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*** d ***elNémo ID: 2402130202232571447Job options:ID = 2402130202232571447 JOBID = d USERID = unknown PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER d HEADER HYDROLASE 18-MAR-18 5ZJ2 TITLE CRYSTAL STRUCTURE OF NDM-1 IN COMPLEX WITH D-CAPTOPRIL COMPND MOL_ID: 1; COMPND 2 MOLECULE: METALLO-BETA-LACTAMASE TYPE 2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: B2 METALLO-BETA-LACTAMASE,BETA-LACTAMASE TYPE II,METALLO- COMPND 5 BETA-LACTAMASE NDM-1,METALLO-BETA-LACTAMASE TYPE II,NEW DELHI COMPND 6 METALLO-BETA-LACTAMASE-1,NDM-1; COMPND 7 EC: 3.5.2.6; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE; SOURCE 3 ORGANISM_TAXID: 573; SOURCE 4 GENE: BLANDM-1; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3); SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PRHISMBP KEYWDS NDM-1, METALLO-BETA-LACTAMASE, ANTIBIOTIC RESISTENT, INHIBITOR, THIO KEYWDS 2 COMPOUNDS, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR H.ZHANG,Q.HAO REVDAT 3 22-NOV-23 5ZJ2 1 REMARK REVDAT 2 16-DEC-20 5ZJ2 1 JRNL REVDAT 1 20-MAR-19 5ZJ2 0 JRNL AUTH G.MA,S.WANG,K.WU,W.ZHANG,A.AHMAD,Q.HAO,X.LEI,H.ZHANG JRNL TITL STRUCTURE-GUIDED OPTIMIZATION OF D-CAPTOPRIL FOR DISCOVERY JRNL TITL 2 OF POTENT NDM-1 INHIBITORS JRNL REF BIOORG.MED.CHEM. V. 29 2020 JRNL REFN ESSN 1464-3391 JRNL DOI 10.1016/J.BMC.2020.115902 REMARK 2 REMARK 2 RESOLUTION. 1.10 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 : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.10 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 27.95 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 93.2 REMARK 3 NUMBER OF REFLECTIONS : 73459 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) : 0.137 REMARK 3 R VALUE (WORKING SET) : 0.136 REMARK 3 FREE R VALUE : 0.162 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 3859 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.10 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.13 REMARK 3 REFLECTION IN BIN (WORKING SET) : 2846 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 49.11 REMARK 3 BIN R VALUE (WORKING SET) : 0.2150 REMARK 3 BIN FREE R VALUE SET COUNT : 155 REMARK 3 BIN FREE R VALUE : 0.2540 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1701 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 16 REMARK 3 SOLVENT ATOMS : 294 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 23.14 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.06000 REMARK 3 B22 (A**2) : -0.41000 REMARK 3 B33 (A**2) : 0.47000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.48000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.030 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.031 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.023 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.098 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.982 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.975 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1807 ; 0.008 ; 0.015 REMARK 3 BOND LENGTHS OTHERS (A): 1607 ; 0.001 ; 0.017 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2471 ; 1.516 ; 1.744 REMARK 3 BOND ANGLES OTHERS (DEGREES): 3761 ; 0.635 ; 1.722 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 243 ; 6.846 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 64 ;29.125 ;20.312 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 246 ;12.974 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;19.676 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 243 ; 0.355 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2106 ; 0.008 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): 338 ; 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): 3414 ; 3.302 ; 3.000 REMARK 3 SPHERICITY; FREE ATOMS (A**2): 185 ;28.713 ; 5.000 REMARK 3 SPHERICITY; BONDED ATOMS (A**2): 3477 ;10.601 ; 5.000 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 : 6 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 42 A 46 REMARK 3 ORIGIN FOR THE GROUP (A): 34.8039 33.9560 47.6209 REMARK 3 T TENSOR REMARK 3 T11: 0.4515 T22: 0.1835 REMARK 3 T33: 0.0584 T12: 0.0106 REMARK 3 T13: 0.0012 T23: 0.0248 REMARK 3 L TENSOR REMARK 3 L11: 7.0937 L22: 5.0821 REMARK 3 L33: 11.7400 L12: -5.1211 REMARK 3 L13: -8.5601 L23: 6.5297 REMARK 3 S TENSOR REMARK 3 S11: -0.4677 S12: 0.3816 S13: -0.4670 REMARK 3 S21: 1.0293 S22: -0.1613 S23: 0.3503 REMARK 3 S31: 0.4764 S32: -0.6020 S33: 0.6291 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 47 A 70 REMARK 3 ORIGIN FOR THE GROUP (A): 32.6730 34.1182 39.0774 REMARK 3 T TENSOR REMARK 3 T11: 0.0697 T22: 0.1187 REMARK 3 T33: 0.0609 T12: -0.0224 REMARK 3 T13: 0.0328 T23: -0.0415 