Browse entries in the PDBbind-CN Database
HEADER CALCIUM BINDING/TRANSPORT PROTEIN 23-OCT-18 6MUD TITLE VOLTAGE-GATED SODIUM CHANNEL NAV1.5 C-TERMINAL DOMAIN IN COMPLEX WITH TITLE 2 CA2+/CALMODULIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CALMODULIN-1; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: SODIUM CHANNEL PROTEIN TYPE 5 SUBUNIT ALPHA; COMPND 7 CHAIN: B; COMPND 8 SYNONYM: HH1,SODIUM CHANNEL PROTEIN CARDIAC MUSCLE SUBUNIT ALPHA, COMPND 9 SODIUM CHANNEL PROTEIN TYPE V SUBUNIT ALPHA,VOLTAGE-GATED SODIUM COMPND 10 CHANNEL SUBUNIT ALPHA NAV1.5; COMPND 11 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: CALM1, CALM, CAM, CAM1; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: SCN5A; SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS VOLTAGE-GATED ION CHANNEL, TRANSPORT PROTEIN, EF-HAND DOMAIN, CALCIUM KEYWDS 2 BINDING-TRANSPORT PROTEIN COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR B.R.GARDILL,C.C.TUNG,F.VAN PETEGEM REVDAT 4 08-JAN-20 6MUD 1 REMARK REVDAT 3 12-JUN-19 6MUD 1 JRNL REVDAT 2 22-MAY-19 6MUD 1 JRNL REVDAT 1 08-MAY-19 6MUD 0 JRNL AUTH B.R.GARDILL,R.E.RIVERA-ACEVEDO,C.C.TUNG,F.VAN PETEGEM JRNL TITL CRYSTAL STRUCTURES OF CA2+-CALMODULIN BOUND TO NAVC-TERMINAL JRNL TITL 2 REGIONS SUGGEST ROLE FOR EF-HAND DOMAIN IN BINDING AND JRNL TITL 3 INACTIVATION. JRNL REF PROC.NATL.ACAD.SCI.USA V. 116 10763 2019 JRNL REFN ESSN 1091-6490 JRNL PMID 31072926 JRNL DOI 10.1073/PNAS.1818618116 REMARK 2 REMARK 2 RESOLUTION. 2.69 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0222 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.31 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 3 NUMBER OF REFLECTIONS : 10016 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) : 0.215 REMARK 3 R VALUE (WORKING SET) : 0.212 REMARK 3 FREE R VALUE : 0.269 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400 REMARK 3 FREE R VALUE TEST SET COUNT : 459 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) : 2.69 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.76 REMARK 3 REFLECTION IN BIN (WORKING SET) : 601 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 75.81 REMARK 3 BIN R VALUE (WORKING SET) : 0.4300 REMARK 3 BIN FREE R VALUE SET COUNT : 10 REMARK 3 BIN FREE R VALUE : 0.3380 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 2203 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 4 REMARK 3 SOLVENT ATOMS : 15 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 71.22 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -2.54000 REMARK 3 B22 (A**2) : -3.79000 REMARK 3 B33 (A**2) : 6.33000 REMARK 3 B12 (A**2) : 0.00000 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): 0.849 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.354 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.334 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 35.519 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.951 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.915 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 2246 ; 0.007 ; 0.014 REMARK 3 BOND LENGTHS OTHERS (A): 1990 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 3017 ; 1.055 ; 1.660 REMARK 3 BOND ANGLES OTHERS (DEGREES): 4684 ; 0.813 ; 1.641 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 274 ; 6.089 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 138 ;31.882 ;23.478 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 423 ;19.353 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 16 ;24.758 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 298 ; 0.049 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2535 ; 0.004 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 397 ; 0.001 ; 0.020 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): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL 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 : 8 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 1 A 64 REMARK 3 ORIGIN FOR THE GROUP (A): -6.932 -6.521 -37.752 REMARK 3 T TENSOR REMARK 3 T11: 0.1355 T22: 0.0081 REMARK 3 T33: 0.4552 T12: -0.0071 REMARK 3 T13: 0.0030 T23: -0.0316 REMARK 3 L TENSOR REMARK 3 L11: 5.4134 L22: 2.2341 REMARK 3 L33: 2.0475 L12: -1.0149 REMARK 3 L13: 2.0029 L23: -0.9614 REMARK 3 S TENSOR REMARK 3 S11: -0.2388 S12: -0.1459 S13: 0.2982 REMARK 3 S21: 0.1558 S22: 0.0043 S23: -0.2223 REMARK 3 S31: -0.0195 S32: -0.0992 S33: 0.2346 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : A 65 A 147 REMARK 3 ORIGIN FOR THE GROUP (A): -30.552 11.441 -24.863 REMARK 3 T TENSOR REMARK 3 T11: 0.1982 T22: 0.2013 REMARK 3 T33: 0.4069 T12: -0.0737 REMARK 3 T13: -0.0365 T23: -0.0605 REMARK 3 L TENSOR REMARK 3 L11: 2.7013 L22: 4.6351 REMARK 3 L33: 2.3536 L12: -2.6209 REMARK 3 L13: -1.7283 L23: 1.0259 REMARK 3 S TENSOR REMARK 3 S11: -0.0102 S12: -0.3799 S13: 0.2543 REMARK 3 S21: 0.5114 S22: 0.2829 S23: -0.3079 REMARK 3 S31: -0.0556 S32: 0.0434 S33: -0.2727 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 1785 B 1801 REMARK 3 ORIGIN FOR THE GROUP (A): -32.826 22.420 -61.364 REMARK 3 T TENSOR REMARK 3 T11: 0.6273 T22: 0.5637 REMARK 3 T33: 0.5132 T12: -0.2205 REMARK 3 T13: 0.0382 T23: 0.1488 REMARK 3 L TENSOR REMARK 3 L11: 0.4455 L22: 7.7752 REMARK 3 L33: 4.4793 L12: 1.2657 REMARK 3 L13: 0.0770 L23: -3.8720 REMARK 3 S TENSOR REMARK 3 S11: -0.3757 S12: 0.3223 S13: 0.1221 REMARK 3 S21: -0.9804 S22: 0.3194 S23: 0.1037 REMARK 3 S31: -0.0260 S32: 0.3950 S33: 0.0563 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1802 B 1837 REMARK 3 ORIGIN FOR THE GROUP (A): -30.323 16.905 -51.248 REMARK 3 T TENSOR REMARK 3 T11: 0.2280 T22: 0.2500 REMARK 3 T33: 0.4305 T12: 0.0065 REMARK 3 T13: 0.0963 T23: 0.0711 REMARK 3 L TENSOR REMARK 3 L11: 4.7463 L22: 7.1684 REMARK 3 L33: 3.4803 L12: 2.5132 REMARK 3 L13: -0.6817 L23: 2.5468 REMARK 3 S TENSOR REMARK 3 S11: -0.2513 S12: 0.2543 S13: 0.0197 REMARK 3 S21: -0.4969 S22: 0.1744 S23: -0.4692 REMARK 3 S31: 0.0944 S32: 0.6271 S33: 0.0769 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1838 B 1862 REMARK 3 ORIGIN FOR THE GROUP (A): -38.931 18.067 -50.085 REMARK 3 T TENSOR REMARK 3 T11: 0.2245 T22: 0.2417 REMARK 3 T33: 0.2925 T12: -0.0134 REMARK 3 T13: -0.0007 T23: 0.0250 REMARK 3 L TENSOR REMARK 3 L11: 0.4497 L22: 9.3894 REMARK 3 L33: 1.0706 L12: 0.6882 REMARK 3 L13: -0.4129 L23: -0.1494 REMARK 3 S TENSOR REMARK 3 S11: -0.1891 S12: 0.1722 S13: 0.0183 REMARK 3 S21: -0.2902 S22: 0.1722 S23: -0.0773 REMARK 3 S31: 0.0435 S32: -0.1716 S33: 0.0169 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1863 B 1878 REMARK 3 ORIGIN FOR THE GROUP (A): -46.070 28.099 -56.039 REMARK 3 T TENSOR REMARK 3 T11: 0.1710 T22: 0.3169 REMARK 3 T33: 0.4344 T12: 0.1054 REMARK 3 T13: -0.0884 T23: -0.0288 REMARK 3 L TENSOR REMARK 3 L11: 0.0433 L22: 9.6717 REMARK 3 L33: 7.9802 L12: 0.3662 REMARK 3 L13: 0.4440 L23: -0.4784 REMARK 3 S TENSOR REMARK 3 S11: -0.0578 S12: -0.0053 S13: 0.0562 REMARK 3 S21: -0.4013 S22: -0.0242 S23: 0.4986 REMARK 3 S31: -0.7038 S32: -0.1097 S33: 0.0820 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1887 B 1894 REMARK 3 ORIGIN FOR THE GROUP (A): -45.653 8.156 -49.658 REMARK 3 T TENSOR REMARK 3 T11: 0.0977 T22: 0.2830 REMARK 3 T33: 0.3651 T12: -0.0817 REMARK 3 T13: 0.0516 T23: 0.0130 REMARK 3 L TENSOR REMARK 3 L11: 1.6292 L22: 6.4448 REMARK 3 L33: 8.7070 L12: 0.6997 REMARK 3 L13: 3.6447 L23: -0.2780 REMARK 3 S TENSOR REMARK 3 S11: -0.0793 S12: 0.0913 S13: -0.0001 REMARK 3 S21: 0.0196 S22: 0.2011 S23: 0.4038 REMARK 3 S31: -0.1960 S32: 0.1659 S33: -0.1218 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : B 1895 B 1920 REMARK 3 ORIGIN FOR THE GROUP (A): -31.521 5.311 -25.964 REMARK 3 T TENSOR REMARK 3 T11: 0.2249 T22: 0.1178 REMARK 3 T33: 0.3789 T12: -0.0373 REMARK 3 T13: -0.0347 T23: -0.0302 REMARK 3 L TENSOR REMARK 3 L11: 1.3336 L22: 3.9651 REMARK 3 L33: 11.5792 L12: -2.0243 REMARK 3 L13: 3.8948 L23: -5.7806 REMARK 3 S TENSOR REMARK 3 S11: 0.0807 S12: 0.0839 S13: 0.1023 REMARK 3 S21: -0.0561 S22: -0.1919 S23: -0.2307 REMARK 3 S31: 0.4026 S32: 0.1923 S33: 0.1112 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : NULL REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 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 U VALUES : WITH TLS ADDED REMARK 4 REMARK 4 6MUD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-18. REMARK 100 THE DEPOSITION ID IS D_1000237596. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 17-SEP-11 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 9.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : APS REMARK 200 BEAMLINE : 23-ID-D REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.033000 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : K-B PAIR OF BIMORPH MIRRORS REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS NOVEMBER 11, 2013 REMARK 200 DATA SCALING SOFTWARE : XDS NOVEMBER 11, 2013 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10476 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690 REMARK 200 RESOLUTION RANGE LOW (A) : 35.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 93.9 REMARK 200 DATA REDUNDANCY : 3.250 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.5100 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.69 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.3 REMARK 200 DATA REDUNDANCY IN SHELL : 2.39 REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.890 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 58.14 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 5-15 % (W/V) PEG 4000, 0.1 M TRIS, PH REMARK 280 9.5, 0.1 M MGCL2, AND 5 % (V/V) ISOPROPANOL, VAPOR DIFFUSION, REMARK 280 HANGING DROP, TEMPERATURE 277K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z REMARK 290 3555 -X,Y,-Z REMARK 290 4555 X,-Y,-Z REMARK 290 5555 X+1/2,Y+1/2,Z+1/2 REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2 REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2 REMARK 290 8555 X+1/2,-Y+1/2,-Z+1/2 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 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000 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 0.00000 REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 32.78950 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 42.01600 REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 70.34200 REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 32.78950 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 42.01600 REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 70.34200 REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 32.78950 REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 42.01600 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 70.34200 REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 32.78950 REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 42.01600 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 70.34200 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: 1660 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 17250 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 LYS A 148 REMARK 465 SER B 1783 REMARK 465 ASN B 1784 REMARK 465 PHE B 1879 REMARK 465 MET B 1880 REMARK 465 ALA B 1881 REMARK 465 ALA B 1882 REMARK 465 ASN B 1883 REMARK 465 PRO B 1884 REMARK 465 SER B 1885 REMARK 465 LYS B 1886 REMARK 465 LEU B 1921 REMARK 465 LYS B 1922 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 2 53.09 -108.53 REMARK 500 LYS A 115 172.17 -54.66 REMARK 500 ASP B1802 59.11 -145.35 REMARK 500 SER B1812 3.93 -64.98 REMARK 500 VAL B1843 -166.33 -75.91 REMARK 500 GLN B1918 33.81 -97.11 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG A 90 0.12 SIDE CHAIN 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 A1001 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 20 OD1 REMARK 620 2 ASP A 22 OD1 77.4 REMARK 620 3 ASP A 24 OD1 82.8 81.8 REMARK 620 4 THR A 26 O 88.1 162.4 86.5 REMARK 620 5 GLU A 31 OE1 123.2 120.3 147.4 76.1 REMARK 620 6 GLU A 31 OE2 94.3 73.5 155.1 118.1 51.7 REMARK 620 7 HOH A1107 O 157.3 102.5 74.8 87.0 76.9 107.5 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1002 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 56 OD1 REMARK 620 2 ASP A 58 OD1 72.7 REMARK 620 3 ASN A 60 OD1 93.0 85.0 REMARK 620 4 THR A 62 O 71.5 139.9 79.5 REMARK 620 5 GLU A 67 OE1 95.4 126.3 148.7 74.8 REMARK 620 6 GLU A 67 OE2 83.7 76.3 161.1 116.6 50.1 REMARK 620 7 HOH A1101 O 152.0 91.1 108.5 128.9 75.7 70.1 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1004 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 93 OD1 REMARK 620 2 ASP A 95 OD1 82.5 REMARK 620 3 ASN A 97 OD1 84.4 92.7 REMARK 620 4 TYR A 99 O 92.3 170.1 78.3 REMARK 620 5 GLU A 104 OE1 95.6 56.1 148.3 133.2 REMARK 620 6 GLU A 104 OE2 108.3 105.5 158.8 84.1 49.6 REMARK 620 7 HOH A1103 O 163.3 93.3 79.7 89.3 95.4 88.4 REMARK 620 N 1 2 3 4 5 6 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A1003 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 129 OD1 REMARK 620 2 ASP A 131 OD2 81.0 REMARK 620 3 ASP A 133 OD1 79.8 85.5 REMARK 620 4 GLN A 135 O 81.4 158.3 78.8 REMARK 620 5 GLU A 140 OE1 112.9 107.7 162.5 90.8 REMARK 620 6 GLU A 140 OE2 86.5 66.7 150.7 124.7 45.9 REMARK 620 7 HOH A1106 O 163.2 82.3 100.6 115.2 70.9 85.4 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 1001 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1002 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1003 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 1004 DBREF 6MUD A 0 148 UNP P0DP23 CALM1_HUMAN 1 149 DBREF 6MUD B 1786 1922 UNP Q14524 SCN5A_HUMAN 1786 1922 SEQADV 6MUD SER B 1783 UNP Q14524 EXPRESSION TAG SEQADV 6MUD ASN B 1784 UNP Q14524 EXPRESSION TAG SEQADV 6MUD ALA B 1785 UNP Q14524 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 140 SER ASN ALA LEU SER GLU ASP ASP PHE ASP MET PHE TYR SEQRES 2 B 140 GLU ILE TRP GLU LYS PHE ASP PRO GLU ALA THR GLN PHE SEQRES 3 B 140 ILE GLU TYR SER VAL LEU SER ASP PHE ALA ASP ALA LEU SEQRES 4 B 140 SER GLU PRO LEU ARG ILE ALA LYS PRO ASN GLN ILE SER SEQRES 5 B 140 LEU ILE ASN MET ASP LEU PRO MET VAL SER GLY ASP ARG SEQRES 6 B 140 ILE HIS CYS MET ASP ILE LEU PHE ALA PHE THR LYS ARG SEQRES 7 B 140 VAL LEU GLY GLU SER GLY GLU MET ASP ALA LEU LYS ILE SEQRES 8 B 140 GLN MET GLU GLU LYS PHE MET ALA ALA ASN PRO SER LYS SEQRES 9 B 140 ILE SER TYR GLU PRO ILE THR THR THR LEU ARG ARG LYS SEQRES 10 B 140 HIS GLU GLU VAL SER ALA MET VAL ILE GLN ARG ALA PHE SEQRES 11 B 140 ARG ARG HIS LEU LEU GLN ARG SER LEU LYS HET CA A1001 1 HET CA A1002 1 HET CA A1003 1 HET CA A1004 1 HETNAM CA CALCIUM ION FORMUL 3 CA 4(CA 2+) FORMUL 7 HOH *15(H2 O) HELIX 1 AA1 THR A 5 ASP A 20 1 16 HELIX 2 AA2 THR A 28 LEU A 39 1 12 HELIX 3 AA3 THR A 44 ASP A 56 1 13 HELIX 4 AA4 PHE A 65 ASP A 80 1 16 HELIX 5 AA5 ASP A 80 ASP A 93 1 14 HELIX 6 AA6 SER A 101 MET A 109 1 9 HELIX 7 AA7 THR A 117 ASP A 129 1 13 HELIX 8 AA8 ASN A 137 MET A 144 1 8 HELIX 9 AA9 SER B 1787 ASP B 1802 1 16 HELIX 10 AB1 VAL B 1813 LEU B 1821 1 9 HELIX 11 AB2 ASN B 1831 MET B 1838 1 8 HELIX 12 AB3 CYS B 1850 GLY B 1863 1 14 HELIX 13 AB4 SER B 1865 LYS B 1878 1 14 HELIX 14 AB5 THR B 1895 GLN B 1918 1 24 SHEET 1 AA1 2 THR A 26 ILE A 27 0 SHEET 2 AA1 2 ILE A 63 ASP A 64 -1 O ILE A 63 N ILE A 27 SHEET 1 AA2 2 PHE B1808 GLU B1810 0 SHEET 2 AA2 2 ARG B1847 HIS B1849 -1 O ILE B1848 N ILE B1809 SHEET 1 AA3 2 PRO B1841 MET B1842 0 SHEET 2 AA3 2 THR B1893 THR B1894 -1 O THR B1893 N MET B1842 LINK OD1 ASP A 20 CA CA A1001 1555 1555 2.41 LINK OD1 ASP A 22 CA CA A1001 1555 1555 2.13 LINK OD1 ASP A 24 CA CA A1001 1555 1555 2.34 LINK O THR A 26 CA CA A1001 1555 1555 2.25 LINK OE1 GLU A 31 CA CA A1001 1555 1555 2.42 LINK OE2 GLU A 31 CA CA A1001 1555 1555 2.66 LINK OD1 ASP A 56 CA CA A1002 1555 1555 2.21 LINK OD1 ASP A 58 CA CA A1002 1555 1555 2.23 LINK OD1 ASN A 60 CA CA A1002 1555 1555 2.69 LINK O THR A 62 CA CA A1002 1555 1555 2.42 LINK OE1 GLU A 67 CA CA A1002 1555 1555 2.66 LINK OE2 GLU A 67 CA CA A1002 1555 1555 2.49 LINK OD1 ASP A 93 CA CA A1004 1555 1555 2.23 LINK OD1 ASP A 95 CA CA A1004 1555 1555 2.14 LINK OD1 ASN A 97 CA CA A1004 1555 1555 2.34 LINK O TYR A 99 CA CA A1004 1555 1555 2.04 LINK OE1 GLU A 104 CA CA A1004 1555 1555 2.81 LINK OE2 GLU A 104 CA CA A1004 1555 1555 2.42 LINK OD1 ASP A 129 CA CA A1003 1555 1555 2.34 LINK OD2 ASP A 131 CA CA A1003 1555 1555 2.15 LINK OD1 ASP A 133 CA CA A1003 1555 1555 2.25 LINK O GLN A 135 CA CA A1003 1555 1555 2.28 LINK OE1 GLU A 140 CA CA A1003 1555 1555 2.55 LINK OE2 GLU A 140 CA CA A1003 1555 1555 2.98 LINK CA CA A1001 O HOH A1107 1555 1555 2.27 LINK CA CA A1002 O HOH A1101 1555 1555 2.00 LINK CA CA A1003 O HOH A1106 1555 1555 2.19 LINK CA CA A1004 O HOH A1103 1555 1555 2.36 CISPEP 1 GLU B 1823 PRO B 1824 0 8.42 CISPEP 2 LYS B 1829 PRO B 1830 0 -2.26 SITE 1 AC1 6 ASP A 20 ASP A 22 ASP A 24 THR A 26 SITE 2 AC1 6 GLU A 31 HOH A1107 SITE 1 AC2 6 ASP A 56 ASP A 58 ASN A 60 THR A 62 SITE 2 AC2 6 GLU A 67 HOH A1101 SITE 1 AC3 6 ASP A 129 ASP A 131 ASP A 133 GLN A 135 SITE 2 AC3 6 GLU A 140 HOH A1106 SITE 1 AC4 6 ASP A 93 ASP A 95 ASN A 97 TYR A 99 SITE 2 AC4 6 GLU A 104 HOH A1103 CRYST1 65.579 84.032 140.684 90.00 90.00 90.00 I 2 2 2 8 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 0.015249 0.000000 0.000000 0.00000 SCALE2 0.000000 0.011900 0.000000 0.00000 SCALE3 0.000000 0.000000 0.007108 0.00000 ATOM 1 N ALA A 1 -22.693 -0.345 -37.586 1.00100.40 N ANISOU 1 N ALA A 1 11181 11747 15220 717 9 -990 N ATOM 2 CA ALA A 1 -23.499 0.599 -38.428 1.00103.61 C ANISOU 2 CA ALA A 1 11499 12044 15823 755 -106 -998 C ATOM 3 C ALA A 1 -23.443 0.176 -39.907 1.00105.21 C ANISOU 3 C ALA A 1 11743 12118 16112 521 -137 -785 C ATOM 4 O ALA A 1 -22.369 -0.161 -40.437 1.00 99.09 O ANISOU 4 O ALA A 1 11093 11217 15337 386 -159 -705 O ATOM 5 CB ALA A 1 -23.005 2.015 -38.240 1.00101.34 C ANISOU 5 CB ALA A 1 11234 11547 15720 918 -302 -1189 C ATOM 6 N ASP A 2 -24.616 0.182 -40.560 1.00107.53 N ANISOU 6 N ASP A 2 11920 12472 16462 489 -140 -701 N ATOM 7 CA ASP A 2 -24.712 0.132 -42.019 1.00105.84 C ANISOU 7 CA ASP A 2 11726 12149 16339 322 -222 -539 C ATOM 8 C ASP A 2 -25.169 1.500 -42.530 1.00103.77 C ANISOU 8 C ASP A 2 11381 11755 16291 421 -389 -559 C ATOM 9 O ASP A 2 -26.136 1.603 -43.277 1.00101.57 O ANISOU 9 O ASP A 2 11003 11510 16078 383 -433 -466 O ATOM 10 CB ASP A 2 -25.658 -0.962 -42.523 1.00107.65 C ANISOU 10 CB ASP A 2 11888 12521 16492 182 -144 -408 C ATOM 11 CG ASP A 2 -25.680 -1.070 -44.044 1.00108.22 C ANISOU 11 CG ASP A 2 11999 12510 16610 25 -244 -273 C ATOM 12 OD1 ASP A 2 -24.694 -0.629 -44.685 1.00107.34 O ANISOU 12 OD1 ASP A 2 11989 12267 16526 -11 -321 -240 O ATOM 13 OD2 ASP A 2 -26.685 -1.578 -44.583 1.00108.76 O ANISOU 13 OD2 ASP A 2 11980 12664 16679 -55 -253 -193 O ATOM 14 N GLN A 3 -24.445 2.542 -42.112 1.00103.59 N ANISOU 14 N GLN A 3 11394 11564 16401 544 -507 -677 N ATOM 15 CA GLN A 3 -24.569 3.876 -42.663 1.00102.28 C ANISOU 15 CA GLN A 3 11167 11192 16501 613 -712 -667 C ATOM 16 C GLN A 3 -23.318 4.172 -43.496 1.00 95.04 C ANISOU 16 C GLN A 3 10349 10081 15679 470 -819 -508 C ATOM 17 O GLN A 3 -23.097 5.318 -43.892 1.00 96.17 O ANISOU 17 O GLN A 3 10449 10010 16078 504 -1015 -457 O ATOM 18 CB GLN A 3 -24.758 4.886 -41.533 1.00107.93 C ANISOU 18 CB GLN A 3 11823 11840 17346 878 -804 -932 C ATOM 19 CG GLN A 3 -25.974 4.590 -40.665 1.00111.22 C ANISOU 19 CG GLN A 3 12112 12518 17628 1048 -667 -1078 C ATOM 20 CD GLN A 3 -26.012 5.447 -39.424 1.00115.77 C ANISOU 20 CD GLN A 3 12647 13090 18251 1347 -735 -1395 C ATOM 21 OE1 GLN A 3 -26.260 4.958 -38.323 1.00117.21 O ANISOU 21 OE1 GLN A 3 12799 13532 18201 1482 -579 -1540 O ATOM 22 NE2 GLN A 3 -25.755 6.736 -39.593 1.00116.81 N ANISOU 22 NE2 GLN A 3 12769 12929 18685 1461 -983 -1503 N ATOM 23 N LEU A 4 -22.539 3.117 -43.779 1.00 85.55 N ANISOU 23 N LEU A 4 9259 8964 14283 314 -694 -411 N ATOM 24 CA LEU A 4 -21.239 3.225 -44.401 1.00 81.17 C ANISOU 24 CA LEU A 4 8784 8293 13764 196 -746 -269 C ATOM 25 C LEU A 4 -21.383 3.161 -45.920 1.00 78.56 C ANISOU 25 C LEU A 4 8428 8003 13416 50 -780 -20 C ATOM 26 O LEU A 4 -21.888 2.202 -46.466 1.00 77.36 O ANISOU 26 O LEU A 4 8295 8020 13078 -35 -679 24 O ATOM 27 CB LEU A 4 -20.326 2.112 -43.890 1.00 79.35 C ANISOU 27 CB LEU A 4 8672 8149 13327 137 -592 -314 C ATOM 28 CG LEU A 4 -19.612 2.429 -42.579 1.00 81.52 C ANISOU 28 CG LEU A 4 8987 8343 13641 259 -616 -500 C ATOM 29 CD1 LEU A 4 -20.621 2.683 -41.468 1.00 83.58 C ANISOU 29 CD1 LEU A 4 9183 8687 13887 448 -602 -719 C ATOM 30 CD2 LEU A 4 -18.647 1.312 -42.199 1.00 79.64 C ANISOU 30 CD2 LEU A 4 8858 8185 13215 184 -478 -498 C ATOM 31 N THR A 5 -20.940 4.238 -46.567 1.00 80.00 N ANISOU 31 N THR A 5 8557 8028 13810 29 -947 143 N ATOM 32 CA THR A 5 -20.814 4.345 -48.000 1.00 79.12 C ANISOU 32 CA THR A 5 8411 7978 13672 -100 -994 423 C ATOM 33 C THR A 5 -19.781 3.335 -48.493 1.00 76.59 C ANISOU 33 C THR A 5 8189 7807 13104 -215 -851 505 C ATOM 34 O THR A 5 -19.028 2.796 -47.697 1.00 75.21 O ANISOU 34 O THR A 5 8097 7616 12861 -199 -756 375 O ATOM 35 CB THR A 5 -20.377 5.763 -48.370 1.00 80.79 C ANISOU 35 CB THR A 5 8524 7968 14203 -98 -1212 615 C ATOM 36 OG1 THR A 5 -19.264 6.044 -47.519 1.00 79.40 O ANISOU 36 OG1 THR A 5 8390 7628 14149 -65 -1243 528 O ATOM 37 CG2 THR A 5 -21.477 6.787 -48.192 1.00 82.63 C ANISOU 37 CG2 THR A 5 8643 8049 14704 18 -1386 564 C ATOM 38 N GLU A 6 -19.729 3.139 -49.811 1.00 77.61 N ANISOU 38 N GLU A 6 8299 8091 13098 -313 -849 721 N ATOM 39 CA GLU A 6 -18.850 2.152 -50.420 1.00 79.05 C ANISOU 39 CA GLU A 6 8561 8456 13016 -389 -714 774 C ATOM 40 C GLU A 6 -17.389 2.580 -50.258 1.00 79.22 C ANISOU 40 C GLU A 6 8574 8394 13132 -408 -716 895 C ATOM 41 O GLU A 6 -16.563 1.767 -49.864 1.00 79.99 O ANISOU 41 O GLU A 6 8755 8535 13101 -411 -591 796 O ATOM 42 CB GLU A 6 -19.221 1.941 -51.887 1.00 83.03 C ANISOU 42 CB GLU A 6 9032 9186 13327 -454 -731 953 C ATOM 43 CG GLU A 6 -20.660 1.488 -52.083 1.00 84.94 C ANISOU 43 CG GLU A 6 9271 9503 13496 -449 -755 840 C ATOM 44 CD GLU A 6 -21.128 0.368 -51.160 1.00 85.24 C ANISOU 44 CD GLU A 6 9394 9531 13460 -427 -645 564 C ATOM 45 OE1 GLU A 6 -22.303 0.409 -50.731 1.00 84.93 O ANISOU 45 OE1 GLU A 6 9303 9456 13509 -396 -681 474 O ATOM 46 OE2 GLU A 6 -20.322 -0.548 -50.872 1.00 84.85 O ANISOU 46 OE2 GLU A 6 9444 9516 13276 -440 -526 463 O ATOM 47 N GLU A 7 -17.095 3.855 -50.543 1.00 80.74 N ANISOU 47 N GLU A 7 8649 8448 13580 -426 -876 1123 N ATOM 48 CA GLU A 7 -15.754 4.422 -50.383 1.00 79.78 C ANISOU 48 CA GLU A 7 8477 8210 13625 -461 -922 1282 C ATOM 49 C GLU A 7 -15.172 4.033 -49.016 1.00 76.48 C ANISOU 49 C GLU A 7 8155 7654 13251 -400 -869 1012 C ATOM 50 O GLU A 7 -14.019 3.625 -48.935 1.00 76.00 O ANISOU 50 O GLU A 7 8115 7636 13123 -434 -787 1057 O ATOM 51 CB GLU A 7 -15.784 5.944 -50.541 1.00 82.83 C ANISOU 51 CB GLU A 7 8713 8360 14396 -477 -1165 1512 C ATOM 52 CG GLU A 7 -14.456 6.610 -50.198 1.00 86.46 C ANISOU 52 CG GLU A 7 9102 8634 15114 -522 -1261 1663 C ATOM 53 CD GLU A 7 -14.195 8.001 -50.772 1.00 91.68 C ANISOU 53 CD GLU A 7 9575 9107 16152 -595 -1503 2036 C ATOM 54 OE1 GLU A 7 -15.160 8.779 -50.961 1.00 91.32 O ANISOU 54 OE1 GLU A 7 9463 8925 16307 -565 -1671 2078 O ATOM 55 OE2 GLU A 7 -13.009 8.315 -51.019 1.00 95.58 O ANISOU 55 OE2 GLU A 7 9969 9582 16765 -686 -1534 2307 O ATOM 56 N GLN A 8 -15.974 4.176 -47.955 1.00 74.52 N ANISOU 56 N GLN A 8 7947 7266 13100 -298 -917 743 N ATOM 57 CA GLN A 8 -15.534 3.949 -46.572 1.00 72.99 C ANISOU 57 CA GLN A 8 7831 6960 12941 -217 -894 486 C ATOM 58 C GLN A 8 -15.340 2.457 -46.298 1.00 69.87 C ANISOU 58 C GLN A 8 7555 6758 12231 -231 -673 352 C ATOM 59 O GLN A 8 -14.387 2.056 -45.628 1.00 68.10 O ANISOU 59 O GLN A 8 7387 6507 11979 -224 -622 281 O ATOM 60 CB GLN A 8 -16.566 4.474 -45.580 1.00 74.90 C ANISOU 60 CB GLN A 8 8065 7078 13313 -75 -987 236 C ATOM 61 CG GLN A 8 -16.736 5.982 -45.640 1.00 78.59 C ANISOU 61 CG GLN A 8 8419 7287 14153 -26 -1246 303 C ATOM 62 CD GLN A 8 -17.818 6.463 -44.707 1.00 80.02 C ANISOU 62 CD GLN A 8 8582 7382 14436 154 -1327 18 C ATOM 63 OE1 GLN A 8 -17.632 7.429 -43.974 1.00 82.24 O ANISOU 63 OE1 GLN A 8 8832 7426 14990 269 -1524 -126 O ATOM 64 NE2 GLN A 8 -18.955 5.786 -44.723 1.00 78.54 N ANISOU 64 NE2 GLN A 8 8406 7395 14039 191 -1185 -73 N ATOM 65 N ILE A 9 -16.279 1.644 -46.782 1.00 68.23 N ANISOU 65 N ILE A 9 7380 6725 11820 -249 -569 315 N ATOM 66 CA ILE A 9 -16.163 0.207 -46.667 1.00 65.95 C ANISOU 66 CA ILE A 9 7190 6586 11281 -275 -397 211 C ATOM 67 C ILE A 9 -14.847 -0.228 -47.318 1.00 66.46 C ANISOU 67 C ILE A 9 7277 6726 11246 -336 -328 342 C ATOM 68 O ILE A 9 -14.159 -1.093 -46.787 1.00 68.54 O ANISOU 68 O ILE A 9 7615 7008 11417 -328 -228 246 O ATOM 69 CB ILE A 9 -17.377 -0.495 -47.299 1.00 66.07 C ANISOU 69 CB ILE A 9 7211 6747 11145 -304 -351 183 C ATOM 70 CG1 ILE A 9 -18.629 -0.299 -46.442 1.00 65.07 C ANISOU 70 CG1 ILE A 9 7046 6584 11094 -232 -376 42 C ATOM 71 CG2 ILE A 9 -17.082 -1.971 -47.560 1.00 66.03 C ANISOU 71 CG2 ILE A 9 7298 6870 10918 -351 -219 119 C ATOM 72 CD1 ILE A 9 -19.923 -0.537 -47.188 1.00 65.02 C ANISOU 72 CD1 ILE A 9 6988 6682 11032 -266 -395 73 C ATOM 73 N ALA A 10 -14.515 0.373 -48.468 1.00 66.27 N ANISOU 73 N ALA A 10 7171 6765 11240 -387 -378 578 N ATOM 74 CA ALA A 10 -13.257 0.088 -49.166 1.00 65.77 C ANISOU 74 CA ALA A 10 7087 6826 11074 -427 -303 738 C ATOM 75 C ALA A 10 -12.077 0.614 -48.339 1.00 64.85 C ANISOU 75 C ALA A 10 6938 6541 11160 -423 -348 777 C ATOM 76 O ALA A 10 -11.054 -0.051 -48.207 1.00 66.28 O ANISOU 76 O ALA A 10 7147 6781 11254 -422 -248 767 O ATOM 77 CB ALA A 10 -13.273 0.674 -50.558 1.00 66.96 C ANISOU 77 CB ALA A 10 7129 7134 11176 -476 -344 1020 C ATOM 78 N GLU A 11 -12.235 1.810 -47.779 1.00 65.27 N ANISOU 78 N GLU A 11 6926 6370 11502 -412 -522 806 N ATOM 79 CA GLU A 11 -11.214 2.395 -46.950 1.00 66.64 C ANISOU 79 CA GLU A 11 7065 6348 11906 -408 -620 815 C ATOM 80 C GLU A 11 -10.836 1.385 -45.862 1.00 63.86 C ANISOU 80 C GLU A 11 6837 6004 11423 -352 -510 564 C ATOM 81 O GLU A 11 -9.682 1.057 -45.696 1.00 63.94 O ANISOU 81 O GLU A 11 6841 6024 11428 -373 -464 614 O ATOM 82 CB GLU A 11 -11.703 3.727 -46.380 1.00 69.90 C ANISOU 82 CB GLU A 11 7417 6491 12651 -368 -856 779 C ATOM 83 CG GLU A 11 -10.593 4.724 -46.116 1.00 73.93 C ANISOU 83 CG GLU A 11 7821 6776 13491 -409 -1043 930 C ATOM 84 CD GLU A 11 -10.960 6.187 -46.347 1.00 79.12 C ANISOU 84 CD GLU A 11 8351 7186 14525 -421 -1309 1075 C ATOM 85 OE1 GLU A 11 -12.152 6.487 -46.618 1.00 78.52 O ANISOU 85 OE1 GLU A 11 8273 7108 14453 -376 -1350 1029 O ATOM 86 OE2 GLU A 11 -10.037 7.031 -46.270 1.00 85.01 O ANISOU 86 OE2 GLU A 11 8983 7724 15591 -481 -1494 1251 O ATOM 87 N PHE A 12 -11.829 0.851 -45.155 1.00 63.15 N ANISOU 87 N PHE A 12 6840 5930 11221 -285 -462 323 N ATOM 88 CA PHE A 12 -11.555 -0.040 -44.035 1.00 63.48 C ANISOU 88 CA PHE A 12 6982 5983 11153 -234 -375 122 C ATOM 89 C PHE A 12 -10.976 -1.377 -44.518 1.00 64.68 C ANISOU 89 C PHE A 12 7190 6295 11088 -276 -201 153 C ATOM 90 O PHE A 12 -10.203 -2.034 -43.787 1.00 64.05 O ANISOU 90 O PHE A 12 7163 6204 10970 -256 -147 80 O ATOM 91 CB PHE A 12 -12.822 -0.273 -43.217 1.00 63.79 C ANISOU 91 CB PHE A 12 7070 6045 11120 -155 -357 -86 C ATOM 92 CG PHE A 12 -13.323 0.950 -42.502 1.00 65.42 C ANISOU 92 CG PHE A 12 7228 6103 11524 -59 -526 -195 C ATOM 93 CD1 PHE A 12 -12.455 1.767 -41.793 1.00 65.82 C ANISOU 93 CD1 PHE A 12 7260 5978 11768 -13 -680 -244 C ATOM 94 CD2 PHE A 12 -14.667 1.273 -42.522 1.00 66.51 C ANISOU 94 CD2 PHE A 12 7331 6270 11666 0 -548 -270 C ATOM 95 CE1 PHE A 12 -12.923 2.886 -41.126 1.00 66.50 C ANISOU 95 CE1 PHE A 12 7307 5909 12049 103 -867 -398 C ATOM 96 CE2 PHE A 12 -15.130 2.400 -41.862 1.00 67.52 C ANISOU 96 CE2 PHE A 12 7409 6262 11982 123 -711 -407 C ATOM 97 CZ PHE A 12 -14.259 3.198 -41.160 1.00 67.48 C ANISOU 97 CZ PHE A 12 7400 6072 12167 182 -876 -488 C ATOM 98 N LYS A 13 -11.360 -1.785 -45.734 1.00 64.84 N ANISOU 98 N LYS A 13 7201 6465 10971 -318 -130 244 N ATOM 99 CA LYS A 13 -10.815 -2.981 -46.349 1.00 63.65 C ANISOU 99 CA LYS A 13 7096 6464 10625 -330 7 244 C ATOM 100 C LYS A 13 -9.302 -2.821 -46.589 1.00 64.46 C ANISOU 100 C LYS A 13 7133 6588 10770 -338 32 392 C ATOM 101 O LYS A 13 -8.552 -3.759 -46.373 1.00 62.35 O ANISOU 101 O LYS A 13 6909 6359 10420 -311 125 327 O ATOM 102 CB LYS A 13 -11.538 -3.303 -47.657 1.00 65.17 C ANISOU 102 CB LYS A 13 7282 6827 10651 -351 42 289 C ATOM 103 CG LYS A 13 -12.034 -4.738 -47.774 1.00 67.02 C ANISOU 103 CG LYS A 13 7616 7137 10710 -339 124 112 C ATOM 104 CD LYS A 13 -11.138 -5.769 -47.110 1.00 67.56 C ANISOU 104 CD LYS A 13 7750 7164 10755 -308 205 10 C ATOM 105 CE LYS A 13 -11.552 -7.191 -47.407 1.00 67.55 C ANISOU 105 CE LYS A 13 7832 7206 10627 -298 250 -144 C ATOM 106 NZ LYS A 13 -11.232 -7.559 -48.805 1.00 70.26 N ANISOU 106 NZ LYS A 13 8166 7731 10796 -262 283 -141 N ATOM 107 N GLU A 14 -8.849 -1.638 -47.033 1.00 65.24 N ANISOU 107 N GLU A 14 7107 6655 11026 -377 -59 611 N ATOM 108 CA GLU A 14 -7.416 -1.413 -47.242 1.00 66.79 C ANISOU 108 CA GLU A 14 7200 6879 11297 -398 -43 799 C ATOM 109 C GLU A 14 -6.638 -1.823 -45.985 1.00 63.24 C ANISOU 109 C GLU A 14 6805 6293 10930 -367 -49 659 C ATOM 110 O GLU A 14 -5.605 -2.495 -46.074 1.00 66.43 O ANISOU 110 O GLU A 14 7189 6781 11269 -349 48 692 O ATOM 111 CB GLU A 14 -7.099 0.051 -47.541 1.00 72.44 C ANISOU 111 CB GLU A 14 7757 7493 12273 -465 -200 1069 C ATOM 112 CG GLU A 14 -7.351 0.474 -48.973 1.00 76.68 C ANISOU 112 CG GLU A 14 8180 8230 12723 -509 -180 1336 C ATOM 113 CD GLU A 14 -6.912 1.905 -49.229 1.00 81.24 C ANISOU 113 CD GLU A 14 8571 8681 13613 -595 -354 1664 C ATOM 114 OE1 GLU A 14 -5.682 2.134 -49.337 1.00 82.65 O ANISOU 114 OE1 GLU A 14 8615 8885 13901 -638 -349 1886 O ATOM 115 OE2 GLU A 14 -7.798 2.794 -49.279 1.00 85.23 O ANISOU 115 OE2 GLU A 14 9054 9043 14286 -618 -510 1704 O ATOM 116 N ALA A 15 -7.141 -1.400 -44.821 1.00 57.86 N ANISOU 116 N ALA A 15 6182 5419 10380 -345 -167 499 N ATOM 117 CA ALA A 15 -6.503 -1.652 -43.541 1.00 54.68 C ANISOU 117 CA ALA A 15 5830 4901 10043 -307 -205 364 C ATOM 118 C ALA A 15 -6.670 -3.120 -43.124 1.00 52.42 C ANISOU 118 C ALA A 15 5665 4709 9541 -264 -56 199 C ATOM 119 O ALA A 15 -5.737 -3.713 -42.596 1.00 51.16 O ANISOU 119 O ALA A 15 5520 4539 9378 -246 -22 180 O ATOM 120 CB ALA A 15 -7.071 -0.727 -42.499 1.00 54.20 C ANISOU 120 CB ALA A 15 5789 4658 10144 -266 -382 225 C ATOM 121 N PHE A 16 -7.863 -3.693 -43.330 1.00 51.18 N ANISOU 121 N PHE A 16 5581 4625 9237 -254 10 95 N ATOM 122 CA PHE A 16 -8.085 -5.105 -42.985 1.00 49.97 C ANISOU 122 CA PHE A 16 5525 4530 8931 -232 122 -28 C ATOM 123 C PHE A 16 -7.047 -5.967 -43.708 1.00 50.25 C ANISOU 123 C PHE A 16 5549 4648 8895 -225 222 27 C ATOM 124 O PHE A 16 -6.491 -6.853 -43.105 1.00 49.97 O ANISOU 124 O PHE A 16 5558 4585 8844 -197 263 -33 O ATOM 125 CB PHE A 16 -9.503 -5.570 -43.316 1.00 48.34 C ANISOU 125 CB PHE A 16 5364 4384 8616 -244 158 -106 C ATOM 126 CG PHE A 16 -9.845 -6.951 -42.815 1.00 47.07 C ANISOU 126 CG PHE A 16 5281 4235 8365 -241 229 -207 C ATOM 127 CD1 PHE A 16 -10.216 -7.159 -41.495 1.00 46.32 C ANISOU 127 CD1 PHE A 16 5213 4106 8278 -220 217 -269 C ATOM 128 CD2 PHE A 16 -9.810 -8.048 -43.666 1.00 47.07 C ANISOU 128 CD2 PHE A 16 5317 4288 8280 -252 293 -235 C ATOM 129 CE1 PHE A 16 -10.544 -8.427 -41.039 1.00 45.30 C ANISOU 129 CE1 PHE A 16 5128 3985 8096 -237 270 -300 C ATOM 130 CE2 PHE A 16 -10.124 -9.317 -43.207 1.00 45.74 C ANISOU 130 CE2 PHE A 16 5206 4081 8092 -261 320 -309 C ATOM 131 CZ PHE A 16 -10.491 -9.502 -41.894 1.00 45.53 C ANISOU 131 CZ PHE A 16 5189 4010 8099 -266 310 -314 C ATOM 132 N SER A 17 -6.789 -5.649 -44.983 1.00 52.55 N ANISOU 132 N SER A 17 5766 5057 9142 -237 256 152 N ATOM 133 CA SER A 17 -5.814 -6.337 -45.845 1.00 54.19 C ANISOU 133 CA SER A 17 5933 5408 9248 -196 364 203 C ATOM 134 C SER A 17 -4.377 -6.150 -45.343 1.00 55.51 C ANISOU 134 C SER A 17 6019 5531 9539 -183 361 304 C ATOM 135 O SER A 17 -3.559 -7.054 -45.467 1.00 55.56 O ANISOU 135 O SER A 17 6021 5599 9487 -122 449 270 O ATOM 136 CB SER A 17 -5.925 -5.863 -47.267 1.00 55.71 C ANISOU 136 CB SER A 17 6040 5793 9332 -200 397 343 C ATOM 137 OG SER A 17 -7.154 -6.276 -47.834 1.00 57.02 O ANISOU 137 OG SER A 17 6283 6021 9358 -200 399 227 O ATOM 138 N LEU A 18 -4.055 -4.956 -44.838 1.00 57.12 N ANISOU 138 N LEU A 18 6145 5621 9935 -234 242 426 N ATOM 139 CA LEU A 18 -2.729 -4.715 -44.280 1.00 58.86 C ANISOU 139 CA LEU A 18 6278 5775 10311 -237 201 524 C ATOM 140 C LEU A 18 -2.376 -5.884 -43.354 1.00 57.61 C ANISOU 140 C LEU A 18 6219 5565 10106 -181 244 359 C ATOM 141 O LEU A 18 -1.301 -6.463 -43.474 1.00 58.74 O ANISOU 141 O LEU A 18 6303 5763 10250 -140 313 407 O ATOM 142 CB LEU A 18 -2.703 -3.386 -43.519 1.00 60.62 C ANISOU 142 CB LEU A 18 6450 5804 10777 -294 3 581 C ATOM 143 CG LEU A 18 -1.488 -2.493 -43.773 1.00 63.67 C ANISOU 143 CG LEU A 18 6648 6155 11385 -351 -82 835 C ATOM 144 CD1 LEU A 18 -1.532 -1.266 -42.876 1.00 66.00 C ANISOU 144 CD1 LEU A 18 6917 6197 11959 -394 -331 822 C ATOM 145 CD2 LEU A 18 -0.184 -3.240 -43.568 1.00 63.81 C ANISOU 145 CD2 LEU A 18 6608 6233 11402 -318 -3 879 C ATOM 146 N PHE A 19 -3.312 -6.226 -42.462 1.00 55.42 N ANISOU 146 N PHE A 19 6071 5198 9787 -174 206 188 N ATOM 147 CA PHE A 19 -3.147 -7.291 -41.485 1.00 55.36 C ANISOU 147 CA PHE A 19 6151 5139 9743 -135 228 70 C ATOM 148 C PHE A 19 -3.261 -8.684 -42.131 1.00 56.47 C ANISOU 148 C PHE A 19 6344 5354 9758 -92 353 0 C ATOM 149 O PHE A 19 -2.411 -9.545 -41.914 1.00 58.21 O ANISOU 149 O PHE A 19 6561 5559 9997 -44 392 -13 O ATOM 150 CB PHE A 19 -4.218 -7.175 -40.402 1.00 54.44 C ANISOU 150 CB PHE A 19 6125 4959 9599 -139 159 -47 C ATOM 151 CG PHE A 19 -4.084 -5.991 -39.488 1.00 54.04 C ANISOU 151 CG PHE A 19 6047 4820 9663 -136 6 -60 C ATOM 152 CD1 PHE A 19 -3.079 -5.945 -38.537 1.00 54.74 C ANISOU 152 CD1 PHE A 19 6120 4847 9831 -113 -78 -60 C ATOM 153 CD2 PHE A 19 -4.984 -4.938 -39.553 1.00 55.05 C ANISOU 153 CD2 PHE A 19 6165 4918 9831 -142 -75 -95 C ATOM 154 CE1 PHE A 19 -2.957 -4.853 -37.689 1.00 55.95 C ANISOU 154 CE1 PHE A 19 6254 4908 10095 -94 -256 -117 C ATOM 155 CE2 PHE A 19 -4.870 -3.853 -38.697 1.00 55.44 C ANISOU 155 CE2 PHE A 19 6194 4863 10006 -112 -247 -157 C ATOM 156 CZ PHE A 19 -3.856 -3.814 -37.766 1.00 55.78 C ANISOU 156 CZ PHE A 19 6229 4844 10120 -86 -345 -180 C ATOM 157 N ASP A 20 -4.332 -8.904 -42.899 1.00 55.89 N ANISOU 157 N ASP A 20 6316 5340 9576 -104 392 -61 N ATOM 158 CA ASP A 20 -4.686 -10.216 -43.418 1.00 56.48 C ANISOU 158 CA ASP A 20 6458 5441 9560 -66 457 -178 C ATOM 159 C ASP A 20 -3.841 -10.504 -44.667 1.00 58.20 C ANISOU 159 C ASP A 20 6610 5803 9700 11 543 -165 C ATOM 160 O ASP A 20 -4.318 -10.484 -45.810 1.00 57.01 O ANISOU 160 O ASP A 20 6453 5787 9420 31 578 -194 O ATOM 161 CB ASP A 20 -6.197 -10.302 -43.651 1.00 55.76 C ANISOU 161 CB ASP A 20 6431 5350 9403 -115 433 -252 C ATOM 162 CG ASP A 20 -6.635 -11.538 -44.413 1.00 55.43 C ANISOU 162 CG ASP A 20 6447 5321 9293 -85 456 -383 C ATOM 163 OD1 ASP A 20 -6.121 -12.622 -44.101 1.00 53.96 O ANISOU 163 OD1 ASP A 20 6292 5051 9158 -41 461 -448 O ATOM 164 OD2 ASP A 20 -7.483 -11.391 -45.320 1.00 57.08 O ANISOU 164 OD2 ASP A 20 6665 5611 9413 -101 446 -423 O ATOM 165 N LYS A 21 -2.573 -10.826 -44.412 1.00 60.05 N ANISOU 165 N LYS A 21 6786 6031 9998 71 576 -126 N ATOM 166 CA LYS A 21 -1.586 -10.995 -45.446 1.00 63.30 C ANISOU 166 CA LYS A 21 7094 6619 10337 169 674 -89 C ATOM 167 C LYS A 21 -1.727 -12.368 -46.117 1.00 64.84 C ANISOU 167 C LYS A 21 7358 6850 10429 287 721 -300 C ATOM 168 O LYS A 21 -1.332 -12.518 -47.279 1.00 66.37 O ANISOU 168 O LYS A 21 7485 7257 10473 397 808 -332 O ATOM 169 CB LYS A 21 -0.191 -10.773 -44.858 1.00 65.97 C ANISOU 169 CB LYS A 21 7321 6934 10811 190 680 41 C ATOM 170 CG LYS A 21 0.458 -9.462 -45.274 1.00 68.92 C ANISOU 170 CG LYS A 21 7527 7426 11232 142 684 282 C ATOM 171 CD LYS A 21 1.220 -8.753 -44.180 1.00 69.81 C ANISOU 171 CD LYS A 21 7572 7392 11560 72 577 412 C ATOM 172 CE LYS A 21 1.643 -7.368 -44.617 1.00 71.73 C ANISOU 172 CE LYS A 21 7646 7699 11907 -6 533 665 C ATOM 173 NZ LYS A 21 1.258 -6.351 -43.615 1.00 72.78 N ANISOU 173 NZ LYS A 21 7814 7618 12219 -112 346 684 N ATOM 174 N ASP A 22 -2.282 -13.359 -45.404 1.00 64.00 N ANISOU 174 N ASP A 22 7368 6544 10402 273 653 -439 N ATOM 175 CA ASP A 22 -2.502 -14.689 -45.997 1.00 65.65 C ANISOU 175 CA ASP A 22 7646 6718 10577 376 643 -661 C ATOM 176 C ASP A 22 -3.829 -14.699 -46.761 1.00 66.56 C ANISOU 176 C ASP A 22 7834 6878 10577 335 599 -768 C ATOM 177 O ASP A 22 -4.166 -15.684 -47.393 1.00 69.33 O ANISOU 177 O ASP A 22 8244 7202 10895 414 556 -975 O ATOM 178 CB ASP A 22 -2.447 -15.819 -44.965 1.00 65.92 C ANISOU 178 CB ASP A 22 7748 6498 10799 371 563 -724 C ATOM 179 CG ASP A 22 -3.391 -15.651 -43.786 1.00 65.39 C ANISOU 179 CG ASP A 22 7742 6277 10824 216 483 -629 C ATOM 180 OD1 ASP A 22 -4.192 -14.693 -43.806 1.00 64.83 O ANISOU 180 OD1 ASP A 22 7674 6280 10676 125 483 -561 O ATOM 181 OD2 ASP A 22 -3.312 -16.472 -42.847 1.00 66.48 O ANISOU 181 OD2 ASP A 22 7911 6240 11106 196 421 -612 O ATOM 182 N GLY A 23 -4.590 -13.602 -46.684 1.00 66.80 N ANISOU 182 N GLY A 23 7855 6958 10567 217 587 -639 N ATOM 183 CA GLY A 23 -5.832 -13.451 -47.450 1.00 66.77 C ANISOU 183 CA GLY A 23 7896 7020 10452 173 543 -708 C ATOM 184 C GLY A 23 -6.901 -14.491 -47.109 1.00 65.98 C ANISOU 184 C GLY A 23 7896 6726 10446 122 435 -854 C ATOM 185 O GLY A 23 -7.834 -14.669 -47.877 1.00 67.83 O ANISOU 185 O GLY A 23 8166 7003 10602 109 376 -958 O ATOM 186 N ASP A 24 -6.801 -15.148 -45.944 1.00 62.88 N ANISOU 186 N ASP A 24 7532 6126 10231 80 395 -833 N ATOM 187 CA ASP A 24 -7.771 -16.159 -45.540 1.00 61.71 C ANISOU 187 CA ASP A 24 7444 5785 10217 10 284 -905 C ATOM 188 C ASP A 24 -9.045 -15.500 -44.986 1.00 61.25 C ANISOU 188 C ASP A 24 7376 5726 10167 -130 257 -784 C ATOM 189 O ASP A 24 -10.018 -16.191 -44.717 1.00 64.15 O ANISOU 189 O ASP A 24 7761 5973 10640 -211 170 -798 O ATOM 190 CB ASP A 24 -7.171 -17.168 -44.558 1.00 61.09 C ANISOU 190 CB ASP A 24 7377 5504 10328 21 246 -884 C ATOM 191 CG ASP A 24 -6.840 -16.663 -43.167 1.00 59.58 C ANISOU 191 CG ASP A 24 7152 5290 10192 -43 284 -681 C ATOM 192 OD1 ASP A 24 -6.894 -15.438 -42.944 1.00 57.19 O ANISOU 192 OD1 ASP A 24 6818 5117 9791 -77 341 -581 O ATOM 193 OD2 ASP A 24 -6.491 -17.514 -42.317 1.00 61.67 O ANISOU 193 OD2 ASP A 24 7422 5403 10607 -49 239 -630 O ATOM 194 N GLY A 25 -9.032 -14.173 -44.810 1.00 58.83 N ANISOU 194 N GLY A 25 7027 5550 9775 -155 321 -663 N ATOM 195 CA GLY A 25 -10.220 -13.400 -44.455 1.00 56.52 C ANISOU 195 CA GLY A 25 6712 5290 9472 -248 300 -582 C ATOM 196 C GLY A 25 -10.396 -13.204 -42.955 1.00 55.22 C ANISOU 196 C GLY A 25 6526 5070 9382 -296 307 -466 C ATOM 197 O GLY A 25 -11.418 -12.635 -42.520 1.00 53.95 O ANISOU 197 O GLY A 25 6333 4953 9211 -349 298 -412 O ATOM 198 N THR A 26 -9.419 -13.666 -42.160 1.00 54.33 N ANISOU 198 N THR A 26 6423 4889 9331 -263 323 -430 N ATOM 199 CA THR A 26 -9.387 -13.362 -40.743 1.00 54.71 C ANISOU 199 CA THR A 26 6449 4939 9396 -281 330 -324 C ATOM 200 C THR A 26 -8.025 -12.777 -40.343 1.00 53.48 C ANISOU 200 C THR A 26 6283 4797 9239 -216 349 -296 C ATOM 201 O THR A 26 -7.004 -12.959 -41.001 1.00 55.98 O ANISOU 201 O THR A 26 6597 5098 9572 -163 369 -328 O ATOM 202 CB THR A 26 -9.711 -14.588 -39.889 1.00 56.36 C ANISOU 202 CB THR A 26 6659 5056 9699 -329 298 -253 C ATOM 203 OG1 THR A 26 -8.637 -15.506 -40.070 1.00 61.79 O ANISOU 203 OG1 THR A 26 7375 5625 10476 -282 280 -288 O ATOM 204 CG2 THR A 26 -11.020 -15.244 -40.259 1.00 58.25 C ANISOU 204 CG2 THR A 26 6883 5255 9994 -413 253 -253 C ATOM 205 N ILE A 27 -8.036 -12.060 -39.224 1.00 50.81 N ANISOU 205 N ILE A 27 5926 4502 8877 -211 333 -240 N ATOM 206 CA ILE A 27 -6.851 -11.570 -38.626 1.00 48.92 C ANISOU 206 CA ILE A 27 5672 4256 8660 -163 311 -213 C ATOM 207 C ILE A 27 -6.571 -12.428 -37.405 1.00 48.47 C ANISOU 207 C ILE A 27 5627 4174 8615 -158 293 -147 C ATOM 208 O ILE A 27 -7.408 -12.495 -36.518 1.00 47.16 O ANISOU 208 O ILE A 27 5454 4077 8384 -176 289 -105 O ATOM 209 CB ILE A 27 -6.991 -10.091 -38.219 1.00 47.24 C ANISOU 209 CB ILE A 27 5430 4096 8421 -142 261 -228 C ATOM 210 CG1 ILE A 27 -7.384 -9.208 -39.401 1.00 46.76 C ANISOU 210 CG1 ILE A 27 5341 4053 8369 -160 262 -246 C ATOM 211 CG2 ILE A 27 -5.710 -9.615 -37.555 1.00 47.10 C ANISOU 211 CG2 ILE A 27 5391 4045 8459 -100 197 -207 C ATOM 212 CD1 ILE A 27 -7.454 -7.724 -39.070 1.00 47.31 C ANISOU 212 CD1 ILE A 27 5371 4119 8482 -136 174 -260 C ATOM 213 N THR A 28 -5.368 -13.008 -37.364 1.00 50.02 N ANISOU 213 N THR A 28 5821 4297 8887 -125 285 -122 N ATOM 214 CA THR A 28 -4.883 -13.704 -36.191 1.00 51.46 C ANISOU 214 CA THR A 28 6003 4456 9091 -114 248 -34 C ATOM 215 C THR A 28 -3.965 -12.776 -35.399 1.00 51.03 C ANISOU 215 C THR A 28 5926 4449 9012 -66 188 -25 C ATOM 216 O THR A 28 -3.427 -11.827 -35.956 1.00 50.60 O ANISOU 216 O THR A 28 5844 4389 8990 -48 173 -72 O ATOM 217 CB THR A 28 -4.135 -14.977 -36.581 1.00 53.82 C ANISOU 217 CB THR A 28 6304 4621 9521 -95 248 -16 C ATOM 218 OG1 THR A 28 -2.863 -14.555 -37.082 1.00 54.50 O ANISOU 218 OG1 THR A 28 6357 4697 9652 -30 257 -52 O ATOM 219 CG2 THR A 28 -4.904 -15.800 -37.592 1.00 53.52 C ANISOU 219 CG2 THR A 28 6292 4503 9538 -124 267 -85 C ATOM 220 N THR A 29 -3.816 -13.080 -34.104 1.00 52.07 N ANISOU 220 N THR A 29 6059 4632 9092 -50 139 50 N ATOM 221 CA THR A 29 -2.949 -12.357 -33.183 1.00 52.96 C ANISOU 221 CA THR A 29 6156 4791 9174 2 45 43 C ATOM 222 C THR A 29 -1.545 -12.241 -33.776 1.00 52.77 C ANISOU 222 C THR A 29 6091 4657 9301 20 17 45 C ATOM 223 O THR A 29 -0.903 -11.221 -33.644 1.00 53.29 O ANISOU 223 O THR A 29 6123 4721 9404 40 -65 8 O ATOM 224 CB THR A 29 -2.820 -13.088 -31.845 1.00 55.58 C ANISOU 224 CB THR A 29 6489 5201 9425 20 2 158 C ATOM 225 OG1 THR A 29 -2.512 -14.442 -32.163 1.00 57.32 O ANISOU 225 OG1 THR A 29 6703 5301 9775 -13 36 270 O ATOM 226 CG2 THR A 29 -4.074 -13.061 -31.004 1.00 57.80 C ANISOU 226 CG2 THR A 29 6773 5670 9516 24 30 192 C ATOM 227 N LYS A 30 -1.087 -13.319 -34.414 1.00 52.81 N ANISOU 227 N LYS A 30 6084 4570 9409 19 75 90 N ATOM 228 CA LYS A 30 0.172 -13.340 -35.128 1.00 53.17 C ANISOU 228 CA LYS A 30 6064 4550 9585 58 85 96 C ATOM 229 C LYS A 30 0.237 -12.213 -36.175 1.00 52.49 C ANISOU 229 C LYS A 30 5932 4500 9511 47 117 50 C ATOM 230 O LYS A 30 1.231 -11.471 -36.216 1.00 54.02 O ANISOU 230 O LYS A 30 6043 4691 9791 57 64 93 O ATOM 231 CB LYS A 30 0.390 -14.698 -35.793 1.00 54.00 C ANISOU 231 CB LYS A 30 6170 4564 9781 91 150 96 C ATOM 232 CG LYS A 30 1.299 -14.671 -37.011 1.00 55.97 C ANISOU 232 CG LYS A 30 6345 4813 10107 156 219 54 C ATOM 233 CD LYS A 30 2.074 -15.949 -37.221 1.00 58.96 C ANISOU 233 CD LYS A 30 6694 5095 10610 243 232 46 C ATOM 234 CE LYS A 30 2.829 -15.962 -38.532 1.00 60.74 C ANISOU 234 CE LYS A 30 6835 5384 10859 343 330 -23 C ATOM 235 NZ LYS A 30 2.917 -17.340 -39.072 1.00 63.66 N ANISOU 235 NZ LYS A 30 7223 5653 11310 447 349 -136 N ATOM 236 N GLU A 31 -0.775 -12.120 -37.043 1.00 50.64 N ANISOU 236 N GLU A 31 5733 4296 9210 21 190 -9 N ATOM 237 CA GLU A 31 -0.808 -11.122 -38.117 1.00 50.92 C ANISOU 237 CA GLU A 31 5716 4383 9248 6 221 -16 C ATOM 238 C GLU A 31 -0.895 -9.692 -37.551 1.00 51.13 C ANISOU 238 C GLU A 31 5718 4409 9300 -25 108 -5 C ATOM 239 O GLU A 31 -0.366 -8.747 -38.132 1.00 48.20 O ANISOU 239 O GLU A 31 5258 4037 9016 -43 77 55 O ATOM 240 CB GLU A 31 -2.011 -11.339 -39.030 1.00 50.85 C ANISOU 240 CB GLU A 31 5759 4414 9147 -16 295 -84 C ATOM 241 CG GLU A 31 -1.823 -12.455 -40.027 1.00 51.76 C ANISOU 241 CG GLU A 31 5878 4531 9255 34 381 -135 C ATOM 242 CD GLU A 31 -3.086 -12.605 -40.902 1.00 53.23 C ANISOU 242 CD GLU A 31 6119 4757 9349 6 416 -220 C ATOM 243 OE1 GLU A 31 -4.207 -12.836 -40.323 1.00 52.73 O ANISOU 243 OE1 GLU A 31 6117 4653 9264 -51 382 -240 O ATOM 244 OE2 GLU A 31 -2.953 -12.659 -42.152 1.00 55.64 O ANISOU 244 OE2 GLU A 31 6396 5147 9597 51 477 -264 O ATOM 245 N LEU A 32 -1.605 -9.549 -36.430 1.00 51.56 N ANISOU 245 N LEU A 32 5838 4470 9281 -24 40 -64 N ATOM 246 CA LEU A 32 -1.680 -8.312 -35.721 1.00 52.25 C ANISOU 246 CA LEU A 32 5915 4547 9390 -15 -96 -114 C ATOM 247 C LEU A 32 -0.263 -7.943 -35.304 1.00 54.26 C ANISOU 247 C LEU A 32 6096 4736 9784 -5 -213 -59 C ATOM 248 O LEU A 32 0.231 -6.876 -35.659 1.00 61.12 O ANISOU 248 O LEU A 32 6884 5539 10797 -31 -309 -26 O ATOM 249 CB LEU A 32 -2.609 -8.483 -34.515 1.00 53.43 C ANISOU 249 CB LEU A 32 6139 4777 9384 23 -124 -195 C ATOM 250 CG LEU A 32 -2.786 -7.275 -33.600 1.00 54.22 C ANISOU 250 CG LEU A 32 6242 4893 9466 81 -282 -316 C ATOM 251 CD1 LEU A 32 -3.356 -6.101 -34.368 1.00 55.39 C ANISOU 251 CD1 LEU A 32 6360 4981 9703 67 -325 -372 C ATOM 252 CD2 LEU A 32 -3.683 -7.624 -32.422 1.00 54.55 C ANISOU 252 CD2 LEU A 32 6337 5095 9292 148 -270 -381 C ATOM 253 N GLY A 33 0.400 -8.840 -34.574 1.00 53.37 N ANISOU 253 N GLY A 33 5994 4629 9652 23 -219 -23 N ATOM 254 CA GLY A 33 1.755 -8.574 -34.102 1.00 52.85 C ANISOU 254 CA GLY A 33 5849 4506 9722 32 -344 33 C ATOM 255 C GLY A 33 2.692 -8.174 -35.237 1.00 52.81 C ANISOU 255 C GLY A 33 5710 4456 9898 -2 -314 150 C ATOM 256 O GLY A 33 3.546 -7.303 -35.060 1.00 52.51 O ANISOU 256 O GLY A 33 5572 4350 10026 -27 -459 204 O ATOM 257 N THR A 34 2.549 -8.834 -36.398 1.00 52.53 N ANISOU 257 N THR A 34 5657 4472 9827 0 -135 195 N ATOM 258 CA THR A 34 3.473 -8.667 -37.514 1.00 53.70 C ANISOU 258 CA THR A 34 5657 4656 10089 -4 -62 326 C ATOM 259 C THR A 34 3.415 -7.219 -38.018 1.00 55.56 C ANISOU 259 C THR A 34 5801 4872 10435 -74 -146 406 C ATOM 260 O THR A 34 4.457 -6.556 -38.181 1.00 59.19 O ANISOU 260 O THR A 34 6102 5306 11082 -110 -225 557 O ATOM 261 CB THR A 34 3.227 -9.703 -38.618 1.00 53.22 C ANISOU 261 CB THR A 34 5611 4688 9919 49 134 305 C ATOM 262 OG1 THR A 34 3.893 -10.913 -38.257 1.00 53.58 O ANISOU 262 OG1 THR A 34 5662 4711 9985 121 170 291 O ATOM 263 CG2 THR A 34 3.750 -9.280 -39.973 1.00 54.11 C ANISOU 263 CG2 THR A 34 5576 4924 10057 56 236 426 C ATOM 264 N VAL A 35 2.203 -6.713 -38.246 1.00 55.31 N ANISOU 264 N VAL A 35 5852 4841 10321 -100 -147 328 N ATOM 265 CA VAL A 35 2.049 -5.330 -38.708 1.00 56.67 C ANISOU 265 CA VAL A 35 5938 4963 10630 -166 -253 411 C ATOM 266 C VAL A 35 2.676 -4.355 -37.691 1.00 58.52 C ANISOU 266 C VAL A 35 6121 5038 11075 -194 -506 405 C ATOM 267 O VAL A 35 3.378 -3.442 -38.085 1.00 59.30 O ANISOU 267 O VAL A 35 6064 5066 11400 -260 -615 570 O ATOM 268 CB VAL A 35 0.579 -4.994 -39.020 1.00 53.24 C ANISOU 268 CB VAL A 35 5603 4543 10080 -174 -227 310 C ATOM 269 CG1 VAL A 35 0.386 -3.504 -39.250 1.00 52.95 C ANISOU 269 CG1 VAL A 35 5485 4401 10230 -233 -391 379 C ATOM 270 CG2 VAL A 35 0.089 -5.791 -40.217 1.00 51.60 C ANISOU 270 CG2 VAL A 35 5415 4486 9704 -160 -20 335 C ATOM 271 N MET A 36 2.440 -4.581 -36.394 1.00 60.01 N ANISOU 271 N MET A 36 6429 5183 11188 -140 -608 226 N ATOM 272 CA MET A 36 2.873 -3.680 -35.325 1.00 63.38 C ANISOU 272 CA MET A 36 6838 5472 11769 -135 -879 144 C ATOM 273 C MET A 36 4.401 -3.620 -35.225 1.00 63.75 C ANISOU 273 C MET A 36 6733 5456 12031 -176 -980 301 C ATOM 274 O MET A 36 4.987 -2.535 -35.033 1.00 65.53 O ANISOU 274 O MET A 36 6849 5526 12521 -229 -1218 347 O ATOM 275 CB MET A 36 2.342 -4.149 -33.970 1.00 67.53 C ANISOU 275 CB MET A 36 7517 6052 12088 -41 -929 -70 C ATOM 276 CG MET A 36 1.498 -3.112 -33.280 1.00 72.96 C ANISOU 276 CG MET A 36 8272 6682 12766 14 -1112 -280 C ATOM 277 SD MET A 36 -0.221 -3.630 -33.222 1.00 78.15 S ANISOU 277 SD MET A 36 9069 7507 13117 81 -921 -414 S ATOM 278 CE MET A 36 -0.259 -4.330 -31.571 1.00 76.92 C ANISOU 278 CE MET A 36 9013 7506 12708 195 -966 -555 C ATOM 279 N AARG A 37 5.033 -4.794 -35.326 0.50 62.60 N ANISOU 279 N AARG A 37 6570 5414 11799 -148 -820 381 N ATOM 280 N BARG A 37 5.036 -4.792 -35.335 0.50 61.82 N ANISOU 280 N BARG A 37 6470 5315 11701 -149 -820 383 N ATOM 281 CA AARG A 37 6.483 -4.928 -35.286 0.50 63.36 C ANISOU 281 CA AARG A 37 6505 5486 12082 -171 -877 545 C ATOM 282 CA BARG A 37 6.485 -4.918 -35.278 0.50 62.13 C ANISOU 282 CA BARG A 37 6349 5329 11928 -171 -879 544 C ATOM 283 C AARG A 37 7.105 -4.248 -36.514 0.50 64.43 C ANISOU 283 C AARG A 37 6424 5627 12429 -254 -839 798 C ATOM 284 C BARG A 37 7.116 -4.271 -36.521 0.50 63.70 C ANISOU 284 C BARG A 37 6331 5538 12334 -253 -835 799 C ATOM 285 O AARG A 37 8.240 -3.765 -36.444 0.50 68.44 O ANISOU 285 O AARG A 37 6748 6067 13189 -310 -975 964 O ATOM 286 O BARG A 37 8.269 -3.830 -36.467 0.50 67.67 O ANISOU 286 O BARG A 37 6648 5978 13085 -307 -962 968 O ATOM 287 CB AARG A 37 6.884 -6.408 -35.194 0.50 61.73 C ANISOU 287 CB AARG A 37 6331 5390 11734 -98 -699 558 C ATOM 288 CB BARG A 37 6.883 -6.393 -35.113 0.50 59.65 C ANISOU 288 CB BARG A 37 6073 5121 11471 -97 -712 550 C ATOM 289 CG AARG A 37 6.909 -6.962 -33.775 0.50 60.92 C ANISOU 289 CG AARG A 37 6347 5268 11529 -41 -816 427 C ATOM 290 CG BARG A 37 6.819 -6.892 -33.675 0.50 58.08 C ANISOU 290 CG BARG A 37 6002 4904 11161 -41 -833 408 C ATOM 291 CD AARG A 37 7.521 -8.355 -33.680 0.50 60.57 C ANISOU 291 CD AARG A 37 6293 5284 11434 19 -689 491 C ATOM 292 CD BARG A 37 7.300 -8.326 -33.481 0.50 56.87 C ANISOU 292 CD BARG A 37 5861 4815 10929 22 -707 455 C ATOM 293 NE AARG A 37 6.696 -9.424 -34.236 0.50 58.26 N ANISOU 293 NE AARG A 37 6104 5066 10966 64 -466 445 N ATOM 294 NE BARG A 37 6.412 -9.346 -34.029 0.50 53.96 N ANISOU 294 NE BARG A 37 5599 4519 10382 61 -487 410 N ATOM 295 CZ AARG A 37 6.861 -9.963 -35.444 0.50 57.36 C ANISOU 295 CZ AARG A 37 5923 5008 10862 91 -275 506 C ATOM 296 CZ BARG A 37 5.380 -9.880 -33.383 0.50 51.36 C ANISOU 296 CZ BARG A 37 5427 4223 9862 84 -464 304 C ATOM 297 NH1AARG A 37 6.061 -10.938 -35.847 0.50 55.91 N ANISOU 297 NH1AARG A 37 5846 4859 10536 134 -125 426 N ATOM 298 NH1BARG A 37 4.665 -10.830 -33.960 0.50 49.81 N ANISOU 298 NH1BARG A 37 5298 4060 9564 103 -291 285 N ATOM 299 NH2AARG A 37 7.825 -9.534 -36.241 0.50 56.37 N ANISOU 299 NH2AARG A 37 5610 4918 10888 82 -243 648 N ATOM 300 NH2BARG A 37 5.075 -9.471 -32.164 0.50 50.87 N ANISOU 300 NH2BARG A 37 5439 4175 9713 94 -624 221 N ATOM 301 N SER A 38 6.364 -4.220 -37.629 1.00 62.88 N ANISOU 301 N SER A 38 6234 5532 12125 -264 -660 848 N ATOM 302 CA SER A 38 6.823 -3.595 -38.879 1.00 64.32 C ANISOU 302 CA SER A 38 6203 5784 12448 -336 -596 1123 C ATOM 303 C SER A 38 6.759 -2.062 -38.786 1.00 64.97 C ANISOU 303 C SER A 38 6193 5672 12818 -448 -859 1216 C ATOM 304 O SER A 38 7.447 -1.358 -39.538 1.00 66.17 O ANISOU 304 O SER A 38 6112 5833 13196 -540 -894 1513 O ATOM 305 CB SER A 38 6.009 -4.086 -40.047 1.00 65.07 C ANISOU 305 CB SER A 38 6348 6070 12303 -297 -342 1128 C ATOM 306 OG SER A 38 4.848 -3.276 -40.235 1.00 66.19 O ANISOU 306 OG SER A 38 6574 6142 12430 -342 -414 1067 O ATOM 307 N LEU A 39 5.887 -1.565 -37.896 1.00 63.56 N ANISOU 307 N LEU A 39 6185 5332 12633 -429 -1043 967 N ATOM 308 CA LEU A 39 5.643 -0.144 -37.681 1.00 64.19 C ANISOU 308 CA LEU A 39 6215 5181 12990 -500 -1331 966 C ATOM 309 C LEU A 39 6.394 0.355 -36.434 1.00 65.13 C ANISOU 309 C LEU A 39 6316 5091 13339 -503 -1655 851 C ATOM 310 O LEU A 39 6.262 1.522 -36.067 1.00 65.06 O ANISOU 310 O LEU A 39 6278 4845 13594 -540 -1956 787 O ATOM 311 CB LEU A 39 4.132 0.054 -37.538 1.00 62.97 C ANISOU 311 CB LEU A 39 6257 5011 12658 -437 -1319 722 C ATOM 312 CG LEU A 39 3.293 -0.256 -38.781 1.00 61.91 C ANISOU 312 CG LEU A 39 6136 5052 12333 -445 -1060 825 C ATOM 313 CD1 LEU A 39 1.813 -0.345 -38.432 1.00 58.81 C ANISOU 313 CD1 LEU A 39 5947 4671 11727 -366 -1028 555 C ATOM 314 CD2 LEU A 39 3.508 0.790 -39.867 1.00 64.11 C ANISOU 314 CD2 LEU A 39 6210 5282 12865 -561 -1127 1136 C ATOM 315 N GLY A 40 7.145 -0.540 -35.773 1.00 64.35 N ANISOU 315 N GLY A 40 6237 5069 13140 -453 -1614 807 N ATOM 316 CA GLY A 40 8.115 -0.171 -34.742 1.00 66.08 C ANISOU 316 CA GLY A 40 6394 5129 13584 -468 -1913 761 C ATOM 317 C GLY A 40 7.605 -0.344 -33.314 1.00 66.34 C ANISOU 317 C GLY A 40 6648 5136 13422 -345 -2066 395 C ATOM 318 O GLY A 40 8.243 0.157 -32.359 1.00 67.17 O ANISOU 318 O GLY A 40 6727 5093 13700 -340 -2380 289 O ATOM 319 N GLN A 41 6.461 -1.052 -33.155 1.00 66.53 N ANISOU 319 N GLN A 41 6874 5321 13081 -245 -1857 211 N ATOM 320 CA GLN A 41 5.926 -1.362 -31.817 1.00 68.01 C ANISOU 320 CA GLN A 41 7252 5572 13015 -114 -1946 -90 C ATOM 321 C GLN A 41 6.041 -2.870 -31.573 1.00 66.57 C ANISOU 321 C GLN A 41 7144 5600 12549 -64 -1699 -46 C ATOM 322 O GLN A 41 5.823 -3.654 -32.484 1.00 64.35 O ANISOU 322 O GLN A 41 6852 5422 12172 -87 -1418 92 O ATOM 323 CB GLN A 41 4.488 -0.856 -31.682 1.00 67.87 C ANISOU 323 CB GLN A 41 7375 5568 12843 -36 -1947 -321 C ATOM 324 CG GLN A 41 4.343 0.648 -31.910 1.00 70.00 C ANISOU 324 CG GLN A 41 7570 5590 13435 -73 -2223 -377 C ATOM 325 CD GLN A 41 5.223 1.499 -31.019 1.00 73.74 C ANISOU 325 CD GLN A 41 7982 5854 14179 -65 -2625 -497 C ATOM 326 OE1 GLN A 41 5.604 1.104 -29.910 1.00 74.38 O ANISOU 326 OE1 GLN A 41 8137 6012 14109 22 -2733 -660 O ATOM 327 NE2 GLN A 41 5.553 2.693 -31.503 1.00 75.43 N ANISOU 327 NE2 GLN A 41 8052 5793 14814 -162 -2876 -405 N ATOM 328 N ASN A 42 6.423 -3.245 -30.346 1.00 69.02 N ANISOU 328 N ASN A 42 7518 5961 12746 9 -1832 -164 N ATOM 329 CA ASN A 42 6.642 -4.649 -29.957 1.00 69.04 C ANISOU 329 CA ASN A 42 7574 6129 12530 54 -1656 -96 C ATOM 330 C ASN A 42 5.782 -4.949 -28.731 1.00 67.32 C ANISOU 330 C ASN A 42 7526 6068 11984 173 -1693 -307 C ATOM 331 O ASN A 42 6.248 -4.875 -27.595 1.00 66.53 O ANISOU 331 O ASN A 42 7449 6006 11821 237 -1900 -404 O ATOM 332 CB ASN A 42 8.123 -4.976 -29.721 1.00 72.89 C ANISOU 332 CB ASN A 42 7924 6566 13202 21 -1761 59 C ATOM 333 CG ASN A 42 8.393 -6.468 -29.583 1.00 78.61 C ANISOU 333 CG ASN A 42 8676 7423 13769 61 -1563 172 C ATOM 334 OD1 ASN A 42 7.651 -7.304 -30.112 1.00 83.72 O ANISOU 334 OD1 ASN A 42 9396 8159 14254 79 -1307 200 O ATOM 335 ND2 ASN A 42 9.456 -6.830 -28.877 1.00 81.00 N ANISOU 335 ND2 ASN A 42 8911 7720 14145 77 -1700 240 N ATOM 336 N PRO A 43 4.492 -5.301 -28.934 1.00 65.75 N ANISOU 336 N PRO A 43 7434 5991 11554 209 -1491 -367 N ATOM 337 CA PRO A 43 3.577 -5.606 -27.834 1.00 65.51 C ANISOU 337 CA PRO A 43 7532 6165 11191 324 -1486 -522 C ATOM 338 C PRO A 43 3.671 -7.080 -27.426 1.00 63.99 C ANISOU 338 C PRO A 43 7370 6127 10814 332 -1324 -362 C ATOM 339 O PRO A 43 4.210 -7.897 -28.189 1.00 63.58 O ANISOU 339 O PRO A 43 7260 6002 10892 259 -1180 -172 O ATOM 340 CB PRO A 43 2.225 -5.322 -28.483 1.00 64.44 C ANISOU 340 CB PRO A 43 7449 6062 10972 328 -1330 -593 C ATOM 341 CG PRO A 43 2.430 -5.854 -29.885 1.00 63.31 C ANISOU 341 CG PRO A 43 7240 5824 10988 211 -1123 -385 C ATOM 342 CD PRO A 43 3.844 -5.454 -30.247 1.00 63.90 C ANISOU 342 CD PRO A 43 7187 5735 11358 143 -1257 -271 C ATOM 343 N THR A 44 3.147 -7.397 -26.241 1.00 63.15 N ANISOU 343 N THR A 44 7341 6240 10411 431 -1355 -435 N ATOM 344 CA THR A 44 3.290 -8.715 -25.678 1.00 62.73 C ANISOU 344 CA THR A 44 7300 6327 10205 436 -1256 -252 C ATOM 345 C THR A 44 2.374 -9.645 -26.466 1.00 62.11 C ANISOU 345 C THR A 44 7241 6264 10091 374 -982 -116 C ATOM 346 O THR A 44 1.653 -9.175 -27.335 1.00 62.66 O ANISOU 346 O THR A 44 7321 6269 10216 343 -887 -188 O ATOM 347 CB THR A 44 3.040 -8.715 -24.164 1.00 64.55 C ANISOU 347 CB THR A 44 7583 6831 10110 562 -1382 -335 C ATOM 348 OG1 THR A 44 1.688 -8.362 -23.861 1.00 62.41 O ANISOU 348 OG1 THR A 44 7370 6761 9580 646 -1300 -472 O ATOM 349 CG2 THR A 44 3.990 -7.781 -23.444 1.00 66.67 C ANISOU 349 CG2 THR A 44 7836 7058 10435 628 -1694 -509 C ATOM 350 N GLU A 45 2.445 -10.946 -26.164 1.00 62.23 N ANISOU 350 N GLU A 45 7252 6345 10046 355 -887 85 N ATOM 351 CA GLU A 45 1.597 -11.956 -26.754 1.00 61.39 C ANISOU 351 CA GLU A 45 7160 6236 9930 296 -677 219 C ATOM 352 C GLU A 45 0.221 -11.879 -26.075 1.00 62.45 C ANISOU 352 C GLU A 45 7334 6616 9774 341 -612 190 C ATOM 353 O GLU A 45 -0.803 -12.117 -26.704 1.00 61.89 O ANISOU 353 O GLU A 45 7273 6543 9696 296 -462 209 O ATOM 354 CB GLU A 45 2.282 -13.320 -26.622 1.00 63.81 C ANISOU 354 CB GLU A 45 7429 6476 10339 264 -652 446 C ATOM 355 CG GLU A 45 2.085 -14.263 -27.801 1.00 64.12 C ANISOU 355 CG GLU A 45 7455 6335 10571 195 -494 531 C ATOM 356 CD GLU A 45 2.078 -13.653 -29.199 1.00 64.87 C ANISOU 356 CD GLU A 45 7542 6289 10816 167 -415 396 C ATOM 357 OE1 GLU A 45 3.076 -12.991 -29.580 1.00 65.17 O ANISOU 357 OE1 GLU A 45 7526 6243 10992 178 -483 343 O ATOM 358 OE2 GLU A 45 1.053 -13.833 -29.913 1.00 66.34 O ANISOU 358 OE2 GLU A 45 7761 6464 10979 129 -290 365 O ATOM 359 N ALA A 46 0.208 -11.505 -24.792 1.00 64.32 N ANISOU 359 N ALA A 46 7584 7091 9762 444 -732 135 N ATOM 360 CA ALA A 46 -1.023 -11.273 -24.041 1.00 66.05 C ANISOU 360 CA ALA A 46 7817 7613 9662 530 -675 84 C ATOM 361 C ALA A 46 -1.714 -9.986 -24.512 1.00 66.30 C ANISOU 361 C ALA A 46 7877 7618 9695 585 -687 -194 C ATOM 362 O ALA A 46 -2.942 -9.920 -24.591 1.00 66.84 O ANISOU 362 O ALA A 46 7939 7830 9626 608 -557 -214 O ATOM 363 CB ALA A 46 -0.707 -11.200 -22.569 1.00 69.12 C ANISOU 363 CB ALA A 46 8205 8295 9760 655 -813 78 C ATOM 364 N GLU A 47 -0.925 -8.945 -24.786 1.00 66.76 N ANISOU 364 N GLU A 47 7949 7488 9927 607 -861 -392 N ATOM 365 CA GLU A 47 -1.479 -7.693 -25.294 1.00 67.49 C ANISOU 365 CA GLU A 47 8057 7495 10092 650 -911 -635 C ATOM 366 C GLU A 47 -2.207 -7.992 -26.609 1.00 65.87 C ANISOU 366 C GLU A 47 7839 7154 10035 533 -709 -537 C ATOM 367 O GLU A 47 -3.315 -7.510 -26.831 1.00 67.59 O ANISOU 367 O GLU A 47 8060 7441 10177 572 -640 -640 O ATOM 368 CB GLU A 47 -0.397 -6.620 -25.477 1.00 68.28 C ANISOU 368 CB GLU A 47 8145 7356 10440 653 -1155 -795 C ATOM 369 CG GLU A 47 -0.146 -5.769 -24.237 1.00 71.40 C ANISOU 369 CG GLU A 47 8568 7881 10678 818 -1414 -1050 C ATOM 370 CD GLU A 47 1.234 -5.117 -24.135 1.00 74.62 C ANISOU 370 CD GLU A 47 8946 8063 11344 796 -1697 -1125 C ATOM 371 OE1 GLU A 47 1.947 -5.061 -25.165 1.00 75.72 O ANISOU 371 OE1 GLU A 47 9022 7928 11818 652 -1688 -989 O ATOM 372 OE2 GLU A 47 1.609 -4.672 -23.020 1.00 76.82 O ANISOU 372 OE2 GLU A 47 9250 8457 11481 927 -1933 -1314 O ATOM 373 N LEU A 48 -1.592 -8.812 -27.466 1.00 64.22 N ANISOU 373 N LEU A 48 7607 6766 10027 406 -621 -350 N ATOM 374 CA LEU A 48 -2.177 -9.130 -28.763 1.00 62.37 C ANISOU 374 CA LEU A 48 7364 6409 9922 308 -455 -280 C ATOM 375 C LEU A 48 -3.502 -9.881 -28.568 1.00 62.29 C ANISOU 375 C LEU A 48 7362 6576 9730 301 -295 -194 C ATOM 376 O LEU A 48 -4.446 -9.650 -29.315 1.00 62.32 O ANISOU 376 O LEU A 48 7363 6561 9754 270 -204 -233 O ATOM 377 CB LEU A 48 -1.185 -9.938 -29.605 1.00 61.74 C ANISOU 377 CB LEU A 48 7255 6144 10057 216 -405 -130 C ATOM 378 CG LEU A 48 0.109 -9.211 -29.976 1.00 62.70 C ANISOU 378 CG LEU A 48 7326 6103 10390 205 -537 -163 C ATOM 379 CD1 LEU A 48 1.150 -10.181 -30.511 1.00 61.83 C ANISOU 379 CD1 LEU A 48 7167 5886 10439 159 -479 -7 C ATOM 380 CD2 LEU A 48 -0.149 -8.096 -30.976 1.00 61.86 C ANISOU 380 CD2 LEU A 48 7195 5891 10419 175 -550 -251 C ATOM 381 N GLN A 49 -3.587 -10.767 -27.572 1.00 63.42 N ANISOU 381 N GLN A 49 7494 6896 9705 321 -271 -49 N ATOM 382 CA GLN A 49 -4.829 -11.508 -27.364 1.00 65.03 C ANISOU 382 CA GLN A 49 7667 7272 9766 295 -127 91 C ATOM 383 C GLN A 49 -5.966 -10.518 -27.096 1.00 65.67 C ANISOU 383 C GLN A 49 7737 7549 9663 393 -103 -79 C ATOM 384 O GLN A 49 -6.975 -10.502 -27.799 1.00 63.38 O ANISOU 384 O GLN A 49 7425 7242 9412 347 2 -77 O ATOM 385 CB GLN A 49 -4.740 -12.493 -26.196 1.00 68.04 C ANISOU 385 CB GLN A 49 8011 7858 9982 307 -122 317 C ATOM 386 CG GLN A 49 -4.414 -13.922 -26.615 1.00 68.93 C ANISOU 386 CG GLN A 49 8102 7792 10297 179 -74 572 C ATOM 387 CD GLN A 49 -5.366 -14.519 -27.625 1.00 67.39 C ANISOU 387 CD GLN A 49 7887 7468 10248 69 44 641 C ATOM 388 OE1 GLN A 49 -6.475 -14.039 -27.836 1.00 66.18 O ANISOU 388 OE1 GLN A 49 7716 7425 10005 75 119 573 O ATOM 389 NE2 GLN A 49 -4.925 -15.593 -28.265 1.00 68.79 N ANISOU 389 NE2 GLN A 49 8064 7404 10668 -21 44 763 N ATOM 390 N ASP A 50 -5.763 -9.684 -26.074 1.00 67.89 N ANISOU 390 N ASP A 50 8029 8012 9751 545 -222 -247 N ATOM 391 CA ASP A 50 -6.769 -8.759 -25.583 1.00 68.43 C ANISOU 391 CA ASP A 50 8079 8311 9610 694 -220 -444 C ATOM 392 C ASP A 50 -7.224 -7.852 -26.728 1.00 67.06 C ANISOU 392 C ASP A 50 7918 7917 9644 668 -224 -612 C ATOM 393 O ASP A 50 -8.411 -7.492 -26.811 1.00 69.57 O ANISOU 393 O ASP A 50 8195 8368 9869 725 -140 -679 O ATOM 394 CB ASP A 50 -6.246 -7.950 -24.392 1.00 70.72 C ANISOU 394 CB ASP A 50 8395 8779 9695 883 -401 -664 C ATOM 395 CG ASP A 50 -5.972 -8.795 -23.156 1.00 74.05 C ANISOU 395 CG ASP A 50 8790 9507 9837 934 -392 -485 C ATOM 396 OD1 ASP A 50 -6.830 -9.674 -22.835 1.00 73.53 O ANISOU 396 OD1 ASP A 50 8649 9691 9597 905 -215 -238 O ATOM 397 OD2 ASP A 50 -4.888 -8.591 -22.535 1.00 75.87 O ANISOU 397 OD2 ASP A 50 9060 9723 10042 991 -572 -562 O ATOM 398 N MET A 51 -6.287 -7.492 -27.610 1.00 64.11 N ANISOU 398 N MET A 51 7582 7227 9549 583 -318 -652 N ATOM 399 CA MET A 51 -6.596 -6.611 -28.731 1.00 62.87 C ANISOU 399 CA MET A 51 7423 6863 9598 547 -339 -764 C ATOM 400 C MET A 51 -7.518 -7.323 -29.732 1.00 61.21 C ANISOU 400 C MET A 51 7188 6628 9438 428 -152 -611 C ATOM 401 O MET A 51 -8.454 -6.730 -30.245 1.00 60.79 O ANISOU 401 O MET A 51 7113 6575 9407 445 -120 -692 O ATOM 402 CB MET A 51 -5.313 -6.109 -29.397 1.00 61.68 C ANISOU 402 CB MET A 51 7285 6429 9722 478 -477 -782 C ATOM 403 CG MET A 51 -4.782 -4.854 -28.702 1.00 63.94 C ANISOU 403 CG MET A 51 7578 6665 10048 600 -723 -1015 C ATOM 404 SD MET A 51 -3.096 -4.367 -29.145 1.00 64.88 S ANISOU 404 SD MET A 51 7670 6487 10492 512 -920 -978 S ATOM 405 CE MET A 51 -3.195 -4.520 -30.927 1.00 62.07 C ANISOU 405 CE MET A 51 7269 5950 10364 346 -763 -788 C ATOM 406 N ILE A 52 -7.276 -8.618 -29.952 1.00 62.80 N ANISOU 406 N ILE A 52 7390 6806 9664 316 -49 -399 N ATOM 407 CA ILE A 52 -8.103 -9.454 -30.822 1.00 60.69 C ANISOU 407 CA ILE A 52 7101 6501 9456 203 91 -263 C ATOM 408 C ILE A 52 -9.446 -9.701 -30.133 1.00 61.34 C ANISOU 408 C ILE A 52 7121 6843 9342 243 185 -206 C ATOM 409 O ILE A 52 -10.465 -9.675 -30.793 1.00 60.98 O ANISOU 409 O ILE A 52 7039 6797 9331 200 258 -196 O ATOM 410 CB ILE A 52 -7.381 -10.774 -31.175 1.00 60.58 C ANISOU 410 CB ILE A 52 7100 6355 9559 96 129 -84 C ATOM 411 CG1 ILE A 52 -6.164 -10.532 -32.069 1.00 58.15 C ANISOU 411 CG1 ILE A 52 6824 5827 9445 65 71 -132 C ATOM 412 CG2 ILE A 52 -8.339 -11.781 -31.802 1.00 61.42 C ANISOU 412 CG2 ILE A 52 7180 6438 9718 -7 235 45 C ATOM 413 CD1 ILE A 52 -6.503 -10.051 -33.459 1.00 56.35 C ANISOU 413 CD1 ILE A 52 6595 5483 9332 17 106 -196 C ATOM 414 N ASN A 53 -9.416 -9.931 -28.813 1.00 63.62 N ANISOU 414 N ASN A 53 7381 7375 9416 331 182 -152 N ATOM 415 CA ASN A 53 -10.589 -10.350 -28.031 1.00 66.85 C ANISOU 415 CA ASN A 53 7693 8097 9608 369 295 -22 C ATOM 416 C ASN A 53 -11.677 -9.278 -28.069 1.00 69.40 C ANISOU 416 C ASN A 53 7970 8563 9835 488 321 -211 C ATOM 417 O ASN A 53 -12.850 -9.596 -28.216 1.00 70.44 O ANISOU 417 O ASN A 53 8007 8826 9928 454 439 -99 O ATOM 418 CB ASN A 53 -10.250 -10.623 -26.565 1.00 68.37 C ANISOU 418 CB ASN A 53 7856 8583 9537 474 277 60 C ATOM 419 CG ASN A 53 -9.446 -11.889 -26.371 1.00 67.63 C ANISOU 419 CG ASN A 53 7769 8400 9528 355 268 324 C ATOM 420 OD1 ASN A 53 -9.452 -12.773 -27.224 1.00 64.28 O ANISOU 420 OD1 ASN A 53 7343 7741 9337 196 306 476 O ATOM 421 ND2 ASN A 53 -8.747 -11.972 -25.252 1.00 69.06 N ANISOU 421 ND2 ASN A 53 7953 8760 9524 443 199 363 N ATOM 422 N GLU A 54 -11.253 -8.020 -27.915 1.00 72.73 N ANISOU 422 N GLU A 54 8446 8942 10245 628 192 -494 N ATOM 423 CA GLU A 54 -12.141 -6.873 -27.813 1.00 75.41 C ANISOU 423 CA GLU A 54 8746 9397 10510 786 172 -724 C ATOM 424 C GLU A 54 -12.928 -6.671 -29.109 1.00 70.66 C ANISOU 424 C GLU A 54 8119 8611 10116 682 224 -709 C ATOM 425 O GLU A 54 -13.989 -6.082 -29.084 1.00 72.48 O ANISOU 425 O GLU A 54 8277 8975 10286 782 262 -807 O ATOM 426 CB GLU A 54 -11.348 -5.597 -27.531 1.00 81.06 C ANISOU 426 CB GLU A 54 9532 9993 11271 932 -37 -1032 C ATOM 427 CG GLU A 54 -11.022 -5.395 -26.066 1.00 88.39 C ANISOU 427 CG GLU A 54 10465 11209 11910 1129 -114 -1164 C ATOM 428 CD GLU A 54 -10.316 -4.079 -25.780 1.00 94.19 C ANISOU 428 CD GLU A 54 11264 11794 12727 1282 -370 -1510 C ATOM 429 OE1 GLU A 54 -9.625 -3.576 -26.698 1.00 94.30 O ANISOU 429 OE1 GLU A 54 11327 11435 13068 1171 -496 -1545 O ATOM 430 OE2 GLU A 54 -10.465 -3.553 -24.646 1.00101.51 O ANISOU 430 OE2 GLU A 54 12183 12989 13396 1518 -455 -1740 O ATOM 431 N VAL A 55 -12.379 -7.117 -30.238 1.00 65.24 N ANISOU 431 N VAL A 55 7488 7635 9663 503 216 -603 N ATOM 432 CA VAL A 55 -13.020 -6.918 -31.525 1.00 62.16 C ANISOU 432 CA VAL A 55 7083 7083 9450 408 244 -592 C ATOM 433 C VAL A 55 -13.709 -8.212 -31.973 1.00 60.93 C ANISOU 433 C VAL A 55 6879 6958 9314 255 375 -358 C ATOM 434 O VAL A 55 -14.708 -8.149 -32.687 1.00 61.62 O ANISOU 434 O VAL A 55 6911 7038 9462 207 420 -338 O ATOM 435 CB VAL A 55 -12.003 -6.439 -32.571 1.00 60.25 C ANISOU 435 CB VAL A 55 6917 6538 9434 332 139 -643 C ATOM 436 CG1 VAL A 55 -12.660 -6.121 -33.904 1.00 59.00 C ANISOU 436 CG1 VAL A 55 6739 6254 9423 252 154 -631 C ATOM 437 CG2 VAL A 55 -11.192 -5.263 -32.061 1.00 60.92 C ANISOU 437 CG2 VAL A 55 7036 6552 9559 455 -29 -837 C ATOM 438 N ASP A 56 -13.156 -9.370 -31.584 1.00 60.17 N ANISOU 438 N ASP A 56 6796 6866 9198 175 409 -184 N ATOM 439 CA ASP A 56 -13.744 -10.676 -31.907 1.00 59.38 C ANISOU 439 CA ASP A 56 6642 6752 9166 25 489 44 C ATOM 440 C ASP A 56 -15.130 -10.718 -31.265 1.00 61.06 C ANISOU 440 C ASP A 56 6712 7252 9235 64 586 144 C ATOM 441 O ASP A 56 -15.265 -10.470 -30.073 1.00 63.28 O ANISOU 441 O ASP A 56 6934 7813 9295 194 622 152 O ATOM 442 CB ASP A 56 -12.850 -11.834 -31.446 1.00 58.60 C ANISOU 442 CB ASP A 56 6572 6596 9098 -43 478 215 C ATOM 443 CG ASP A 56 -13.361 -13.229 -31.774 1.00 58.18 C ANISOU 443 CG ASP A 56 6461 6461 9182 -202 512 450 C ATOM 444 OD1 ASP A 56 -14.010 -13.400 -32.816 1.00 56.48 O ANISOU 444 OD1 ASP A 56 6237 6115 9107 -289 511 430 O ATOM 445 OD2 ASP A 56 -13.085 -14.137 -30.990 1.00 58.66 O ANISOU 445 OD2 ASP A 56 6483 6577 9227 -238 515 653 O ATOM 446 N ALA A 57 -16.147 -10.980 -32.084 1.00 61.12 N ANISOU 446 N ALA A 57 6652 7210 9358 -34 621 210 N ATOM 447 CA ALA A 57 -17.538 -10.927 -31.642 1.00 64.65 C ANISOU 447 CA ALA A 57 6934 7926 9704 -2 714 311 C ATOM 448 C ALA A 57 -18.092 -12.332 -31.380 1.00 66.04 C ANISOU 448 C ALA A 57 6987 8161 9942 -159 769 643 C ATOM 449 O ALA A 57 -19.097 -12.455 -30.698 1.00 68.97 O ANISOU 449 O ALA A 57 7184 8824 10197 -133 864 809 O ATOM 450 CB ALA A 57 -18.377 -10.207 -32.667 1.00 64.00 C ANISOU 450 CB ALA A 57 6828 7760 9728 -6 696 183 C ATOM 451 N ASP A 58 -17.453 -13.373 -31.927 1.00 64.65 N ANISOU 451 N ASP A 58 6886 7711 9967 -315 699 744 N ATOM 452 CA ASP A 58 -18.017 -14.719 -31.881 1.00 66.48 C ANISOU 452 CA ASP A 58 7001 7903 10356 -489 696 1051 C ATOM 453 C ASP A 58 -17.140 -15.649 -31.040 1.00 66.40 C ANISOU 453 C ASP A 58 7002 7881 10346 -524 676 1253 C ATOM 454 O ASP A 58 -17.468 -16.810 -30.876 1.00 68.79 O ANISOU 454 O ASP A 58 7201 8126 10810 -670 648 1542 O ATOM 455 CB ASP A 58 -18.254 -15.278 -33.287 1.00 66.40 C ANISOU 455 CB ASP A 58 7039 7561 10628 -641 595 1001 C ATOM 456 CG ASP A 58 -17.063 -15.185 -34.223 1.00 65.68 C ANISOU 456 CG ASP A 58 7147 7178 10629 -627 507 765 C ATOM 457 OD1 ASP A 58 -15.943 -14.922 -33.738 1.00 67.17 O ANISOU 457 OD1 ASP A 58 7428 7370 10723 -537 511 694 O ATOM 458 OD2 ASP A 58 -17.268 -15.360 -35.438 1.00 65.55 O ANISOU 458 OD2 ASP A 58 7180 6958 10766 -698 433 655 O ATOM 459 N GLY A 59 -16.042 -15.128 -30.493 1.00 65.56 N ANISOU 459 N GLY A 59 7006 7819 10081 -394 669 1116 N ATOM 460 CA GLY A 59 -15.158 -15.917 -29.647 1.00 66.22 C ANISOU 460 CA GLY A 59 7100 7913 10146 -409 639 1302 C ATOM 461 C GLY A 59 -14.438 -17.044 -30.384 1.00 64.50 C ANISOU 461 C GLY A 59 6958 7305 10241 -550 527 1363 C ATOM 462 O GLY A 59 -14.094 -18.051 -29.754 1.00 66.32 O ANISOU 462 O GLY A 59 7137 7511 10550 -618 489 1625 O ATOM 463 N ASN A 60 -14.170 -16.877 -31.690 1.00 61.05 N ANISOU 463 N ASN A 60 6639 6581 9974 -576 466 1123 N ATOM 464 CA ASN A 60 -13.465 -17.909 -32.467 1.00 60.33 C ANISOU 464 CA ASN A 60 6624 6137 10161 -665 355 1114 C ATOM 465 C ASN A 60 -11.967 -17.563 -32.568 1.00 59.57 C ANISOU 465 C ASN A 60 6664 5933 10034 -561 326 931 C ATOM 466 O ASN A 60 -11.228 -18.177 -33.353 1.00 58.45 O ANISOU 466 O ASN A 60 6598 5522 10086 -581 250 843 O ATOM 467 CB ASN A 60 -14.153 -18.175 -33.812 1.00 59.06 C ANISOU 467 CB ASN A 60 6477 5763 10197 -754 297 