C ATOM 196 C ILE A 27 -0.155 -29.572 -18.277 1.00 29.42 C ANISOU 196 C ILE A 27 5337 3577 2263 455 450 -165 C ATOM 197 O ILE A 27 -0.925 -30.374 -18.856 1.00 29.40 O ANISOU 197 O ILE A 27 5533 3488 2150 450 388 -236 O ATOM 198 CB ILE A 27 -1.404 -27.368 -18.431 1.00 26.67 C ANISOU 198 CB ILE A 27 4822 3326 1984 257 451 -103 C ATOM 199 CG1 ILE A 27 -1.258 -25.876 -18.765 1.00 26.92 C ANISOU 199 CG1 ILE A 27 4743 3416 2071 230 505 -25 C ATOM 200 CG2 ILE A 27 -1.774 -27.473 -16.925 1.00 25.48 C ANISOU 200 CG2 ILE A 27 4643 3136 1901 160 369 -119 C ATOM 201 CD1 ILE A 27 -2.580 -25.148 -18.792 1.00 29.04 C ANISOU 201 CD1 ILE A 27 5033 3687 2313 165 456 -36 C ATOM 202 N THR A 28 0.648 -29.935 -17.283 1.00 28.99 N ANISOU 202 N THR A 28 5222 3512 2281 493 436 -142 N ATOM 203 CA THR A 28 0.672 -31.317 -16.816 1.00 29.99 C ANISOU 203 CA THR A 28 5529 3509 2356 554 365 -194 C ATOM 204 C THR A 28 -0.203 -31.475 -15.564 1.00 28.41 C ANISOU 204 C THR A 28 5351 3242 2200 369 254 -197 C ATOM 205 O THR A 28 -0.651 -30.500 -14.968 1.00 27.05 O ANISOU 205 O THR A 28 5042 3143 2092 246 247 -167 O ATOM 206 CB THR A 28 2.091 -31.746 -16.431 1.00 31.34 C ANISOU 206 CB THR A 28 5624 3726 2559 746 412 -150 C ATOM 207 OG1 THR A 28 2.520 -30.918 -15.331 1.00 30.69 O ANISOU 207 OG1 THR A 28 5321 3730 2609 641 384 -80 O ATOM 208 CG2 THR A 28 3.060 -31.584 -17.634 1.00 32.42 C ANISOU 208 CG2 THR A 28 5686 3995 2637 966 561 -107 C ATOM 209 N THR A 29 -0.450 -32.715 -15.149 1.00 28.97 N ANISOU 209 N THR A 29 5616 3170 2222 363 169 -222 N ATOM 210 CA THR A 29 -1.179 -32.918 -13.894 1.00 27.65 C ANISOU 210 CA THR A 29 5451 2971 2084 195 86 -184 C ATOM 211 C THR A 29 -0.475 -32.238 -12.705 1.00 27.11 C ANISOU 211 C THR A 29 5207 2997 2097 218 103 -138 C ATOM 212 O THR A 29 -1.122 -31.749 -11.783 1.00 25.92 O ANISOU 212 O THR A 29 4992 2899 1959 99 78 -110 O ATOM 213 CB THR A 29 -1.318 -34.402 -13.547 1.00 28.75 C ANISOU 213 CB THR A 29 5841 2919 2164 185 -13 -185 C ATOM 214 OG1 THR A 29 -0.024 -35.001 -13.608 1.00 30.29 O ANISOU 214 OG1 THR A 29 6111 3052 2345 429 12 -203 O ATOM 215 CG2 THR A 29 -2.251 -35.111 -14.554 1.00 29.48 C ANISOU 215 CG2 THR A 29 6154 2879 2168 81 -97 -230 C ATOM 216 N LYS A 30 0.850 -32.240 -12.720 1.00 27.83 N ANISOU 216 N LYS A 30 5226 3124 2226 382 137 -125 N ATOM 217 CA LYS A 30 1.614 -31.668 -11.606 1.00 28.56 C ANISOU 217 CA LYS A 30 5161 3299 2391 385 106 -79 C ATOM 218 C LYS A 30 1.409 -30.158 -11.545 1.00 27.27 C ANISOU 218 C LYS A 30 4841 3234 2288 271 122 -74 C ATOM 219 O LYS A 30 1.313 -29.577 -10.457 1.00 27.17 O ANISOU 219 O LYS A 30 4791 3241 2291 198 58 -69 O ATOM 220 CB LYS A 30 3.128 -31.911 -11.790 1.00 27.97 C ANISOU 220 CB LYS A 30 4977 3294 2355 578 133 -35 C ATOM 221 CG LYS A 30 3.597 -33.371 -11.768 1.00 34.24 C ANISOU 221 CG LYS A 30 5944 3984 3080 775 115 -37 C ATOM 222 CD LYS A 30 5.135 -33.336 -11.860 1.00 37.47 C ANISOU 222 CD LYS A 30 6151 4550 3536 990 157 38 C ATOM 223 CE LYS A 30 5.775 -34.661 -12.125 1.00 41.78 C ANISOU 223 CE LYS A 30 6855 5024 3995 1285 176 38 C ATOM 224 NZ LYS A 30 5.242 -35.325 -13.402 1.00 39.51 N ANISOU 224 NZ LYS A 30 6832 4596 3585 1394 245 -51 N ATOM 225 N GLU A 31 1.404 -29.526 -12.703 1.00 26.87 N ANISOU 225 N GLU A 31 4730 3228 2252 278 199 -74 N ATOM 226 CA GLU A 31 1.158 -28.074 -12.795 1.00 26.91 C ANISOU 226 CA GLU A 31 4635 3282 2306 177 208 -63 C ATOM 227 C GLU A 31 -0.263 -27.715 -12.327 1.00 24.68 C ANISOU 227 C GLU A 31 4434 2973 1970 86 181 -104 C ATOM 228 O GLU A 31 -0.462 -26.749 -11.618 1.00 26.29 O ANISOU 228 O GLU A 31 4618 3183 2187 40 142 -111 O ATOM 229 CB GLU A 31 1.442 -27.583 -14.238 1.00 25.39 C ANISOU 229 CB GLU A 31 4380 3144 2122 217 307 -28 C ATOM 230 CG GLU A 31 2.956 -27.514 -14.489 1.00 31.30 C ANISOU 230 CG GLU A 31 4962 3993 2940 296 349 63 C ATOM 231 CD GLU A 31 3.349 -27.259 -15.930 1.00 31.56 C ANISOU 231 CD GLU A 31 4929 4117 2946 375 482 127 C ATOM 232 OE1 GLU A 31 2.704 -27.807 -16.833 1.00 31.77 O ANISOU 232 OE1 GLU A 31 5101 4110 2862 458 539 69 O ATOM 233 OE2 GLU A 31 4.328 -26.512 -16.177 1.00 33.39 O ANISOU 233 OE2 GLU A 31 4964 4465 3259 346 521 250 O ATOM 234 N LEU A 32 -1.257 -28.485 -12.729 1.00 25.21 N ANISOU 234 N LEU A 32 4595 3019 1965 66 193 -122 N ATOM 235 CA ALEU A 32 -2.626 -28.286 -12.213 0.50 24.86 C ANISOU 235 CA ALEU A 32 4569 3011 1865 -14 177 -120 C ATOM 236 CA BLEU A 32 -2.622 -28.297 -12.240 0.50 26.03 C ANISOU 236 CA BLEU A 32 4718 3159 2013 -14 178 -120 C ATOM 237 C LEU A 32 -2.686 -28.483 -10.714 1.00 25.97 C ANISOU 237 C LEU A 32 4729 3160 1980 -29 133 -104 C ATOM 238 O LEU A 32 -3.298 -27.686 -9.990 1.00 26.24 O ANISOU 238 O LEU A 32 4741 3257 1973 -27 138 -103 O ATOM 239 CB ALEU A 32 -3.592 -29.296 -12.836 0.50 25.02 C ANISOU 239 CB ALEU A 32 4668 3017 1823 -83 160 -110 C ATOM 240 CB BLEU A 32 -3.517 -29.325 -12.947 0.50 27.03 C ANISOU 240 CB BLEU A 32 4926 3264 2078 -77 162 -113 C ATOM 241 CG ALEU A 32 -3.870 -29.141 -14.315 0.50 21.74 C ANISOU 241 CG ALEU A 32 4269 2608 1384 -73 182 -132 C ATOM 242 CG BLEU A 32 -5.031 -29.204 -12.982 0.50 29.10 C ANISOU 242 CG BLEU A 32 5149 3621 2286 -179 150 -73 C ATOM 243 CD1ALEU A 32 -4.612 -30.338 -14.796 0.50 20.70 C ANISOU 243 CD1ALEU A 32 4263 2417 1186 -166 108 -133 C ATOM 244 CD1BLEU A 32 -5.474 -27.809 -13.481 0.50 29.71 C ANISOU 244 CD1BLEU A 32 5129 3795 2366 -125 201 -78 C ATOM 245 CD2ALEU A 32 -4.692 -27.860 -14.614 0.50 17.94 C ANISOU 245 CD2ALEU A 32 3684 2235 896 -79 216 -114 C ATOM 246 CD2BLEU A 32 -5.542 -30.313 -13.930 0.50 31.38 C ANISOU 246 CD2BLEU A 32 5547 3846 2531 -273 83 -73 C ATOM 247 N GLY A 33 -2.040 -29.542 -10.230 1.00 26.73 N ANISOU 247 N GLY A 33 4888 3192 2077 -12 92 -89 N ATOM 248 CA GLY A 33 -2.008 -29.839 -8.786 1.00 26.12 C ANISOU 248 CA GLY A 33 4848 3122 1954 -16 44 -60 C ATOM 249 C GLY A 33 -1.401 -28.658 -8.020 1.00 27.58 C ANISOU 249 C GLY A 33 4981 3342 2155 27 7 -93 C ATOM 250 O GLY A 33 -1.935 -28.222 -7.004 1.00 26.71 O ANISOU 250 O GLY A 33 4907 3279 1962 34 -6 -96 O ATOM 251 N THR A 34 -0.293 -28.118 -8.511 1.00 26.87 N ANISOU 251 N THR A 34 4818 3234 2158 53 -17 -111 N ATOM 252 CA THR A 34 0.382 -27.041 -7.795 1.00 28.25 C ANISOU 252 CA THR A 34 4966 3408 2360 43 -105 -134 C ATOM 253 C THR A 34 -0.518 -25.788 -7.680 1.00 27.08 C ANISOU 253 C THR A 34 4876 3254 2159 32 -93 -182 C ATOM 254 O THR A 34 -0.595 -25.143 -6.628 1.00 27.09 O ANISOU 254 O THR A 34 4969 3236 2087 54 -169 -225 O ATOM 255 CB THR A 34 1.692 -26.721 -8.532 1.00 29.52 C ANISOU 255 CB THR A 34 4991 3578 2647 30 -128 -97 C ATOM 256 OG1 THR A 34 2.669 -27.612 -8.015 1.00 35.52 O ANISOU 256 OG1 THR A 34 5704 4365 3425 86 -187 -56 O ATOM 257 CG2 THR A 34 2.188 -25.290 -8.304 1.00 31.02 C ANISOU 257 CG2 THR A 34 5153 3740 2895 -59 -225 -104 C ATOM 258 N VAL A 35 -1.234 -25.474 -8.761 1.00 27.43 N ANISOU 258 N VAL A 35 4893 3313 2217 28 -2 -178 N ATOM 259 CA VAL A 35 -2.101 -24.276 -8.755 1.00 28.16 C ANISOU 259 CA VAL A 35 5045 3400 2253 66 16 -213 C ATOM 260 C VAL A 35 -3.298 -24.505 -7.800 1.00 28.96 C ANISOU 260 C VAL A 35 5204 3592 2206 142 57 -217 C ATOM 261 O VAL A 35 -3.603 -23.651 -6.957 1.00 29.62 O ANISOU 261 O VAL A 35 5395 3667 2194 233 29 -265 O ATOM 262 CB VAL A 35 -2.580 -23.895 -10.186 1.00 28.46 C ANISOU 262 CB VAL A 35 5031 3451 2331 61 96 -190 C ATOM 263 CG1 VAL A 35 -3.730 -22.859 -10.075 1.00 27.72 C ANISOU 263 CG1 VAL A 35 5006 3379 2149 155 125 -214 C ATOM 264 CG2 VAL A 35 -1.371 -23.296 -10.991 1.00 27.07 C ANISOU 264 CG2 VAL A 35 4805 3203 2276 -2 68 -161 C ATOM 265 N MET A 36 -3.947 -25.667 -7.882 1.00 28.87 N ANISOU 265 N MET A 36 5137 3669 2163 106 118 -155 N ATOM 266 CA AMET A 36 -5.099 -25.886 -7.037 0.50 30.41 C ANISOU 266 CA AMET A 36 5334 3998 2221 154 176 -107 C ATOM 267 CA BMET A 36 -5.116 -25.963 -7.042 0.50 30.86 C ANISOU 267 CA BMET A 36 5388 4059 2279 149 177 -102 C ATOM 268 C MET A 36 -4.710 -25.926 -5.574 1.00 31.47 C ANISOU 268 C MET A 36 5571 4130 2257 215 127 -124 C ATOM 269 O MET A 36 -5.439 -25.385 -4.727 1.00 32.67 O ANISOU 269 O MET A 36 5774 4380 2258 340 172 -127 O ATOM 270 CB AMET A 36 -5.856 -27.118 -7.466 0.50 29.81 C ANISOU 270 CB AMET A 36 5178 4003 2147 42 219 -7 C ATOM 271 CB BMET A 36 -5.758 -27.323 -7.360 0.50 30.92 C ANISOU 271 CB BMET A 36 5327 4133 2288 28 211 -1 C ATOM 272 CG AMET A 36 -6.435 -26.921 -8.837 0.50 31.58 C ANISOU 272 CG AMET A 36 5321 4255 2424 2 247 1 C ATOM 273 CG BMET A 36 -6.429 -27.481 -8.736 0.50 34.31 C ANISOU 273 CG BMET A 36 5673 4595 2770 -47 236 27 C ATOM 274 SD AMET A 36 -6.794 -28.481 -9.586 0.50 31.26 S ANISOU 274 SD AMET A 36 5267 4193 2415 -181 212 75 S ATOM 275 SD BMET A 36 -7.313 -26.028 -9.348 0.50 42.52 S ANISOU 275 SD BMET A 36 6636 5743 3775 73 297 9 S ATOM 276 CE AMET A 36 -8.064 -29.044 -8.489 0.50 36.24 C ANISOU 276 CE AMET A 36 5817 5016 2937 -255 251 226 C ATOM 277 CE BMET A 36 -9.016 -26.279 -8.814 0.50 39.18 C ANISOU 277 CE BMET A 36 6060 5600 3226 81 377 150 C ATOM 278 N ARG A 37 -3.545 -26.513 -5.277 1.00 30.65 N ANISOU 278 N ARG A 37 5501 3928 2216 161 35 -136 N ATOM 279 CA ARG A 37 -3.047 -26.494 -3.899 1.00 30.63 C ANISOU 279 CA ARG A 37 5608 3917 2112 219 -47 -158 C ATOM 280 C ARG A 37 -2.721 -25.090 -3.409 1.00 32.27 C ANISOU 280 C ARG A 37 5938 4058 2267 302 -135 -268 C ATOM 281 O ARG A 37 -2.953 -24.791 -2.225 1.00 31.50 O ANISOU 281 O ARG A 37 5980 3994 1996 412 -165 -302 O ATOM 282 CB ARG A 37 -1.848 -27.444 -3.680 1.00 30.48 C ANISOU 282 CB ARG A 37 5586 3827 2170 164 -144 -131 C ATOM 283 CG ARG A 37 -2.230 -28.934 -3.619 1.00 29.86 C ANISOU 283 CG ARG A 37 5503 3771 2070 116 -92 -22 C ATOM 284 CD ARG A 37 -1.034 -29.776 -3.203 1.00 29.93 C ANISOU 284 CD ARG A 37 5549 3705 2118 132 -198 1 C ATOM 285 NE ARG A 37 0.086 -29.728 -4.164 1.00 27.16 N ANISOU 285 NE ARG A 37 5106 3288 1925 135 -242 -33 N ATOM 286 CZ ARG A 37 0.197 -30.472 -5.261 1.00 29.54 C ANISOU 286 CZ ARG A 37 5377 3537 2308 127 -190 -10 C ATOM 287 NH1 ARG A 37 -0.766 -31.324 -5.627 1.00 29.08 N ANISOU 287 NH1 ARG A 37 5390 3448 2212 71 -125 35 N ATOM 288 NH2 ARG A 37 1.303 -30.382 -6.002 1.00 28.94 N ANISOU 288 NH2 ARG A 37 5205 3449 2342 177 -210 -23 N ATOM 289 N SER A 38 -2.216 -24.222 -4.289 1.00 32.08 N ANISOU 289 N SER A 38 5892 3928 2369 254 -184 -318 N ATOM 290 CA SER A 38 -1.978 -22.829 -3.849 1.00 35.77 C ANISOU 290 CA SER A 38 6530 4277 2783 307 -299 -420 C ATOM 291 C SER A 38 -3.300 -22.108 -3.482 1.00 38.32 C ANISOU 291 C SER A 38 6982 4660 2920 504 -200 -462 C ATOM 292 O SER A 38 -3.270 -21.099 -2.784 1.00 39.65 O ANISOU 292 O SER A 38 7375 4723 2965 615 -295 -564 O ATOM 293 CB SER A 38 -1.185 -22.007 -4.859 1.00 34.62 C ANISOU 293 CB SER A 38 6345 3996 2812 186 -377 -429 C ATOM 294 OG SER A 38 -1.965 -21.776 -6.004 1.00 34.80 O ANISOU 294 OG SER A 38 6295 4050 2877 211 -241 -397 O ATOM 295 N LEU A 39 -4.440 -22.659 -3.908 1.00 38.79 N ANISOU 295 N LEU A 39 6904 4891 2943 555 -23 -378 N ATOM 296 CA LEU A 39 -5.748 -22.125 -3.528 1.00 41.85 C ANISOU 296 CA LEU A 39 7341 5417 3143 773 100 -374 C ATOM 297 C LEU A 39 -6.420 -22.880 -2.385 1.00 44.03 C ANISOU 297 C LEU A 39 7601 5900 3228 869 196 -298 C ATOM 298 O LEU A 39 -7.614 -22.690 -2.144 1.00 47.86 O ANISOU 298 O LEU A 39 8037 6588 3559 1046 345 -237 O ATOM 299 CB LEU A 39 -6.685 -22.058 -4.727 1.00 41.67 C ANISOU 299 CB LEU A 39 7145 5501 3187 778 223 -301 C ATOM 300 CG LEU A 39 -6.262 -21.092 -5.835 1.00 42.43 C ANISOU 300 CG LEU A 39 7288 5418 3417 743 158 -359 C ATOM 301 CD1 LEU A 39 -6.910 -21.466 -7.128 1.00 43.37 C ANISOU 301 CD1 LEU A 39 7205 5646 3628 675 251 -269 C ATOM 302 CD2 LEU A 39 -6.554 -19.651 -5.452 1.00 46.26 C ANISOU 302 CD2 LEU A 39 8013 5791 3772 966 121 -458 C ATOM 303 N GLY A 40 -5.676 -23.716 -1.677 1.00 42.53 N ANISOU 303 N GLY A 40 7439 5682 3038 769 121 -278 N ATOM 304 CA GLY A 40 -6.236 -24.462 -0.569 1.00 44.09 C ANISOU 304 CA GLY A 40 7639 6066 3047 843 210 -180 C ATOM 305 C GLY A 40 -7.020 -25.718 -0.925 1.00 43.58 C ANISOU 305 C GLY A 40 7347 6181 3030 703 341 13 C ATOM 306 O GLY A 40 -7.635 -26.326 -0.045 1.00 44.52 O ANISOU 306 O GLY A 40 7442 6485 2989 744 437 142 O ATOM 307 N GLN A 41 -6.989 -26.132 -2.195 1.00 41.02 N ANISOU 307 N GLN A 41 6877 5798 2911 526 333 44 N ATOM 308 CA GLN A 41 -7.609 -27.389 -2.592 1.00 40.78 C ANISOU 308 CA GLN A 41 6686 5869 2938 344 395 212 C ATOM 309 C GLN A 41 -6.600 -28.541 -2.587 1.00 40.01 C ANISOU 309 C GLN A 41 6654 5600 2949 183 286 229 C ATOM 310 O GLN A 41 -5.387 -28.333 -2.563 1.00 40.11 O ANISOU 310 O GLN A 41 6765 5442 3033 204 172 115 O ATOM 311 CB GLN A 41 -8.268 -27.249 -3.967 1.00 40.63 C ANISOU 311 CB GLN A 41 6511 5888 3040 262 430 235 C ATOM 312 CG GLN A 41 -9.324 -26.169 -3.938 1.00 44.49 C ANISOU 312 CG GLN A 41 6922 6572 3409 460 542 244 C ATOM 313 CD GLN A 41 -9.978 -25.938 -5.251 1.00 47.38 C ANISOU 313 CD GLN A 41 7135 6993 3875 406 560 271 C ATOM 314 OE1 GLN A 41 -9.681 -26.605 -6.246 1.00 51.94 O ANISOU 314 OE1 GLN A 41 7675 7459 4602 206 488 276 O ATOM 315 NE2 GLN A 41 -10.867 -24.970 -5.285 1.00 46.30 N ANISOU 315 NE2 GLN A 41 6929 7027 3636 614 652 284 N ATOM 316 N ASN A 42 -7.106 -29.768 -2.560 1.00 39.40 N ANISOU 316 N ASN A 42 6524 5571 2875 25 312 388 N ATOM 317 CA AASN A 42 -6.227 -30.929 -2.524 0.50 38.11 C ANISOU 317 CA AASN A 42 6466 5224 2790 -86 210 412 C ATOM 318 CA BASN A 42 -6.273 -30.933 -2.486 0.50 38.34 C ANISOU 318 CA BASN A 42 6493 5262 2812 -86 214 418 C ATOM 319 C ASN A 42 -6.737 -32.010 -3.460 1.00 37.35 C ANISOU 319 C ASN A 42 6332 5067 2792 -298 192 513 C ATOM 320 O ASN A 42 -7.182 -33.049 -3.029 1.00 37.61 O ANISOU 320 O ASN A 42 6400 5108 2784 -437 187 673 O ATOM 321 CB AASN A 42 -6.031 -31.465 -1.099 0.50 40.29 C ANISOU 321 CB AASN A 42 6852 5537 2917 -43 202 503 C ATOM 322 CB BASN A 42 -6.260 -31.426 -1.037 0.50 40.76 C ANISOU 322 CB BASN A 42 6894 5638 2956 -44 225 524 C ATOM 323 CG AASN A 42 -4.823 -32.413 -0.982 0.50 40.74 C ANISOU 323 CG AASN A 42 7049 5380 3049 -72 70 490 C ATOM 324 CG BASN A 42 -5.478 -30.498 -0.139 0.50 42.25 C ANISOU 324 CG BASN A 42 7193 5818 3042 156 175 391 C ATOM 325 OD1AASN A 42 -3.869 -32.349 -1.766 0.50 39.21 O ANISOU 325 OD1AASN A 42 6865 5035 2997 -51 -12 375 O ATOM 326 OD1BASN A 42 -4.302 -30.231 -0.397 0.50 44.09 O ANISOU 326 OD1BASN A 42 7483 5889 3379 186 50 260 O ATOM 327 ND2AASN A 42 -4.874 -33.294 0.009 0.50 42.93 N ANISOU 327 ND2AASN A 42 7427 5668 3217 -99 60 631 N ATOM 328 ND2BASN A 42 -6.128 -29.960 0.879 0.50 45.09 N ANISOU 328 ND2BASN A 42 7580 6363 3189 297 263 426 N ATOM 329 N PRO A 43 -6.632 -31.754 -4.778 1.00 34.79 N ANISOU 329 N PRO A 43 5965 4662 2592 -331 165 420 N ATOM 330 CA PRO A 43 -7.085 -32.760 -5.740 1.00 34.22 C ANISOU 330 CA PRO A 43 5910 4500 2591 -527 111 485 C ATOM 331 C PRO A 43 -6.212 -34.046 -5.671 1.00 34.94 C ANISOU 331 C PRO A 43 6212 4344 2719 -574 5 494 C ATOM 332 O PRO A 43 -4.984 -33.962 -5.461 1.00 35.07 O ANISOU 332 O PRO A 43 6311 4251 2763 -418 -29 396 O ATOM 333 CB PRO A 43 -6.904 -32.041 -7.090 1.00 32.98 C ANISOU 333 CB PRO A 43 5702 4305 2524 -478 106 351 C ATOM 334 CG PRO A 43 -5.775 -31.119 -6.870 1.00 32.89 C ANISOU 334 CG PRO A 43 5711 4246 2539 -290 115 218 C ATOM 335 CD PRO A 43 -6.085 -30.560 -5.465 1.00 32.88 C ANISOU 335 CD PRO A 43 5686 4390 2416 -202 168 260 C ATOM 336 N THR A 44 -6.826 -35.214 -5.794 1.00 33.53 N ANISOU 336 N THR A 44 6123 4080 2536 -781 -59 624 N ATOM 337 CA THR A 44 -6.064 -36.449 -5.874 1.00 33.62 C ANISOU 337 CA THR A 44 6392 3810 2573 -800 -174 623 C ATOM 338 C THR A 44 -5.457 -36.642 -7.265 1.00 32.23 C ANISOU 338 C THR A 44 6331 3444 2471 -734 -238 467 C ATOM 339 O THR A 44 -5.846 -35.965 -8.231 1.00 29.55 O ANISOU 339 O THR A 44 5875 3189 2164 -748 -210 394 O ATOM 340 CB THR A 44 -6.940 -37.669 -5.630 1.00 36.86 C ANISOU 340 CB THR A 44 6921 4132 2951 -1076 -255 819 C ATOM 341 OG1 THR A 44 -7.812 -37.858 -6.755 1.00 37.85 O ANISOU 341 OG1 THR A 44 7021 4239 3121 -1284 -324 829 O ATOM 342 CG2 THR A 44 -7.701 -37.593 -4.249 1.00 38.40 C ANISOU 342 CG2 THR A 44 6983 4564 3044 -1162 -164 1032 C ATOM 343 N GLU A 45 -4.496 -37.554 -7.374 1.00 33.26 N ANISOU 343 N GLU A 45 6700 3330 2608 -626 -318 423 N ATOM 344 CA GLU A 45 -3.924 -37.877 -8.685 1.00 35.55 C ANISOU 344 CA GLU A 45 7139 3442 2925 -519 -365 285 C ATOM 345 C GLU A 45 -4.993 -38.279 -9.711 1.00 36.28 C ANISOU 345 C GLU A 45 7320 3459 3007 -747 -452 292 C ATOM 346 O GLU A 45 -4.948 -37.867 -10.894 1.00 35.82 O ANISOU 346 O GLU A 45 7246 3410 2956 -685 -442 174 O ATOM 347 CB GLU A 45 -2.833 -38.946 -8.554 1.00 36.87 C ANISOU 347 CB GLU A 45 7582 3359 3069 -332 -437 259 C ATOM 348 CG GLU A 45 -3.328 -40.386 -8.207 1.00 42.57 C ANISOU 348 CG GLU A 45 8628 3806 3739 -507 -582 375 C ATOM 349 CD GLU A 45 -4.105 -40.495 -6.895 1.00 44.35 C ANISOU 349 CD GLU A 45 8770 4140 3941 -728 -578 576 C ATOM 350 OE1 GLU A 45 -3.493 -40.407 -5.811 1.00 48.92 O