REMARK 3 L TENSOR REMARK 3 L11: 1.4395 L22: 4.9999 REMARK 3 L33: 1.3049 L12: 0.7769 REMARK 3 L13: -0.5283 L23: 0.2724 REMARK 3 S TENSOR REMARK 3 S11: 0.0629 S12: -0.1459 S13: 0.1540 REMARK 3 S21: -0.0095 S22: -0.0790 S23: 0.2078 REMARK 3 S31: -0.1310 S32: -0.0067 S33: 0.0161 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 : A 71 A 210 REMARK 3 ORIGIN FOR THE GROUP (A): 35.7350 25.4835 28.2323 REMARK 3 T TENSOR REMARK 3 T11: 0.0397 T22: 0.0672 REMARK 3 T33: 0.0411 T12: 0.0112 REMARK 3 T13: 0.0163 T23: -0.0061 REMARK 3 L TENSOR REMARK 3 L11: 0.5003 L22: 1.8266 REMARK 3 L33: 1.4034 L12: 0.2637 REMARK 3 L13: -0.2756 L23: 0.0600 REMARK 3 S TENSOR REMARK 3 S11: 0.0070 S12: -0.0710 S13: -0.0178 REMARK 3 S21: -0.1563 S22: -0.1148 S23: 0.0398 REMARK 3 S31: 0.0531 S32: -0.0079 S33: 0.1078 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 : A 211 A 220 REMARK 3 ORIGIN FOR THE GROUP (A): 19.3646 40.2584 28.7574 REMARK 3 T TENSOR REMARK 3 T11: 0.5766 T22: 0.3679 REMARK 3 T33: 0.4510 T12: -0.1581 REMARK 3 T13: -0.0569 T23: -0.3366 REMARK 3 L TENSOR REMARK 3 L11: 2.7754 L22: 12.0908 REMARK 3 L33: 5.4900 L12: 3.1929 REMARK 3 L13: 2.3309 L23: -2.7188 REMARK 3 S TENSOR REMARK 3 S11: -0.8818 S12: -0.2760 S13: 0.8221 REMARK 3 S21: -0.5823 S22: 0.0880 S23: 0.6117 REMARK 3 S31: -1.1532 S32: -0.3532 S33: 0.7938 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 : A 221 A 265 REMARK 3 ORIGIN FOR THE GROUP (A): 19.1263 30.5510 26.0150 REMARK 3 T TENSOR REMARK 3 T11: 0.0245 T22: 0.1245 REMARK 3 T33: 0.2593 T12: 0.0052 REMARK 3 T13: -0.0663 T23: 0.0201 REMARK 3 L TENSOR REMARK 3 L11: 3.2500 L22: 1.2250 REMARK 3 L33: 1.1215 L12: -0.6225 REMARK 3 L13: -0.1934 L23: -0.1583 REMARK 3 S TENSOR REMARK 3 S11: 0.0822 S12: 0.1674 S13: 0.2550 REMARK 3 S21: -0.1698 S22: 0.0342 S23: 0.4545 REMARK 3 S31: 0.0070 S32: -0.2447 S33: -0.1164 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 : A 266 A 270 REMARK 3 ORIGIN FOR THE GROUP (A): 13.5337 37.8450 17.1572 REMARK 3 T TENSOR REMARK 3 T11: 0.3402 T22: 0.2362 REMARK 3 T33: 0.1832 T12: 0.1190 REMARK 3 T13: -0.0397 T23: 0.1600 REMARK 3 L TENSOR REMARK 3 L11: 12.2044 L22: 10.7042 REMARK 3 L33: 13.9088 L12: 6.6194 REMARK 3 L13: -6.2371 L23: -3.4949 REMARK 3 S TENSOR REMARK 3 S11: 0.0925 S12: 1.2293 S13: 0.9966 REMARK 3 S21: -0.8363 S22: 0.4669 S23: 0.4244 REMARK 3 S31: 0.0779 S32: -0.6374 S33: -0.5594 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK 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 5ZJ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-MAR-18. REMARK 100 THE DEPOSITION ID IS D_1300007166. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 27-JUN-16 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 5.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SSRF REMARK 200 BEAMLINE : BL17U1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97920 REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82705 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.100 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 4.800 REMARK 200 R MERGE (I) : 0.08000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 10.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.10 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.14 REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0 REMARK 200 DATA REDUNDANCY IN SHELL : 4.60 REMARK 200 R MERGE FOR SHELL (I) : 0.67100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: 3Q6X REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 39.53 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.03 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS PH5.5, 15% PEG3350, 20MM REMARK 280 L-PROLINE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 295K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z 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 29.94600 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 150 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 9750 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -56.