997 C ATOM 468 CG ASN A 60 -13.909 -17.117 -34.862 1.00 56.49 C ANISOU 468 CG ASN A 60 6264 5403 9794 -670 313 684 C ATOM 469 OD1 ASN A 60 -13.044 -16.264 -34.704 1.00 57.38 O ANISOU 469 OD1 ASN A 60 6454 5579 9770 -558 348 548 O ATOM 470 ND2 ASN A 60 -14.660 -17.168 -35.948 1.00 55.41 N ANISOU 470 ND2 ASN A 60 6127 5166 9758 -731 271 587 N ATOM 471 N GLY A 61 -11.527 -16.582 -31.767 1.00 59.51 N ANISOU 471 N GLY A 61 6676 6144 9789 -439 374 866 N ATOM 472 CA GLY A 61 -10.117 -16.273 -31.574 1.00 58.36 C ANISOU 472 CA GLY A 61 6621 5935 9616 -352 331 756 C ATOM 473 C GLY A 61 -9.524 -15.398 -32.670 1.00 56.14 C ANISOU 473 C GLY A 61 6435 5519 9376 -300 317 486 C ATOM 474 O GLY A 61 -8.321 -15.143 -32.646 1.00 56.14 O ANISOU 474 O GLY A 61 6489 5449 9392 -240 278 409 O ATOM 475 N THR A 62 -10.345 -14.935 -33.624 1.00 54.62 N ANISOU 475 N THR A 62 6245 5303 9205 -326 345 372 N ATOM 476 CA THR A 62 -9.861 -14.099 -34.734 1.00 52.38 C ANISOU 476 CA THR A 62 6027 4921 8952 -287 334 167 C ATOM 477 C THR A 62 -10.939 -13.105 -35.170 1.00 51.14 C ANISOU 477 C THR A 62 5845 4865 8721 -278 364 77 C ATOM 478 O THR A 62 -12.069 -13.143 -34.685 1.00 52.37 O ANISOU 478 O THR A 62 5928 5160 8810 -298 400 155 O ATOM 479 CB THR A 62 -9.461 -14.922 -35.963 1.00 52.02 C ANISOU 479 CB THR A 62 6025 4663 9076 -332 308 113 C ATOM 480 OG1 THR A 62 -10.673 -15.388 -36.548 1.00 53.90 O ANISOU 480 OG1 THR A 62 6234 4873 9372 -414 304 130 O ATOM 481 CG2 THR A 62 -8.541 -16.075 -35.646 1.00 52.82 C ANISOU 481 CG2 THR A 62 6138 4626 9303 -336 265 197 C ATOM 482 N ILE A 63 -10.554 -12.240 -36.115 1.00 49.04 N ANISOU 482 N ILE A 63 5619 4534 8479 -248 346 -63 N ATOM 483 CA ILE A 63 -11.306 -11.089 -36.536 1.00 47.40 C ANISOU 483 CA ILE A 63 5389 4394 8226 -221 346 -152 C ATOM 484 C ILE A 63 -11.556 -11.203 -38.036 1.00 45.72 C ANISOU 484 C ILE A 63 5195 4087 8089 -278 343 -198 C ATOM 485 O ILE A 63 -10.624 -11.158 -38.806 1.00 43.48 O ANISOU 485 O ILE A 63 4948 3723 7848 -268 331 -239 O ATOM 486 CB ILE A 63 -10.515 -9.811 -36.199 1.00 48.14 C ANISOU 486 CB ILE A 63 5496 4496 8295 -130 292 -245 C ATOM 487 CG1 ILE A 63 -10.238 -9.692 -34.699 1.00 48.84 C ANISOU 487 CG1 ILE A 63 5575 4702 8277 -50 270 -239 C ATOM 488 CG2 ILE A 63 -11.207 -8.566 -36.743 1.00 48.54 C ANISOU 488 CG2 ILE A 63 5519 4566 8357 -100 260 -333 C ATOM 489 CD1 ILE A 63 -9.646 -8.364 -34.298 1.00 49.42 C ANISOU 489 CD1 ILE A 63 5658 4770 8349 47 170 -371 C ATOM 490 N ASP A 64 -12.824 -11.344 -38.422 1.00 47.68 N ANISOU 490 N ASP A 64 5402 4376 8338 -330 352 -185 N ATOM 491 CA ASP A 64 -13.235 -11.253 -39.820 1.00 49.01 C ANISOU 491 CA ASP A 64 5582 4499 8540 -370 329 -244 C ATOM 492 C ASP A 64 -13.583 -9.791 -40.099 1.00 48.34 C ANISOU 492 C ASP A 64 5467 4480 8420 -321 313 -289 C ATOM 493 O ASP A 64 -13.547 -8.962 -39.183 1.00 46.99 O ANISOU 493 O ASP A 64 5270 4366 8218 -252 308 -304 O ATOM 494 CB ASP A 64 -14.395 -12.190 -40.164 1.00 51.89 C ANISOU 494 CB ASP A 64 5911 4845 8959 -461 310 -205 C ATOM 495 CG ASP A 64 -15.664 -11.970 -39.357 1.00 56.30 C ANISOU 495 CG ASP A 64 6367 5531 9493 -479 337 -118 C ATOM 496 OD1 ASP A 64 -15.748 -10.936 -38.646 1.00 59.91 O ANISOU 496 OD1 ASP A 64 6791 6107 9864 -394 370 -135 O ATOM 497 OD2 ASP A 64 -16.574 -12.841 -39.441 1.00 60.89 O ANISOU 497 OD2 ASP A 64 6889 6094 10152 -572 314 -36 O ATOM 498 N PHE A 65 -13.899 -9.492 -41.363 1.00 60.34 N ANISOU 498 N PHE A 65 7490 5445 9989 411 416 220 N ATOM 499 CA PHE A 65 -14.031 -8.128 -41.809 1.00 59.92 C ANISOU 499 CA PHE A 65 7346 5429 9992 373 485 197 C ATOM 500 C PHE A 65 -15.319 -7.507 -41.272 1.00 57.84 C ANISOU 500 C PHE A 65 7084 5281 9612 220 324 133 C ATOM 501 O PHE A 65 -15.333 -6.338 -40.901 1.00 58.43 O ANISOU 501 O PHE A 65 6993 5427 9780 158 312 112 O ATOM 502 CB PHE A 65 -13.941 -8.040 -43.330 1.00 60.71 C ANISOU 502 CB PHE A 65 7637 5412 10018 494 698 225 C ATOM 503 CG PHE A 65 -14.054 -6.623 -43.815 1.00 60.62 C ANISOU 503 CG PHE A 65 7566 5411 10055 494 821 231 C ATOM 504 CD1 PHE A 65 -13.142 -5.664 -43.391 1.00 61.46 C ANISOU 504 CD1 PHE A 65 7396 5510 10443 474 927 251 C ATOM 505 CD2 PHE A 65 -15.090 -6.236 -44.650 1.00 60.80 C ANISOU 505 CD2 PHE A 65 7799 5447 9854 522 826 202 C ATOM 506 CE1 PHE A 65 -13.246 -4.345 -43.812 1.00 61.65 C ANISOU 506 CE1 PHE A 65 7376 5507 10541 470 1085 263 C ATOM 507 CE2 PHE A 65 -15.190 -4.917 -45.074 1.00 61.57 C ANISOU 507 CE2 PHE A 65 7869 5542 9982 555 968 230 C ATOM 508 CZ PHE A 65 -14.272 -3.974 -44.652 1.00 61.63 C ANISOU 508 CZ PHE A 65 7620 5509 10284 522 1119 271 C ATOM 509 N PRO A 66 -16.455 -8.231 -41.237 1.00 56.67 N ANISOU 509 N PRO A 66 7108 5139 9284 148 213 90 N ATOM 510 CA PRO A 66 -17.624 -7.744 -40.506 1.00 54.62 C ANISOU 510 CA PRO A 66 6807 4988 8955 2 65 36 C ATOM 511 C PRO A 66 -17.298 -7.298 -39.073 1.00 53.31 C ANISOU 511 C PRO A 66 6442 4923 8890 -48 -36 53 C ATOM 512 O PRO A 66 -17.733 -6.226 -38.659 1.00 53.51 O ANISOU 512 O PRO A 66 6359 5041 8932 -126 -90 20 O ATOM 513 CB PRO A 66 -18.555 -8.967 -40.549 1.00 54.89 C ANISOU 513 CB PRO A 66 7020 4964 8871 -55 1 -11 C ATOM 514 CG PRO A 66 -18.237 -9.598 -41.885 1.00 55.64 C ANISOU 514 CG PRO A 66 7294 4939 8904 62 108 -31 C ATOM 515 CD PRO A 66 -16.731 -9.472 -41.985 1.00 56.84 C ANISOU 515 CD PRO A 66 7363 5048 9185 199 245 68 C ATOM 516 N GLU A 67 -16.544 -8.109 -38.324 1.00 53.08 N ANISOU 516 N GLU A 67 6380 4879 8908 21 -69 98 N ATOM 517 CA GLU A 67 -16.209 -7.755 -36.918 1.00 52.65 C ANISOU 517 CA GLU A 67 6162 4938 8904 27 -203 94 C ATOM 518 C GLU A 67 -15.404 -6.447 -36.891 1.00 52.05 C ANISOU 518 C GLU A 67 5838 4923 9014 31 -197 39 C ATOM 519 O GLU A 67 -15.587 -5.609 -36.016 1.00 50.71 O ANISOU 519 O GLU A 67 5538 4859 8870 -24 -310 -19 O ATOM 520 CB GLU A 67 -15.437 -8.878 -36.221 1.00 53.23 C ANISOU 520 CB GLU A 67 6262 4990 8972 169 -239 155 C ATOM 521 CG GLU A 67 -16.306 -10.023 -35.744 1.00 53.08 C ANISOU 521 CG GLU A 67 6464 4909 8795 153 -240 210 C ATOM 522 CD GLU A 67 -15.552 -11.302 -35.428 1.00 55.36 C ANISOU 522 CD GLU A 67 6852 5117 9063 325 -201 298 C ATOM 523 OE1 GLU A 67 -14.372 -11.411 -35.813 1.00 56.73 O ANISOU 523 OE1 GLU A 67 6932 5279 9344 455 -169 311 O ATOM 524 OE2 GLU A 67 -16.138 -12.202 -34.790 1.00 56.66 O ANISOU 524 OE2 GLU A 67 7191 5216 9119 341 -176 361 O ATOM 525 N PHE A 68 -14.509 -6.305 -37.872 1.00 52.87 N ANISOU 525 N PHE A 68 5886 4937 9263 100 -38 54 N ATOM 526 CA PHE A 68 -13.610 -5.176 -38.010 1.00 53.66 C ANISOU 526 CA PHE A 68 5738 5032 9615 103 42 2 C ATOM 527 C PHE A 68 -14.441 -3.930 -38.321 1.00 52.90 C ANISOU 527 C PHE A 68 5649 4950 9500 -10 96 -29 C ATOM 528 O PHE A 68 -14.308 -2.901 -37.665 1.00 52.38 O ANISOU 528 O PHE A 68 5390 4942 9570 -78 41 -109 O ATOM 529 CB PHE A 68 -12.584 -5.481 -39.103 1.00 54.69 C ANISOU 529 CB PHE A 68 5860 5024 9895 218 267 58 C ATOM 530 CG PHE A 68 -11.474 -4.475 -39.246 1.00 56.27 C ANISOU 530 CG PHE A 68 5768 5173 10438 228 407 6 C ATOM 531 CD1 PHE A 68 -10.396 -4.485 -38.378 1.00 57.67 C ANISOU 531 CD1 PHE A 68 5648 5408 10854 271 292 -79 C ATOM 532 CD2 PHE A 68 -11.492 -3.539 -40.271 1.00 56.96 C ANISOU 532 CD2 PHE A 68 5877 5142 10622 212 668 36 C ATOM 533 CE1 PHE A 68 -9.371 -3.563 -38.514 1.00 60.04 C ANISOU 533 CE1 PHE A 68 5632 5641 11538 256 430 -164 C ATOM 534 CE2 PHE A 68 -10.464 -2.615 -40.407 1.00 59.03 C ANISOU 534 CE2 PHE A 68 5858 5311 11256 206 855 -10 C ATOM 535 CZ PHE A 68 -9.409 -2.624 -39.522 1.00 60.53 C ANISOU 535 CZ PHE A 68 5709 5551 11736 207 733 -125 C ATOM 536 N LEU A 69 -15.320 -4.062 -39.320 1.00 52.61 N ANISOU 536 N LEU A 69 5844 4861 9283 -13 189 19 N ATOM 537 CA LEU A 69 -16.218 -2.998 -39.721 1.00 52.21 C ANISOU 537 CA LEU A 69 5843 4830 9162 -75 237 4 C ATOM 538 C LEU A 69 -16.992 -2.479 -38.509 1.00 50.57 C ANISOU 538 C LEU A 69 5550 4753 8910 -199 46 -58 C ATOM 539 O LEU A 69 -17.084 -1.290 -38.311 1.00 50.27 O ANISOU 539 O LEU A 69 5399 4735 8963 -253 80 -97 O ATOM 540 CB LEU A 69 -17.177 -3.526 -40.787 1.00 53.09 C ANISOU 540 CB LEU A 69 6228 4912 9032 -28 269 31 C ATOM 541 CG LEU A 69 -17.265 -2.705 -42.067 1.00 55.01 C ANISOU 541 CG LEU A 69 6584 5082 9234 75 476 68 C ATOM 542 CD1 LEU A 69 -15.902 -2.167 -42.484 1.00 58.15 C ANISOU 542 CD1 LEU A 69 6861 5349 9882 161 733 125 C ATOM 543 CD2 LEU A 69 -17.848 -3.551 -43.181 1.00 55.49 C ANISOU 543 CD2 LEU A 69 6919 5109 9056 187 480 66 C ATOM 544 N THR A 70 -17.546 -3.388 -37.706 1.00 50.24 N ANISOU 544 N THR A 70 5578 4779 8730 -233 -121 -59 N ATOM 545 CA THR A 70 -18.324 -2.985 -36.542 1.00 49.91 C ANISOU 545 CA THR A 70 5493 4850 8620 -323 -273 -100 C ATOM 546 C THR A 70 -17.469 -2.095 -35.630 1.00 51.41 C ANISOU 546 C THR A 70 5451 5095 8984 -324 -337 -175 C ATOM 547 O THR A 70 -17.865 -0.999 -35.258 1.00 51.79 O ANISOU 547 O THR A 70 5422 5191 9064 -396 -357 -232 O ATOM 548 CB THR A 70 -18.926 -4.204 -35.840 1.00 49.06 C ANISOU 548 CB THR A 70 5515 4763 8361 -330 -378 -67 C ATOM 549 OG1 THR A 70 -20.100 -4.519 -36.591 1.00 48.92 O ANISOU 549 OG1 THR A 70 5650 4713 8223 -392 -342 -64 O ATOM 550 CG2 THR A 70 -19.283 -3.952 -34.393 1.00 48.57 C ANISOU 550 CG2 THR A 70 5405 4805 8245 -356 -513 -87 C ATOM 551 N MET A 71 -16.268 -2.559 -35.313 1.00 54.06 N ANISOU 551 N MET A 71 5666 5422 9451 -235 -372 -195 N ATOM 552 CA MET A 71 -15.381 -1.850 -34.419 1.00 55.65 C ANISOU 552 CA MET A 71 5616 5687 9839 -219 -481 -316 C ATOM 553 C MET A 71 -15.027 -0.472 -34.996 1.00 56.24 C ANISOU 553 C MET A 71 5519 5685 10162 -297 -324 -387 C ATOM 554 O MET A 71 -14.960 0.492 -34.248 1.00 55.70 O ANISOU 554 O MET A 71 5291 5668 10202 -356 -410 -512 O ATOM 555 CB MET A 71 -14.112 -2.673 -34.175 1.00 57.61 C ANISOU 555 CB MET A 71 5748 5937 10204 -80 -542 -332 C ATOM 556 CG MET A 71 -13.041 -1.954 -33.375 1.00 59.44 C ANISOU 556 CG MET A 71 5662 6237 10685 -47 -677 -508 C ATOM 557 SD MET A 71 -11.906 -1.064 -34.450 1.00 60.92 S ANISOU 557 SD MET A 71 5571 6264 11309 -98 -425 -576 S ATOM 558 CE MET A 71 -10.903 -2.407 -35.079 1.00 61.21 C ANISOU 558 CE MET A 71 5620 6235 11402 66 -339 -474 C ATOM 559 N MET A 72 -14.809 -0.390 -36.314 1.00 57.71 N ANISOU 559 N MET A 72 5760 5734 10432 -280 -77 -308 N ATOM 560 CA MET A 72 -14.285 0.837 -36.944 1.00 60.27 C ANISOU 560 CA MET A 72 5933 5933 11030 -319 151 -347 C ATOM 561 C MET A 72 -15.379 1.907 -36.998 1.00 61.15 C ANISOU 561 C MET A 72 6137 6055 11040 -404 198 -345 C ATOM 562 O MET A 72 -15.088 3.104 -36.847 1.00 64.93 O ANISOU 562 O MET A 72 6450 6470 11748 -471 299 -431 O ATOM 563 CB MET A 72 -13.773 0.589 -38.369 1.00 61.22 C ANISOU 563 CB MET A 72 6144 5889 11225 -226 446 -231 C ATOM 564 CG MET A 72 -12.395 -0.075 -38.443 1.00 62.43 C ANISOU 564 CG MET A 72 6122 5982 11616 -143 494 -247 C ATOM 565 SD MET A 72 -11.088 0.824 -37.570 1.00 64.82 S ANISOU 565 SD MET A 72 5957 6268 12400 -208 457 -456 S ATOM 566 CE MET A 72 -10.485 1.944 -38.835 1.00 66.14 C ANISOU 566 CE MET A 72 6037 6164 12926 -224 938 -409 C ATOM 567 N ALA A 73 -16.623 1.469 -37.234 1.00 59.98 N ANISOU 567 N ALA A 73 6239 5975 10576 -400 137 -260 N ATOM 568 CA ALA A 73 -17.773 2.352 -37.303 1.00 58.19 C ANISOU 568 CA ALA A 73 6108 5779 10219 -452 160 -249 C ATOM 569 C ALA A 73 -18.106 2.864 -35.900 1.00 58.33 C ANISOU 569 C ALA A 73 6008 5911 10240 -547 -37 -357 C ATOM 570 O ALA A 73 -18.427 4.043 -35.720 1.00 58.37 O ANISOU 570 O ALA A 73 5961 5901 10315 -604 22 -405 O ATOM 571 CB ALA A 73 -18.932 1.620 -37.913 1.00 57.15 C ANISOU 571 CB ALA A 73 6224 5698 9791 -414 118 -166 C ATOM 572 N ARG A 74 -18.012 1.963 -34.916 1.00 58.30 N ANISOU 572 N ARG A 74 5990 6012 10148 -538 -257 -389 N ATOM 573 CA ARG A 74 -18.165 2.303 -33.510 1.00 59.52 C ANISOU 573 CA ARG A 74 6060 6280 10274 -572 -456 -495 C ATOM 574 C ARG A 74 -17.209 3.431 -33.092 1.00 62.61 C ANISOU 574 C ARG A 74 6195 6634 10959 -610 -452 -662 C ATOM 575 O ARG A 74 -17.541 4.191 -32.173 1.00 64.75 O ANISOU 575 O ARG A 74 6414 6970 11218 -655 -563 -770 O ATOM 576 CB ARG A 74 -17.885 1.086 -32.633 1.00 60.49 C ANISOU 576 CB ARG A 74 6220 6492 10272 -488 -650 -489 C ATOM 577 CG ARG A 74 -18.504 1.173 -31.247 1.00 61.91 C ANISOU 577 CG ARG A 74 6448 6798 10277 -476 -836 -536 C ATOM 578 CD ARG A 74 -17.502 1.446 -30.157 1.00 65.44 C ANISOU 578 CD ARG A 74 6716 7325 10820 -394 -1031 -702 C ATOM 579 NE ARG A 74 -16.513 0.377 -30.076 1.00 68.92 N ANISOU 579 NE ARG A 74 7118 7780 11285 -258 -1112 -690 N ATOM 580 CZ ARG A 74 -15.231 0.567 -29.774 1.00 70.88 C ANISOU 580 CZ ARG A 74 7122 8056 11751 -184 -1228 -846 C ATOM 581 NH1 ARG A 74 -14.369 -0.424 -29.906 1.00 71.47 N ANISOU 581 NH1 ARG A 74 7162 8132 11861 -52 -1265 -812 N ATOM 582 NH2 ARG A 74 -14.818 1.755 -29.364 1.00 73.12 N ANISOU 582 NH2 ARG A 74 7184 8357 12241 -243 -1301 -1053 N ATOM 583 N LYS A 75 -16.030 3.507 -33.730 1.00 62.94 N ANISOU 583 N LYS A 75 6068 6561 11282 -590 -319 -697 N ATOM 584 CA LYS A 75 -14.997 4.486 -33.416 1.00 65.90 C ANISOU 584 CA LYS A 75 6144 6866 12026 -642 -291 -886 C ATOM 585 C LYS A 75 -15.285 5.833 -34.100 1.00 67.50 C ANISOU 585 C LYS A 75 6335 6912 12399 -733 -12 -881 C ATOM 586 O LYS A 75 -14.928 6.874 -33.576 1.00 68.00 O ANISOU 586 O LYS A 75 6201 6925 12711 -817 -9 -1058 O ATOM 587 CB LYS A 75 -13.623 3.970 -33.849 1.00 67.89 C ANISOU 587 CB LYS A 75 6198 7039 12555 -582 -224 -920 C ATOM 588 CG LYS A 75 -13.151 2.711 -33.138 1.00 68.72 C ANISOU 588 CG LYS A 75 6288 7288 12531 -457 -490 -937 C ATOM 589 CD LYS A 75 -12.273 2.953 -31.932 1.00 71.09 C ANISOU 589 CD LYS A 75 6301 7696 13011 -420 -765 -1190 C ATOM 590 CE LYS A 75 -11.754 1.657 -31.341 1.00 72.13 C ANISOU 590 CE LYS A 75 6449 7965 12991 -237 -1000 -1177 C ATOM 591 NZ LYS A 75 -10.304 1.718 -31.032 1.00 75.74 N ANISOU 591 NZ LYS A 75 6533 8439 13806 -166 -1118 -1391 N ATOM 592 N MET A 76 -15.899 5.807 -35.286 1.00 69.70 N ANISOU 592 N MET A 76 6833 7105 12545 -697 226 -690 N ATOM 593 CA MET A 76 -16.431 7.013 -35.918 1.00 72.80 C ANISOU 593 CA MET A 76 7300 7369 12989 -727 487 -640 C ATOM 594 C MET A 76 -17.566 7.610 -35.077 1.00 75.33 C ANISOU 594 C MET A 76 7699 7807 13113 -787 331 -685 C ATOM 595 O MET A 76 -17.633 8.825 -34.945 1.00 79.68 O ANISOU 595 O MET A 76 8181 8263 13828 -850 463 -757 O ATOM 596 CB MET A 76 -16.993 6.731 -37.311 1.00 74.48 C ANISOU 596 CB MET A 76 7782 7516 12999 -611 710 -428 C ATOM 597 CG MET A 76 -15.953 6.335 -38.320 1.00 78.01 C ANISOU 597 CG MET A 76 8203 7807 13626 -524 951 -355 C ATOM 598 SD MET A 76 -16.686 6.174 -39.968 1.00 81.13 S ANISOU 598 SD MET A 76 8966 8130 13728 -332 1208 -129 S ATOM 599 CE MET A 76 -15.266 6.653 -40.958 1.00 84.78 C ANISOU 599 CE MET A 76 9331 8301 14581 -254 1666 -70 C ATOM 600 N LYS A 77 -18.475 6.778 -34.548 1.00 76.37 N ANISOU 600 N LYS A 77 7983 8119 12914 -765 93 -634 N ATOM 601 CA LYS A 77 -19.584 7.299 -33.745 1.00 79.69 C ANISOU 601 CA LYS A 77 8481 8645 13152 -809 -25 -661 C ATOM 602 C LYS A 77 -19.064 7.755 -32.375 1.00 81.12 C ANISOU 602 C LYS A 77 8478 8880 13463 -866 -218 -869 C ATOM 603 O LYS A 77 -19.777 8.440 -31.646 1.00 82.87 O ANISOU 603 O LYS A 77 8736 9154 13594 -902 -283 -926 O ATOM 604 CB LYS A 77 -20.733 6.290 -33.616 1.00 83.52 C ANISOU 604 CB LYS A 77 9165 9272 13294 -773 -171 -547 C ATOM 605 CG LYS A 77 -20.657 5.301 -32.453 1.00 87.29 C ANISOU 605 CG LYS A 77 9639 9880 13648 -759 -424 -590 C ATOM 606 CD LYS A 77 -22.004 4.662 -32.106 1.00 88.24 C ANISOU 606 CD LYS A 77 9937 10101 13486 -757 -505 -496 C ATOM 607 CE LYS A 77 -21.913 3.192 -31.731 1.00 87.13 C ANISOU 607 CE LYS A 77 9875 10010 13220 -706 -623 -441 C ATOM 608 NZ LYS A 77 -21.745 2.318 -32.920 1.00 85.04 N ANISOU 608 NZ LYS A 77 9676 9677 12958 -680 -533 -354 N ATOM 609 N ASP A 78 -17.831 7.366 -32.030 1.00 83.08 N ANISOU 609 N ASP A 78 8530 9123 13913 -853 -321 -995 N ATOM 610 CA ASP A 78 -17.158 7.860 -30.825 1.00 85.00 C ANISOU 610 CA ASP A 78 8562 9417 14317 -879 -529 -1248 C ATOM 611 C ASP A 78 -16.705 9.314 -31.014 1.00 83.86 C ANISOU 611 C ASP A 78 8227 9095 14541 -992 -337 -1405 C ATOM 612 O ASP A 78 -16.876 10.127 -30.108 1.00 83.03 O ANISOU 612 O ASP A 78 8059 9017 14471 -1040 -452 -1585 O ATOM 613 CB ASP A 78 -15.964 6.987 -30.428 1.00 87.71 C ANISOU 613 CB ASP A 78 8728 9823 14773 -800 -721 -1356 C ATOM 614 CG ASP A 78 -16.264 6.014 -29.302 1.00 89.12 C ANISOU 614 CG ASP A 78 9032 10208 14618 -673 -1034 -1355 C ATOM 615 OD1 ASP A 78 -17.126 6.350 -28.456 1.00 89.09 O ANISOU 615 OD1 ASP A 78 9160 10295 14391 -666 -1145 -1379 O ATOM 616 OD2 ASP A 78 -15.632 4.926 -29.281 1.00 91.57 O ANISOU 616 OD2 ASP A 78 9326 10574 14893 -563 -1136 -1318 O ATOM 617 N THR A 79 -16.123 9.633 -32.175 1.00 83.16 N ANISOU 617 N THR A 79 8060 8806 14732 -1023 -22 -1339 N ATOM 618 CA THR A 79 -15.531 10.956 -32.386 1.00 87.34 C ANISOU 618 CA THR A 79 8384 9112 15687 -1132 221 -1490 C ATOM 619 C THR A 79 -16.637 12.024 -32.482 1.00 85.90 C ANISOU 619 C THR A 79 8386 8865 15385 -1169 389 -1419 C ATOM 620 O THR A 79 -16.358 13.193 -32.240 1.00 89.27 O ANISOU 620 O THR A 79 8667 9136 16113 -1268 520 -1588 O ATOM 621 CB THR A 79 -14.544 10.971 -33.567 1.00 88.91 C ANISOU 621 CB THR A 79 8456 9086 16238 -1132 565 -1422 C ATOM 622 OG1 THR A 79 -15.183 10.552 -34.772 1.00 87.98 O ANISOU 622 OG1 THR A 79 8632 8929 15864 -1027 796 -1119 O ATOM 623 CG2 THR A 79 -13.338 10.087 -33.336 1.00 90.34 C ANISOU 623 CG2 THR A 79 8389 9320 16616 -1103 396 -1541 C ATOM 624 N ASP A 80 -17.883 11.620 -32.780 1.00 82.88 N ANISOU 624 N ASP A 80 8303 8602 14585 -1088 373 -1195 N ATOM 625 CA ASP A 80 -19.021 12.554 -32.922 1.00 81.57 C ANISOU 625 CA ASP A 80 8319 8400 14271 -1086 520 -1106 C ATOM 626 C ASP A 80 -19.883 12.643 -31.652 1.00 80.62 C ANISOU 626 C ASP A 80 8263 8464 13903 -1104 238 -1196 C ATOM 627 O ASP A 80 -20.794 13.464 -31.607 1.00 81.47 O ANISOU 627 O ASP A 80 8494 8550 13910 -1104 340 -1150 O ATOM 628 CB ASP A 80 -19.984 12.139 -34.034 1.00 79.88 C ANISOU 628 CB ASP A 80 8378 8218 13754 -964 662 -830 C ATOM 629 CG ASP A 80 -19.341 11.843 -35.374 1.00 80.66 C ANISOU 629 CG ASP A 80 8511 8168 13968 -883 930 -693 C ATOM 630 OD1 ASP A 80 -18.431 12.609 -35.770 1.00 81.09 O ANISOU 630 OD1 ASP A 80 8428 7992 14388 -919 1213 -747 O ATOM 631 OD2 ASP A 80 -19.775 10.846 -36.013 1.00 79.04 O ANISOU 631 OD2 ASP A 80 8473 8065 13492 -779 870 -540 O ATOM 632 N SER A 81 -19.629 11.797 -30.645 1.00 81.18 N ANISOU 632 N SER A 81 8277 8711 13856 -1089 -91 -1303 N ATOM 633 CA SER A 81 -20.585 11.589 -29.528 1.00 80.59 C ANISOU 633 CA SER A 81 8340 8823 13455 -1052 -330 -1315 C ATOM 634 C SER A 81 -20.927 12.918 -28.834 1.00 77.62 C ANISOU 634 C SER A 81 7944 8391 13155 -1109 -300 -1471 C ATOM 635 O SER A 81 -22.105 13.233 -28.633 1.00 72.40 O ANISOU 635 O SER A 81 7461 7785 12262 -1084 -266 -1368 O ATOM 636 CB SER A 81 -20.071 10.581 -28.526 1.00 82.38 C ANISOU 636 CB SER A 81 8520 9213 13566 -984 -649 -1417 C ATOM 637 OG SER A 81 -19.414 11.242 -27.451 1.00 86.41 O ANISOU 637 OG SER A 81 8867 9738 14224 -999 -832 -1707 O ATOM 638 N GLU A 82 -19.887 13.673 -28.461 1.00 78.30 N ANISOU 638 N GLU A 82 7799 8363 13587 -1186 -314 -1736 N ATOM 639 CA GLU A 82 -20.036 14.941 -27.751 1.00 80.32 C ANISOU 639 CA GLU A 82 8010 8538 13966 -1252 -298 -1942 C ATOM 640 C GLU A 82 -21.101 15.798 -28.456 1.00 78.12 C ANISOU 640 C GLU A 82 7917 8144 13621 -1261 17 -1747 C ATOM 641 O GLU A 82 -22.000 16.312 -27.784 1.00 75.33 O ANISOU 641 O GLU A 82 7697 7849 13076 -1240 -26 -1759 O ATOM 642 CB GLU A 82 -18.686 15.654 -27.635 1.00 84.34 C ANISOU 642 CB GLU A 82 8200 8873 14972 -1364 -274 -2256 C ATOM 643 CG GLU A 82 -18.700 16.822 -26.660 1.00 88.36 C ANISOU 643 CG GLU A 82 8636 9320 15616 -1432 -349 -2556 C ATOM 644 CD GLU A 82 -17.341 17.308 -26.168 1.00 94.44 C ANISOU 644 CD GLU A 82 9042 9984 16855 -1532 -476 -2970 C ATOM 645 OE1 GLU A 82 -17.274 18.466 -25.712 1.00 96.92 O ANISOU 645 OE1 GLU A 82 9268 10152 17403 -1629 -424 -3223 O ATOM 646 OE2 GLU A 82 -16.349 16.528 -26.220 1.00 95.70 O ANISOU 646 OE2 GLU A 82 8993 10207 17162 -1510 -637 -3059 O ATOM 647 N GLU A 83 -21.015 15.896 -29.795 1.00 77.29 N ANISOU 647 N GLU A 83 7838 7887 13642 -1257 330 -1558 N ATOM 648 CA GLU A 83 -21.919 16.710 -30.634 1.00 77.92 C ANISOU 648 CA GLU A 83 8099 7848 13657 -1212 650 -1360 C ATOM 649 C GLU A 83 -23.291 16.032 -30.794 1.00 76.29 C ANISOU 649 C GLU A 83 8130 7850 13006 -1095 557 -1122 C ATOM 650 O GLU A 83 -24.328 16.655 -30.568 1.00 74.16 O ANISOU 650 O GLU A 83 7991 7608 12575 -1056 608 -1065 O ATOM 651 CB GLU A 83 -21.293 16.974 -32.004 1.00 79.48 C ANISOU 651 CB GLU A 83 8273 7816 14107 -1193 1016 -1237 C ATOM 652 CG GLU A 83 -21.985 18.091 -32.786 1.00 82.99 C ANISOU 652 CG GLU A 83 8893 8083 14553 -1118 1391 -1079 C ATOM 653 CD GLU A 83 -21.536 19.527 -32.500 1.00 84.92 C ANISOU 653 CD GLU A 83 9030 8051 15182 -1223 1648 -1256 C ATOM 654 OE1 GLU A 83 -21.816 20.044 -31.386 1.00 83.60 O ANISOU 654 OE1 GLU A 83 8820 7931 15011 -1302 1477 -1450 O ATOM 655 OE2 GLU A 83 -20.913 20.138 -33.403 1.00 84.97 O ANISOU 655 OE2 GLU A 83 9011 7775 15498 -1218 2047 -1200 O ATOM 656 N GLU A 84 -23.276 14.762 -31.213 1.00 77.23 N ANISOU 656 N GLU A 84 8285 8097 12961 -1042 433 -999 N ATOM 657 CA GLU A 84 -24.460 13.906 -31.361 1.00 75.15 C ANISOU 657 CA GLU A 84 8192 8022 12338 -957 319 -818 C ATOM 658 C GLU A 84 -25.375 14.008 -30.133 1.00 70.70 C ANISOU 658 C GLU A 84 7689 7600 11572 -964 143 -868 C ATOM 659 O GLU A 84 -26.591 13.989 -30.260 1.00 68.12 O ANISOU 659 O GLU A 84 7488 7360 11033 -905 166 -737 O ATOM 660 CB GLU A 84 -24.012 12.454 -31.524 1.00 80.06 C ANISOU 660 CB GLU A 84 8792 8745 12882 -943 151 -776 C ATOM 661 CG GLU A 84 -24.747 11.685 -32.612 1.00 83.25 C ANISOU 661 CG GLU A 84 9336 9208 13086 -853 199 -578 C ATOM 662 CD GLU A 84 -24.492 10.190 -32.503 1.00 87.22 C ANISOU 662 CD GLU A 84 9837 9815 13487 -852 9 -554 C ATOM 663 OE1 GLU A 84 -23.319 9.766 -32.710 1.00 91.27 O ANISOU 663 OE1 GLU A 84 10253 10263 14163 -864 8 -602 O ATOM 664 OE2 GLU A 84 -25.446 9.459 -32.158 1.00 86.04 O ANISOU 664 OE2 GLU A 84 9771 9796 13121 -840 -119 -494 O ATOM 665 N ILE A 85 -24.765 14.060 -28.946 1.00 69.57 N ANISOU 665 N ILE A 85 7453 7485 11492 -1015 -39 -1066 N ATOM 666 CA ILE A 85 -25.465 14.286 -27.702 1.00 69.31 C ANISOU 666 CA ILE A 85 7498 7558 11276 -995 -179 -1136 C ATOM 667 C ILE A 85 -26.064 15.693 -27.714 1.00 71.18 C ANISOU 667 C ILE A 85 7783 7687 11574 -1007 15 -1157 C ATOM 668 O ILE A 85 -27.256 15.843 -27.500 1.00 71.53 O ANISOU 668 O ILE A 85 7958 7808 11410 -952 47 -1045 O ATOM 669 CB ILE A 85 -24.539 14.078 -26.490 1.00 70.35 C ANISOU 669 CB ILE A 85 7535 7745 11449 -999 -434 -1373 C ATOM 670 CG1 ILE A 85 -24.411 12.595 -26.148 1.00 69.89 C ANISOU 670 CG1 ILE A 85 7521 7840 11192 -925 -638 -1300 C ATOM 671 CG2 ILE A 85 -25.012 14.885 -25.290 1.00 71.24 C ANISOU 671 CG2 ILE A 85 7721 7888 11457 -974 -511 -1517 C ATOM 672 CD1 ILE A 85 -23.428 12.315 -25.038 1.00 72.51 C ANISOU 672 CD1 ILE A 85 7772 8245 11531 -869 -908 -1526 C ATOM 673 N ARG A 86 -25.232 16.712 -27.957 1.00 73.25 N ANISOU 673 N ARG A 86 7930 7753 12146 -1077 164 -1303 N ATOM 674 CA ARG A 86 -25.710 18.096 -27.997 1.00 74.98 C ANISOU 674 CA ARG A 86 8205 7826 12456 -1085 391 -1327 C ATOM 675 C ARG A 86 -26.915 18.198 -28.935 1.00 72.08 C ANISOU 675 C ARG A 86 8003 7487 11897 -977 585 -1051 C ATOM 676 O ARG A 86 -27.953 18.739 -28.567 1.00 72.07 O ANISOU 676 O ARG A 86 8114 7528 11739 -921 628 -998 O ATOM 677 CB ARG A 86 -24.628 19.076 -28.467 1.00 80.52 C ANISOU 677 CB ARG A 86 8758 8256 13578 -1179 619 -1476 C ATOM 678 CG ARG A 86 -23.941 19.855 -27.352 1.00 85.56 C ANISOU 678 CG ARG A 86 9257 8804 14444 -1283 510 -1819 C ATOM 679 CD ARG A 86 -23.551 21.260 -27.785 1.00 90.70 C ANISOU 679 CD ARG A 86 9843 9139 15477 -1366 857 -1921 C ATOM 680 NE ARG A 86 -22.552 21.881 -26.916 1.00 95.10 N ANISOU 680 NE ARG A 86 10182 9571 16378 -1502 747 -2314 N ATOM 681 CZ ARG A 86 -22.766 22.270 -25.658 1.00 97.53 C ANISOU 681 CZ ARG A 86 10510 9957 16590 -1509 516 -2556 C ATOM 682 NH1 ARG A 86 -23.914 21.995 -25.054 1.00 95.49 N ANISOU 682 NH1 ARG A 86 10480 9907 15892 -1386 376 -2420 N ATOM 683 NH2 ARG A 86 -21.824 22.930 -25.006 1.00100.88 N ANISOU 683 NH2 ARG A 86 10717 10240 17370 -1630 429 -2949 N ATOM 684 N GLU A 87 -26.772 17.665 -30.150 1.00 71.09 N ANISOU 684 N GLU A 87 7889 7343 11776 -926 689 -887 N ATOM 685 CA GLU A 87 -27.755 17.910 -31.169 1.00 71.31 C ANISOU 685 CA GLU A 87 8061 7380 11650 -788 872 -668 C ATOM 686 C GLU A 87 -29.034 17.147 -30.822 1.00 66.92 C ANISOU 686 C GLU A 87 7581 7063 10781 -727 679 -567 C ATOM 687 O GLU A 87 -30.066 17.473 -31.365 1.00 66.89 O ANISOU 687 O GLU A 87 7672 7104 10636 -607 776 -431 O ATOM 688 CB GLU A 87 -27.202 17.607 -32.563 1.00 74.86 C ANISOU 688 CB GLU A 87 8531 7736 12174 -715 1040 -544 C ATOM 689 CG GLU A 87 -27.397 16.185 -33.041 1.00 78.50 C ANISOU 689 CG GLU A 87 9011 8374 12442 -672 849 -447 C ATOM 690 CD GLU A 87 -26.764 15.885 -34.396 1.00 84.09 C ANISOU 690 CD GLU A 87 9760 8980 13208 -580 1017 -340 C ATOM 691 OE1 GLU A 87 -26.523 16.853 -35.162 1.00 87.42 O ANISOU 691 OE1 GLU A 87 10254 9210 13750 -490 1330 -273 O ATOM 692 OE2 GLU A 87 -26.509 14.680 -34.690 1.00 87.38 O ANISOU 692 OE2 GLU A 87 10158 9494 13546 -583 862 -316 O ATOM 693 N ALA A 88 -28.953 16.182 -29.894 1.00 63.43 N ANISOU 693 N ALA A 88 7090 6758 10250 -798 426 -638 N ATOM 694 CA ALA A 88 -30.123 15.421 -29.395 1.00 60.37 C ANISOU 694 CA ALA A 88 6757 6559 9619 -762 283 -555 C ATOM 695 C ALA A 88 -30.897 16.202 -28.324 1.00 58.21 C ANISOU 695 C ALA A 88 6541 6310 9266 -749 299 -599 C ATOM 696 O ALA A 88 -32.110 16.040 -28.191 1.00 57.81 O ANISOU 696 O ALA A 88 6537 6367 9059 -690 302 -496 O ATOM 697 CB ALA A 88 -29.678 14.091 -28.845 1.00 60.26 C ANISOU 697 CB ALA A 88 6707 6641 9547 -814 70 -588 C ATOM 698 N PHE A 89 -30.176 16.997 -27.529 1.00 57.10 N ANISOU 698 N PHE A 89 6382 6068 9245 -802 301 -773 N ATOM 699 CA PHE A 89 -30.754 17.933 -26.546 1.00 56.29 C ANISOU 699 CA PHE A 89 6353 5948 9084 -780 341 -847 C ATOM 700 C PHE A 89 -31.636 18.968 -27.261 1.00 55.49 C ANISOU 700 C PHE A 89 6317 5778 8989 -699 586 -725 C ATOM 701 O PHE A 89 -32.788 19.178 -26.911 1.00 54.51 O ANISOU 701 O PHE A 89 6264 5736 8712 -623 622 -641 O ATOM 702 CB PHE A 89 -29.629 18.630 -25.782 1.00 57.02 C ANISOU 702 CB PHE A 89 6389 5917 9357 -856 289 -1107 C ATOM 703 CG PHE A 89 -30.085 19.428 -24.595 1.00 57.86 C ANISOU 703 CG PHE A 89 6590 6019 9375 -825 273 -1230 C ATOM 704 CD1 PHE A 89 -30.225 18.824 -23.357 1.00 58.05 C ANISOU 704 CD1 PHE A 89 6687 6181 9187 -775 62 -1301 C ATOM 705 CD2 PHE A 89 -30.370 20.778 -24.717 1.00 58.08 C ANISOU 705 CD2 PHE A 89 6660 5890 9516 -821 492 -1268 C ATOM 706 CE1 PHE A 89 -30.633 19.563 -22.258 1.00 59.77 C ANISOU 706 CE1 PHE A 89 7022 6392 9294 -718 54 -1420 C ATOM 707 CE2 PHE A 89 -30.789 21.511 -23.621 1.00 59.47 C ANISOU 707 CE2 PHE A 89 6939 6053 9603 -785 482 -1393 C ATOM 708 CZ PHE A 89 -30.919 20.904 -22.393 1.00 60.53 C ANISOU 708 CZ PHE A 89 7149 6336 9512 -731 255 -1473 C ATOM 709 N ARG A 90 -31.064 19.580 -28.301 1.00 55.27 N ANISOU 709 N ARG A 90 6267 5590 9142 -692 773 -705 N ATOM 710 CA ARG A 90 -31.743 20.504 -29.191 1.00 54.56 C ANISOU 710 CA ARG A 90 6263 5418 9047 -566 1028 -564 C ATOM 711 C ARG A 90 -32.963 19.868 -29.877 1.00 51.77 C ANISOU 711 C ARG A 90 5947 5255 8468 -427 983 -367 C ATOM 712 O ARG A 90 -33.793 20.577 -30.421 1.00 51.88 O ANISOU 712 O ARG A 90 6036 5263 8410 -276 1140 -252 O ATOM 713 CB ARG A 90 -30.740 20.989 -30.241 1.00 57.04 C ANISOU 713 CB ARG A 90 6562 5518 9590 -565 1248 -557 C ATOM 714 CG ARG A 90 -29.623 21.854 -29.672 1.00 60.03 C ANISOU 714 CG ARG A 90 6867 5663 10276 -706 1352 -778 C ATOM 715 CD ARG A 90 -29.113 22.883 -30.666 1.00 62.98 C ANISOU 715 CD ARG A 90 7282 5754 10893 -660 1731 -725 C ATOM 716 NE ARG A 90 -28.118 22.312 -31.558 1.00 64.32 N ANISOU 716 NE ARG A 90 7376 5845 11217 -685 1791 -693 N ATOM 717 CZ ARG A 90 -26.808 22.499 -31.441 1.00 66.58 C ANISOU 717 CZ ARG A 90 7505 5934 11858 -839 1863 -876 C ATOM 718 NH1 ARG A 90 -26.330 23.558 -30.809 1.00 66.63 N ANISOU 718 NH1 ARG A 90 7438 5723 12155 -957 1995 -1085 N ATOM 719 NH2 ARG A 90 -25.981 21.585 -31.918 1.00 68.45 N ANISOU 719 NH2 ARG A 90 7637 6196 12172 -878 1784 -871 N ATOM 720 N VAL A 91 -33.043 18.535 -29.909 1.00 49.81 N ANISOU 720 N VAL A 91 5636 5165 8123 -467 772 -342 N ATOM 721 CA VAL A 91 -34.175 17.844 -30.491 1.00 48.34 C ANISOU 721 CA VAL A 91 5441 5154 7772 -365 697 -213 C ATOM 722 C VAL A 91 -35.303 17.818 -29.453 1.00 48.39 C ANISOU 722 C VAL A 91 5437 5275 7672 -366 643 -207 C ATOM 723 O VAL A 91 -36.462 18.017 -29.788 1.00 48.38 O ANISOU 723 O VAL A 91 5427 5368 7587 -247 682 -120 O ATOM 724 CB VAL A 91 -33.791 16.435 -30.984 1.00 47.48 C ANISOU 724 CB VAL A 91 5269 5128 7643 -418 527 -205 C ATOM 725 CG1 VAL A 91 -35.013 15.567 -31.248 1.00 47.10 C ANISOU 725 CG1 VAL A 91 5169 5261 7467 -366 406 -138 C ATOM 726 CG2 VAL A 91 -32.912 16.483 -32.227 1.00 47.46 C ANISOU 726 CG2 VAL A 91 5297 5021 7712 -361 620 -171 C ATOM 727 N PHE A 92 -34.945 17.590 -28.188 1.00 48.66 N ANISOU 727 N PHE A 92 5477 5302 7708 -476 559 -305 N ATOM 728 CA PHE A 92 -35.893 17.587 -27.090 1.00 49.37 C ANISOU 728 CA PHE A 92 5594 5470 7693 -461 551 -294 C ATOM 729 C PHE A 92 -36.294 19.010 -26.688 1.00 51.33 C ANISOU 729 C PHE A 92 5924 5634 7943 -388 720 -313 C ATOM 730 O PHE A 92 -37.449 19.246 -26.317 1.00 51.53 O ANISOU 730 O PHE A 92 5962 5730 7884 -310 788 -241 O ATOM 731 CB PHE A 92 -35.293 16.912 -25.862 1.00 50.42 C ANISOU 731 CB PHE A 92 5760 5615 7781 -546 416 -390 C ATOM 732 CG PHE A 92 -35.202 15.407 -25.936 1.00 50.35 C ANISOU 732 CG PHE A 92 5699 5693 7737 -597 278 -344 C ATOM 733 CD1 PHE A 92 -36.346 14.633 -26.092 1.00 50.27 C ANISOU 733 CD1 PHE A 92 5635 5782 7683 -580 291 -232 C ATOM 734 CD2 PHE A 92 -33.982 14.763 -25.798 1.00 49.80 C ANISOU 734 CD2 PHE A 92 5623 5594 7702 -662 146 -428 C ATOM 735 CE1 PHE A 92 -36.270 13.250 -26.147 1.00 49.48 C ANISOU 735 CE1 PHE A 92 5493 5725 7582 -638 197 -200 C ATOM 736 CE2 PHE A 92 -33.915 13.377 -25.836 1.00 50.08 C ANISOU 736 CE2 PHE A 92 5633 5692 7701 -694 44 -375 C ATOM 737 CZ PHE A 92 -35.055 12.625 -26.015 1.00 49.12 C ANISOU 737 CZ PHE A 92 5477 5643 7542 -689 81 -261 C ATOM 738 N ASP A 93 -35.328 19.938 -26.738 1.00 52.61 N ANISOU 738 N ASP A 93 6129 5629 8228 -420 805 -420 N ATOM 739 CA ASP A 93 -35.497 21.259 -26.187 1.00 53.89 C ANISOU 739 CA ASP A 93 6383 5671 8421 -380 964 -483 C ATOM 740 C ASP A 93 -35.990 22.201 -27.281 1.00 54.73 C ANISOU 740 C ASP A 93 6526 5700 8567 -245 1192 -359 C ATOM 741 O ASP A 93 -35.314 23.165 -27.617 1.00 54.89 O ANISOU 741 O ASP A 93 6594 5520 8739 -249 1367 -414 O ATOM 742 CB ASP A 93 -34.219 21.798 -25.549 1.00 55.26 C ANISOU 742 CB ASP A 93 6568 5680 8747 -494 941 -709 C ATOM 743 CG ASP A 93 -34.430 23.163 -24.909 1.00 57.12 C ANISOU 743 CG ASP A 93 6905 5772 9024 -461 1104 -809 C ATOM 744 OD1 ASP A 93 -35.538 23.396 -24.388 1.00 56.50 O ANISOU 744 OD1 ASP A 93 6908 5772 8785 -363 1156 -727 O ATOM 745 OD2 ASP A 93 -33.489 23.991 -24.948 1.00 59.43 O ANISOU 745 OD2 ASP A 93 7185 5860 9534 -537 1196 -974 O ATOM 746 N LYS A 94 -37.224 21.948 -27.733 1.00 55.40 N ANISOU 746 N LYS A 94 6589 5939 8521 -112 1199 -202 N ATOM 747 CA LYS A 94 -37.841 22.618 -28.880 1.00 55.91 C ANISOU 747 CA LYS A 94 6689 5995 8558 84 1362 -62 C ATOM 748 C LYS A 94 -38.238 24.072 -28.554 1.00 56.36 C ANISOU 748 C LYS A 94 6868 5913 8632 191 1606 -50 C ATOM 749 O LYS A 94 -38.276 24.883 -29.459 1.00 57.38 O ANISOU 749 O LYS A 94 7080 5940 8781 349 1806 41 O ATOM 750 CB LYS A 94 -39.040 21.794 -29.362 1.00 55.90 C ANISOU 750 CB LYS A 94 6582 6229 8428 192 1231 46 C ATOM 751 CG LYS A 94 -38.696 20.362 -29.751 1.00 55.45 C ANISOU 751 CG LYS A 94 6414 6284 8368 89 1011 26 C ATOM 752 CD LYS A 94 -39.542 19.791 -30.869 1.00 55.81 C ANISOU 752 CD LYS A 94 6370 6500 8335 238 913 103 C ATOM 753 CE LYS A 94 -39.283 18.317 -31.105 1.00 54.94 C ANISOU 753 CE LYS A 94 6150 6485 8238 113 699 58 C ATOM 754 NZ LYS A 94 -38.218 18.085 -32.111 1.00 54.52 N ANISOU 754 NZ LYS A 94 6159 6357 8197 127 686 56 N ATOM 755 N ASP A 95 -38.534 24.404 -27.290 1.00 55.69 N ANISOU 755 N ASP A 95 6819 5814 8526 132 1611 -133 N ATOM 756 CA ASP A 95 -38.806 25.798 -26.925 1.00 57.00 C ANISOU 756 CA ASP A 95 7116 5818 8723 221 1851 -146 C ATOM 757 C ASP A 95 -37.480 26.568 -26.841 1.00 58.14 C ANISOU 757 C ASP A 95 7326 5687 9075 97 1975 -310 C ATOM 758 O ASP A 95 -37.448 27.768 -27.021 1.00 60.05 O ANISOU 758 O ASP A 95 7678 5725 9410 171 2237 -308 O ATOM 759 CB ASP A 95 -39.672 25.915 -25.669 1.00 57.94 C ANISOU 759 CB ASP A 95 7269 6013 8730 236 1835 -172 C ATOM 760 CG ASP A 95 -39.139 25.239 -24.421 1.00 58.41 C ANISOU 760 CG ASP A 95 7331 6104 8758 71 1647 -333 C ATOM 761 OD1 ASP A 95 -38.236 24.384 -24.542 1.00 57.91 O ANISOU 761 OD1 ASP A 95 7194 6064 8742 -60 1469 -408 O ATOM 762 OD2 ASP A 95 -39.663 25.550 -23.334 1.00 59.54 O ANISOU 762 OD2 ASP A 95 7562 6253 8807 105 1683 -374 O ATOM 763 N GLY A 96 -36.376 25.851 -26.634 1.00 57.36 N ANISOU 763 N GLY A 96 7145 5574 9076 -87 1799 -453 N ATOM 764 CA GLY A 96 -35.054 26.400 -26.784 1.00 57.57 C ANISOU 764 CA GLY A 96 7161 5352 9360 -214 1900 -616 C ATOM 765 C GLY A 96 -34.538 26.994 -25.490 1.00 59.26 C ANISOU 765 C GLY A 96 7400 5440 9673 -341 1859 -885 C ATOM 766 O GLY A 96 -33.521 27.683 -25.494 1.00 62.15 O ANISOU 766 O GLY A 96 7739 5564 10310 -455 1972 -1070 O ATOM 767 N ASN A 97 -35.207 26.689 -24.374 1.00 58.74 N ANISOU 767 N ASN A 97 7383 5534 9401 -318 1698 -923 N ATOM 768 CA ASN A 97 -34.966 27.386 -23.117 1.00 60.62 C ANISOU 768 CA ASN A 97 7703 5669 9661 -367 1671 -1169 C ATOM 769 C ASN A 97 -33.845 26.712 -22.311 1.00 60.78 C ANISOU 769 C ASN A 97 7639 5729 9724 -509 1370 -1434 C ATOM 770 O ASN A 97 -33.552 27.131 -21.192 1.00 62.07 O ANISOU 770 O ASN A 97 7867 5844 9870 -531 1269 -1684 O ATOM 771 CB ASN A 97 -36.261 27.527 -22.311 1.00 60.73 C ANISOU 771 CB ASN A 97 7850 5808 9416 -224 1698 -1071 C ATOM 772 CG ASN A 97 -36.675 26.265 -21.589 1.00 59.27 C ANISOU 772 CG ASN A 97 7653 5875 8990 -204 1454 -1018 C ATOM 773 OD1 ASN A 97 -36.359 25.158 -22.017 1.00 57.90 O ANISOU 773 OD1 ASN A 97 7366 5827 8804 -260 1292 -953 O ATOM 774 ND2 ASN A 97 -37.392 26.427 -20.492 1.00 