ANISOU 350 OE1 GLU A 45 9310 4785 4493 -591 -537 627 O ATOM 351 OE2 GLU A 45 -5.336 -40.716 -6.933 1.00 48.58 O ANISOU 351 OE2 GLU A 45 9279 4709 4472 -1042 -622 702 O ATOM 352 N ALA A 46 -5.977 -39.062 -9.262 1.00 36.84 N ANISOU 352 N ALA A 46 7474 3470 3055 -1031 -548 450 N ATOM 353 CA ALA A 46 -7.037 -39.491 -10.175 1.00 38.84 C ANISOU 353 CA ALA A 46 7800 3656 3303 -1305 -678 482 C ATOM 354 C ALA A 46 -7.870 -38.305 -10.672 1.00 37.01 C ANISOU 354 C ALA A 46 7232 3737 3094 -1366 -595 478 C ATOM 355 O ALA A 46 -8.179 -38.237 -11.873 1.00 36.86 O ANISOU 355 O ALA A 46 7259 3680 3067 -1412 -670 391 O ATOM 356 CB ALA A 46 -7.928 -40.597 -9.523 1.00 41.77 C ANISOU 356 CB ALA A 46 8303 3909 3657 -1657 -818 702 C ATOM 357 N GLU A 47 -8.228 -37.377 -9.781 1.00 35.68 N ANISOU 357 N GLU A 47 6757 3868 2932 -1335 -447 567 N ATOM 358 CA GLU A 47 -8.996 -36.167 -10.150 1.00 35.84 C ANISOU 358 CA GLU A 47 6469 4188 2959 -1327 -354 568 C ATOM 359 C GLU A 47 -8.217 -35.323 -11.141 1.00 34.62 C ANISOU 359 C GLU A 47 6316 4008 2828 -1088 -302 368 C ATOM 360 O GLU A 47 -8.771 -34.766 -12.105 1.00 35.00 O ANISOU 360 O GLU A 47 6264 4158 2877 -1113 -312 332 O ATOM 361 CB GLU A 47 -9.343 -35.321 -8.899 1.00 36.09 C ANISOU 361 CB GLU A 47 6246 4508 2956 -1248 -194 673 C ATOM 362 CG GLU A 47 -10.474 -35.939 -8.046 1.00 41.59 C ANISOU 362 CG GLU A 47 6833 5361 3608 -1505 -203 931 C ATOM 363 CD GLU A 47 -10.544 -35.449 -6.572 1.00 46.78 C ANISOU 363 CD GLU A 47 7352 6242 4178 -1375 -42 1037 C ATOM 364 OE1 GLU A 47 -9.710 -34.669 -6.097 1.00 45.26 O ANISOU 364 OE1 GLU A 47 7181 6055 3961 -1105 45 902 O ATOM 365 OE2 GLU A 47 -11.473 -35.884 -5.875 1.00 51.42 O ANISOU 365 OE2 GLU A 47 7816 7010 4711 -1562 -14 1275 O ATOM 366 N LEU A 48 -6.913 -35.224 -10.930 1.00 33.26 N ANISOU 366 N LEU A 48 6245 3719 2672 -857 -250 259 N ATOM 367 CA LEU A 48 -6.085 -34.428 -11.842 1.00 32.05 C ANISOU 367 CA LEU A 48 6069 3564 2543 -646 -187 110 C ATOM 368 C LEU A 48 -6.050 -35.104 -13.215 1.00 34.24 C ANISOU 368 C LEU A 48 6553 3670 2786 -664 -283 26 C ATOM 369 O LEU A 48 -6.169 -34.437 -14.275 1.00 33.52 O ANISOU 369 O LEU A 48 6403 3650 2682 -610 -256 -42 O ATOM 370 CB LEU A 48 -4.679 -34.300 -11.263 1.00 31.39 C ANISOU 370 CB LEU A 48 6016 3423 2489 -428 -129 53 C ATOM 371 CG LEU A 48 -4.566 -33.433 -10.009 1.00 31.14 C ANISOU 371 CG LEU A 48 5813 3549 2468 -379 -56 95 C ATOM 372 CD1 LEU A 48 -3.175 -33.570 -9.410 1.00 31.73 C ANISOU 372 CD1 LEU A 48 5937 3551 2568 -209 -59 59 C ATOM 373 CD2 LEU A 48 -4.864 -31.969 -10.385 1.00 32.56 C ANISOU 373 CD2 LEU A 48 5806 3897 2668 -328 25 53 C ATOM 374 N GLN A 49 -5.868 -36.421 -13.218 1.00 35.49 N ANISOU 374 N GLN A 49 6992 3583 2908 -719 -404 27 N ATOM 375 CA GLN A 49 -5.907 -37.128 -14.473 1.00 38.61 C ANISOU 375 CA GLN A 49 7654 3782 3232 -727 -524 -68 C ATOM 376 C GLN A 49 -7.272 -36.995 -15.159 1.00 39.45 C ANISOU 376 C GLN A 49 7692 3979 3318 -993 -635 -21 C ATOM 377 O GLN A 49 -7.302 -36.791 -16.341 1.00 40.09 O ANISOU 377 O GLN A 49 7846 4045 3340 -933 -668 -121 O ATOM 378 CB GLN A 49 -5.571 -38.589 -14.299 1.00 41.55 C ANISOU 378 CB GLN A 49 8402 3829 3554 -744 -665 -75 C ATOM 379 CG GLN A 49 -4.101 -38.886 -14.216 1.00 43.00 C ANISOU 379 CG GLN A 49 8731 3892 3716 -394 -585 -165 C ATOM 380 CD GLN A 49 -3.874 -40.386 -14.161 1.00 49.67 C ANISOU 380 CD GLN A 49 10013 4372 4485 -380 -747 -179 C ATOM 381 OE1 GLN A 49 -4.443 -41.072 -13.316 1.00 51.39 O ANISOU 381 OE1 GLN A 49 10327 4475 4725 -616 -857 -53 O ATOM 382 NE2 GLN A 49 -3.044 -40.896 -15.052 1.00 48.98 N ANISOU 382 NE2 GLN A 49 10211 4104 4296 -89 -756 -321 N ATOM 383 N ASP A 50 -8.382 -37.109 -14.428 1.00 40.76 N ANISOU 383 N ASP A 50 7702 4267 3519 -1276 -691 146 N ATOM 384 CA ASP A 50 -9.717 -36.920 -15.017 1.00 42.74 C ANISOU 384 CA ASP A 50 7806 4674 3760 -1533 -800 228 C ATOM 385 C ASP A 50 -9.945 -35.511 -15.595 1.00 40.99 C ANISOU 385 C ASP A 50 7304 4727 3542 -1384 -672 186 C ATOM 386 O ASP A 50 -10.610 -35.348 -16.629 1.00 40.88 O ANISOU 386 O ASP A 50 7273 4773 3486 -1472 -775 168 O ATOM 387 CB ASP A 50 -10.832 -37.282 -14.033 1.00 45.27 C ANISOU 387 CB ASP A 50 7944 5140 4117 -1850 -852 464 C ATOM 388 CG ASP A 50 -10.811 -38.774 -13.616 1.00 51.83 C ANISOU 388 CG ASP A 50 9094 5661 4939 -2081 -1032 543 C ATOM 389 OD1 ASP A 50 -11.607 -39.157 -12.723 1.00 56.16 O ANISOU 389 OD1 ASP A 50 9505 6319 5514 -2351 -1062 770 O ATOM 390 OD2 ASP A 50 -10.018 -39.570 -14.181 1.00 55.51 O ANISOU 390 OD2 ASP A 50 9959 5775 5357 -1983 -1142 393 O ATOM 391 N MET A 51 -9.374 -34.502 -14.952 1.00 38.16 N ANISOU 391 N MET A 51 6760 4514 3227 -1160 -472 170 N ATOM 392 CA MET A 51 -9.438 -33.135 -15.464 1.00 36.75 C ANISOU 392 CA MET A 51 6379 4533 3051 -994 -355 127 C ATOM 393 C MET A 51 -8.771 -32.981 -16.800 1.00 35.16 C ANISOU 393 C MET A 51 6340 4217 2803 -845 -366 -16 C ATOM 394 O MET A 51 -9.333 -32.363 -17.692 1.00 34.58 O ANISOU 394 O MET A 51 6185 4263 2693 -842 -385 -22 O ATOM 395 CB MET A 51 -8.837 -32.133 -14.467 1.00 34.55 C ANISOU 395 CB MET A 51 5946 4361 2819 -798 -177 126 C ATOM 396 CG MET A 51 -9.736 -31.869 -13.281 1.00 39.42 C ANISOU 396 CG MET A 51 6353 5190 3435 -877 -126 271 C ATOM 397 SD MET A 51 -8.826 -30.833 -12.099 1.00 44.18 S ANISOU 397 SD MET A 51 6900 5831 4055 -631 32 222 S ATOM 398 CE MET A 51 -8.771 -29.275 -12.954 1.00 42.96 C ANISOU 398 CE MET A 51 6652 5762 3910 -448 106 140 C ATOM 399 N ILE A 52 -7.577 -33.547 -16.939 1.00 34.86 N ANISOU 399 N ILE A 52 6524 3971 2749 -697 -345 -117 N ATOM 400 CA ILE A 52 -6.912 -33.551 -18.244 1.00 35.71 C ANISOU 400 CA ILE A 52 6807 3986 2775 -526 -338 -238 C ATOM 401 C ILE A 52 -7.678 -34.401 -19.283 1.00 38.63 C ANISOU 401 C ILE A 52 7411 4236 3031 -678 -543 -282 C ATOM 402 O ILE A 52 -7.890 -33.956 -20.443 1.00 38.67 O ANISOU 402 O ILE A 52 7441 4301 2949 -620 -562 -334 O ATOM 403 CB ILE A 52 -5.445 -33.949 -18.119 1.00 35.45 C ANISOU 403 CB ILE A 52 6918 3812 2738 -288 -248 -312 C ATOM 404 CG1 ILE A 52 -4.712 -32.867 -17.278 1.00 34.70 C ANISOU 404 CG1 ILE A 52 6561 3869 2754 -169 -79 -265 C ATOM 405 CG2 ILE A 52 -4.832 -34.136 -19.494 1.00 37.15 C ANISOU 405 CG2 ILE A 52 7337 3952 2827 -89 -230 -420 C ATOM 406 CD1 ILE A 52 -3.228 -33.030 -17.247 1.00 34.76 C ANISOU 406 CD1 ILE A 52 6613 3822 2771 66 17 -303 C ATOM 407 N ASN A 53 -8.110 -35.589 -18.852 1.00 40.50 N ANISOU 407 N ASN A 53 7831 4296 3260 -888 -714 -249 N ATOM 408 CA AASN A 53 -8.841 -36.505 -19.735 0.50 43.22 C ANISOU 408 CA AASN A 53 8449 4474 3499 -1089 -968 -288 C ATOM 409 CA BASN A 53 -8.857 -36.529 -19.707 0.50 43.85 C ANISOU 409 CA BASN A 53 8530 4552 3581 -1096 -972 -285 C ATOM 410 C ASN A 53 -10.090 -35.898 -20.367 1.00 44.44 C ANISOU 410 C ASN A 53 8395 4853 3637 -1284 -1070 -218 C ATOM 411 O ASN A 53 -10.364 -36.152 -21.541 1.00 45.65 O ANISOU 411 O ASN A 53 8754 4927 3663 -1310 -1229 -306 O ATOM 412 CB AASN A 53 -9.223 -37.809 -19.023 0.50 45.21 C ANISOU 412 CB AASN A 53 8910 4496 3771 -1357 -1159 -216 C ATOM 413 CB BASN A 53 -9.266 -37.804 -18.925 0.50 46.28 C ANISOU 413 CB BASN A 53 9025 4642 3917 -1373 -1157 -202 C ATOM 414 CG AASN A 53 -9.739 -38.850 -19.986 0.50 48.15 C ANISOU 414 CG AASN A 53 9673 4604 4019 -1551 -1460 -289 C ATOM 415 CG BASN A 53 -8.086 -38.733 -18.640 0.50 48.91 C ANISOU 415 CG BASN A 53 9712 4661 4210 -1165 -1140 -300 C ATOM 416 OD1AASN A 53 -9.029 -39.242 -20.903 0.50 49.45 O ANISOU 416 OD1AASN A 53 10197 4553 4040 -1320 -1496 -469 O ATOM 417 OD1BASN A 53 -7.013 -38.556 -19.207 0.50 51.31 O ANISOU 417 OD1BASN A 53 10139 4914 4442 -818 -1014 -438 O ATOM 418 ND2AASN A 53 -10.987 -39.275 -19.809 0.50 49.60 N ANISOU 418 ND2AASN A 53 9786 4819 4241 -1973 -1685 -141 N ATOM 419 ND2BASN A 53 -8.282 -39.732 -17.764 0.50 51.69 N ANISOU 419 ND2BASN A 53 10220 4820 4601 -1365 -1262 -206 N ATOM 420 N GLU A 54 -10.860 -35.111 -19.607 1.00 43.88 N ANISOU 420 N GLU A 54 7929 5072 3672 -1394 -989 -60 N ATOM 421 CA AGLU A 54 -12.059 -34.433 -20.141 0.50 45.28 C ANISOU 421 CA AGLU A 54 7849 5520 3837 -1528 -1065 32 C ATOM 422 CA BGLU A 54 -12.055 -34.461 -20.163 0.50 45.34 C ANISOU 422 CA BGLU A 54 7867 5520 3842 -1530 -1071 29 C ATOM 423 C GLU A 54 -11.760 -33.614 -21.416 1.00 44.22 C ANISOU 423 C GLU A 54 7760 5436 3604 -1296 -1018 -85 C ATOM 424 O GLU A 54 -12.632 -33.430 -22.287 1.00 45.11 O ANISOU 424 O GLU A 54 7825 5670 3645 -1404 -1170 -59 O ATOM 425 CB AGLU A 54 -12.675 -33.524 -19.061 0.50 44.59 C ANISOU 425 CB AGLU A 54 7336 5752 3853 -1532 -905 202 C ATOM 426 CB BGLU A 54 -12.717 -33.591 -19.100 0.50 44.88 C ANISOU 426 CB BGLU A 54 7383 5782 3886 -1550 -922 203 C ATOM 427 CG AGLU A 54 -14.013 -34.013 -18.479 0.50 49.38 C ANISOU 427 CG AGLU A 54 7718 6544 4499 -1878 -1044 419 C ATOM 428 CG BGLU A 54 -13.315 -34.375 -17.949 0.50 48.57 C ANISOU 428 CG BGLU A 54 7756 6280 4420 -1821 -982 374 C ATOM 429 CD AGLU A 54 -15.207 -33.297 -19.104 0.50 52.99 C ANISOU 429 CD AGLU A 54 7873 7329 4931 -1944 -1115 529 C ATOM 430 CD BGLU A 54 -14.154 -33.495 -17.066 0.50 51.85 C ANISOU 430 CD BGLU A 54 7744 7071 4885 -1809 -836 557 C ATOM 431 OE1AGLU A 54 -15.183 -32.041 -19.199 0.50 52.04 O ANISOU 431 OE1AGLU A 54 7559 7407 4807 -1672 -939 515 O ATOM 432 OE1BGLU A 54 -14.687 -32.480 -17.580 0.50 52.48 O ANISOU 432 OE1BGLU A 54 7605 7392 4942 -1687 -789 576 O ATOM 433 OE2AGLU A 54 -16.164 -33.990 -19.506 0.50 56.08 O ANISOU 433 OE2AGLU A 54 8230 7772 5305 -2273 -1364 639 O ATOM 434 OE2BGLU A 54 -14.282 -33.814 -15.865 0.50 53.73 O ANISOU 434 OE2BGLU A 54 7883 7366 5165 -1891 -766 685 O ATOM 435 N VAL A 55 -10.538 -33.086 -21.520 1.00 41.96 N ANISOU 435 N VAL A 55 7544 5086 3312 -987 -810 -188 N ATOM 436 CA VAL A 55 -10.221 -32.177 -22.642 1.00 40.68 C ANISOU 436 CA VAL A 55 7389 5006 3062 -767 -725 -253 C ATOM 437 C VAL A 55 -9.050 -32.650 -23.519 1.00 42.06 C ANISOU 437 C VAL A 55 7900 4974 3106 -543 -683 -406 C ATOM 438 O VAL A 55 -8.673 -31.957 -24.461 1.00 41.40 O ANISOU 438 O VAL A 55 7836 4962 2930 -349 -589 -442 O ATOM 439 CB VAL A 55 -9.964 -30.697 -22.171 1.00 38.80 C ANISOU 439 CB VAL A 55 6852 4967 2921 -589 -492 -184 C ATOM 440 CG1 VAL A 55 -11.200 -30.076 -21.535 1.00 37.45 C ANISOU 440 CG1 VAL A 55 6368 5040 2822 -715 -515 -42 C ATOM 441 CG2 VAL A 55 -8.731 -30.589 -21.204 1.00 34.20 C ANISOU 441 CG2 VAL A 55 6262 4294 2440 -446 -308 -208 C ATOM 442 N ASP A 56 -8.470 -33.806 -23.206 1.00 42.80 N ANISOU 442 N ASP A 56 8258 4827 3178 -542 -739 -480 N ATOM 443 CA ASP A 56 -7.234 -34.214 -23.836 1.00 43.99 C ANISOU 443 CA ASP A 56 8689 4820 3205 -250 -645 -608 C ATOM 444 C ASP A 56 -7.528 -34.785 -25.240 1.00 46.42 C ANISOU 444 C ASP A 56 9353 5007 3277 -217 -823 -731 C ATOM 445 O ASP A 56 -7.536 -35.988 -25.421 1.00 48.79 O ANISOU 445 O ASP A 56 10026 5042 3471 -261 -1008 -830 O ATOM 446 CB ASP A 56 -6.511 -35.235 -22.949 1.00 44.06 C ANISOU 446 CB ASP A 56 8867 4613 3261 -210 -643 -638 C ATOM 447 CG ASP A 56 -5.116 -35.563 -23.443 1.00 45.59 C ANISOU 447 CG ASP A 56 9275 4706 3340 162 -496 -740 C ATOM 448 OD1 ASP A 56 -4.566 -36.609 -23.017 1.00 45.35 O ANISOU 448 OD1 ASP A 56 9491 4455 3285 247 -540 -793 O ATOM 449 OD2 ASP A 56 -4.562 -34.772 -24.253 1.00 44.07 O ANISOU 449 OD2 ASP A 56 8999 4672 3075 385 -328 -748 O ATOM 450 N ALA A 57 -7.763 -33.911 -26.226 1.00 47.21 N ANISOU 450 N ALA A 57 9374 5283 3282 -131 -781 -724 N ATOM 451 CA ALA A 57 -8.170 -34.347 -27.587 1.00 49.94 C ANISOU 451 CA ALA A 57 10053 5545 3375 -109 -974 -837 C ATOM 452 C ALA A 57 -7.163 -35.252 -28.298 1.00 53.06 C ANISOU 452 C ALA A 57 10906 5711 3542 191 -952 -1006 C ATOM 453 O ALA A 57 -7.554 -36.146 -29.074 1.00 56.00 O ANISOU 453 O ALA A 57 11697 5875 3703 150 -1205 -1141 O ATOM 454 CB ALA A 57 -8.534 -33.124 -28.482 1.00 49.43 C ANISOU 454 CB ALA A 57 9800 5740 3241 -31 -903 -775 C ATOM 455 N ASP A 58 -5.869 -35.033 -28.088 1.00 52.25 N ANISOU 455 N ASP A 58 10744 5650 3459 509 -663 -1000 N ATOM 456 CA ASP A 58 -4.873 -35.879 -28.804 1.00 55.88 C ANISOU 456 CA ASP A 58 11622 5939 3670 875 -605 -1148 C ATOM 457 C ASP A 58 -4.390 -37.074 -27.966 1.00 57.33 C ANISOU 457 C ASP A 58 12040 5844 3898 912 -669 -1215 C ATOM 458 O ASP A 58 -3.505 -37.814 -28.374 1.00 59.57 O ANISOU 458 O ASP A 58 12662 5980 3991 1261 -605 -1329 O ATOM 459 CB ASP A 58 -3.688 -35.040 -29.317 1.00 55.37 C ANISOU 459 CB ASP A 58 11381 6117 3539 1253 -253 -1084 C ATOM 460 CG ASP A 58 -3.024 -34.204 -28.212 1.00 51.60 C ANISOU 460 CG ASP A 58 10427 5826 3351 1232 -15 -917 C ATOM 461 OD1 ASP A 58 -2.097 -33.439 -28.530 1.00 49.46 O ANISOU 461 OD1 ASP A 58 9954 5768 3071 1460 250 -821 O ATOM 462 OD2 ASP A 58 -3.424 -34.307 -27.021 1.00 46.61 O ANISOU 462 OD2 ASP A 58 9629 5132 2947 977 -103 -870 O ATOM 463 N GLY A 59 -4.983 -37.245 -26.788 1.00 56.22 N ANISOU 463 N GLY A 59 11721 5646 3995 578 -784 -1130 N ATOM 464 CA GLY A 59 -4.659 -38.367 -25.918 1.00 57.71 C ANISOU 464 CA GLY A 59 12133 5559 4236 564 -872 -1163 C ATOM 465 C GLY A 59 -3.243 -38.390 -25.352 1.00 56.90 C ANISOU 465 C GLY A 59 11934 5502 4183 923 -601 -1139 C ATOM 466 O GLY A 59 -2.795 -39.438 -24.890 1.00 58.95 O ANISOU 466 O GLY A 59 12481 5507 4412 1033 -667 -1195 O ATOM 467 N ASN A 60 -2.542 -37.252 -25.364 1.00 53.68 N ANISOU 467 N ASN A 60 11127 5413 3856 1093 -317 -1040 N ATOM 468 CA ASN A 60 -1.129 -37.240 -24.970 1.00 52.47 C ANISOU 468 CA ASN A 60 10848 5354 3735 1439 -71 -996 C ATOM 469 C ASN A 60 -0.868 -37.014 -23.457 1.00 49.95 C ANISOU 469 C ASN A 60 10198 5093 3687 1291 -22 -870 C ATOM 470 O ASN A 60 0.280 -36.969 -23.023 1.00 50.08 O ANISOU 470 O ASN A 60 10064 5211 3754 1539 151 -813 O ATOM 471 CB ASN A 60 -0.311 -36.277 -25.852 1.00 52.72 C ANISOU 471 CB ASN A 60 10663 5688 3682 1722 202 -935 C ATOM 472 CG ASN A 60 -0.480 -34.794 -25.449 1.00 48.76 C ANISOU 472 CG ASN A 60 9656 5467 3404 1502 323 -769 C ATOM 473 OD1 ASN A 60 -1.447 -34.416 -24.783 1.00 46.33 O ANISOU 473 OD1 ASN A 60 9201 5143 3259 1160 192 -730 O ATOM 474 ND2 ASN A 60 0.447 -33.953 -25.899 1.00 47.37 N ANISOU 474 ND2 ASN A 60 9234 5547 3217 1709 571 -661 N ATOM 475 N GLY A 61 -1.930 -36.872 -22.672 1.00 46.36 N ANISOU 475 N GLY A 61 9626 4601 3388 903 -176 -816 N ATOM 476 CA GLY A 61 -1.798 -36.814 -21.236 1.00 44.77 C ANISOU 476 CA GLY A 61 9199 4422 3391 770 -160 -715 C ATOM 477 C GLY A 61 -1.519 -35.437 -20.660 1.00 40.31 C ANISOU 477 C GLY A 61 8167 4148 3002 721 11 -593 C ATOM 478 O GLY A 61 -1.482 -35.288 -19.456 1.00 39.80 O ANISOU 478 O GLY A 61 7924 4113 3086 606 11 -517 O ATOM 479 N THR A 62 -1.338 -34.425 -21.508 1.00 39.46 N ANISOU 479 N THR A 62 7893 4235 2865 804 143 -570 N ATOM 480 CA THR A 62 -1.142 -33.042 -21.044 1.00 35.74 C ANISOU 480 CA THR A 62 7034 3991 2554 729 271 -455 C ATOM 481 C THR A 62 -2.113 -32.112 -21.805 1.00 35.56 C ANISOU 481 C THR A 62 6935 4072 2504 590 252 -438 C ATOM 482 O THR A 62 -2.694 -32.479 -22.853 1.00 33.90 O ANISOU 482 O THR A 62 6940 3806 2135 600 170 -510 O ATOM 483 CB THR A 62 0.306 -32.545 -21.299 1.00 37.14 C ANISOU 483 CB THR A 62 7035 4332 2744 986 476 -385 C ATOM 484 OG1 THR A 62 0.532 -32.531 -22.717 1.00 36.00 O ANISOU 484 OG1 THR A 62 7018 4245 2417 1183 565 -415 O ATOM 485 CG2 THR A 62 1.386 -33.461 -20.631 1.00 38.57 C ANISOU 485 CG2 THR A 62 7262 4457 2938 1189 504 -385 C ATOM 486 N ILE A 63 -2.254 -30.890 -21.315 1.00 33.33 N ANISOU 486 N ILE A 63 6373 3932 2357 485 315 -346 N ATOM 487 CA ILE A 63 -3.179 -29.945 -21.916 1.00 32.95 C ANISOU 487 CA ILE A 63 6246 3981 2291 383 297 -315 C ATOM 488 C ILE A 63 -2.366 -28.916 -22.713 1.00 33.82 C ANISOU 488 C ILE A 63 6244 4222 2386 527 464 -241 C ATOM 489 O ILE A 63 -1.500 -28.217 -22.141 1.00 33.61 O ANISOU 489 O ILE A 63 6026 4260 2484 546 567 -157 O ATOM 490 CB ILE A 63 -3.996 -29.237 -20.795 1.00 32.86 C ANISOU 490 CB ILE A 63 6041 4024 2420 196 250 -257 C ATOM 491 CG1 ILE A 63 -4.997 -30.206 -20.148 1.00 31.50 C ANISOU 491 CG1 ILE A 63 5949 3775 2244 21 93 -281 C ATOM 492 CG2 ILE A 63 -4.794 -28.057 -21.348 1.00 31.99 C ANISOU 492 CG2 ILE A 63 5824 4032 2300 159 259 -204 C ATOM 493 CD1 ILE A 63 -5.777 -29.521 -18.959 1.00 30.72 C ANISOU 493 CD1 ILE A 63 5641 3780 2253 -109 86 -205 C ATOM 494 N ASP A 64 -2.634 -28.810 -24.016 1.00 33.38 N ANISOU 494 N ASP A 64 6307 4206 2170 608 477 -256 N ATOM 495 CA ASP A 64 -2.054 -27.718 -24.829 1.00 34.42 C ANISOU 495 CA ASP A 64 6329 4476 2275 709 634 -147 C ATOM 496 C ASP A 64 -2.970 -26.477 -24.875 1.00 32.71 C ANISOU 496 C ASP A 64 5998 4314 2118 576 594 -76 C ATOM 497 O ASP A 64 -4.020 -26.444 -24.217 1.00 30.33 O ANISOU 497 O ASP A 64 5664 3980 1879 431 465 -108 O ATOM 498 CB ASP A 64 -1.674 -28.221 -26.240 1.00 35.94 C ANISOU 498 CB ASP A 64 6724 4705 2227 929 705 -182 C ATOM 499 CG ASP A 64 -2.875 -28.640 -27.062 1.00 39.67 C ANISOU 499 CG ASP A 64 7432 5118 2524 883 534 -284 C ATOM 500 OD1 ASP A 64 -4.015 -28.285 -26.724 1.00 38.25 O ANISOU 500 OD1 ASP A 64 7187 4930 