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 GLY A 29 REMARK 465 GLU A 30 REMARK 465 ILE A 31 REMARK 465 ARG A 32 REMARK 465 PRO A 33 REMARK 465 THR A 34 REMARK 465 ILE A 35 REMARK 465 GLY A 36 REMARK 465 GLN A 37 REMARK 465 GLN A 38 REMARK 465 MET A 39 REMARK 465 GLU A 40 REMARK 465 THR A 41 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS REMARK 500 REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15 REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375 REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS. REMARK 500 REMARK 500 DISTANCE CUTOFF: REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE REMARK 500 OD1 ASP A 66 O HOH A 578 2757 2.05 REMARK 500 OD2 ASP A 66 O HOH A 574 2757 2.14 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASP A 90 142.48 76.30 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 52 0.10 SIDE CHAIN REMARK 500 ARG A 85 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH A 694 DISTANCE = 6.21 ANGSTROMS 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 ZN A 302 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 HIS A 120 NE2 REMARK 620 2 HIS A 122 ND1 99.0 REMARK 620 3 HIS A 189 NE2 101.3 114.9 REMARK 620 4 MCO A 303 S 136.1 109.0 96.7 REMARK 620 N 1 2 3 REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 ZN A 301 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 124 OD2 REMARK 620 2 CYS A 208 SG 111.0 REMARK 620 3 HIS A 250 NE2 91.4 104.6 REMARK 620 4 MCO A 303 S 117.5 112.0 118.3 REMARK 620 N 1 2 3 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 301 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 302 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: binding site for residue MCO A 303 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 5ZIO RELATED DB: PDB REMARK 900 NDM-1 IN COMPLEX WITH L-CAPTOPRIL REMARK 900 RELATED ID: 5ZJ1 RELATED DB: PDB REMARK 900 NDM-1 IN COMPLEX WITH D-CAPTOPRIL DERIVATIVE CYT-14 DBREF 5ZJ2 A 29 270 UNP C7C422 BLAN1_KLEPN 29 270 SEQRES 1 A 242 GLY GLU ILE ARG PRO THR ILE GLY GLN GLN MET GLU THR SEQRES 2 A 242 GLY ASP GLN ARG PHE GLY ASP LEU VAL PHE ARG GLN LEU SEQRES 3 A 242 ALA PRO ASN VAL TRP GLN HIS THR SER TYR LEU ASP MET SEQRES 4 A 242 PRO GLY PHE GLY ALA VAL ALA SER ASN GLY LEU ILE VAL SEQRES 5 A 242 ARG ASP GLY GLY ARG VAL LEU VAL VAL ASP THR ALA TRP SEQRES 6 A 242 THR ASP ASP GLN THR ALA GLN ILE LEU ASN TRP ILE LYS SEQRES 7 A 242 GLN GLU ILE ASN LEU PRO VAL ALA LEU ALA VAL VAL THR SEQRES 8 A 242 HIS ALA HIS GLN ASP LYS MET GLY GLY MET ASP ALA LEU SEQRES 9 A 242 HIS ALA ALA GLY ILE ALA THR TYR ALA ASN ALA LEU SER SEQRES 10 A 242 ASN GLN LEU ALA PRO GLN GLU GLY MET VAL ALA ALA GLN SEQRES 11 A 242 HIS SER LEU THR PHE ALA ALA ASN GLY TRP VAL GLU PRO SEQRES 12 A 242 ALA THR ALA PRO ASN PHE GLY PRO LEU LYS VAL PHE TYR SEQRES 13 A 242 PRO GLY PRO GLY HIS THR SER ASP ASN ILE THR VAL GLY SEQRES 14 A 242 ILE ASP GLY THR ASP ILE ALA PHE GLY GLY CYS LEU ILE SEQRES 15 A 242 LYS ASP SER LYS ALA LYS SER LEU GLY ASN LEU GLY ASP SEQRES 16 A 242 ALA ASP THR GLU HIS TYR ALA ALA SER ALA ARG ALA PHE SEQRES 17 A 242 GLY ALA ALA PHE PRO LYS ALA SER MET ILE VAL MET SER SEQRES 18 A 242 HIS SER ALA PRO ASP SER ARG ALA ALA ILE THR HIS THR SEQRES 19 A 242 ALA ARG MET ALA ASP LYS LEU ARG HET ZN A 301 1 HET ZN A 302 1 HET MCO A 303 14 HETNAM ZN ZINC ION HETNAM MCO 1-(3-MERCAPTO-2-METHYL-PROPIONYL)-PYRROLIDINE-2- HETNAM 2 MCO CARBOXYLIC ACID FORMUL 2 ZN 2(ZN 2+) FORMUL 4 MCO C9 H15 N O3 S FORMUL 5 HOH *294(H2 O) HELIX 1 AA1 THR A 94 ILE A 109 1 16 HELIX 2 AA2 HIS A 122 GLY A 127 1 6 HELIX 3 AA3 GLY A 128 ALA A 135 1 8 HELIX 4 AA4 ALA A 143 GLY A 153 1 11 HELIX 5 AA5 GLU A 170 ALA A 174 5 5 HELIX 6 AA6 CYS A 208 ILE A 210 5 3 HELIX 7 AA7 HIS A 228 PHE A 240 1 13 HELIX 8 AA8 ARG A 256 LYS A 268 1 13 SHEET 1 AA1 8 GLN A 44 PHE A 46 0 SHEET 2 AA1 8 LEU A 49 ALA A 55 -1 O LEU A 49 N PHE A 46 SHEET 3 AA1 8 VAL A 58 MET A 67 -1 O GLN A 60 N ARG A 52 SHEET 4 AA1 8 GLY A 71 ASP A 82 -1 O VAL A 73 N LEU A 65 SHEET 5 AA1 8 ARG A 85 VAL A 89 -1 O LEU A 87 N VAL A 80 SHEET 6 AA1 8 VAL A 113 VAL A 118 1 O VAL A 117 N VAL A 88 SHEET 7 AA1 8 ALA A 138 ASN A 142 1 O TYR A 140 N ALA A 116 SHEET 8 AA1 8 HIS A 159 LEU A 161 1 O LEU A 161 N ALA A 141 SHEET 1 AA2 4 LEU A 180 PHE A 183 0 SHEET 2 AA2 4 THR A 195 ILE A 198 -1 O GLY A 197 N LYS A 181 SHEET 3 AA2 4 ILE A 203 GLY A 207 -1 O PHE A 205 N VAL A 196 SHEET 4 AA2 4 MET A 245 MET A 248 1 O VAL A 247 N GLY A 206 LINK NE2 HIS A 120 ZN ZN A 302 1555 1555 2.05 LINK ND1 HIS A 122 ZN ZN A 302 1555 1555 2.07 LINK OD2 ASP A 124 ZN ZN A 301 1555 1555 1.92 LINK NE2 HIS A 189 ZN ZN A 302 1555 1555 2.04 LINK SG CYS A 208 ZN ZN A 301 1555 1555 2.29 LINK NE2 HIS A 250 ZN ZN A 301 1555 1555 2.06 LINK ZN ZN A 301 S MCO A 303 1555 1555 2.32 LINK ZN ZN A 302 S MCO A 303 1555 1555 2.32 SITE 1 AC1 5 ASP A 124 CYS A 208 HIS A 250 ZN A 302 SITE 2 AC1 5 MCO A 303 SITE 1 AC2 5 HIS A 120 HIS A 122 HIS A 189 ZN A 301 SITE 2 AC2 5 MCO A 303 SITE 1 AC3 15 PHE A 70 VAL A 73 TRP A 93 HIS A 122 SITE 2 AC3 15 ASP A 124 HIS A 189 GLY A 219 ASN A 220 SITE 3 AC3 15 HIS A 250 ZN A 301 ZN A 302 HOH A 405 SITE 4 AC3 15 HOH A 409 HOH A 412 HOH A 487 CRYST1 41.698 59.892 42.138 90.00 97.78 90.00 P 1 21 1 2 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 0.023982 0.000000 0.003277 0.00000 SCALE2 0.000000 0.016697 0.000000 0.00000 SCALE3 0.000000 0.000000 0.023952 