59.87 N ANISOU 774 ND2 ASN A 97 7863 6006 8875 -111 1458 -1036 N ATOM 775 N GLY A 98 -33.223 25.675 -22.878 1.00 59.93 N ANISOU 775 N GLY A 98 7397 5716 9658 -579 1216 -1390 N ATOM 776 CA GLY A 98 -32.110 24.977 -22.238 1.00 61.18 C ANISOU 776 CA GLY A 98 7457 5923 9863 -684 926 -1624 C ATOM 777 C GLY A 98 -32.549 24.046 -21.117 1.00 61.14 C ANISOU 777 C GLY A 98 7541 6148 9538 -601 676 -1622 C ATOM 778 O GLY A 98 -31.720 23.478 -20.419 1.00 62.60 O ANISOU 778 O GLY A 98 7689 6399 9695 -629 417 -1816 O ATOM 779 N TYR A 99 -33.859 23.886 -20.938 1.00 61.03 N ANISOU 779 N TYR A 99 7647 6251 9289 -478 770 -1399 N ATOM 780 CA TYR A 99 -34.401 22.954 -19.966 1.00 61.41 C ANISOU 780 CA TYR A 99 7796 6489 9048 -383 618 -1339 C ATOM 781 C TYR A 99 -35.344 21.994 -20.701 1.00 58.74 C ANISOU 781 C TYR A 99 7401 6292 8626 -350 682 -1032 C ATOM 782 O TYR A 99 -36.140 22.438 -21.527 1.00 56.58 O ANISOU 782 O TYR A 99 7093 5997 8406 -317 873 -867 O ATOM 783 CB TYR A 99 -35.107 23.712 -18.840 1.00 64.23 C ANISOU 783 CB TYR A 99 8348 6823 9230 -262 695 -1404 C ATOM 784 CG TYR A 99 -34.212 24.577 -17.988 1.00 67.39 C ANISOU 784 CG TYR A 99 8813 7098 9691 -281 587 -1757 C ATOM 785 CD1 TYR A 99 -33.345 24.014 -17.064 1.00 68.96 C ANISOU 785 CD1 TYR A 99 9044 7378 9781 -253 289 -1986 C ATOM 786 CD2 TYR A 99 -34.243 25.962 -18.086 1.00 69.42 C ANISOU 786 CD2 TYR A 99 9104 7153 10117 -310 776 -1881 C ATOM 787 CE1 TYR A 99 -32.522 24.798 -16.272 1.00 71.96 C ANISOU 787 CE1 TYR A 99 9458 7658 10224 -259 141 -2363 C ATOM 788 CE2 TYR A 99 -33.425 26.763 -17.302 1.00 72.16 C ANISOU 788 CE2 TYR A 99 9489 7367 10559 -344 667 -2252 C ATOM 789 CZ TYR A 99 -32.562 26.177 -16.391 1.00 73.97 C ANISOU 789 CZ TYR A 99 9722 7698 10683 -321 329 -2511 C ATOM 790 OH TYR A 99 -31.754 26.946 -15.608 1.00 78.35 O ANISOU 790 OH TYR A 99 10292 8141 11337 -342 174 -2925 O ATOM 791 N ILE A 100 -35.204 20.691 -20.415 1.00 58.41 N ANISOU 791 N ILE A 100 7344 6385 8465 -349 515 -979 N ATOM 792 CA ILE A 100 -36.052 19.632 -20.972 1.00 57.82 C ANISOU 792 CA ILE A 100 7201 6431 8334 -337 552 -736 C ATOM 793 C ILE A 100 -37.173 19.309 -19.988 1.00 58.76 C ANISOU 793 C ILE A 100 7445 6629 8252 -222 637 -621 C ATOM 794 O ILE A 100 -36.903 18.931 -18.851 1.00 59.94 O ANISOU 794 O ILE A 100 7738 6805 8229 -151 548 -694 O ATOM 795 CB ILE A 100 -35.255 18.358 -21.280 1.00 57.57 C ANISOU 795 CB ILE A 100 7085 6463 8324 -408 369 -734 C ATOM 796 CG1 ILE A 100 -34.227 18.589 -22.389 1.00 58.39 C ANISOU 796 CG1 ILE A 100 7052 6484 8647 -513 332 -809 C ATOM 797 CG2 ILE A 100 -36.204 17.227 -21.627 1.00 56.66 C ANISOU 797 CG2 ILE A 100 6918 6454 8154 -398 413 -520 C ATOM 798 CD1 ILE A 100 -33.497 17.332 -22.806 1.00 57.99 C ANISOU 798 CD1 ILE A 100 6915 6493 8625 -572 175 -788 C ATOM 799 N SER A 101 -38.418 19.447 -20.451 1.00 58.70 N ANISOU 799 N SER A 101 7378 6657 8269 -183 815 -444 N ATOM 800 CA SER A 101 -39.582 19.152 -19.643 1.00 60.17 C ANISOU 800 CA SER A 101 7638 6896 8326 -83 953 -315 C ATOM 801 C SER A 101 -40.029 17.713 -19.909 1.00 60.19 C ANISOU 801 C SER A 101 7528 6984 8355 -127 938 -170 C ATOM 802 O SER A 101 -39.601 17.076 -20.881 1.00 60.10 O ANISOU 802 O SER A 101 7373 7001 8459 -227 824 -162 O ATOM 803 CB SER A 101 -40.692 20.121 -19.925 1.00 60.47 C ANISOU 803 CB SER A 101 7644 6920 8411 -8 1159 -227 C ATOM 804 OG SER A 101 -41.004 20.131 -21.309 1.00 59.30 O ANISOU 804 OG SER A 101 7301 6811 8419 -46 1167 -146 O ATOM 805 N ALA A 102 -40.899 17.218 -19.027 1.00 60.98 N ANISOU 805 N ALA A 102 7705 7101 8360 -47 1082 -59 N ATOM 806 CA ALA A 102 -41.600 15.979 -19.234 1.00 59.86 C ANISOU 806 CA ALA A 102 7438 7000 8304 -93 1152 84 C ATOM 807 C ALA A 102 -42.267 16.019 -20.612 1.00 59.03 C ANISOU 807 C ALA A 102 7059 6953 8415 -170 1152 129 C ATOM 808 O ALA A 102 -42.102 15.108 -21.421 1.00 59.46 O ANISOU 808 O ALA A 102 6965 7042 8583 -269 1048 138 O ATOM 809 CB ALA A 102 -42.605 15.782 -18.132 1.00 61.54 C ANISOU 809 CB ALA A 102 7763 7185 8432 20 1396 205 C ATOM 810 N ALA A 103 -42.998 17.104 -20.871 1.00 59.67 N ANISOU 810 N ALA A 103 7092 7046 8533 -97 1260 146 N ATOM 811 CA ALA A 103 -43.715 17.305 -22.120 1.00 59.78 C ANISOU 811 CA ALA A 103 6872 7135 8705 -97 1252 181 C ATOM 812 C ALA A 103 -42.780 17.079 -23.309 1.00 58.86 C ANISOU 812 C ALA A 103 6687 7036 8638 -173 1051 112 C ATOM 813 O ALA A 103 -43.158 16.454 -24.294 1.00 59.53 O ANISOU 813 O ALA A 103 6583 7199 8835 -205 973 129 O ATOM 814 CB ALA A 103 -44.291 18.694 -22.152 1.00 60.86 C ANISOU 814 CB ALA A 103 7042 7263 8819 32 1382 196 C ATOM 815 N GLU A 104 -41.556 17.594 -23.196 1.00 58.02 N ANISOU 815 N GLU A 104 6733 6852 8459 -195 974 19 N ATOM 816 CA GLU A 104 -40.618 17.583 -24.293 1.00 57.00 C ANISOU 816 CA GLU A 104 6560 6708 8389 -247 843 -35 C ATOM 817 C GLU A 104 -40.076 16.165 -24.485 1.00 56.00 C ANISOU 817 C GLU A 104 6372 6613 8290 -358 695 -44 C ATOM 818 O GLU A 104 -39.786 15.775 -25.617 1.00 55.28 O ANISOU 818 O GLU A 104 6184 6551 8269 -388 600 -48 O ATOM 819 CB GLU A 104 -39.533 18.633 -24.050 1.00 57.31 C ANISOU 819 CB GLU A 104 6743 6624 8408 -248 849 -149 C ATOM 820 CG GLU A 104 -40.020 20.043 -24.340 1.00 58.24 C ANISOU 820 CG GLU A 104 6901 6684 8541 -136 1015 -129 C ATOM 821 CD GLU A 104 -39.009 21.154 -24.125 1.00 59.03 C ANISOU 821 CD GLU A 104 7126 6619 8681 -155 1066 -262 C ATOM 822 OE1 GLU A 104 -39.040 22.152 -24.900 1.00 58.12 O ANISOU 822 OE1 GLU A 104 7027 6418 8635 -83 1204 -236 O ATOM 823 OE2 GLU A 104 -38.201 21.023 -23.180 1.00 58.69 O ANISOU 823 OE2 GLU A 104 7164 6526 8606 -226 974 -400 O ATOM 824 N LEU A 105 -39.932 15.415 -23.386 1.00 56.28 N ANISOU 824 N LEU A 105 6495 6634 8255 -390 690 -41 N ATOM 825 CA LEU A 105 -39.608 13.996 -23.476 1.00 56.81 C ANISOU 825 CA LEU A 105 6516 6717 8350 -474 597 -21 C ATOM 826 C LEU A 105 -40.773 13.274 -24.155 1.00 57.76 C ANISOU 826 C LEU A 105 6438 6900 8607 -507 644 52 C ATOM 827 O LEU A 105 -40.603 12.659 -25.193 1.00 58.96 O ANISOU 827 O LEU A 105 6470 7085 8847 -564 532 28 O ATOM 828 CB LEU A 105 -39.359 13.407 -22.084 1.00 57.64 C ANISOU 828 CB LEU A 105 6794 6785 8322 -444 630 -5 C ATOM 829 CG LEU A 105 -37.980 13.658 -21.477 1.00 57.58 C ANISOU 829 CG LEU A 105 6947 6741 8190 -417 487 -128 C ATOM 830 CD1 LEU A 105 -37.738 12.731 -20.295 1.00 57.83 C ANISOU 830 CD1 LEU A 105 7148 6761 8061 -344 486 -95 C ATOM 831 CD2 LEU A 105 -36.883 13.484 -22.514 1.00 56.61 C ANISOU 831 CD2 LEU A 105 6726 6612 8170 -506 321 -208 C ATOM 832 N ARG A 106 -41.963 13.390 -23.566 1.00 58.59 N ANISOU 832 N ARG A 106 6500 7017 8743 -461 812 122 N ATOM 833 CA ARG A 106 -43.156 12.731 -24.071 1.00 59.65 C ANISOU 833 CA ARG A 106 6400 7203 9062 -499 867 156 C ATOM 834 C ARG A 106 -43.288 12.919 -25.586 1.00 57.09 C ANISOU 834 C ARG A 106 5895 6972 8822 -488 710 91 C ATOM 835 O ARG A 106 -43.764 12.033 -26.287 1.00 58.57 O ANISOU 835 O ARG A 106 5890 7205 9158 -551 636 52 O ATOM 836 CB ARG A 106 -44.416 13.298 -23.411 1.00 63.00 C ANISOU 836 CB ARG A 106 6770 7634 9530 -418 1080 225 C ATOM 837 CG ARG A 106 -44.851 12.577 -22.144 1.00 65.54 C ANISOU 837 CG ARG A 106 7174 7865 9861 -430 1297 316 C ATOM 838 CD ARG A 106 -45.385 11.189 -22.434 1.00 67.22 C ANISOU 838 CD ARG A 106 7186 8045 10306 -556 1342 327 C ATOM 839 NE ARG A 106 -46.670 11.232 -23.115 1.00 68.94 N ANISOU 839 NE ARG A 106 7078 8334 10782 -575 1381 292 N ATOM 840 CZ ARG A 106 -47.789 10.683 -22.657 1.00 70.78 C ANISOU 840 CZ ARG A 106 7136 8506 11249 -616 1614 338 C ATOM 841 NH1 ARG A 106 -47.781 10.018 -21.513 1.00 71.77 N ANISOU 841 NH1 ARG A 106 7427 8481 11361 -629 1868 454 N ATOM 842 NH2 ARG A 106 -48.908 10.803 -23.349 1.00 71.22 N ANISOU 842 NH2 ARG A 106 6852 8648 11558 -624 1602 265 N ATOM 843 N HIS A 107 -42.931 14.108 -26.063 1.00 54.26 N ANISOU 843 N HIS A 107 5611 6633 8370 -387 677 74 N ATOM 844 CA HIS A 107 -43.221 14.507 -27.419 1.00 53.63 C ANISOU 844 CA HIS A 107 5411 6645 8320 -295 577 42 C ATOM 845 C HIS A 107 -42.352 13.692 -28.386 1.00 52.41 C ANISOU 845 C HIS A 107 5246 6493 8171 -358 401 -15 C ATOM 846 O HIS A 107 -42.817 13.361 -29.469 1.00 52.55 O ANISOU 846 O HIS A 107 5119 6605 8240 -307 284 -63 O ATOM 847 CB HIS A 107 -43.082 16.039 -27.577 1.00 52.52 C ANISOU 847 CB HIS A 107 5396 6483 8076 -145 661 69 C ATOM 848 CG HIS A 107 -43.277 16.513 -28.979 1.00 52.04 C ANISOU 848 CG HIS A 107 5276 6502 7994 8 585 62 C ATOM 849 ND1 HIS A 107 -44.525 16.676 -29.535 1.00 53.63 N ANISOU 849 ND1 HIS A 107 5299 6840 8238 151 562 64 N ATOM 850 CD2 HIS A 107 -42.391 16.809 -29.954 1.00 51.69 C ANISOU 850 CD2 HIS A 107 5331 6421 7884 71 531 53 C ATOM 851 CE1 HIS A 107 -44.404 17.065 -30.790 1.00 54.04 C ANISOU 851 CE1 HIS A 107 5369 6951 8209 322 478 57 C ATOM 852 NE2 HIS A 107 -43.101 17.159 -31.072 1.00 52.93 N ANISOU 852 NE2 HIS A 107 5413 6694 8002 276 482 63 N ATOM 853 N VAL A 108 -41.119 13.362 -27.967 1.00 52.12 N ANISOU 853 N VAL A 108 5360 6361 8081 -451 373 -25 N ATOM 854 CA VAL A 108 -40.077 12.747 -28.832 1.00 52.46 C ANISOU 854 CA VAL A 108 5428 6382 8119 -497 236 -69 C ATOM 855 C VAL A 108 -39.944 11.232 -28.578 1.00 52.52 C ANISOU 855 C VAL A 108 5384 6371 8197 -633 171 -86 C ATOM 856 O VAL A 108 -39.875 10.451 -29.525 1.00 52.66 O ANISOU 856 O VAL A 108 5322 6419 8267 -658 56 -133 O ATOM 857 CB VAL A 108 -38.722 13.464 -28.633 1.00 52.83 C ANISOU 857 CB VAL A 108 5644 6327 8101 -497 255 -84 C ATOM 858 CG1 VAL A 108 -37.549 12.654 -29.167 1.00 51.48 C ANISOU 858 CG1 VAL A 108 5498 6113 7948 -568 144 -121 C ATOM 859 CG2 VAL A 108 -38.724 14.862 -29.244 1.00 52.97 C ANISOU 859 CG2 VAL A 108 5715 6322 8087 -363 345 -69 C ATOM 860 N MET A 109 -39.865 10.824 -27.304 1.00 53.16 N ANISOU 860 N MET A 109 5544 6390 8264 -697 256 -48 N ATOM 861 CA MET A 109 -39.490 9.452 -26.910 1.00 52.82 C ANISOU 861 CA MET A 109 5522 6287 8257 -798 237 -38 C ATOM 862 C MET A 109 -40.528 8.437 -27.399 1.00 54.36 C ANISOU 862 C MET A 109 5522 6501 8631 -872 247 -59 C ATOM 863 O MET A 109 -41.717 8.593 -27.182 1.00 56.67 O ANISOU 863 O MET A 109 5681 6822 9026 -865 349 -48 O ATOM 864 CB MET A 109 -39.372 9.298 -25.391 1.00 53.20 C ANISOU 864 CB MET A 109 5726 6268 8219 -787 361 26 C ATOM 865 CG MET A 109 -38.111 9.869 -24.781 1.00 52.22 C ANISOU 865 CG MET A 109 5788 6116 7937 -734 293 -6 C ATOM 866 SD MET A 109 -36.584 9.236 -25.501 1.00 51.83 S ANISOU 866 SD MET A 109 5758 6043 7892 -782 108 -71 S ATOM 867 CE MET A 109 -36.753 7.470 -25.208 1.00 51.74 C ANISOU 867 CE MET A 109 5756 5979 7922 -840 144 -3 C ATOM 868 N THR A 110 -40.022 7.365 -28.008 1.00 55.02 N ANISOU 868 N THR A 110 5582 6552 8770 -947 148 -103 N ATOM 869 CA THR A 110 -40.788 6.255 -28.519 1.00 56.18 C ANISOU 869 CA THR A 110 5549 6685 9113 -1042 135 -168 C ATOM 870 C THR A 110 -40.060 4.973 -28.085 1.00 56.23 C ANISOU 870 C THR A 110 5662 6562 9140 -1133 174 -133 C ATOM 871 O THR A 110 -38.826 4.961 -28.001 1.00 53.80 O ANISOU 871 O THR A 110 5523 6230 8686 -1100 105 -104 O ATOM 872 CB THR A 110 -40.977 6.423 -30.035 1.00 56.67 C ANISOU 872 CB THR A 110 5476 6855 9198 -992 -58 -291 C ATOM 873 OG1 THR A 110 -41.939 5.477 -30.487 1.00 59.76 O ANISOU 873 OG1 THR A 110 5644 7248 9813 -1080 -91 -405 O ATOM 874 CG2 THR A 110 -39.713 6.231 -30.844 1.00 55.18 C ANISOU 874 CG2 THR A 110 5418 6654 8892 -964 -194 -313 C ATOM 875 N ASN A 111 -40.831 3.915 -27.789 1.00 58.22 N ANISOU 875 N ASN A 111 5808 6718 9594 -1238 304 -138 N ATOM 876 CA ASN A 111 -40.300 2.628 -27.321 1.00 58.71 C ANISOU 876 CA ASN A 111 5983 6627 9695 -1308 399 -85 C ATOM 877 C ASN A 111 -41.325 1.519 -27.572 1.00 61.63 C ANISOU 877 C ASN A 111 6144 6887 10382 -1454 513 -162 C ATOM 878 O ASN A 111 -42.510 1.670 -27.266 1.00 63.50 O ANISOU 878 O ASN A 111 6205 7111 10809 -1495 658 -175 O ATOM 879 CB ASN A 111 -39.944 2.659 -25.833 1.00 58.87 C ANISOU 879 CB ASN A 111 6238 6565 9563 -1229 590 78 C ATOM 880 CG ASN A 111 -39.243 1.402 -25.359 1.00 59.32 C ANISOU 880 CG ASN A 111 6462 6473 9601 -1238 680 154 C ATOM 881 OD1 ASN A 111 -38.281 0.940 -25.978 1.00 57.43 O ANISOU 881 OD1 ASN A 111 6273 6236 9311 -1246 523 110 O ATOM 882 ND2 ASN A 111 -39.700 0.858 -24.243 1.00 61.24 N ANISOU 882 ND2 ASN A 111 6816 6579 9874 -1211 958 284 N ATOM 883 N LEU A 112 -40.836 0.393 -28.102 1.00 62.38 N ANISOU 883 N LEU A 112 6254 6888 10559 -1534 462 -220 N ATOM 884 CA LEU A 112 -41.664 -0.740 -28.540 1.00 64.30 C ANISOU 884 CA LEU A 112 6285 7005 11140 -1695 536 -349 C ATOM 885 C LEU A 112 -42.751 -0.241 -29.499 1.00 65.77 C ANISOU 885 C LEU A 112 6153 7334 11502 -1726 371 -554 C ATOM 886 O LEU A 112 -43.917 -0.692 -29.456 1.00 68.52 O ANISOU 886 O LEU A 112 6238 7608 12185 -1846 489 -661 O ATOM 887 CB LEU A 112 -42.233 -1.464 -27.313 1.00 66.16 C ANISOU 887 CB LEU A 112 6559 7024 11555 -1761 909 -216 C ATOM 888 CG LEU A 112 -41.292 -2.464 -26.632 1.00 65.83 C ANISOU 888 CG LEU A 112 6801 6797 11412 -1734 1071 -64 C ATOM 889 CD1 LEU A 112 -40.146 -2.872 -27.550 1.00 63.88 C ANISOU 889 CD1 LEU A 112 6644 6591 11034 -1722 816 -139 C ATOM 890 CD2 LEU A 112 -40.743 -1.927 -25.318 1.00 64.84 C ANISOU 890 CD2 LEU A 112 6973 6679 10984 -1553 1209 160 C ATOM 891 N GLY A 113 -42.320 0.675 -30.377 1.00 64.35 N ANISOU 891 N GLY A 113 5999 7350 11101 -1599 104 -611 N ATOM 892 CA GLY A 113 -43.094 1.253 -31.467 1.00 65.90 C ANISOU 892 CA GLY A 113 5963 7724 11350 -1539 -118 -799 C ATOM 893 C GLY A 113 -44.332 2.016 -31.019 1.00 66.88 C ANISOU 893 C GLY A 113 5879 7924 11606 -1516 -23 -802 C ATOM 894 O GLY A 113 -45.308 2.030 -31.777 1.00 67.72 O ANISOU 894 O GLY A 113 5699 8132 11898 -1514 -166 -1004 O ATOM 895 N GLU A 114 -44.283 2.633 -29.821 1.00 66.71 N ANISOU 895 N GLU A 114 5999 7861 11485 -1479 200 -598 N ATOM 896 CA GLU A 114 -45.359 3.519 -29.291 1.00 69.63 C ANISOU 896 CA GLU A 114 6221 8301 11935 -1424 323 -562 C ATOM 897 C GLU A 114 -44.794 4.463 -28.216 1.00 68.22 C ANISOU 897 C GLU A 114 6322 8114 11482 -1314 472 -343 C ATOM 898 O GLU A 114 -43.679 4.287 -27.744 1.00 68.03 O ANISOU 898 O GLU A 114 6568 8018 11260 -1300 498 -234 O ATOM 899 CB GLU A 114 -46.553 2.717 -28.750 1.00 72.86 C ANISOU 899 CB GLU A 114 6366 8570 12745 -1579 560 -613 C ATOM 900 CG GLU A 114 -46.432 2.255 -27.299 1.00 74.16 C ANISOU 900 CG GLU A 114 6722 8518 12935 -1633 938 -397 C ATOM 901 CD GLU A 114 -47.554 1.346 -26.781 1.00 78.55 C ANISOU 901 CD GLU A 114 7034 8876 13935 -1795 1251 -428 C ATOM 902 OE1 GLU A 114 -47.348 0.694 -25.733 1.00 78.85 O ANISOU 902 OE1 GLU A 114 7268 8696 13995 -1829 1579 -250 O ATOM 903 OE2 GLU A 114 -48.643 1.290 -27.407 1.00 79.98 O ANISOU 903 OE2 GLU A 114 6826 9112 14450 -1872 1182 -634 O ATOM 904 N LYS A 115 -45.600 5.463 -27.842 1.00 69.18 N ANISOU 904 N LYS A 115 6362 8316 11606 -1226 558 -303 N ATOM 905 CA LYS A 115 -45.274 6.493 -26.845 1.00 69.24 C ANISOU 905 CA LYS A 115 6606 8324 11376 -1109 695 -136 C ATOM 906 C LYS A 115 -44.852 5.877 -25.505 1.00 70.17 C ANISOU 906 C LYS A 115 6954 8266 11439 -1146 944 18 C ATOM 907 O LYS A 115 -44.946 4.644 -25.311 1.00 74.45 O ANISOU 907 O LYS A 115 7460 8665 12161 -1264 1066 22 O ATOM 908 CB LYS A 115 -46.483 7.402 -26.606 1.00 71.82 C ANISOU 908 CB LYS A 115 6761 8730 11795 -1028 804 -126 C ATOM 909 CG LYS A 115 -46.466 8.686 -27.413 1.00 73.18 C ANISOU 909 CG LYS A 115 6924 9078 11800 -865 614 -170 C ATOM 910 CD LYS A 115 -47.603 9.653 -27.100 1.00 76.50 C ANISOU 910 CD LYS A 115 7206 9574 12284 -753 737 -140 C ATOM 911 CE LYS A 115 -47.171 11.112 -27.041 1.00 76.68 C ANISOU 911 CE LYS A 115 7440 9663 12031 -577 721 -62 C ATOM 912 NZ LYS A 115 -45.994 11.424 -27.896 1.00 74.07 N ANISOU 912 NZ LYS A 115 7283 9368 11491 -524 515 -92 N ATOM 913 N LEU A 116 -44.382 6.756 -24.600 1.00 67.53 N ANISOU 913 N LEU A 116 6871 7938 10849 -1023 1020 135 N ATOM 914 CA LEU A 116 -44.131 6.450 -23.186 1.00 67.32 C ANISOU 914 CA LEU A 116 7099 7779 10700 -972 1259 285 C ATOM 915 C LEU A 116 -45.293 6.999 -22.365 1.00 69.10 C ANISOU 915 C LEU A 116 7276 7977 11001 -909 1530 369 C ATOM 916 O LEU A 116 -46.051 7.831 -22.851 1.00 69.22 O ANISOU 916 O LEU A 116 7096 8101 11103 -884 1486 311 O ATOM 917 CB LEU A 116 -42.826 7.093 -22.708 1.00 65.46 C ANISOU 917 CB LEU A 116 7168 7579 10125 -854 1130 314 C ATOM 918 CG LEU A 116 -41.561 6.803 -23.519 1.00 63.90 C ANISOU 918 CG LEU A 116 7017 7418 9843 -891 864 232 C ATOM 919 CD1 LEU A 116 -40.326 7.212 -22.731 1.00 63.53 C ANISOU 919 CD1 LEU A 116 7249 7370 9518 -779 788 252 C ATOM 920 CD2 LEU A 116 -41.456 5.340 -23.916 1.00 64.15 C ANISOU 920 CD2 LEU A 116 6980 7356 10034 -1008 874 222 C ATOM 921 N THR A 117 -45.398 6.537 -21.116 1.00 71.47 N ANISOU 921 N THR A 117 7778 8131 11246 -851 1820 516 N ATOM 922 CA THR A 117 -46.430 6.987 -20.201 1.00 75.09 C ANISOU 922 CA THR A 117 8242 8533 11755 -766 2134 624 C ATOM 923 C THR A 117 -45.913 8.170 -19.382 1.00 75.59 C ANISOU 923 C THR A 117 8610 8660 11450 -572 2107 675 C ATOM 924 O THR A 117 -44.711 8.395 -19.297 1.00 75.01 O ANISOU 924 O THR A 117 8761 8633 11106 -511 1892 637 O ATOM 925 CB THR A 117 -46.875 5.872 -19.254 1.00 77.66 C ANISOU 925 CB THR A 117 8659 8637 12211 -772 2525 774 C ATOM 926 OG1 THR A 117 -45.804 5.649 -18.337 1.00 77.78 O ANISOU 926 OG1 THR A 117 9092 8596 11865 -617 2540 881 O ATOM 927 CG2 THR A 117 -47.240 4.599 -19.985 1.00 78.72 C ANISOU 927 CG2 THR A 117 8520 8662 12727 -981 2568 703 C ATOM 928 N ASP A 118 -46.852 8.896 -18.766 1.00 77.94 N ANISOU 928 N ASP A 118 8898 8948 11766 -477 2336 745 N ATOM 929 CA ASP A 118 -46.546 10.020 -17.906 1.00 78.21 C ANISOU 929 CA ASP A 118 9219 9017 11478 -287 2355 781 C ATOM 930 C ASP A 118 -45.652 9.546 -16.755 1.00 79.55 C ANISOU 930 C ASP A 118 9793 9096 11333 -143 2420 865 C ATOM 931 O ASP A 118 -44.771 10.274 -16.322 1.00 78.75 O ANISOU 931 O ASP A 118 9941 9056 10922 -17 2245 804 O ATOM 932 CB ASP A 118 -47.825 10.695 -17.397 1.00 80.40 C ANISOU 932 CB ASP A 118 9416 9271 11859 -203 2650 863 C ATOM 933 CG ASP A 118 -48.467 11.668 -18.379 1.00 79.34 C ANISOU 933 CG ASP A 118 8982 9278 11883 -239 2512 762 C ATOM 934 OD1 ASP A 118 -48.000 11.742 -19.536 1.00 76.13 O ANISOU 934 OD1 ASP A 118 8419 8981 11524 -332 2203 635 O ATOM 935 OD2 ASP A 118 -49.436 12.346 -17.978 1.00 81.60 O ANISOU 935 OD2 ASP A 118 9208 9561 12232 -147 2729 822 O ATOM 936 N GLU A 119 -45.882 8.320 -16.275 1.00 82.91 N ANISOU 936 N GLU A 119 10279 9371 11852 -150 2672 992 N ATOM 937 CA GLU A 119 -45.128 7.765 -15.151 1.00 86.06 C ANISOU 937 CA GLU A 119 11087 9679 11932 43 2768 1098 C ATOM 938 C GLU A 119 -43.688 7.474 -15.587 1.00 82.85 C ANISOU 938 C GLU A 119 10769 9356 11352 20 2387 982 C ATOM 939 O GLU A 119 -42.754 7.691 -14.821 1.00 81.94 O ANISOU 939 O GLU A 119 10972 9277 10883 215 2260 962 O ATOM 940 CB GLU A 119 -45.795 6.497 -14.612 1.00 91.63 C ANISOU 940 CB GLU A 119 11831 10166 12816 49 3193 1287 C ATOM 941 CG GLU A 119 -47.123 6.752 -13.912 1.00 96.99 C ANISOU 941 CG GLU A 119 12485 10726 13638 122 3642 1430 C ATOM 942 CD GLU A 119 -48.356 6.702 -14.806 1.00 99.66 C ANISOU 942 CD GLU A 119 12324 11048 14493 -120 3757 1376 C ATOM 943 OE1 GLU A 119 -49.347 6.050 -14.408 1.00103.05 O ANISOU 943 OE1 GLU A 119 12652 11282 15219 -150 4198 1506 O ATOM 944 OE2 GLU A 119 -48.323 7.311 -15.903 1.00 99.49 O ANISOU 944 OE2 GLU A 119 12012 11203 14586 -263 3413 1196 O ATOM 945 N GLU A 120 -43.530 6.979 -16.819 1.00 81.40 N ANISOU 945 N GLU A 120 10294 9206 11427 -202 2203 889 N ATOM 946 CA GLU A 120 -42.219 6.653 -17.384 1.00 80.28 C ANISOU 946 CA GLU A 120 10189 9132 11179 -243 1868 783 C ATOM 947 C GLU A 120 -41.395 7.939 -17.578 1.00 77.14 C ANISOU 947 C GLU A 120 9837 8888 10585 -194 1553 628 C ATOM 948 O GLU A 120 -40.243 8.003 -17.159 1.00 76.50 O ANISOU 948 O GLU A 120 9961 8846 10259 -82 1360 565 O ATOM 949 CB GLU A 120 -42.377 5.847 -18.677 1.00 80.39 C ANISOU 949 CB GLU A 120 9890 9132 11520 -479 1782 721 C ATOM 950 CG GLU A 120 -42.782 4.405 -18.430 1.00 84.12 C ANISOU 950 CG GLU A 120 10368 9417 12175 -530 2060 841 C ATOM 951 CD GLU A 120 -43.096 3.583 -19.671 1.00 85.71 C ANISOU 951 CD GLU A 120 10244 9584 12735 -770 1994 746 C ATOM 952 OE1 GLU A 120 -43.989 3.989 -20.440 1.00 84.98 O ANISOU 952 OE1 GLU A 120 9837 9555 12897 -898 1963 649 O ATOM 953 OE2 GLU A 120 -42.451 2.523 -19.860 1.00 88.65 O ANISOU 953 OE2 GLU A 120 10684 9870 13126 -810 1967 759 O ATOM 954 N VAL A 121 -41.984 8.976 -18.180 1.00 74.98 N ANISOU 954 N VAL A 121 9368 8690 10430 -263 1513 558 N ATOM 955 CA VAL A 121 -41.242 10.212 -18.412 1.00 73.09 C ANISOU 955 CA VAL A 121 9165 8549 10053 -230 1272 416 C ATOM 956 C VAL A 121 -40.899 10.848 -17.056 1.00 74.60 C ANISOU 956 C VAL A 121 9677 8730 9937 -18 1310 407 C ATOM 957 O VAL A 121 -39.800 11.376 -16.879 1.00 74.13 O ANISOU 957 O VAL A 121 9735 8717 9712 37 1077 264 O ATOM 958 CB VAL A 121 -41.991 11.187 -19.341 1.00 72.02 C ANISOU 958 CB VAL A 121 8787 8481 10096 -309 1260 367 C ATOM 959 CG1 VAL A 121 -42.365 10.540 -20.665 1.00 70.52 C ANISOU 959 CG1 VAL A 121 8299 8321 10173 -471 1190 348 C ATOM 960 CG2 VAL A 121 -43.218 11.788 -18.684 1.00 75.03 C ANISOU 960 CG2 VAL A 121 9176 8839 10492 -220 1524 454 C ATOM 961 N ASP A 122 -41.830 10.767 -16.096 1.00 77.16 N ANISOU 961 N ASP A 122 10136 8985 10195 106 1609 544 N ATOM 962 CA ASP A 122 -41.644 11.357 -14.762 1.00 79.54 C ANISOU 962 CA ASP A 122 10778 9274 10169 349 1670 539 C ATOM 963 C ASP A 122 -40.356 10.815 -14.132 1.00 80.09 C ANISOU 963 C ASP A 122 11103 9363 9964 493 1465 473 C ATOM 964 O ASP A 122 -39.554 11.589 -13.605 1.00 79.96 O ANISOU 964 O ASP A 122 11255 9408 9719 620 1254 307 O ATOM 965 CB ASP A 122 -42.845 11.106 -13.843 1.00 82.17 C ANISOU 965 CB ASP A 122 11239 9502 10476 484 2080 738 C ATOM 966 CG ASP A 122 -43.940 12.158 -13.932 1.00 82.91 C ANISOU 966 CG ASP A 122 11206 9603 10691 470 2252 754 C ATOM 967 OD1 ASP A 122 -43.950 12.920 -14.927 1.00 81.71 O ANISOU 967 OD1 ASP A 122 10810 9533 10703 326 2077 640 O ATOM 968 OD2 ASP A 122 -44.779 12.205 -13.005 1.00 84.92 O ANISOU 968 OD2 ASP A 122 11620 9775 10870 626 2581 894 O ATOM 969 N GLU A 123 -40.170 9.492 -14.208 1.00 80.63 N ANISOU 969 N GLU A 123 11183 9376 10076 476 1523 585 N ATOM 970 CA GLU A 123 -39.031 8.819 -13.595 1.00 82.01 C ANISOU 970 CA GLU A 123 11604 9567 9986 652 1357 555 C ATOM 971 C GLU A 123 -37.743 9.144 -14.361 1.00 78.43 C ANISOU 971 C GLU A 123 11001 9223 9572 539 945 331 C ATOM 972 O GLU A 123 -36.681 9.278 -13.755 1.00 79.70 O ANISOU 972 O GLU A 123 11340 9452 9490 710 705 193 O ATOM 973 CB GLU A 123 -39.261 7.308 -13.543 1.00 84.76 C ANISOU 973 CB GLU A 123 12001 9797 10406 660 1582 756 C ATOM 974 CG GLU A 123 -38.185 6.557 -12.773 1.00 88.26 C ANISOU 974 CG GLU A 123 12751 10251 10530 914 1459 766 C ATOM 975 CD GLU A 123 -38.070 6.900 -11.294 1.00 93.37 C ANISOU 975 CD GLU A 123 13818 10914 10740 1294 1516 787 C ATOM 976 OE1 GLU A 123 -37.070 6.470 -10.661 1.00 95.45 O ANISOU 976 OE1 GLU A 123 14335 11234 10695 1550 1328 742 O ATOM 977 OE2 GLU A 123 -38.983 7.589 -10.772 1.00 95.98 O ANISOU 977 OE2 GLU A 123 14233 11207 11025 1361 1744 844 O ATOM 978 N MET A 124 -37.837 9.265 -15.687 1.00 73.93 N ANISOU 978 N MET A 124 10106 8669 9314 273 870 286 N ATOM 979 CA MET A 124 -36.684 9.620 -16.493 1.00 70.89 C ANISOU 979 CA MET A 124 9570 8357 9006 163 548 97 C ATOM 980 C MET A 124 -36.094 10.941 -15.993 1.00 71.81 C ANISOU 980 C MET A 124 9771 8530 8983 251 369 -109 C ATOM 981 O MET A 124 -34.889 11.039 -15.809 1.00 72.65 O ANISOU 981 O MET A 124 9913 8685 9003 309 107 -284 O ATOM 982 CB MET A 124 -37.060 9.740 -17.968 1.00 67.75 C ANISOU 982 CB MET A 124 8854 7960 8926 -87 544 96 C ATOM 983 CG MET A 124 -37.308 8.396 -18.604 1.00 67.05 C ANISOU 983 CG MET A 124 8656 7822 8998 -195 624 217 C ATOM 984 SD MET A 124 -37.536 8.472 -20.392 1.00 65.97 S ANISOU 984 SD MET A 124 8177 7712 9173 -435 540 167 S ATOM 985 CE MET A 124 -35.864 8.833 -20.930 1.00 64.24 C ANISOU 985 CE MET A 124 7943 7542 8920 -452 234 -1 C ATOM 986 N ILE A 125 -36.959 11.934 -15.755 1.00 73.26 N ANISOU 986 N ILE A 125 9972 8696 9165 265 519 -103 N ATOM 987 CA ILE A 125 -36.549 13.215 -15.170 1.00 74.90 C ANISOU 987 CA ILE A 125 10287 8925 9244 357 397 -305 C ATOM 988 C ILE A 125 -35.962 12.974 -13.769 1.00 78.65 C ANISOU 988 C ILE A 125 11083 9435 9365 635 290 -383 C ATOM 989 O ILE A 125 -34.817 13.328 -13.519 1.00 79.10 O ANISOU 989 O ILE A 125 11163 9543 9346 691 -1 -624 O ATOM 990 CB ILE A 125 -37.714 14.231 -15.151 1.00 74.72 C ANISOU 990 CB ILE A 125 10248 8864 9276 343 625 -249 C ATOM 991 CG1 ILE A 125 -37.793 15.035 -16.454 1.00 71.97 C ANISOU 991 CG1 ILE A 125 9627 8506 9212 137 599 -303 C ATOM 992 CG2 ILE A 125 -37.622 15.154 -13.942 1.00 77.38 C ANISOU 992 CG2 ILE A 125 10849 9197 9354 547 606 -385 C ATOM 993 CD1 ILE A 125 -38.964 14.680 -17.332 1.00 70.70 C ANISOU 993 CD1 ILE A 125 9265 8343 9254 26 799 -111 C ATOM 994 N ARG A 126 -36.758 12.361 -12.882 1.00 82.56 N ANISOU 994 N ARG A 126 11816 9896 9657 825 536 -183 N ATOM 995 CA ARG A 126 -36.418 12.113 -11.458 1.00 86.99 C ANISOU 995 CA ARG A 126 12757 10484 9809 1169 497 -208 C ATOM 996 C ARG A 126 -35.031 11.454 -11.326 1.00 89.56 C ANISOU 996 C ARG A 126 13125 10893 10010 1271 162 -352 C ATOM 997 O ARG A 126 -34.290 11.756 -10.389 1.00 93.21 O ANISOU 997 O ARG A 126 13805 11433 10177 1524 -69 -548 O ATOM 998 CB ARG A 126 -37.504 11.242 -10.808 1.00 88.81 C ANISOU 998 CB ARG A 126 13202 10623 9917 1326 898 103 C ATOM 999 CG ARG A 126 -37.663 11.406 -9.301 1.00 92.59 C ANISOU 999 CG ARG A 126 14122 11099 9959 1716 999 124 C ATOM 1000 CD ARG A 126 -36.825 10.464 -8.445 1.00 94.87 C ANISOU 1000 CD ARG A 126 14726 11430 9889 2041 874 138 C ATOM 1001 NE ARG A 126 -37.228 9.062 -8.528 1.00 95.64 N ANISOU 1001 NE ARG A 126 14877 11419 10043 2061 1174 442 N ATOM 1002 CZ ARG A 126 -37.510 8.275 -7.489 1.00 99.01 C ANISOU 1002 CZ ARG A 126 15697 11767 10155 2406 1445 658 C ATOM 1003 NH1 ARG A 126 -37.718 6.980 -7.675 1.00 98.10 N ANISOU 1003 NH1 ARG A 126 15599 11528 10144 2393 1702 908 N ATOM 1004 NH2 ARG A 126 -37.570 8.779 -6.269 1.00101.99 N ANISOU 1004 NH2 ARG A 126 16468 12173 10107 2780 1473 623 N ATOM 1005 N GLU A 127 -34.682 10.553 -12.254 1.00 88.08 N ANISOU 1005 N GLU A 127 12727 10695 10042 1093 125 -270 N ATOM 1006 CA GLU A 127 -33.388 9.870 -12.240 1.00 88.83 C ANISOU 1006 CA GLU A 127 12826 10866 10059 1180 -170 -385 C ATOM 1007 C GLU A 127 -32.264 10.852 -12.597 1.00 88.28 C ANISOU 1007 C GLU A 127 12554 10873 10114 1077 -538 -731 C ATOM 1008 O GLU A 127 -31.144 10.710 -12.106 1.00 90.30 O ANISOU 1008 O GLU A 127 12868 11221 10219 1248 -845 -931 O ATOM 1009 CB GLU A 127 -33.395 8.692 -13.217 1.00 88.45 C ANISOU 1009 CB GLU A 127 12600 10763 10244 998 -75 -202 C ATOM 1010 CG GLU A 127 -32.082 7.925 -13.259 1.00 89.89 C ANISOU 1010 CG GLU A 127 12778 11015 10361 1093 -354 -296 C ATOM 1011 CD GLU A 127 -32.072 6.671 -14.120 1.00 89.91 C ANISOU 1011 CD GLU A 127 12659 10947 10556 951 -242 -111 C ATOM 1012 OE1 GLU A 127 -30.977 6.076 -14.260 1.00 90.87 O ANISOU 1012 OE1 GLU A 127 12750 11121 10652 1016 -465 -187 O ATOM 1013 OE2 GLU A 127 -33.147 6.290 -14.655 1.00 89.48 O ANISOU 1013 OE2 GLU A 127 12524 10784 10689 779 57 87 O ATOM 1014 N ALA A 128 -32.565 11.827 -13.465 1.00 85.85 N ANISOU 1014 N ALA A 128 12000 10518 10100 810 -492 -803 N ATOM 1015 CA ALA A 128 -31.555 12.708 -14.078 1.00 85.07 C ANISOU 1015 CA ALA A 128 11655 10433 10235 646 -748 -1093 C ATOM 1016 C ALA A 128 -31.481 14.077 -13.383 1.00 86.93 C ANISOU 1016 C ALA A 128 11967 10663 10396 715 -839 -1353 C ATOM 1017 O ALA A 128 -30.452 14.746 -13.461 1.00 89.03 O ANISOU 1017 O ALA A 128 12090 10938 10798 660 -1093 -1660 O ATOM 1018 CB ALA A 128 -31.860 12.871 -15.547 1.00 81.74 C ANISOU 1018 CB ALA A 128 10941 9938 10177 339 -612 -994 C ATOM 1019 N ASP A 129 -32.569 14.489 -12.723 1.00 86.81 N ANISOU 1019 N ASP A 129 12166 10618 10199 829 -617 -1239 N ATOM 1020 CA ASP A 129 -32.720 15.828 -12.173 1.00 87.19 C ANISOU 1020 CA ASP A 129 12296 10632 10198 874 -636 -1452 C ATOM 1021 C ASP A 129 -31.944 15.936 -10.851 1.00 91.09 C ANISOU 1021 C ASP A 129 13037 11217 10354 1178 -927 -1725 C ATOM 1022 O ASP A 129 -32.538 15.869 -9.774 1.00 93.41 O ANISOU 1022 O ASP A 129 13665 11536 10291 1455 -829 -1652 O ATOM 1023 CB ASP A 129 -34.208 16.147 -12.008 1.00 87.02 C ANISOU 1023 CB ASP A 129 12404 10545 10112 897 -269 -1207 C ATOM 1024 CG ASP A 129 -34.507 17.563 -11.549 1.00 88.89 C ANISOU 1024 CG ASP A 129 12730 10725 10320 930 -232 -1390 C ATOM 1025 OD1 ASP A 129 -33.658 18.445 -11.785 1.00 89.84 O ANISOU 1025 OD1 ASP A 129 12710 10812 10612 820 -436 -1694 O ATOM 1026 OD2 ASP A 129 -35.595 17.773 -10.964 1.00 88.74 O ANISOU 1026 OD2 ASP A 129 12912 10675 10129 1063 27 -1228 O ATOM 1027 N ILE A 130 -30.621 16.132 -10.956 1.00 91.99 N ANISOU 1027 N ILE A 130 12978 11379 10595 1138 -1283 -2054 N ATOM 1028 CA ILE A 130 -29.688 16.259 -9.808 1.00 95.50 C ANISOU 1028 CA ILE A 130 13584 11937 10765 1426 -1657 -2401 C ATOM 1029 C ILE A 130 -30.063 17.464 -8.928 1.00 97.82 C ANISOU 1029 C ILE A 130 14078 12196 10894 1552 -1664 -2627 C ATOM 1030 O ILE A 130 -30.079 17.343 -7.698 1.00102.08 O ANISOU 1030 O ILE A 130 14958 12828 10998 1915 -1790 -2717 O ATOM 1031 CB ILE A 130 -28.221 16.354 -10.290 1.00 96.17 C ANISOU 1031 CB ILE A 130 13335 12057 11146 1290 -2019 -2741 C ATOM 1032 CG1 ILE A 130 -27.704 15.001 -10.791 1.00 94.63 C ANISOU 1032 CG1 ILE A 130 13041 11936 10975 1297 -2079 -2552 C ATOM 1033 CG2 ILE A 130 -27.320 16.937 -9.202 1.00100.82 C ANISOU 1033 CG2 ILE A 130 14003 12742 11560 1526 -2430 -3216 C ATOM 1034 CD1 ILE A 130 -26.278 15.020 -11.300 1.00 94.96 C ANISOU 1034 CD1 ILE A 130 12737 12010 11331 1172 -2401 -2858 C ATOM 1035 N ASP A 131 -30.316 18.623 -9.553 1.00 95.80 N ANISOU 1035 N ASP A 131 13631 11798 10968 1280 -1531 -2726 N ATOM 1036 CA ASP A 131 -30.547 19.888 -8.831 1.00 97.25 C ANISOU 1036 CA ASP A 131 13964 11917 11069 1357 -1546 -2992 C ATOM 1037 C ASP A 131 -31.961 19.888 -8.230 1.00 95.11 C ANISOU 1037 C ASP A 131 14037 11623 10474 1544 -1197 -2679 C ATOM 1038 O ASP A 131 -32.166 20.389 -7.137 1.00 98.24 O ANISOU 1038 O ASP A 131 14735 12038 10551 1804 -1249 -2837 O ATOM 1039 CB ASP A 131 -30.247 21.104 -9.719 1.00 97.61 C ANISOU 1039 CB ASP A 131 13693 11789 11603 1014 -1495 -3204 C ATOM 1040 CG ASP A 131 -31.355 21.512 -10.679 1.00 95.70 C ANISOU 1040 CG ASP A 131 13372 11410 11578 796 -1064 -2868 C ATOM 1041 OD1 ASP A 131 -31.763 22.698 -10.637 1.00 97.49 O ANISOU 1041 OD1 ASP A 131 13630 11500 11909 733 -915 -2978 O ATOM 1042 OD2 ASP A 131 -31.782 20.655 -11.481 1.00 93.72 O ANISOU 1042 OD2 ASP A 131 13023 11186 11399 699 -892 -2519 O ATOM 1043 N GLY A 132 -32.925 19.312 -8.950 1.00 90.23 N ANISOU 1043 N GLY A 132 13363 10964 9954 1418 -846 -2251 N ATOM 1044 CA GLY A 132 -34.242 19.018 -8.406 1.00 89.24 C ANISOU 1044 CA GLY A 132 13521 10824 9561 1599 -495 -1916 C ATOM 1045 C GLY A 132 -35.283 20.042 -8.815 1.00 87.08 C ANISOU 1045 C GLY A 132 13191 10423 9471 1448 -178 -1814 C ATOM 1046 O GLY A 132 -36.227 20.292 -8.069 1.00 89.34 O ANISOU 1046 O GLY A 132 13745 10681 9520 1641 59 -1685 O ATOM 1047 N ASP A 133 -35.134 20.604 -10.018 1.00 83.35 N ANISOU 1047 N ASP A 133 12383 9870 9416 1128 -148 -1848 N ATOM 1048 CA ASP A 133 -36.047 21.631 -10.515 1.00 81.87 C ANISOU 1048 CA ASP A 133 12127 9561 9417 1001 139 -1758 C ATOM 1049 C ASP A 133 -37.138 20.984 -11.379 1.00 78.29 C ANISOU 1049 C ASP A 133 11529 9112 9105 891 445 -1352 C ATOM 1050 O ASP A 133 -37.939 21.690 -11.996 1.00 77.30 O ANISOU 1050 O ASP A 133 11296 8911 9162 788 678 -1237 O ATOM 1051 CB ASP A 133 -35.295 22.747 -11.256 1.00 82.06 C ANISOU 1051 CB ASP A 133 11917 9468 9793 770 33 -2037 C ATOM 1052 CG ASP A 133 -34.377 22.293 -12.382 1.00 80.34 C ANISOU 1052 CG ASP A 133 11378 9254 9894 534 -113 -2068 C ATOM 1053 OD1 ASP A 133 -34.438 21.104 -12.764 1.00 78.84 O ANISOU 1053 OD1 ASP A 133 11119 9160 9674 521 -120 -1842 O ATOM 1054 OD2 ASP A 133 -33.597 23.133 -12.868 1.00 80.79 O ANISOU 1054 OD2 ASP A 133 11259 9197 10240 368 -197 -2321 O ATOM 1055 N GLY A 134 -37.170 19.645 -11.412 1.00 76.42 N ANISOU 1055 N GLY A 134 11287 8959 8788 927 439 -1152 N ATOM 1056 CA GLY A 134 -38.144 18.890 -12.198 1.00 73.54 C ANISOU 1056 CA GLY A 134 10761 8599 8582 816 693 -815 C ATOM 1057 C GLY A 134 -37.972 19.109 -13.693 1.00 70.30 C ANISOU 1057 C GLY A 134 10006 8164 8538 541 667 -805 C ATOM 1058 O GLY A 134 -38.929 18.955 -14.459 1.00 66.96 O ANISOU 1058 O GLY A 134 9424 7736 8280 450 875 -588 O ATOM 1059 N GLN A 135 -36.743 19.465 -14.092 1.00 70.14 N ANISOU 1059 N GLN A 135 9874 8129 8647 431 412 -1052 N ATOM 1060 CA GLN A 135 -36.354 19.659 -15.487 1.00 68.13 C ANISOU 1060 CA GLN A 135 9333 7834 8718 204 385 -1057 C ATOM 1061 C GLN A 135 -34.911 19.171 -15.671 1.00 67.57 C ANISOU 1061 C GLN A 135 9162 7788 8720 133 92 -1249 C ATOM 1062 O GLN A 135 -34.187 18.993 -14.697 1.00 70.38 O ANISOU 1062 O GLN A 135 9658 8188 8892 262 -117 -1438 O ATOM 1063 CB GLN A 135 -36.504 21.131 -15.874 1.00 68.90 C ANISOU 1063 CB GLN A 135 9386 7811 8982 139 501 -1166 C ATOM 1064 CG GLN A 135 -37.953 21.595 -15.986 1.00 69.30 C ANISOU 1064 CG GLN A 135 9470 7845 9014 199 800 -947 C ATOM 1065 CD GLN A 135 -38.089 22.878 -16.772 1.00 68.86 C ANISOU 1065 CD GLN A 135 9325 7668 9169 125 938 -990 C ATOM 1066 OE1 GLN A 135 -38.710 22.911 -17.834 1.00 67.82 O ANISOU 1066 OE1 GLN A 135 9040 7545 9181 76 1077 -807 O ATOM 1067 NE2 GLN A 135 -37.481 23.943 -16.269 1.00 69.39 N ANISOU 1067 NE2 GLN A 135 9493 7615 9256 133 900 -1246 N ATOM 1068 N VAL A 136 -34.507 18.960 -16.928 1.00 64.41 N ANISOU 1068 N VAL A 136 8525 7364 8581 -46 78 -1205 N ATOM 1069 CA VAL A 136 -33.180 18.448 -17.267 1.00 63.56 C ANISOU 1069 CA VAL A 136 8285 7271 8592 -126 -159 -1355 C ATOM 1070 C VAL A 136 -32.472 19.470 -18.168 1.00 62.66 C ANISOU 1070 C VAL A 136 7982 7022 8801 -291 -141 -1518 C ATOM 1071 O VAL A 136 -32.950 19.792 -19.250 1.00 59.84 O ANISOU 1071 O VAL A 136 7521 6603 8611 -384 50 -1366 O ATOM 1072 CB VAL A 136 -33.281 17.058 -17.935 1.00 62.34 C ANISOU 1072 CB VAL A 136 8042 7193 8448 -169 -161 -1132 C ATOM 1073 CG1 VAL A 136 -31.941 16.344 -18.012 1.00 61.41 C ANISOU 1073 CG1 VAL A 136 7838 7113 8383 -193 -412 -1270 C ATOM 1074 CG2 VAL A 136 -34.305 16.168 -17.237 1.00 63.30 C ANISOU 1074 CG2 VAL A 136 8334 