2418 683 391 -282 O ATOM 501 OD2 ASP A 64 -2.690 -29.299 -28.098 1.00 44.66 O ANISOU 501 OD2 ASP A 64 8315 5729 2925 1061 536 -361 O ATOM 502 N PHE A 65 -2.632 -25.484 -25.692 1.00 32.47 N ANISOU 502 N PHE A 65 5913 4374 2048 641 707 34 N ATOM 503 CA PHE A 65 -3.407 -24.247 -25.645 1.00 31.83 C ANISOU 503 CA PHE A 65 5750 4315 2031 548 669 111 C ATOM 504 C PHE A 65 -4.891 -24.427 -26.011 1.00 31.78 C ANISOU 504 C PHE A 65 5829 4320 1926 501 509 46 C ATOM 505 O PHE A 65 -5.766 -23.991 -25.261 1.00 31.05 O ANISOU 505 O PHE A 65 5642 4229 1926 408 425 52 O ATOM 506 CB PHE A 65 -2.752 -23.121 -26.461 1.00 32.72 C ANISOU 506 CB PHE A 65 5815 4497 2121 608 809 271 C ATOM 507 CG PHE A 65 -3.170 -21.764 -26.023 1.00 33.53 C ANISOU 507 CG PHE A 65 5839 4553 2346 514 778 362 C ATOM 508 CD1 PHE A 65 -2.503 -21.120 -24.974 1.00 36.31 C ANISOU 508 CD1 PHE A 65 6075 4833 2888 413 794 418 C ATOM 509 CD2 PHE A 65 -4.270 -21.140 -26.612 1.00 34.49 C ANISOU 509 CD2 PHE A 65 6028 4692 2382 540 707 383 C ATOM 510 CE1 PHE A 65 -2.915 -19.847 -24.551 1.00 37.92 C ANISOU 510 CE1 PHE A 65 6282 4945 3181 350 742 481 C ATOM 511 CE2 PHE A 65 -4.696 -19.867 -26.208 1.00 35.79 C ANISOU 511 CE2 PHE A 65 6168 4792 2641 507 675 461 C ATOM 512 CZ PHE A 65 -4.017 -19.218 -25.162 1.00 37.04 C ANISOU 512 CZ PHE A 65 6259 4838 2976 416 692 501 C ATOM 513 N PRO A 66 -5.191 -25.050 -27.164 1.00 34.26 N ANISOU 513 N PRO A 66 6317 4662 2037 576 459 -8 N ATOM 514 CA PRO A 66 -6.617 -25.124 -27.483 1.00 34.48 C ANISOU 514 CA PRO A 66 6382 4731 1988 494 274 -41 C ATOM 515 C PRO A 66 -7.379 -26.042 -26.539 1.00 33.92 C ANISOU 515 C PRO A 66 6283 4612 1994 327 115 -120 C ATOM 516 O PRO A 66 -8.554 -25.797 -26.332 1.00 33.85 O ANISOU 516 O PRO A 66 6169 4686 2007 226 -8 -87 O ATOM 517 CB PRO A 66 -6.651 -25.682 -28.923 1.00 36.58 C ANISOU 517 CB PRO A 66 6884 5017 1997 603 227 -95 C ATOM 518 CG PRO A 66 -5.346 -26.213 -29.172 1.00 38.36 C ANISOU 518 CG PRO A 66 7217 5200 2159 754 382 -125 C ATOM 519 CD PRO A 66 -4.353 -25.504 -28.286 1.00 34.97 C ANISOU 519 CD PRO A 66 6567 4780 1938 752 563 -18 C ATOM 520 N GLU A 67 -6.736 -27.082 -25.992 1.00 32.54 N ANISOU 520 N GLU A 67 6191 4321 1850 308 120 -200 N ATOM 521 CA GLU A 67 -7.391 -27.920 -25.000 1.00 32.78 C ANISOU 521 CA GLU A 67 6197 4295 1964 130 -18 -239 C ATOM 522 C GLU A 67 -7.654 -27.130 -23.718 1.00 30.28 C ANISOU 522 C GLU A 67 5631 4044 1829 64 39 -159 C ATOM 523 O GLU A 67 -8.710 -27.301 -23.098 1.00 30.30 O ANISOU 523 O GLU A 67 5527 4112 1873 -77 -68 -127 O ATOM 524 CB GLU A 67 -6.583 -29.177 -24.670 1.00 33.13 C ANISOU 524 CB GLU A 67 6420 4173 1993 152 -24 -331 C ATOM 525 CG GLU A 67 -6.459 -30.098 -25.892 1.00 34.23 C ANISOU 525 CG GLU A 67 6880 4213 1911 243 -113 -440 C ATOM 526 CD GLU A 67 -5.426 -31.166 -25.681 1.00 38.26 C ANISOU 526 CD GLU A 67 7596 4558 2383 375 -71 -527 C ATOM 527 OE1 GLU A 67 -4.588 -31.028 -24.749 1.00 37.59 O ANISOU 527 OE1 GLU A 67 7363 4476 2442 429 66 -483 O ATOM 528 OE2 GLU A 67 -5.453 -32.172 -26.421 1.00 39.50 O ANISOU 528 OE2 GLU A 67 8085 4570 2354 436 -191 -644 O ATOM 529 N PHE A 68 -6.725 -26.251 -23.331 1.00 28.55 N ANISOU 529 N PHE A 68 5324 3819 1704 164 198 -115 N ATOM 530 CA PHE A 68 -6.986 -25.346 -22.180 1.00 28.39 C ANISOU 530 CA PHE A 68 5131 3836 1819 134 234 -57 C ATOM 531 C PHE A 68 -8.173 -24.402 -22.456 1.00 29.00 C ANISOU 531 C PHE A 68 5116 4037 1864 153 191 9 C ATOM 532 O PHE A 68 -9.009 -24.128 -21.579 1.00 27.39 O ANISOU 532 O PHE A 68 4788 3912 1706 125 161 41 O ATOM 533 CB PHE A 68 -5.743 -24.536 -21.867 1.00 28.36 C ANISOU 533 CB PHE A 68 5090 3775 1908 208 365 -20 C ATOM 534 CG PHE A 68 -5.945 -23.507 -20.795 1.00 29.19 C ANISOU 534 CG PHE A 68 5098 3874 2119 198 377 17 C ATOM 535 CD1 PHE A 68 -5.975 -23.890 -19.455 1.00 28.24 C ANISOU 535 CD1 PHE A 68 4933 3730 2068 143 349 -17 C ATOM 536 CD2 PHE A 68 -6.094 -22.150 -21.120 1.00 32.31 C ANISOU 536 CD2 PHE A 68 5488 4266 2521 262 408 85 C ATOM 537 CE1 PHE A 68 -6.190 -22.940 -18.442 1.00 32.07 C ANISOU 537 CE1 PHE A 68 5375 4201 2607 171 353 -3 C ATOM 538 CE2 PHE A 68 -6.276 -21.178 -20.106 1.00 32.80 C ANISOU 538 CE2 PHE A 68 5530 4278 2652 286 400 96 C ATOM 539 CZ PHE A 68 -6.325 -21.571 -18.785 1.00 34.17 C ANISOU 539 CZ PHE A 68 5669 4441 2874 251 373 43 C ATOM 540 N LEU A 69 -8.228 -23.847 -23.660 1.00 29.23 N ANISOU 540 N LEU A 69 5204 4102 1800 236 202 43 N ATOM 541 CA LEU A 69 -9.360 -22.995 -24.033 1.00 30.31 C ANISOU 541 CA LEU A 69 5265 4364 1888 288 148 114 C ATOM 542 C LEU A 69 -10.662 -23.750 -23.909 1.00 31.73 C ANISOU 542 C LEU A 69 5351 4682 2024 176 -7 115 C ATOM 543 O LEU A 69 -11.677 -23.174 -23.457 1.00 33.59 O ANISOU 543 O LEU A 69 5421 5064 2276 211 -35 189 O ATOM 544 CB LEU A 69 -9.247 -22.513 -25.509 1.00 31.02 C ANISOU 544 CB LEU A 69 5465 4477 1845 387 158 156 C ATOM 545 CG LEU A 69 -8.166 -21.466 -25.761 1.00 31.76 C ANISOU 545 CG LEU A 69 5611 4477 1978 482 309 226 C ATOM 546 CD1 LEU A 69 -8.204 -21.024 -27.229 1.00 34.12 C ANISOU 546 CD1 LEU A 69 6018 4829 2119 581 322 296 C ATOM 547 CD2 LEU A 69 -8.310 -20.295 -24.813 1.00 33.11 C ANISOU 547 CD2 LEU A 69 5712 4597 2273 520 343 281 C ATOM 548 N THR A 70 -10.660 -25.005 -24.361 1.00 32.54 N ANISOU 548 N THR A 70 5563 4744 2057 50 -117 48 N ATOM 549 CA THR A 70 -11.847 -25.893 -24.236 1.00 34.40 C ANISOU 549 CA THR A 70 5720 5088 2264 -139 -307 68 C ATOM 550 C THR A 70 -12.285 -26.117 -22.777 1.00 34.32 C ANISOU 550 C THR A 70 5522 5141 2375 -240 -288 122 C ATOM 551 O THR A 70 -13.495 -26.085 -22.447 1.00 34.69 O ANISOU 551 O THR A 70 5356 5400 2426 -321 -369 227 O ATOM 552 CB THR A 70 -11.607 -27.251 -24.973 1.00 36.14 C ANISOU 552 CB THR A 70 6186 5169 2378 -266 -456 -35 C ATOM 553 OG1 THR A 70 -11.428 -26.970 -26.378 1.00 37.86 O ANISOU 553 OG1 THR A 70 6567 5383 2434 -146 -481 -70 O ATOM 554 CG2 THR A 70 -12.795 -28.171 -24.842 1.00 37.41 C ANISOU 554 CG2 THR A 70 6283 5408 2524 -528 -691 6 C ATOM 555 N MET A 71 -11.300 -26.383 -21.934 1.00 32.28 N ANISOU 555 N MET A 71 5334 4731 2200 -227 -181 66 N ATOM 556 CA MET A 71 -11.511 -26.523 -20.503 1.00 33.22 C ANISOU 556 CA MET A 71 5317 4894 2411 -283 -135 112 C ATOM 557 C MET A 71 -12.204 -25.290 -19.916 1.00 33.88 C ANISOU 557 C MET A 71 5201 5160 2513 -138 -49 198 C ATOM 558 O MET A 71 -13.172 -25.428 -19.127 1.00 34.70 O ANISOU 558 O MET A 71 5111 5452 2621 -190 -63 295 O ATOM 559 CB MET A 71 -10.215 -26.813 -19.777 1.00 30.95 C ANISOU 559 CB MET A 71 5149 4415 2195 -248 -37 37 C ATOM 560 CG MET A 71 -10.415 -26.914 -18.198 1.00 31.12 C ANISOU 560 CG MET A 71 5051 4486 2285 -287 11 86 C ATOM 561 SD MET A 71 -8.890 -27.388 -17.395 1.00 37.83 S ANISOU 561 SD MET A 71 6044 5123 3206 -257 79 4 S ATOM 562 CE MET A 71 -7.912 -25.927 -17.546 1.00 34.85 C ANISOU 562 CE MET A 71 5672 4696 2873 -67 197 -29 C ATOM 563 N MET A 72 -11.723 -24.108 -20.293 1.00 33.54 N ANISOU 563 N MET A 72 5212 5063 2468 54 42 178 N ATOM 564 CA MET A 72 -12.269 -22.837 -19.773 1.00 35.84 C ANISOU 564 CA MET A 72 5400 5461 2757 248 117 238 C ATOM 565 C MET A 72 -13.664 -22.563 -20.295 1.00 38.38 C ANISOU 565 C MET A 72 5543 6041 3000 299 45 345 C ATOM 566 O MET A 72 -14.546 -22.145 -19.518 1.00 38.95 O ANISOU 566 O MET A 72 5437 6309 3053 411 86 428 O ATOM 567 CB MET A 72 -11.340 -21.658 -20.073 1.00 36.87 C ANISOU 567 CB MET A 72 5685 5413 2911 403 201 202 C ATOM 568 CG MET A 72 -9.991 -21.789 -19.365 1.00 38.34 C ANISOU 568 CG MET A 72 5984 5395 3187 353 263 127 C ATOM 569 SD MET A 72 -9.993 -21.962 -17.557 1.00 43.43 S ANISOU 569 SD MET A 72 6581 6044 3875 355 297 100 S ATOM 570 CE MET A 72 -10.227 -20.236 -17.143 1.00 49.18 C ANISOU 570 CE MET A 72 7383 6726 4576 598 343 109 C ATOM 571 N ALA A 73 -13.877 -22.822 -21.591 1.00 38.22 N ANISOU 571 N ALA A 73 5563 6045 2915 235 -64 352 N ATOM 572 CA ALA A 73 -15.172 -22.596 -22.206 1.00 42.48 C ANISOU 572 CA ALA A 73 5920 6845 3374 270 -169 464 C ATOM 573 C ALA A 73 -16.240 -23.507 -21.613 1.00 44.75 C ANISOU 573 C ALA A 73 5955 7376 3671 78 -266 566 C ATOM 574 O ALA A 73 -17.366 -23.053 -21.347 1.00 46.70 O ANISOU 574 O ALA A 73 5937 7921 3887 180 -268 705 O ATOM 575 CB ALA A 73 -15.102 -22.740 -23.761 1.00 41.56 C ANISOU 575 CB ALA A 73 5940 6690 3159 230 -293 439 C ATOM 576 N ARG A 74 -15.891 -24.776 -21.392 1.00 45.63 N ANISOU 576 N ARG A 74 6144 7371 3821 -189 -342 519 N ATOM 577 CA ARG A 74 -16.808 -25.688 -20.695 1.00 49.03 C ANISOU 577 CA ARG A 74 6351 8001 4279 -423 -430 645 C ATOM 578 C ARG A 74 -17.201 -25.137 -19.323 1.00 50.40 C ANISOU 578 C ARG A 74 6307 8362 4481 -267 -255 743 C ATOM 579 O ARG A 74 -18.385 -25.110 -18.979 1.00 52.25 O ANISOU 579 O ARG A 74 6223 8939 4689 -283 -271 923 O ATOM 580 CB ARG A 74 -16.195 -27.086 -20.546 1.00 48.66 C ANISOU 580 CB ARG A 74 6501 7716 4270 -707 -527 569 C ATOM 581 CG ARG A 74 -16.369 -27.915 -21.816 1.00 51.21 C ANISOU 581 CG ARG A 74 6984 7950 4522 -918 -771 523 C ATOM 582 CD ARG A 74 -15.862 -29.331 -21.657 1.00 53.46 C ANISOU 582 CD ARG A 74 7512 7975 4827 -1175 -890 449 C ATOM 583 NE ARG A 74 -15.721 -29.952 -22.976 1.00 55.94 N ANISOU 583 NE ARG A 74 8105 8118 5031 -1273 -1099 338 N ATOM 584 CZ ARG A 74 -15.152 -31.132 -23.181 1.00 56.20 C ANISOU 584 CZ ARG A 74 8466 7856 5030 -1422 -1225 225 C ATOM 585 NH1 ARG A 74 -14.687 -31.838 -22.155 1.00 55.13 N ANISOU 585 NH1 ARG A 74 8399 7568 4979 -1509 -1169 226 N ATOM 586 NH2 ARG A 74 -15.057 -31.606 -24.414 1.00 56.78 N ANISOU 586 NH2 ARG A 74 8829 7782 4964 -1458 -1414 108 N ATOM 587 N LYS A 75 -16.199 -24.691 -18.563 1.00 49.77 N ANISOU 587 N LYS A 75 6397 8075 4438 -108 -93 633 N ATOM 588 CA LYS A 75 -16.400 -24.200 -17.207 1.00 52.43 C ANISOU 588 CA LYS A 75 6619 8534 4768 63 68 686 C ATOM 589 C LYS A 75 -17.241 -22.925 -17.141 1.00 55.69 C ANISOU 589 C LYS A 75 6870 9188 5101 394 158 768 C ATOM 590 O LYS A 75 -18.052 -22.771 -16.227 1.00 57.65 O ANISOU 590 O LYS A 75 6895 9715 5296 514 252 895 O ATOM 591 CB LYS A 75 -15.053 -23.997 -16.513 1.00 49.80 C ANISOU 591 CB LYS A 75 6546 7894 4482 141 170 532 C ATOM 592 CG LYS A 75 -15.118 -23.799 -15.002 1.00 52.34 C ANISOU 592 CG LYS A 75 6816 8295 4776 264 302 562 C ATOM 593 CD LYS A 75 -15.609 -25.063 -14.255 1.00 55.11 C ANISOU 593 CD LYS A 75 7012 8795 5132 16 278 688 C ATOM 594 CE LYS A 75 -17.061 -24.898 -13.773 1.00 58.72 C ANISOU 594 CE LYS A 75 7123 9683 5505 91 340 902 C ATOM 595 NZ LYS A 75 -17.525 -26.141 -13.092 1.00 63.11 N ANISOU 595 NZ LYS A 75 7520 10385 6073 -201 310 1066 N ATOM 596 N MET A 76 -17.027 -22.004 -18.073 1.00 57.57 N ANISOU 596 N MET A 76 7236 9321 5316 571 142 707 N ATOM 597 CA MET A 76 -17.850 -20.783 -18.164 1.00 62.60 C ANISOU 597 CA MET A 76 7760 10158 5866 916 203 788 C ATOM 598 C MET A 76 -19.328 -21.103 -18.347 1.00 66.77 C ANISOU 598 C MET A 76 7896 11135 6338 891 137 997 C ATOM 599 O MET A 76 -20.183 -20.538 -17.653 1.00 69.41 O ANISOU 599 O MET A 76 8014 11764 6595 1159 249 1118 O ATOM 600 CB MET A 76 -17.419 -19.895 -19.326 1.00 62.26 C ANISOU 600 CB MET A 76 7928 9921 5807 1053 161 720 C ATOM 601 CG MET A 76 -16.221 -19.018 -19.052 1.00 63.52 C ANISOU 601 CG MET A 76 8418 9716 6000 1193 250 580 C ATOM 602 SD MET A 76 -15.775 -18.100 -20.554 1.00 70.57 S ANISOU 602 SD MET A 76 9530 10412 6870 1288 194 563 S ATOM 603 CE MET A 76 -14.008 -17.833 -20.259 1.00 67.19 C ANISOU 603 CE MET A 76 9430 9553 6546 1190 257 421 C ATOM 604 N LYS A 77 -19.599 -21.998 -19.296 1.00 68.34 N ANISOU 604 N LYS A 77 8013 11388 6564 578 -52 1041 N ATOM 605 CA LYS A 77 -20.928 -22.537 -19.581 1.00 72.87 C ANISOU 605 CA LYS A 77 8201 12375 7110 423 -186 1254 C ATOM 606 C LYS A 77 -21.535 -23.266 -18.370 1.00 74.75 C ANISOU 606 C LYS A 77 8150 12883 7369 276 -119 1417 C ATOM 607 O LYS A 77 -22.746 -23.226 -18.162 1.00 78.56 O ANISOU 607 O LYS A 77 8226 13816 7806 317 -119 1649 O ATOM 608 CB LYS A 77 -20.817 -23.476 -20.798 1.00 72.79 C ANISOU 608 CB LYS A 77 8291 12245 7120 60 -443 1213 C ATOM 609 CG LYS A 77 -22.111 -24.012 -21.409 1.00 77.21 C ANISOU 609 CG LYS A 77 8505 13182 7651 -163 -670 1418 C ATOM 610 CD LYS A 77 -21.787 -24.787 -22.699 1.00 77.63 C ANISOU 610 CD LYS A 77 8802 13010 7683 -462 -938 1308 C ATOM 611 CE LYS A 77 -22.954 -25.638 -23.198 1.00 81.87 C ANISOU 611 CE LYS A 77 9051 13848 8207 -823 -1237 1495 C ATOM 612 NZ LYS A 77 -24.086 -24.812 -23.692 1.00 83.99 N ANISOU 612 NZ LYS A 77 8963 14547 8403 -619 -1298 1681 N ATOM 613 N ASP A 78 -20.679 -23.894 -17.566 1.00 73.57 N ANISOU 613 N ASP A 78 8197 12478 7278 125 -51 1316 N ATOM 614 CA AASP A 78 -21.142 -24.699 -16.438 0.50 75.17 C ANISOU 614 CA AASP A 78 8174 12894 7494 -55 7 1479 C ATOM 615 CA BASP A 78 -21.067 -24.719 -16.416 0.50 75.13 C ANISOU 615 CA BASP A 78 8191 12864 7493 -59 10 1467 C ATOM 616 C ASP A 78 -21.335 -23.913 -15.131 1.00 76.21 C ANISOU 616 C ASP A 78 8207 13212 7538 320 271 1531 C ATOM 617 O ASP A 78 -21.815 -24.470 -14.136 1.00 77.98 O ANISOU 617 O ASP A 78 8211 13680 7738 227 358 1700 O ATOM 618 CB AASP A 78 -20.222 -25.910 -16.226 0.50 73.32 C ANISOU 618 CB AASP A 78 8201 12310 7348 -415 -78 1373 C ATOM 619 CB BASP A 78 -19.962 -25.754 -16.152 0.50 72.90 C ANISOU 619 CB BASP A 78 8221 12185 7295 -354 -44 1323 C ATOM 620 CG AASP A 78 -20.588 -27.085 -17.122 0.50 74.26 C ANISOU 620 CG AASP A 78 8291 12406 7517 -862 -355 1439 C ATOM 621 CG BASP A 78 -20.412 -26.890 -15.249 0.50 74.74 C ANISOU 621 CG BASP A 78 8271 12571 7554 -665 -59 1508 C ATOM 622 OD1AASP A 78 -21.795 -27.295 -17.357 0.50 77.25 O ANISOU 622 OD1AASP A 78 8310 13159 7881 -1014 -468 1667 O ATOM 623 OD1BASP A 78 -21.426 -27.545 -15.572 0.50 77.70 O ANISOU 623 OD1BASP A 78 8358 13221 7945 -954 -212 1722 O ATOM 624 OD2AASP A 78 -19.675 -27.806 -17.582 0.50 71.64 O ANISOU 624 OD2AASP A 78 8302 11689 7230 -1054 -472 1269 O ATOM 625 OD2BASP A 78 -19.737 -27.137 -14.226 0.50 73.19 O ANISOU 625 OD2BASP A 78 8227 12219 7365 -641 64 1453 O ATOM 626 N THR A 79 -21.008 -22.611 -15.142 1.00 75.68 N ANISOU 626 N THR A 79 8318 13033 7402 750 391 1398 N ATOM 627 CA THR A 79 -21.088 -21.753 -13.924 1.00 76.48 C ANISOU 627 CA THR A 79 8441 13236 7384 1165 624 1393 C ATOM 628 C THR A 79 -22.281 -20.772 -13.889 1.00 80.12 C ANISOU 628 C THR A 79 8619 14119 7703 1597 733 1554 C ATOM 629 O THR A 79 -22.182 -19.628 -14.356 1.00 80.36 O ANISOU 629 O THR A 79 8831 14024 7678 1946 750 1452 O ATOM 630 CB THR A 79 -19.745 -20.970 -13.661 1.00 73.58 C ANISOU 630 CB THR A 79 8556 12380 7022 1358 677 1115 C ATOM 631 OG1 THR A 79 -18.646 -21.884 -13.573 1.00 70.32 O ANISOU 631 OG1 THR A 79 8357 11636 6726 1011 600 992 O ATOM 632 CG2 THR A 79 -19.812 -20.184 -12.369 1.00 73.98 C ANISOU 632 CG2 THR A 79 8691 12494 6924 1757 872 1088 C ATOM 633 N ASP A 80 -23.402 -21.227 -13.333 1.00 83.36 N ANISOU 633 N ASP A 80 8584 15039 8051 1579 810 1825 N ATOM 634 CA ASP A 80 -24.565 -20.355 -13.086 1.00 87.16 C ANISOU 634 CA ASP A 80 8746 16002 8370 2051 961 2012 C ATOM 635 C ASP A 80 -24.962 -20.406 -11.612 1.00 88.80 C ANISOU 635 C ASP A 80 8794 16519 8426 2277 1213 2143 C ATOM 636 O ASP A 80 -25.650 -19.500 -11.120 1.00 92.12 O ANISOU 636 O ASP A 80 9093 17252 8658 2814 1405 2225 O ATOM 637 CB ASP A 80 -25.797 -20.734 -13.938 1.00 90.62 C ANISOU 637 CB ASP A 80 8665 16928 8840 1882 826 2297 C ATOM 638 CG ASP A 80 -25.492 -21.754 -15.031 1.00 89.60 C ANISOU 638 CG ASP A 80 8570 16584 8888 1291 527 2267 C ATOM 639 OD1 ASP A 80 -25.737 -21.443 -16.221 1.00 91.28 O ANISOU 639 OD1 ASP A 80 8762 16797 9122 1290 355 2257 O ATOM 640 OD2 ASP A 80 -25.033 -22.872 -14.700 1.00 88.84 O ANISOU 640 OD2 ASP A 80 8544 16322 8890 848 459 2257 O ATOM 641 N SER A 81 -24.528 -21.469 -10.924 1.00 75.24 N ANISOU 641 N SER A 81 10733 8175 9680 -1256 -868 -1379 N ATOM 642 CA SER A 81 -24.946 -21.763 -9.547 1.00 73.96 C ANISOU 642 CA SER A 81 10433 7880 9789 -1379 -646 -1154 C ATOM 643 C SER A 81 -24.402 -20.748 -8.563 1.00 70.14 C ANISOU 643 C SER A 81 9982 7560 9109 -1250 -457 -877 C ATOM 644 O SER A 81 -23.207 -20.446 -8.584 1.00 68.08 O ANISOU 644 O SER A 81 9909 7362 8597 -1098 -398 -816 O ATOM 645 CB SER A 81 -24.542 -23.188 -9.115 1.00 75.56 C ANISOU 645 CB SER A 81 10730 7755 10223 -1465 -506 -1145 C ATOM 646 OG SER A 81 -23.255 -23.572 -9.584 1.00 74.53 O ANISOU 646 OG SER A 81 10860 7577 9882 -1319 -496 -1206 O ATOM 647 N GLU A 82 -25.282 -20.215 -7.717 1.00 68.53 N ANISOU 647 N GLU A 82 9585 7425 9029 -1308 -368 -724 N ATOM 648 CA GLU A 82 -24.859 -19.326 -6.646 1.00 65.36 C ANISOU 648 CA GLU A 82 9217 7151 8466 -1190 -188 -479 C ATOM 649 C GLU A 82 -23.828 -20.022 -5.755 1.00 62.91 C ANISOU 649 C GLU A 82 9073 6693 8137 -1135 15 -324 C ATOM 650 O GLU A 82 -22.911 -19.384 -5.256 1.00 60.02 O ANISOU 650 O GLU A 82 8826 6438 7543 -989 89 -204 O ATOM 651 CB GLU A 82 -26.049 -18.829 -5.810 1.00 66.68 C ANISOU 651 CB GLU A 82 9154 7386 8795 -1253 -94 -343 C ATOM 652 CG GLU A 82 -25.614 -18.100 -4.520 1.00 