0.00000 ATOM 1 N GLY A 42 27.999 30.252 49.961 1.00 57.11 N ANISOU 1 N GLY A 42 8728 6675 6293 -2346 4726 -2852 N ATOM 2 CA GLY A 42 27.552 31.452 49.189 1.00 53.88 C ANISOU 2 CA GLY A 42 7308 7335 5827 -2237 4197 -2928 C ATOM 3 C GLY A 42 28.611 31.902 48.197 1.00 48.79 C ANISOU 3 C GLY A 42 6148 6922 5466 -1768 3459 -2869 C ATOM 4 O GLY A 42 29.203 31.082 47.496 1.00 50.28 O ANISOU 4 O GLY A 42 6404 6974 5726 -1753 3610 -3013 O ATOM 5 N ASP A 43 28.851 33.202 48.108 1.00 43.98 N ANISOU 5 N ASP A 43 5665 6767 4279 -1431 2655 -2754 N ATOM 6 CA ASP A 43 29.981 33.643 47.305 1.00 38.04 C ANISOU 6 CA ASP A 43 5194 6154 3102 -1357 1895 -2524 C ATOM 7 C ASP A 43 31.242 33.529 48.171 1.00 35.75 C ANISOU 7 C ASP A 43 5610 5357 2616 -1166 1785 -1687 C ATOM 8 O ASP A 43 31.288 33.907 49.342 1.00 38.73 O ANISOU 8 O ASP A 43 6589 5315 2809 -630 1475 -2214 O ATOM 9 CB ASP A 43 29.771 35.053 46.744 1.00 39.20 C ANISOU 9 CB ASP A 43 5103 6685 3104 -957 1790 -2043 C ATOM 10 CG ASP A 43 28.714 35.159 45.650 1.00 43.20 C ANISOU 10 CG ASP A 43 4797 8011 3604 -713 1833 -2359 C ATOM 11 OD1 ASP A 43 28.364 34.118 45.058 1.00 45.44 O ANISOU 11 OD1 ASP A 43 4622 8504 4139 -908 2067 -3028 O ATOM 12 OD2 ASP A 43 28.263 36.301 45.400 1.00 47.83 O ANISOU 12 OD2 ASP A 43 4992 8671 4510 -415 1784 -1572 O ATOM 13 N GLN A 44 32.268 32.975 47.576 1.00 31.12 N ANISOU 13 N GLN A 44 5457 4325 2041 -1281 1433 -1316 N ATOM 14 CA GLN A 44 33.550 32.911 48.187 1.00 28.92 C ANISOU 14 CA GLN A 44 5744 3723 1519 -1016 1119 -656 C ATOM 15 C GLN A 44 34.503 33.817 47.406 1.00 25.28 C ANISOU 15 C GLN A 44 5142 3165 1296 -757 667 -545 C ATOM 16 O GLN A 44 34.762 33.568 46.231 1.00 24.74 O ANISOU 16 O GLN A 44 4680 3370 1349 -759 567 -683 O ATOM 17 CB GLN A 44 34.005 31.466 48.131 1.00 31.72 C ANISOU 17 CB GLN A 44 6093 3743 2213 -1104 1556 -613 C ATOM 18 CG GLN A 44 35.425 31.230 48.598 1.00 35.42 C ANISOU 18 CG GLN A 44 6386 4230 2841 -639 1332 -201 C ATOM 19 CD GLN A 44 35.616 29.750 48.810 1.00 40.89 C ANISOU 19 CD GLN A 44 7401 4458 3676 -179 1930 59 C ATOM 20 OE1 GLN A 44 36.659 29.188 48.499 1.00 45.13 O ANISOU 20 OE1 GLN A 44 8726 5558 2864 423 2773 235 O ATOM 21 NE2 GLN A 44 34.569 29.094 49.284 1.00 45.50 N ANISOU 21 NE2 GLN A 44 8459 5039 3788 -549 3063 -217 N ATOM 22 N ARG A 45 35.018 34.849 48.060 1.00 24.35 N ANISOU 22 N ARG A 45 5226 2901 1122 -553 469 -413 N ATOM 23 CA ARG A 45 35.952 35.780 47.424 1.00 23.12 C ANISOU 23 CA ARG A 45 4897 2646 1238 -371 268 -346 C ATOM 24 C ARG A 45 37.353 35.187 47.559 1.00 23.47 C ANISOU 24 C ARG A 45 4892 2691 1333 -295 95 -322 C ATOM 25 O ARG A 45 37.788 34.804 48.636 1.00 27.27 O ANISOU 25 O ARG A 45 5296 3605 1459 20 110 -123 O ATOM 26 CB ARG A 45 35.862 37.136 48.125 1.00 24.04 C ANISOU 26 CB ARG A 45 5080 2604 1449 -262 297 -346 C ATOM 27 CG ARG A 45 34.502 37.810 47.993 1.00 24.28 C ANISOU 27 CG ARG A 45 5105 2669 1449 -125 475 -374 C ATOM 28 CD ARG A 45 34.474 39.220 48.559 1.00 25.09 C ANISOU 28 CD ARG A 45 5419 2575 1538 -2 535 -258 C ATOM 29 NE ARG A 45 34.831 39.273 49.971 1.00 25.42 N ANISOU 29 NE ARG A 45 5746 2380 1532 -23 506 -221 N ATOM 30 CZ ARG A 45 33.964 39.222 50.978 1.00 26.17 C ANISOU 30 CZ ARG A 45 6021 2339 1583 1 649 -251 C ATOM 31 NH1 ARG A 45 32.674 39.055 50.742 1.00 28.25 N ANISOU 31 NH1 ARG A 45 5851 2700 2182 78 845 -170 N ATOM 32 NH2 ARG A 45 34.410 39.358 52.210 1.00 27.05 N ANISOU 32 NH2 ARG A 45 6491 2297 1488 7 609 -193 N ATOM 33 N PHE A 46 38.060 35.145 46.443 1.00 22.25 N ANISOU 33 N PHE A 46 4475 2605 1371 -174 -54 -323 N ATOM 34 CA PHE A 46 39.398 34.569 46.405 1.00 22.48 C ANISOU 34 CA PHE A 46 4441 2562 1536 -47 -228 -154 C ATOM 35 C PHE A 46 40.238 35.455 45.491 1.00 23.40 C ANISOU 35 C PHE A 46 4309 2637 1943 73 -203 165 C ATOM 36 O PHE A 46 40.008 35.446 44.278 1.00 22.61 O ANISOU 36 O PHE A 46 4124 2555 1911 -141 13 95 O ATOM 37 CB PHE A 46 39.347 33.124 45.916 1.00 22.65 C ANISOU 37 CB PHE A 46 4465 2545 1593 -97 -82 -131 C ATOM 38 CG PHE A 46 40.676 32.409 45.880 1.00 23.26 C ANISOU 38 CG PHE A 46 4523 2653 1659 25 -292 -166 C ATOM 39 CD1 PHE A 46 41.479 32.457 44.744 1.00 22.10 C ANISOU 39 CD1 PHE A 46 4131 2648 1618 -92 -446 -129 C ATOM 40 CD2 PHE A 46 41.120 31.686 46.973 1.00 26.38 C ANISOU 40 CD2 PHE A 46 5158 2984 1879 367 -224 0 C ATOM 41 CE1 PHE A 46 42.690 31.778 44.713 1.00 23.94 C ANISOU 41 CE1 PHE A 46 4271 2959 1864 91 -496 -187 C ATOM 42 CE2 PHE A 46 42.326 31.007 46.938 1.00 28.00 C ANISOU 42 CE2 PHE A 46 5325 3361 1953 621 -419 -45 C ATOM 43 CZ PHE A 46 43.114 31.066 45.813 1.00 26.30 C ANISOU 43 CZ PHE A 46 4847 3208 1936 447 -549 -184 C ATOM 44 N GLY A 47 41.132 36.251 46.079 1.00 23.48 N ANISOU 44 N GLY A 47 2800 3327 