7389 8327 -34 -44 -912 C ATOM 1075 N ASN A 137 -31.331 19.982 -17.696 1.00 65.48 N ANISOU 1075 N ASN A 137 8299 7326 9252 -309 -335 -1840 N ATOM 1076 CA ASN A 137 -30.458 20.868 -18.482 1.00 66.79 C ANISOU 1076 CA ASN A 137 8264 7326 9785 -479 -302 -2027 C ATOM 1077 C ASN A 137 -29.348 20.023 -19.125 1.00 66.15 C ANISOU 1077 C ASN A 137 7983 7271 9876 -569 -457 -2064 C ATOM 1078 O ASN A 137 -29.357 18.805 -19.022 1.00 62.41 O ANISOU 1078 O ASN A 137 7541 6942 9229 -501 -576 -1929 O ATOM 1079 CB ASN A 137 -29.916 22.016 -17.627 1.00 70.02 C ANISOU 1079 CB ASN A 137 8705 7627 10272 -472 -391 -2392 C ATOM 1080 CG ASN A 137 -28.977 21.565 -16.528 1.00 72.75 C ANISOU 1080 CG ASN A 137 9070 8085 10484 -365 -758 -2689 C ATOM 1081 OD1 ASN A 137 -28.419 20.468 -16.583 1.00 72.62 O ANISOU 1081 OD1 ASN A 137 8988 8194 10409 -332 -943 -2649 O ATOM 1082 ND2 ASN A 137 -28.791 22.414 -15.531 1.00 75.37 N ANISOU 1082 ND2 ASN A 137 9499 8375 10760 -291 -875 -3003 N ATOM 1083 N TYR A 138 -28.389 20.673 -19.787 1.00 69.03 N ANISOU 1083 N TYR A 138 8147 7477 10604 -718 -425 -2245 N ATOM 1084 CA TYR A 138 -27.408 19.930 -20.561 1.00 70.58 C ANISOU 1084 CA TYR A 138 8144 7676 10998 -805 -507 -2243 C ATOM 1085 C TYR A 138 -26.600 18.994 -19.653 1.00 72.92 C ANISOU 1085 C TYR A 138 8422 8133 11148 -706 -862 -2414 C ATOM 1086 O TYR A 138 -26.531 17.787 -19.882 1.00 70.97 O ANISOU 1086 O TYR A 138 8180 8009 10775 -658 -943 -2241 O ATOM 1087 CB TYR A 138 -26.461 20.838 -21.349 1.00 71.99 C ANISOU 1087 CB TYR A 138 8101 7622 11627 -974 -369 -2422 C ATOM 1088 CG TYR A 138 -25.542 20.033 -22.227 1.00 72.38 C ANISOU 1088 CG TYR A 138 7958 7668 11872 -1047 -403 -2374 C ATOM 1089 CD1 TYR A 138 -26.059 19.057 -23.062 1.00 69.94 C ANISOU 1089 CD1 TYR A 138 7705 7454 11414 -1012 -324 -2046 C ATOM 1090 CD2 TYR A 138 -24.163 20.171 -22.174 1.00 76.19 C ANISOU 1090 CD2 TYR A 138 8196 8062 12687 -1139 -533 -2674 C ATOM 1091 CE1 TYR A 138 -25.245 18.266 -23.852 1.00 69.55 C ANISOU 1091 CE1 TYR A 138 7509 7403 11513 -1059 -352 -1995 C ATOM 1092 CE2 TYR A 138 -23.332 19.391 -22.966 1.00 75.81 C ANISOU 1092 CE2 TYR A 138 7976 8012 12814 -1190 -548 -2615 C ATOM 1093 CZ TYR A 138 -23.875 18.433 -23.810 1.00 72.44 C ANISOU 1093 CZ TYR A 138 7645 7675 12203 -1143 -451 -2264 C ATOM 1094 OH TYR A 138 -23.092 17.634 -24.596 1.00 72.49 O ANISOU 1094 OH TYR A 138 7511 7677 12354 -1176 -455 -2197 O ATOM 1095 N GLU A 139 -26.015 19.562 -18.602 1.00 77.75 N ANISOU 1095 N GLU A 139 9031 8746 11764 -652 -1078 -2765 N ATOM 1096 CA GLU A 139 -25.003 18.873 -17.809 1.00 81.39 C ANISOU 1096 CA GLU A 139 9429 9347 12145 -538 -1449 -3006 C ATOM 1097 C GLU A 139 -25.596 17.571 -17.261 1.00 80.82 C ANISOU 1097 C GLU A 139 9593 9485 11627 -327 -1545 -2750 C ATOM 1098 O GLU A 139 -24.940 16.522 -17.294 1.00 81.95 O ANISOU 1098 O GLU A 139 9675 9736 11725 -260 -1721 -2726 O ATOM 1099 CB GLU A 139 -24.483 19.777 -16.689 1.00 85.82 C ANISOU 1099 CB GLU A 139 9986 9893 12728 -474 -1684 -3447 C ATOM 1100 CG GLU A 139 -23.729 21.003 -17.191 1.00 88.65 C ANISOU 1100 CG GLU A 139 10068 10006 13605 -704 -1587 -3751 C ATOM 1101 CD GLU A 139 -24.562 22.084 -17.871 1.00 88.44 C ANISOU 1101 CD GLU A 139 10102 9759 13742 -846 -1177 -3596 C ATOM 1102 OE1 GLU A 139 -25.799 21.931 -17.961 1.00 87.74 O ANISOU 1102 OE1 GLU A 139 10253 9726 13357 -765 -985 -3258 O ATOM 1103 OE2 GLU A 139 -23.972 23.078 -18.323 1.00 90.86 O ANISOU 1103 OE2 GLU A 139 10206 9827 14489 -1028 -1033 -3813 O ATOM 1104 N GLU A 140 -26.835 17.656 -16.767 1.00 79.68 N ANISOU 1104 N GLU A 140 9715 9377 11180 -219 -1397 -2556 N ATOM 1105 CA GLU A 140 -27.555 16.504 -16.242 1.00 79.50 C ANISOU 1105 CA GLU A 140 9931 9501 10772 -28 -1394 -2287 C ATOM 1106 C GLU A 140 -27.801 15.506 -17.376 1.00 76.86 C ANISOU 1106 C GLU A 140 9503 9166 10532 -140 -1238 -1971 C ATOM 1107 O GLU A 140 -27.663 14.297 -17.186 1.00 78.46 O ANISOU 1107 O GLU A 140 9777 9468 10565 -29 -1323 -1842 O ATOM 1108 CB GLU A 140 -28.881 16.932 -15.608 1.00 79.66 C ANISOU 1108 CB GLU A 140 10214 9518 10535 76 -1196 -2140 C ATOM 1109 CG GLU A 140 -28.724 17.582 -14.245 1.00 83.04 C ANISOU 1109 CG GLU A 140 10834 9987 10730 278 -1377 -2421 C ATOM 1110 CD GLU A 140 -29.938 18.362 -13.767 1.00 84.19 C ANISOU 1110 CD GLU A 140 11196 10078 10713 341 -1142 -2326 C ATOM 1111 OE1 GLU A 140 -30.753 18.774 -14.616 1.00 82.99 O ANISOU 1111 OE1 GLU A 140 10969 9828 10734 179 -853 -2120 O ATOM 1112 OE2 GLU A 140 -30.068 18.566 -12.544 1.00 87.15 O ANISOU 1112 OE2 GLU A 140 11823 10512 10775 577 -1250 -2460 O ATOM 1113 N PHE A 141 -28.178 16.035 -18.544 1.00 75.19 N ANISOU 1113 N PHE A 141 9153 8834 10579 -337 -1004 -1854 N ATOM 1114 CA PHE A 141 -28.468 15.230 -19.722 1.00 72.93 C ANISOU 1114 CA PHE A 141 8780 8540 10387 -438 -859 -1587 C ATOM 1115 C PHE A 141 -27.205 14.468 -20.136 1.00 75.09 C ANISOU 1115 C PHE A 141 8890 8834 10806 -471 -1036 -1672 C ATOM 1116 O PHE A 141 -27.284 13.277 -20.432 1.00 74.19 O ANISOU 1116 O PHE A 141 8803 8784 10601 -440 -1043 -1487 O ATOM 1117 CB PHE A 141 -29.014 16.107 -20.852 1.00 70.65 C ANISOU 1117 CB PHE A 141 8398 8125 10318 -584 -603 -1490 C ATOM 1118 CG PHE A 141 -29.306 15.386 -22.142 1.00 67.75 C ANISOU 1118 CG PHE A 141 7948 7755 10036 -662 -477 -1254 C ATOM 1119 CD1 PHE A 141 -30.403 14.550 -22.254 1.00 66.59 C ANISOU 1119 CD1 PHE A 141 7892 7690 9717 -619 -393 -1013 C ATOM 1120 CD2 PHE A 141 -28.498 15.559 -23.254 1.00 68.00 C ANISOU 1120 CD2 PHE A 141 7812 7689 10335 -770 -429 -1287 C ATOM 1121 CE1 PHE A 141 -30.678 13.890 -23.443 1.00 64.94 C ANISOU 1121 CE1 PHE A 141 7602 7484 9587 -682 -311 -844 C ATOM 1122 CE2 PHE A 141 -28.771 14.893 -24.440 1.00 66.58 C ANISOU 1122 CE2 PHE A 141 7589 7513 10193 -807 -328 -1085 C ATOM 1123 CZ PHE A 141 -29.862 14.062 -24.535 1.00 64.20 C ANISOU 1123 CZ PHE A 141 7375 7312 9706 -763 -291 -880 C ATOM 1124 N VAL A 142 -26.052 15.152 -20.114 1.00 77.09 N ANISOU 1124 N VAL A 142 8964 9022 11303 -531 -1169 -1965 N ATOM 1125 CA VAL A 142 -24.778 14.553 -20.516 1.00 79.01 C ANISOU 1125 CA VAL A 142 9008 9273 11740 -565 -1326 -2074 C ATOM 1126 C VAL A 142 -24.483 13.322 -19.647 1.00 81.41 C ANISOU 1126 C VAL A 142 9430 9749 11751 -361 -1571 -2058 C ATOM 1127 O VAL A 142 -24.297 12.223 -20.173 1.00 79.35 O ANISOU 1127 O VAL A 142 9152 9525 11471 -351 -1564 -1884 O ATOM 1128 CB VAL A 142 -23.610 15.549 -20.431 1.00 81.49 C ANISOU 1128 CB VAL A 142 9082 9481 12398 -656 -1435 -2443 C ATOM 1129 CG1 VAL A 142 -22.296 14.865 -20.778 1.00 83.05 C ANISOU 1129 CG1 VAL A 142 9047 9698 12807 -672 -1601 -2560 C ATOM 1130 CG2 VAL A 142 -23.827 16.763 -21.314 1.00 80.35 C ANISOU 1130 CG2 VAL A 142 8839 9122 12565 -842 -1138 -2443 C ATOM 1131 N GLN A 143 -24.438 13.523 -18.322 1.00 85.68 N ANISOU 1131 N GLN A 143 10114 10388 12052 -174 -1777 -2241 N ATOM 1132 CA GLN A 143 -24.089 12.474 -17.353 1.00 89.17 C ANISOU 1132 CA GLN A 143 10711 10994 12173 89 -2018 -2250 C ATOM 1133 C GLN A 143 -24.977 11.236 -17.550 1.00 91.13 C ANISOU 1133 C GLN A 143 11163 11274 12185 154 -1831 -1861 C ATOM 1134 O GLN A 143 -24.541 10.104 -17.314 1.00 92.56 O ANISOU 1134 O GLN A 143 11411 11538 12220 307 -1943 -1784 O ATOM 1135 CB GLN A 143 -24.217 12.992 -15.920 1.00 91.61 C ANISOU 1135 CB GLN A 143 11225 11393 12187 318 -2206 -2462 C ATOM 1136 CG GLN A 143 -22.950 13.661 -15.409 1.00 95.67 C ANISOU 1136 CG GLN A 143 11536 11945 12866 362 -2553 -2925 C ATOM 1137 CD GLN A 143 -23.081 14.114 -13.975 1.00100.40 C ANISOU 1137 CD GLN A 143 12370 12651 13123 631 -2774 -3158 C ATOM 1138 OE1 GLN A 143 -24.112 14.639 -13.554 1.00100.19 O ANISOU 1138 OE1 GLN A 143 12577 12587 12904 664 -2599 -3060 O ATOM 1139 NE2 GLN A 143 -22.020 13.924 -13.207 1.00104.47 N ANISOU 1139 NE2 GLN A 143 12827 13309 13557 848 -3175 -3485 N ATOM 1140 N MET A 144 -26.221 11.461 -17.988 1.00 91.67 N ANISOU 1140 N MET A 144 11318 11269 12244 41 -1540 -1629 N ATOM 1141 CA MET A 144 -27.204 10.400 -18.185 1.00 88.81 C ANISOU 1141 CA MET A 144 11111 10908 11724 66 -1335 -1295 C ATOM 1142 C MET A 144 -27.020 9.731 -19.559 1.00 85.09 C ANISOU 1142 C MET A 144 10460 10378 11490 -113 -1238 -1151 C ATOM 1143 O MET A 144 -27.737 8.793 -19.881 1.00 84.20 O ANISOU 1143 O MET A 144 10428 10250 11311 -124 -1083 -912 O ATOM 1144 CB MET A 144 -28.624 10.971 -18.068 1.00 88.42 C ANISOU 1144 CB MET A 144 11184 10812 11599 27 -1084 -1147 C ATOM 1145 CG MET A 144 -29.619 9.995 -17.483 1.00 89.83 C ANISOU 1145 CG MET A 144 11598 11008 11524 164 -915 -890 C ATOM 1146 SD MET A 144 -29.797 10.109 -15.675 1.00 96.19 S ANISOU 1146 SD MET A 144 12750 11887 11910 502 -980 -949 S ATOM 1147 CE MET A 144 -28.102 9.960 -15.105 1.00 97.43 C ANISOU 1147 CE MET A 144 12880 12157 11980 686 -1397 -1249 C ATOM 1148 N MET A 145 -26.070 10.220 -20.366 1.00 83.38 N ANISOU 1148 N MET A 145 10004 10112 11562 -249 -1312 -1308 N ATOM 1149 CA MET A 145 -25.773 9.647 -21.676 1.00 81.64 C ANISOU 1149 CA MET A 145 9635 9832 11552 -386 -1223 -1191 C ATOM 1150 C MET A 145 -24.359 9.052 -21.670 1.00 85.44 C ANISOU 1150 C MET A 145 9988 10347 12125 -326 -1432 -1326 C ATOM 1151 O MET A 145 -24.159 7.872 -21.985 1.00 86.16 O ANISOU 1151 O MET A 145 10110 10457 12167 -283 -1435 -1186 O ATOM 1152 CB MET A 145 -25.878 10.708 -22.777 1.00 77.76 C ANISOU 1152 CB MET A 145 8984 9225 11333 -572 -1060 -1217 C ATOM 1153 CG MET A 145 -27.257 11.347 -22.892 1.00 75.03 C ANISOU 1153 CG MET A 145 8740 8854 10914 -613 -860 -1088 C ATOM 1154 SD MET A 145 -28.622 10.174 -23.166 1.00 69.16 S ANISOU 1154 SD MET A 145 8129 8155 9993 -597 -714 -790 S ATOM 1155 CE MET A 145 -28.556 10.016 -24.949 1.00 67.74 C ANISOU 1155 CE MET A 145 7800 7905 10031 -731 -600 -697 C ATOM 1156 N THR A 146 -23.389 9.887 -21.298 1.00 90.64 N ANISOU 1156 N THR A 146 10491 11007 12939 -322 -1605 -1615 N ATOM 1157 CA THR A 146 -21.977 9.555 -21.348 1.00 94.27 C ANISOU 1157 CA THR A 146 10752 11493 13570 -282 -1809 -1798 C ATOM 1158 C THR A 146 -21.673 8.291 -20.529 1.00 96.50 C ANISOU 1158 C THR A 146 11186 11916 13561 -35 -2003 -1743 C ATOM 1159 O THR A 146 -22.448 7.893 -19.650 1.00 93.14 O ANISOU 1159 O THR A 146 11031 11564 12794 129 -2002 -1626 O ATOM 1160 CB THR A 146 -21.136 10.729 -20.844 1.00 97.15 C ANISOU 1160 CB THR A 146 10919 11840 14151 -307 -1983 -2169 C ATOM 1161 OG1 THR A 146 -19.776 10.405 -21.128 1.00104.29 O ANISOU 1161 OG1 THR A 146 11563 12748 15311 -305 -2141 -2340 O ATOM 1162 CG2 THR A 146 -21.316 10.994 -19.366 1.00 99.71 C ANISOU 1162 CG2 THR A 146 11415 12293 14178 -100 -2213 -2345 C ATOM 1163 N ALA A 147 -20.514 7.690 -20.838 1.00 99.18 N ANISOU 1163 N ALA A 147 11352 12280 14052 4 -2142 -1823 N ATOM 1164 CA ALA A 147 -20.002 6.482 -20.194 1.00100.70 C ANISOU 1164 CA ALA A 147 11655 12595 14008 261 -2328 -1781 C ATOM 1165 C ALA A 147 -18.473 6.563 -20.116 1.00102.72 C ANISOU 1165 C ALA A 147 11619 12911 14499 328 -2604 -2076 C ATOM 1166 O ALA A 147 -17.880 7.576 -20.489 1.00102.36 O ANISOU 1166 O ALA A 147 11286 12793 14811 158 -2629 -2319 O ATOM 1167 CB ALA A 147 -20.454 5.262 -20.961 1.00 98.02 C ANISOU 1167 CB ALA A 147 11440 12196 13605 229 -2116 -1454 C TER 1168 ALA A 147 ATOM 1169 N ALA B1785 -36.245 36.887 -57.189 1.00114.72 N ANISOU 1169 N ALA B1785 17074 12291 14220 -1889 -113 2358 N ATOM 1170 CA ALA B1785 -35.547 35.947 -56.259 1.00113.41 C ANISOU 1170 CA ALA B1785 16842 12281 13965 -1923 -24 2196 C ATOM 1171 C ALA B1785 -35.294 34.592 -56.944 1.00110.83 C ANISOU 1171 C ALA B1785 16042 12332 13735 -2020 -92 2141 C ATOM 1172 O ALA B1785 -34.245 33.984 -56.722 1.00108.42 O ANISOU 1172 O ALA B1785 15655 12243 13296 -2200 -123 2026 O ATOM 1173 CB ALA B1785 -36.347 35.795 -54.983 1.00113.84 C ANISOU 1173 CB ALA B1785 17038 12077 14138 -1565 261 2198 C ATOM 1174 N LEU B1786 -36.248 34.130 -57.770 1.00110.42 N ANISOU 1174 N LEU B1786 15707 12332 13915 -1908 -127 2251 N ATOM 1175 CA LEU B1786 -36.154 32.839 -58.478 1.00108.44 C ANISOU 1175 CA LEU B1786 15115 12367 13721 -1996 -193 2209 C ATOM 1176 C LEU B1786 -36.577 32.995 -59.943 1.00109.30 C ANISOU 1176 C LEU B1786 15161 12507 13860 -2144 -405 2340 C ATOM 1177 O LEU B1786 -37.326 33.905 -60.282 1.00111.98 O ANISOU 1177 O LEU B1786 15595 12642 14309 -2083 -492 2508 O ATOM 1178 CB LEU B1786 -37.035 31.807 -57.769 1.00107.27 C ANISOU 1178 CB LEU B1786 14724 12211 13820 -1720 -47 2227 C ATOM 1179 CG LEU B1786 -36.286 30.613 -57.182 1.00105.42 C ANISOU 1179 CG LEU B1786 14360 12189 13505 -1748 41 2050 C ATOM 1180 CD1 LEU B1786 -35.201 31.061 -56.217 1.00105.41 C ANISOU 1180 CD1 LEU B1786 14597 12160 13291 -1832 102 1927 C ATOM 1181 CD2 LEU B1786 -37.246 29.660 -56.493 1.00105.67 C ANISOU 1181 CD2 LEU B1786 14180 12187 13780 -1485 178 2086 C ATOM 1182 N SER B1787 -36.107 32.062 -60.783 1.00107.72 N ANISOU 1182 N SER B1787 14838 12535 13555 -2329 -477 2272 N ATOM 1183 CA SER B1787 -36.241 32.130 -62.236 1.00108.64 C ANISOU 1183 CA SER B1787 15018 12676 13583 -2551 -684 2361 C ATOM 1184 C SER B1787 -36.285 30.722 -62.842 1.00109.32 C ANISOU 1184 C SER B1787 14983 12917 13636 -2620 -708 2315 C ATOM 1185 O SER B1787 -36.015 29.735 -62.157 1.00108.97 O ANISOU 1185 O SER B1787 14787 12993 13621 -2505 -549 2194 O ATOM 1186 CB SER B1787 -35.103 32.914 -62.818 1.00109.70 C ANISOU 1186 CB SER B1787 15374 12874 13433 -2818 -706 2302 C ATOM 1187 OG SER B1787 -33.860 32.348 -62.430 1.00108.68 O ANISOU 1187 OG SER B1787 15177 12957 13157 -2893 -531 2145 O ATOM 1188 N GLU B1788 -36.608 30.650 -64.140 1.00111.30 N ANISOU 1188 N GLU B1788 15366 13129 13791 -2825 -921 2416 N ATOM 1189 CA GLU B1788 -36.579 29.397 -64.900 1.00111.87 C ANISOU 1189 CA GLU B1788 15488 13284 13731 -2950 -962 2372 C ATOM 1190 C GLU B1788 -35.131 28.913 -65.025 1.00111.83 C ANISOU 1190 C GLU B1788 15571 13472 13445 -3038 -693 2160 C ATOM 1191 O GLU B1788 -34.888 27.710 -65.088 1.00112.75 O ANISOU 1191 O GLU B1788 15674 13677 13488 -3011 -572 2063 O ATOM 1192 CB GLU B1788 -37.190 29.557 -66.293 1.00113.88 C ANISOU 1192 CB GLU B1788 15991 13398 13880 -3205 -1281 2542 C ATOM 1193 CG GLU B1788 -38.643 29.125 -66.378 1.00115.03 C ANISOU 1193 CG GLU B1788 15987 13403 14314 -3165 -1580 2786 C ATOM 1194 CD GLU B1788 -39.095 28.745 -67.778 1.00118.02 C ANISOU 1194 CD GLU B1788 16678 13656 14508 -3491 -1934 2932 C ATOM 1195 OE1 GLU B1788 -38.437 29.174 -68.755 1.00118.64 O ANISOU 1195 OE1 GLU B1788 17126 13703 14247 -3735 -1959 2872 O ATOM 1196 OE2 GLU B1788 -40.098 28.011 -67.891 1.00118.76 O ANISOU 1196 OE2 GLU B1788 16673 13667 14783 -3526 -2194 3121 O ATOM 1197 N ASP B1789 -34.187 29.862 -65.067 1.00112.28 N ANISOU 1197 N ASP B1789 15711 13581 13369 -3141 -598 2123 N ATOM 1198 CA ASP B1789 -32.756 29.560 -65.041 1.00112.07 C ANISOU 1198 CA ASP B1789 15663 13749 13169 -3205 -324 1999 C ATOM 1199 C ASP B1789 -32.469 28.622 -63.859 1.00110.75 C ANISOU 1199 C ASP B1789 15220 13707 13151 -2983 -143 1892 C ATOM 1200 O ASP B1789 -31.750 27.636 -64.012 1.00111.47 O ANISOU 1200 O ASP B1789 15261 13933 13160 -2963 66 1810 O ATOM 1201 CB ASP B1789 -31.912 30.838 -64.980 1.00111.94 C ANISOU 1201 CB ASP B1789 15702 13757 13071 -3351 -308 2036 C ATOM 1202 CG ASP B1789 -32.044 31.724 -66.210 1.00113.15 C ANISOU 1202 CG ASP B1789 16154 13797 13041 -3593 -463 2133 C ATOM 1203 OD1 ASP B1789 -33.156 31.783 -66.773 1.00112.66 O ANISOU 1203 OD1 ASP B1789 16228 13564 13012 -3608 -700 2220 O ATOM 1204 OD2 ASP B1789 -31.033 32.344 -66.598 1.00113.77 O ANISOU 1204 OD2 ASP B1789 16315 13952 12956 -3781 -365 2151 O ATOM 1205 N ASP B1790 -33.063 28.928 -62.697 1.00110.05 N ANISOU 1205 N ASP B1790 14991 13545 13276 -2805 -206 1906 N ATOM 1206 CA ASP B1790 -32.867 28.167 -61.451 1.00108.84 C ANISOU 1206 CA ASP B1790 14625 13472 13256 -2608 -66 1815 C ATOM 1207 C ASP B1790 -33.588 26.813 -61.521 1.00108.24 C ANISOU 1207 C ASP B1790 14461 13404 13260 -2479 -53 1780 C ATOM 1208 O ASP B1790 -33.087 25.812 -61.008 1.00107.03 O ANISOU 1208 O ASP B1790 14177 13369 13117 -2381 102 1681 O ATOM 1209 CB ASP B1790 -33.370 28.941 -60.227 1.00108.81 C ANISOU 1209 CB ASP B1790 14612 13323 13405 -2461 -107 1845 C ATOM 1210 CG ASP B1790 -32.746 30.316 -60.048 1.00109.71 C ANISOU 1210 CG ASP B1790 14900 13371 13414 -2603 -160 1886 C ATOM 1211 OD1 ASP B1790 -31.503 30.389 -59.959 1.00107.82 O ANISOU 1211 OD1 ASP B1790 14631 13276 13059 -2760 -107 1860 O ATOM 1212 OD2 ASP B1790 -33.512 31.305 -59.995 1.00110.64 O ANISOU 1212 OD2 ASP B1790 15175 13279 13583 -2557 -258 1973 O ATOM 1213 N PHE B1791 -34.781 26.795 -62.127 1.00108.47 N ANISOU 1213 N PHE B1791 14558 13293 13359 -2493 -247 1893 N ATOM 1214 CA PHE B1791 -35.587 25.578 -62.227 1.00107.70 C ANISOU 1214 CA PHE B1791 14403 13174 13344 -2427 -310 1911 C ATOM 1215 C PHE B1791 -34.992 24.617 -63.271 1.00107.61 C ANISOU 1215 C PHE B1791 14602 13223 13061 -2576 -247 1827 C ATOM 1216 O PHE B1791 -35.209 23.411 -63.174 1.00107.83 O ANISOU 1216 O PHE B1791 14620 13262 13085 -2513 -214 1776 O ATOM 1217 CB PHE B1791 -37.050 25.927 -62.511 1.00109.40 C ANISOU 1217 CB PHE B1791 14585 13210 13771 -2427 -584 2134 C ATOM 1218 CG PHE B1791 -37.764 26.614 -61.372 1.00109.70 C ANISOU 1218 CG PHE B1791 14414 13151 14112 -2190 -540 2233 C ATOM 1219 CD1 PHE B1791 -37.785 26.055 -60.101 1.00108.00 C ANISOU 1219 CD1 PHE B1791 14026 12978 14032 -1964 -342 2148 C ATOM 1220 CD2 PHE B1791 -38.436 27.813 -61.570 1.00111.86 C ANISOU 1220 CD2 PHE B1791 14710 13262 14529 -2177 -669 2423 C ATOM 1221 CE1 PHE B1791 -38.443 26.685 -59.055 1.00108.10 C ANISOU 1221 CE1 PHE B1791 13936 12854 14281 -1731 -235 2239 C ATOM 1222 CE2 PHE B1791 -39.097 28.440 -60.523 1.00112.17 C ANISOU 1222 CE2 PHE B1791 14618 13165 14835 -1913 -548 2524 C ATOM 1223 CZ PHE B1791 -39.099 27.876 -59.268 1.00110.36 C ANISOU 1223 CZ PHE B1791 14263 12963 14706 -1690 -312 2427 C ATOM 1224 N ASP B1792 -34.246 25.146 -64.253 1.00106.45 N ANISOU 1224 N ASP B1792 14684 13088 12672 -2766 -202 1817 N ATOM 1225 CA ASP B1792 -33.462 24.324 -65.188 1.00105.62 C ANISOU 1225 CA ASP B1792 14838 13018 12275 -2867 -11 1729 C ATOM 1226 C ASP B1792 -32.394 23.545 -64.413 1.00102.49 C ANISOU 1226 C ASP B1792 14228 12800 11911 -2681 327 1597 C ATOM 1227 O ASP B1792 -32.199 22.356 -64.652 1.00101.66 O ANISOU 1227 O ASP B1792 14237 12693 11694 -2618 484 1521 O ATOM 1228 CB ASP B1792 -32.766 25.161 -66.266 1.00108.36 C ANISOU 1228 CB ASP B1792 15448 13348 12374 -3083 48 1760 C ATOM 1229 CG ASP B1792 -33.616 25.498 -67.479 1.00110.47 C ANISOU 1229 CG ASP B1792 16096 13405 12470 -3327 -256 1878 C ATOM 1230 OD1 ASP B1792 -34.785 25.065 -67.521 1.00109.83 O ANISOU 1230 OD1 ASP B1792 16047 13191 12490 -3346 -553 1970 O ATOM 1231 OD2 ASP B1792 -33.091 26.193 -68.376 1.00111.94 O ANISOU 1231 OD2 ASP B1792 16542 13556 12431 -3518 -212 1905 O ATOM 1232 N MET B1793 -31.698 24.241 -63.507 1.00 99.90 N ANISOU 1232 N MET B1793 13626 12600 11729 -2613 416 1595 N ATOM 1233 CA MET B1793 -30.619 23.655 -62.711 1.00 99.64 C ANISOU 1233 CA MET B1793 13344 12737 11775 -2472 673 1533 C ATOM 1234 C MET B1793 -31.155 22.475 -61.893 1.00 96.70 C ANISOU 1234 C MET B1793 12852 12357 11531 -2272 673 1454 C ATOM 1235 O MET B1793 -30.557 21.399 -61.909 1.00 98.30 O ANISOU 1235 O MET B1793 13029 12627 11692 -2165 895 1392 O ATOM 1236 CB MET B1793 -30.004 24.672 -61.745 1.00100.28 C ANISOU 1236 CB MET B1793 13201 12903 11997 -2493 634 1585 C ATOM 1237 CG MET B1793 -29.107 24.039 -60.679 1.00100.76 C ANISOU 1237 CG MET B1793 12975 13109 12199 -2363 780 1566 C ATOM 1238 SD MET B1793 -29.204 24.842 -59.049 1.00100.93 S ANISOU 1238 SD MET B1793 12873 13089 12386 -2345 579 1589 S ATOM 1239 CE MET B1793 -30.950 24.692 -58.679 1.00 99.77 C ANISOU 1239 CE MET B1793 12853 12742 12311 -2187 432 1525 C ATOM 1240 N PHE B1794 -32.252 22.704 -61.159 1.00 92.42 N ANISOU 1240 N PHE B1794 12235 11724 11156 -2205 457 1477 N ATOM 1241 CA PHE B1794 -32.820 21.710 -60.248 1.00 88.84 C ANISOU 1241 CA PHE B1794 11648 11259 10848 -2025 453 1424 C ATOM 1242 C PHE B1794 -33.097 20.413 -61.017 1.00 90.27 C ANISOU 1242 C PHE B1794 12010 11395 10892 -2029 485 1381 C ATOM 1243 O PHE B1794 -32.689 19.348 -60.588 1.00 89.64 O ANISOU 1243 O PHE B1794 11870 11373 10816 -1897 642 1295 O ATOM 1244 CB PHE B1794 -34.093 22.241 -59.587 1.00 86.07 C ANISOU 1244 CB PHE B1794 11222 10781 10698 -1959 260 1508 C ATOM 1245 CG PHE B1794 -34.680 21.352 -58.517 1.00 82.66 C ANISOU 1245 CG PHE B1794 10637 10334 10434 -1773 286 1476 C ATOM 1246 CD1 PHE B1794 -34.225 21.416 -57.210 1.00 80.11 C ANISOU 1246 CD1 PHE B1794 10188 10051 10198 -1643 398 1413 C ATOM 1247 CD2 PHE B1794 -35.700 20.461 -58.813 1.00 81.95 C ANISOU 1247 CD2 PHE B1794 10563 10170 10402 -1763 171 1532 C ATOM 1248 CE1 PHE B1794 -34.769 20.604 -56.227 1.00 78.37 C ANISOU 1248 CE1 PHE B1794 9866 9801 10109 -1481 437 1384 C ATOM 1249 CE2 PHE B1794 -36.240 19.648 -57.830 1.00 79.91 C ANISOU 1249 CE2 PHE B1794 10158 9900 10301 -1606 205 1519 C ATOM 1250 CZ PHE B1794 -35.773 19.720 -56.539 1.00 78.08 C ANISOU 1250 CZ PHE B1794 9808 9712 10145 -1453 359 1435 C ATOM 1251 N TYR B1795 -33.763 20.536 -62.168 1.00 92.51 N ANISOU 1251 N TYR B1795 12567 11547 11034 -2203 315 1453 N ATOM 1252 CA TYR B1795 -34.142 19.398 -62.988 1.00 95.29 C ANISOU 1252 CA TYR B1795 13224 11784 11194 -2275 274 1435 C ATOM 1253 C TYR B1795 -32.932 18.814 -63.730 1.00 97.45 C ANISOU 1253 C TYR B1795 13751 12086 11187 -2270 612 1329 C ATOM 1254 O TYR B1795 -32.932 17.629 -64.078 1.00 99.63 O ANISOU 1254 O TYR B1795 14287 12272 11294 -2238 707 1264 O ATOM 1255 CB TYR B1795 -35.244 19.803 -63.965 1.00 98.37 C ANISOU 1255 CB TYR B1795 13865 11993 11518 -2513 -80 1592 C ATOM 1256 CG TYR B1795 -36.578 20.085 -63.320 1.00 99.17 C ANISOU 1256 CG TYR B1795 13697 12037 11945 -2483 -380 1760 C ATOM 1257 CD1 TYR B1795 -37.125 19.211 -62.391 1.00 98.71 C ANISOU 1257 CD1 TYR B1795 13424 11997 12082 -2331 -387 1760 C ATOM 1258 CD2 TYR B1795 -37.315 21.208 -63.663 1.00100.64 C ANISOU 1258 CD2 TYR B1795 13840 12134 12261 -2595 -634 1949 C ATOM 1259 CE1 TYR B1795 -38.358 19.454 -61.806 1.00 99.35 C ANISOU 1259 CE1 TYR B1795 13232 12020 12496 -2281 -597 1956 C ATOM 1260 CE2 TYR B1795 -38.549 21.467 -63.088 1.00100.71 C ANISOU 1260 CE2 TYR B1795 13565 12077 12623 -2523 -848 2157 C ATOM 1261 CZ TYR B1795 -39.073 20.587 -62.157 1.00100.26 C ANISOU 1261 CZ TYR B1795 13274 12047 12772 -2362 -810 2168 C ATOM 1262 OH TYR B1795 -40.289 20.831 -61.590 1.00101.05 O ANISOU 1262 OH TYR B1795 13064 12077 13250 -2270 -958 2411 O ATOM 1263 N GLU B1796 -31.919 19.644 -63.996 1.00 98.46 N ANISOU 1263 N GLU B1796 13826 12316 11267 -2299 811 1335 N ATOM 1264 CA GLU B1796 -30.650 19.157 -64.534 1.00100.28 C ANISOU 1264 CA GLU B1796 14181 12600 11321 -2232 1227 1285 C ATOM 1265 C GLU B1796 -29.932 18.328 -63.458 1.00 98.83 C ANISOU 1265 C GLU B1796 13655 12562 11333 -1971 1460 1230 C ATOM 1266 O GLU B1796 -29.599 17.166 -63.693 1.00101.37 O ANISOU 1266 O GLU B1796 14148 12829 11538 -1837 1706 1166 O ATOM 1267 CB GLU B1796 -29.788 20.317 -65.036 1.00101.96 C ANISOU 1267 CB GLU B1796 14353 12898 11486 -2350 1362 1361 C ATOM 1268 CG GLU B1796 -30.104 20.733 -66.462 1.00104.76 C ANISOU 1268 CG GLU B1796 15206 13075 11523 -2591 1297 1397 C ATOM 1269 CD GLU B1796 -29.228 21.853 -66.997 1.00106.75 C ANISOU 1269 CD GLU B1796 15438 13408 11712 -2720 1454 1480 C ATOM 1270 OE1 GLU B1796 -28.465 22.440 -66.202 1.00105.74 O ANISOU 1270 OE1 GLU B1796 14876 13479 11820 -2655 1537 1534 O ATOM 1271 OE2 GLU B1796 -29.308 22.135 -68.208 1.00109.67 O ANISOU 1271 OE2 GLU B1796 16258 13625 11783 -2913 1470 1506 O ATOM 1272 N ILE B1797 -29.735 18.924 -62.273 1.00 95.16 N ANISOU 1272 N ILE B1797 12763 12247 11146 -1909 1361 1263 N ATOM 1273 CA ILE B1797 -28.973 18.320 -61.166 1.00 93.48 C ANISOU 1273 CA ILE B1797 12204 12174 11139 -1709 1515 1251 C ATOM 1274 C ILE B1797 -29.720 17.093 -60.615 1.00 92.38 C ANISOU 1274 C ILE B1797 12116 11953 11028 -1565 1446 1153 C ATOM 1275 O ILE B1797 -29.112 16.207 -60.020 1.00 92.54 O ANISOU 1275 O ILE B1797 11981 12037 11141 -1383 1622 1126 O ATOM 1276 CB ILE B1797 -28.690 19.365 -60.064 1.00 91.91 C ANISOU 1276 CB ILE B1797 11669 12089 11162 -1753 1347 1323 C ATOM 1277 CG1 ILE B1797 -27.805 20.511 -60.562 1.00 94.10 C ANISOU 1277 CG1 ILE B1797 11881 12453 11416 -1918 1410 1445 C ATOM 1278 CG2 ILE B1797 -28.096 18.710 -58.826 1.00 91.30 C ANISOU 1278 CG2 ILE B1797 11289 12112 11287 -1591 1400 1326 C ATOM 1279 CD1 ILE B1797 -26.333 20.162 -60.683 1.00 96.68 C ANISOU 1279 CD1 ILE B1797 11970 12936 11826 -1850 1736 1560 C ATOM 1280 N TRP B1798 -31.041 17.049 -60.814 1.00 91.72 N ANISOU 1280 N TRP B1798 12230 11728 10890 -1658 1173 1135 N ATOM 1281 CA TRP B1798 -31.895 15.952 -60.352 1.00 90.08 C ANISOU 1281 CA TRP B1798 12077 11432 10714 -1574 1060 1080 C ATOM 1282 C TRP B1798 -31.677 14.688 -61.193 1.00 92.47 C ANISOU 1282 C TRP B1798 12752 11617 10765 -1537 1245 1012 C ATOM 1283 O TRP B1798 -31.592 13.590 -60.641 1.00 91.72 O ANISOU 1283 O TRP B1798 12636 11511 10702 -1379 1336 946 O ATOM 1284 CB TRP B1798 -33.362 16.385 -60.380 1.00 88.56 C ANISOU 1284 CB TRP B1798 11929 11126 10593 -1709 706 1162 C ATOM 1285 CG TRP B1798 -34.333 15.283 -60.105 1.00 88.13 C ANISOU 1285 CG TRP B1798 11946 10969 10570 -1685 556 1162 C ATOM 1286 CD1 TRP B1798 -34.967 14.506 -61.027 1.00 89.49 C ANISOU 1286 CD1 TRP B1798 12487 10974 10542 -1832 410 1192 C ATOM 1287 CD2 TRP B1798 -34.806 14.847 -58.817 1.00 86.13 C ANISOU 1287 CD2 TRP B1798 11425 10753 10547 -1539 515 1154 C ATOM 1288 NE1 TRP B1798 -35.800 13.619 -60.403 1.00 88.71 N ANISOU 1288 NE1 TRP B1798 12324 10822 10558 -1796 262 1219 N ATOM 1289 CE2 TRP B1798 -35.725 13.805 -59.049 1.00 86.19 C ANISOU 1289 CE2 TRP B1798 11603 10633 10509 -1603 347 1193 C ATOM 1290 CE3 TRP B1798 -34.549 15.232 -57.496 1.00 84.67 C ANISOU 1290 CE3 TRP B1798 10928 10668 10573 -1386 591 1130 C ATOM 1291 CZ2 TRP B1798 -36.378 13.143 -58.010 1.00 85.62 C ANISOU 1291 CZ2 TRP B1798 11345 10560 10624 -1501 287 1210 C ATOM 1292 CZ3 TRP B1798 -35.200 14.581 -56.471 1.00 83.36 C ANISOU 1292 CZ3 TRP B1798 10632 10478 10561 -1277 548 1129 C ATOM 1293 CH2 TRP B1798 -36.101 13.547 -56.726 1.00 83.52 C ANISOU 1293 CH2 TRP B1798 10771 10399 10562 -1325 414 1170 C ATOM 1294 N GLU B1799 -31.603 14.847 -62.521 1.00 95.07 N ANISOU 1294 N GLU B1799 13485 11822 10813 -1688 1304 1028 N ATOM 1295 CA GLU B1799 -31.458 13.711 -63.435 1.00 97.70 C ANISOU 1295 CA GLU B1799 14336 11963 10822 -1677 1494 962 C ATOM 1296 C GLU B1799 -30.220 12.883 -63.060 1.00 97.72 C ANISOU 1296 C GLU B1799 14216 12044 10866 -1380 1955 902 C ATOM 1297 O GLU B1799 -30.226 11.672 -63.240 1.00 99.53 O ANISOU 1297 O GLU B1799 14768 12121 10928 -1273 2099 830 O ATOM 1298 CB GLU B1799 -31.379 14.168 -64.893 1.00101.50 C ANISOU 1298 CB GLU B1799 15318 12282 10963 -1888 1546 994 C ATOM 1299 CG GLU B1799 -31.272 13.008 -65.873 1.00105.72 C ANISOU 1299 CG GLU B1799 16542 12542 11085 -1896 1757 923 C ATOM 1300 CD GLU B1799 -31.493 13.340 -67.340 1.00110.14 C ANISOU 1300 CD GLU B1799 17768 12851 11226 -2175 1707 956 C ATOM 1301 OE1 GLU B1799 -31.612 14.540 -67.671 1.00110.32 O ANISOU 1301 OE1 GLU B1799 17673 12943 11297 -2353 1540 1041 O ATOM 1302 OE2 GLU B1799 -31.551 12.388 -68.153 1.00114.19 O ANISOU 1302 OE2 GLU B1799 18981 13069 11336 -2227 1828 899 O ATOM 1303 N LYS B1800 -29.171 13.536 -62.544 1.00 96.17 N ANISOU 1303 N LYS B1800 13564 12070 10906 -1260 2162 964 N ATOM 1304 CA LYS B1800 -27.937 12.855 -62.136 1.00 97.29 C ANISOU 1304 CA LYS B1800 13472 12311 11183 -979 2573 987 C ATOM 1305 C LYS B1800 -28.243 11.765 -61.106 1.00 95.10 C ANISOU 1305 C LYS B1800 13071 12024 11038 -808 2485 916 C ATOM 1306 O LYS B1800 -27.751 10.642 -61.204 1.00 96.63 O ANISOU 1306 O LYS B1800 13420 12129 11165 -590 2787 884 O ATOM 1307 CB LYS B1800 -26.936 13.842 -61.530 1.00 97.53 C ANISOU 1307 CB LYS B1800 12943 12594 11517 -959 2640 1129 C ATOM 1308 CG LYS B1800 -26.240 14.755 -62.530 1.00100.08 C ANISOU 1308 CG LYS B1800 13327 12954 11743 -1071 2863 1236 C ATOM 1309 CD LYS B1800 -24.902 15.261 -62.042 1.00101.85 C ANISOU 1309 CD LYS B1800 13009 13410 12279 -992 3068 1435 C ATOM 1310 CE LYS B1800 -24.335 16.353 -62.926 1.00104.62 C ANISOU 1310 CE LYS B1800 13374 13815 12559 -1162 3213 1563 C ATOM 1311 NZ LYS B1800 -22.869 16.498 -62.760 1.00107.23 N ANISOU 1311 NZ LYS B1800 13226 14338 13179 -1047 3555 1817 N ATOM 1312 N PHE B1801 -29.061 12.125 -60.118 1.00 92.17 N ANISOU 1312 N PHE B1801 12447 11722 10849 -896 2096 902 N ATOM 1313 CA PHE B1801 -29.337 11.277 -58.973 1.00 90.33 C ANISOU 1313 CA PHE B1801 12041 11505 10774 -758 1991 852 C ATOM 1314 C PHE B1801 -30.511 10.335 -59.256 1.00 89.72 C ANISOU 1314 C PHE B1801 12366 11222 10501 -825 1809 766 C ATOM 1315 O PHE B1801 -30.668 9.359 -58.546 1.00 88.45 O ANISOU 1315 O PHE B1801 12178 11029 10397 -698 1793 715 O ATOM 1316 CB PHE B1801 -29.645 12.133 -57.744 1.00 87.67 C ANISOU 1316 CB PHE B1801 11303 11305 10700 -819 1712 892 C ATOM 1317 CG PHE B1801 -28.498 12.977 -57.248 1.00 86.96 C ANISOU 1317 CG PHE B1801 10835 11396 10808 -800 1798 1002 C ATOM 1318 CD1 PHE B1801 -28.152 14.150 -57.899 1.00 87.62 C ANISOU 1318 CD1 PHE B1801 10893 11538 10858 -951 1813 1083 C ATOM 1319 CD2 PHE B1801 -27.776 12.606 -56.122 1.00 86.19 C ANISOU 1319 CD2 PHE B1801 10422 11397 10929 -668 1817 1053 C ATOM 1320 CE1 PHE B1801 -27.098 14.927 -57.442 1.00 88.69 C ANISOU 1320 CE1 PHE B1801 10688 11832 11178 -983 1845 1223 C ATOM 1321 CE2 PHE B1801 -26.730 13.387 -55.659 1.00 86.90 C ANISOU 1321 CE2 PHE B1801 10172 11636 11207 -713 1817 1207 C ATOM 1322 CZ PHE B1801 -26.390 14.545 -56.322 1.00 88.59 C ANISOU 1322 CZ PHE B1801 10358 11912 11390 -877 1829 1297 C ATOM 1323 N ASP B1802 -31.327 10.654 -60.270 1.00 81.48 N ANISOU 1323 N ASP B1802 10933 9872 10154 -674 2336 -285 N ATOM 1324 CA ASP B1802 -32.539 9.894 -60.607 1.00 82.84 C ANISOU 1324 CA ASP B1802 11283 9984 10208 -710 2210 -391 C ATOM 1325 C ASP B1802 -32.762 9.884 -62.118 1.00 86.66 C ANISOU 1325 C ASP B1802 12101 10599 10224 -1053 2284 -504 C ATOM 1326 O ASP B1802 -33.817 10.291 -62.603 1.00 86.09 O ANISOU 1326 O ASP B1802 12246 10566 9897 -1192 1947 -409 O ATOM 1327 CB ASP B1802 -33.760 10.475 -59.890 1.00 80.40 C ANISOU 1327 CB ASP B1802 10961 9607 9979 -621 1774 -200 C ATOM 1328 CG ASP B1802 -35.066 9.776 -60.232 1.00 81.65 C ANISOU 1328 CG ASP B1802 11251 9712 10058 -679 1623 -338 C ATOM 1329 OD1 ASP B1802 -35.028 8.556 -60.545 1.00 83.12 O ANISOU 1329 OD1 ASP B1802 11477 9849 10255 -689 1883 -588 O ATOM 1330 OD2 ASP B1802 -36.111 10.458 -60.198 1.00 79.97 O ANISOU 1330 OD2 ASP B1802 11077 9494 9812 -716 1249 -221 O ATOM 1331 N PRO B1803 -31.804 9.366 -62.917 1.00 91.92 N ANISOU 1331 N PRO B1803 12822 11335 10769 -1210 2722 -738 N ATOM 1332 CA PRO B1803 -31.936 9.396 -64.374 1.00 97.36 C ANISOU 1332 CA PRO B1803 13888 12173 10930 -1602 2831 -858 C ATOM 1333 C PRO B1803 -33.151 8.589 -64.861 1.00 99.19 C ANISOU 1333 C PRO B1803 14317 12392 10978 -1687 2660 -1016 C ATOM 1334 O PRO B1803 -33.729 8.913 -65.906 1.00101.48 O ANISOU 1334 O PRO B1803 14962 12818 10778 -1995 2475 -993 O ATOM 1335 CB PRO B1803 -30.610 8.799 -64.881 1.00100.90 C ANISOU 1335 CB PRO B1803 14256 12656 11423 -1712 3433 -1170 C ATOM 1336 CG PRO B1803 -30.087 7.977 -63.715 1.00 98.46 C ANISOU 1336 CG PRO B1803 13515 12161 11735 -1301 3581 -1274 C ATOM 1337 CD PRO B1803 -30.580 8.684 -62.468 1.00 93.69 C ANISOU 1337 CD PRO B1803 12744 11486 11366 -1028 3130 -927 C ATOM 1338 N GLU B1804 -33.536 7.573 -64.074 1.00 98.13 N ANISOU 1338 N GLU B1804 13963 12087 11233 -1425 2698 -1162 N ATOM 1339 CA GLU B1804 -34.606 6.633 -64.412 1.00 97.98 C ANISOU 1339 CA GLU B1804 14063 12022 11142 -1495 2622 -1384 C ATOM 1340 C GLU B1804 -35.977 7.298 -64.241 1.00 94.06 C ANISOU 1340 C GLU B1804 13626 11548 10562 -1499 2051 -1178 C ATOM 1341 O GLU B1804 -36.998 6.679 -64.539 1.00 93.68 O ANISOU 1341 O GLU B1804 13652 11486 10454 -1583 1908 -1357 O ATOM 1342 CB GLU B1804 -34.490 5.369 -63.554 1.00 98.25 C ANISOU 1342 CB GLU B1804 13857 11815 11658 -1221 2886 -1582 C ATOM 1343 CG GLU B1804 -33.144 4.668 -63.683 1.00101.80 C ANISOU 1343 CG GLU B1804 14181 12191 12308 -1159 3415 -1806 C ATOM 1344 CD GLU B1804 -32.608 4.535 -65.103 1.00107.33 C ANISOU 1344 CD GLU B1804 15113 13060 12607 -1527 3765 -2086 C ATOM 1345 OE1 GLU B1804 -33.259 3.854 -65.920 1.00111.01 O ANISOU 1345 OE1 GLU B1804 15805 13558 12814 -1762 3833 -2353 O ATOM 1346 OE2 GLU B1804 -31.543 5.121 -65.396 1.00108.51 O ANISOU 1346 OE2 GLU B1804 15223 13315 12689 -1613 3989 -2062 O ATOM 1347 N ALA B1805 -35.984 8.550 -63.765 1.00 90.29 N ANISOU 1347 N ALA B1805 13085 11092 10126 -1412 1740 -837 N ATOM 1348 CA ALA B1805 -37.189 9.362 -63.654 1.00 88.64 C ANISOU 1348 CA ALA B1805 12899 10884 9895 -1405 1191 -638 C ATOM 1349 C ALA B1805 -38.200 8.676 -62.723 1.00 85.77 C ANISOU 1349 C ALA B1805 12297 10360 9928 -1206 1083 -770 C ATOM 1350 O ALA B1805 -39.408 8.751 -62.943 1.00 86.67 O ANISOU 1350 O ALA B1805 12424 10478 10025 -1267 722 -816 O ATOM 1351 CB ALA B1805 -37.769 9.617 -65.026 1.00 91.97 C ANISOU 1351 CB ALA B1805 13676 11468 9800 -1725 922 -648 C ATOM 1352 N THR B1806 -37.690 8.031 -61.664 1.00 81.87 N ANISOU 1352 N THR B1806 11590 9716 9801 -979 1387 -827 N ATOM 1353 CA THR B1806 -38.525 7.425 -60.634 1.00 78.94 C ANISOU 1353 CA THR B1806 11035 9164 9794 -816 1353 -918 C ATOM 1354 C THR B1806 -39.308 8.510 -59.892 1.00 76.19 C ANISOU 1354 C THR B1806 10533 8784 9628 -726 963 -717 C ATOM 1355 O THR B1806 -40.275 8.205 -59.224 1.00 76.40 O ANISOU 1355 O THR B1806 10427 8691 9909 -672 878 -822 O ATOM 1356 CB THR B1806 -37.708 6.647 -59.594 1.00 77.78 C ANISOU 1356 CB THR B1806 10752 8844 9956 -590 1709 -936 C ATOM 1357 OG1 THR B1806 -36.974 7.589 -58.811 1.00 75.60 O ANISOU 1357 OG1 THR B1806 10343 8589 9792 -437 1640 -669 O ATOM 1358 CG2 THR B1806 -36.767 5.630 -60.202 1.00 80.23 C ANISOU 1358 CG2 THR B1806 11142 9129 10210 -618 2123 -1140 C ATOM 1359 N GLN B1807 -38.840 9.760 -59.999 1.00 75.53 N ANISOU 1359 N GLN B1807 10467 8789 9442 -726 779 -454 N ATOM 1360 CA GLN B1807 -39.344 10.920 -59.269 1.00 72.05 C ANISOU 1360 CA GLN B1807 9868 8291 9215 -627 461 -257 C ATOM 1361 C GLN B1807 -39.006 10.794 -57.780 1.00 68.27 C ANISOU 1361 C GLN B1807 9179 7688 9072 -426 651 -228 C ATOM 1362 O GLN B1807 -39.646 11.407 -56.948 1.00 66.84 O ANISOU 1362 O GLN B1807 8837 7421 9135 -355 