67.56 C ANISOU 652 CG GLU A 82 9329 7591 8751 -1123 115 -97 C ATOM 653 CD GLU A 82 -26.698 -17.245 -3.873 1.00 71.83 C ANISOU 653 CD GLU A 82 9675 8268 9351 -1117 186 13 C ATOM 654 OE1 GLU A 82 -27.894 -17.586 -4.032 1.00 74.87 O ANISOU 654 OE1 GLU A 82 9829 8611 10007 -1255 163 -30 O ATOM 655 OE2 GLU A 82 -26.337 -16.239 -3.192 1.00 71.37 O ANISOU 655 OE2 GLU A 82 9688 8352 9080 -971 264 134 O ATOM 656 N GLU A 83 -23.983 -21.332 -5.569 1.00 63.29 N ANISOU 656 N GLU A 83 9125 6483 8439 -1249 93 -333 N ATOM 657 CA GLU A 83 -23.048 -22.087 -4.747 1.00 61.04 C ANISOU 657 CA GLU A 83 9005 6043 8145 -1176 283 -177 C ATOM 658 C GLU A 83 -21.628 -22.075 -5.334 1.00 57.54 C ANISOU 658 C GLU A 83 8774 5641 7448 -1020 215 -256 C ATOM 659 O GLU A 83 -20.662 -21.894 -4.602 1.00 55.42 O ANISOU 659 O GLU A 83 8618 5421 7019 -877 327 -102 O ATOM 660 CB GLU A 83 -23.540 -23.522 -4.530 1.00 64.93 C ANISOU 660 CB GLU A 83 9467 6212 8993 -1331 386 -170 C ATOM 661 CG GLU A 83 -24.788 -23.635 -3.631 1.00 68.88 C ANISOU 661 CG GLU A 83 9753 6645 9773 -1469 552 -4 C ATOM 662 CD GLU A 83 -26.087 -23.849 -4.424 1.00 74.20 C ANISOU 662 CD GLU A 83 10182 7256 10754 -1691 396 -205 C ATOM 663 OE1 GLU A 83 -26.458 -22.952 -5.235 1.00 73.27 O ANISOU 663 OE1 GLU A 83 9970 7362 10507 -1679 175 -371 O ATOM 664 OE2 GLU A 83 -26.735 -24.917 -4.220 1.00 78.36 O ANISOU 664 OE2 GLU A 83 10606 7503 11663 -1873 496 -193 O ATOM 665 N GLU A 84 -21.495 -22.259 -6.646 1.00 55.71 N ANISOU 665 N GLU A 84 8591 5403 7174 -1034 32 -496 N ATOM 666 CA GLU A 84 -20.164 -22.232 -7.248 1.00 52.85 C ANISOU 666 CA GLU A 84 8416 5090 6574 -874 -2 -560 C ATOM 667 C GLU A 84 -19.574 -20.821 -7.183 1.00 47.65 C ANISOU 667 C GLU A 84 7763 4707 5634 -741 -14 -474 C ATOM 668 O GLU A 84 -18.416 -20.659 -6.804 1.00 45.17 O ANISOU 668 O GLU A 84 7547 4438 5177 -608 69 -375 O ATOM 669 CB GLU A 84 -20.155 -22.750 -8.696 1.00 54.96 C ANISOU 669 CB GLU A 84 8760 5297 6824 -888 -179 -841 C ATOM 670 CG GLU A 84 -20.120 -24.294 -8.841 1.00 61.92 C ANISOU 670 CG GLU A 84 9729 5857 7941 -959 -153 -953 C ATOM 671 CD GLU A 84 -19.876 -24.766 -10.284 1.00 67.51 C ANISOU 671 CD GLU A 84 10565 6522 8563 -916 -331 -1254 C ATOM 672 OE1 GLU A 84 -19.695 -23.912 -11.193 1.00 69.24 O ANISOU 672 OE1 GLU A 84 10816 6976 8517 -814 -461 -1356 O ATOM 673 OE2 GLU A 84 -19.852 -26.000 -10.509 1.00 72.52 O ANISOU 673 OE2 GLU A 84 11287 6879 9387 -968 -331 -1388 O ATOM 674 N ILE A 85 -20.374 -19.812 -7.548 1.00 44.62 N ANISOU 674 N ILE A 85 7263 4494 5195 -776 -121 -514 N ATOM 675 CA ILE A 85 -19.888 -18.449 -7.591 1.00 40.71 C ANISOU 675 CA ILE A 85 6779 4223 4466 -663 -136 -445 C ATOM 676 C ILE A 85 -19.508 -17.937 -6.192 1.00 38.71 C ANISOU 676 C ILE A 85 6509 4017 4181 -608 12 -232 C ATOM 677 O ILE A 85 -18.473 -17.297 -6.016 1.00 34.93 O ANISOU 677 O ILE A 85 6098 3635 3540 -496 41 -172 O ATOM 678 CB ILE A 85 -20.847 -17.488 -8.341 1.00 40.82 C ANISOU 678 CB ILE A 85 6691 4395 4424 -686 -285 -529 C ATOM 679 CG1 ILE A 85 -21.002 -17.919 -9.814 1.00 43.56 C ANISOU 679 CG1 ILE A 85 7097 4735 4721 -684 -460 -758 C ATOM 680 CG2 ILE A 85 -20.286 -16.076 -8.310 1.00 39.24 C ANISOU 680 CG2 ILE A 85 6519 4381 4009 -568 -269 -434 C ATOM 681 CD1 ILE A 85 -21.998 -17.045 -10.591 1.00 47.51 C ANISOU 681 CD1 ILE A 85 7498 5401 5152 -679 -634 -844 C ATOM 682 N ARG A 86 -20.347 -18.223 -5.192 1.00 38.96 N ANISOU 682 N ARG A 86 6448 3982 4374 -682 106 -124 N ATOM 683 CA ARG A 86 -20.080 -17.815 -3.824 1.00 37.56 C ANISOU 683 CA ARG A 86 6277 3853 4139 -605 243 66 C ATOM 684 C ARG A 86 -18.773 -18.465 -3.327 1.00 37.12 C ANISOU 684 C ARG A 86 6363 3724 4016 -496 323 138 C ATOM 685 O ARG A 86 -17.964 -17.833 -2.630 1.00 36.01 O ANISOU 685 O ARG A 86 6267 3693 3724 -376 350 224 O ATOM 686 CB ARG A 86 -21.285 -18.259 -2.969 1.00 41.04 C ANISOU 686 CB ARG A 86 6602 4209 4782 -698 362 174 C ATOM 687 CG ARG A 86 -21.443 -17.675 -1.603 1.00 43.66 C ANISOU 687 CG ARG A 86 6921 4628 5040 -612 501 359 C ATOM 688 CD ARG A 86 -21.357 -16.172 -1.460 1.00 42.45 C ANISOU 688 CD ARG A 86 6751 4683 4694 -521 437 354 C ATOM 689 NE ARG A 86 -22.645 -15.446 -1.487 1.00 43.58 N ANISOU 689 NE ARG A 86 6738 4913 4908 -571 428 351 N ATOM 690 CZ ARG A 86 -22.758 -14.172 -1.123 1.00 42.27 C ANISOU 690 CZ ARG A 86 6560 4899 4603 -480 413 374 C ATOM 691 NH1 ARG A 86 -21.681 -13.529 -0.665 1.00 38.24 N ANISOU 691 NH1 ARG A 86 6177 4456 3898 -358 401 393 N ATOM 692 NH2 ARG A 86 -23.933 -13.543 -1.172 1.00 44.03 N ANISOU 692 NH2 ARG A 86 6635 5197 4896 -505 410 374 N ATOM 693 N GLU A 87 -18.567 -19.726 -3.696 1.00 38.10 N ANISOU 693 N GLU A 87 6552 3660 4263 -530 346 89 N ATOM 694 CA GLU A 87 -17.308 -20.442 -3.390 1.00 38.42 C ANISOU 694 CA GLU A 87 6726 3620 4250 -406 411 144 C ATOM 695 C GLU A 87 -16.071 -19.713 -3.942 1.00 35.10 C ANISOU 695 C GLU A 87 6351 3355 3631 -288 333 82 C ATOM 696 O GLU A 87 -15.081 -19.489 -3.228 1.00 33.24 O ANISOU 696 O GLU A 87 6150 3189 3291 -160 370 178 O ATOM 697 CB GLU A 87 -17.349 -21.904 -3.896 1.00 41.39 C ANISOU 697 CB GLU A 87 7174 3742 4809 -462 439 68 C ATOM 698 CG GLU A 87 -16.049 -22.623 -3.518 1.00 46.43 C ANISOU 698 CG GLU A 87 7948 4301 5390 -301 517 144 C ATOM 699 CD GLU A 87 -15.901 -24.023 -4.057 1.00 55.34 C ANISOU 699 CD GLU A 87 9180 5164 6682 -319 548 59 C ATOM 700 OE1 GLU A 87 -14.769 -24.358 -4.491 1.00 57.37 O ANISOU 700 OE1 GLU A 87 9536 5411 6849 -183 538 7 O ATOM 701 OE2 GLU A 87 -16.896 -24.787 -4.027 1.00 59.76 O ANISOU 701 OE2 GLU A 87 9714 5515 7476 -466 590 44 O ATOM 702 N ALA A 88 -16.134 -19.324 -5.214 1.00 33.54 N ANISOU 702 N ALA A 88 6145 3216 3382 -324 226 -73 N ATOM 703 CA ALA A 88 -15.060 -18.520 -5.826 1.00 31.73 C ANISOU 703 CA ALA A 88 5940 3133 2982 -224 185 -110 C ATOM 704 C ALA A 88 -14.911 -17.139 -5.172 1.00 30.75 C ANISOU 704 C ALA A 88 5743 3181 2759 -195 176 -19 C ATOM 705 O ALA A 88 -13.779 -16.677 -4.884 1.00 30.29 O ANISOU 705 O ALA A 88 5686 3202 2622 -102 192 26 O ATOM 706 CB ALA A 88 -15.314 -18.363 -7.323 1.00 32.01 C ANISOU 706 CB ALA A 88 6000 3201 2959 -250 91 -273 C ATOM 707 N PHE A 89 -16.043 -16.490 -4.888 1.00 29.50 N ANISOU 707 N PHE A 89 5511 3071 2626 -272 150 0 N ATOM 708 CA PHE A 89 -16.013 -15.198 -4.198 1.00 29.12 C ANISOU 708 CA PHE A 89 5412 3158 2496 -239 143 70 C ATOM 709 C PHE A 89 -15.199 -15.267 -2.897 1.00 30.11 C ANISOU 709 C PHE A 89 5561 3296 2582 -144 199 174 C ATOM 710 O PHE A 89 -14.328 -14.416 -2.651 1.00 29.12 O ANISOU 710 O PHE A 89 5423 3266 2377 -81 166 179 O ATOM 711 CB PHE A 89 -17.434 -14.690 -3.909 1.00 28.37 C ANISOU 711 CB PHE A 89 5236 3094 2451 -312 132 88 C ATOM 712 CG PHE A 89 -17.472 -13.307 -3.258 1.00 29.03 C ANISOU 712 CG PHE A 89 5284 3299 2446 -264 123 137 C ATOM 713 CD1 PHE A 89 -17.202 -12.156 -4.031 1.00 29.45 C ANISOU 713 CD1 PHE A 89 5331 3435 2423 -249 56 89 C ATOM 714 CD2 PHE A 89 -17.782 -13.163 -1.901 1.00 30.81 C ANISOU 714 CD2 PHE A 89 5502 3543 2662 -220 192 232 C ATOM 715 CE1 PHE A 89 -17.249 -10.902 -3.480 1.00 28.06 C ANISOU 715 CE1 PHE A 89 5135 3331 2196 -211 46 119 C ATOM 716 CE2 PHE A 89 -17.818 -11.874 -1.292 1.00 27.37 C ANISOU 716 CE2 PHE A 89 5055 3206 2140 -161 173 247 C ATOM 717 CZ PHE A 89 -17.548 -10.733 -2.096 1.00 26.48 C ANISOU 717 CZ PHE A 89 4929 3148 1985 -168 93 181 C ATOM 718 N ARG A 90 -15.481 -16.283 -2.076 1.00 31.45 N ANISOU 718 N ARG A 90 5766 3366 2818 -129 279 256 N ATOM 719 CA ARG A 90 -14.795 -16.433 -0.794 1.00 33.72 C ANISOU 719 CA ARG A 90 6097 3679 3036 -3 325 366 C ATOM 720 C ARG A 90 -13.287 -16.677 -0.907 1.00 34.09 C ANISOU 720 C ARG A 90 6174 3746 3031 105 289 347 C ATOM 721 O ARG A 90 -12.562 -16.357 0.042 1.00 34.18 O ANISOU 721 O ARG A 90 6189 3842 2955 221 262 397 O ATOM 722 CB ARG A 90 -15.457 -17.502 0.108 1.00 35.93 C ANISOU 722 CB ARG A 90 6425 3837 3389 11 452 497 C ATOM 723 CG ARG A 90 -16.941 -17.215 0.473 1.00 38.72 C ANISOU 723 CG ARG A 90 6712 4188 3810 -79 519 547 C ATOM 724 CD ARG A 90 -17.578 -18.320 1.389 1.00 45.39 C ANISOU 724 CD ARG A 90 7595 4893 4757 -68 695 713 C ATOM 725 NE ARG A 90 -16.977 -19.634 1.195 1.00 50.09 N ANISOU 725 NE ARG A 90 8277 5311 5443 -47 744 742 N ATOM 726 CZ ARG A 90 -17.591 -20.680 0.637 1.00 53.26 C ANISOU 726 CZ ARG A 90 8667 5505 6066 -177 804 722 C ATOM 727 NH1 ARG A 90 -18.858 -20.590 0.231 1.00 54.80 N ANISOU 727 NH1 ARG A 90 8739 5658 6425 -347 813 675 N ATOM 728 NH2 ARG A 90 -16.933 -21.819 0.476 1.00 55.32 N ANISOU 728 NH2 ARG A 90 9028 5592 6399 -134 846 738 N ATOM 729 N VAL A 91 -12.824 -17.272 -2.017 1.00 33.54 N ANISOU 729 N VAL A 91 6123 3606 3014 85 286 271 N ATOM 730 CA VAL A 91 -11.388 -17.408 -2.311 1.00 33.54 C ANISOU 730 CA VAL A 91 6120 3642 2982 190 267 247 C ATOM 731 C VAL A 91 -10.706 -16.029 -2.280 1.00 32.78 C ANISOU 731 C VAL A 91 5929 3706 2822 202 193 217 C ATOM 732 O VAL A 91 -9.580 -15.879 -1.760 1.00 33.29 O ANISOU 732 O VAL A 91 5946 3840 2865 302 158 235 O ATOM 733 CB VAL A 91 -11.157 -18.102 -3.702 1.00 34.50 C ANISOU 733 CB VAL A 91 6283 3675 3149 170 290 148 C ATOM 734 CG1 VAL A 91 -9.702 -17.993 -4.159 1.00 36.09 C ANISOU 734 CG1 VAL A 91 6447 3946 3318 278 294 125 C ATOM 735 CG2 VAL A 91 -11.599 -19.583 -3.631 1.00 34.73 C ANISOU 735 CG2 VAL A 91 6412 3505 3280 170 357 162 C ATOM 736 N PHE A 92 -11.395 -15.014 -2.807 1.00 31.08 N ANISOU 736 N PHE A 92 5678 3539 2593 100 163 170 N ATOM 737 CA PHE A 92 -10.826 -13.654 -2.915 1.00 29.25 C ANISOU 737 CA PHE A 92 5363 3414 2337 89 110 142 C ATOM 738 C PHE A 92 -11.157 -12.756 -1.747 1.00 30.95 C ANISOU 738 C PHE A 92 5555 3692 2514 96 54 161 C ATOM 739 O PHE A 92 -10.322 -11.904 -1.344 1.00 32.43 O ANISOU 739 O PHE A 92 5674 3946 2702 123 -11 133 O ATOM 740 CB PHE A 92 -11.285 -12.991 -4.234 1.00 27.85 C ANISOU 740 CB PHE A 92 5183 3245 2156 7 119 92 C ATOM 741 CG PHE A 92 -10.752 -13.686 -5.429 1.00 29.54 C ANISOU 741 CG PHE A 92 5430 3425 2367 34 170 55 C ATOM 742 CD1 PHE A 92 -11.523 -14.654 -6.083 1.00 29.30 C ANISOU 742 CD1 PHE A 92 5485 3314 2334 11 180 4 C ATOM 743 CD2 PHE A 92 -9.446 -13.450 -5.849 1.00 29.77 C ANISOU 743 CD2 PHE A 92 5403 3498 2412 90 211 60 C ATOM 744 CE1 PHE A 92 -11.011 -15.379 -7.211 1.00 30.02 C ANISOU 744 CE1 PHE A 92 5638 3368 2400 63 222 -59 C ATOM 745 CE2 PHE A 92 -8.925 -14.112 -6.954 1.00 29.53 C ANISOU 745 CE2 PHE A 92 5416 3446 2359 146 283 28 C ATOM 746 CZ PHE A 92 -9.711 -15.107 -7.651 1.00 28.57 C ANISOU 746 CZ PHE A 92 5416 3243 2196 144 285 -40 C ATOM 747 N ASP A 93 -12.361 -12.913 -1.189 1.00 29.42 N ANISOU 747 N ASP A 93 5409 3475 2297 75 78 199 N ATOM 748 CA ASP A 93 -12.737 -12.058 -0.027 1.00 30.91 C ANISOU 748 CA ASP A 93 5597 3730 2419 114 41 213 C ATOM 749 C ASP A 93 -12.124 -12.616 1.262 1.00 31.79 C ANISOU 749 C ASP A 93 5750 3873 2454 252 25 265 C ATOM 750 O ASP A 93 -12.807 -13.207 2.082 1.00 31.76 O ANISOU 750 O ASP A 93 5815 3850 2400 309 93 351 O ATOM 751 CB ASP A 93 -14.254 -11.927 0.058 1.00 30.16 C ANISOU 751 CB ASP A 93 5516 3616 2327 59 95 245 C ATOM 752 CG ASP A 93 -14.706 -11.103 1.218 1.00 28.25 C ANISOU 752 CG ASP A 93 5292 3442 2001 125 83 258 C ATOM 753 OD1 ASP A 93 -15.858 -11.316 1.654 1.00 27.36 O ANISOU 753 OD1 ASP A 93 5192 3319 1885 124 164 322 O ATOM 754 OD2 ASP A 93 -13.906 -10.274 1.701 1.00 29.33 O ANISOU 754 OD2 ASP A 93 5424 3637 2085 180 -5 199 O ATOM 755 N LYS A 94 -10.807 -12.434 1.404 1.00 33.35 N ANISOU 755 N LYS A 94 5898 4123 2651 316 -61 219 N ATOM 756 CA LYS A 94 -10.037 -13.055 2.484 1.00 35.52 C ANISOU 756 CA LYS A 94 6204 4446 2847 477 -106 260 C ATOM 757 C LYS A 94 -10.597 -12.813 3.882 1.00 35.41 C ANISOU 757 C LYS A 94 6276 4496 2680 590 -126 298 C ATOM 758 O LYS A 94 -10.628 -13.736 4.698 1.00 36.19 O ANISOU 758 O LYS A 94 6467 4594 2689 727 -76 406 O ATOM 759 CB LYS A 94 -8.583 -12.558 2.462 1.00 37.24 C ANISOU 759 CB LYS A 94 6303 4739 3107 515 -235 172 C ATOM 760 CG LYS A 94 -7.837 -12.805 1.131 1.00 40.03 C ANISOU 760 CG LYS A 94 6564 5048 3598 442 -188 151 C ATOM 761 CD LYS A 94 -7.890 -14.260 0.751 1.00 43.34 C ANISOU 761 CD LYS A 94 7060 5382 4025 496 -81 232 C ATOM 762 CE LYS A 94 -6.980 -15.110 1.625 1.00 49.93 C ANISOU 762 CE LYS A 94 7902 6254 4816 682 -126 284 C ATOM 763 NZ LYS A 94 -7.674 -16.416 1.921 1.00 52.87 N ANISOU 763 NZ LYS A 94 8427 6511 5149 749 -11 402 N ATOM 764 N ASP A 95 -11.029 -11.585 4.181 1.00 33.69 N ANISOU 764 N ASP A 95 6047 4332 2424 556 -185 218 N ATOM 765 CA ASP A 95 -11.477 -11.308 5.552 1.00 34.16 C ANISOU 765 CA ASP A 95 6205 4469 2304 700 -205 236 C ATOM 766 C ASP A 95 -12.964 -11.499 5.739 1.00 32.94 C ANISOU 766 C ASP A 95 6123 4275 2118 680 -39 342 C ATOM 767 O ASP A 95 -13.480 -11.255 6.837 1.00 33.69 O ANISOU 767 O ASP A 95 6308 4437 2055 811 -11 375 O ATOM 768 CB ASP A 95 -11.090 -9.915 6.039 1.00 35.37 C ANISOU 768 CB ASP A 95 6328 4699 2411 720 -369 74 C ATOM 769 CG ASP A 95 -11.797 -8.783 5.240 1.00 35.25 C ANISOU 769 CG ASP A 95 6263 4625 2506 559 -345 5 C ATOM 770 OD1 ASP A 95 -12.636 -9.017 4.322 1.00 33.09 O ANISOU 770 OD1 ASP A 95 5973 4280 2322 444 -219 76 O ATOM 771 OD2 ASP A 95 -11.499 -7.623 5.536 1.00 33.61 O ANISOU 771 OD2 ASP A 95 6033 4436 2299 556 -466 -131 O ATOM 772 N GLY A 96 -13.631 -11.933 4.678 1.00 30.71 N ANISOU 772 N GLY A 96 5793 3892 1984 529 66 387 N ATOM 773 CA GLY A 96 -15.045 -12.299 4.729 1.00 30.28 C ANISOU 773 CA GLY A 96 5757 3785 1962 484 225 490 C ATOM 774 C GLY A 96 -15.998 -11.124 4.944 1.00 30.12 C ANISOU 774 C GLY A 96 5718 3820 1907 469 233 445 C ATOM 775 O GLY A 96 -17.149 -11.329 5.317 1.00 30.57 O ANISOU 775 O GLY A 96 5781 3868 1967 478 372 540 O ATOM 776 N ASN A 97 -15.540 -9.897 4.697 1.00 28.80 N ANISOU 776 N ASN A 97 5518 3694 1729 447 99 307 N ATOM 777 CA ASN A 97 -16.414 -8.722 4.931 1.00 28.72 C ANISOU 777 CA ASN A 97 5508 3719 1686 458 105 257 C ATOM 778 C ASN A 97 -17.385 -8.402 3.784 1.00 26.58 C ANISOU 778 C ASN A 97 5147 3397 1557 317 152 261 C ATOM 779 O ASN A 97 -18.162 -7.467 3.890 1.00 26.87 O ANISOU 779 O ASN A 97 5172 3455 1581 336 166 232 O ATOM 780 CB ASN A 97 -15.604 -7.458 5.344 1.00 29.66 C ANISOU 780 CB ASN A 97 5651 3878 1739 513 -55 101 C ATOM 781 CG ASN A 97 -14.958 -6.754 4.155 1.00 29.39 C ANISOU 781 CG ASN A 97 5528 3781 1859 369 -147 10 C ATOM 782 OD1 ASN A 97 -14.686 -7.372 3.114 1.00 28.59 O ANISOU 782 OD1 ASN A 97 5366 3634 1863 266 -119 52 O ATOM 783 ND2 ASN A 97 -14.685 -5.453 4.307 1.00 28.75 N ANISOU 783 ND2 ASN A 97 5448 3685 1790 370 -245 -115 N ATOM 784 N GLY A 98 -17.350 -9.187 2.705 1.00 26.39 N ANISOU 784 N GLY A 98 5064 3309 1654 198 169 288 N ATOM 785 CA GLY A 98 -18.295 -9.053 1.603 1.00 25.27 C ANISOU 785 CA GLY A 98 4840 3136 1625 86 189 284 C ATOM 786 C GLY A 98 -17.806 -8.158 0.473 1.00 26.76 C ANISOU 786 C GLY A 98 5003 3315 1851 23 90 198 C ATOM 787 O GLY A 98 -18.562 -7.911 -0.500 1.00 25.68 O ANISOU 787 O GLY A 98 4813 3171 1774 -38 83 190 O ATOM 788 N TYR A 99 -16.583 -7.640 0.621 1.00 27.19 N ANISOU 788 N TYR A 99 5087 3370 1874 49 17 140 N ATOM 789 CA TYR A 99 -15.933 -6.747 -0.370 1.00 27.91 C ANISOU 789 CA TYR A 99 5154 3433 2018 -7 -42 85 C ATOM 790 C TYR A 99 -14.529 -7.245 -0.663 1.00 28.44 C ANISOU 790 C TYR A 99 5206 3486 2115 -25 -71 66 C ATOM 791 O TYR A 99 -13.714 -7.403 0.269 1.00 28.90 O ANISOU 791 O TYR A 99 5271 3568 2142 34 -117 41 O ATOM 792 CB TYR A 99 -15.851 -5.273 0.133 1.00 27.46 C ANISOU 792 CB TYR A 99 5114 3366 1953 29 -94 21 C ATOM 793 CG TYR A 99 -17.219 -4.677 0.343 1.00 28.78 C ANISOU 793 CG TYR A 99 5292 3548 2096 70 -55 39 C ATOM 794 CD1 TYR A 99 -17.879 -4.838 1.564 1.00 28.40 C ANISOU 794 CD1 TYR A 99 5278 3549 1962 165 -13 53 C ATOM 795 CD2 TYR A 99 -17.906 -4.058 -0.711 1.00 26.64 C ANISOU 795 CD2 TYR A 99 4994 3254 1874 37 -45 61 C ATOM 796 CE1 TYR A 99 -19.182 -4.342 1.760 1.00 30.94 C ANISOU 796 CE1 TYR A 99 5586 3895 2273 218 48 80 C ATOM 797 CE2 TYR A 99 -19.216 -3.544 -0.525 1.00 29.77 C ANISOU 797 CE2 TYR A 99 5376 3678 2259 94 -11 82 C ATOM 798 CZ TYR A 99 -19.833 -3.683 0.715 1.00 31.51 C ANISOU 798 CZ TYR A 99 5609 3944 2418 179 40 89 C ATOM 799 OH TYR A 99 -21.127 -3.220 0.918 1.00 34.37 O ANISOU 799 OH TYR A 99 5935 4342 2781 249 96 118 O ATOM 800 N ILE A 100 -14.250 -7.503 -1.943 1.00 28.30 N ANISOU 800 N ILE A 100 5167 3442 2144 -84 -48 77 N ATOM 801 CA ILE A 100 -12.890 -7.800 -2.382 1.00 29.13 C ANISOU 801 CA ILE A 100 5238 3537 2292 -92 -50 65 C ATOM 802 C ILE A 100 -12.153 -6.476 -2.565 1.00 29.09 C ANISOU 802 C ILE A 100 5185 3510 2359 -123 -76 34 C ATOM 803 O ILE A 100 -12.524 -5.633 -3.400 1.00 28.56 O ANISOU 803 O ILE A 100 5127 3410 2314 -159 -44 55 O ATOM 804 CB ILE A 100 -12.831 -8.606 -3.689 1.00 29.25 C ANISOU 804 CB ILE A 100 5268 3535 2310 -117 5 85 C ATOM 805 CG1 ILE A 100 -13.580 -9.941 -3.513 1.00 27.59 C ANISOU 805 CG1 ILE A 100 5099 3306 2077 -110 25 98 C ATOM 806 CG2 ILE A 100 -11.381 -8.863 -4.094 1.00 30.13 C ANISOU 806 CG2 ILE A 100 5334 3646 2468 -101 