2794 -857 -226 -518 N ATOM 45 CA GLY A 47 41.664 37.400 45.394 1.00 24.06 C ANISOU 45 CA GLY A 47 2714 3406 3021 -643 -217 -230 C ATOM 46 C GLY A 47 40.544 38.220 44.795 1.00 22.46 C ANISOU 46 C GLY A 47 3001 3107 2424 -678 -201 -155 C ATOM 47 O GLY A 47 39.560 38.558 45.463 1.00 22.82 O ANISOU 47 O GLY A 47 3320 2885 2462 -654 -147 -208 O ATOM 48 N ASP A 48 40.665 38.482 43.503 1.00 20.02 N ANISOU 48 N ASP A 48 2568 2672 2364 -457 -76 -232 N ATOM 49 CA ASP A 48 39.743 39.350 42.775 1.00 17.85 C ANISOU 49 CA ASP A 48 2302 2466 2012 -441 250 -339 C ATOM 50 C ASP A 48 38.662 38.539 42.049 1.00 16.61 C ANISOU 50 C ASP A 48 2036 2373 1899 -252 324 -360 C ATOM 51 O ASP A 48 37.915 39.106 41.257 1.00 17.32 O ANISOU 51 O ASP A 48 2299 2403 1876 -156 249 -381 O ATOM 52 CB ASP A 48 40.497 40.244 41.789 1.00 18.03 C ANISOU 52 CB ASP A 48 2301 2514 2036 -367 335 -339 C ATOM 53 CG ASP A 48 39.767 41.541 41.505 1.00 18.60 C ANISOU 53 CG ASP A 48 2562 2550 1954 -235 373 -392 C ATOM 54 OD1 ASP A 48 39.311 42.189 42.481 1.00 19.63 O ANISOU 54 OD1 ASP A 48 2682 2777 2000 -203 575 -351 O ATOM 55 OD2 ASP A 48 39.692 41.917 40.311 1.00 19.60 O ANISOU 55 OD2 ASP A 48 2598 2892 1956 -86 628 -299 O ATOM 56 N LEU A 49 38.578 37.245 42.339 1.00 16.06 N ANISOU 56 N LEU A 49 2042 2400 1657 -395 370 -353 N ATOM 57 CA LEU A 49 37.580 36.349 41.734 1.00 15.88 C ANISOU 57 CA LEU A 49 2103 2395 1535 -374 457 -383 C ATOM 58 C LEU A 49 36.557 35.934 42.786 1.00 16.16 C ANISOU 58 C LEU A 49 2242 2501 1395 -455 441 -394 C ATOM 59 O LEU A 49 36.762 36.103 43.995 1.00 16.56 O ANISOU 59 O LEU A 49 2306 2643 1340 -436 436 -358 O ATOM 60 CB LEU A 49 38.274 35.122 41.136 1.00 16.93 C ANISOU 60 CB LEU A 49 2065 2460 1906 -349 593 -386 C ATOM 61 CG LEU A 49 38.997 35.376 39.790 1.00 18.57 C ANISOU 61 CG LEU A 49 2330 2639 2087 -354 765 -312 C ATOM 62 CD1 LEU A 49 40.325 36.074 39.978 1.00 20.44 C ANISOU 62 CD1 LEU A 49 2556 2786 2424 -525 796 -345 C ATOM 63 CD2 LEU A 49 39.191 34.096 39.010 1.00 19.77 C ANISOU 63 CD2 LEU A 49 2468 2820 2223 -288 755 -402 C ATOM 64 N VAL A 50 35.453 35.373 42.310 1.00 15.90 N ANISOU 64 N VAL A 50 2109 2610 1323 -424 517 -402 N ATOM 65 CA VAL A 50 34.403 34.854 43.161 1.00 15.99 C ANISOU 65 CA VAL A 50 2326 2552 1196 -407 601 -373 C ATOM 66 C VAL A 50 34.075 33.422 42.734 1.00 16.40 C ANISOU 66 C VAL A 50 2412 2560 1258 -344 494 -425 C ATOM 67 O VAL A 50 33.984 33.143 41.545 1.00 16.32 O ANISOU 67 O VAL A 50 2276 2663 1262 -489 520 -427 O ATOM 68 CB VAL A 50 33.168 35.775 43.135 1.00 17.28 C ANISOU 68 CB VAL A 50 2346 2715 1503 -283 682 -583 C ATOM 69 CG1 VAL A 50 32.006 35.169 43.912 1.00 19.72 C ANISOU 69 CG1 VAL A 50 2477 2930 2083 -440 748 -376 C ATOM 70 CG2 VAL A 50 33.497 37.179 43.625 1.00 18.80 C ANISOU 70 CG2 VAL A 50 2564 2856 1720 -343 676 -720 C ATOM 71 N PHE A 51 33.903 32.543 43.724 1.00 16.57 N ANISOU 71 N PHE A 51 2394 2611 1290 -517 597 -424 N ATOM 72 CA PHE A 51 33.550 31.141 43.463 1.00 16.64 C ANISOU 72 CA PHE A 51 2367 2580 1372 -523 672 -327 C ATOM 73 C PHE A 51 32.271 30.811 44.230 1.00 17.24 C ANISOU 73 C PHE A 51 2461 2721 1368 -539 732 -438 C ATOM 74 O PHE A 51 32.128 31.213 45.377 1.00 19.41 O ANISOU 74 O PHE A 51 3003 3009 1363 -704 864 -495 O ATOM 75 CB PHE A 51 34.689 30.219 43.895 1.00 16.90 C ANISOU 75 CB PHE A 51 2403 2639 1378 -636 476 -182 C ATOM 76 CG PHE A 51 35.956 30.476 43.134 1.00 16.86 C ANISOU 76 CG PHE A 51 2357 2682 1365 -401 521 -207 C ATOM 77 CD1 PHE A 51 36.812 31.505 43.493 1.00 17.82 C ANISOU 77 CD1 PHE A 51 2534 2809 1426 -441 418 -329 C ATOM 78 CD2 PHE A 51 36.254 29.734 41.999 1.00 17.04 C ANISOU 78 CD2 PHE A 51 2455 2558 1459 -281 451 -216 C ATOM 79 CE1 PHE A 51 37.951 31.760 42.735 1.00 17.75 C ANISOU 79 CE1 PHE A 51 2327 3004 1412 -537 246 -332 C ATOM 80 CE2 PHE A 51 37.389 29.997 41.258 1.00 17.12 C ANISOU 80 CE2 PHE A 51 2226 2832 1444 -131 371 -288 C ATOM 81 CZ PHE A 51 38.228 31.008 41.619 1.00 17.56 C ANISOU 81 CZ PHE A 51 2193 2946 1533 -220 283 -267 C ATOM 82 N AARG A 52 31.350 30.078 43.602 0.50 17.13 N ANISOU 82 N AARG A 52 2354 2711 1441 -575 869 -429 N ATOM 83 N BARG A 52 31.371 30.076 43.584 0.50 17.03 N ANISOU 83 N BARG A 52 2359 2692 1418 -581 848 -399 N ATOM 84 CA AARG A 52 30.068 29.754 44.237 0.50 18.07 C ANISOU 84 CA AARG A 52 2440 2802 1623 -511 1072 -461 C ATOM 85 CA BARG A 52 30.095 29.725 44.179 0.50 17.88 C ANISOU 85 CA BARG A 52 2398 2742 1651 -530 1006 -397 C ATOM 86 C AARG A 52 29.734 28.294 43.929 0.50 17.35 C ANISOU 86 C AARG A 52 2277 2757 1555 -470 954 -403 C ATOM 87 C BARG A 52 29.865 28.238 43.922 0.50 17.38 C ANISOU 87 C BARG A 52 2292 2714 1598 -512 890 -356 C ATOM 88 O AARG A 52 29.620 27.912 42.763 0.50 16.04 O