475 -182 O ATOM 1363 CB GLN B1807 -40.850 11.081 -59.448 1.00 72.92 C ANISOU 1363 CB GLN B1807 9909 8357 9440 -674 81 -357 C ATOM 1364 CG GLN B1807 -41.268 11.416 -60.867 1.00 76.81 C ANISOU 1364 CG GLN B1807 10624 8977 9581 -867 -250 -325 C ATOM 1365 CD GLN B1807 -42.603 12.118 -60.838 1.00 78.39 C ANISOU 1365 CD GLN B1807 10666 9107 10011 -835 -758 -314 C ATOM 1366 OE1 GLN B1807 -43.592 11.596 -60.326 1.00 77.70 O ANISOU 1366 OE1 GLN B1807 10350 8930 10239 -790 -796 -554 O ATOM 1367 NE2 GLN B1807 -42.628 13.335 -61.354 1.00 81.31 N ANISOU 1367 NE2 GLN B1807 11140 9486 10268 -855 -1144 -39 N ATOM 1368 N PHE B1808 -37.975 10.015 -57.458 1.00 67.51 N ANISOU 1368 N PHE B1808 9088 7575 8985 -342 1000 -262 N ATOM 1369 CA PHE B1808 -37.594 9.785 -56.087 1.00 65.32 C ANISOU 1369 CA PHE B1808 8670 7185 8962 -161 1138 -211 C ATOM 1370 C PHE B1808 -36.074 9.680 -55.996 1.00 65.44 C ANISOU 1370 C PHE B1808 8655 7253 8955 -64 1363 -125 C ATOM 1371 O PHE B1808 -35.403 9.356 -56.977 1.00 67.68 O ANISOU 1371 O PHE B1808 9024 7617 9073 -140 1535 -200 O ATOM 1372 CB PHE B1808 -38.202 8.490 -55.545 1.00 65.78 C ANISOU 1372 CB PHE B1808 8746 7073 9172 -119 1312 -397 C ATOM 1373 CG PHE B1808 -39.695 8.494 -55.342 1.00 65.64 C ANISOU 1373 CG PHE B1808 8681 6977 9279 -211 1151 -538 C ATOM 1374 CD1 PHE B1808 -40.255 8.987 -54.174 1.00 63.80 C ANISOU 1374 CD1 PHE B1808 8321 6657 9261 -171 1077 -502 C ATOM 1375 CD2 PHE B1808 -40.541 7.957 -56.300 1.00 67.53 C ANISOU 1375 CD2 PHE B1808 8987 7233 9438 -357 1097 -753 C ATOM 1376 CE1 PHE B1808 -41.628 8.964 -53.985 1.00 63.83 C ANISOU 1376 CE1 PHE B1808 8229 6578 9445 -269 979 -695 C ATOM 1377 CE2 PHE B1808 -41.913 7.929 -56.107 1.00 67.14 C ANISOU 1377 CE2 PHE B1808 8829 7112 9569 -441 948 -931 C ATOM 1378 CZ PHE B1808 -42.453 8.437 -54.951 1.00 65.94 C ANISOU 1378 CZ PHE B1808 8515 6859 9678 -393 904 -910 C ATOM 1379 N ILE B1809 -35.564 9.956 -54.795 1.00 63.54 N ANISOU 1379 N ILE B1809 8280 6970 8892 86 1362 0 N ATOM 1380 CA ILE B1809 -34.186 9.673 -54.416 1.00 63.64 C ANISOU 1380 CA ILE B1809 8195 6999 8986 231 1535 54 C ATOM 1381 C ILE B1809 -34.202 9.173 -52.972 1.00 61.06 C ANISOU 1381 C ILE B1809 7822 6531 8847 402 1523 118 C ATOM 1382 O ILE B1809 -35.094 9.509 -52.199 1.00 58.26 O ANISOU 1382 O ILE B1809 7486 6120 8528 364 1392 149 O ATOM 1383 CB ILE B1809 -33.289 10.917 -54.571 1.00 64.23 C ANISOU 1383 CB ILE B1809 8159 7233 9010 186 1470 189 C ATOM 1384 CG1 ILE B1809 -33.823 12.093 -53.746 1.00 62.52 C ANISOU 1384 CG1 ILE B1809 7877 7023 8854 164 1219 328 C ATOM 1385 CG2 ILE B1809 -33.114 11.282 -56.041 1.00 66.05 C ANISOU 1385 CG2 ILE B1809 8514 7584 8996 -16 1537 144 C ATOM 1386 CD1 ILE B1809 -32.885 13.272 -53.683 1.00 63.36 C ANISOU 1386 CD1 ILE B1809 7864 7247 8962 125 1179 450 C ATOM 1387 N GLU B1810 -33.210 8.364 -52.620 1.00 62.13 N ANISOU 1387 N GLU B1810 7904 6594 9105 580 1660 130 N ATOM 1388 CA GLU B1810 -33.161 7.824 -51.301 1.00 63.21 C ANISOU 1388 CA GLU B1810 8068 6583 9365 734 1612 234 C ATOM 1389 C GLU B1810 -32.772 8.965 -50.374 1.00 60.17 C ANISOU 1389 C GLU B1810 7559 6329 8971 744 1409 393 C ATOM 1390 O GLU B1810 -32.126 9.902 -50.794 1.00 60.92 O ANISOU 1390 O GLU B1810 7502 6596 9045 700 1363 417 O ATOM 1391 CB GLU B1810 -32.207 6.633 -51.232 1.00 68.10 C ANISOU 1391 CB GLU B1810 8664 7051 10160 954 1755 220 C ATOM 1392 CG GLU B1810 -32.565 5.524 -52.203 1.00 71.57 C ANISOU 1392 CG GLU B1810 9220 7345 10627 919 2001 14 C ATOM 1393 CD GLU B1810 -32.329 4.138 -51.633 1.00 76.65 C ANISOU 1393 CD GLU B1810 9961 7682 11480 1123 2109 29 C ATOM 1394 OE1 GLU B1810 -33.093 3.736 -50.717 1.00 79.41 O ANISOU 1394 OE1 GLU B1810 10506 7857 11808 1114 2055 125 O ATOM 1395 OE2 GLU B1810 -31.372 3.475 -52.077 1.00 79.81 O ANISOU 1395 OE2 GLU B1810 10245 7994 12082 1284 2259 -56 O ATOM 1396 N TYR B1811 -33.203 8.876 -49.123 1.00 59.76 N ANISOU 1396 N TYR B1811 7601 6188 8916 762 1315 483 N ATOM 1397 CA TYR B1811 -32.946 9.906 -48.157 1.00 60.38 C ANISOU 1397 CA TYR B1811 7595 6386 8962 731 1138 593 C ATOM 1398 C TYR B1811 -31.436 10.136 -48.031 1.00 62.01 C ANISOU 1398 C TYR B1811 7593 6718 9249 884 1055 680 C ATOM 1399 O TYR B1811 -30.963 11.267 -48.066 1.00 64.11 O ANISOU 1399 O TYR B1811 7688 7158 9513 813 970 693 O ATOM 1400 CB TYR B1811 -33.556 9.525 -46.811 1.00 61.92 C ANISOU 1400 CB TYR B1811 7984 6450 9091 702 1102 655 C ATOM 1401 CG TYR B1811 -33.272 10.505 -45.706 1.00 63.16 C ANISOU 1401 CG TYR B1811 8087 6734 9174 640 936 738 C ATOM 1402 CD1 TYR B1811 -33.292 11.868 -45.941 1.00 63.02 C ANISOU 1402 CD1 TYR B1811 7888 6878 9178 520 867 685 C ATOM 1403 CD2 TYR B1811 -33.015 10.071 -44.418 1.00 67.34 C ANISOU 1403 CD2 TYR B1811 8784 7205 9595 678 845 869 C ATOM 1404 CE1 TYR B1811 -33.044 12.776 -44.927 1.00 65.18 C ANISOU 1404 CE1 TYR B1811 8108 7258 9397 437 744 716 C ATOM 1405 CE2 TYR B1811 -32.758 10.964 -43.391 1.00 69.49 C ANISOU 1405 CE2 TYR B1811 9031 7617 9755 581 694 913 C ATOM 1406 CZ TYR B1811 -32.772 12.323 -43.649 1.00 68.77 C ANISOU 1406 CZ TYR B1811 8718 7692 9717 457 661 813 C ATOM 1407 OH TYR B1811 -32.521 13.221 -42.652 1.00 73.61 O ANISOU 1407 OH TYR B1811 9297 8435 10235 338 540 813 O ATOM 1408 N SER B1812 -30.689 9.038 -47.936 1.00 62.45 N ANISOU 1408 N SER B1812 7643 6660 9424 1096 1088 716 N ATOM 1409 CA SER B1812 -29.266 9.048 -47.674 1.00 63.23 C ANISOU 1409 CA SER B1812 7501 6839 9681 1285 978 775 C ATOM 1410 C SER B1812 -28.455 9.698 -48.803 1.00 62.38 C ANISOU 1410 C SER B1812 7122 6909 9670 1235 1106 641 C ATOM 1411 O SER B1812 -27.239 9.664 -48.746 1.00 63.41 O ANISOU 1411 O SER B1812 6987 7106 9997 1380 1068 621 O ATOM 1412 CB SER B1812 -28.791 7.641 -47.467 1.00 65.90 C ANISOU 1412 CB SER B1812 7890 6951 10197 1543 990 822 C ATOM 1413 OG SER B1812 -28.870 6.937 -48.693 1.00 65.92 O ANISOU 1413 OG SER B1812 7884 6852 10308 1554 1268 644 O ATOM 1414 N VAL B1813 -29.095 10.246 -49.839 1.00 61.35 N ANISOU 1414 N VAL B1813 7061 6843 9407 1022 1254 543 N ATOM 1415 CA VAL B1813 -28.343 11.023 -50.839 1.00 63.23 C ANISOU 1415 CA VAL B1813 7115 7249 9658 905 1383 449 C ATOM 1416 C VAL B1813 -28.900 12.451 -50.914 1.00 62.23 C ANISOU 1416 C VAL B1813 7036 7239 9368 673 1284 510 C ATOM 1417 O VAL B1813 -28.613 13.184 -51.869 1.00 62.75 O ANISOU 1417 O VAL B1813 7072 7404 9363 505 1395 467 O ATOM 1418 CB VAL B1813 -28.339 10.340 -52.220 1.00 63.72 C ANISOU 1418 CB VAL B1813 7244 7269 9694 846 1669 278 C ATOM 1419 CG1 VAL B1813 -27.998 8.862 -52.103 1.00 65.84 C ANISOU 1419 CG1 VAL B1813 7492 7349 10174 1082 1780 199 C ATOM 1420 CG2 VAL B1813 -29.652 10.540 -52.961 1.00 61.89 C ANISOU 1420 CG2 VAL B1813 7287 7017 9208 636 1685 261 C ATOM 1421 N LEU B1814 -29.668 12.852 -49.895 1.00 61.06 N ANISOU 1421 N LEU B1814 6974 7055 9169 652 1093 603 N ATOM 1422 CA LEU B1814 -30.330 14.144 -49.913 1.00 60.12 C ANISOU 1422 CA LEU B1814 6890 6980 8969 459 999 636 C ATOM 1423 C LEU B1814 -29.298 15.227 -49.583 1.00 61.48 C ANISOU 1423 C LEU B1814 6844 7299 9215 405 945 661 C ATOM 1424 O LEU B1814 -29.350 16.325 -50.136 1.00 61.11 O ANISOU 1424 O LEU B1814 6790 7290 9138 233 957 675 O ATOM 1425 CB LEU B1814 -31.490 14.129 -48.915 1.00 58.23 C ANISOU 1425 CB LEU B1814 6784 6635 8703 439 880 654 C ATOM 1426 CG LEU B1814 -32.400 15.358 -48.925 1.00 56.55 C ANISOU 1426 CG LEU B1814 6587 6403 8494 267 788 644 C ATOM 1427 CD1 LEU B1814 -33.049 15.566 -50.287 1.00 55.61 C ANISOU 1427 CD1 LEU B1814 6559 6242 8325 174 803 627 C ATOM 1428 CD2 LEU B1814 -33.459 15.240 -47.840 1.00 55.16 C ANISOU 1428 CD2 LEU B1814 6497 6122 8338 233 743 591 C ATOM 1429 N SER B1815 -28.359 14.878 -48.694 1.00 63.37 N ANISOU 1429 N SER B1815 6913 7603 9561 550 868 669 N ATOM 1430 CA SER B1815 -27.228 15.727 -48.314 1.00 64.47 C ANISOU 1430 CA SER B1815 6786 7901 9809 513 808 648 C ATOM 1431 C SER B1815 -26.346 16.024 -49.538 1.00 67.19 C ANISOU 1431 C SER B1815 6975 8325 10228 424 1032 556 C ATOM 1432 O SER B1815 -26.017 17.181 -49.799 1.00 69.92 O ANISOU 1432 O SER B1815 7239 8746 10580 231 1077 540 O ATOM 1433 CB SER B1815 -26.445 15.087 -47.201 1.00 65.36 C ANISOU 1433 CB SER B1815 6753 8059 10020 714 625 674 C ATOM 1434 OG SER B1815 -25.163 15.675 -47.086 1.00 67.98 O ANISOU 1434 OG SER B1815 6750 8560 10520 705 585 598 O ATOM 1435 N ASP B1816 -25.981 14.975 -50.285 1.00 69.14 N ANISOU 1435 N ASP B1816 7202 8533 10534 537 1208 477 N ATOM 1436 CA ASP B1816 -25.205 15.100 -51.525 1.00 71.03 C ANISOU 1436 CA ASP B1816 7336 8839 10812 411 1502 342 C ATOM 1437 C ASP B1816 -25.912 16.061 -52.495 1.00 70.23 C ANISOU 1437 C ASP B1816 7495 8729 10460 119 1596 401 C ATOM 1438 O ASP B1816 -25.275 16.956 -53.057 1.00 71.38 O ANISOU 1438 O ASP B1816 7572 8953 10593 -90 1746 366 O ATOM 1439 CB ASP B1816 -24.979 13.739 -52.191 1.00 72.43 C ANISOU 1439 CB ASP B1816 7513 8935 11073 556 1707 214 C ATOM 1440 CG ASP B1816 -23.994 12.824 -51.470 1.00 75.94 C ANISOU 1440 CG ASP B1816 7645 9354 11854 859 1635 141 C ATOM 1441 OD1 ASP B1816 -23.004 13.350 -50.896 1.00 76.34 O ANISOU 1441 OD1 ASP B1816 7368 9528 12107 898 1530 103 O ATOM 1442 OD2 ASP B1816 -24.210 11.578 -51.506 1.00 75.96 O ANISOU 1442 OD2 ASP B1816 7725 9196 11939 1059 1670 116 O ATOM 1443 N PHE B1817 -27.223 15.870 -52.679 1.00 67.72 N ANISOU 1443 N PHE B1817 7473 8297 9958 103 1493 493 N ATOM 1444 CA PHE B1817 -28.013 16.581 -53.691 1.00 67.61 C ANISOU 1444 CA PHE B1817 7734 8243 9711 -126 1505 570 C ATOM 1445 C PHE B1817 -28.082 18.076 -53.355 1.00 68.19 C ANISOU 1445 C PHE B1817 7792 8311 9805 -276 1370 686 C ATOM 1446 O PHE B1817 -27.691 18.938 -54.158 1.00 69.16 O ANISOU 1446 O PHE B1817 7991 8452 9832 -499 1484 728 O ATOM 1447 CB PHE B1817 -29.413 15.970 -53.770 1.00 65.91 C ANISOU 1447 CB PHE B1817 7752 7907 9384 -67 1365 605 C ATOM 1448 CG PHE B1817 -30.391 16.696 -54.656 1.00 65.81 C ANISOU 1448 CG PHE B1817 7998 7834 9170 -255 1248 705 C ATOM 1449 CD1 PHE B1817 -30.238 16.695 -56.032 1.00 68.91 C ANISOU 1449 CD1 PHE B1817 8597 8269 9315 -446 1390 698 C ATOM 1450 CD2 PHE B1817 -31.492 17.339 -54.119 1.00 64.40 C ANISOU 1450 CD2 PHE B1817 7865 7547 9057 -244 985 793 C ATOM 1451 CE1 PHE B1817 -31.148 17.350 -56.851 1.00 69.83 C ANISOU 1451 CE1 PHE B1817 8988 8322 9221 -609 1202 830 C ATOM 1452 CE2 PHE B1817 -32.401 17.990 -54.938 1.00 65.65 C ANISOU 1452 CE2 PHE B1817 8230 7621 9092 -375 809 894 C ATOM 1453 CZ PHE B1817 -32.230 17.992 -56.303 1.00 67.82 C ANISOU 1453 CZ PHE B1817 8737 7940 9089 -548 883 937 C ATOM 1454 N ALA B1818 -28.573 18.355 -52.145 1.00 66.19 N ANISOU 1454 N ALA B1818 7461 8014 9674 -174 1153 725 N ATOM 1455 CA ALA B1818 -28.647 19.679 -51.580 1.00 65.45 C ANISOU 1455 CA ALA B1818 7310 7891 9666 -288 1033 783 C ATOM 1456 C ALA B1818 -27.354 20.468 -51.842 1.00 67.84 C ANISOU 1456 C ALA B1818 7444 8298 10034 -444 1195 746 C ATOM 1457 O ALA B1818 -27.414 21.692 -52.024 1.00 68.91 O ANISOU 1457 O ALA B1818 7637 8361 10184 -631 1180 818 O ATOM 1458 CB ALA B1818 -28.931 19.554 -50.107 1.00 64.22 C ANISOU 1458 CB ALA B1818 7037 7736 9626 -160 869 746 C ATOM 1459 N ASP B1819 -26.207 19.772 -51.856 1.00 68.82 N ANISOU 1459 N ASP B1819 7345 8562 10239 -370 1355 619 N ATOM 1460 CA ASP B1819 -24.875 20.382 -52.072 1.00 71.61 C ANISOU 1460 CA ASP B1819 7457 9034 10716 -522 1551 512 C ATOM 1461 C ASP B1819 -24.602 20.606 -53.567 1.00 73.09 C ANISOU 1461 C ASP B1819 7833 9205 10733 -769 1853 510 C ATOM 1462 O ASP B1819 -24.038 21.622 -53.936 1.00 75.46 O ANISOU 1462 O ASP B1819 8122 9509 11038 -1022 2005 508 O ATOM 1463 CB ASP B1819 -23.761 19.521 -51.469 1.00 73.55 C ANISOU 1463 CB ASP B1819 7330 9423 11190 -322 1574 343 C ATOM 1464 CG ASP B1819 -22.554 20.300 -50.970 1.00 76.11 C ANISOU 1464 CG ASP B1819 7289 9886 11742 -423 1607 207 C ATOM 1465 OD1 ASP B1819 -22.744 21.202 -50.128 1.00 75.25 O ANISOU 1465 OD1 ASP B1819 7152 9782 11658 -496 1424 250 O ATOM 1466 OD2 ASP B1819 -21.425 19.970 -51.398 1.00 79.21 O ANISOU 1466 OD2 ASP B1819 7398 10381 12317 -433 1827 21 O ATOM 1467 N ALA B1820 -24.987 19.650 -54.416 1.00 74.12 N ANISOU 1467 N ALA B1820 8158 9312 10690 -728 1959 497 N ATOM 1468 CA ALA B1820 -24.736 19.723 -55.860 1.00 77.73 C ANISOU 1468 CA ALA B1820 8849 9776 10907 -997 2265 472 C ATOM 1469 C ALA B1820 -25.575 20.835 -56.505 1.00 79.70 C ANISOU 1469 C ALA B1820 9499 9891 10889 -1238 2143 716 C ATOM 1470 O ALA B1820 -25.241 21.322 -57.583 1.00 84.24 O ANISOU 1470 O ALA B1820 10314 10459 11234 -1542 2372 752 O ATOM 1471 CB ALA B1820 -25.017 18.393 -56.509 1.00 77.68 C ANISOU 1471 CB ALA B1820 8959 9778 10777 -897 2383 369 C ATOM 1472 N LEU B1821 -26.675 21.222 -55.853 1.00 78.55 N ANISOU 1472 N LEU B1821 9440 9620 10786 -1108 1784 878 N ATOM 1473 CA LEU B1821 -27.468 22.364 -56.290 1.00 79.44 C ANISOU 1473 CA LEU B1821 9860 9555 10768 -1274 1596 1113 C ATOM 1474 C LEU B1821 -26.602 23.631 -56.312 1.00 82.26 C ANISOU 1474 C LEU B1821 10175 9875 11205 -1523 1753 1151 C ATOM 1475 O LEU B1821 -25.615 23.751 -55.580 1.00 80.85 O ANISOU 1475 O LEU B1821 9644 9809 11264 -1510 1899 982 O ATOM 1476 CB LEU B1821 -28.658 22.545 -55.342 1.00 76.41 C ANISOU 1476 CB LEU B1821 9432 9038 10560 -1062 1230 1187 C ATOM 1477 CG LEU B1821 -29.798 21.542 -55.500 1.00 74.45 C ANISOU 1477 CG LEU B1821 9308 8762 10217 -890 1052 1182 C ATOM 1478 CD1 LEU B1821 -31.022 22.020 -54.742 1.00 72.68 C ANISOU 1478 CD1 LEU B1821 9057 8368 10188 -765 731 1242 C ATOM 1479 CD2 LEU B1821 -30.140 21.311 -56.964 1.00 76.66 C ANISOU 1479 CD2 LEU B1821 9949 9029 10147 -1053 1071 1276 C ATOM 1480 N SER B1822 -26.996 24.570 -57.175 1.00 85.46 N ANISOU 1480 N SER B1822 10956 10104 11409 -1757 1700 1381 N ATOM 1481 CA SER B1822 -26.373 25.874 -57.277 1.00 88.55 C ANISOU 1481 CA SER B1822 11402 10379 11862 -2026 1833 1467 C ATOM 1482 C SER B1822 -27.220 26.892 -56.511 1.00 88.04 C ANISOU 1482 C SER B1822 11330 10070 12049 -1926 1492 1614 C ATOM 1483 O SER B1822 -28.343 26.581 -56.074 1.00 85.87 O ANISOU 1483 O SER B1822 11043 9720 11861 -1678 1169 1654 O ATOM 1484 CB SER B1822 -26.193 26.286 -58.713 1.00 92.52 C ANISOU 1484 CB SER B1822 12377 10801 11973 -2379 2015 1646 C ATOM 1485 OG SER B1822 -25.641 25.223 -59.473 1.00 94.24 O ANISOU 1485 OG SER B1822 12633 11234 11940 -2467 2329 1471 O ATOM 1486 N GLU B1823 -26.658 28.097 -56.354 1.00 90.50 N ANISOU 1486 N GLU B1823 11629 10246 12508 -2140 1607 1656 N ATOM 1487 CA GLU B1823 -27.333 29.193 -55.683 1.00 90.30 C ANISOU 1487 CA GLU B1823 11593 9946 12768 -2090 1352 1761 C ATOM 1488 C GLU B1823 -28.481 29.653 -56.578 1.00 90.72 C ANISOU 1488 C GLU B1823 12096 9697 12673 -2097 1042 2095 C ATOM 1489 O GLU B1823 -28.345 29.666 -57.798 1.00 92.92 O ANISOU 1489 O GLU B1823 12774 9941 12588 -2309 1116 2292 O ATOM 1490 CB GLU B1823 -26.355 30.327 -55.367 1.00 93.82 C ANISOU 1490 CB GLU B1823 11922 10311 13413 -2351 1596 1694 C ATOM 1491 CG GLU B1823 -25.192 29.915 -54.476 1.00 94.38 C ANISOU 1491 CG GLU B1823 11507 10693 13657 -2343 1836 1349 C ATOM 1492 CD GLU B1823 -25.534 29.536 -53.041 1.00 93.16 C ANISOU 1492 CD GLU B1823 10984 10658 13754 -2057 1616 1153 C ATOM 1493 OE1 GLU B1823 -26.732 29.608 -52.651 1.00 92.07 O ANISOU 1493 OE1 GLU B1823 10933 10353 13695 -1871 1324 1242 O ATOM 1494 OE2 GLU B1823 -24.590 29.168 -52.307 1.00 93.42 O ANISOU 1494 OE2 GLU B1823 10640 10950 13905 -2035 1735 901 O ATOM 1495 N PRO B1824 -29.613 30.023 -55.973 1.00 87.77 N ANISOU 1495 N PRO B1824 11657 9106 12585 -1877 688 2144 N ATOM 1496 CA PRO B1824 -29.758 30.181 -54.536 1.00 84.78 C ANISOU 1496 CA PRO B1824 10868 8741 12603 -1709 651 1900 C ATOM 1497 C PRO B1824 -30.228 28.930 -53.779 1.00 81.01 C ANISOU 1497 C PRO B1824 10133 8503 12142 -1437 570 1687 C ATOM 1498 O PRO B1824 -30.152 28.913 -52.555 1.00 79.61 O ANISOU 1498 O PRO B1824 9647 8404 12196 -1347 596 1465 O ATOM 1499 CB PRO B1824 -30.832 31.267 -54.424 1.00 85.94 C ANISOU 1499 CB PRO B1824 11116 8470 13064 -1644 343 2052 C ATOM 1500 CG PRO B1824 -31.737 30.981 -55.591 1.00 87.94 C ANISOU 1500 CG PRO B1824 11731 8596 13084 -1580 44 2331 C ATOM 1501 CD PRO B1824 -30.806 30.495 -56.681 1.00 89.59 C ANISOU 1501 CD PRO B1824 12223 9018 12796 -1817 297 2440 C ATOM 1502 N LEU B1825 -30.689 27.905 -54.506 1.00 80.37 N ANISOU 1502 N LEU B1825 10213 8529 11794 -1342 487 1750 N ATOM 1503 CA LEU B1825 -31.438 26.795 -53.905 1.00 77.23 C ANISOU 1503 CA LEU B1825 9650 8256 11437 -1093 368 1593 C ATOM 1504 C LEU B1825 -30.515 25.906 -53.061 1.00 74.17 C ANISOU 1504 C LEU B1825 8981 8167 11033 -1028 601 1361 C ATOM 1505 O LEU B1825 -30.993 25.255 -52.125 1.00 72.62 O ANISOU 1505 O LEU B1825 8613 8036 10943 -852 530 1214 O ATOM 1506 CB LEU B1825 -32.128 25.986 -55.010 1.00 79.12 C ANISOU 1506 CB LEU B1825 10153 8513 11393 -1049 228 1711 C ATOM 1507 CG LEU B1825 -33.427 26.580 -55.561 1.00 81.29 C ANISOU 1507 CG LEU B1825 10626 8501 11757 -999 -157 1901 C ATOM 1508 CD1 LEU B1825 -34.008 25.710 -56.667 1.00 81.44 C ANISOU 1508 CD1 LEU B1825 10902 8594 11445 -989 -309 1987 C ATOM 1509 CD2 LEU B1825 -34.456 26.767 -54.456 1.00 80.36 C ANISOU 1509 CD2 LEU B1825 10227 8234 12069 -799 -343 1740 C ATOM 1510 N ARG B1826 -29.217 25.897 -53.397 1.00 73.50 N ANISOU 1510 N ARG B1826 8853 8242 10831 -1180 868 1329 N ATOM 1511 CA ARG B1826 -28.202 25.071 -52.743 1.00 71.93 C ANISOU 1511 CA ARG B1826 8363 8312 10654 -1105 1050 1123 C ATOM 1512 C ARG B1826 -28.280 25.208 -51.222 1.00 69.59 C ANISOU 1512 C ARG B1826 7794 8054 10590 -988 937 973 C ATOM 1513 O ARG B1826 -28.582 26.264 -50.697 1.00 71.06 O ANISOU 1513 O ARG B1826 7950 8092 10957 -1068 859 969 O ATOM 1514 CB ARG B1826 -26.791 25.476 -53.178 1.00 75.29 C ANISOU 1514 CB ARG B1826 8695 8849 11060 -1326 1345 1064 C ATOM 1515 CG ARG B1826 -25.678 24.609 -52.595 1.00 75.06 C ANISOU 1515 CG ARG B1826 8311 9087 11122 -1222 1492 838 C ATOM 1516 CD ARG B1826 -24.276 25.120 -52.898 1.00 77.41 C ANISOU 1516 CD ARG B1826 8417 9492 11502 -1454 1791 710 C ATOM 1517 NE ARG B1826 -23.254 24.358 -52.189 1.00 77.37 N ANISOU 1517 NE ARG B1826 7992 9723 11679 -1306 1841 477 N ATOM 1518 CZ ARG B1826 -22.041 24.806 -51.877 1.00 79.49 C ANISOU 1518 CZ ARG B1826 7920 10124 12158 -1437 1992 286 C ATOM 1519 NH1 ARG B1826 -21.646 25.999 -52.285 1.00 81.10 N ANISOU 1519 NH1 ARG B1826 8179 10241 12393 -1759 2187 289 N ATOM 1520 NH2 ARG B1826 -21.230 24.063 -51.144 1.00 79.80 N ANISOU 1520 NH2 ARG B1826 7560 10364 12396 -1245 1929 93 N ATOM 1521 N ILE B1827 -27.982 24.100 -50.541 1.00 68.47 N ANISOU 1521 N ILE B1827 7481 8103 10429 -811 936 849 N ATOM 1522 CA ILE B1827 -27.789 24.041 -49.106 1.00 66.62 C ANISOU 1522 CA ILE B1827 7024 7970 10317 -731 842 709 C ATOM 1523 C ILE B1827 -26.466 23.320 -48.867 1.00 67.27 C ANISOU 1523 C ILE B1827 6861 8294 10405 -663 928 604 C ATOM 1524 O ILE B1827 -26.416 22.099 -48.892 1.00 65.95 O ANISOU 1524 O ILE B1827 6691 8200 10167 -476 917 599 O ATOM 1525 CB ILE B1827 -28.960 23.315 -48.424 1.00 64.89 C ANISOU 1525 CB ILE B1827 6899 7690 10064 -566 690 697 C ATOM 1526 CG1 ILE B1827 -30.305 23.851 -48.925 1.00 65.28 C ANISOU 1526 CG1 ILE B1827 7143 7493 10168 -598 600 777 C ATOM 1527 CG2 ILE B1827 -28.832 23.395 -46.911 1.00 64.67 C ANISOU 1527 CG2 ILE B1827 6724 7753 10093 -553 601 563 C ATOM 1528 CD1 ILE B1827 -31.485 22.980 -48.596 1.00 63.84 C ANISOU 1528 CD1 ILE B1827 7048 7247 9961 -458 509 738 C ATOM 1529 N ALA B1828 -25.405 24.105 -48.672 1.00 68.36 N ANISOU 1529 N ALA B1828 6776 8527 10669 -817 1013 505 N ATOM 1530 CA ALA B1828 -24.053 23.595 -48.560 1.00 69.64 C ANISOU 1530 CA ALA B1828 6628 8907 10923 -771 1091 368 C ATOM 1531 C ALA B1828 -23.903 22.746 -47.292 1.00 67.93 C ANISOU 1531 C ALA B1828 6254 8831 10724 -543 845 309 C ATOM 1532 O ALA B1828 -24.542 23.019 -46.285 1.00 65.96 O ANISOU 1532 O ALA B1828 6082 8555 10424 -544 665 314 O ATOM 1533 CB ALA B1828 -23.080 24.752 -48.558 1.00 72.47 C ANISOU 1533 CB ALA B1828 6770 9321 11444 -1025 1226 245 C ATOM 1534 N LYS B1829 -23.019 21.744 -47.358 1.00 69.39 N ANISOU 1534 N LYS B1829 6225 9148 10989 -364 847 245 N ATOM 1535 CA LYS B1829 -22.676 20.908 -46.211 1.00 70.73 C ANISOU 1535 CA LYS B1829 6248 9437 11188 -134 568 226 C ATOM 1536 C LYS B1829 -21.904 21.746 -45.201 1.00 72.90 C ANISOU 1536 C LYS B1829 6250 9883 11566 -254 397 93 C ATOM 1537 O LYS B1829 -21.138 22.609 -45.621 1.00 74.91 O ANISOU 1537 O LYS B1829 6277 10201 11982 -453 563 -43 O ATOM 1538 CB LYS B1829 -21.800 19.731 -46.640 1.00 73.39 C ANISOU 1538 CB LYS B1829 6367 9831 11687 97 608 173 C ATOM 1539 CG LYS B1829 -22.385 18.843 -47.729 1.00 73.51 C ANISOU 1539 CG LYS B1829 6616 9694 11619 189 821 243 C ATOM 1540 CD LYS B1829 -21.704 17.483 -47.847 1.00 76.84 C ANISOU 1540 CD LYS B1829 6851 10116 12226 478 812 187 C ATOM 1541 CE LYS B1829 -22.384 16.574 -48.851 1.00 76.57 C ANISOU 1541 CE LYS B1829 7081 9923 12089 543 1032 226 C ATOM 1542 NZ LYS B1829 -22.090 15.143 -48.598 1.00 79.03 N ANISOU 1542 NZ LYS B1829 7311 10152 12562 869 942 221 N ATOM 1543 N PRO B1830 -22.092 21.505 -43.891 1.00 73.95 N ANISOU 1543 N PRO B1830 6424 10092 11581 -172 85 119 N ATOM 1544 CA PRO B1830 -23.008 20.537 -43.298 1.00 72.48 C ANISOU 1544 CA PRO B1830 6548 9814 11176 4 -77 277 C ATOM 1545 C PRO B1830 -24.480 20.984 -43.292 1.00 68.62 C ANISOU 1545 C PRO B1830 6419 9141 10510 -138 37 337 C ATOM 1546 O PRO B1830 -24.777 22.070 -42.810 1.00 70.13 O ANISOU 1546 O PRO B1830 6626 9333 10686 -358 46 246 O ATOM 1547 CB PRO B1830 -22.574 20.380 -41.825 1.00 74.97 C ANISOU 1547 CB PRO B1830 6803 10296 11384 45 -445 264 C ATOM 1548 CG PRO B1830 -21.249 21.098 -41.704 1.00 77.89 C ANISOU 1548 CG PRO B1830 6731 10880 11981 -47 -525 76 C ATOM 1549 CD PRO B1830 -21.187 22.057 -42.872 1.00 77.07 C ANISOU 1549 CD PRO B1830 6529 10702 12051 -258 -146 -28 C ATOM 1550 N ASN B1831 -25.379 20.130 -43.795 1.00 65.79 N ANISOU 1550 N ASN B1831 6315 8620 10061 -11 121 455 N ATOM 1551 CA ASN B1831 -26.784 20.487 -44.048 1.00 62.56 C ANISOU 1551 CA ASN B1831 6177 8021 9571 -121 240 483 C ATOM 1552 C ASN B1831 -27.741 19.408 -43.518 1.00 62.56 C ANISOU 1552 C ASN B1831 6448 7917 9403 -3 185 559 C ATOM 1553 O ASN B1831 -28.946 19.429 -43.822 1.00 62.34 O ANISOU 1553 O ASN B1831 6611 7724 9350 -55 289 558 O ATOM 1554 CB ASN B1831 -27.024 20.691 -45.545 1.00 60.70 C ANISOU 1554 CB ASN B1831 5981 7668 9413 -151 446 524 C ATOM 1555 CG ASN B1831 -26.675 19.459 -46.350 1.00 60.09 C ANISOU 1555 CG ASN B1831 5911 7592 9328 39 523 578 C ATOM 1556 OD1 ASN B1831 -26.372 18.423 -45.777 1.00 59.90 O ANISOU 1556 OD1 ASN B1831 5868 7606 9284 227 413 603 O ATOM 1557 ND2 ASN B1831 -26.715 19.552 -47.667 1.00 59.75 N ANISOU 1557 ND2 ASN B1831 5919 7489 9294 -18 709 595 N ATOM 1558 N GLN B1832 -27.223 18.476 -42.717 1.00 63.31 N ANISOU 1558 N GLN B1832 6562 8091 9401 146 11 622 N ATOM 1559 CA GLN B1832 -28.025 17.383 -42.219 1.00 63.81 C ANISOU 1559 CA GLN B1832 6920 8029 9293 237 -15 714 C ATOM 1560 C GLN B1832 -29.208 17.955 -41.424 1.00 61.96 C ANISOU 1560 C GLN B1832 6898 7724 8918 10 45 627 C ATOM 1561 O GLN B1832 -30.371 17.689 -41.741 1.00 60.31 O ANISOU 1561 O GLN B1832 6863 7344 8705 -25 203 602 O ATOM 1562 CB GLN B1832 -27.167 16.441 -41.369 1.00 68.80 C ANISOU 1562 CB GLN B1832 7563 8737 9839 421 -272 833 C ATOM 1563 CG GLN B1832 -27.510 14.961 -41.528 1.00 70.49 C ANISOU 1563 CG GLN B1832 8002 8765 10012 632 -254 975 C ATOM 1564 CD GLN B1832 -26.567 14.222 -42.452 1.00 72.31 C ANISOU 1564 CD GLN B1832 8003 8975 10497 893 -243 1002 C ATOM 1565 OE1 GLN B1832 -25.430 13.914 -42.093 1.00 75.37 O ANISOU 1565 OE1 GLN B1832 8181 9451 11003 1070 -474 1046 O ATOM 1566 NE2 GLN B1832 -27.044 13.920 -43.652 1.00 70.32 N ANISOU 1566 NE2 GLN B1832 7773 8602 10341 912 21 951 N ATOM 1567 N ILE B1833 -28.902 18.785 -40.423 1.00 61.80 N ANISOU 1567 N ILE B1833 6829 7838 8813 -161 -60 534 N ATOM 1568 CA ILE B1833 -29.908 19.247 -39.478 1.00 61.96 C ANISOU 1568 CA ILE B1833 7049 7803 8689 -400 24 402 C ATOM 1569 C ILE B1833 -30.957 20.068 -40.239 1.00 60.43 C ANISOU 1569 C ILE B1833 6799 7432 8728 -506 249 268 C ATOM 1570 O ILE B1833 -32.128 19.925 -39.986 1.00 60.17 O ANISOU 1570 O ILE B1833 6928 7252 8680 -600 391 175 O ATOM 1571 CB ILE B1833 -29.288 20.035 -38.309 1.00 63.64 C ANISOU 1571 CB ILE B1833 7210 8212 8758 -595 -123 289 C ATOM 1572 CG1 ILE B1833 -28.071 19.327 -37.705 1.00 67.42 C ANISOU 1572 CG1 ILE B1833 7670 8883 9063 -450 -450 441 C ATOM 1573 CG2 ILE B1833 -30.330 20.330 -37.249 1.00 63.69 C ANISOU 1573 CG2 ILE B1833 7469 8160 8569 -870 12 120 C ATOM 1574 CD1 ILE B1833 -26.735 19.871 -38.187 1.00 69.30 C ANISOU 1574 CD1 ILE B1833 7505 9295 9530 -365 -591 412 C ATOM 1575 N SER B1834 -30.511 20.892 -41.195 1.00 61.42 N ANISOU 1575 N SER B1834 6695 7558 9081 -491 270 263 N ATOM 1576 CA SER B1834 -31.383 21.720 -42.055 1.00 60.25 C ANISOU 1576 CA SER B1834 6502 7216 9173 -557 402 198 C ATOM 1577 C SER B1834 -32.464 20.854 -42.714 1.00 57.85 C ANISOU 1577 C SER B1834 6349 6747 8884 -448 475 247 C ATOM 1578 O SER B1834 -33.643 21.188 -42.693 1.00 55.16 O ANISOU 1578 O SER B1834 6043 6235 8679 -529 557 124 O ATOM 1579 CB SER B1834 -30.591 22.446 -43.126 1.00 61.11 C ANISOU 1579 CB SER B1834 6432 7342 9443 -542 401 268 C ATOM 1580 OG SER B1834 -29.495 23.168 -42.583 1.00 65.35 O ANISOU 1580 OG SER B1834 6792 8043 9994 -650 346 198 O ATOM 1581 N LEU B1835 -32.022 19.753 -43.326 1.00 57.93 N ANISOU 1581 N LEU B1835 6413 6801 8795 -266 449 397 N ATOM 1582 CA LEU B1835 -32.873 18.900 -44.149 1.00 56.51 C ANISOU 1582 CA LEU B1835 6357 6485 8630 -169 518 434 C ATOM 1583 C LEU B1835 -33.861 18.129 -43.261 1.00 55.91 C ANISOU 1583 C LEU B1835 6472 6315 8456 -216 593 351 C ATOM 1584 O LEU B1835 -35.059 18.116 -43.513 1.00 55.39 O ANISOU 1584 O LEU B1835 6444 6096 8506 -272 679 240 O ATOM 1585 CB LEU B1835 -31.972 17.957 -44.949 1.00 56.57 C ANISOU 1585 CB LEU B1835 6355 6566 8571 10 510 570 C ATOM 1586 CG LEU B1835 -31.113 18.629 -46.017 1.00 56.50 C ANISOU 1586 CG LEU B1835 6188 6631 8648 5 522 618 C ATOM 1587 CD1 LEU B1835 -29.993 17.712 -46.458 1.00 57.63 C ANISOU 1587 CD1 LEU B1835 6259 6875 8761 163 551 679 C ATOM 1588 CD2 LEU B1835 -31.948 19.044 -47.214 1.00 55.64 C ANISOU 1588 CD2 LEU B1835 6148 6391 8599 -52 560 631 C ATOM 1589 N ILE B1836 -33.334 17.495 -42.212 1.00 56.79 N ANISOU 1589 N ILE B1836 6707 6513 8357 -206 549 404 N ATOM 1590 CA ILE B1836 -34.134 16.862 -41.169 1.00 56.96 C ANISOU 1590 CA ILE B1836 6976 6452 8213 -320 646 338 C ATOM 1591 C ILE B1836 -35.286 17.791 -40.767 1.00 55.60 C ANISOU 1591 C ILE B1836 6762 6183 8181 -552 797 83 C ATOM 1592 O ILE B1836 -36.417 17.369 -40.658 1.00 55.84 O ANISOU 1592 O ILE B1836 6894 6064 8259 -639 965 -48 O ATOM 1593 CB ILE B1836 -33.239 16.517 -39.959 1.00 59.79 C ANISOU 1593 CB ILE B1836 7480 6949 8289 -335 501 447 C ATOM 1594 CG1 ILE B1836 -32.445 15.232 -40.201 1.00 60.38 C ANISOU 1594 CG1 ILE B1836 7647 7017 8277 -81 373 679 C ATOM 1595 CG2 ILE B1836 -34.051 16.450 -38.671 1.00 61.77 C ANISOU 1595 CG2 ILE B1836 8001 7150 8315 -593 629 323 C ATOM 1596 CD1 ILE B1836 -31.617 14.785 -39.018 1.00 63.35 C ANISOU 1596 CD1 ILE B1836 8192 7493 8385 -58 148 831 C ATOM 1597 N ASN B1837 -34.967 19.066 -40.539 1.00 55.32 N ANISOU 1597 N ASN B1837 6548 6216 8254 -658 754 -13 N ATOM 1598 CA ASN B1837 -35.873 19.998 -39.908 1.00 55.45 C ANISOU 1598 CA ASN B1837 6509 6135 8424 -886 905 -288 C ATOM 1599 C ASN B1837 -36.881 20.537 -40.932 1.00 55.43 C ANISOU 1599 C ASN B1837 6318 5927 8815 -839 947 -395 C ATOM 1600 O ASN B1837 -37.902 21.072 -40.546 1.00 56.38 O ANISOU 1600 O ASN B1837 6359 5899 9161 -984 1094 -658 O ATOM 1601 CB ASN B1837 -35.088 21.044 -39.123 1.00 55.62 C ANISOU 1601 CB ASN B1837 6444 6298 8389 -1034 847 -369 C ATOM 1602 CG ASN B1837 -34.667 20.482 -37.783 1.00 57.44 C ANISOU 1602 CG ASN B1837 6928 6687 8208 -1174 830 -361 C ATOM 1603 OD1 ASN B1837 -35.510 20.216 -36.939 1.00 59.59 O ANISOU 1603 OD1 ASN B1837 7401 6892 8348 -1379 1024 -529 O ATOM 1604 ND2 ASN B1837 -33.387 20.236 -37.586 1.00 58.07 N ANISOU 1604 ND2 ASN B1837 7016 6970 8077 -1075 593 -166 N ATOM 1605 N MET B1838 -36.629 20.320 -42.224 1.00 55.39 N ANISOU 1605 N MET B1838 7461 6201 7384 269 -554 240 N ATOM 1606 CA MET B1838 -37.624 20.552 -43.257 1.00 56.00 C ANISOU 1606 CA MET B1838 7335 6470 7470 247 -336 260 C ATOM 1607 C MET B1838 -38.796 19.571 -43.123 1.00 56.96 C ANISOU 1607 C MET B1838 7494 6633 7514 235 -150 257 C ATOM 1608 O MET B1838 -39.841 19.769 -43.751 1.00 54.68 O ANISOU 1608 O MET B1838 7062 6451 7262 219 -8 281 O ATOM 1609 CB MET B1838 -37.023 20.346 -44.644 1.00 57.24 C ANISOU 1609 CB MET B1838 7226 6746 7776 195 -332 250 C ATOM 1610 CG MET B1838 -35.994 21.361 -45.020 1.00 58.22 C ANISOU 1610 CG MET B1838 7257 6828 8036 193 -426 253 C ATOM 1611 SD MET B1838 -35.516 21.070 -46.731 1.00 60.96 S ANISOU 1611 SD MET B1838 7390 7263 8508 118 -287 240 S ATOM 1612 CE MET B1838 -34.319 22.389 -46.920 1.00 62.07 C ANISOU 1612 CE MET B1838 7440 7292 8849 120 -346 241 C ATOM 1613 N ASP B1839 -38.579 18.474 -42.383 1.00 59.33 N ANISOU 1613 N ASP B1839 7966 6828 7747 236 -178 229 N ATOM 1614 CA ASP B1839 -39.619 17.498 -42.045 1.00 58.91 C ANISOU 1614 CA ASP B1839 7995 6761 7625 222 18 220 C ATOM 1615 C ASP B1839 -40.213 16.926 -43.328 1.00 55.76 C ANISOU 1615 C ASP B1839 7296 6549 7340 161 110 220 C ATOM 1616 O ASP B1839 -41.422 16.838 -43.466 1.00 53.87 O ANISOU 1616 O ASP B1839 6977 6340 7149 143 276 235 O ATOM 1617 CB ASP B1839 -40.726 18.128 -41.200 1.00 62.05 C ANISOU 1617 CB ASP B1839 8581 7047 7947 256 236 240 C ATOM 1618 CG ASP B1839 -41.630 17.101 -40.542 1.00 65.60 C ANISOU 1618 CG ASP B1839 9191 7388 8343 242 479 222 C ATOM 1619 OD1 ASP B1839 -41.139 15.999 -40.250 1.00 65.95 O ANISOU 1619 OD1 ASP B1839 9370 7380 8306 225 404 195 O ATOM 1620 OD2 ASP B1839 -42.821 17.416 -40.325 1.00 69.96 O ANISOU 1620 OD2 ASP B1839 9722 7883 8974 249 759 237 O ATOM 1621 N LEU B1840 -39.336 16.569 -44.268 1.00 54.30 N ANISOU 1621 N LEU B1840 6960 6447 7223 124 0 204 N ATOM 1622 CA LEU B1840 -39.767 16.040 -45.542 1.00 53.91 C ANISOU 1622 CA LEU B1840 6727 6531 7223 50 55 200 C ATOM 1623 C LEU B1840 -40.462 14.695 -45.328 1.00 54.72 C ANISOU 1623 C LEU B1840 6864 6623 7303 12 158 176 C ATOM 1624 O LEU B1840 -40.021 13.867 -44.536 1.00 53.51 O ANISOU 1624 O LEU B1840 6857 6373 7101 34 157 150 O ATOM 1625 CB LEU B1840 -38.556 15.885 -46.461 1.00 53.56 C ANISOU 1625 CB LEU B1840 6602 6505 7242 16 -7 177 C ATOM 1626 CG LEU B1840 -37.851 17.179 -46.862 1.00 53.08 C ANISOU 1626 CG LEU B1840 6484 6440 7241 34 -68 197 C ATOM 1627 CD1 LEU B1840 -36.525 16.861 -47.519 1.00 53.48 C ANISOU 1627 CD1 LEU B1840 6461 6430 7429 6 -56 164 C ATOM 1628 CD2 LEU B1840 -38.701 18.021 -47.805 1.00 53.00 C ANISOU 1628 CD2 LEU B1840 6419 6531 7188 0 -39 236 C ATOM 1629 N PRO B1841 -41.592 14.439 -46.020 1.00 55.68 N ANISOU 1629 N PRO B1841 6858 6819 7477 -49 224 189 N ATOM 1630 CA PRO B1841 -42.253 13.143 -45.942 1.00 55.27 C ANISOU 1630 CA PRO B1841 6808 6748 7440 -102 319 162 C ATOM 1631 C PRO B1841 -41.506 12.092 -46.770 1.00 54.70 C ANISOU 1631 C PRO B1841 6744 6718 7322 -167 273 122 C ATOM 1632 O PRO B1841 -41.076 12.380 -47.895 1.00 52.81 O ANISOU 1632 O PRO B1841 6455 6538 7070 -214 202 124 O ATOM 1633 CB PRO B1841 -43.633 13.440 -46.536 1.00 56.21 C ANISOU 1633 CB PRO B1841 6742 6904 7710 -153 333 197 C ATOM 1634 CG PRO B1841 -43.363 14.515 -47.555 1.00 55.79 C ANISOU 1634 CG PRO B1841 6614 6930 7650 -162 172 233 C ATOM 1635 CD PRO B1841 -42.292 15.376 -46.918 1.00 55.77 C ANISOU 1635 CD PRO B1841 6720 6904 7564 -75 168 233 C ATOM 1636 N MET B1842 -41.396 10.889 -46.200 1.00 56.07 N ANISOU 1636 N MET B1842 7014 6827 7462 -172 345 87 N ATOM 1637 CA MET B1842 -40.739 9.758 -46.833 1.00 57.67 C ANISOU 1637 CA MET B1842 7238 7033 7641 -225 347 46 C ATOM 1638 C MET B1842 -41.737 8.613 -47.019 1.00 58.67 C ANISOU 1638 C MET B1842 7357 7163 7770 -310 434 24 C ATOM 1639 O MET B1842 -42.424 8.219 -46.070 1.00 59.30 O ANISOU 1639 O MET B1842 7490 7173 7866 -292 540 23 O ATOM 1640 CB MET B1842 -39.580 9.246 -45.976 1.00 58.64 C ANISOU 1640 CB MET B1842 7479 7040 7759 -151 317 26 C ATOM 1641 CG MET B1842 -38.700 10.351 -45.454 1.00 59.50 C ANISOU 1641 CG MET B1842 7604 7093 7908 -65 189 50 C ATOM 1642 SD MET B1842 -37.140 9.727 -44.806 1.00 60.97 S ANISOU 1642 SD MET B1842 7857 7101 8206 4 43 34 S ATOM 1643 CE MET B1842 -37.531 9.647 -43.059 1.00 62.73 C ANISOU 1643 CE MET B1842 8404 7163 8265 72 -39 54 C ATOM 1644 N VAL B1843 -41.779 8.098 -48.254 1.00 59.35 N ANISOU 1644 N VAL B1843 7416 7297 7835 -412 405 4 N ATOM 1645 CA VAL B1843 -42.416 6.829 -48.606 1.00 60.05 C ANISOU 1645 CA VAL B1843 7527 7369 7917 -512 454 -29 C ATOM 1646 C VAL B1843 -41.499 5.679 -48.140 1.00 60.56 C ANISOU 1646 C VAL B1843 7715 7360 7934 -480 552 -73 C ATOM 1647 O VAL B1843 -40.605 5.891 -47.331 1.00 61.42 O ANISOU 1647 O VAL B1843 7873 7412 8051 -375 547 -67 O ATOM 1648 CB VAL B1843 -42.753 6.783 -50.113 1.00 59.83 C ANISOU 1648 CB VAL B1843 7514 7375 7841 -643 343 -32 C ATOM 1649 CG1 VAL B1843 -43.659 7.927 -50.522 1.00 59.56 C ANISOU 1649 CG1 VAL B1843 7363 7380 7887 -664 181 23 C ATOM 1650 CG2 VAL B1843 -41.520 6.755 -51.000 1.00 59.75 C ANISOU 1650 CG2 VAL B1843 7646 7342 7713 -661 382 -59 C ATOM 1651 N SER B1844 -41.747 4.449 -48.602 1.00 62.51 N ANISOU 1651 N SER B1844 8018 7582 8149 -572 612 -113 N ATOM 1652 CA SER B1844 -41.015 3.288 -48.112 1.00 63.04 C ANISOU 1652 CA SER B1844 8194 7560 8196 -538 709 -149 C ATOM 1653 C SER B1844 -39.706 3.122 -48.892 1.00 64.62 C ANISOU 1653 C SER B1844 8427 7717 8406 -530 739 -173 C ATOM 1654 O SER B1844 -39.594 3.530 -50.049 1.00 65.91 O ANISOU 1654 O SER B1844 8604 7909 8529 -602 742 -179 O ATOM 1655 CB SER B1844 -41.849 2.054 -48.188 1.00 63.32 C ANISOU 1655 CB SER B1844 8278 7567 8213 -635 791 -182 C ATOM 1656 OG SER B1844 -42.114 1.737 -49.540 1.00 65.47 O ANISOU 1656 OG SER B1844 8571 7868 8435 -770 754 -208 O ATOM 1657 N GLY B1845 -38.729 2.498 -48.230 1.00 66.09 N ANISOU 1657 N GLY B1845 8648 7791 8669 -442 772 -184 N ATOM 1658 CA GLY B1845 -37.369 2.415 -48.699 1.00 66.92 C ANISOU 1658 CA GLY B1845 8716 7796 8914 -401 827 -200 C ATOM 1659 C GLY B1845 -36.617 3.690 -48.379 1.00 69.02 C ANISOU 1659 C GLY B1845 8865 8047 9311 -307 714 -163 C ATOM 1660 O GLY B1845 -35.486 3.882 -48.856 1.00 73.19 O ANISOU 1660 O GLY B1845 9304 8473 10031 -278 778 -173 O ATOM 1661 N ASP B1846 -37.237 4.542 -47.546 1.00 66.98 N ANISOU 1661 N ASP B1846 8610 7859 8980 -263 576 -123 N ATOM 1662 CA ASP B1846 -36.763 5.881 -47.261 1.00 65.24 C ANISOU 1662 CA ASP B1846 8308 7642 8837 -194 454 -88 C ATOM 1663 C ASP B1846 -36.399 6.571 -48.575 1.00 64.35 C ANISOU 1663 C ASP B1846 8110 7571 8769 -253 547 -97 C ATOM 1664 O ASP B1846 -35.241 6.849 -48.821 1.00 66.10 O ANISOU 1664 O ASP B1846 8236 7684 9193 -214 579 -103 O ATOM 1665 CB ASP B1846 -35.568 5.855 -46.309 1.00 66.66 C ANISOU 1665 CB ASP B1846 8470 7647 9208 -79 297 -73 C ATOM 1666 CG ASP B1846 -35.875 5.162 -44.999 1.00 68.00 C ANISOU 1666 CG ASP B1846 8839 7723 9275 -26 188 -60 C ATOM 1667 OD1 ASP B1846 -37.062 4.875 -44.763 1.00 69.18 O ANISOU 1667 OD1 ASP B1846 9111 7951 9223 -74 288 -64 O ATOM 1668 OD2 ASP B1846 -34.927 4.912 -44.235 1.00 69.37 O ANISOU 1668 OD2 ASP B1846 9053 7711 9593 57 0 -44 O ATOM 1669 N ARG B1847 -37.408 6.792 -49.418 1.00 63.55 N ANISOU 1669 N ARG B1847 8060 7587 8497 -353 589 -96 N ATOM 1670 CA ARG B1847 -37.291 7.591 -50.636 1.00 63.41 C ANISOU 1670 CA ARG B1847 8064 7592 8434 -421 643 -94 C ATOM 1671 C ARG B1847 -38.139 8.861 -50.454 1.00 61.87 C ANISOU 1671 C ARG B1847 7824 7512 8170 -407 494 -42 C ATOM 1672 O ARG B1847 -39.053 8.878 -49.635 1.00 59.18 O ANISOU 1672 O ARG B1847 7448 7229 7806 -380 409 -19 O ATOM 1673 CB ARG B1847 -37.717 6.768 -51.855 1.00 64.24 C ANISOU 1673 CB ARG B1847 8344 7679 8384 -560 754 -130 C ATOM 1674 CG ARG B1847 -37.154 5.355 -51.871 1.00 65.91 C ANISOU 1674 CG ARG B1847 8611 7779 8652 -573 915 -182 C ATOM 1675 CD ARG B1847 -37.754 4.540 -52.993 1.00 67.43 C ANISOU 1675 CD ARG B1847 9034 7944 8642 -727 995 -219 C ATOM 1676 NE ARG B1847 -39.170 4.302 -52.768 1.00 68.36 N ANISOU 1676 NE ARG B1847 9152 8174 8647 -789 807 -201 N ATOM 1677 CZ ARG B1847 -40.088 4.291 -53.729 1.00 70.41 C ANISOU 1677 CZ ARG B1847 9570 8441 8739 -929 694 -200 C ATOM 1678 NH1 ARG B1847 -39.741 4.597 -54.971 1.00 73.29 N ANISOU 1678 NH1 ARG B1847 10187 8713 8947 -1021 750 -212 N ATOM 1679 NH2 ARG B1847 -41.341 3.979 -53.445 1.00 67.27 N ANISOU 1679 NH2 ARG B1847 9100 8106 8353 -983 524 -184 N ATOM 1680 N ILE B1848 -37.789 9.922 -51.195 1.00 61.91 N ANISOU 1680 N ILE B1848 7838 7515 8168 -422 501 -24 N ATOM 1681 CA ILE B1848 -38.408 11.247 -51.086 1.00 61.31 C ANISOU 1681 CA ILE B1848 7712 7523 8058 -396 367 28 C ATOM 1682 C ILE B1848 -38.707 11.750 -52.501 1.00 63.21 C ANISOU 1682 C ILE B1848 8100 7759 8156 -500 362 41 C ATOM 1683 O ILE B1848 -37.849 11.688 -53.367 1.00 66.56 O ANISOU 1683 O ILE B1848 8655 8081 8553 -548 521 12 O ATOM 1684 CB ILE B1848 -37.489 12.211 -50.311 1.00 60.55 C ANISOU 1684 CB ILE B1848 7510 7389 8107 -286 338 45 C ATOM 1685 CG1 ILE B1848 -37.116 11.647 -48.938 1.00 60.48 C ANISOU 1685 CG1 ILE B1848 7458 7323 8198 -196 282 35 C ATOM 1686 CG2 ILE B1848 -38.108 13.597 -50.192 1.00 61.42 C ANISOU 1686 CG2 ILE B1848 7586 7572 8176 -256 226 98 C ATOM 1687 CD1 ILE B1848 -36.222 12.552 -48.126 1.00 60.63 C ANISOU 1687 CD1 ILE B1848 7412 7262 8359 -103 172 53 C ATOM 1688 N HIS B1849 -39.932 12.234 -52.720 1.00 64.72 N ANISOU 1688 N HIS B1849 8290 8021 8278 -536 184 88 N ATOM 1689 CA HIS B1849 -40.395 12.642 -54.039 1.00 67.61 C ANISOU 1689 CA HIS B1849 8855 8350 8483 -645 79 113 C ATOM 1690 C HIS B1849 -39.756 13.974 -54.454 1.00 70.52 C ANISOU 1690 C HIS B1849 9285 8685 8823 -613 111 142 C ATOM 1691 O HIS B1849 -39.445 14.817 -53.616 1.00 68.87 O ANISOU 1691 O HIS B1849 8896 8525 8747 -504 116 163 O ATOM 1692 CB HIS B1849 -41.919 12.755 -54.059 1.00 68.34 C ANISOU 1692 CB HIS B1849 8864 8489 8611 -683 -180 164 C ATOM 1693 CG HIS B1849 -42.472 12.854 -55.437 1.00 70.78 C ANISOU 1693 CG HIS B1849 9432 8712 8747 -818 -384 190 C ATOM 1694 ND1 HIS B1849 -42.765 14.063 -56.027 1.00 73.13 N ANISOU 1694 ND1 HIS B1849 9812 8978 8994 -821 -565 255 N ATOM 1695 CD2 HIS B1849 -42.763 11.902 -56.348 1.00 72.94 C ANISOU 1695 CD2 HIS B1849 9960 8891 8861 -961 -463 163 C ATOM 1696 CE1 HIS B1849 -43.223 13.854 -57.244 1.00 76.02 C ANISOU 1696 CE1 HIS B1849 10494 9222 9166 -962 -777 271 C ATOM 1697 NE2 HIS B1849 -43.227 12.535 -57.467 1.00 76.16 N ANISOU 1697 NE2 HIS B1849 10634 9195 9106 -1055 -719 213 N ATOM 1698 N CYS B1850 -39.599 14.151 -55.770 1.00 74.19 N ANISOU 1698 N CYS B1850 10060 9039 9089 -720 132 143 N ATOM 1699 CA CYS B1850 -39.019 15.340 -56.374 1.00 77.13 C ANISOU 1699 CA CYS B1850 10575 9336 9395 -718 200 168 C ATOM 1700 C CYS B1850 -39.665 16.625 -55.834 1.00 77.30 C ANISOU 1700 C CYS B1850 10404 9460 9505 -630 -16 241 C ATOM 1701 O CYS B1850 -38.983 17.590 -55.497 1.00 73.72 O ANISOU 1701 O CYS B1850 9861 9006 9140 -554 78 251 O ATOM 1702 CB CYS B1850 -39.198 15.303 -57.886 1.00 80.63 C ANISOU 1702 CB CYS B1850 11486 9615 9533 -868 178 173 C ATOM 1703 SG CYS B1850 -38.484 16.743 -58.721 1.00 83.90 S ANISOU 1703 SG CYS B1850 12171 9884 9821 -881 316 203 S ATOM 1704 N MET B1851 -40.997 16.639 -55.787 1.00 80.02 N ANISOU 1704 N MET B1851 10679 9862 9863 -645 -302 293 N ATOM 1705 CA MET B1851 -41.734 17.856 -55.528 1.00 81.35 C ANISOU 1705 CA MET B1851 10705 10074 10127 -577 -502 370 C ATOM 1706 C MET B1851 -41.614 18.216 -54.047 1.00 76.91 C ANISOU 1706 C MET B1851 9819 9614 9787 -435 -400 367 C ATOM 1707 O MET B1851 -41.335 19.361 -53.713 1.00 77.69 O ANISOU 1707 O MET B1851 9857 9724 9935 -357 -382 397 O ATOM 1708 CB MET B1851 -43.203 17.703 -55.929 1.00 87.02 C ANISOU 1708 CB MET B1851 11397 10769 10898 -636 -841 429 C ATOM 1709 CG MET B1851 -43.388 17.405 -57.416 1.00 93.53 C ANISOU 1709 CG MET B1851 12638 11443 11454 -792 -1035 441 C ATOM 1710 SD MET B1851 -42.638 18.638 -58.532 1.00 99.76 S ANISOU 1710 SD MET B1851 13854 12094 11956 -828 -1005 476 S ATOM 1711 CE MET B1851 -43.559 20.102 -58.058 1.00 99.42 C ANISOU 1711 CE MET B1851 13519 12104 12151 -709 -1286 583 C ATOM 1712 N ASP B1852 -41.792 17.224 -53.172 1.00 73.50 N ANISOU 1712 N ASP B1852 9239 9228 9459 -410 -327 328 N ATOM 1713 CA ASP B1852 -41.579 17.405 -51.736 1.00 70.94 C ANISOU 1713 CA ASP B1852 8734 8944 9274 -292 -218 316 C ATOM 1714 C ASP B1852 -40.281 18.187 -51.483 1.00 68.20 C ANISOU 1714 C ASP B1852 8418 8573 8919 -232 -115 300 C ATOM 1715 O ASP B1852 -40.218 19.012 -50.579 1.00 69.24 O ANISOU 1715 O ASP B1852 8468 8710 9128 -142 -117 319 O ATOM 1716 CB ASP B1852 -41.505 16.062 -51.010 1.00 71.36 C ANISOU 1716 CB ASP B1852 8753 9000 9360 -293 -114 261 C ATOM 1717 CG ASP B1852 -42.838 15.352 -50.908 1.00 72.76 C ANISOU 1717 CG ASP B1852 8837 9182 9626 -337 -179 274 C ATOM 1718 OD1 ASP B1852 -43.830 16.053 -50.676 1.00 71.35 O ANISOU 1718 OD1 ASP B1852 8522 8994 9592 -304 -254 327 O ATOM 1719 OD2 ASP B1852 -42.864 14.100 -51.057 1.00 74.97 O ANISOU 1719 OD2 ASP B1852 9164 9451 9870 -403 -139 230 O ATOM 1720 N ILE B1853 -39.237 17.890 -52.265 1.00 64.72 N ANISOU 1720 N ILE B1853 8103 8073 8415 -289 -5 261 N ATOM 1721 CA ILE B1853 -37.936 18.511 -52.098 1.00 62.56 C ANISOU 1721 CA ILE B1853 7807 7732 8230 -247 109 240 C ATOM 1722 C ILE B1853 -38.006 19.952 -52.628 1.00 62.62 C ANISOU 1722 C ILE B1853 7873 7727 8190 -242 67 289 C ATOM 1723 O ILE B1853 -37.686 20.893 -51.906 1.00 59.49 O ANISOU 1723 O ILE B1853 7379 7332 7893 -165 41 306 O ATOM 1724 CB ILE B1853 -36.838 17.654 -52.764 1.00 60.87 C ANISOU 1724 CB ILE B1853 7672 7405 8050 -310 313 179 C ATOM 1725 CG1 ILE B1853 -36.621 16.353 -51.995 1.00 60.38 C ANISOU 1725 CG1 ILE B1853 7517 7340 8085 -284 335 136 C ATOM 1726 CG2 ILE B1853 -35.534 18.416 -52.909 1.00 61.54 C ANISOU 1726 CG2 ILE B1853 7712 7367 8302 -290 462 162 C ATOM 1727 CD1 ILE B1853 -35.995 15.259 -52.823 1.00 61.61 C ANISOU 1727 CD1 ILE B1853 7777 7389 8243 -363 539 82 C ATOM 1728 N LEU B1854 -38.476 20.103 -53.870 1.00 64.30 N ANISOU 1728 N LEU B1854 8289 7909 8233 -330 31 317 N ATOM 1729 CA LEU B1854 -38.528 21.378 -54.548 1.00 66.65 C ANISOU 1729 CA LEU B1854 8715 8160 8446 -339 -11 368 C ATOM 1730 C LEU B1854 -39.274 22.411 -53.695 1.00 69.52 C ANISOU 1730 C LEU B1854 8895 8607 8909 -237 -175 427 C ATOM 1731 O LEU B1854 -38.809 23.558 -53.568 1.00 70.93 O ANISOU 1731 O LEU B1854 9066 8759 9125 -191 -141 447 O ATOM 1732 CB LEU B1854 -39.210 21.190 -55.904 1.00 67.56 C ANISOU 1732 CB LEU B1854 9140 8204 8326 -455 -126 399 C ATOM 1733 CG LEU B1854 -39.267 22.435 -56.785 1.00 68.80 C ANISOU 1733 CG LEU B1854 9536 8267 8338 -481 -192 458 C ATOM 1734 CD1 LEU B1854 -37.935 23.168 -56.795 1.00 69.37 C ANISOU 1734 CD1 LEU B1854 9633 8253 8471 -461 100 425 C ATOM 1735 CD2 LEU B1854 -39.677 22.072 -58.201 1.00 71.36 C ANISOU 1735 CD2 LEU B1854 10300 8445 8368 -621 -299 478 C ATOM 1736 N PHE B1855 -40.408 22.001 -53.108 1.00 71.59 N ANISOU 1736 N PHE B1855 9016 8942 9241 -205 -313 452 N ATOM 1737 CA PHE B1855 -41.252 22.895 -52.302 1.00 73.57 C ANISOU 1737 CA PHE B1855 9101 9225 9624 -109 -403 507 C ATOM 1738 C PHE B1855 -40.461 23.408 -51.090 1.00 70.85 C ANISOU 1738 C PHE B1855 8681 8880 9356 -18 -278 477 C ATOM 1739 O PHE B1855 -40.383 24.610 -50.877 1.00 70.58 O ANISOU 1739 O PHE B1855 8642 8826 9349 36 -290 511 O ATOM 1740 CB PHE B1855 -42.552 22.204 -51.866 1.00 77.58 C ANISOU 1740 CB PHE B1855 9454 9756 10266 -101 -486 527 C ATOM 1741 CG PHE B1855 -43.334 22.946 -50.806 1.00 82.59 C ANISOU 1741 CG PHE B1855 9911 10374 11092 5 -454 566 C ATOM 1742 CD1 PHE B1855 -44.018 24.118 -51.110 1.00 87.32 C ANISOU 1742 CD1 PHE B1855 10451 10932 11795 47 -570 643 C ATOM 1743 CD2 PHE B1855 -43.364 22.493 -49.492 1.00 84.34 C ANISOU 1743 CD2 PHE B1855 10074 10585 11384 63 -284 526 C ATOM 1744 CE1 PHE B1855 -44.718 24.810 -50.129 1.00 88.67 C ANISOU 1744 CE1 PHE B1855 10470 11051 12169 148 -475 675 C ATOM 1745 CE2 PHE B1855 -44.068 23.182 -48.513 1.00 85.91 C ANISOU 1745 CE2 PHE B1855 10188 10716 11736 153 -179 555 C ATOM 1746 CZ PHE B1855 -44.744 24.341 -48.834 1.00 88.66 C ANISOU 1746 CZ PHE B1855 10442 11023 12220 197 -253 627 C ATOM 1747 N ALA B1856 -39.888 22.483 -50.309 1.00 68.75 N ANISOU 1747 N ALA B1856 8387 8614 9120 -8 -193 417 N ATOM 1748 CA ALA B1856 -39.202 22.808 -49.048 1.00 66.87 C ANISOU 1748 CA ALA B1856 8134 8329 8943 67 -158 391 C ATOM 1749 C ALA B1856 -37.945 23.635 -49.324 1.00 63.94 C ANISOU 1749 C ALA B1856 7784 7897 8613 63 -143 377 C ATOM 1750 O ALA B1856 -37.540 24.442 -48.488 1.00 62.52 O ANISOU 1750 O ALA B1856 7609 7660 8484 120 -182 379 O ATOM 1751 CB ALA B1856 -38.847 21.542 -48.303 1.00 67.55 C ANISOU 1751 CB ALA B1856 8228 8390 9045 67 -128 338 C ATOM 1752 N PHE B1857 -37.346 23.394 -50.495 1.00 62.03 N ANISOU 1752 N PHE B1857 7580 7633 8356 -12 -67 361 N ATOM 1753 CA PHE B1857 -36.087 23.982 -50.904 1.00 62.75 C ANISOU 1753 CA PHE B1857 7670 7620 8551 -35 27 338 C ATOM 1754 C PHE B1857 -36.312 25.444 -51.315 1.00 63.98 C ANISOU 1754 C PHE B1857 7889 7769 8651 -23 9 389 C ATOM 1755 O PHE B1857 -35.497 26.310 -50.987 1.00 65.00 O ANISOU 1755 O PHE B1857 7972 7820 8905 -1 28 381 O ATOM 1756 CB PHE B1857 -35.450 23.134 -52.011 1.00 63.42 C ANISOU 1756 CB PHE B1857 7824 7632 8638 -127 208 297 C ATOM 1757 CG PHE B1857 -34.599 21.979 -51.531 1.00 63.16 C ANISOU 1757 CG PHE B1857 7675 7531 8791 -124 269 237 C ATOM 1758 CD1 PHE B1857 -34.858 21.335 -50.326 1.00 62.42 C ANISOU 1758 CD1 PHE B1857 7500 7484 8733 -62 118 228 C ATOM 1759 CD2 PHE B1857 -33.530 21.528 -52.291 1.00 63.99 C ANISOU 1759 CD2 PHE B1857 7774 7485 9052 -184 502 190 C ATOM 1760 CE1 PHE B1857 -34.060 20.288 -49.888 1.00 61.82 C ANISOU 1760 CE1 PHE B1857 7334 7318 8835 -54 131 183 C ATOM 1761 CE2 PHE B1857 -32.732 20.480 -51.851 1.00 63.90 C ANISOU 1761 CE2 PHE B1857 7619 7381 9279 -170 548 142 C ATOM 1762 CZ PHE B1857 -32.995 19.866 -50.649 1.00 62.68 C ANISOU 1762 CZ PHE B1857 7378 7287 9149 -103 329 142 C ATOM 1763 N THR B1858 -37.426 25.703 -52.009 1.00 63.38 N ANISOU 1763 N THR B1858 7912 7753 8416 -40 -59 445 N ATOM 1764 CA THR B1858 -37.812 27.041 -52.414 1.00 63.02 C ANISOU 1764 CA THR B1858 7939 7691 8312 -20 -114 508 C ATOM 1765 C THR B1858 -38.413 27.793 -51.220 1.00 62.19 C ANISOU 1765 C THR B1858 7716 7624 8286 84 -205 540 C ATOM 1766 O THR B1858 -38.189 28.990 -51.038 1.00 62.55 O ANISOU 1766 O THR B1858 7779 7629 8357 123 -204 564 O ATOM 1767 CB THR B1858 -38.771 26.994 -53.606 1.00 63.74 C ANISOU 1767 CB THR B1858 8199 7782 8236 -78 -222 565 C ATOM 1768 OG1 THR B1858 -39.872 26.173 -53.239 1.00 65.43 O ANISOU 1768 OG1 THR B1858 8302 8072 8483 -62 -356 580 O ATOM 1769 CG2 THR B1858 -38.141 26.426 -54.856 1.00 65.25 C ANISOU 1769 CG2 THR B1858 8637 7874 8278 -195 -94 534 C ATOM 1770 N LYS B1859 -39.175 27.094 -50.388 1.00 62.02 N ANISOU 1770 N LYS B1859 7608 7654 8301 125 -244 536 N ATOM 1771 CA LYS B1859 -39.681 27.706 -49.188 1.00 64.03 C ANISOU 1771 CA LYS B1859 7820 7888 8618 217 -246 553 C ATOM 1772 C LYS B1859 -38.508 28.277 -48.384 1.00 64.32 C ANISOU 1772 C LYS B1859 7908 7848 8683 240 -230 512 C ATOM 1773 O LYS B1859 -38.589 29.386 -47.886 1.00 65.14 O ANISOU 1773 O LYS B1859 8055 7899 8794 292 -236 537 O ATOM 1774 CB LYS B1859 -40.474 26.700 -48.355 1.00 65.81 C ANISOU 1774 CB LYS B1859 7997 8126 8880 241 -211 538 C ATOM 1775 CG LYS B1859 -41.246 27.305 -47.196 1.00 68.06 C ANISOU 1775 CG LYS B1859 8296 8337 9224 329 -131 560 C ATOM 1776 CD LYS B1859 -41.863 26.266 -46.295 1.00 69.73 C ANISOU 1776 CD LYS B1859 8521 8511 9462 342 -23 532 C ATOM 1777 CE LYS B1859 -42.627 26.883 -45.144 1.00 72.90 C ANISOU 1777 CE LYS B1859 9005 8776 9917 422 148 549 C ATOM 1778 NZ LYS B1859 -42.719 25.951 -43.994 1.00 74.06 N ANISOU 1778 NZ LYS B1859 9320 8821 9997 427 287 500 N ATOM 1779 N ARG B1860 -37.408 27.523 -48.278 1.00 64.80 N ANISOU 1779 N ARG B1860 7956 7873 8791 198 -231 452 N ATOM 1780 CA ARG B1860 -36.269 27.954 -47.455 1.00 64.87 C ANISOU 1780 CA ARG B1860 7983 7764 8900 212 -298 416 C ATOM 1781 C ARG B1860 -35.744 29.297 -47.995 1.00 65.07 C ANISOU 1781 C ARG B1860 8004 7740 8979 200 -276 436 C ATOM 1782 O ARG B1860 -35.304 30.153 -47.223 1.00 65.49 O ANISOU 1782 O ARG B1860 8104 7698 9082 227 -357 431 O ATOM 1783 CB ARG B1860 -35.208 26.845 -47.353 1.00 64.54 C ANISOU 1783 CB ARG B1860 7869 7658 8994 172 -329 358 C ATOM 1784 CG ARG B1860 -33.850 27.160 -47.970 1.00 66.17 C ANISOU 1784 CG ARG B1860 7958 7753 9428 121 -289 329 C ATOM 1785 CD ARG B1860 -32.741 26.165 -47.617 1.00 66.67 C ANISOU 1785 CD ARG B1860 7899 7691 9740 102 -353 277 C ATOM 1786 NE ARG B1860 -32.473 26.043 -46.176 1.00 66.87 N ANISOU 1786 NE ARG B1860 7992 7607 9805 149 -619 267 N ATOM 1787 CZ ARG B1860 -31.273 26.247 -45.572 1.00 68.54 C ANISOU 1787 CZ ARG B1860 8119 7614 10310 144 -830 244 C ATOM 1788 NH1 ARG B1860 -30.176 26.416 -46.301 1.00 71.32 N ANISOU 1788 NH1 ARG B1860 8228 7846 11023 98 -742 221 N ATOM 1789 NH2 ARG B1860 -31.172 26.266 -44.242 1.00 67.11 N ANISOU 1789 NH2 ARG B1860 8114 7304 10080 179 -1128 244 N ATOM 1790 N VAL B1861 -35.831 29.490 -49.314 1.00 64.97 N ANISOU 1790 N VAL B1861 7987 7766 8929 151 -173 460 N ATOM 1791 CA VAL B1861 -35.298 30.676 -49.984 1.00 66.64 C ANISOU 1791 CA VAL B1861 8234 7908 9177 126 -106 478 C ATOM 1792 C VAL B1861 -36.322 31.825 -49.955 1.00 68.51 C ANISOU 1792 C VAL B1861 8551 8185 9295 186 -155 549 C ATOM 1793 O VAL B1861 -35.971 32.939 -49.559 1.00 69.44 O ANISOU 1793 O VAL B1861 8693 8232 9459 212 -169 556 O ATOM 1794 CB VAL B1861 -34.862 30.344 -51.423 1.00 66.35 C ANISOU 1794 CB VAL B1861 8257 7832 9118 36 63 469 C ATOM 1795 CG1 VAL B1861 -34.505 31.596 -52.211 1.00 66.79 C ANISOU 1795 CG1 VAL B1861 8424 7795 9159 6 170 497 C ATOM 1796 CG2 VAL B1861 -33.710 29.350 -51.439 1.00 66.25 C ANISOU 1796 CG2 VAL B1861 8131 7726 9311 -15 173 396 C ATOM 1797 N LEU B1862 -37.564 31.555 -50.386 1.00 69.75 N ANISOU 1797 N LEU B1862 8732 8428 9342 206 -195 602 N ATOM 1798 CA LEU B1862 -38.616 32.579 -50.544 1.00 70.68 C ANISOU 1798 CA LEU B1862 8882 8550 9421 267 -253 682 C ATOM 1799 C LEU B1862 -39.361 32.842 -49.233 1.00 72.17 C ANISOU 1799 C LEU B1862 9016 8729 9675 362 -257 693 C ATOM 1800 O LEU B1862 -39.996 33.879 -49.096 1.00 73.49 O ANISOU 1800 O LEU B1862 9194 8855 9873 427 -258 749 O ATOM 1801 CB LEU B1862 -39.614 32.127 -51.609 1.00 72.10 C ANISOU 1801 CB LEU B1862 9091 8770 9533 238 -348 740 C ATOM 1802 CG LEU B1862 -39.274 32.559 -53.029 1.00 75.21 C ANISOU 1802 CG LEU B1862 9687 9099 9790 163 -357 771 C ATOM 1803 CD1 LEU B1862 -37.825 32.250 -53.351 1.00 76.67 C ANISOU 1803 CD1 LEU B1862 9947 9224 9957 79 -165 693 C ATOM 1804 CD2 LEU B1862 -40.193 31.893 -54.035 1.00 77.58 C ANISOU 1804 CD2 LEU B1862 10086 9400 9990 112 -523 820 C ATOM 1805 N GLY B1863 -39.304 31.891 -48.298 1.00 85.39 N ANISOU 1805 N GLY B1863 10508 10653 11284 -386 -1395 -86 N ATOM 1806 CA GLY B1863 -40.059 31.967 -47.060 1.00 87.99 C ANISOU 1806 CA GLY B1863 11277 10732 11422 -244 -1381 -128 C ATOM 1807 C GLY B1863 -41.524 31.669 -47.307 1.00 89.44 C ANISOU 1807 C GLY B1863 11464 10868 11649 120 -1068 -200 C ATOM 1808 O GLY B1863 -41.923 31.371 -48.436 1.00 88.03 O ANISOU 1808 O GLY B1863 10963 10842 11642 245 -946 -213 O ATOM 1809 N GLU B1864 -42.327 31.779 -46.246 1.00 95.12 N ANISOU 1809 N GLU B1864 12567 11362 12213 275 -937 -243 N ATOM 1810 CA GLU B1864 -43.723 31.375 -46.271 1.00 99.14 C ANISOU 1810 CA GLU B1864 12988 11858 12823 602 -614 -303 C ATOM 1811 C GLU B1864 -44.580 32.543 -46.790 1.00102.79 C ANISOU 1811 C GLU B1864 13642 12172 13240 789 -479 -333 C ATOM 1812 O GLU B1864 -45.392 33.102 -46.049 1.00105.24 O ANISOU 1812 O GLU B1864 14318 12251 13417 989 -271 -371 O ATOM 1813 CB GLU B1864 -44.129 30.903 -44.870 1.00103.13 C ANISOU 1813 CB GLU B1864 13814 12186 13183 674 -466 -331 C ATOM 1814 CG GLU B1864 -45.028 29.680 -44.872 1.00104.37 C ANISOU 1814 CG GLU B1864 13637 12477 13539 849 -206 -365 C ATOM 1815 CD GLU B1864 -45.972 29.571 -46.060 1.00104.63 C ANISOU 1815 CD GLU B1864 13203 12693 13855 1032 -59 -386 C ATOM 1816 OE1 GLU B1864 -46.806 30.482 -46.233 1.00108.68 O ANISOU 1816 OE1 GLU B1864 13805 13104 14383 1225 93 -412 O ATOM 1817 OE2 GLU B1864 -45.859 28.585 -46.819 1.00102.70 O ANISOU 1817 OE2 GLU B1864 12546 12669 13803 997 -131 -373 O ATOM 1818 N SER B1865 -44.419 32.879 -48.079 1.00104.29 N ANISOU 1818 N SER B1865 13618 12474 13531 759 -579 -315 N ATOM 1819 CA SER B1865 -45.023 34.082 -48.683 1.00106.49 C ANISOU 1819 CA SER B1865 14163 12575 13723 919 -551 -333 C ATOM 1820 C SER B1865 -46.153 33.710 -49.659 1.00108.08 C ANISOU 1820 C SER B1865 13976 12903 14186 1224 -457 -363 C ATOM 1821 O SER B1865 -46.410 32.530 -49.912 1.00107.67 O ANISOU 1821 O SER B1865 13469 13072 14365 1251 -415 -366 O ATOM 1822 CB SER B1865 -43.964 34.934 -49.347 1.00106.25 C ANISOU 1822 CB SER B1865 14353 12488 13529 607 -769 -285 C ATOM 1823 OG SER B1865 -43.670 34.478 -50.659 1.00103.62 O ANISOU 1823 OG SER B1865 13637 12367 13364 536 -822 -263 O ATOM 1824 N GLY B1866 -46.822 34.745 -50.190 1.00113.05 N ANISOU 1824 N GLY B1866 14837 13357 14758 1450 -469 -381 N ATOM 1825 CA GLY B1866 -47.955 34.624 -51.119 1.00115.60 C ANISOU 1825 CA GLY B1866 14850 13748 15322 1768 -477 -403 C ATOM 1826 C GLY B1866 -47.504 34.533 -52.568 1.00117.46 C ANISOU 1826 C GLY B1866 14996 14060 15571 1622 -710 -372 C ATOM 1827 O GLY B1866 -48.134 33.852 -53.379 1.00119.90 O ANISOU 1827 O GLY B1866 14943 14506 16107 1742 -785 -375 O ATOM 1828 N GLU B1867 -46.420 35.248 -52.891 1.00118.24 N ANISOU 1828 N GLU B1867 15473 14042 15408 1334 -816 -339 N ATOM 1829 CA GLU B1867 -45.651 35.060 -54.129 1.00117.82 C ANISOU 1829 CA GLU B1867 15382 14064 15318 1089 -936 -302 C ATOM 1830 C GLU B1867 -45.232 33.583 -54.257 1.00114.45 C ANISOU 1830 C GLU B1867 14444 13936 15103 962 -884 -287 C ATOM 1831 O GLU B1867 -45.175 33.043 -55.365 1.00111.00 O ANISOU 1831 O GLU B1867 13871 13577 14726 938 -936 -275 O ATOM 1832 CB GLU B1867 -44.445 36.006 -54.103 1.00119.81 C ANISOU 1832 CB GLU B1867 16065 14175 15282 717 -973 -261 C ATOM 1833 CG GLU B1867 -43.396 35.738 -55.174 1.00120.84 C ANISOU 1833 CG GLU B1867 16109 14419 15385 385 -977 -214 C ATOM 1834 CD GLU B1867 -41.964 35.650 -54.659 1.00122.57 C ANISOU 1834 CD GLU B1867 16213 14777 15581 -47 -937 -161 C ATOM 1835 OE1 GLU B1867 -41.710 36.100 -53.519 1.00125.53 O ANISOU 1835 OE1 GLU B1867 16757 15072 15865 -157 -992 -154 O ATOM 1836 OE2 GLU B1867 -41.103 35.122 -55.394 1.00120.73 O ANISOU 1836 OE2 GLU B1867 15723 14723 15426 -264 -857 -122 O ATOM 1837 N MET B1868 -44.945 32.953 -53.108 1.00112.64 N ANISOU 1837 N MET B1868 14030 13824 14942 898 -789 -289 N ATOM 1838 CA MET B1868 -44.475 31.564 -52.991 1.00109.77 C ANISOU 1838 CA MET B1868 13268 13700 14736 804 -747 -276 C ATOM 1839 C MET B1868 -45.651 30.577 -53.088 1.00110.47 C ANISOU 1839 C MET B1868 13051 13878 15042 1040 -696 -309 C ATOM 1840 O MET B1868 -45.506 29.490 -53.670 1.00105.78 O ANISOU 1840 O MET B1868 12212 13426 14551 1002 -711 -299 O ATOM 1841 CB MET B1868 -43.754 31.365 -51.652 1.00107.77 C ANISOU 1841 CB MET B1868 13046 13474 14428 657 -728 -263 C ATOM 1842 CG MET B1868 -42.664 30.315 -51.695 1.00105.51 C ANISOU 1842 CG MET B1868 12459 13400 14230 490 -764 -227 C ATOM 1843 SD MET B1868 -43.277 28.648 -51.388 1.00101.18 S ANISOU 1843 SD MET B1868 11603 12985 13853 672 -679 -254 S ATOM 1844 CE MET B1868 -42.363 27.735 -52.628 1.00100.53 C ANISOU 1844 CE MET B1868 11244 13093 13858 611 -690 -220 C ATOM 1845 N ASP B1869 -46.793 30.946 -52.488 1.00112.77 N ANISOU 1845 N ASP B1869 13365 14079 15402 1271 -615 -345 N ATOM 1846 CA ASP B1869 -48.057 30.199 -52.605 1.00114.04 C ANISOU 1846 CA ASP B1869 13182 14329 15819 1466 -566 -369 C ATOM 1847 C ASP B1869 -48.454 30.079 -54.083 1.00117.49 C ANISOU 1847 C ASP B1869 13510 14783 16345 1518 -785 -357 C ATOM 1848 O ASP B1869 -48.920 29.021 -54.522 1.00113.72 O ANISOU 1848 O ASP B1869 12749 14422 16035 1500 -842 -353 O ATOM 1849 CB ASP B1869 -49.186 30.872 -51.818 1.00115.20 C ANISOU 1849 CB ASP B1869 13348 14372 16049 1740 -399 -403 C ATOM 1850 CG ASP B1869 -49.203 30.538 -50.337 1.00114.18 C ANISOU 1850 CG ASP B1869 13285 14221 15875 1713 -121 -422 C ATOM 1851 OD1 ASP B1869 -49.028 29.351 -50.006 1.00112.63 O ANISOU 1851 OD1 ASP B1869 12898 14152 15743 1562 -58 -416 O ATOM 1852 OD2 ASP B1869 -49.403 31.468 -49.527 1.00114.38 O ANISOU 1852 OD2 ASP B1869 13633 14061 15762 1853 32 -443 O ATOM 1853 N ALA B1870 -48.282 31.183 -54.824 1.00123.24 N ANISOU 1853 N ALA B1870 14553 15352 16920 1565 -927 -349 N ATOM 1854 CA ALA B1870 -48.507 31.239 -56.270 1.00126.37 C ANISOU 1854 CA ALA B1870 15031 15682 17301 1596 -1170 -334 C ATOM 1855 C ALA B1870 -47.525 30.303 -56.988 1.00128.14 C ANISOU 1855 C ALA B1870 15251 15998 17438 1341 -1166 -307 C ATOM 1856 O ALA B1870 -47.930 29.539 -57.863 1.00131.11 O ANISOU 1856 O ALA B1870 15540 16391 17884 1352 -1309 -300 O ATOM 1857 CB ALA B1870 -48.381 32.662 -56.764 1.00127.15 C ANISOU 1857 CB ALA B1870 15599 15535 17174 1670 -1285 -332 C ATOM 1858 N LEU B1871 -46.243 30.357 -56.597 1.00127.79 N ANISOU 1858 N LEU B1871 15300 16003 17249 1122 -1010 -288 N ATOM 1859 CA LEU B1871 -45.187 29.536 -57.215 1.00126.51 C ANISOU 1859 CA LEU B1871 15100 15941 17025 933 -935 -259 C ATOM 1860 C LEU B1871 -45.472 28.046 -56.967 1.00125.01 C ANISOU 1860 C LEU B1871 14600 15901 16997 974 -904 -267 C ATOM 1861 O LEU B1871 -45.292 27.218 -57.864 1.00124.26 O ANISOU 1861 O LEU B1871 14529 15813 16869 948 -922 -256 O ATOM 1862 CB LEU B1871 -43.816 29.939 -56.656 1.00126.93 C ANISOU 1862 CB LEU B1871 15189 16059 16979 708 -795 -230 C ATOM 1863 CG LEU B1871 -42.685 30.045 -57.682 1.00128.80 C ANISOU 1863 CG LEU B1871 15550 16299 17086 506 -691 -191 C ATOM 1864 CD1 LEU B1871 -41.335 30.141 -56.990 1.00130.17 C ANISOU 1864 CD1 LEU B1871 15550 16625 17282 273 -573 -151 C ATOM 1865 CD2 LEU B1871 -42.691 28.876 -58.657 1.00127.64 C ANISOU 1865 CD2 LEU B1871 15338 16196 16961 577 -640 -189 C ATOM 1866 N LYS B1872 -45.932 27.719 -55.753 1.00122.86 N ANISOU 1866 N LYS B1872 14123 15705 16854 1032 -841 -287 N ATOM 1867 CA LYS B1872 -46.296 26.351 -55.376 1.00121.11 C ANISOU 1867 CA LYS B1872 13677 15585 16755 1040 -800 -296 C ATOM 1868 C LYS B1872 -47.334 25.769 -56.351 1.00122.44 C ANISOU 1868 C LYS B1872 13781 15717 17022 1091 -964 -299 C ATOM 1869 O LYS B1872 -47.364 24.564 -56.558 1.00118.19 O ANISOU 1869 O LYS B1872 13191 15215 16500 1032 -974 -294 O ATOM 1870 CB LYS B1872 -46.835 26.316 -53.943 1.00120.50 C ANISOU 1870 CB LYS B1872 13484 15531 16767 1085 -674 -319 C ATOM 1871 CG LYS B1872 -47.379 24.964 -53.503 1.00121.02 C ANISOU 1871 CG LYS B1872 13377 15662 16940 1056 -608 -328 C ATOM 1872 CD LYS B1872 -47.751 24.909 -52.045 1.00123.44 C ANISOU 1872 CD LYS B1872 13672 15954 17272 1067 -413 -349 C ATOM 1873 CE LYS B1872 -47.708 23.503 -51.486 1.00124.02 C ANISOU 1873 CE LYS B1872 13734 16055 17331 970 -333 -350 C ATOM 1874 NZ LYS B1872 -47.886 23.486 -50.014 1.00125.39 N ANISOU 1874 NZ LYS B1872 14035 16160 17447 958 -123 -369 N ATOM 1875 N ILE B1873 -48.194 26.626 -56.918 1.00124.02 N ANISOU 1875 N ILE B1873 14019 15821 17279 1203 -1133 -304 N ATOM 1876 CA ILE B1873 -49.248 26.211 -57.851 1.00124.77 C ANISOU 1876 CA ILE B1873 14043 15867 17494 1244 -1397 -298 C ATOM 1877 C ILE B1873 -48.643 25.939 -59.235 1.00125.27 C ANISOU 1877 C ILE B1873 14461 15801 17332 1161 -1538 -276 C ATOM 1878 O ILE B1873 -48.837 24.861 -59.792 1.00127.95 O ANISOU 1878 O ILE B1873 14836 16118 17660 1077 -1644 -266 O ATOM 1879 CB ILE B1873 -50.359 27.276 -57.932 1.00127.56 C ANISOU 1879 CB ILE B1873 14300 16156 18009 1454 -1572 -307 C ATOM 1880 CG1 ILE B1873 -51.050 27.480 -56.580 1.00129.33 C ANISOU 1880 CG1 ILE B1873 14189 16490 18458 1572 -1348 -331 C ATOM 1881 CG2 ILE B1873 -51.357 26.932 -59.027 1.00129.27 C ANISOU 1881 CG2 ILE B1873 14452 16308 18355 1485 -1957 -289 C ATOM 1882 CD1 ILE B1873 -51.753 28.814 -56.437 1.00131.02 C ANISOU 1882 CD1 ILE B1873 14408 16614 18758 1858 -1395 -346 C ATOM 1883 N GLN B1874 -47.938 26.939 -59.777 1.00124.71 N ANISOU 1883 N GLN B1874 14716 15611 17055 1166 -1517 -269 N ATOM 1884 CA GLN B1874 -47.477 26.958 -61.172 1.00127.83 C ANISOU 1884 CA GLN B1874 15549 15821 17197 1104 -1611 -250 C ATOM 1885 C GLN B1874 -46.644 25.710 -61.482 1.00127.95 C ANISOU 1885 C GLN B1874 15632 15881 17101 993 -1426 -238 C ATOM 1886 O GLN B1874 -47.024 24.906 -62.339 1.00127.76 O ANISOU 1886 O GLN B1874 15812 15733 16997 973 -1593 -231 O ATOM 1887 CB GLN B1874 -46.659 28.222 -61.448 1.00130.37 C ANISOU 1887 CB GLN B1874 16201 16028 17302 1060 -1493 -241 C ATOM 1888 CG GLN B1874 -47.506 29.486 -61.527 1.00134.68 C ANISOU 1888 CG GLN B1874 16901 16415 17856 1218 -1736 -252 C ATOM 1889 CD GLN B1874 -46.707 30.764 -61.407 1.00136.37 C ANISOU 1889 CD GLN B1874 17432 16523 17859 1136 -1584 -245 C ATOM 1890 OE1 GLN B1874 -45.483 30.754 -61.289 1.00138.14 O ANISOU 1890 OE1 GLN B1874 17703 16819 17964 919 -1300 -227 O ATOM 1891 NE2 GLN B1874 -47.407 31.888 -61.433 1.00135.43 N ANISOU 1891 NE2 GLN B1874 17529 16223 17703 1311 -1786 -256 N ATOM 1892 N MET B1875 -45.516 25.564 -60.774 1.00129.01 N ANISOU 1892 N MET B1875 15619 16172 17227 938 -1111 -234 N ATOM 1893 CA MET B1875 -44.516 24.517 -61.051 1.00129.53 C ANISOU 1893 CA MET B1875 15739 16285 17191 908 -883 -221 C ATOM 1894 C MET B1875 -45.017 23.144 -60.579 1.00125.80 C ANISOU 1894 C MET B1875 15107 15871 16819 944 -943 -233 C ATOM 1895 O MET B1875 -44.479 22.115 -61.004 1.00122.42 O ANISOU 1895 O MET B1875 14839 15404 16270 970 -827 -226 O ATOM 1896 CB MET B1875 -43.172 24.836 -60.384 1.00131.58 C ANISOU 1896 CB MET B1875 15801 16718 17474 856 -593 -205 C ATOM 1897 CG MET B1875 -43.197 24.802 -58.860 1.00132.92 C ANISOU 1897 CG MET B1875 15608 17064 17832 867 -599 -215 C ATOM 1898 SD MET B1875 -41.739 25.602 -58.119 1.00137.16 S ANISOU 1898 SD MET B1875 15959 17757 18396 740 -421 -183 S ATOM 1899 CE MET B1875 -42.288 25.815 -56.426 1.00132.70 C ANISOU 1899 CE MET B1875 15212 17250 17958 756 -547 -204 C ATOM 1900 N GLU B1876 -46.041 23.143 -59.714 1.00121.93 N ANISOU 1900 N GLU B1876 14343 15451 16533 947 -1090 -249 N ATOM 1901 CA GLU B1876 -46.663 21.930 -59.184 1.00119.61 C ANISOU 1901 CA GLU B1876 13912 15195 16338 914 -1138 -257 C ATOM 1902 C GLU B1876 -47.499 21.240 -60.272 1.00122.87 C ANISOU 1902 C GLU B1876 14559 15437 16688 845 -1408 -247 C ATOM 1903 O GLU B1876 -47.854 20.074 -60.124 1.00128.46 O ANISOU 1903 O GLU B1876 15293 16119 17397 762 -1454 -245 O ATOM 1904 CB GLU B1876 -47.510 22.273 -57.955 1.00118.05 C ANISOU 1904 CB GLU B1876 13363 15114 16377 911 -1135 -274 C ATOM 1905 CG GLU B1876 -48.019 21.070 -57.175 1.00116.79 C ANISOU 1905 CG GLU B1876 13074 14998 16303 825 -1090 -281 C ATOM 1906 CD GLU B1876 -49.260 20.389 -57.729 1.00119.25 C ANISOU 1906 CD GLU B1876 13342 15243 16722 697 -1326 -271 C ATOM 1907 OE1 GLU B1876 -49.436 19.188 -57.458 1.00118.87 O ANISOU 1907 OE1 GLU B1876 13355 15166 16641 567 -1302 -267 O ATOM 1908 OE2 GLU B1876 -50.046 21.053 -58.438 1.00122.29 O ANISOU 1908 OE2 GLU B1876 13653 15589 17220 715 -1569 -262 O ATOM 1909 N GLU B1877 -47.825 21.959 -61.351 1.00122.43 N ANISOU 1909 N GLU B1877 14737 15228 16549 858 -1623 -237 N ATOM 1910 CA GLU B1877 -48.549 21.376 -62.482 1.00123.04 C ANISOU 1910 CA GLU B1877 15136 15090 16521 776 -1961 -220 C ATOM 1911 C GLU B1877 -47.548 20.760 -63.466 1.00120.69 C ANISOU 1911 C GLU B1877 15397 14599 15861 784 -1805 -212 C ATOM 1912 O GLU B1877 -47.827 19.734 -64.098 1.00120.92 O ANISOU 1912 O GLU B1877 15771 14443 15730 703 -1961 -202 O ATOM 1913 CB GLU B1877 -49.450 22.441 -63.103 1.00125.88 C ANISOU 1913 CB GLU B1877 15517 15347 16962 818 -2326 -212 C ATOM 1914 CG GLU B1877 -50.629 22.785 -62.207 1.00127.15 C ANISOU 1914 CG GLU B1877 15097 15692 17521 848 -2475 -217 C ATOM 1915 CD GLU B1877 -51.123 24.218 -62.293 1.00128.82 C ANISOU 1915 CD GLU B1877 15212 15882 17849 1030 -2639 -220 C ATOM 1916 OE1 GLU B1877 -51.184 24.759 -63.414 1.00129.34 O ANISOU 1916 OE1 GLU B1877 15695 15718 17729 1077 -2925 -207 O ATOM 1917 OE2 GLU B1877 -51.447 24.787 -61.233 1.00128.51 O ANISOU 1917 OE2 GLU B1877 14758 16018 18050 1140 -2475 -238 O ATOM 1918 N LYS B1878 -46.370 21.381 -63.553 1.00117.55 N ANISOU 1918 N LYS B1878 15088 14238 15337 871 -1468 -214 N ATOM 1919 CA LYS B1878 -45.258 20.903 -64.360 1.00118.58 C ANISOU 1919 CA LYS B1878 15650 14235 15170 923 -1171 -207 C ATOM 1920 C LYS B1878 -44.558 19.749 -63.630 1.00114.08 C ANISOU 1920 C LYS B1878 14911 13802 14633 1009 -901 -212 C ATOM 1921 O LYS B1878 -45.138 18.680 -63.446 1.00109.74 O ANISOU 1921 O LYS B1878 14431 13188 14075 972 -1058 -216 O ATOM 1922 CB LYS B1878 -44.302 22.067 -64.635 1.00118.96 C ANISOU 1922 CB LYS B1878 15745 14313 15139 940 -888 -198 C ATOM 1923 CG LYS B1878 -44.949 23.266 -65.317 1.00120.31 C ANISOU 1923 CG LYS B1878 16180 14301 15229 880 -1161 -194 C ATOM 1924 CD LYS B1878 -44.311 24.600 -64.989 1.00119.15 C ANISOU 1924 CD LYS B1878 15896 14255 15118 844 -962 -189 C ATOM 1925 CE LYS B1878 -45.256 25.763 -65.220 1.00121.10 C ANISOU 1925 CE LYS B1878 16288 14355 15368 847 -1329 -193 C ATOM 1926 NZ LYS B1878 -44.642 27.060 -64.851 1.00120.70 N ANISOU 1926 NZ LYS B1878 16197 14358 15306 787 -1143 -188 N ATOM 1927 N ILE B1887 -48.511 6.917 -61.086 1.00108.49 N ANISOU 1927 N ILE B1887 13576 13301 14340 -1485 -919 316 N ATOM 1928 CA ILE B1887 -47.526 7.088 -60.007 1.00108.23 C ANISOU 1928 CA ILE B1887 13287 13548 14284 -1403 -586 229 C ATOM 1929 C ILE B1887 -48.116 6.568 -58.688 1.00102.99 C ANISOU 1929 C ILE B1887 12323 12871 13938 -1265 -561 267 C ATOM 1930 O ILE B1887 -49.325 6.663 -58.462 1.00104.91 O ANISOU 1930 O ILE B1887 12451 12955 14455 -1271 -738 388 O ATOM 1931 CB ILE B1887 -47.083 8.564 -59.890 1.00111.41 C ANISOU 1931 CB ILE B1887 13696 14030 14605 -1547 -494 263 C ATOM 1932 CG1 ILE B1887 -46.064 8.783 -58.763 1.00109.32 C ANISOU 1932 CG1 ILE B1887 13188 14031 14318 -1503 -209 196 C ATOM 1933 CG2 ILE B1887 -48.288 9.491 -59.746 1.00111.93 C ANISOU 1933 CG2 ILE B1887 13764 13839 14925 -1554 -743 389 C ATOM 1934 CD1 ILE B1887 -44.732 8.100 -58.989 1.00109.49 C ANISOU 1934 CD1 ILE B1887 13158 14364 14077 -1474 24 55 C ATOM 1935 N SER B1888 -47.239 6.038 -57.824 1.00 95.99 N ANISOU 1935 N SER B1888 11299 12173 12997 -1151 -339 166 N ATOM 1936 CA SER B1888 -47.595 5.544 -56.496 1.00 91.03 C ANISOU 1936 CA SER B1888 10454 11546 12585 -1056 -281 196 C ATOM 1937 C SER B1888 -46.786 6.279 -55.414 1.00 88.51 C ANISOU 1937 C SER B1888 9975 11404 12248 -1018 -45 148 C ATOM 1938 O SER B1888 -45.549 6.276 -55.426 1.00 88.39 O ANISOU 1938 O SER B1888 9960 11584 12041 -993 91 36 O ATOM 1939 CB SER B1888 -47.388 4.061 -56.417 1.00 88.60 C ANISOU 1939 CB SER B1888 10247 11199 12216 -958 -348 131 C ATOM 1940 OG SER B1888 -47.778 3.581 -55.143 1.00 87.30 O ANISOU 1940 OG SER B1888 9935 11012 12222 -933 -313 188 O ATOM 1941 N TYR B1889 -47.501 6.884 -54.458 1.00 83.90 N ANISOU 1941 N TYR B1889 9247 10768 11861 -1003 -6 231 N ATOM 1942 CA TYR B1889 -46.911 7.802 -53.493 1.00 79.80 C ANISOU 1942 CA TYR B1889 8672 10338 11310 -983 153 204 C ATOM 1943 C TYR B1889 -47.700 7.747 -52.181 1.00 76.63 C ANISOU 1943 C TYR B1889 8134 9891 11090 -887 240 257 C ATOM 1944 O TYR B1889 -48.728 8.420 -52.035 1.00 77.03 O ANISOU 1944 O TYR B1889 8110 9863 11294 -839 216 324 O ATOM 1945 CB TYR B1889 -46.885 9.215 -54.082 1.00 80.67 C ANISOU 1945 CB TYR B1889 8907 10397 11347 -1085 87 237 C ATOM 1946 CG TYR B1889 -46.560 10.313 -53.100 1.00 81.14 C ANISOU 1946 CG TYR B1889 8997 10450 11379 -1075 165 237 C ATOM 1947 CD1 TYR B1889 -45.264 10.509 -52.640 1.00 80.86 C ANISOU 1947 CD1 TYR B1889 8977 10571 11173 -1164 267 187 C ATOM 1948 CD2 TYR B1889 -47.549 11.161 -52.626 1.00 81.27 C ANISOU 1948 CD2 TYR B1889 9037 10306 11536 -955 110 280 C ATOM 1949 CE1 TYR B1889 -44.965 11.514 -51.731 1.00 80.93 C ANISOU 1949 CE1 TYR B1889 9089 10526 11134 -1185 278 202 C ATOM 1950 CE2 TYR B1889 -47.267 12.170 -51.719 1.00 81.18 C ANISOU 1950 CE2 TYR B1889 9152 10236 11455 -910 149 263 C ATOM 1951 CZ TYR B1889 -45.969 12.352 -51.271 1.00 80.85 C ANISOU 1951 CZ TYR B1889 9193 10300 11224 -1052 215 234 C ATOM 1952 OH TYR B1889 -45.694 13.348 -50.375 1.00 77.31 O ANISOU 1952 OH TYR B1889 8940 9746 10685 -1037 196 231 O ATOM 1953 N GLU B1890 -47.211 6.938 -51.235 1.00 72.73 N ANISOU 1953 N GLU B1890 7617 9455 10561 -842 338 216 N ATOM 1954 CA GLU B1890 -47.837 6.811 -49.925 1.00 70.82 C ANISOU 1954 CA GLU B1890 7299 9191 10415 -790 461 267 C ATOM 1955 C GLU B1890 -46.806 7.077 -48.836 1.00 66.42 C ANISOU 1955 C GLU B1890 