31 82 C ATOM 807 CD1 ILE A 100 -13.974 -10.531 -4.899 1.00 30.06 C ANISOU 807 CD1 ILE A 100 5443 3595 2382 -141 45 73 C ATOM 808 N SER A 101 -11.113 -6.300 -1.774 1.00 28.37 N ANISOU 808 N SER A 101 5038 3428 2314 -104 -139 -15 N ATOM 809 CA SER A 101 -10.329 -5.091 -1.872 1.00 29.59 C ANISOU 809 CA SER A 101 5119 3534 2591 -158 -169 -60 C ATOM 810 C SER A 101 -9.177 -5.350 -2.835 1.00 30.37 C ANISOU 810 C SER A 101 5125 3622 2792 -197 -100 -21 C ATOM 811 O SER A 101 -8.913 -6.500 -3.181 1.00 29.60 O ANISOU 811 O SER A 101 5031 3566 2648 -155 -56 14 O ATOM 812 CB SER A 101 -9.797 -4.689 -0.526 1.00 30.98 C ANISOU 812 CB SER A 101 5261 3727 2782 -123 -301 -164 C ATOM 813 OG SER A 101 -8.891 -5.669 -0.085 1.00 32.04 O ANISOU 813 OG SER A 101 5340 3929 2905 -65 -348 -174 O ATOM 814 N ALA A 102 -8.529 -4.276 -3.293 1.00 30.77 N ANISOU 814 N ALA A 102 5095 3603 2992 -270 -68 -20 N ATOM 815 CA ALA A 102 -7.297 -4.370 -4.107 1.00 32.53 C ANISOU 815 CA ALA A 102 5195 3816 3349 -306 25 28 C ATOM 816 C ALA A 102 -6.223 -5.157 -3.333 1.00 33.21 C ANISOU 816 C ALA A 102 5161 3973 3485 -263 -61 -34 C ATOM 817 O ALA A 102 -5.551 -6.034 -3.885 1.00 32.74 O ANISOU 817 O ALA A 102 5051 3958 3432 -220 16 14 O ATOM 818 CB ALA A 102 -6.777 -2.909 -4.455 1.00 34.37 C ANISOU 818 CB ALA A 102 5339 3930 3790 -411 75 42 C ATOM 819 N ALA A 103 -6.070 -4.873 -2.039 1.00 32.93 N ANISOU 819 N ALA A 103 5091 3956 3465 -248 -229 -145 N ATOM 820 CA ALA A 103 -5.109 -5.649 -1.221 1.00 32.99 C ANISOU 820 CA ALA A 103 4995 4053 3486 -170 -342 -204 C ATOM 821 C ALA A 103 -5.412 -7.172 -1.193 1.00 32.81 C ANISOU 821 C ALA A 103 5075 4102 3291 -47 -301 -136 C ATOM 822 O ALA A 103 -4.492 -7.995 -1.303 1.00 32.21 O ANISOU 822 O ALA A 103 4909 4075 3254 18 -288 -116 O ATOM 823 CB ALA A 103 -5.019 -5.074 0.231 1.00 34.77 C ANISOU 823 CB ALA A 103 5206 4304 3700 -139 -557 -353 C ATOM 824 N GLU A 104 -6.683 -7.554 -1.036 1.00 29.71 N ANISOU 824 N GLU A 104 4856 3702 2730 -14 -274 -100 N ATOM 825 CA GLU A 104 -7.018 -8.983 -1.035 1.00 29.67 C ANISOU 825 CA GLU A 104 4946 3721 2607 77 -221 -35 C ATOM 826 C GLU A 104 -6.728 -9.625 -2.396 1.00 28.76 C ANISOU 826 C GLU A 104 4823 3576 2529 61 -82 24 C ATOM 827 O GLU A 104 -6.201 -10.734 -2.465 1.00 28.86 O ANISOU 827 O GLU A 104 4834 3601 2530 146 -51 50 O ATOM 828 CB GLU A 104 -8.477 -9.228 -0.638 1.00 27.63 C ANISOU 828 CB GLU A 104 4842 3445 2212 90 -202 -5 C ATOM 829 CG GLU A 104 -8.724 -8.914 0.857 1.00 31.19 C ANISOU 829 CG GLU A 104 5334 3946 2570 169 -316 -49 C ATOM 830 CD GLU A 104 -10.194 -8.915 1.207 1.00 29.41 C ANISOU 830 CD GLU A 104 5231 3705 2238 175 -264 -8 C ATOM 831 OE1 GLU A 104 -10.535 -9.346 2.318 1.00 32.29 O ANISOU 831 OE1 GLU A 104 5673 4113 2485 283 -282 17 O ATOM 832 OE2 GLU A 104 -11.024 -8.487 0.373 1.00 28.64 O ANISOU 832 OE2 GLU A 104 5149 3562 2172 86 -197 9 O ATOM 833 N LEU A 105 -7.064 -8.933 -3.481 1.00 28.28 N ANISOU 833 N LEU A 105 4773 3474 2498 -23 6 47 N ATOM 834 CA LEU A 105 -6.812 -9.481 -4.798 1.00 30.02 C ANISOU 834 CA LEU A 105 5013 3682 2711 -9 138 94 C ATOM 835 C LEU A 105 -5.296 -9.605 -5.037 1.00 31.84 C ANISOU 835 C LEU A 105 5085 3944 3068 27 189 105 C ATOM 836 O LEU A 105 -4.850 -10.605 -5.566 1.00 32.09 O ANISOU 836 O LEU A 105 5132 3987 3075 109 266 126 O ATOM 837 CB LEU A 105 -7.490 -8.616 -5.892 1.00 29.38 C ANISOU 837 CB LEU A 105 4991 3569 2602 -73 217 129 C ATOM 838 CG LEU A 105 -7.302 -9.121 -7.322 1.00 32.26 C ANISOU 838 CG LEU A 105 5411 3940 2906 -28 351 170 C ATOM 839 CD1 LEU A 105 -7.832 -10.583 -7.544 1.00 31.27 C ANISOU 839 CD1 LEU A 105 5406 3807 2666 40 343 130 C ATOM 840 CD2 LEU A 105 -7.966 -8.151 -8.305 1.00 31.07 C ANISOU 840 CD2 LEU A 105 5330 3774 2700 -60 412 220 C ATOM 841 N ARG A 106 -4.515 -8.610 -4.607 1.00 32.03 N ANISOU 841 N ARG A 106 4947 3975 3247 -32 140 82 N ATOM 842 CA ARG A 106 -3.064 -8.679 -4.679 1.00 35.11 C ANISOU 842 CA ARG A 106 5133 4404 3804 -9 169 85 C ATOM 843 C ARG A 106 -2.510 -9.941 -3.933 1.00 35.64 C ANISOU 843 C ARG A 106 5174 4539 3830 131 89 60 C ATOM 844 O ARG A 106 -1.686 -10.712 -4.477 1.00 35.48 O ANISOU 844 O ARG A 106 5085 4548 3850 219 186 97 O ATOM 845 CB ARG A 106 -2.494 -7.370 -4.097 1.00 37.03 C ANISOU 845 CB ARG A 106 5200 4624 4247 -120 76 27 C ATOM 846 CG ARG A 106 -0.981 -7.265 -4.036 1.00 45.28 C ANISOU 846 CG ARG A 106 5970 5708 5528 -127 75 11 C ATOM 847 CD ARG A 106 -0.506 -5.845 -3.587 1.00 52.48 C ANISOU 847 CD ARG A 106 6700 6554 6687 -279 -16 -65 C ATOM 848 NE ARG A 106 -1.460 -4.763 -3.892 1.00 54.02 N ANISOU 848 NE ARG A 106 7031 6630 6864 -389 30 -46 N ATOM 849 CZ ARG A 106 -1.972 -3.926 -2.983 1.00 56.77 C ANISOU 849 CZ ARG A 106 7425 6924 7222 -447 -139 -160 C ATOM 850 NH1 ARG A 106 -2.826 -2.963 -3.348 1.00 55.00 N ANISOU 850 NH1 ARG A 106 7326 6584 6989 -525 -75 -128 N ATOM 851 NH2 ARG A 106 -1.629 -4.028 -1.700 1.00 59.49 N ANISOU 851 NH2 ARG A 106 7700 7331 7570 -404 -375 -310 N ATOM 852 N HIS A 107 -2.990 -10.156 -2.712 1.00 35.18 N ANISOU 852 N HIS A 107 5187 4502 3678 175 -71 10 N ATOM 853 CA HIS A 107 -2.601 -11.325 -1.921 1.00 36.63 C ANISOU 853 CA HIS A 107 5385 4739 3794 332 -145 12 C ATOM 854 C HIS A 107 -2.893 -12.649 -2.611 1.00 35.10 C ANISOU 854 C HIS A 107 5331 4498 3508 420 -11 80 C ATOM 855 O HIS A 107 -2.018 -13.494 -2.670 1.00 35.82 O ANISOU 855 O HIS A 107 5358 4615 3637 542 17 101 O ATOM 856 CB HIS A 107 -3.188 -11.260 -0.508 1.00 38.12 C ANISOU 856 CB HIS A 107 5663 4960 3860 384 -312 -29 C ATOM 857 CG HIS A 107 -2.761 -10.034 0.253 1.00 45.23 C ANISOU 857 CG HIS A 107 6431 5907 4849 325 -479 -138 C ATOM 858 ND1 HIS A 107 -3.381 -9.616 1.418 1.00 51.31 N ANISOU 858 ND1 HIS A 107 7297 6705 5494 359 -622 -202 N ATOM 859 CD2 HIS A 107 -1.801 -9.108 -0.014 1.00 51.57 C ANISOU 859 CD2 HIS A 107 7012 6716 5866 230 -517 -203 C ATOM 860 CE1 HIS A 107 -2.802 -8.503 1.846 1.00 53.80 C ANISOU 860 CE1 HIS A 107 7469 7040 5934 293 -768 -328 C ATOM 861 NE2 HIS A 107 -1.846 -8.171 0.992 1.00 54.70 N ANISOU 861 NE2 HIS A 107 7377 7130 6276 199 -708 -328 N ATOM 862 N VAL A 108 -4.093 -12.819 -3.159 1.00 33.32 N ANISOU 862 N VAL A 108 5284 4197 3180 360 64 99 N ATOM 863 CA VAL A 108 -4.437 -14.058 -3.831 1.00 33.03 C ANISOU 863 CA VAL A 108 5386 4090 3076 425 169 127 C ATOM 864 C VAL A 108 -3.567 -14.249 -5.076 1.00 34.07 C ANISOU 864 C VAL A 108 5452 4228 3264 464 305 133 C ATOM 865 O VAL A 108 -3.024 -15.348 -5.323 1.00 33.79 O ANISOU 865 O VAL A 108 5442 4168 3227 591 368 143 O ATOM 866 CB VAL A 108 -5.949 -14.127 -4.230 1.00 33.56 C ANISOU 866 CB VAL A 108 5625 4079 3048 336 195 120 C ATOM 867 CG1 VAL A 108 -6.201 -15.409 -5.096 1.00 35.42 C ANISOU 867 CG1 VAL A 108 5990 4221 3245 389 288 108 C ATOM 868 CG2 VAL A 108 -6.835 -14.121 -2.994 1.00 32.75 C ANISOU 868 CG2 VAL A 108 5588 3966 2890 324 106 137 C ATOM 869 N MET A 109 -3.428 -13.180 -5.874 1.00 32.40 N ANISOU 869 N MET A 109 5168 4044 3100 371 371 139 N ATOM 870 CA MET A 109 -2.541 -13.244 -7.040 1.00 34.34 C ANISOU 870 CA MET A 109 5343 4312 3391 423 536 170 C ATOM 871 C MET A 109 -1.100 -13.663 -6.656 1.00 34.90 C ANISOU 871 C MET A 109 5216 4446 3600 535 547 185 C ATOM 872 O MET A 109 -0.471 -14.506 -7.323 1.00 35.22 O ANISOU 872 O MET A 109 5259 4490 3634 664 673 201 O ATOM 873 CB MET A 109 -2.563 -11.919 -7.837 1.00 34.36 C ANISOU 873 CB MET A 109 5290 4326 3438 313 626 212 C ATOM 874 CG MET A 109 -3.947 -11.692 -8.399 1.00 35.24 C ANISOU 874 CG MET A 109 5606 4393 3392 256 620 200 C ATOM 875 SD MET A 109 -4.300 -12.838 -9.751 1.00 42.36 S ANISOU 875 SD MET A 109 6708 5273 4112 376 737 172 S ATOM 876 CE MET A 109 -5.748 -13.595 -9.080 1.00 41.86 C ANISOU 876 CE MET A 109 6809 5136 3961 333 575 91 C ATOM 877 N THR A 110 -0.582 -13.066 -5.594 1.00 34.31 N ANISOU 877 N THR A 110 4966 4425 3647 498 407 167 N ATOM 878 CA THR A 110 0.764 -13.410 -5.137 1.00 37.24 C ANISOU 878 CA THR A 110 5113 4875 4161 608 374 167 C ATOM 879 C THR A 110 0.850 -14.890 -4.719 1.00 37.28 C ANISOU 879 C THR A 110 5227 4869 4069 800 348 175 C ATOM 880 O THR A 110 1.811 -15.581 -5.068 1.00 37.89 O ANISOU 880 O THR A 110 5205 4979 4212 943 436 200 O ATOM 881 CB THR A 110 1.195 -12.476 -3.988 1.00 38.01 C ANISOU 881 CB THR A 110 5014 5036 4391 534 172 108 C ATOM 882 OG1 THR A 110 1.216 -11.134 -4.509 1.00 41.15 O ANISOU 882 OG1 THR A 110 5306 5404 4924 355 232 109 O ATOM 883 CG2 THR A 110 2.577 -12.862 -3.467 1.00 42.02 C ANISOU 883 CG2 THR A 110 5266 5648 5054 661 96 92 C ATOM 884 N ASN A 111 -0.156 -15.369 -3.985 1.00 36.58 N ANISOU 884 N ASN A 111 5341 4722 3837 810 249 166 N ATOM 885 CA AASN A 111 -0.212 -16.773 -3.530 0.50 38.17 C ANISOU 885 CA AASN A 111 5679 4869 3956 983 240 196 C ATOM 886 CA BASN A 111 -0.125 -16.752 -3.550 0.50 38.16 C ANISOU 886 CA BASN A 111 5661 4874 3964 986 242 196 C ATOM 887 C ASN A 111 -0.224 -17.696 -4.758 1.00 38.95 C ANISOU 887 C ASN A 111 5901 4875 4026 1051 426 202 C ATOM 888 O ASN A 111 0.354 -18.774 -4.749 1.00 40.05 O ANISOU 888 O ASN A 111 6063 4980 4175 1228 473 223 O ATOM 889 CB AASN A 111 -1.472 -17.045 -2.681 0.50 37.08 C ANISOU 889 CB AASN A 111 5749 4657 3685 949 157 210 C ATOM 890 CB BASN A 111 -1.221 -17.035 -2.540 0.50 37.08 C ANISOU 890 CB BASN A 111 5709 4680 3700 974 139 212 C ATOM 891 CG AASN A 111 -1.426 -16.395 -1.304 0.50 39.20 C ANISOU 891 CG AASN A 111 5944 5021 3928 956 -29 201 C ATOM 892 CG BASN A 111 -0.991 -18.316 -1.821 0.50 40.38 C ANISOU 892 CG BASN A 111 6218 5055 4071 1173 120 273 C ATOM 893 OD1AASN A 111 -0.395 -15.862 -0.885 0.50 43.55 O ANISOU 893 OD1AASN A 111 6285 5691 4571 996 -136 166 O ATOM 894 OD1BASN A 111 0.030 -18.485 -1.151 0.50 41.16 O ANISOU 894 OD1BASN A 111 6178 5251 4209 1326 30 290 O ATOM 895 ND2AASN A 111 -2.556 -16.441 -0.583 0.50 39.42 N ANISOU 895 ND2AASN A 111 6141 5001 3834 923 -72 225 N ATOM 896 ND2BASN A 111 -1.907 -19.259 -1.986 0.50 41.94 N ANISOU 896 ND2BASN A 111 6640 5096 4201 1180 205 307 N ATOM 897 N LEU A 112 -0.897 -17.259 -5.829 1.00 38.09 N ANISOU 897 N LEU A 112 5884 4723 3866 930 525 173 N ATOM 898 CA LEU A 112 -0.948 -18.046 -7.101 1.00 39.13 C ANISOU 898 CA LEU A 112 6154 4779 3935 1005 686 145 C ATOM 899 C LEU A 112 0.347 -18.059 -7.871 1.00 42.21 C ANISOU 899 C LEU A 112 6389 5247 4402 1125 836 167 C ATOM 900 O LEU A 112 0.538 -18.895 -8.774 1.00 44.41 O ANISOU 900 O LEU A 112 6780 5472 4620 1253 972 138 O ATOM 901 CB LEU A 112 -2.026 -17.496 -8.036 1.00 37.65 C ANISOU 901 CB LEU A 112 6107 4556 3642 867 724 102 C ATOM 902 CG LEU A 112 -3.475 -17.875 -7.735 1.00 38.95 C ANISOU 902 CG LEU A 112 6466 4609 3724 775 631 58 C ATOM 903 CD1 LEU A 112 -4.422 -17.075 -8.652 1.00 39.34 C ANISOU 903 CD1 LEU A 112 6595 4671 3682 649 641 19 C ATOM 904 CD2 LEU A 112 -3.714 -19.386 -7.877 1.00 40.48 C ANISOU 904 CD2 LEU A 112 6834 4652 3894 879 661 10 C ATOM 905 N GLY A 113 1.235 -17.123 -7.557 1.00 43.60 N ANISOU 905 N GLY A 113 6300 5544 4721 1086 820 210 N ATOM 906 CA GLY A 113 2.522 -17.014 -8.245 1.00 48.79 C ANISOU 906 CA GLY A 113 6749 6289 5500 1184 985 253 C ATOM 907 C GLY A 113 2.520 -15.994 -9.378 1.00 50.84 C ANISOU 907 C GLY A 113 6972 6581 5764 1080 1156 293 C ATOM 908 O GLY A 113 3.500 -15.880 -10.113 1.00 52.47 O ANISOU 908 O GLY A 113 7024 6853 6061 1161 1349 350 O ATOM 909 N GLU A 114 1.414 -15.256 -9.504 1.00 50.72 N ANISOU 909 N GLU A 114 7097 6521 5652 917 1099 278 N ATOM 910 CA GLU A 114 1.239 -14.199 -10.527 1.00 53.37 C ANISOU 910 CA GLU A 114 7437 6874 5966 824 1248 336 C ATOM 911 C GLU A 114 1.866 -12.891 -10.120 1.00 55.06 C ANISOU 911 C GLU A 114 7379 7131 6409 680 1241 399 C ATOM 912 O GLU A 114 1.355 -12.236 -9.204 1.00 55.54 O ANISOU 912 O GLU A 114 7416 7167 6520 541 1053 360 O ATOM 913 CB GLU A 114 -0.245 -13.891 -10.698 1.00 50.96 C ANISOU 913 CB GLU A 114 7375 6504 5482 716 1156 294 C ATOM 914 CG GLU A 114 -0.954 -14.744 -11.664 1.00 53.60 C ANISOU 914 CG GLU A 114 7977 6795 5595 816 1215 234 C ATOM 915 CD GLU A 114 -0.398 -14.581 -13.082 1.00 58.02 C ANISOU 915 CD GLU A 114 8566 7411 6068 931 1462 293 C ATOM 916 OE1 GLU A 114 0.251 -15.541 -13.550 1.00 60.33 O ANISOU 916 OE1 GLU A 114 8891 7712 6321 1108 1579 266 O ATOM 917 OE2 GLU A 114 -0.570 -13.488 -13.683 1.00 57.91 O ANISOU 917 OE2 GLU A 114 8544 7429 6029 861 1553 377 O ATOM 918 N LYS A 115 2.896 -12.475 -10.843 1.00 58.09 N ANISOU 918 N LYS A 115 7571 7565 6934 709 1457 492 N ATOM 919 CA LYS A 115 3.636 -11.258 -10.535 1.00 60.39 C ANISOU 919 CA LYS A 115 7563 7871 7511 558 1477 552 C ATOM 920 C LYS A 115 2.996 -10.010 -11.173 1.00 59.83 C ANISOU 920 C LYS A 115 7577 7733 7422 410 1576 631 C ATOM 921 O LYS A 115 3.329 -9.639 -12.298 1.00 61.94 O ANISOU 921 O LYS A 115 7840 8006 7687 445 1847 759 O ATOM 922 CB LYS A 115 5.089 -11.427 -10.993 1.00 63.81 C ANISOU 922 CB LYS A 115 7711 8382 8154 656 1690 634 C ATOM 923 CG LYS A 115 6.148 -11.133 -9.925 1.00 68.09 C ANISOU 923 CG LYS A 115 7870 8975 9025 592 1540 594 C ATOM 924 CD LYS A 115 6.016 -12.056 -8.693 1.00 70.02 C ANISOU 924 CD LYS A 115 8155 9256 9195 686 1244 465 C ATOM 925 CE LYS A 115 7.263 -11.991 -7.798 1.00 74.81 C ANISOU 925 CE LYS A 115 8369 9957 10098 702 1104 423 C ATOM 926 NZ LYS A 115 7.742 -10.591 -7.501 1.00 77.71 N ANISOU 926 NZ LYS A 115 8435 10306 10785 472 1054 413 N ATOM 927 N LEU A 116 2.081 -9.375 -10.443 1.00 57.94 N ANISOU 927 N LEU A 116 7424 7430 7158 268 1369 567 N ATOM 928 CA LEU A 116 1.307 -8.217 -10.926 1.00 57.09 C ANISOU 928 CA LEU A 116 7431 7244 7016 146 1426 634 C ATOM 929 C LEU A 116 1.689 -6.920 -10.218 1.00 57.26 C ANISOU 929 C LEU A 116 7226 7193 7338 -49 1351 633 C ATOM 930 O LEU A 116 1.833 -6.905 -8.993 1.00 57.10 O ANISOU 930 O LEU A 116 7086 7178 7432 -110 1111 509 O ATOM 931 CB LEU A 116 -0.195 -8.457 -10.717 1.00 54.75 C ANISOU 931 CB LEU A 116 7429 6919 6455 145 1256 554 C ATOM 932 CG LEU A 116 -1.073 -9.085 -11.813 1.00 55.96 C ANISOU 932 CG LEU A 116 7872 7090 6302 268 1344 567 C ATOM 933 CD1 LEU A 116 -0.385 -10.149 -12.644 1.00 58.64 C ANISOU 933 CD1 LEU A 116 8241 7492 6549 449 1514 583 C ATOM 934 CD2 LEU A 116 -2.277 -9.675 -11.126 1.00 54.90 C ANISOU 934 CD2 LEU A 116 7914 6934 6011 256 1115 444 C ATOM 935 N THR A 117 1.826 -5.829 -10.978 1.00 57.57 N ANISOU 935 N THR A 117 7223 7153 7497 -136 1553 769 N ATOM 936 CA THR A 117 2.049 -4.507 -10.372 1.00 57.05 C ANISOU 936 CA THR A 117 6977 6967 7733 -340 1485 758 C ATOM 937 C THR A 117 0.800 -4.070 -9.607 1.00 54.39 C ANISOU 937 C THR A 117 6838 6566 7262 -407 1241 646 C ATOM 938 O THR A 117 -0.308 -4.545 -9.882 1.00 52.05 O ANISOU 938 O THR A 117 6817 6302 6657 -315 1203 638 O ATOM 939 CB THR A 117 2.388 -3.412 -11.413 1.00 59.34 C ANISOU 939 CB THR A 117 7209 7148 8190 -415 1793 961 C ATOM 940 OG1 THR A 117 1.258 -3.198 -12.265 1.00 56.35 O ANISOU 940 OG1 THR A 117 7157 6743 7510 -340 1888 1056 O ATOM 941 CG2 THR A 117 3.608 -3.802 -12.255 1.00 61.23 C ANISOU 941 CG2 THR A 117 7249 7456 8558 -333 2092 1103 C ATOM 942 N ASP A 118 0.991 -3.164 -8.653 1.00 54.50 N ANISOU 942 N ASP A 118 6700 6488 7519 -563 1076 549 N ATOM 943 CA ASP A 118 -0.114 -2.540 -7.945 1.00 52.89 C ANISOU 943 CA ASP A 118 6667 6207 7223 -624 881 452 C ATOM 944 C ASP A 118 -1.136 -1.930 -8.917 1.00 50.89 C ANISOU 944 C ASP A 118 6657 5873 6806 -608 1040 590 C ATOM 945 O ASP A 118 -2.337 -2.133 -8.738 1.00 48.99 O ANISOU 945 O ASP A 118 6644 5657 6313 -549 925 543 O ATOM 946 CB ASP A 118 0.407 -1.508 -6.919 1.00 55.22 C ANISOU 946 CB ASP A 118 6751 6390 7840 -792 709 321 C ATOM 947 CG ASP A 118 1.020 -2.177 -5.658 1.00 57.84 C ANISOU 947 CG ASP A 118 6921 6839 8218 -760 436 130 C ATOM 948 OD1 ASP A 118 1.055 -3.440 -5.563 1.00 55.16 O ANISOU 948 OD1 ASP A 118 6632 6651 7677 -607 402 123 O ATOM 949 OD2 ASP A 118 1.501 -1.430 -4.770 1.00 62.33 O ANISOU 949 OD2 ASP A 118 7312 7340 9031 -877 252 -17 O ATOM 950 N GLU A 119 -0.645 -1.272 -9.971 1.00 51.36 N ANISOU 950 N GLU A 119 6662 5851 7000 -641 1314 772 N ATOM 951 CA AGLU A 119 -1.496 -0.653 -10.992 0.50 50.55 C ANISOU 951 CA AGLU A 119 6790 5681 6735 -592 1485 934 C ATOM 952 CA BGLU A 119 -1.509 -0.654 -10.990 0.50 50.82 C ANISOU 952 CA BGLU A 119 6827 5715 6767 -592 1483 933 C ATOM 953 C GLU A 119 -2.336 -1.687 -11.744 1.00 48.23 C ANISOU 953 C GLU A 119 6752 5537 6037 -401 1506 960 C ATOM 954 O GLU A 119 -3.502 -1.442 -12.077 1.00 46.96 O ANISOU 954 O GLU A 119 6818 5368 5657 -342 1467 983 O ATOM 955 CB AGLU A 119 -0.650 0.152 -11.990 0.50 53.50 C ANISOU 955 CB AGLU A 119 7050 5947 7332 -638 1815 1157 C ATOM 956 CB BGLU A 119 -0.700 0.163 -12.005 0.50 53.94 C ANISOU 956 CB BGLU A 119 7117 6002 7377 -635 1814 1159 C ATOM 957 CG AGLU A 119 0.449 1.011 -11.356 0.50 56.35 C ANISOU 957 CG AGLU A 119 7085 6154 8170 -848 1822 1128 C ATOM 958 CG BGLU A 119 0.158 1.267 -11.417 0.50 58.08 C ANISOU 958 CG BGLU A 119 7369 6337 8364 -852 1824 1145 C ATOM 959 CD AGLU A 119 1.798 0.299 -11.271 0.50 57.05 C ANISOU 959 CD