ANISOU 88 O AARG A 52 1811 2691 1592 -448 962 -450 O ATOM 89 O BARG A 52 30.008 27.771 42.791 0.50 16.06 O ANISOU 89 O BARG A 52 2228 2340 1534 -415 714 -246 O ATOM 90 CB AARG A 52 28.963 30.683 43.721 0.50 20.52 C ANISOU 90 CB AARG A 52 2633 2960 2201 -186 1083 -625 C ATOM 91 CB BARG A 52 28.980 30.572 43.560 0.50 18.99 C ANISOU 91 CB BARG A 52 2291 2864 2058 -368 1102 -468 C ATOM 92 CG AARG A 52 27.587 30.385 44.301 0.50 23.25 C ANISOU 92 CG AARG A 52 2775 3378 2679 -65 1343 -713 C ATOM 93 CG BARG A 52 27.593 30.190 44.048 0.50 21.28 C ANISOU 93 CG BARG A 52 2373 3185 2527 -421 1225 -497 C ATOM 94 CD AARG A 52 26.460 31.227 43.717 0.50 27.39 C ANISOU 94 CD AARG A 52 3031 3876 3500 67 929 -538 C ATOM 95 CD BARG A 52 26.467 30.992 43.419 0.50 22.39 C ANISOU 95 CD BARG A 52 2124 3408 2973 -388 1089 -685 C ATOM 96 NE AARG A 52 25.179 30.529 43.613 0.50 30.94 N ANISOU 96 NE AARG A 52 3254 4244 4257 -153 767 -331 N ATOM 97 NE BARG A 52 26.490 32.376 43.886 0.50 24.12 N ANISOU 97 NE BARG A 52 2509 3387 3268 -553 1009 -671 N ATOM 98 CZ AARG A 52 24.117 30.994 42.955 0.50 31.46 C ANISOU 98 CZ AARG A 52 3038 4387 4525 133 965 -485 C ATOM 99 CZ BARG A 52 25.607 33.312 43.542 0.50 25.70 C ANISOU 99 CZ BARG A 52 2468 3718 3577 -426 1125 -549 C ATOM 100 NH1AARG A 52 24.027 32.281 42.671 0.50 32.41 N ANISOU 100 NH1AARG A 52 3399 4404 4510 77 789 -488 N ATOM 101 NH1BARG A 52 24.560 33.005 42.795 0.50 27.51 N ANISOU 101 NH1BARG A 52 2628 4114 3711 -573 1003 -565 N ATOM 102 NH2AARG A 52 23.168 30.168 42.544 0.50 29.69 N ANISOU 102 NH2AARG A 52 2842 4375 4064 219 1158 -525 N ATOM 103 NH2BARG A 52 25.782 34.560 43.936 0.50 28.23 N ANISOU 103 NH2BARG A 52 2888 3694 4142 -342 1063 -641 N ATOM 104 N GLN A 53 29.564 27.484 44.971 1.00 18.27 N ANISOU 104 N GLN A 53 2593 2732 1615 -548 1005 -381 N ATOM 105 CA GLN A 53 29.204 26.097 44.786 1.00 18.11 C ANISOU 105 CA GLN A 53 2487 2664 1728 -431 1031 -348 C ATOM 106 C GLN A 53 27.760 26.022 44.300 1.00 18.21 C ANISOU 106 C GLN A 53 2356 2618 1942 -457 1187 -393 C ATOM 107 O GLN A 53 26.870 26.616 44.928 1.00 22.11 O ANISOU 107 O GLN A 53 2704 3282 2411 -324 1479 -711 O ATOM 108 CB GLN A 53 29.392 25.295 46.067 1.00 20.70 C ANISOU 108 CB GLN A 53 3091 3112 1661 -617 1028 -225 C ATOM 109 CG GLN A 53 29.288 23.803 45.806 1.00 21.65 C ANISOU 109 CG GLN A 53 3249 3061 1914 -661 884 -21 C ATOM 110 CD GLN A 53 29.787 22.952 46.944 1.00 24.18 C ANISOU 110 CD GLN A 53 3859 3460 1867 -639 982 225 C ATOM 111 OE1 GLN A 53 29.859 23.388 48.091 1.00 29.58 O ANISOU 111 OE1 GLN A 53 5279 3827 2132 -540 493 -33 O ATOM 112 NE2 GLN A 53 30.047 21.688 46.648 1.00 26.24 N ANISOU 112 NE2 GLN A 53 4029 3401 2540 -525 656 335 N ATOM 113 N LEU A 54 27.542 25.279 43.219 1.00 17.72 N ANISOU 113 N LEU A 54 2303 2485 1945 -350 1027 -304 N ATOM 114 CA LEU A 54 26.198 25.100 42.657 1.00 18.55 C ANISOU 114 CA LEU A 54 2177 2664 2204 -295 1050 -345 C ATOM 115 C LEU A 54 25.613 23.710 42.930 1.00 19.66 C ANISOU 115 C LEU A 54 1969 2740 2758 -281 1124 -187 C ATOM 116 O LEU A 54 24.399 23.555 42.886 1.00 22.43 O ANISOU 116 O LEU A 54 2013 3041 3465 -485 1108 3 O ATOM 117 CB LEU A 54 26.237 25.318 41.149 1.00 18.70 C ANISOU 117 CB LEU A 54 2058 2816 2231 -416 779 -265 C ATOM 118 CG LEU A 54 26.771 26.665 40.676 1.00 19.01 C ANISOU 118 CG LEU A 54 2083 2838 2299 -494 558 -176 C ATOM 119 CD1 LEU A 54 26.621 26.766 39.170 1.00 18.43 C ANISOU 119 CD1 LEU A 54 1610 3050 2341 -610 456 -138 C ATOM 120 CD2 LEU A 54 26.044 27.815 41.343 1.00 21.29 C ANISOU 120 CD2 LEU A 54 2647 2787 2652 -268 484 -190 C ATOM 121 N ALA A 55 26.469 22.724 43.133 1.00 18.95 N ANISOU 121 N ALA A 55 2208 2633 2359 -234 1159 -201 N ATOM 122 CA ALA A 55 26.077 21.342 43.334 1.00 20.10 C ANISOU 122 CA ALA A 55 2383 2737 2515 -419 1232 -141 C ATOM 123 C ALA A 55 27.242 20.642 44.024 1.00 19.37 C ANISOU 123 C ALA A 55 2587 2514 2258 -269 1321 -173 C ATOM 124 O ALA A 55 28.320 21.205 44.061 1.00 19.13 O ANISOU 124 O ALA A 55 2532 2842 1893 -325 965 -14 O ATOM 125 CB ALA A 55 25.743 20.681 42.014 1.00 20.96 C ANISOU 125 CB ALA A 55 2458 2688 2817 -594 859 -114 C ATOM 126 N PRO A 56 27.059 19.416 44.511 1.00 20.62 N ANISOU 126 N PRO A 56 2742 2812 2278 -422 1388 194 N ATOM 127 CA PRO A 56 28.173 18.758 45.244 1.00 22.25 C ANISOU 127 CA PRO A 56 3006 2987 2458 -294 1299 311 C ATOM 128 C PRO A 56 29.548 18.758 44.561 1.00 21.55 C ANISOU 128 C PRO A 56 2919 3147 2119 -257 1068 234 C ATOM 129 O PRO A 56 30.577 18.913 45.212 1.00 22.71 O ANISOU 129 O PRO A 56 3257 3179 2191 -219 784 44 O ATOM 130 CB PRO A 56 27.597 17.347 45.485 1.00 23.54 C ANISOU 130 CB PRO A 56 3241 3022 2679 -340 1534 497 C ATOM 131 CG PRO A 56 26.107 17.593 45.676 1.00 24.71 C