6834 8678 9723 -749 572 194 C ATOM 1956 O GLU B1890 -46.130 6.162 -48.379 1.00 69.02 O ANISOU 1956 O GLU B1890 7220 9026 9976 -736 554 146 O ATOM 1957 CB GLU B1890 -48.473 5.432 -49.766 1.00 73.54 C ANISOU 1957 CB GLU B1890 7611 9498 10833 -847 403 336 C ATOM 1958 CG GLU B1890 -49.886 5.365 -50.315 1.00 76.86 C ANISOU 1958 CG GLU B1890 7864 9885 11452 -919 316 466 C ATOM 1959 CD GLU B1890 -50.893 6.234 -49.577 1.00 79.75 C ANISOU 1959 CD GLU B1890 8008 10325 11968 -846 483 529 C ATOM 1960 OE1 GLU B1890 -51.961 6.514 -50.155 1.00 81.11 O ANISOU 1960 OE1 GLU B1890 7979 10507 12331 -846 391 610 O ATOM 1961 OE2 GLU B1890 -50.609 6.624 -48.422 1.00 81.51 O ANISOU 1961 OE2 GLU B1890 8266 10595 12108 -763 692 486 O ATOM 1962 N PRO B1891 -46.653 8.338 -48.385 1.00 61.71 N ANISOU 1962 N PRO B1891 6301 8064 9083 -720 635 184 N ATOM 1963 CA PRO B1891 -45.734 8.655 -47.294 1.00 59.22 C ANISOU 1963 CA PRO B1891 6115 7751 8634 -710 690 135 C ATOM 1964 C PRO B1891 -46.152 7.997 -45.971 1.00 56.54 C ANISOU 1964 C PRO B1891 5824 7364 8293 -650 810 155 C ATOM 1965 O PRO B1891 -47.325 7.995 -45.613 1.00 57.96 O ANISOU 1965 O PRO B1891 5934 7528 8560 -600 936 215 O ATOM 1966 CB PRO B1891 -45.767 10.190 -47.194 1.00 60.94 C ANISOU 1966 CB PRO B1891 6475 7885 8793 -702 675 140 C ATOM 1967 CG PRO B1891 -47.055 10.595 -47.880 1.00 62.80 C ANISOU 1967 CG PRO B1891 6627 8058 9175 -618 659 184 C ATOM 1968 CD PRO B1891 -47.335 9.526 -48.916 1.00 62.37 C ANISOU 1968 CD PRO B1891 6398 8074 9223 -690 591 215 C ATOM 1969 N ILE B1892 -45.155 7.462 -45.263 1.00 53.65 N ANISOU 1969 N ILE B1892 5571 6997 7815 -666 764 106 N ATOM 1970 CA ILE B1892 -45.353 6.631 -44.089 1.00 52.01 C ANISOU 1970 CA ILE B1892 5494 6715 7551 -660 819 129 C ATOM 1971 C ILE B1892 -44.609 7.211 -42.880 1.00 50.42 C ANISOU 1971 C ILE B1892 5531 6431 7192 -642 821 92 C ATOM 1972 O ILE B1892 -44.809 6.768 -41.737 1.00 50.22 O ANISOU 1972 O ILE B1892 5704 6311 7064 -648 885 116 O ATOM 1973 CB ILE B1892 -44.911 5.192 -44.409 1.00 52.03 C ANISOU 1973 CB ILE B1892 5501 6714 7554 -676 656 102 C ATOM 1974 CG1 ILE B1892 -43.408 5.065 -44.650 1.00 51.51 C ANISOU 1974 CG1 ILE B1892 5430 6719 7421 -609 484 -17 C ATOM 1975 CG2 ILE B1892 -45.694 4.664 -45.601 1.00 52.97 C ANISOU 1975 CG2 ILE B1892 5467 6862 7796 -711 613 148 C ATOM 1976 CD1 ILE B1892 -42.930 3.636 -44.722 1.00 51.69 C ANISOU 1976 CD1 ILE B1892 5531 6696 7414 -522 293 -86 C ATOM 1977 N THR B1893 -43.745 8.199 -43.128 1.00 48.19 N ANISOU 1977 N THR B1893 5272 6173 6864 -664 725 52 N ATOM 1978 CA THR B1893 -42.962 8.802 -42.064 1.00 47.50 C ANISOU 1978 CA THR B1893 5440 5983 6624 -687 649 33 C ATOM 1979 C THR B1893 -42.470 10.182 -42.523 1.00 47.32 C ANISOU 1979 C THR B1893 5458 5965 6555 -773 556 39 C ATOM 1980 O THR B1893 -42.768 10.626 -43.645 1.00 46.30 O ANISOU 1980 O THR B1893 5176 5912 6500 -808 565 56 O ATOM 1981 CB THR B1893 -41.866 7.822 -41.623 1.00 46.38 C ANISOU 1981 CB THR B1893 5316 5859 6446 -703 463 -12 C ATOM 1982 OG1 THR B1893 -41.289 8.282 -40.404 1.00 46.80 O ANISOU 1982 OG1 THR B1893 5673 5761 6348 -735 363 -11 O ATOM 1983 CG2 THR B1893 -40.796 7.623 -42.669 1.00 45.91 C ANISOU 1983 CG2 THR B1893 4964 6018 6458 -731 312 -70 C ATOM 1984 N THR B1894 -41.749 10.858 -41.625 1.00 48.44 N ANISOU 1984 N THR B1894 5871 5984 6548 -838 429 42 N ATOM 1985 CA THR B1894 -41.010 12.079 -41.946 1.00 49.64 C ANISOU 1985 CA THR B1894 6122 6122 6616 -1016 247 77 C ATOM 1986 C THR B1894 -39.604 12.028 -41.333 1.00 50.62 C ANISOU 1986 C THR B1894 6285 6284 6665 -1182 4 89 C ATOM 1987 O THR B1894 -39.288 11.223 -40.463 1.00 50.58 O ANISOU 1987 O THR B1894 6339 6232 6645 -1108 -45 56 O ATOM 1988 CB THR B1894 -41.748 13.339 -41.473 1.00 51.02 C ANISOU 1988 CB THR B1894 6697 6032 6657 -935 265 87 C ATOM 1989 OG1 THR B1894 -41.765 13.356 -40.043 1.00 52.48 O ANISOU 1989 OG1 THR B1894 7248 6010 6680 -839 273 62 O ATOM 1990 CG2 THR B1894 -43.166 13.434 -41.990 1.00 50.50 C ANISOU 1990 CG2 THR B1894 6542 5951 6694 -719 478 64 C ATOM 1991 N THR B1895 -38.768 12.947 -41.802 1.00 44.64 N ANISOU 1991 N THR B1895 5539 4529 6893 -342 -178 -239 N ATOM 1992 CA THR B1895 -37.399 13.050 -41.393 1.00 44.72 C ANISOU 1992 CA THR B1895 5508 4530 6953 -252 -92 -230 C ATOM 1993 C THR B1895 -37.331 13.495 -39.930 1.00 45.10 C ANISOU 1993 C THR B1895 5435 4624 7076 -296 -117 -246 C ATOM 1994 O THR B1895 -36.402 13.134 -39.209 1.00 45.64 O ANISOU 1994 O THR B1895 5472 4691 7175 -287 -98 -220 O ATOM 1995 CB THR B1895 -36.648 14.004 -42.321 1.00 44.83 C ANISOU 1995 CB THR B1895 5469 4569 6994 -188 -32 -159 C ATOM 1996 OG1 THR B1895 -37.185 15.306 -42.107 1.00 45.39 O ANISOU 1996 OG1 THR B1895 5489 4630 7124 -258 -102 -182 O ATOM 1997 CG2 THR B1895 -36.782 13.632 -43.780 1.00 45.44 C ANISOU 1997 CG2 THR B1895 5701 4606 6956 -82 6 -148 C ATOM 1998 N LEU B1896 -38.322 14.273 -39.494 1.00 46.61 N ANISOU 1998 N LEU B1896 5587 4868 7254 -288 -159 -272 N ATOM 1999 CA LEU B1896 -38.396 14.653 -38.101 1.00 48.20 C ANISOU 1999 CA LEU B1896 5777 5096 7441 -232 -187 -296 C ATOM 2000 C LEU B1896 -38.878 13.458 -37.275 1.00 48.97 C ANISOU 2000 C LEU B1896 5799 5301 7504 -280 -175 -267 C ATOM 2001 O LEU B1896 -38.379 13.269 -36.170 1.00 49.67 O ANISOU 2001 O LEU B1896 5895 5370 7606 -265 -179 -287 O ATOM 2002 CB LEU B1896 -39.310 15.867 -37.916 1.00 49.95 C ANISOU 2002 CB LEU B1896 6058 5362 7556 -60 -218 -315 C ATOM 2003 CG LEU B1896 -39.275 16.494 -36.517 1.00 52.31 C ANISOU 2003 CG LEU B1896 6506 5619 7751 113 -274 -355 C ATOM 2004 CD1 LEU B1896 -37.841 16.680 -36.005 1.00 51.92 C ANISOU 2004 CD1 LEU B1896 6589 5345 7793 -36 -395 -367 C ATOM 2005 CD2 LEU B1896 -40.042 17.813 -36.490 1.00 53.02 C ANISOU 2005 CD2 LEU B1896 6809 5691 7642 409 -322 -385 C ATOM 2006 N ARG B1897 -39.827 12.670 -37.811 1.00 49.93 N ANISOU 2006 N ARG B1897 5872 5526 7573 -385 -207 -185 N ATOM 2007 CA ARG B1897 -40.301 11.444 -37.126 1.00 51.26 C ANISOU 2007 CA ARG B1897 5997 5786 7691 -534 -275 -85 C ATOM 2008 C ARG B1897 -39.144 10.445 -37.037 1.00 49.59 C ANISOU 2008 C ARG B1897 5975 5358 7507 -578 -295 -163 C ATOM 2009 O ARG B1897 -38.892 9.868 -35.985 1.00 48.75 O ANISOU 2009 O ARG B1897 5857 5263 7400 -605 -304 -158 O ATOM 2010 CB ARG B1897 -41.484 10.791 -37.846 1.00 54.43 C ANISOU 2010 CB ARG B1897 6364 6303 8011 -752 -418 97 C ATOM 2011 CG ARG B1897 -42.830 11.463 -37.608 1.00 57.44 C ANISOU 2011 CG ARG B1897 6437 7072 8314 -698 -393 302 C ATOM 2012 CD ARG B1897 -44.005 10.662 -38.164 1.00 60.66 C ANISOU 2012 CD ARG B1897 6733 7673 8638 -1031 -606 611 C ATOM 2013 NE ARG B1897 -44.748 9.916 -37.137 1.00 63.99 N ANISOU 2013 NE ARG B1897 6906 8430 8978 -1219 -697 920 N ATOM 2014 CZ ARG B1897 -44.910 8.589 -37.097 1.00 66.70 C ANISOU 2014 CZ ARG B1897 7381 8679 9280 -1639 -976 1101 C ATOM 2015 NH1 ARG B1897 -44.332 7.819 -38.007 1.00 68.27 N ANISOU 2015 NH1 ARG B1897 8058 8404 9475 -1831 -1186 951 N ATOM 2016 NH2 ARG B1897 -45.666 8.036 -36.157 1.00 68.99 N ANISOU 2016 NH2 ARG B1897 7372 9352 9486 -1841 -1068 1460 N ATOM 2017 N ARG B1898 -38.426 10.290 -38.152 1.00 49.26 N ANISOU 2017 N ARG B1898 6110 5150 7454 -518 -280 -217 N ATOM 2018 CA ARG B1898 -37.227 9.447 -38.236 1.00 49.50 C ANISOU 2018 CA ARG B1898 6330 5040 7436 -402 -250 -256 C ATOM 2019 C ARG B1898 -36.137 9.890 -37.248 1.00 48.73 C ANISOU 2019 C ARG B1898 6063 5010 7442 -313 -148 -264 C ATOM 2020 O ARG B1898 -35.449 9.048 -36.678 1.00 48.74 O ANISOU 2020 O ARG B1898 6138 4976 7404 -254 -142 -263 O ATOM 2021 CB ARG B1898 -36.652 9.473 -39.653 1.00 50.05 C ANISOU 2021 CB ARG B1898 6570 5027 7419 -225 -194 -259 C ATOM 2022 CG ARG B1898 -35.391 8.635 -39.825 1.00 51.58 C ANISOU 2022 CG ARG B1898 6952 5171 7474 50 -112 -243 C ATOM 2023 CD ARG B1898 -35.513 7.193 -39.355 1.00 51.59 C ANISOU 2023 CD ARG B1898 7309 4983 7308 51 -256 -282 C ATOM 2024 NE ARG B1898 -36.497 6.472 -40.136 1.00 53.20 N ANISOU 2024 NE ARG B1898 7929 4946 7335 -81 -495 -296 N ATOM 2025 CZ ARG B1898 -36.294 6.008 -41.365 1.00 55.84 C ANISOU 2025 CZ ARG B1898 8710 5085 7420 159 -545 -317 C ATOM 2026 NH1 ARG B1898 -35.168 6.287 -41.997 1.00 56.88 N ANISOU 2026 NH1 ARG B1898 8820 5335 7457 596 -300 -299 N ATOM 2027 NH2 ARG B1898 -37.210 5.257 -41.955 1.00 57.50 N ANISOU 2027 NH2 ARG B1898 9405 5002 7440 -35 -867 -309 N ATOM 2028 N LYS B1899 -35.953 11.202 -37.071 1.00 48.63 N ANISOU 2028 N LYS B1899 5880 5063 7531 -314 -117 -253 N ATOM 2029 CA LYS B1899 -34.923 11.686 -36.167 1.00 49.44 C ANISOU 2029 CA LYS B1899 5885 5188 7712 -316 -121 -210 C ATOM 2030 C LYS B1899 -35.320 11.381 -34.717 1.00 50.31 C ANISOU 2030 C LYS B1899 6002 5292 7821 -357 -168 -266 C ATOM 2031 O LYS B1899 -34.470 11.038 -33.902 1.00 50.03 O ANISOU 2031 O LYS B1899 5944 5247 7814 -361 -180 -239 O ATOM 2032 CB LYS B1899 -34.655 13.182 -36.360 1.00 49.80 C ANISOU 2032 CB LYS B1899 5887 5216 7816 -370 -190 -155 C ATOM 2033 CG LYS B1899 -33.548 13.752 -35.476 1.00 50.40 C ANISOU 2033 CG LYS B1899 5924 5272 7952 -476 -310 -39 C ATOM 2034 CD LYS B1899 -32.193 13.060 -35.635 1.00 51.04 C ANISOU 2034 CD LYS B1899 5818 5518 8057 -463 -241 158 C ATOM 2035 CE LYS B1899 -31.138 13.528 -34.655 1.00 51.72 C ANISOU 2035 CE LYS B1899 5820 5625 8205 -642 -412 343 C ATOM 2036 NZ LYS B1899 -29.794 13.586 -35.276 1.00 53.91 N ANISOU 2036 NZ LYS B1899 5799 6187 8496 -686 -393 710 N ATOM 2037 N HIS B1900 -36.611 11.518 -34.391 1.00 52.00 N ANISOU 2037 N HIS B1900 6214 5565 7978 -361 -186 -300 N ATOM 2038 CA HIS B1900 -37.067 11.253 -33.028 1.00 52.50 C ANISOU 2038 CA HIS B1900 6253 5701 7994 -343 -200 -303 C ATOM 2039 C HIS B1900 -36.820 9.784 -32.675 1.00 51.97 C ANISOU 2039 C HIS B1900 6212 5615 7917 -444 -216 -281 C ATOM 2040 O HIS B1900 -36.468 9.482 -31.536 1.00 51.79 O ANISOU 2040 O HIS B1900 6188 5590 7897 -437 -225 -292 O ATOM 2041 CB HIS B1900 -38.531 11.645 -32.836 1.00 53.65 C ANISOU 2041 CB HIS B1900 6308 6052 8022 -258 -179 -239 C ATOM 2042 CG HIS B1900 -38.789 13.106 -32.967 1.00 54.50 C ANISOU 2042 CG HIS B1900 6499 6145 8063 -55 -178 -281 C ATOM 2043 ND1 HIS B1900 -40.001 13.603 -33.389 1.00 55.88 N ANISOU 2043 ND1 HIS B1900 6587 6527 8118 87 -133 -203 N ATOM 2044 CD2 HIS B1900 -37.999 14.177 -32.746 1.00 55.48 C ANISOU 2044 CD2 HIS B1900 6834 6054 8190 19 -265 -363 C ATOM 2045 CE1 HIS B1900 -39.951 14.920 -33.410 1.00 56.68 C ANISOU 2045 CE1 HIS B1900 6892 6513 8129 311 -166 -280 C ATOM 2046 NE2 HIS B1900 -38.735 15.300 -33.022 1.00 55.95 N ANISOU 2046 NE2 HIS B1900 7020 6129 8109 236 -281 -377 N ATOM 2047 N GLU B1901 -36.985 8.896 -33.663 1.00 51.86 N ANISOU 2047 N GLU B1901 6302 5541 7858 -522 -254 -255 N ATOM 2048 CA GLU B1901 -36.738 7.467 -33.479 1.00 53.01 C ANISOU 2048 CA GLU B1901 6639 5577 7925 -591 -337 -242 C ATOM 2049 C GLU B1901 -35.258 7.237 -33.116 1.00 53.08 C ANISOU 2049 C GLU B1901 6692 5512 7962 -424 -260 -292 C ATOM 2050 O GLU B1901 -34.970 6.570 -32.119 1.00 53.50 O ANISOU 2050 O GLU B1901 6781 5544 8001 -443 -290 -298 O ATOM 2051 CB GLU B1901 -37.142 6.687 -34.733 1.00 54.64 C ANISOU 2051 CB GLU B1901 7121 5637 8003 -660 -463 -213 C ATOM 2052 CG GLU B1901 -38.642 6.616 -34.957 1.00 57.01 C ANISOU 2052 CG GLU B1901 7355 6050 8256 -929 -618 -63 C ATOM 2053 CD GLU B1901 -39.082 6.293 -36.385 1.00 60.01 C ANISOU 2053 CD GLU B1901 8006 6269 8524 -1018 -775 -27 C ATOM 2054 OE1 GLU B1901 -38.275 5.685 -37.124 1.00 62.61 O ANISOU 2054 OE1 GLU B1901 8729 6329 8730 -848 -807 -129 O ATOM 2055 OE2 GLU B1901 -40.239 6.649 -36.766 1.00 60.69 O ANISOU 2055 OE2 GLU B1901 7928 6521 8608 -1215 -868 126 O ATOM 2056 N GLU B1902 -34.334 7.804 -33.911 1.00 52.25 N ANISOU 2056 N GLU B1902 6538 5426 7886 -267 -165 -274 N ATOM 2057 CA GLU B1902 -32.886 7.628 -33.724 1.00 52.51 C ANISOU 2057 CA GLU B1902 6509 5522 7917 -94 -84 -199 C ATOM 2058 C GLU B1902 -32.444 8.163 -32.352 1.00 50.92 C ANISOU 2058 C GLU B1902 6128 5375 7844 -204 -122 -174 C ATOM 2059 O GLU B1902 -31.625 7.540 -31.689 1.00 53.48 O ANISOU 2059 O GLU B1902 6441 5729 8149 -134 -112 -127 O ATOM 2060 CB GLU B1902 -32.094 8.321 -34.833 1.00 54.32 C ANISOU 2060 CB GLU B1902 6605 5886 8146 47 15 -67 C ATOM 2061 CG GLU B1902 -32.309 7.723 -36.210 1.00 56.34 C ANISOU 2061 CG GLU B1902 7111 6079 8217 257 64 -86 C ATOM 2062 CD GLU B1902 -31.857 8.590 -37.380 1.00 59.50 C ANISOU 2062 CD GLU B1902 7352 6637 8616 367 168 48 C ATOM 2063 OE1 GLU B1902 -31.520 8.005 -38.426 1.00 62.14 O ANISOU 2063 OE1 GLU B1902 7883 6993 8734 689 262 96 O ATOM 2064 OE2 GLU B1902 -31.845 9.859 -37.254 1.00 60.76 O ANISOU 2064 OE2 GLU B1902 7251 6881 8952 153 133 119 O ATOM 2065 N VAL B1903 -32.981 9.309 -31.933 1.00 48.64 N ANISOU 2065 N VAL B1903 5764 5074 7640 -336 -186 -203 N ATOM 2066 CA VAL B1903 -32.690 9.889 -30.622 1.00 48.75 C ANISOU 2066 CA VAL B1903 5759 5055 7706 -413 -283 -200 C ATOM 2067 C VAL B1903 -33.261 8.981 -29.528 1.00 49.03 C ANISOU 2067 C VAL B1903 5867 5073 7689 -409 -281 -284 C ATOM 2068 O VAL B1903 -32.614 8.697 -28.547 1.00 48.60 O ANISOU 2068 O VAL B1903 5815 4997 7652 -422 -322 -269 O ATOM 2069 CB VAL B1903 -33.249 11.323 -30.505 1.00 48.65 C ANISOU 2069 CB VAL B1903 5826 4968 7690 -448 -384 -232 C ATOM 2070 CG1 VAL B1903 -33.156 11.872 -29.088 1.00 48.48 C ANISOU 2070 CG1 VAL B1903 5962 4832 7626 -453 -528 -265 C ATOM 2071 CG2 VAL B1903 -32.562 12.262 -31.479 1.00 49.21 C ANISOU 2071 CG2 VAL B1903 5843 5036 7815 -529 -450 -103 C ATOM 2072 N SER B1904 -34.503 8.535 -29.704 1.00 51.24 N ANISOU 2072 N SER B1904 6180 5393 7895 -426 -256 -323 N ATOM 2073 CA SER B1904 -35.114 7.606 -28.752 1.00 52.98 C ANISOU 2073 CA SER B1904 6424 5656 8046 -483 -280 -315 C ATOM 2074 C SER B1904 -34.219 6.374 -28.551 1.00 52.93 C ANISOU 2074 C SER B1904 6533 5550 8026 -488 -304 -321 C ATOM 2075 O SER B1904 -33.919 6.006 -27.417 1.00 52.18 O ANISOU 2075 O SER B1904 6446 5447 7930 -496 -327 -329 O ATOM 2076 CB SER B1904 -36.502 7.226 -29.183 1.00 53.87 C ANISOU 2076 CB SER B1904 6500 5894 8073 -589 -307 -230 C ATOM 2077 OG SER B1904 -37.416 8.248 -28.822 1.00 54.82 O ANISOU 2077 OG SER B1904 6481 6206 8142 -484 -253 -183 O ATOM 2078 N ALA B1905 -33.781 5.770 -29.659 1.00 53.78 N ANISOU 2078 N ALA B1905 6776 5578 8079 -417 -296 -316 N ATOM 2079 CA ALA B1905 -32.976 4.547 -29.629 1.00 55.71 C ANISOU 2079 CA ALA B1905 7236 5717 8213 -291 -317 -318 C ATOM 2080 C ALA B1905 -31.668 4.805 -28.871 1.00 56.93 C ANISOU 2080 C ALA B1905 7223 5961 8444 -168 -246 -273 C ATOM 2081 O ALA B1905 -31.308 4.036 -27.974 1.00 56.65 O ANISOU 2081 O ALA B1905 7270 5885 8370 -147 -281 -284 O ATOM 2082 CB ALA B1905 -32.721 4.070 -31.034 1.00 56.38 C ANISOU 2082 CB ALA B1905 7564 5712 8145 -100 -304 -313 C ATOM 2083 N MET B1906 -30.989 5.903 -29.236 1.00 58.49 N ANISOU 2083 N MET B1906 7188 6288 8746 -136 -189 -179 N ATOM 2084 CA MET B1906 -29.756 6.376 -28.588 1.00 59.56 C ANISOU 2084 CA MET B1906 7108 6554 8968 -135 -202 -29 C ATOM 2085 C MET B1906 -29.958 6.439 -27.069 1.00 56.93 C ANISOU 2085 C MET B1906 6809 6128 8693 -287 -310 -103 C ATOM 2086 O MET B1906 -29.152 5.949 -26.294 1.00 56.40 O ANISOU 2086 O MET B1906 6708 6097 8624 -253 -334 -39 O ATOM 2087 CB MET B1906 -29.374 7.756 -29.136 1.00 63.03 C ANISOU 2087 CB MET B1906 7342 7095 9509 -248 -244 120 C ATOM 2088 CG MET B1906 -28.587 8.626 -28.172 1.00 68.65 C ANISOU 2088 CG MET B1906 7928 7830 10325 -458 -424 277 C ATOM 2089 SD MET B1906 -27.514 9.858 -29.000 1.00 79.77 S ANISOU 2089 SD MET B1906 9051 9455 11804 -634 -543 660 S ATOM 2090 CE MET B1906 -28.559 10.426 -30.348 1.00 75.04 C ANISOU 2090 CE MET B1906 8554 8773 11182 -580 -450 512 C ATOM 2091 N VAL B1907 -31.078 7.023 -26.654 1.00 55.30 N ANISOU 2091 N VAL B1907 6679 5833 8499 -398 -360 -222 N ATOM 2092 CA VAL B1907 -31.383 7.209 -25.253 1.00 53.80 C ANISOU 2092 CA VAL B1907 6562 5580 8299 -452 -440 -282 C ATOM 2093 C VAL B1907 -31.514 5.836 -24.594 1.00 52.71 C ANISOU 2093 C VAL B1907 6495 5434 8098 -435 -412 -321 C ATOM 2094 O VAL B1907 -30.892 5.574 -23.594 1.00 52.33 O ANISOU 2094 O VAL B1907 6463 5357 8061 -440 -462 -310 O ATOM 2095 CB VAL B1907 -32.659 8.057 -25.086 1.00 53.13 C ANISOU 2095 CB VAL B1907 6549 5491 8146 -425 -444 -356 C ATOM 2096 CG1 VAL B1907 -33.151 8.082 -23.647 1.00 53.78 C ANISOU 2096 CG1 VAL B1907 6738 5568 8127 -355 -476 -399 C ATOM 2097 CG2 VAL B1907 -32.464 9.469 -25.610 1.00 53.20 C ANISOU 2097 CG2 VAL B1907 6605 5428 8178 -432 -533 -332 C ATOM 2098 N ILE B1908 -32.322 4.973 -25.207 1.00 53.81 N ANISOU 2098 N ILE B1908 6715 5573 8156 -452 -380 -344 N ATOM 2099 CA ILE B1908 -32.674 3.647 -24.672 1.00 55.07 C ANISOU 2099 CA ILE B1908 7028 5680 8216 -516 -436 -346 C ATOM 2100 C ILE B1908 -31.427 2.751 -24.605 1.00 55.50 C ANISOU 2100 C ILE B1908 7212 5648 8228 -368 -440 -348 C ATOM 2101 O ILE B1908 -31.217 2.051 -23.614 1.00 55.94 O ANISOU 2101 O ILE B1908 7350 5655 8246 -388 -490 -359 O ATOM 2102 CB ILE B1908 -33.809 3.013 -25.509 1.00 55.18 C ANISOU 2102 CB ILE B1908 7167 5673 8124 -656 -511 -299 C ATOM 2103 CG1 ILE B1908 -35.131 3.761 -25.309 1.00 54.83 C ANISOU 2103 CG1 ILE B1908 6912 5837 8083 -770 -492 -213 C ATOM 2104 CG2 ILE B1908 -33.958 1.524 -25.216 1.00 56.68 C ANISOU 2104 CG2 ILE B1908 7649 5717 8171 -776 -673 -263 C ATOM 2105 CD1 ILE B1908 -36.102 3.634 -26.466 1.00 55.69 C ANISOU 2105 CD1 ILE B1908 7040 5985 8134 -914 -563 -117 C ATOM 2106 N GLN B1909 -30.614 2.764 -25.660 1.00 56.94 N ANISOU 2106 N GLN B1909 7403 5852 8379 -169 -371 -308 N ATOM 2107 CA GLN B1909 -29.402 1.960 -25.696 1.00 61.02 C ANISOU 2107 CA GLN B1909 8011 6388 8784 106 -328 -249 C ATOM 2108 C GLN B1909 -28.441 2.376 -24.569 1.00 63.43 C ANISOU 2108 C GLN B1909 8060 6827 9213 82 -326 -157 C ATOM 2109 O GLN B1909 -27.809 1.521 -23.935 1.00 67.79 O ANISOU 2109 O GLN B1909 8706 7369 9682 216 -337 -137 O ATOM 2110 CB GLN B1909 -28.723 2.080 -27.057 1.00 63.02 C ANISOU 2110 CB GLN B1909 8243 6763 8936 406 -207 -147 C ATOM 2111 CG GLN B1909 -29.280 1.130 -28.104 1.00 65.45 C ANISOU 2111 CG GLN B1909 9020 6855 8991 576 -255 -236 C ATOM 2112 CD GLN B1909 -28.576 1.310 -29.426 1.00 69.52 C ANISOU 2112 CD GLN B1909 9528 7524 9359 966 -101 -123 C ATOM 2113 OE1 GLN B1909 -27.620 0.601 -29.749 1.00 73.85 O ANISOU 2113 OE1 GLN B1909 10239 8166 9653 1447 -2 -28 O ATOM 2114 NE2 GLN B1909 -29.027 2.291 -30.194 1.00 69.86 N ANISOU 2114 NE2 GLN B1909 9373 7640 9530 818 -62 -105 N ATOM 2115 N ARG B1910 -28.319 3.687 -24.332 1.00 64.64 N ANISOU 2115 N ARG B1910 7954 7069 9536 -94 -358 -88 N ATOM 2116 CA ARG B1910 -27.422 4.230 -23.313 1.00 64.74 C ANISOU 2116 CA ARG B1910 7791 7156 9651 -200 -456 39 C ATOM 2117 C ARG B1910 -27.996 3.963 -21.916 1.00 63.37 C ANISOU 2117 C ARG B1910 7783 6816 9477 -319 -544 -111 C ATOM 2118 O ARG B1910 -27.243 3.777 -20.980 1.00 64.41 O ANISOU 2118 O ARG B1910 7882 6960 9629 -339 -619 -43 O ATOM 2119 CB ARG B1910 -27.167 5.720 -23.567 1.00 65.72 C ANISOU 2119 CB ARG B1910 7742 7332 9894 -393 -568 177 C ATOM 2120 CG ARG B1910 -26.202 5.974 -24.716 1.00 68.64 C ANISOU 2120 CG ARG B1910 7832 7982 10265 -302 -500 461 C ATOM 2121 CD ARG B1910 -26.076 7.442 -25.070 1.00 70.95 C ANISOU 2121 CD ARG B1910 8006 8288 10661 -571 -669 622 C ATOM 2122 NE ARG B1910 -25.126 7.710 -26.146 1.00 74.48 N ANISOU 2122 NE ARG B1910 8109 9088 11102 -520 -610 985 N ATOM 2123 CZ ARG B1910 -23.801 7.695 -26.011 1.00 79.58 C ANISOU 2123 CZ ARG B1910 8395 10092 11749 -551 -668 1411 C ATOM 2124 NH1 ARG B1910 -23.244 7.221 -24.907 1.00 82.33 N ANISOU 2124 NH1 ARG B1910 8717 10460 12105 -586 -757 1476 N ATOM 2125 NH2 ARG B1910 -23.034 8.144 -26.990 1.00 83.63 N ANISOU 2125 NH2 ARG B1910 8534 10999 12243 -545 -632 1825 N ATOM 2126 N ALA B1911 -29.325 3.944 -21.791 1.00 63.38 N ANISOU 2126 N ALA B1911 7926 6717 9437 -386 -530 -264 N ATOM 2127 CA ALA B1911 -30.012 3.682 -20.521 1.00 64.95 C ANISOU 2127 CA ALA B1911 8238 6852 9587 -451 -575 -347 C ATOM 2128 C ALA B1911 -29.683 2.271 -20.032 1.00 66.86 C ANISOU 2128 C ALA B1911 8595 7049 9757 -415 -583 -356 C ATOM 2129 O ALA B1911 -29.514 2.022 -18.834 1.00 69.93 O ANISOU 2129 O ALA B1911 9031 7402 10134 -444 -636 -372 O ATOM 2130 CB ALA B1911 -31.506 3.840 -20.693 1.00 64.39 C ANISOU 2130 CB ALA B1911 8188 6832 9443 -494 -529 -386 C ATOM 2131 N PHE B1912 -29.616 1.344 -20.984 1.00 67.78 N ANISOU 2131 N PHE B1912 8837 7132 9784 -324 -553 -352 N ATOM 2132 CA PHE B1912 -29.408 -0.050 -20.686 1.00 70.30 C ANISOU 2132 CA PHE B1912 9415 7333 9960 -256 -611 -373 C ATOM 2133 C PHE B1912 -28.142 -0.232 -19.846 1.00 70.92 C ANISOU 2133 C PHE B1912 9420 7460 10065 -115 -605 -325 C ATOM 2134 O PHE B1912 -28.214 -0.808 -18.771 1.00 70.23 O ANISOU 2134 O PHE B1912 9440 7297 9948 -185 -675 -360 O ATOM 2135 CB PHE B1912 -29.317 -0.847 -21.983 1.00 71.83 C ANISOU 2135 CB PHE B1912 9889 7423 9979 -69 -618 -377 C ATOM 2136 CG PHE B1912 -29.380 -2.328 -21.760 1.00 73.54 C ANISOU 2136 CG PHE B1912 10569 7406 9967 -19 -769 -414 C ATOM 2137 CD1 PHE B1912 -30.522 -2.904 -21.230 1.00 73.99 C ANISOU 2137 CD1 PHE B1912 10805 7332 9973 -369 -957 -405 C ATOM 2138 CD2 PHE B1912 -28.299 -3.139 -22.064 1.00 75.52 C ANISOU 2138 CD2 PHE B1912 11087 7595 10012 393 -743 -409 C ATOM 2139 CE1 PHE B1912 -30.585 -4.272 -21.024 1.00 75.29 C ANISOU 2139 CE1 PHE B1912 11475 7225 9904 -396 -1181 -408 C ATOM 2140 CE2 PHE B1912 -28.365 -4.506 -21.856 1.00 75.98 C ANISOU 2140 CE2 PHE B1912 11708 7358 9799 473 -934 -460 C ATOM 2141 CZ PHE B1912 -29.505 -5.067 -21.333 1.00 76.01 C ANISOU 2141 CZ PHE B1912 11949 7152 9776 32 -1184 -469 C ATOM 2142 N ARG B1913 -27.009 0.277 -20.355 1.00 72.88 N ANISOU 2142 N ARG B1913 9446 7882 10361 60 -533 -190 N ATOM 2143 CA ARG B1913 -25.716 0.195 -19.674 1.00 76.71 C ANISOU 2143 CA ARG B1913 9761 8514 10869 174 -546 -36 C ATOM 2144 C ARG B1913 -25.840 0.778 -18.266 1.00 75.44 C ANISOU 2144 C ARG B1913 9546 8274 10840 -97 -680 -70 C ATOM 2145 O ARG B1913 -25.353 0.191 -17.310 1.00 79.10 O ANISOU 2145 O ARG B1913 10064 8714 11275 -69 -733 -59 O ATOM 2146 CB ARG B1913 -24.609 0.931 -20.439 1.00 80.89 C ANISOU 2146 CB ARG B1913 9926 9359 11447 293 -484 245 C ATOM 2147 CG ARG B1913 -24.064 0.168 -21.641 1.00 86.28 C ANISOU 2147 CG ARG B1913 10657 10218 11907 754 -311 355 C ATOM 2148 CD ARG B1913 -22.620 0.479 -22.013 1.00 89.68 C ANISOU 2148 CD ARG B1913 10639 11131 12303 994 -219 772 C ATOM 2149 NE ARG B1913 -22.231 -0.204 -23.249 1.00 93.07 N ANISOU 2149 NE ARG B1913 11166 11758 12435 1566 -6 876 N ATOM 2150 CZ ARG B1913 -21.827 -1.475 -23.336 1.00 95.65 C ANISOU 2150 CZ ARG B1913 11825 12084 12432 2113 92 853 C ATOM 2151 NH1 ARG B1913 -21.607 -2.018 -24.522 1.00 98.10 N ANISOU 2151 NH1 ARG B1913 12366 12505 12403 2699 266 912 N ATOM 2152 NH2 ARG B1913 -21.632 -2.198 -22.246 1.00 94.73 N ANISOU 2152 NH2 ARG B1913 11874 11835 12281 2122 7 771 N ATOM 2153 N ARG B1914 -26.499 1.932 -18.162 1.00 74.32 N ANISOU 2153 N ARG B1914 9364 8077 10798 -306 -740 -117 N ATOM 2154 CA ARG B1914 -26.588 2.685 -16.925 1.00 75.07 C ANISOU 2154 CA ARG B1914 9521 8062 10940 -474 -894 -145 C ATOM 2155 C ARG B1914 -27.423 1.910 -15.904 1.00 76.78 C ANISOU 2155 C ARG B1914 9941 8169 11061 -465 -872 -300 C ATOM 2156 O ARG B1914 -27.043 1.825 -14.745 1.00 79.13 O ANISOU 2156 O ARG B1914 10316 8401 11349 -496 -970 -299 O ATOM 2157 CB ARG B1914 -27.195 4.070 -17.170 1.00 73.61 C ANISOU 2157 CB ARG B1914 9378 7805 10782 -578 -967 -173 C ATOM 2158 CG ARG B1914 -27.234 4.952 -15.930 1.00 74.65 C ANISOU 2158 CG ARG B1914 9740 7752 10868 -661 -1178 -205 C ATOM 2159 CD ARG B1914 -27.639 6.394 -16.206 1.00 74.20 C ANISOU 2159 CD ARG B1914 9860 7562 10769 -703 -1317 -216 C ATOM 2160 NE ARG B1914 -29.088 6.608 -16.150 1.00 73.08 N ANISOU 2160 NE ARG B1914 9874 7415 10477 -499 -1167 -387 N ATOM 2161 CZ ARG B1914 -29.912 6.767 -17.236 1.00 72.69 C ANISOU 2161 CZ ARG B1914 9704 7486 10427 -433 -1004 -416 C ATOM 2162 NH1 ARG B1914 -29.405 6.896 -18.456 1.00 70.83 N ANISOU 2162 NH1 ARG B1914 9272 7314 10326 -543 -990 -329 N ATOM 2163 NH2 ARG B1914 -31.232 6.739 -17.077 1.00 71.99 N ANISOU 2163 NH2 ARG B1914 9656 7508 10186 -245 -849 -485 N ATOM 2164 N HIS B1915 -28.562 1.364 -16.341 1.00 79.57 N ANISOU 2164 N HIS B1915 10369 8527 11335 -459 -773 -381 N ATOM 2165 CA HIS B1915 -29.480 0.703 -15.426 1.00 85.45 C ANISOU 2165 CA HIS B1915 11235 9258 11974 -514 -773 -423 C ATOM 2166 C HIS B1915 -28.798 -0.515 -14.799 1.00 85.33 C ANISOU 2166 C HIS B1915 11343 9162 11914 -495 -827 -423 C ATOM 2167 O HIS B1915 -28.921 -0.752 -13.596 1.00 84.38 O ANISOU 2167 O HIS B1915 11292 9017 11748 -531 -871 -436 O ATOM 2168 CB HIS B1915 -30.797 0.359 -16.127 1.00 91.08 C ANISOU 2168 CB HIS B1915 11944 10054 12606 -603 -722 -391 C ATOM 2169 CG HIS B1915 -31.720 1.527 -16.237 1.00 97.70 C ANISOU 2169 CG HIS B1915 12663 11032 13427 -568 -652 -370 C ATOM 2170 ND1 HIS B1915 -32.250 2.151 -15.121 1.00101.26 N ANISOU 2170 ND1 HIS B1915 13126 11574 13772 -457 -625 -356 N ATOM 2171 CD2 HIS B1915 -32.208 2.185 -17.313 1.00100.39 C ANISOU 2171 CD2 HIS B1915 12912 11437 13791 -558 -600 -358 C ATOM 2172 CE1 HIS B1915 -33.023 3.146 -15.507 1.00104.47 C ANISOU 2172 CE1 HIS B1915 13475 12104 14114 -335 -554 -333 C ATOM 2173 NE2 HIS B1915 -33.015 3.188 -16.849 1.00103.65 N ANISOU 2173 NE2 HIS B1915 13285 11985 14112 -429 -542 -335 N ATOM 2174 N LEU B1916 -28.056 -1.251 -15.628 1.00 86.41 N ANISOU 2174 N LEU B1916 11540 9266 12024 -375 -818 -403 N ATOM 2175 CA LEU B1916 -27.321 -2.424 -15.194 1.00 89.06 C ANISOU 2175 CA LEU B1916 12057 9519 12261 -254 -868 -401 C ATOM 2176 C LEU B1916 -26.228 -2.021 -14.201 1.00 90.59 C ANISOU 2176 C LEU B1916 12094 9776 12547 -211 -904 -340 C ATOM 2177 O LEU B1916 -26.197 -2.524 -13.078 1.00 92.38 O ANISOU 2177 O LEU B1916 12435 9926 12737 -259 -971 -374 O ATOM 2178 CB LEU B1916 -26.703 -3.122 -16.410 1.00 89.75 C ANISOU 2178 CB LEU B1916 12293 9591 12217 23 -826 -371 C ATOM 2179 CG LEU B1916 -27.686 -3.817 -17.351 1.00 87.64 C ANISOU 2179 CG LEU B1916 12360 9150 11787 -28 -893 -427 C ATOM 2180 CD1 LEU B1916 -26.945 -4.583 -18.433 1.00 87.50 C ANISOU 2180 CD1 LEU B1916 12649 9058 11539 378 -873 -417 C ATOM 2181 CD2 LEU B1916 -28.614 -4.744 -16.584 1.00 88.50 C ANISOU 2181 CD2 LEU B1916 12758 9079 11789 -302 -1074 -446 C ATOM 2182 N LEU B1917 -25.341 -1.117 -14.628 1.00 92.20 N ANISOU 2182 N LEU B1917 12038 10131 12860 -166 -895 -206 N ATOM 2183 CA LEU B1917 -24.096 -0.863 -13.907 1.00 94.23 C ANISOU 2183 CA LEU B1917 12122 10496 13184 -163 -993 -38 C ATOM 2184 C LEU B1917 -24.364 -0.132 -12.586 1.00 93.06 C ANISOU 2184 C LEU B1917 12062 10196 13097 -395 -1159 -97 C ATOM 2185 O LEU B1917 -23.486 -0.117 -11.740 1.00 91.56 O ANISOU 2185 O LEU B1917 11830 10020 12936 -445 -1297 17 O ATOM 2186 CB LEU B1917 -23.117 -0.093 -14.801 1.00 97.66 C ANISOU 2186 CB LEU B1917 12212 11198 13696 -129 -992 235 C ATOM 2187 CG LEU B1917 -22.492 -0.893 -15.952 1.00101.27 C ANISOU 2187 CG LEU B1917 12572 11895 14011 258 -807 371 C ATOM 2188 CD1 LEU B1917 -21.478 -0.050 -16.715 1.00102.48 C ANISOU 2188 CD1 LEU B1917 12274 12434 14230 275 -801 750 C ATOM 2189 CD2 LEU B1917 -21.834 -2.180 -15.458 1.00103.49 C ANISOU 2189 CD2 LEU B1917 12988 12214 14119 574 -766 396 C ATOM 2190 N GLN B1918 -25.570 0.428 -12.401 1.00 96.22 N ANISOU 2190 N GLN B1918 12612 10473 13472 -483 -1146 -251 N ATOM 2191 CA GLN B1918 -26.017 0.926 -11.078 1.00100.05 C ANISOU 2191 CA GLN B1918 13305 10811 13897 -546 -1259 -334 C ATOM 2192 C GLN B1918 -26.885 -0.141 -10.385 1.00100.98 C ANISOU 2192 C GLN B1918 13555 10918 13892 -496 -1155 -436 C ATOM 2193 O GLN B1918 -27.816 0.175 -9.647 1.00100.47 O ANISOU 2193 O GLN B1918 13614 10848 13710 -462 -1131 -489 O ATOM 2194 CB GLN B1918 -26.695 2.297 -11.208 1.00100.03 C ANISOU 2194 CB GLN B1918 13416 10734 13857 -560 -1314 -375 C ATOM 2195 CG GLN B1918 -28.151 2.272 -11.665 1.00 99.22 C ANISOU 2195 CG GLN B1918 13315 10727 13654 -456 -1116 -466 C ATOM 2196 CD GLN B1918 -28.710 3.663 -11.854 1.00100.74 C ANISOU 2196 CD GLN B1918 13648 10861 13768 -374 -1164 -495 C ATOM 2197 OE1 GLN B1918 -29.905 3.845 -12.083 1.00100.58 O ANISOU 2197 OE1 GLN B1918 13618 10970 13626 -235 -1011 -524 O ATOM 2198 NE2 GLN B1918 -27.850 4.666 -11.756 1.00 99.97 N ANISOU 2198 NE2 GLN B1918 13701 10575 13706 -467 -1415 -446 N ATOM 2199 N ARG B1919 -26.548 -1.413 -10.626 1.00104.91 N ANISOU 2199 N ARG B1919 14052 11434 14373 -463 -1112 -424 N ATOM 2200 CA ARG B1919 -27.031 -2.563 -9.862 1.00108.31 C ANISOU 2200 CA ARG B1919 14651 11814 14686 -490 -1113 -462 C ATOM 2201 C ARG B1919 -25.852 -3.532 -9.697 1.00108.56 C ANISOU 2201 C ARG B1919 14750 11790 14705 -381 -1170 -435 C ATOM 2202 O ARG B1919 -25.579 -4.337 -10.582 1.00107.90 O ANISOU 2202 O ARG B1919 14750 11695 14552 -252 -1140 -423 O ATOM 2203 CB ARG B1919 -28.208 -3.252 -10.567 1.00110.32 C ANISOU 2203 CB ARG B1919 14970 12102 14843 -584 -1062 -449 C ATOM 2204 CG ARG B1919 -29.433 -2.375 -10.794 1.00111.58 C ANISOU 2204 CG ARG B1919 14994 12416 14983 -645 -978 -410 C ATOM 2205 CD ARG B1919 -30.333 -2.930 -11.887 1.00112.66 C ANISOU 2205 CD ARG B1919 15136 12604 15063 -785 -977 -334 C ATOM 2206 NE ARG B1919 -30.886 -4.243 -11.568 1.00114.24 N ANISOU 2206 NE ARG B1919 15515 12763 15125 -993 -1107 -228 N ATOM 2207 CZ ARG B1919 -32.185 -4.522 -11.477 1.00116.07 C ANISOU 2207 CZ ARG B1919 15662 13191 15249 -1235 -1151 -17 C ATOM 2208 NH1 ARG B1919 -32.576 -5.715 -11.062 1.00116.12 N ANISOU 2208 NH1 ARG B1919 15851 13145 15121 -1499 -1342 136 N ATOM 2209 NH2 ARG B1919 -33.089 -3.612 -11.799 1.00116.12 N ANISOU 2209 NH2 ARG B1919 15392 13471 15255 -1222 -1028 90 N ATOM 2210 N SER B1920 -25.139 -3.418 -8.571 1.00110.83 N ANISOU 2210 N SER B1920 15045 12043 15020 -384 -1265 -414 N ATOM 2211 CA SER B1920 -23.893 -4.160 -8.335 1.00113.61 C ANISOU 2211 CA SER B1920 15390 12415 15359 -241 -1318 -335 C ATOM 2212 C SER B1920 -24.168 -5.668 -8.263 1.00115.65 C ANISOU 2212 C SER B1920 15945 12552 15444 -147 -1311 -409 C ATOM 2213 O SER B1920 -25.264 -6.103 -7.891 1.00116.55 O ANISOU 2213 O SER B1920 16244 12562 15476 -315 -1334 -478 O ATOM 2214 CB SER B1920 -23.203 -3.671 -7.086 1.00112.34 C ANISOU 2214 CB SER B1920 15199 12224 15259 -328 -1470 -278 C ATOM 2215 OG SER B1920 -23.059 -2.260 -7.110 1.00110.32 O ANISOU 2215 OG SER B1920 14831 11976 15107 -472 -1581 -205 O TER 2216 SER B1920 HETATM 2217 CA CA A1001 -5.325 -13.865 -42.202 1.00 55.81 CA HETATM 2218 CA CA A1002 -14.345 -13.925 -34.931 1.00 53.35 CA HETATM 2219 CA CA A1003 -32.626 19.891 -13.301 1.00 76.37 CA HETATM 2220 CA CA A1004 -37.278 23.250 -23.007 1.00 58.94 CA HETATM 2221 O HOH A1101 -15.482 -13.989 -36.577 1.00 40.90 O HETATM 2222 O HOH A1102 -43.219 9.490 -25.247 1.00 43.14 O HETATM 2223 O HOH A1103 -38.945 23.744 -21.413 1.00 56.31 O HETATM 2224 O HOH A1104 -2.202 -16.132 -39.230 1.00 38.57 O HETATM 2225 O HOH A1105 -5.701 -15.020 -33.465 1.00 50.31 O HETATM 2226 O HOH A1106 -31.356 21.438 -14.193 1.00 63.85 O HETATM 2227 O HOH A1107 -5.279 -15.530 -40.656 1.00 67.39 O HETATM 2228 O HOH A1108 -10.705 -18.238 -36.318 1.00 47.53 O HETATM 2229 O HOH A1109 -21.054 6.875 -29.381 1.00 48.25 O HETATM 2230 O HOH A1110 -38.341 29.644 -20.438 1.00 57.68 O HETATM 2231 O HOH A1111 7.432 4.616 -34.740 1.00 38.54 O HETATM 2232 O HOH A1112 -26.067 11.002 -35.965 1.00 52.30 O HETATM 2233 O HOH A1113 -32.960 10.939 -19.840 1.00 44.84 O HETATM 2234 O HOH B2001 -26.164 -1.234 -30.854 1.00 44.05 O HETATM 2235 O HOH B2002 -26.262 9.310 -58.425 1.00 65.62 O CONECT 163 2217 CONECT 180 2217 CONECT 192 2217 CONECT 201 2217 CONECT 243 2217 CONECT 244 2217 CONECT 444 2218 CONECT 457 2218 CONECT 469 2218 CONECT 478 2218 CONECT 523 2218 CONECT 524 2218 CONECT 744 2220 CONECT 761 2220 CONECT 773 2220 CONECT 782 2220 CONECT 822 2220 CONECT 823 2220 CONECT 1025 2219 CONECT 1042 2219 CONECT 1053 2219 CONECT 1062 2219 CONECT 1111 2219 CONECT 1112 2219 CONECT 2217 163 180 192 201 CONECT 2217 243 244 2227 CONECT 2218 444 457 469 478 CONECT 2218 523 524 2221 CONECT 2219 1025 1042 1053 1062 CONECT 2219 1111 1112 2226 CONECT 2220 744 761 773 782 CONECT 2220 822 823 2223 CONECT 2221 2218 CONECT 2223 2220 CONECT 2226 2219 CONECT 2227 2217 MASTER 529 0 4 14 6 0 8 6 2222 2 36 23 END
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Related entries of code: 6mud
Entries with 90% protein sequence similarity cutoff in PDBbind
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Protein Sequence Similarity
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PDBbind
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1xa5
RCSB PDB
PDBbind
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RCSB PDB
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PDBbind
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RCSB PDB
PDBbind
74aa, >1YRU_2|Chain... at 100%
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PDBbind
148aa, >2N27_1|Chain... at 100%
2wel
RCSB PDB
PDBbind
150aa, >2WEL_2|Chain... at 99%
3if7
RCSB PDB
PDBbind
148aa, >3IF7_1|Chain... at 100%
4byf
RCSB PDB
PDBbind
149aa, >4BYF_2|Chains... at 100%
4dck
RCSB PDB
PDBbind
149aa, >4DCK_2|Chain... at 100%
4ovn
RCSB PDB
PDBbind
149aa, >4OVN_1|Chains... at 100%
4r8g
RCSB PDB
PDBbind
148aa, >4R8G_2|Chains... at 100%
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RCSB PDB
PDBbind
147aa, >6PLM_2|Chains... at 99%
6o5g
RCSB PDB
PDBbind
152aa, >6O5G_1|Chain... at 100%
6mc9
RCSB PDB
PDBbind
149aa, >6MC9_2|Chain... at 100%
6mba
RCSB PDB
PDBbind
149aa, >6MBA_2|Chain... at 100%
6m7h
RCSB PDB
PDBbind
147aa, >6M7H_1|Chain... at 100%
6k4r
RCSB PDB
PDBbind
149aa, >6K4R_2|Chains... at 100%
6k4k
RCSB PDB
PDBbind
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RCSB PDB
PDBbind
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Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
No complexes with the same small molecule ligand are found!
Entry Information
PDB ID
6mud
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
Ca2+/ Calmodulin-1
Ligand Name
Sodium channel protein type 5 subunit alpha, NaV 1.5 (1786-1922)
EC.Number
E.C.-.-.-.-
Resolution
2.69(Å)
Affinity (Kd/Ki/IC50)
Kd=1.02uM
Release Year
2019
Protein/NA Sequence
Check fasta file
Primary Reference
(2019) Proc.Natl.Acad.Sci.USA Vol. 116: pp. 10763-10772
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q14524
P0DP23
Entrez Gene ID
NCBI Entrez Gene ID:
6331
801
805
808
ASD
Information of known allosteric effects of PDB entries
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