AGLU A 119 6871 6346 8458 -856 1884 1109 C ATOM 960 CD BGLU A 119 -0.623 2.231 -10.557 0.50 58.97 C ANISOU 960 CD BGLU A 119 7561 6290 8553 -963 1611 1022 C ATOM 961 OE1AGLU A 119 2.140 -0.201 -10.175 0.50 53.70 O ANISOU 961 OE1AGLU A 119 6294 5995 8113 -892 1616 901 O ATOM 962 OE1BGLU A 119 -1.873 2.194 -10.598 0.50 56.63 O ANISOU 962 OE1BGLU A 119 7536 6024 7955 -864 1516 1005 O ATOM 963 OE2AGLU A 119 2.514 0.250 -12.301 0.50 59.53 O ANISOU 963 OE2AGLU A 119 7101 6675 8840 -807 2207 1311 O ATOM 964 OE2BGLU A 119 0.023 3.029 -9.839 0.50 61.58 O ANISOU 964 OE2BGLU A 119 7674 6465 9259 -1147 1533 930 O ATOM 965 N GLU A 120 -1.735 -2.836 -12.028 1.00 47.16 N ANISOU 965 N GLU A 120 6570 5532 5818 -299 1561 945 N ATOM 966 CA GLU A 120 -2.444 -3.896 -12.738 1.00 44.64 C ANISOU 966 CA GLU A 120 6484 5335 5142 -124 1566 933 C ATOM 967 C GLU A 120 -3.564 -4.451 -11.845 1.00 41.45 C ANISOU 967 C GLU A 120 6207 4962 4581 -126 1279 760 C ATOM 968 O GLU A 120 -4.682 -4.728 -12.302 1.00 39.26 O ANISOU 968 O GLU A 120 6145 4721 4050 -47 1226 745 O ATOM 969 CB GLU A 120 -1.476 -4.991 -13.156 1.00 45.95 C ANISOU 969 CB GLU A 120 6567 5605 5286 -10 1691 939 C ATOM 970 CG GLU A 120 -0.562 -4.541 -14.315 1.00 49.44 C ANISOU 970 CG GLU A 120 6936 6042 5806 44 2036 1144 C ATOM 971 CD GLU A 120 0.667 -5.406 -14.455 1.00 54.76 C ANISOU 971 CD GLU A 120 7426 6803 6576 127 2169 1149 C ATOM 972 OE1 GLU A 120 1.354 -5.282 -15.490 1.00 58.66 O ANISOU 972 OE1 GLU A 120 7889 7324 7076 219 2478 1318 O ATOM 973 OE2 GLU A 120 0.956 -6.201 -13.535 1.00 54.68 O ANISOU 973 OE2 GLU A 120 7305 6837 6632 118 1978 999 O ATOM 974 N VAL A 121 -3.272 -4.602 -10.562 1.00 39.92 N ANISOU 974 N VAL A 121 5870 4758 4539 -210 1094 633 N ATOM 975 CA VAL A 121 -4.309 -5.045 -9.627 1.00 37.60 C ANISOU 975 CA VAL A 121 5688 4486 4113 -209 858 499 C ATOM 976 C VAL A 121 -5.459 -4.014 -9.505 1.00 36.89 C ANISOU 976 C VAL A 121 5719 4320 3976 -264 791 506 C ATOM 977 O VAL A 121 -6.651 -4.391 -9.538 1.00 35.01 O ANISOU 977 O VAL A 121 5646 4119 3537 -212 701 468 O ATOM 978 CB VAL A 121 -3.687 -5.500 -8.278 1.00 37.19 C ANISOU 978 CB VAL A 121 5478 4461 4190 -241 685 375 C ATOM 979 CG1 VAL A 121 -4.768 -5.866 -7.299 1.00 37.43 C ANISOU 979 CG1 VAL A 121 5635 4508 4079 -228 485 271 C ATOM 980 CG2 VAL A 121 -2.758 -6.728 -8.526 1.00 37.61 C ANISOU 980 CG2 VAL A 121 5455 4601 4234 -135 753 378 C ATOM 981 N ASP A 122 -5.121 -2.724 -9.410 1.00 38.40 N ANISOU 981 N ASP A 122 5822 4397 4372 -365 841 557 N ATOM 982 CA ASP A 122 -6.142 -1.669 -9.368 1.00 39.47 C ANISOU 982 CA ASP A 122 6077 4440 4479 -395 803 579 C ATOM 983 C ASP A 122 -7.023 -1.697 -10.631 1.00 38.77 C ANISOU 983 C ASP A 122 6188 4391 4152 -279 913 698 C ATOM 984 O ASP A 122 -8.231 -1.492 -10.547 1.00 37.53 O ANISOU 984 O ASP A 122 6164 4241 3856 -241 813 672 O ATOM 985 CB ASP A 122 -5.518 -0.259 -9.229 1.00 42.26 C ANISOU 985 CB ASP A 122 6310 4620 5126 -521 876 629 C ATOM 986 CG ASP A 122 -5.037 0.069 -7.790 1.00 46.38 C ANISOU 986 CG ASP A 122 6674 5086 5863 -635 679 453 C ATOM 987 OD1 ASP A 122 -5.311 -0.676 -6.809 1.00 49.26 O ANISOU 987 OD1 ASP A 122 7048 5549 6118 -598 485 308 O ATOM 988 OD2 ASP A 122 -4.369 1.118 -7.644 1.00 52.15 O ANISOU 988 OD2 ASP A 122 7273 5661 6881 -759 721 459 O ATOM 989 N GLU A 123 -6.405 -1.933 -11.787 1.00 39.31 N ANISOU 989 N GLU A 123 6270 4497 4170 -208 1116 825 N ATOM 990 CA AGLU A 123 -7.089 -2.090 -13.088 0.50 39.61 C ANISOU 990 CA AGLU A 123 6510 4605 3936 -58 1215 927 C ATOM 991 CA BGLU A 123 -7.181 -2.026 -13.010 0.50 39.53 C ANISOU 991 CA BGLU A 123 6502 4588 3929 -65 1198 920 C ATOM 992 C GLU A 123 -8.121 -3.219 -13.011 1.00 37.25 C ANISOU 992 C GLU A 123 6335 4426 3393 20 1031 787 C ATOM 993 O GLU A 123 -9.210 -3.115 -13.539 1.00 36.92 O ANISOU 993 O GLU A 123 6443 4424 3159 102 972 795 O ATOM 994 CB AGLU A 123 -6.078 -2.394 -14.239 0.50 42.10 C ANISOU 994 CB AGLU A 123 6816 4967 4212 35 1472 1063 C ATOM 995 CB BGLU A 123 -6.289 -2.007 -14.247 0.50 42.06 C ANISOU 995 CB BGLU A 123 6831 4930 4218 23 1471 1089 C ATOM 996 CG AGLU A 123 -5.490 -1.184 -15.021 0.50 46.45 C ANISOU 996 CG AGLU A 123 7348 5411 4891 31 1743 1293 C ATOM 997 CG BGLU A 123 -5.809 -0.629 -14.581 0.50 46.93 C ANISOU 997 CG BGLU A 123 7397 5398 5036 -36 1672 1278 C ATOM 998 CD AGLU A 123 -4.560 -1.547 -16.225 0.50 50.35 C ANISOU 998 CD AGLU A 123 7852 5975 5303 161 2037 1451 C ATOM 999 CD BGLU A 123 -6.951 0.298 -14.923 0.50 49.98 C ANISOU 999 CD BGLU A 123 7964 5724 5301 21 1643 1358 C ATOM 1000 OE1AGLU A 123 -3.970 -2.651 -16.288 0.50 50.25 O ANISOU 1000 OE1AGLU A 123 7786 6070 5238 217 2051 1372 O ATOM 1001 OE1BGLU A 123 -7.725 -0.020 -15.849 0.50 52.11 O ANISOU 1001 OE1BGLU A 123 8435 6108 5258 194 1645 1402 O ATOM 1002 OE2AGLU A 123 -4.402 -0.694 -17.133 0.50 55.86 O ANISOU 1002 OE2AGLU A 123 8622 6615 5988 224 2281 1672 O ATOM 1003 OE2BGLU A 123 -7.073 1.348 -14.269 0.50 50.68 O ANISOU 1003 OE2BGLU A 123 7996 5652 5607 -96 1606 1367 O ATOM 1004 N MET A 124 -7.736 -4.334 -12.381 1.00 34.45 N ANISOU 1004 N MET A 124 5905 4121 3062 1 946 664 N ATOM 1005 CA MET A 124 -8.636 -5.474 -12.247 1.00 32.97 C ANISOU 1005 CA MET A 124 5817 4010 2700 51 791 536 C ATOM 1006 C MET A 124 -9.828 -5.124 -11.343 1.00 32.13 C ANISOU 1006 C MET A 124 5728 3877 2601 -12 611 465 C ATOM 1007 O MET A 124 -10.974 -5.456 -11.656 1.00 32.14 O ANISOU 1007 O MET A 124 5834 3926 2451 35 518 419 O ATOM 1008 CB MET A 124 -7.891 -6.666 -11.651 1.00 32.69 C ANISOU 1008 CB MET A 124 5698 3999 2724 46 760 446 C ATOM 1009 CG MET A 124 -7.014 -7.447 -12.668 1.00 39.24 C ANISOU 1009 CG MET A 124 6553 4881 3474 160 919 477 C ATOM 1010 SD MET A 124 -5.835 -8.540 -11.782 1.00 47.33 S ANISOU 1010 SD MET A 124 7421 5911 4650 159 905 406 S ATOM 1011 CE MET A 124 -6.808 -9.945 -11.373 1.00 46.81 C ANISOU 1011 CE MET A 124 7488 5845 4452 193 736 262 C ATOM 1012 N ILE A 125 -9.558 -4.472 -10.213 1.00 30.80 N ANISOU 1012 N ILE A 125 5450 3641 2612 -109 559 445 N ATOM 1013 CA ILE A 125 -10.662 -4.026 -9.361 1.00 31.40 C ANISOU 1013 CA ILE A 125 5552 3695 2685 -142 421 388 C ATOM 1014 C ILE A 125 -11.587 -3.043 -10.148 1.00 32.32 C ANISOU 1014 C ILE A 125 5770 3791 2718 -92 448 472 C ATOM 1015 O ILE A 125 -12.805 -3.228 -10.144 1.00 31.66 O ANISOU 1015 O ILE A 125 5750 3757 2522 -52 348 432 O ATOM 1016 CB ILE A 125 -10.128 -3.381 -8.076 1.00 30.96 C ANISOU 1016 CB ILE A 125 5384 3568 2813 -229 361 337 C ATOM 1017 CG1 ILE A 125 -9.401 -4.423 -7.181 1.00 29.65 C ANISOU 1017 CG1 ILE A 125 5130 3448 2687 -239 293 251 C ATOM 1018 CG2 ILE A 125 -11.263 -2.600 -7.330 1.00 32.30 C ANISOU 1018 CG2 ILE A 125 5601 3699 2971 -236 260 297 C ATOM 1019 CD1 ILE A 125 -10.294 -5.523 -6.553 1.00 28.53 C ANISOU 1019 CD1 ILE A 125 5053 3368 2418 -198 192 184 C ATOM 1020 N ARG A 126 -11.007 -2.063 -10.848 1.00 34.94 N ANISOU 1020 N ARG A 126 6109 4052 3113 -85 591 597 N ATOM 1021 CA ARG A 126 -11.825 -1.115 -11.641 1.00 38.70 C ANISOU 1021 CA ARG A 126 6702 4504 3499 -5 631 705 C ATOM 1022 C ARG A 126 -12.711 -1.797 -12.673 1.00 39.17 C ANISOU 1022 C ARG A 126 6888 4696 3298 128 586 704 C ATOM 1023 O ARG A 126 -13.840 -1.375 -12.888 1.00 40.27 O ANISOU 1023 O ARG A 126 7098 4864 3340 199 503 715 O ATOM 1024 CB ARG A 126 -10.972 -0.048 -12.354 1.00 42.76 C ANISOU 1024 CB ARG A 126 7221 4905 4122 -4 837 878 C ATOM 1025 CG ARG A 126 -10.538 1.090 -11.419 1.00 47.55 C ANISOU 1025 CG ARG A 126 7728 5333 5007 -133 844 874 C ATOM 1026 CD ARG A 126 -9.767 2.207 -12.154 1.00 59.08 C ANISOU 1026 CD ARG A 126 9185 6638 6625 -152 1071 1065 C ATOM 1027 NE ARG A 126 -8.754 2.804 -11.261 1.00 65.76 N ANISOU 1027 NE ARG A 126 9856 7325 7806 -325 1083 1009 N ATOM 1028 CZ ARG A 126 -7.433 2.561 -11.310 1.00 69.00 C ANISOU 1028 CZ ARG A 126 10101 7716 8400 -414 1194 1029 C ATOM 1029 NH1 ARG A 126 -6.917 1.748 -12.225 1.00 68.78 N ANISOU 1029 NH1 ARG A 126 10075 7811 8246 -334 1336 1120 N ATOM 1030 NH2 ARG A 126 -6.609 3.155 -10.447 1.00 71.32 N ANISOU 1030 NH2 ARG A 126 10217 7867 9015 -576 1159 948 N ATOM 1031 N GLU A 127 -12.189 -2.810 -13.349 1.00 40.83 N ANISOU 1031 N GLU A 127 7126 4988 3398 176 634 683 N ATOM 1032 CA GLU A 127 -12.964 -3.541 -14.358 1.00 42.45 C ANISOU 1032 CA GLU A 127 7459 5319 3353 306 564 639 C ATOM 1033 C GLU A 127 -14.213 -4.202 -13.738 1.00 40.07 C ANISOU 1033 C GLU A 127 7131 5066 3026 270 346 485 C ATOM 1034 O GLU A 127 -15.291 -4.195 -14.338 1.00 40.28 O ANISOU 1034 O GLU A 127 7226 5170 2907 357 236 457 O ATOM 1035 CB GLU A 127 -12.063 -4.598 -15.006 1.00 45.06 C ANISOU 1035 CB GLU A 127 7820 5705 3596 358 654 607 C ATOM 1036 CG GLU A 127 -12.687 -5.451 -16.116 1.00 51.20 C ANISOU 1036 CG GLU A 127 8747 6603 4105 502 576 523 C ATOM 1037 CD GLU A 127 -13.201 -4.655 -17.333 1.00 60.89 C ANISOU 1037 CD GLU A 127 10129 7901 5105 676 612 638 C ATOM 1038 OE1 GLU A 127 -12.671 -3.551 -17.653 1.00 63.96 O ANISOU 1038 OE1 GLU A 127 10540 8236 5526 715 797 836 O ATOM 1039 OE2 GLU A 127 -14.150 -5.167 -17.981 1.00 64.77 O ANISOU 1039 OE2 GLU A 127 10720 8500 5391 780 446 526 O ATOM 1040 N ALA A 128 -14.090 -4.745 -12.527 1.00 35.72 N ANISOU 1040 N ALA A 128 6473 4474 2626 151 287 394 N ATOM 1041 CA ALA A 128 -15.229 -5.420 -11.959 1.00 33.50 C ANISOU 1041 CA ALA A 128 6159 4228 2343 115 128 278 C ATOM 1042 C ALA A 128 -16.103 -4.466 -11.128 1.00 31.52 C ANISOU 1042 C ALA A 128 5854 3948 2174 88 70 302 C ATOM 1043 O ALA A 128 -17.260 -4.787 -10.829 1.00 31.24 O ANISOU 1043 O ALA A 128 5781 3956 2132 82 -43 236 O ATOM 1044 CB ALA A 128 -14.749 -6.625 -11.103 1.00 33.44 C ANISOU 1044 CB ALA A 128 6088 4192 2426 34 112 188 C ATOM 1045 N ASP A 129 -15.550 -3.318 -10.713 1.00 30.01 N ANISOU 1045 N ASP A 129 5647 3672 2082 67 152 385 N ATOM 1046 CA ASP A 129 -16.294 -2.420 -9.804 1.00 28.91 C ANISOU 1046 CA ASP A 129 5471 3487 2025 54 104 386 C ATOM 1047 C ASP A 129 -17.382 -1.732 -10.647 1.00 30.05 C ANISOU 1047 C ASP A 129 5677 3675 2064 168 65 446 C ATOM 1048 O ASP A 129 -17.083 -1.121 -11.660 1.00 33.83 O ANISOU 1048 O ASP A 129 6242 4142 2470 248 141 552 O ATOM 1049 CB ASP A 129 -15.314 -1.429 -9.187 1.00 28.73 C ANISOU 1049 CB ASP A 129 5424 3338 2154 -3 186 427 C ATOM 1050 CG ASP A 129 -15.963 -0.426 -8.222 1.00 28.35 C ANISOU 1050 CG ASP A 129 5365 3220 2188 -1 142 405 C ATOM 1051 OD1 ASP A 129 -15.345 0.624 -8.001 1.00 30.09 O ANISOU 1051 OD1 ASP A 129 5590 3312 2532 -31 200 438 O ATOM 1052 OD2 ASP A 129 -17.041 -0.683 -7.653 1.00 27.02 O ANISOU 1052 OD2 ASP A 129 5176 3112 1979 28 60 350 O ATOM 1053 N ILE A 130 -18.634 -1.913 -10.293 1.00 29.05 N ANISOU 1053 N ILE A 130 5502 3613 1923 191 -45 389 N ATOM 1054 CA ILE A 130 -19.742 -1.289 -11.035 1.00 30.66 C ANISOU 1054 CA ILE A 130 5736 3881 2034 319 -111 435 C ATOM 1055 C ILE A 130 -20.167 0.007 -10.328 1.00 30.47 C ANISOU 1055 C ILE A 130 5704 3770 2102 359 -82 492 C ATOM 1056 O ILE A 130 -20.317 1.055 -10.977 1.00 31.81 O ANISOU 1056 O ILE A 130 5955 3900 2231 471 -44 602 O ATOM 1057 CB ILE A 130 -20.947 -2.238 -11.116 1.00 30.66 C ANISOU 1057 CB ILE A 130 5648 4006 1998 324 -260 330 C ATOM 1058 CG1 ILE A 130 -20.550 -3.503 -11.917 1.00 34.61 C ANISOU 1058 CG1 ILE A 130 6180 4565 2405 296 -303 249 C ATOM 1059 CG2 ILE A 130 -22.178 -1.515 -11.731 1.00 31.24 C ANISOU 1059 CG2 ILE A 130 5711 4163 1998 470 -358 368 C ATOM 1060 CD1 ILE A 130 -21.595 -4.664 -11.843 1.00 36.50 C ANISOU 1060 CD1 ILE A 130 6308 4881 2680 243 -451 109 C ATOM 1061 N ASP A 131 -20.304 -0.053 -9.007 1.00 30.02 N ANISOU 1061 N ASP A 131 5573 3675 2160 286 -86 422 N ATOM 1062 CA ASP A 131 -20.834 1.103 -8.272 1.00 31.43 C ANISOU 1062 CA ASP A 131 5753 3777 2413 346 -69 443 C ATOM 1063 C ASP A 131 -19.814 2.211 -8.031 1.00 31.04 C ANISOU 1063 C ASP A 131 5784 3550 2461 320 27 489 C ATOM 1064 O ASP A 131 -20.193 3.330 -7.713 1.00 32.44 O ANISOU 1064 O ASP A 131 6000 3629 2697 391 48 515 O ATOM 1065 CB ASP A 131 -21.595 0.709 -6.977 1.00 32.04 C ANISOU 1065 CB ASP A 131 5733 3900 2543 324 -103 356 C ATOM 1066 CG ASP A 131 -20.745 -0.060 -5.981 1.00 32.59 C ANISOU 1066 CG ASP A 131 5781 3944 2655 208 -78 282 C ATOM 1067 OD1 ASP A 131 -19.477 0.018 -5.991 1.00 31.20 O ANISOU 1067 OD1 ASP A 131 5652 3689 2514 141 -40 279 O ATOM 1068 OD2 ASP A 131 -21.369 -0.778 -5.163 1.00 34.10 O ANISOU 1068 OD2 ASP A 131 5898 4203 2854 194 -92 236 O ATOM 1069 N GLY A 132 -18.531 1.916 -8.207 1.00 29.78 N ANISOU 1069 N GLY A 132 5636 3336 2341 222 87 494 N ATOM 1070 CA GLY A 132 -17.537 2.981 -8.095 1.00 30.34 C ANISOU 1070 CA GLY A 132 5751 3225 2554 176 179 538 C ATOM 1071 C GLY A 132 -17.004 3.219 -6.689 1.00 29.47 C ANISOU 1071 C GLY A 132 5595 3022 2580 87 148 411 C ATOM 1072 O GLY A 132 -16.361 4.226 -6.449 1.00 30.41 O ANISOU 1072 O GLY A 132 5737 2967 2850 45 193 411 O ATOM 1073 N ASP A 133 -17.299 2.310 -5.765 1.00 28.85 N ANISOU 1073 N ASP A 133 5460 3053 2449 68 69 303 N ATOM 1074 CA ASP A 133 -16.754 2.400 -4.366 1.00 30.59 C ANISOU 1074 CA ASP A 133 5654 3223 2745 16 19 171 C ATOM 1075 C ASP A 133 -15.294 1.946 -4.236 1.00 30.51 C ANISOU 1075 C ASP A 133 5584 3188 2820 -97 18 131 C ATOM 1076 O ASP A 133 -14.696 2.048 -3.150 1.00 32.58 O ANISOU 1076 O ASP A 133 5820 3417 3145 -133 -50 12 O ATOM 1077 CB ASP A 133 -17.656 1.685 -3.345 1.00 29.25 C ANISOU 1077 CB ASP A 133 5463 3177 2472 72 -37 100 C ATOM 1078 CG ASP A 133 -17.581 0.172 -3.418 1.00 30.70 C ANISOU 1078 CG ASP A 133 5591 3495 2579 32 -48 106 C ATOM 1079 OD1 ASP A 133 -18.101 -0.478 -2.495 1.00 30.72 O ANISOU 1079 OD1 ASP A 133 5574 3575 2524 62 -66 66 O ATOM 1080 OD2 ASP A 133 -17.034 -0.415 -4.368 1.00 26.20 O ANISOU 1080 OD2 ASP A 133 5004 2947 2003 -18 -25 156 O ATOM 1081 N GLY A 134 -14.726 1.431 -5.324 1.00 29.67 N ANISOU 1081 N GLY A 134 5456 3113 2705 -134 86 222 N ATOM 1082 CA GLY A 134 -13.325 1.001 -5.331 1.00 29.85 C ANISOU 1082 CA GLY A 134 5398 3120 2823 -226 108 203 C ATOM 1083 C GLY A 134 -13.093 -0.419 -4.809 1.00 29.39 C ANISOU 1083 C GLY A 134 5292 3196 2680 -229 48 140 C ATOM 1084 O GLY A 134 -11.944 -0.815 -4.578 1.00 30.30 O ANISOU 1084 O GLY A 134 5326 3312 2873 -282 42 105 O ATOM 1085 N GLN A 135 -14.166 -1.190 -4.588 1.00 27.59 N ANISOU 1085 N GLN A 135 5100 3070 2312 -169 10 130 N ATOM 1086 CA GLN A 135 -14.058 -2.565 -4.149 1.00 27.39 C ANISOU 1086 CA GLN A 135 5048 3140 2218 -167 -21 96 C ATOM 1087 C GLN A 135 -15.007 -3.398 -4.971 1.00 27.08 C ANISOU 1087 C GLN A 135 5038 3173 2078 -139 -3 142 C ATOM 1088 O GLN A 135 -15.865 -2.839 -5.674 1.00 27.16 O ANISOU 1088 O GLN A 135 5082 3187 2053 -104 6 185 O ATOM 1089 CB GLN A 135 -14.476 -2.668 -2.658 1.00 28.06 C ANISOU 1089 CB GLN A 135 5142 3255 2266 -126 -91 20 C ATOM 1090 CG GLN A 135 -13.694 -1.765 -1.750 1.00 30.62 C ANISOU 1090 CG GLN A 135 5451 3512 2670 -135 -155 -71 C ATOM 1091 CD GLN A 135 -13.713 -2.244 -0.291 1.00 33.08 C ANISOU 1091 CD GLN A 135 5783 3892 2895 -65 -232 -151 C ATOM 1092 OE1 GLN A 135 -12.840 -2.980 0.117 1.00 35.92 O ANISOU 1092 OE1 GLN A 135 6104 4296 3248 -62 -275 -176 O ATOM 1093 NE2 GLN A 135 -14.710 -1.841 0.459 1.00 30.33 N ANISOU 1093 NE2 GLN A 135 5499 3558 2466 13 -238 -177 N ATOM 1094 N VAL A 136 -14.846 -4.717 -4.907 1.00 26.99 N ANISOU 1094 N VAL A 136 5014 3213 2030 -148 -7 125 N ATOM 1095 CA VAL A 136 -15.758 -5.657 -5.582 1.00 26.70 C ANISOU 1095 CA VAL A 136 4993 3225 1928 -140 -14 131 C ATOM 1096 C VAL A 136 -16.663 -6.428 -4.600 1.00 27.16 C ANISOU 1096 C VAL A 136 5028 3308 1985 -141 -35 111 C ATOM 1097 O VAL A 136 -16.164 -7.263 -3.791 1.00 27.39 O ANISOU 1097 O VAL A 136 5054 3329 2025 -143 -22 104 O ATOM 1098 CB VAL A 136 -14.968 -6.615 -6.462 1.00 26.98 C ANISOU 1098 CB VAL A 136 5046 3266 1939 -147 18 126 C ATOM 1099 CG1 VAL A 136 -15.939 -7.565 -7.255 1.00 26.81 C ANISOU 1099 CG1 VAL A 136 5050 3277 1858 -144 -19 91 C ATOM 1100 CG2 VAL A 136 -14.176 -5.791 -7.499 1.00 26.48 C ANISOU 1100 CG2 VAL A 136 5006 3187 1870 -130 82 177 C ATOM 1101 N ASN A 137 -17.972 -6.114 -4.632 1.00 27.57 N ANISOU 1101 N ASN A 137 5056 3390 2032 -126 -53 119 N ATOM 1102 CA ASN A 137 -18.970 -6.823 -3.787 1.00 27.64 C ANISOU 1102 CA ASN A 137 5015 3420 2068 -132 -37 126 C ATOM 1103 C ASN A 137 -19.457 -8.110 -4.489 1.00 28.03 C ANISOU 1103 C ASN A 137 5031 3464 2156 -191 -54 103 C ATOM 1104 O ASN A 137 -19.034 -8.427 -5.628 1.00 26.75 O ANISOU 1104 O ASN A 137 4903 3297 1964 -206 -91 65 O ATOM 1105 CB ASN A 137 -20.134 -5.911 -3.334 1.00 27.94 C ANISOU 1105 CB ASN A 137 5011 3493 2113 -80 -33 145 C ATOM 1106 CG ASN A 137 -21.132 -5.561 -4.475 1.00 31.09 C ANISOU 1106 CG ASN A 137 5358 3934 2519 -70 -90 142 C ATOM 1107 OD1 ASN A 137 -21.199 -6.231 -5.517 1.00 27.74 O ANISOU 1107 OD1 ASN A 137 4924 3524 2091 -109 -142 112 O ATOM 1108 ND2 ASN A 137 -21.928 -4.512 -4.249 1.00 29.55 N ANISOU 1108 ND2 ASN A 137 5137 3766 2326 3 -89 164 N ATOM 1109 N TYR A 138 -20.282 -8.896 -3.813 1.00 27.42 N ANISOU 1109 N TYR A 138 4892 3376 