ANISOU 131 CG PRO A 56 3241 3034 3112 -454 1620 349 C ATOM 132 CD PRO A 56 25.805 18.660 44.651 1.00 22.63 C ANISOU 132 CD PRO A 56 2930 2793 2874 -514 1575 104 C ATOM 133 N ASN A 57 29.539 18.633 43.251 1.00 19.49 N ANISOU 133 N ASN A 57 2903 2511 1989 -132 1167 325 N ATOM 134 CA ASN A 57 30.778 18.526 42.438 1.00 17.76 C ANISOU 134 CA ASN A 57 2578 2445 1724 -191 922 205 C ATOM 135 C ASN A 57 30.891 19.669 41.414 1.00 16.13 C ANISOU 135 C ASN A 57 2219 2345 1563 -229 753 76 C ATOM 136 O ASN A 57 31.657 19.532 40.448 1.00 15.97 O ANISOU 136 O ASN A 57 1975 2341 1749 -84 784 77 O ATOM 137 CB ASN A 57 30.802 17.174 41.715 1.00 17.64 C ANISOU 137 CB ASN A 57 2479 2339 1883 -128 922 247 C ATOM 138 CG ASN A 57 31.036 15.960 42.592 1.00 19.66 C ANISOU 138 CG ASN A 57 2862 2488 2118 17 940 400 C ATOM 139 OD1 ASN A 57 30.628 15.932 43.740 1.00 21.69 O ANISOU 139 OD1 ASN A 57 3279 2914 2046 315 857 548 O ATOM 140 ND2 ASN A 57 31.679 14.935 42.056 1.00 20.73 N ANISOU 140 ND2 ASN A 57 3028 2496 2352 184 758 356 N ATOM 141 N VAL A 58 30.157 20.769 41.577 1.00 15.39 N ANISOU 141 N VAL A 58 1817 2412 1616 -316 734 27 N ATOM 142 CA VAL A 58 30.140 21.852 40.569 1.00 14.88 C ANISOU 142 CA VAL A 58 1788 2219 1646 -158 616 -95 C ATOM 143 C VAL A 58 30.237 23.214 41.254 1.00 14.54 C ANISOU 143 C VAL A 58 1684 2341 1499 -212 671 -152 C ATOM 144 O VAL A 58 29.455 23.513 42.173 1.00 15.62 O ANISOU 144 O VAL A 58 1918 2418 1598 -266 859 -149 O ATOM 145 CB VAL A 58 28.876 21.817 39.691 1.00 15.54 C ANISOU 145 CB VAL A 58 1739 2393 1772 -191 642 -199 C ATOM 146 CG1 VAL A 58 28.953 22.885 38.597 1.00 15.74 C ANISOU 146 CG1 VAL A 58 1945 2323 1712 -129 383 -247 C ATOM 147 CG2 VAL A 58 28.685 20.435 39.071 1.00 16.25 C ANISOU 147 CG2 VAL A 58 1919 2428 1827 -276 570 -216 C ATOM 148 N TRP A 59 31.142 24.047 40.736 1.00 14.64 N ANISOU 148 N TRP A 59 1652 2456 1454 -325 658 -246 N ATOM 149 CA TRP A 59 31.306 25.415 41.193 1.00 14.97 C ANISOU 149 CA TRP A 59 1862 2464 1361 -346 764 -173 C ATOM 150 C TRP A 59 31.301 26.354 39.993 1.00 14.48 C ANISOU 150 C TRP A 59 1729 2386 1386 -235 598 -216 C ATOM 151 O TRP A 59 31.773 25.983 38.916 1.00 15.01 O ANISOU 151 O TRP A 59 1980 2281 1439 -96 705 -181 O ATOM 152 CB TRP A 59 32.614 25.582 41.949 1.00 15.87 C ANISOU 152 CB TRP A 59 1920 2587 1522 -519 652 -171 C ATOM 153 CG TRP A 59 32.753 24.730 43.170 1.00 17.34 C ANISOU 153 CG TRP A 59 2148 2934 1504 -418 617 -122 C ATOM 154 CD1 TRP A 59 32.627 25.148 44.456 1.00 19.39 C ANISOU 154 CD1 TRP A 59 2472 3432 1463 -409 526 -89 C ATOM 155 CD2 TRP A 59 33.120 23.341 43.231 1.00 17.97 C ANISOU 155 CD2 TRP A 59 2180 2905 1740 -516 407 115 C ATOM 156 NE1 TRP A 59 32.836 24.109 45.319 1.00 20.73 N ANISOU 156 NE1 TRP A 59 2664 3754 1457 -238 634 112 N ATOM 157 CE2 TRP A 59 33.174 22.995 44.599 1.00 20.39 C ANISOU 157 CE2 TRP A 59 2667 3343 1737 -461 603 189 C ATOM 158 CE3 TRP A 59 33.446 22.370 42.271 1.00 18.05 C ANISOU 158 CE3 TRP A 59 1961 2884 2010 -390 578 118 C ATOM 159 CZ2 TRP A 59 33.497 21.707 45.021 1.00 23.16 C ANISOU 159 CZ2 TRP A 59 3072 3417 2308 -350 520 375 C ATOM 160 CZ3 TRP A 59 33.770 21.099 42.695 1.00 21.08 C ANISOU 160 CZ3 TRP A 59 2521 2904 2582 -334 242 161 C ATOM 161 CH2 TRP A 59 33.811 20.782 44.053 1.00 22.62 C ANISOU 161 CH2 TRP A 59 2941 3045 2608 -452 473 382 C ATOM 162 N GLN A 60 30.805 27.569 40.228 1.00 15.04 N ANISOU 162 N GLN A 60 1891 2306 1516 -288 687 -274 N ATOM 163 CA GLN A 60 30.893 28.647 39.266 1.00 14.21 C ANISOU 163 CA GLN A 60 1727 2216 1454 -208 549 -345 C ATOM 164 C GLN A 60 32.105 29.512 39.594 1.00 13.79 C ANISOU 164 C GLN A 60 1745 2186 1307 -240 564 -293 C ATOM 165 O GLN A 60 32.221 29.960 40.754 1.00 15.07 O ANISOU 165 O GLN A 60 1879 2488 1359 -402 671 -385 O ATOM 166 CB GLN A 60 29.601 29.459 39.302 1.00 14.83 C ANISOU 166 CB GLN A 60 1763 2271 1601 -153 651 -343 C ATOM 167 CG GLN A 60 29.530 30.538 38.257 1.00 14.80 C ANISOU 167 CG GLN A 60 1536 2264 1821 -159 526 -255 C ATOM 168 CD GLN A 60 28.263 31.347 38.356 1.00 15.78 C ANISOU 168 CD GLN A 60 1536 2436 2021 -117 573 -416 C ATOM 169 OE1 GLN A 60 27.368 31.225 37.525 1.00 18.30 O ANISOU 169 OE1 GLN A 60 1672 3076 2202 20 502 -621 O ATOM 170 NE2 GLN A 60 28.154 32.128 39.428 1.00 17.31 N ANISOU 170 NE2 GLN A 60 1869 2546 2160 -69 729 -505 N ATOM 171 N HIS A 61 32.935 29.804 38.586 1.00 13.57 N ANISOU 171 N HIS A 61 1626 2176 1353 -210 568 -262 N ATOM 172 CA HIS A 61 34.018 30.786 38.761 1.00 13.43 C ANISOU 172 CA HIS A 61 1626 2251 1222 -241 471 -280 C ATOM 173 C HIS A 61 33.571 32.098 38.125 1.00 13.34 C ANISOU 173 C HIS A 61 1563 2161 1344 -263 472 -351 C ATOM 174 O HIS A 61 32.939 32.079 37.066 1.00 13.66 O ANISOU 174 O HIS A 61 1685 