2149 -222 -15 122 N ATOM 1110 CA TYR A 138 -20.665 -10.169 -4.403 1.00 28.71 C ANISOU 1110 CA TYR A 138 5021 3494 2393 -300 -34 82 C ATOM 1111 C TYR A 138 -21.412 -10.034 -5.755 1.00 29.70 C ANISOU 1111 C TYR A 138 5099 3662 2522 -322 -148 3 C ATOM 1112 O TYR A 138 -21.164 -10.795 -6.689 1.00 29.81 O ANISOU 1112 O TYR A 138 5150 3645 2530 -354 -208 -77 O ATOM 1113 CB TYR A 138 -21.457 -11.026 -3.387 1.00 28.31 C ANISOU 1113 CB TYR A 138 4898 3397 2461 -343 57 140 C ATOM 1114 CG TYR A 138 -21.933 -12.296 -4.009 1.00 31.27 C ANISOU 1114 CG TYR A 138 5222 3687 2970 -448 32 84 C ATOM 1115 CD1 TYR A 138 -23.276 -12.469 -4.340 1.00 34.74 C ANISOU 1115 CD1 TYR A 138 5511 4137 3550 -522 -9 48 C ATOM 1116 CD2 TYR A 138 -21.022 -13.331 -4.328 1.00 30.78 C ANISOU 1116 CD2 TYR A 138 5254 3527 2914 -470 35 46 C ATOM 1117 CE1 TYR A 138 -23.723 -13.656 -4.920 1.00 38.81 C ANISOU 1117 CE1 TYR A 138 5967 4551 4226 -639 -55 -36 C ATOM 1118 CE2 TYR A 138 -21.463 -14.497 -4.908 1.00 34.40 C ANISOU 1118 CE2 TYR A 138 5681 3878 3512 -567 4 -31 C ATOM 1119 CZ TYR A 138 -22.816 -14.651 -5.205 1.00 38.81 C ANISOU 1119 CZ TYR A 138 6087 4434 4224 -662 -50 -82 C ATOM 1120 OH TYR A 138 -23.261 -15.796 -5.835 1.00 38.74 O ANISOU 1120 OH TYR A 138 6035 4301 4383 -776 -111 -195 O ATOM 1121 N GLU A 139 -22.362 -9.106 -5.832 1.00 29.93 N ANISOU 1121 N GLU A 139 5053 3767 2552 -284 -186 17 N ATOM 1122 CA AGLU A 139 -23.152 -8.897 -7.015 0.50 30.36 C ANISOU 1122 CA AGLU A 139 5054 3888 2593 -271 -315 -51 C ATOM 1123 CA BGLU A 139 -23.138 -8.970 -7.052 0.50 30.70 C ANISOU 1123 CA BGLU A 139 5098 3928 2638 -276 -318 -56 C ATOM 1124 C GLU A 139 -22.235 -8.534 -8.198 1.00 30.81 C ANISOU 1124 C GLU A 139 5249 3966 2492 -207 -369 -81 C ATOM 1125 O GLU A 139 -22.428 -8.984 -9.311 1.00 31.11 O ANISOU 1125 O GLU A 139 5306 4034 2481 -200 -475 -170 O ATOM 1126 CB AGLU A 139 -24.165 -7.782 -6.723 0.50 31.22 C ANISOU 1126 CB AGLU A 139 5069 4077 2717 -201 -324 -1 C ATOM 1127 CB BGLU A 139 -24.356 -8.044 -6.898 0.50 32.06 C ANISOU 1127 CB BGLU A 139 5149 4186 2846 -221 -349 -23 C ATOM 1128 CG AGLU A 139 -25.229 -8.129 -5.667 0.50 30.20 C ANISOU 1128 CG AGLU A 139 4780 3950 2746 -245 -249 39 C ATOM 1129 CG BGLU A 139 -25.151 -7.841 -8.218 0.50 33.24 C ANISOU 1129 CG BGLU A 139 5243 4428 2959 -178 -521 -102 C ATOM 1130 CD AGLU A 139 -24.672 -8.432 -4.246 0.50 32.88 C ANISOU 1130 CD AGLU A 139 5172 4222 3099 -256 -85 121 C ATOM 1131 CD BGLU A 139 -25.599 -9.153 -8.866 0.50 35.60 C ANISOU 1131 CD BGLU A 139 5464 4707 3354 -281 -635 -235 C ATOM 1132 OE1AGLU A 139 -23.747 -7.745 -3.682 0.50 24.00 O ANISOU 1132 OE1AGLU A 139 4174 3084 1860 -186 -34 157 O ATOM 1133 OE1BGLU A 139 -25.398 -9.327 -10.095 0.50 32.14 O ANISOU 1133 OE1BGLU A 139 5105 4309 2799 -241 -770 -334 O ATOM 1134 OE2AGLU A 139 -25.202 -9.406 -3.672 0.50 36.66 O ANISOU 1134 OE2AGLU A 139 5559 4657 3715 -332 -9 148 O ATOM 1135 OE2BGLU A 139 -26.141 -10.015 -8.134 0.50 36.31 O ANISOU 1135 OE2BGLU A 139 5425 4732 3638 -398 -582 -242 O ATOM 1136 N GLU A 140 -21.221 -7.704 -7.918 1.00 29.89 N ANISOU 1136 N GLU A 140 5225 3830 2301 -156 -288 -8 N ATOM 1137 CA GLU A 140 -20.248 -7.289 -8.957 1.00 30.03 C ANISOU 1137 CA GLU A 140 5363 3857 2192 -94 -284 2 C ATOM 1138 C GLU A 140 -19.377 -8.457 -9.464 1.00 30.43 C ANISOU 1138 C GLU A 140 5479 3868 2214 -124 -271 -60 C ATOM 1139 O GLU A 140 -19.091 -8.605 -10.668 1.00 30.09 O ANISOU 1139 O GLU A 140 5519 3860 2054 -66 -305 -100 O ATOM 1140 CB GLU A 140 -19.390 -6.143 -8.429 1.00 27.84 C ANISOU 1140 CB GLU A 140 5130 3539 1908 -62 -192 91 C ATOM 1141 CG GLU A 140 -20.196 -4.844 -8.279 1.00 26.32 C ANISOU 1141 CG GLU A 140 4915 3368 1717 4 -207 145 C ATOM 1142 CD GLU A 140 -19.449 -3.763 -7.491 1.00 30.12 C ANISOU 1142 CD GLU A 140 5431 3772 2241 13 -127 199 C ATOM 1143 OE1 GLU A 140 -18.540 -4.079 -6.685 1.00 27.76 O ANISOU 1143 OE1 GLU A 140 5133 3426 1990 -42 -83 181 O ATOM 1144 OE2 GLU A 140 -19.747 -2.572 -7.688 1.00 28.96 O ANISOU 1144 OE2 GLU A 140 5313 3604 2087 81 -119 251 O ATOM 1145 N PHE A 141 -18.974 -9.284 -8.526 1.00 29.31 N ANISOU 1145 N PHE A 141 5314 3657 2166 -191 -215 -64 N ATOM 1146 CA PHE A 141 -18.289 -10.535 -8.812 1.00 29.62 C ANISOU 1146 CA PHE A 141 5405 3636 2212 -214 -198 -125 C ATOM 1147 C PHE A 141 -19.152 -11.466 -9.639 1.00 31.15 C ANISOU 1147 C PHE A 141 5592 3822 2421 -246 -305 -249 C ATOM 1148 O PHE A 141 -18.701 -11.959 -10.696 1.00 33.78 O ANISOU 1148 O PHE A 141 6018 4156 2659 -200 -338 -332 O ATOM 1149 CB PHE A 141 -17.809 -11.148 -7.481 1.00 29.47 C ANISOU 1149 CB PHE A 141 5362 3542 2292 -255 -117 -79 C ATOM 1150 CG PHE A 141 -16.914 -12.338 -7.658 1.00 30.45 C ANISOU 1150 CG PHE A 141 5550 3592 2429 -250 -79 -117 C ATOM 1151 CD1 PHE A 141 -17.447 -13.597 -7.601 1.00 26.88 C ANISOU 1151 CD1 PHE A 141 5095 3047 2073 -308 -94 -176 C ATOM 1152 CD2 PHE A 141 -15.540 -12.182 -7.854 1.00 30.30 C ANISOU 1152 CD2 PHE A 141 5579 3581 2352 -187 -18 -90 C ATOM 1153 CE1 PHE A 141 -16.637 -14.751 -7.752 1.00 31.45 C ANISOU 1153 CE1 PHE A 141 5747 3527 2674 -288 -52 -214 C ATOM 1154 CE2 PHE A 141 -14.701 -13.296 -7.975 1.00 32.64 C ANISOU 1154 CE2 PHE A 141 5927 3810 2665 -158 26 -120 C ATOM 1155 CZ PHE A 141 -15.234 -14.592 -7.912 1.00 30.96 C ANISOU 1155 CZ PHE A 141 5740 3492 2531 -199 9 -182 C ATOM 1156 N VAL A 142 -20.427 -11.634 -9.281 1.00 31.29 N ANISOU 1156 N VAL A 142 5494 3841 2554 -314 -370 -277 N ATOM 1157 CA VAL A 142 -21.336 -12.429 -10.106 1.00 34.37 C ANISOU 1157 CA VAL A 142 5841 4223 2993 -361 -509 -423 C ATOM 1158 C VAL A 142 -21.350 -11.887 -11.566 1.00 36.63 C ANISOU 1158 C VAL A 142 6214 4625 3080 -247 -631 -499 C ATOM 1159 O VAL A 142 -21.205 -12.660 -12.544 1.00 38.30 O ANISOU 1159 O VAL A 142 6509 4823 3220 -223 -719 -641 O ATOM 1160 CB VAL A 142 -22.804 -12.392 -9.582 1.00 35.25 C ANISOU 1160 CB VAL A 142 5765 4352 3277 -443 -563 -426 C ATOM 1161 CG1 VAL A 142 -23.773 -12.984 -10.613 1.00 38.63 C ANISOU 1161 CG1 VAL A 142 6120 4801 3759 -485 -759 -606 C ATOM 1162 CG2 VAL A 142 -22.973 -13.151 -8.231 1.00 35.58 C ANISOU 1162 CG2 VAL A 142 5727 4272 3520 -549 -427 -349 C ATOM 1163 N GLN A 143 -21.532 -10.574 -11.699 1.00 37.30 N ANISOU 1163 N GLN A 143 6294 4813 3064 -158 -630 -403 N ATOM 1164 CA GLN A 143 -21.614 -9.921 -13.022 1.00 40.93 C ANISOU 1164 CA GLN A 143 6847 5390 3313 -17 -725 -428 C ATOM 1165 C GLN A 143 -20.371 -10.188 -13.826 1.00 41.20 C ANISOU 1165 C GLN A 143 7058 5415 3181 66 -652 -437 C ATOM 1166 O GLN A 143 -20.446 -10.499 -15.012 1.00 43.99 O ANISOU 1166 O GLN A 143 7512 5833 3368 162 -754 -543 O ATOM 1167 CB GLN A 143 -21.857 -8.422 -12.906 1.00 41.39 C ANISOU 1167 CB GLN A 143 6893 5521 3313 73 -690 -283 C ATOM 1168 CG GLN A 143 -23.267 -8.079 -12.470 1.00 47.18 C ANISOU 1168 CG GLN A 143 7456 6308 4164 51 -790 -293 C ATOM 1169 CD GLN A 143 -24.270 -8.582 -13.470 1.00 56.19 C ANISOU 1169 CD GLN A 143 8539 7543 5266 83 -1012 -448 C ATOM 1170 OE1 GLN A 143 -24.958 -9.584 -13.234 1.00 59.77 O ANISOU 1170 OE1 GLN A 143 8858 7960 5892 -41 -1102 -575 O ATOM 1171 NE2 GLN A 143 -24.329 -7.927 -14.617 1.00 58.42 N ANISOU 1171 NE2 GLN A 143 8929 7942 5327 254 -1104 -443 N ATOM 1172 N MET A 144 -19.228 -10.091 -13.179 1.00 40.75 N ANISOU 1172 N MET A 144 7034 5285 3164 41 -480 -333 N ATOM 1173 CA MET A 144 -17.979 -10.385 -13.820 1.00 43.60 C ANISOU 1173 CA MET A 144 7527 5634 3407 116 -377 -326 C ATOM 1174 C MET A 144 -17.921 -11.839 -14.367 1.00 46.10 C ANISOU 1174 C MET A 144 7908 5902 3706 110 -447 -504 C ATOM 1175 O MET A 144 -17.470 -12.062 -15.510 1.00 47.51 O ANISOU 1175 O MET A 144 8228 6131 3694 235 -449 -566 O ATOM 1176 CB MET A 144 -16.799 -10.079 -12.904 1.00 42.26 C ANISOU 1176 CB MET A 144 7329 5395 3332 76 -204 -199 C ATOM 1177 CG MET A 144 -15.506 -10.440 -13.588 1.00 46.40 C ANISOU 1177 CG MET A 144 7954 5915 3762 158 -85 -188 C ATOM 1178 SD MET A 144 -14.057 -10.387 -12.588 1.00 48.58 S ANISOU 1178 SD MET A 144 8160 6119 4177 113 79 -85 S ATOM 1179 CE MET A 144 -14.414 -11.653 -11.350 1.00 45.10 C ANISOU 1179 CE MET A 144 7653 5581 3902 6 14 -167 C ATOM 1180 N MET A 145 -18.404 -12.796 -13.574 1.00 46.89 N ANISOU 1180 N MET A 145 7920 5898 4000 -23 -494 -583 N ATOM 1181 CA MET A 145 -18.414 -14.223 -13.931 1.00 50.62 C ANISOU 1181 CA MET A 145 8446 6270 4519 -55 -557 -758 C ATOM 1182 C MET A 145 -19.450 -14.651 -14.946 1.00 54.19 C ANISOU 1182 C MET A 145 8914 6761 4913 -41 -774 -963 C ATOM 1183 O MET A 145 -19.194 -15.571 -15.707 1.00 56.82 O ANISOU 1183 O MET A 145 9364 7045 5180 4 -831 -1131 O ATOM 1184 CB MET A 145 -18.699 -15.065 -12.676 1.00 49.75 C ANISOU 1184 CB MET A 145 8226 6006 4669 -210 -518 -746 C ATOM 1185 CG MET A 145 -17.764 -14.787 -11.565 1.00 50.02 C ANISOU 1185 CG MET A 145 8241 6007 4759 -214 -346 -574 C ATOM 1186 SD MET A 145 -16.148 -15.205 -12.150 1.00 54.95 S ANISOU 1186 SD MET A 145 9009 6611 5256 -88 -229 -576 S ATOM 1187 CE MET A 145 -16.101 -16.870 -11.415 1.00 54.55 C ANISOU 1187 CE MET A 145 8967 6350 5408 -167 -203 -642 C ATOM 1188 N THR A 146 -20.641 -14.064 -14.922 1.00 56.52 N ANISOU 1188 N THR A 146 9084 7140 5252 -78 -908 -972 N ATOM 1189 CA THR A 146 -21.733 -14.580 -15.762 1.00 62.35 C ANISOU 1189 CA THR A 146 9787 7912 5989 -89 -1156 -1196 C ATOM 1190 C THR A 146 -22.013 -13.695 -16.964 1.00 65.20 C ANISOU 1190 C THR A 146 10237 8474 6062 102 -1288 -1222 C ATOM 1191 O THR A 146 -22.734 -14.083 -17.881 1.00 68.20 O ANISOU 1191 O THR A 146 10631 8919 6361 149 -1522 -1432 O ATOM 1192 CB THR A 146 -23.049 -14.731 -14.977 1.00 62.66 C ANISOU 1192 CB THR A 146 9583 7911 6314 -261 -1250 -1220 C ATOM 1193 OG1 THR A 146 -23.403 -13.469 -14.391 1.00 61.34 O ANISOU 1193 OG1 THR A 146 9314 7851 6142 -232 -1184 -1027 O ATOM 1194 CG2 THR A 146 -22.934 -15.828 -13.902 1.00 62.49 C ANISOU 1194 CG2 THR A 146 9489 7673 6583 -442 -1130 -1210 C ATOM 1195 N ALA A 147 -21.474 -12.485 -16.929 1.00 66.11 N ANISOU 1195 N ALA A 147 10408 8680 6029 214 -1145 -1008 N ATOM 1196 CA ALA A 147 -21.688 -11.533 -18.001 1.00 69.58 C ANISOU 1196 CA ALA A 147 10950 9298 6190 417 -1225 -973 C ATOM 1197 C ALA A 147 -20.455 -11.513 -18.909 1.00 71.60 C ANISOU 1197 C ALA A 147 11445 9587 6172 592 -1088 -932 C ATOM 1198 O ALA A 147 -19.328 -11.259 -18.454 1.00 70.51 O ANISOU 1198 O ALA A 147 11346 9381 6064 580 -846 -769 O ATOM 1199 CB ALA A 147 -22.025 -10.136 -17.440 1.00 68.07 C ANISOU 1199 CB ALA A 147 10667 9164 6034 438 -1150 -753 C ATOM 1200 N LYS A 148 -20.696 -11.862 -20.173 1.00 75.66 N ANISOU 1200 N LYS A 148 12106 10210 6433 756 -1252 -1102 N ATOM 1201 CA LYS A 148 -19.736 -11.755 -21.286 1.00 78.25 C ANISOU 1201 CA LYS A 148 12685 10620 6426 988 -1137 -1068 C ATOM 1202 C LYS A 148 -20.513 -11.900 -22.590 1.00 81.85 C ANISOU 1202 C LYS A 148 13271 11245 6585 1188 -1407 -1267 C ATOM 1203 O LYS A 148 -21.463 -12.688 -22.671 1.00 83.60 O ANISOU 1203 O LYS A 148 13404 11455 6906 1104 -1686 -1531 O ATOM 1204 CB LYS A 148 -18.649 -12.845 -21.198 1.00 78.60 C ANISOU 1204 CB LYS A 148 12817 10534 6514 951 -993 -1149 C TER 1205 LYS A 148 ATOM 1206 N GLY B 784 -9.627 -1.496 -15.768 1.00 99.65 N ANISOU 1206 N GLY B 784 19282 6288 12291 412 2120 1749 N ATOM 1207 CA GLY B 784 -9.821 -2.111 -17.114 1.00100.61 C ANISOU 1207 CA GLY B 784 19898 6737 11593 709 2005 2370 C ATOM 1208 C GLY B 784 -8.899 -3.276 -17.467 1.00 95.55 C ANISOU 1208 C GLY B 784 18854 6870 10580 185 2438 2292 C ATOM 1209 O GLY B 784 -8.122 -3.174 -18.422 1.00102.00 O ANISOU 1209 O GLY B 784 20326 7408 11021 -183 3148 2754 O ATOM 1210 N ARG B 785 -8.979 -4.368 -16.695 1.00 85.51 N ANISOU 1210 N ARG B 785 16576 6472 9443 172 2134 1729 N ATOM 1211 CA ARG B 785 -8.358 -5.665 -17.038 1.00 80.24 C ANISOU 1211 CA ARG B 785 15489 6540 8459 -71 2387 1629 C ATOM 1212 C ARG B 785 -9.227 -6.838 -16.563 1.00 71.15 C ANISOU 1212 C ARG B 785 13696 6179 7158 336 1692 1247 C ATOM 1213 O ARG B 785 -9.396 -7.071 -15.345 1.00 64.87 O ANISOU 1213 O ARG B 785 12173 5661 6812 291 1448 779 O ATOM 1214 CB ARG B 785 -6.918 -5.788 -16.501 1.00 80.55 C ANISOU 1214 CB ARG B 785 14806 6625 9176 -839 3033 1374 C ATOM 1215 CG ARG B 785 -6.218 -7.087 -16.915 1.00 79.36 C ANISOU 1215 CG ARG B 785 14182 7081 8891 -970 3426 1301 C ATOM 1216 CD ARG B 785 -4.764 -7.186 -16.430 1.00 84.52 C ANISOU 1216 CD ARG B 785 13876 7724 10515 -1645 3982 1099 C ATOM 1217 NE ARG B 785 -3.820 -6.463 -17.291 1.00 96.47 N ANISOU 1217 NE ARG B 785 15718 8607 12330 -2153 5102 1493 N ATOM 1218 CZ ARG B 785 -2.497 -6.641 -17.293 1.00103.05 C ANISOU 1218 CZ ARG B 785 15646 9380 14126 -2728 5886 1428 C ATOM 1219 NH1 ARG B 785 -1.932 -7.537 -16.486 1.00 99.97 N ANISOU 1219 NH1 ARG B 785 13984 9530 14468 -2784 5474 1010 N ATOM 1220 NH2 ARG B 785 -1.731 -5.925 -18.113 1.00114.07 N ANISOU 1220 NH2 ARG B 785 17384 10115 15843 -3238 7113 1825 N ATOM 1221 N ASN B 786 -9.763 -7.599 -17.517 1.00 70.45 N ANISOU 1221 N ASN B 786 13990 6397 6382 669 1398 1433 N ATOM 1222 CA ASN B 786 -10.660 -8.711 -17.146 1.00 64.34 C ANISOU 1222 CA ASN B 786 12603 6257 5587 968 743 1085 C ATOM 1223 C ASN B 786 -9.961 -9.940 -16.492 1.00 56.06 C ANISOU 1223 C ASN B 786 10791 5768 4742 626 1020 683 C ATOM 1224 O ASN B 786 -9.022 -10.490 -17.089 1.00 57.39 O ANISOU 1224 O ASN B 786 11111 6007 4686 377 1564 739 O ATOM 1225 CB ASN B 786 -11.636 -9.082 -18.283 1.00 69.71 C ANISOU 1225 CB ASN B 786 13897 7004 5586 1410 25 1325 C ATOM 1226 CG ASN B 786 -12.781 -9.960 -17.787 1.00 68.89 C ANISOU 1226 CG ASN B 786 12976 7382 5818 1673 -730 961 C ATOM 1227 OD1 ASN B 786 -12.590 -11.157 -17.546 1.00 67.83 O ANISOU 1227 OD1 ASN B 786 12412 7704 5656 1442 -632 635 O ATOM 1228 ND2 ASN B 786 -13.960 -9.364 -17.591 1.00 72.57 N ANISOU 1228 ND2 ASN B 786 13145 7664 6763 2155 -1392 1023 N ATOM 1229 N TRP B 787 -10.460 -10.299 -15.274 1.00 48.29 N ANISOU 1229 N TRP B 787 9081 5076 4192 672 715 318 N ATOM 1230 CA ATRP B 787 -9.962 -11.227 -14.230 0.50 42.53 C ANISOU 1230 CA ATRP B 787 7693 4738 3729 416 791 -12 C ATOM 1231 CA BTRP B 787 -9.833 -11.393 -14.506 0.50 42.17 C ANISOU 1231 CA BTRP B 787 7704 4716 3602 406 841 32 C ATOM 1232 C TRP B 787 -10.785 -12.546 -14.133 1.00 38.68 C ANISOU 1232 C TRP B 787 6901 4674 3122 590 460 -181 C ATOM 1233 O TRP B 787 -10.522 -13.362 -13.250 1.00 34.72 O ANISOU 1233 O TRP B 787 6005 4414 2775 439 486 -368 O ATOM 1234 CB ATRP B 787 -9.892 -10.416 -12.868 0.50 42.04 C ANISOU 1234 CB ATRP B 787 7438 4490 4045 261 776 -254 C ATOM 1235 CB BTRP B 787 -9.116 -10.881 -13.264 0.50 40.44 C ANISOU 1235 CB BTRP B 787 7148 4394 3823 80 941 -170 C ATOM 1236 CG ATRP B 787 -10.422 -10.894 -11.395 0.50 37.79 C ANISOU 1236 CG ATRP B 787 6597 4202 3561 265 615 -617 C ATOM 1237 CG BTRP B 787 -9.992 -10.118 -12.324 0.50 37.37 C ANISOU 1237 CG BTRP B 787 6826 3823 3552 234 750 -376 C ATOM 1238 CD1ATRP B 787 -10.350 -12.152 -10.826 0.50 32.15 C ANISOU 1238 CD1ATRP B 787 5595 3885 2736 183 515 -713 C ATOM 1239 CD1BTRP B 787 -10.476 -8.854 -12.492 0.50 36.09 C ANISOU 1239 CD1BTRP B 787 7053 3148 3511 422 796 -300 C ATOM 1240 CD2ATRP B 787 -10.966 -10.031 -10.343 0.50 38.33 C ANISOU 1240 CD2ATRP B 787 6860 3990 3712 322 693 -899 C ATOM 1241 CD2BTRP B 787 -10.482 -10.576 -11.060 0.50 31.85 C ANISOU 1241 CD2BTRP B 787 5905 3350 2846 248 632 -696 C ATOM 1242 NE1ATRP B 787 -10.852 -12.124 -9.533 0.50 35.76 N ANISOU 1242 NE1ATRP B 787 6143 4353 3091 161 545 -965 N ATOM 1243 NE1BTRP B 787 -11.241 -8.496 -11.407 0.50 40.45 N ANISOU 1243 NE1BTRP B 787 7555 3595 4218 592 782 -634 N ATOM 1244 CE2ATRP B 787 -11.229 -10.845 -9.214 0.50 36.08 C ANISOU 1244 CE2ATRP B 787 6484 4000 3223 247 705 -1133 C ATOM 1245 CE2BTRP B 787 -11.250 -9.532 -10.508 0.50 34.26 C ANISOU 1245 CE2BTRP B 787 6456 3279 3283 449 741 -880 C ATOM 1246 CE3ATRP B 787 -11.261 -8.662 -10.261 0.50 41.64 C ANISOU 1246 CE3ATRP B 787 7647 3844 4329 452 839 -979 C ATOM 1247 CE3BTRP B 787 -10.328 -11.760 -10.331 0.50 26.65 C ANISOU 1247 CE3BTRP B 787 4987 3085 2051 124 526 -814 C ATOM 1248 CZ2ATRP B 787 -11.782 -10.337 -8.028 0.50 39.25 C ANISOU 1248 CZ2ATRP B 787 7228 4196 3489 280 965 -1480 C ATOM 1249 CZ2BTRP B 787 -11.885 -9.645 -9.282 0.50 33.52 C ANISOU 1249 CZ2BTRP B 787 6388 3231 3117 506 903 -1226 C ATOM 1250 CZ3ATRP B 787 -11.822 -8.163 -9.084 0.50 44.44 C ANISOU 1250 CZ3ATRP B 787 8236 3965 4684 534 1061 -1388 C ATOM 1251 CZ3BTRP B 787 -10.960 -11.855 -9.077 0.50 26.40 C ANISOU 1251 CZ3BTRP B 787 5078 3089 1863 139 591 -1072 C ATOM 1252 CH2ATRP B 787 -12.074 -9.000 -7.983 0.50 42.52 C ANISOU 1252 CH2ATRP B 787 7970 4072 4114 435 1174 -1654 C ATOM 1253 CH2BTRP B 787 -11.721 -10.806 -8.584 0.50 29.64 C ANISOU 1253 CH2BTRP B 787 5764 3160 2339 312 852 -1299 C ATOM 1254 N LYS B 788 -11.820 -12.671 -14.949 1.00 40.03 N ANISOU 1254 N LYS B 788 7275 4852 3081 882 56 -100 N ATOM 1255 CA LYS B 788 -12.765 -13.775 -14.941 1.00 39.55 C ANISOU 1255 CA LYS B 788 6870 5073 3085 959 -342 -287 C ATOM 1256 C LYS B 788 -12.071 -15.147 -15.017 1.00 36.73 C ANISOU 1256 C LYS B 788 6488 4915 2553 721 -130 -429 C ATOM 1257 O LYS B 788 -12.477 -16.064 -14.308 1.00 33.75 O ANISOU 1257 O LYS B 788 5690 4697 2435 623 -183 -606 O ATOM 1258 CB LYS B 788 -13.729 -13.600 -16.139 1.00 45.70 C ANISOU 1258 CB LYS B 788 7993 5748 3621 1251 -1038 -148 C ATOM 1259 CG LYS B 788 -14.675 -14.752 -16.429 1.00 49.15 C ANISOU 1259 CG LYS B 788 8106 6396 4172 1215 -1633 -378 C ATOM 1260 CD LYS B 788 -15.464 -14.484 -17.708 1.00 57.24 C ANISOU 1260 CD LYS B 788 9623 7281 4845 1477 -2603 -230 C ATOM 1261 CE LYS B 788 -16.559 -15.522 -17.896 1.00 61.44 C ANISOU 1261 CE LYS B 788 9612 7968 5762 1360 -3407 -534 C ATOM 1262 NZ LYS B 788 -17.549 -15.121 -18.947 1.00 74.49 N ANISOU 1262 NZ LYS B 788 11498 9480 7325 1666 -4721 -396 N ATOM 1263 N ASN B 789 -11.036 -15.280 -15.854 1.00 37.27 N ANISOU 1263 N ASN B 789 7029 4885 2248 646 236 -337 N ATOM 1264 CA ASN B 789 -10.373 -16.574 -16.024 1.00 37.62 C ANISOU 1264 CA ASN B 789 7058 4992 2242 545 528 -503 C ATOM 1265 C ASN B 789 -9.709 -17.021 -14.712 1.00 34.25 C ANISOU 1265 C ASN B 789 5980 4667 2367 428 706 -548 C ATOM 1266 O ASN B 789 -9.637 -18.240 -14.404 1.00 33.61 O ANISOU 1266 O ASN B 789 5733 4609 2427 420 696 -667 O ATOM 1267 CB ASN B 789 -9.348 -16.509 -17.161 1.00 41.63 C ANISOU 1267 CB ASN B 789 8180 5297 2341 538 1164 -419 C ATOM 1268 CG ASN B 789 -9.995 -16.291 -18.512 1.00 49.00 C ANISOU 1268 CG ASN B 789 10131 6084 2403 651 890 -362 C ATOM 1269 OD1 ASN B 789 -11.138 -16.679 -18.724 1.00 53.21 O ANISOU 1269 OD1 ASN B 789 10779 6700 2740 725 76 -504 O ATOM 1270 ND2 ASN B 789 -9.254 -15.687 -19.453 1.00 57.48 N ANISOU 1270 ND2 ASN B 789 11994 6894 2950 631 1550 -140 N ATOM 1271 N PHE B 790 -9.208 -16.049 -13.947 1.00 32.73 N ANISOU 1271 N PHE B 790 5539 4451 2445 330 780 -445 N ATOM 1272 CA PHE B 790 -8.589 -16.384 -12.655 1.00 32.39 C ANISOU 1272 CA PHE B 790 5056 4484 2765 210 680 -474 C ATOM 1273 C PHE B 790 -9.622 -16.777 -11.630 1.00 31.28 C ANISOU 1273 C PHE B 790 4896 4460 2530 212 402 -557 C ATOM 1274 O PHE B 790 -9.366 -17.688 -10.822 1.00 31.06 O ANISOU 1274 O PHE B 790 4776 4462 2564 174 296 -528 O ATOM 1275 CB PHE B 790 -7.706 -15.225 -12.115 1.00 35.39 C ANISOU 1275 CB PHE B 790 5263 4744 3440 -3 694 -430 C ATOM 1276 CG PHE B 790 -6.445 -15.044 -12.895 1.00 41.34 C ANISOU 1276 CG PHE B 790 5781 5341 4585 -114 1149 -325 C ATOM 1277 CD1 PHE B 790 -5.356 -15.860 -12.666 1.00 45.38 C ANISOU 1277 CD1 PHE B 790 5705 5870 5666 -105 1200 -316 C ATOM 1278 CD2 PHE B 790 -6.346 -14.061 -13.875 1.00 48.97 C ANISOU 1278 CD2 PHE B 790 7106 6067 5432 -200 1609 -193 C ATOM 1279 CE1 PHE B 790 -4.183 -15.732 -13.440 1.00 52.23 C ANISOU 1279 CE1 PHE B 790 6163 6550 7131 -188 1866 -244 C ATOM 1280 CE2 PHE B 790 -5.161 -13.914 -14.641 1.00 55.07 C ANISOU 1280 CE2 PHE B 790 7678 6630 6615 -367 2339 -74 C ATOM 1281 CZ PHE B 790 -4.083 -14.755 -14.414 1.00 54.99 C ANISOU 1281 CZ PHE B 790 6893 6673 7328 -368 2534 -135 C ATOM 1282 N ALA B 791 -10.768 -16.072 -11.653 1.00 30.63 N ANISOU 1282 N ALA B 791 4906 4372 2362 285 349 -620 N ATOM 1283 CA ALA B 791 -11.857 -16.335 -10.705 1.00 31.68 C ANISOU 1283 CA ALA B 791 4930 4560 2546 273 374 -722 C ATOM 1284 C ALA B 791 -12.463 -17.715 -10.946 1.00 31.50 C ANISOU 1284 C ALA B 791 4762 4588 2618 216 338 -745 C ATOM 1285 O ALA B 791 -13.004 -18.303 -10.035 1.00 32.97 O ANISOU 1285 O ALA B 791 4892 4762 2874 87 529 -755 O ATOM 1286 CB ALA B 791 -12.945 -15.227 -10.772 1.00 33.16 C ANISOU 1286 CB ALA B 791 5034 4649 2917 465 417 -806 C ATOM 1287 N LEU B 792 -12.335 -18.232 -12.171 1.00 32.26 N ANISOU 1287 N LEU B 792 4939 4659 2661 263 161 -770 N ATOM 1288 CA LEU B 792 -12.845 -19.557 -12.519 1.00 34.08 C ANISOU 1288 CA LEU B 792 5141 4813 2996 140 57 -884 C ATOM 1289 C LEU B 792 -11.945 -20.686 -12.040 1.00 33.10 C ANISOU 1289 C LEU B 792 5150 4543 2883 86 253 -808 C ATOM 1290 O LEU B 792 -12.408 -21.810 -11.904 1.00 37.09 O ANISOU 1290 O LEU B 792 5674 4863 3556 -70 269 -861 O ATOM 1291 CB LEU B 792 -13.012 -19.727 -14.059 1.00 35.93 C ANISOU 1291 CB LEU B 792 5696 4980 2978 200 -275 -1032 C ATOM 1292 CG LEU B 792 -14.238 -19.063 -14.683 1.00 43.13 C ANISOU 1292 CG LEU B 792 6467 5944 3978 270 -834 -1092 C ATOM 1293 CD1 LEU B 792 -14.265 -19.243 -16.236 1.00 47.19 C ANISOU 1293 CD1 LEU B 792 7665 6348 3915 319 -1339 -1214 C ATOM 1294 CD2 LEU B 792 -15.513 -19.597 -14.056 1.00 48.68 C ANISOU 1294 CD2 LEU B 792 6482 6648 5364 65 -981 -1224 C ATOM 1295 N VAL B 793 -10.669 -20.403 -11.823 1.00 30.97 N ANISOU 1295 N VAL B 793 4915 4279 2573 215 357 -671 N ATOM 1296 CA VAL B 793 -9.681 -21.433 -11.479 1.00 32.13 C ANISOU 1296 CA VAL B 793 5064 4225 2917 315 413 -553 C ATOM 1297 C VAL B 793 -10.124 -22.285 -10.232 1.00 33.15 C ANISOU 1297 C VAL B 793 5332 4209 3054 194 333 -368 C ATOM 1298 O VAL B 793 -10.087 -23.513 -10.292 1.00 35.42 O ANISOU 1298 O VAL B 793 5775 4169 3513 220 386 -325 O ATOM 1299 CB VAL B 793 -8.248 -20.821 -11.336 1.00 33.25 C ANISOU 1299 CB VAL B 793 4931 4409 3294 455 414 -424 C ATOM 1300 CG1 VAL B 793 -7.297 -21.780 -10.630 1.00 36.14 C ANISOU 1300 CG1 VAL B 793 5117 4561 4054 644 220 -218 C ATOM 1301 CG2 VAL B 793 -7.668 -20.396 -12.754 1.00 35.28 C ANISOU 1301 CG2 VAL B 793 5185 4626 3593 551 848 -555 C ATOM 1302 N PRO B 794 -10.575 -21.649 -9.138 1.00 33.20 N ANISOU 1302 N PRO B 794 5439 4359 2816 51 315 -267 N ATOM 1303 CA PRO B 794 -11.061 -22.497 -8.035 1.00 35.84 C ANISOU 1303 CA PRO B 794 6146 4479 2992 -110 446 -46 C ATOM 1304 C PRO B 794 -12.246 -23.394 -8.375 1.00 36.82 C ANISOU 1304 C PRO B 794 6213 4386 3391 -365 784 -142 C ATOM 1305 O PRO B 794 -12.609 -24.240 -7.563 1.00 41.27 O ANISOU 1305 O PRO B 794 7132 4645 3902 -561 1046 94 O ATOM 1306 CB PRO B 794 -11.546 -21.493 -6.989 1.00 37.35 C ANISOU 1306 CB PRO B 794 6585 4844 2764 -245 620 -55 C ATOM 1307 CG PRO B 794 -11.017 -20.155 -7.429 1.00 34.00 C ANISOU 1307 CG PRO B 794 5903 4660 2355 -121 389 -251 C ATOM 1308 CD PRO B 794 -10.688 -20.199 -8.841 1.00 31.31 C ANISOU 1308 CD PRO B 794 5152 4359 2386 19 301 -361 C ATOM 1309 N LEU B 795 -12.882 -23.169 -9.519 1.00 34.77 N ANISOU 1309 N LEU B 795 5567 4234 3412 -415 731 -464 N ATOM 1310 CA LEU B 795 -14.083 -23.914 -9.890 1.00 38.79 C ANISOU 1310 CA LEU B 795 5853 4537 4350 -754 843 -642 C ATOM 1311 C LEU B 795 -13.771 -25.027 -10.894 1.00 41.58 C ANISOU 1311 C LEU B 795 6417 4536 4846 -779 614 -831 C ATOM 1312 O LEU B 795 -14.636 -25.826 -11.224 1.00 45.22 O ANISOU 1312 O LEU B 795 6780 4701 5701 -1148 585 -1029 O ATOM 1313 CB LEU B 795 -15.163 -22.953 -10.436 1.00 39.04 C ANISOU 1313 CB LEU B 795 5306 4852 4675 -799 701 -898 C ATOM 1314 CG LEU B 795 -15.592 -21.897 -9.403 1.00 38.64 C ANISOU 1314 CG LEU B 795 5080 5002 4598 -736 1133 -800 C ATOM 1315 CD1 LEU B 795 -16.544 -20.908 -10.020 1.00 41.58 C ANISOU 1315 CD1 LEU B 795 4811 5557 5430 -603 922 -1015 C ATOM 1316 CD2 LEU B 795 -16.204 -22.583 -8.139 1.00 40.98 C ANISOU 1316 CD2 LEU B 795 5502 5052 5018 -1080 1888 -620 C ATOM 1317 N LEU B 796 -12.518 -25.097 -11.328 1.00 39.85 N ANISOU 1317 N LEU B 796 6471 4273 4396 -412 526 -805 N ATOM 1318 CA LEU B 796 -12.133 -26.037 -12.390 1.00 44.60 C ANISOU 1318 CA LEU B 796 7403 4483 5062 -337 491 -1089 C ATOM 1319 C LEU B 796 -12.335 -27.467 -11.967 1.00 50.61 C ANISOU 1319 C LEU B 796 8450 4609 6170 -537 647 -1024 C ATOM 1320 O LEU B 796 -12.662 -28.343 -12.797 1.00 54.40 O ANISOU 1320 O LEU B 796 9226 4641 6801 -731 588 -1408 O ATOM 1321 CB LEU B 796 -10.695 -25.797 -12.839 1.00 43.86 C ANISOU 1321 CB LEU B 796 7408 4412 4846 142 650 -1058 C ATOM 1322 CG LEU B 796 -10.507 -24.540 -13.689 1.00 43.28 C ANISOU 1322 CG LEU B 796 7274 4761 4410 247 627 -1193 C ATOM 1323 CD1 LEU B 796 -9.021 -24.374 -14.001 1.00 45.76 C ANISOU 1323 CD1 LEU B 796 7525 5016 4844 634 1028 -1122 C ATOM 1324 CD2 LEU B 796 -11.323 -24.624 -14.994 1.00 49.56 C ANISOU 1324 CD2 LEU B 796 8496 5494 4839 65 396 -1614 C ATOM 1325 N ARG B 797 -12.181 -27.686 -10.667 1.00 51.99 N ANISOU 1325 N ARG B 797 8691 4672 6391 -531 816 -542 N ATOM 1326 CA ARG B 797 -12.340 -28.984 -10.067 1.00 59.99 C ANISOU 1326 CA ARG B 797 10127 4986 7679 -710 1025 -296 C ATOM 1327 C ARG B 797 -13.799 -29.469 -10.169 1.00 65.33 C ANISOU 1327 C ARG B 797 10669 5411 8743 -1420 1213 -521 C ATOM 1328 O ARG B 797 -14.052 -30.682 -10.293 1.00 72.16 O ANISOU 1328 O ARG B 797 11885 5533 10002 -1710 1350 -583 O ATOM 1329 CB ARG B 797 -11.826 -28.963 -8.625 1.00 61.74 C ANISOU 1329 CB ARG B 797 10673 5163 7621 -523 1066 357 C ATOM 1330 CG ARG B 797 -11.012 -30.214 -8.290 1.00 67.53 C ANISOU 1330 CG ARG B 797 11961 5114 8584 -188 996 736 C ATOM 1331 CD ARG B 797 -11.865 -31.250 -7.621 1.00 77.02 C ANISOU 1331 CD ARG B 797 13747 5617 9901 -678 1401 1047 C ATOM 1332 NE ARG B 797 -11.132 -32.031 -6.628 1.00 83.36 N ANISOU 1332 NE ARG B 797 15317 5793 10565 -318 1243 1768 N ATOM 1333 CZ ARG B 797 -10.589 -31.530 -5.517 1.00 83.93 C ANISOU 1333 CZ ARG B 797 15758 6125 10006 -47 884 2321 C ATOM 1334 NH1 ARG B 797 -10.662 -30.232 -5.251 1.00 76.89 N ANISOU 1334 NH1 ARG B 797 14528 6080 8608 -117 768 2164 N ATOM 1335 NH2 ARG B 797 -9.954 -32.337 -4.674 1.00 93.16 N ANISOU 1335 NH2 ARG B 797 17744 6625 11028 314 541 3031 N ATOM 1336 N ASP B 798 -14.738 -28.513 -10.143 1.00 64.07 N ANISOU 1336 N ASP B 798 9920 5794 8629 -1690 1210 -666 N ATOM 1337 CA ASP B 798 -16.164 -28.747 -10.476 1.00 70.32 C ANISOU 1337 CA ASP B 798 10168 6466 10085 -2339 1222 -991 C ATOM 1338 C ASP B 798 -16.824 -29.821 -9.614 1.00 78.53 C ANISOU 1338 C ASP B 798 11358 6835 11645 -2928 1857 -719 C ATOM 1339 O ASP B 798 -17.789 -30.469 -10.027 1.00 86.42 O ANISOU 1339 O ASP B 798 11975 7438 13422 -3566 1828 -1035 O ATOM 1340 CB ASP B 798 -16.346 -29.063 -12.002 1.00 72.36 C ANISOU 1340 CB ASP B 798 10420 6592 10482 -2452 517 -1625 C TER 1341 ASP B 798 HETATM 1342 CA CA A 501 4.305 -26.988 -18.543 1.00 34.32 CA ANISOU 1342 CA CA A 501 5157 4696 3185 596 767 283 CA HETATM 1343 CA CA A 502 -3.357 -33.042 -25.038 1.00 40.37 CA ANISOU 1343 CA CA A 502 8193 4546 2599 716 44 -653 CA HETATM 1344 CA CA A 503 -12.769 -8.286 2.062 1.00 28.96 CA ANISOU 1344 CA CA A 503 5324 3648 2033 194 -181 38 CA HETATM 1345 CA CA A 504 -17.964 -1.824 -5.956 1.00 27.71 CA ANISOU 1345 CA CA A 504 5176 3287 2064 0 -31 224 CA HETATM 1346 S SO4 A 149 -10.569 -30.368 -1.384 1.00 83.53 S HETATM 1347 O1 SO4 A 149 -9.788 -31.080 -2.388 1.00 82.86 O HETATM 1348 O2 SO4 A 149 -11.947 -30.853 -1.456 1.00 83.67 O HETATM 1349 O3 SO4 A 149 -10.017 -30.635 -0.059 1.00 82.90 O HETATM 1350 O4 SO4 A 149 -10.550 -28.927 -1.648 1.00 83.31 O HETATM 1351 O HOH A 150 -12.257 -23.325 -2.531 1.00 32.27 O HETATM 1352 O HOH A 151 -9.989 -30.335 -26.164 1.00 21.48 O HETATM 1353 O HOH A 152 -6.922 -2.283 -0.716 1.00 14.67 O HETATM 1354 O HOH A 153 3.702 -19.006 -11.212 1.00 41.74 O HETATM 1355 O HOH A 154 -8.889 -5.668 2.525 1.00 23.68 O HETATM 1356 O HOH A 155 3.250 -20.704 -21.316 1.00 26.59 O HETATM 1357 O HOH A 156 -0.270 -5.146 0.340 1.00 35.73 O HETATM 1358 O HOH A 157 -20.989 -8.543 -1.025 1.00 13.19 O HETATM 1359 O HOH A 158 -18.570 -6.617 -12.339 1.00 10.80 O HETATM 1360 O HOH A 159 -19.226 -2.530 -3.970 1.00 13.63 O HETATM 1361 O HOH A 160 1.082 -25.473 -4.504 1.00 9.92 O HETATM 1362 O HOH A 161 0.298 -34.569 -17.234 1.00 11.02 O HETATM 1363 O HOH A 162 -22.916 -6.658 -0.808 1.00 24.60 O HETATM 1364 O HOH A 163 -17.069 -13.530 1.686 1.00 17.10 O HETATM 1365 O HOH A 164 0.228 -24.979 -26.333 1.00 17.82 O HETATM 1366 O HOH A 165 -9.993 -1.711 -3.080 1.00 15.41 O HETATM 1367 O HOH A 166 -11.735 -6.546 2.910 1.00 18.17 O HETATM 1368 O HOH A 167 -0.931 -25.173 -0.204 1.00 14.10 O HETATM 1369 O HOH A 168 -10.503 -14.351 -21.890 1.00 28.02 O HETATM 1370 O HOH A 169 0.438 -21.818 -8.020 1.00 19.87 O HETATM 1371 O HOH A 170 -3.783 -11.209 -28.390 1.00 18.54 O HETATM 1372 O HOH A 171 -2.919 -37.233 -17.515 1.00 21.60 O HETATM 1373 O HOH A 172 -3.030 -32.205 -4.385 1.00 25.66 O HETATM 1374 O HOH A 173 -9.775 -39.623 -6.343 1.00 17.37 O HETATM 1375 O HOH A 174 -20.716 0.038 -1.408 1.00 24.77 O HETATM 1376 O HOH A 175 -2.075 -31.922 -26.330 1.00 18.14 O HETATM 1377 O HOH A 176 -10.441 -1.162 0.008 1.00 32.50 O HETATM 1378 O HOH A 177 -3.310 -2.439 -6.021 1.00 27.09 O HETATM 1379 O HOH A 178 -3.025 -37.887 -4.883 1.00 23.32 O HETATM 1380 O HOH A 179 -14.213 -21.053 -1.167 1.00 20.57 O HETATM 1381 O HOH A 180 -8.990 0.456 -6.126 1.00 47.47 O HETATM 1382 O HOH A 181 -10.644 -17.121 1.726 1.00 24.60 O HETATM 1383 O HOH A 182 -12.487 -5.364 7.111 1.00 41.24 O HETATM 1384 O HOH A 183 -13.924 -27.365 -17.555 1.00 20.33 O HETATM 1385 O HOH A 184 -14.398 -15.455 2.857 1.00 28.85 O HETATM 1386 O HOH A 185 3.681 -1.680 -7.989 1.00 19.21 O HETATM 1387 O HOH A 186 -7.464 -41.960 -13.160 1.00 29.31 O HETATM 1388 O HOH A 187 -5.157 -41.707 -3.726 1.00 42.21 O HETATM 1389 O HOH A 188 -14.918 5.321 -8.629 1.00 28.44 O HETATM 1390 O HOH A 189 -8.125 -9.033 3.985 1.00 21.14 O HETATM 1391 O HOH A 190 -18.752 -15.837 3.540 1.00 36.94 O HETATM 1392 O HOH A 191 -18.214 -6.698 -15.051 1.00 32.36 O HETATM 1393 O HOH A 192 -20.223 -11.819 2.170 1.00 16.20 O HETATM 1394 O HOH A 193 -1.101 -33.836 -3.311 1.00 23.29 O HETATM 1395 O HOH A 194 -12.732 -4.055 2.490 1.00 16.29 O HETATM 1396 O HOH A 195 5.365 -29.024 -17.839 1.00 17.39 O HETATM 1397 O HOH A 196 1.715 -24.816 -12.216 1.00 23.75 O HETATM 1398 O HOH A 197 0.997 -9.470 -1.781 1.00 33.97 O HETATM 1399 O HOH A 198 -16.950 -0.185 -0.172 0.50 10.76 O HETATM 1400 O HOH A 199 -15.557 -23.859 0.702 1.00 32.65 O HETATM 1401 O HOH A 200 -11.640 -30.574 -17.240 1.00 23.61 O HETATM 1402 O HOH A 201 -18.346 -13.892 6.256 1.00 27.04 O HETATM 1403 O HOH A 202 0.835 -37.170 -15.345 1.00 21.63 O HETATM 1404 O HOH A 203 -5.221 -31.348 -28.929 1.00 22.40 O HETATM 1405 O HOH A 204 4.545 -28.527 -11.167 1.00 32.64 O HETATM 1406 O HOH A 205 -25.683 -15.504 -7.454 1.00 31.23 O HETATM 1407 O HOH A 206 -19.282 -14.835 0.708 1.00 32.22 O HETATM 1408 O HOH A 207 6.196 -26.844 -14.119 1.00 25.83 O HETATM 1409 O HOH A 208 -4.527 -0.989 -1.544 1.00 40.44 O HETATM 1410 O HOH A 209 -6.968 -13.774 -17.623 1.00 23.00 O HETATM 1411 O HOH A 210 -4.543 -19.553 -0.598 1.00 31.98 O HETATM 1412 O HOH A 211 -14.707 6.745 -13.071 1.00 55.90 O HETATM 1413 O HOH A 212 -0.267 -14.053 -28.669 1.00 16.95 O HETATM 1414 O HOH A 213 -12.286 -37.305 -11.020 1.00 35.22 O HETATM 1415 O HOH A 214 -15.725 5.707 -15.296 1.00 35.38 O HETATM 1416 O HOH A 215 -1.094 -12.142 -22.204 1.00 21.80 O HETATM 1417 O HOH A 216 -17.271 -2.273 -14.501 1.00 41.38 O HETATM 1418 O HOH A 217 -0.097 -9.324 -6.781 1.00 26.46 O HETATM 1419 O HOH A 218 -22.536 -4.059 -1.230 1.00 46.42 O HETATM 1420 O HOH A 219 -0.056 -31.173 -24.918 1.00 24.93 O HETATM 1421 O HOH A 220 -1.175 -38.451 -16.231 1.00 29.09 O HETATM 1422 O HOH A 221 0.322 -15.539 -15.992 1.00 24.81 O HETATM 1423 O HOH A 222 -4.491 -6.406 3.547 1.00 44.92 O HETATM 1424 O HOH A 223 -4.000 -27.516 -0.220 1.00 28.29 O HETATM 1425 O HOH A 224 1.334 -22.009 -26.396 1.00 48.03 O HETATM 1426 O HOH A 225 -5.271 -17.237 -1.558 1.00 43.76 O HETATM 1427 O HOH A 226 -26.567 -10.791 -6.006 1.00 33.01 O HETATM 1428 O HOH A 227 -26.734 -10.670 -3.148 1.00 24.90 O HETATM 1429 O HOH A 228 1.207 -19.664 -24.913 1.00 35.20 O HETATM 1430 O HOH A 229 -20.851 -13.446 -30.747 1.00 35.96 O HETATM 1431 O HOH A 230 -24.504 -10.251 -1.447 1.00 34.53 O HETATM 1432 O HOH A 231 -11.565 -34.011 -25.875 1.00 35.77 O HETATM 1433 O HOH A 232 5.198 -27.054 -8.758 1.00 40.50 O HETATM 1434 O HOH A 233 -7.926 -17.634 -0.952 1.00 29.79 O HETATM 1435 O HOH A 234 -5.347 -37.860 -18.293 1.00 27.66 O HETATM 1436 O HOH A 235 -5.713 -37.975 -20.855 1.00 35.16 O HETATM 1437 O HOH A 236 -13.460 -29.789 -18.946 1.00 23.95 O HETATM 1438 O HOH A 237 -13.283 1.590 -9.288 1.00 22.13 O HETATM 1439 O HOH A 238 2.986 -35.375 -17.486 1.00 29.54 O HETATM 1440 O HOH A 239 2.655 -34.987 -14.633 1.00 34.75 O HETATM 1441 O HOH B 78 -12.633 -28.145 -15.617 1.00 27.11 O CONECT 152 1342 CONECT 169 1342 CONECT 182 1342 CONECT 190 1342 CONECT 232 1342 CONECT 233 1342 CONECT 449 1343 CONECT 462 1343 CONECT 473 1343 CONECT 482 1343 CONECT 527 1343 CONECT 528 1343 CONECT 754 1344 CONECT 770 1344 CONECT 782 1344 CONECT 791 1344 CONECT 831 1344 CONECT 832 1344 CONECT 1052 1345 CONECT 1067 1345 CONECT 1080 1345 CONECT 1088 1345 CONECT 1143 1345 CONECT 1144 1345 CONECT 1342 152 169 182 190 CONECT 1342 232 233 1396 CONECT 1343 449 462 473 482 CONECT 1343 527 528 1376 CONECT 1344 754 770 782 791 CONECT 1344 831 832 1367 CONECT 1345 1052 1067 1080 1088 CONECT 1345 1143 1144 1360 CONECT 1346 1347 1348 1349 1350 CONECT 1347 1346 CONECT 1348 1346 CONECT 1349 1346 CONECT 1350 1346 CONECT 1360 1345 CONECT 1367 1344 CONECT 1376 1343 CONECT 1396 1342 MASTER 491 0 5 10 2 0 9 6 1368 2 41 15 END