2079 1424 -81 368 -347 O ATOM 175 CB HIS A 61 35.351 30.277 38.180 1.00 13.24 C ANISOU 175 CB HIS A 61 1541 2226 1262 -94 273 -236 C ATOM 176 CG HIS A 61 35.475 30.043 36.705 1.00 12.55 C ANISOU 176 CG HIS A 61 1359 2145 1265 -216 402 -142 C ATOM 177 ND1 HIS A 61 35.623 31.060 35.799 1.00 12.72 N ANISOU 177 ND1 HIS A 61 1415 2144 1273 -146 397 -154 N ATOM 178 CD2 HIS A 61 35.594 28.881 36.014 1.00 12.52 C ANISOU 178 CD2 HIS A 61 1375 2130 1248 -216 343 -44 C ATOM 179 CE1 HIS A 61 35.838 30.508 34.598 1.00 12.34 C ANISOU 179 CE1 HIS A 61 1286 2066 1334 -100 314 -247 C ATOM 180 NE2 HIS A 61 35.815 29.184 34.698 1.00 12.74 N ANISOU 180 NE2 HIS A 61 1442 2156 1240 -138 362 -50 N ATOM 181 N THR A 62 33.938 33.217 38.746 1.00 13.73 N ANISOU 181 N THR A 62 1675 2209 1331 -213 435 -395 N ATOM 182 CA THR A 62 33.563 34.505 38.245 1.00 13.87 C ANISOU 182 CA THR A 62 1732 2203 1333 -221 490 -378 C ATOM 183 C THR A 62 34.772 35.438 38.303 1.00 14.31 C ANISOU 183 C THR A 62 1723 2361 1351 -274 497 -457 C ATOM 184 O THR A 62 35.440 35.527 39.346 1.00 15.62 O ANISOU 184 O THR A 62 2081 2476 1375 -485 377 -363 O ATOM 185 CB THR A 62 32.437 35.150 39.061 1.00 15.05 C ANISOU 185 CB THR A 62 1782 2419 1518 -262 560 -487 C ATOM 186 OG1 THR A 62 31.335 34.249 39.101 1.00 15.72 O ANISOU 186 OG1 THR A 62 1814 2320 1838 -218 665 -402 O ATOM 187 CG2 THR A 62 32.022 36.489 38.505 1.00 15.85 C ANISOU 187 CG2 THR A 62 1796 2380 1845 -126 545 -615 C ATOM 188 N SER A 63 35.033 36.124 37.178 1.00 14.01 N ANISOU 188 N SER A 63 1691 2214 1418 -287 386 -404 N ATOM 189 CA SER A 63 36.155 37.038 37.051 1.00 14.70 C ANISOU 189 CA SER A 63 1749 2234 1603 -327 353 -474 C ATOM 190 C SER A 63 35.637 38.327 36.411 1.00 14.69 C ANISOU 190 C SER A 63 1828 2134 1617 -327 568 -434 C ATOM 191 O SER A 63 34.576 38.333 35.763 1.00 14.99 O ANISOU 191 O SER A 63 1918 2048 1730 -125 456 -515 O ATOM 192 CB SER A 63 37.287 36.416 36.250 1.00 14.39 C ANISOU 192 CB SER A 63 1789 2095 1582 -305 420 -311 C ATOM 193 OG SER A 63 36.877 36.088 34.923 1.00 14.02 O ANISOU 193 OG SER A 63 1682 2132 1511 -162 475 -349 O ATOM 194 N TYR A 64 36.385 39.409 36.580 1.00 15.85 N ANISOU 194 N TYR A 64 2056 2123 1840 -336 464 -632 N ATOM 195 CA TYR A 64 35.913 40.738 36.221 1.00 16.31 C ANISOU 195 CA TYR A 64 2288 2078 1828 -340 599 -589 C ATOM 196 C TYR A 64 36.932 41.460 35.354 1.00 16.95 C ANISOU 196 C TYR A 64 2280 2064 2094 -429 596 -586 C ATOM 197 O TYR A 64 38.139 41.389 35.620 1.00 18.12 O ANISOU 197 O TYR A 64 2262 2393 2228 -529 522 -599 O ATOM 198 CB TYR A 64 35.693 41.605 37.472 1.00 17.68 C ANISOU 198 CB TYR A 64 2568 2083 2064 -446 629 -743 C ATOM 199 CG TYR A 64 34.639 41.061 38.389 1.00 17.66 C ANISOU 199 CG TYR A 64 2518 2330 1859 -408 682 -880 C ATOM 200 CD1 TYR A 64 34.935 40.058 39.304 1.00 19.86 C ANISOU 200 CD1 TYR A 64 3031 2527 1988 -489 568 -724 C ATOM 201 CD2 TYR A 64 33.324 41.469 38.258 1.00 19.99 C ANISOU 201 CD2 TYR A 64 2570 2927 2097 -288 599 -999 C ATOM 202 CE1 TYR A 64 33.936 39.465 40.053 1.00 21.86 C ANISOU 202 CE1 TYR A 64 3454 2815 2036 -683 838 -834 C ATOM 203 CE2 TYR A 64 32.323 40.909 39.023 1.00 21.59 C ANISOU 203 CE2 TYR A 64 2788 3051 2361 -632 745 -1294 C ATOM 204 CZ TYR A 64 32.631 39.892 39.900 1.00 22.00 C ANISOU 204 CZ TYR A 64 3089 2788 2481 -1027 1047 -1084 C ATOM 205 OH TYR A 64 31.625 39.352 40.640 1.00 29.34 O ANISOU 205 OH TYR A 64 4460 3828 2860 -1932 1825 -1434 O ATOM 206 N LEU A 65 36.428 42.206 34.377 1.00 17.55 N ANISOU 206 N LEU A 65 2438 2031 2199 -301 669 -477 N ATOM 207 CA LEU A 65 37.266 43.067 33.547 1.00 19.17 C ANISOU 207 CA LEU A 65 2869 2123 2290 -383 936 -520 C ATOM 208 C LEU A 65 36.544 44.384 33.257 1.00 20.46 C ANISOU 208 C LEU A 65 2918 2002 2852 -413 1156 -475 C ATOM 209 O LEU A 65 35.358 44.407 32.898 1.00 22.16 O ANISOU 209 O LEU A 65 2964 2208 3245 -152 1030 -273 O ATOM 210 CB LEU A 65 37.602 42.388 32.215 1.00 19.56 C ANISOU 210 CB LEU A 65 3153 2080 2198 -402 874 -488 C ATOM 211 CG LEU A 65 38.637 43.138 31.391 1.00 21.97 C ANISOU 211 CG LEU A 65 3482 2456 2407 -545 1139 -547 C ATOM 212 CD1 LEU A 65 40.025 42.959 31.978 1.00 23.67 C ANISOU 212 CD1 LEU A 65 3332 3018 2644 -439 1268 -679 C ATOM 213 CD2 LEU A 65 38.627 42.677 29.958 1.00 23.27 C ANISOU 213 CD2 LEU A 65 4028 2476 2336 -532 1208 -446 C ATOM 214 N ASP A 66 37.282 45.477 33.389 1.00 23.47 N ANISOU 214 N ASP A 66 3273 2184 3460 -618 1301 -717 N ATOM 215 CA AASP A 66 36.762 46.780 32.989 0.50 24.67 C ANISOU 215 CA AASP A 66 3986 2248 3137 -544 1473 -536 C ATOM 216 CA BASP A 66 36.795 46.798 32.982 0.50 25.85 C ANISOU 216 CA BASP A 66 4166 2394 3259 -420 1385 -530 C ATOM 217 C ASP A 66 36.476 46.787 31.482 1.00 26.97 C ANISOU 217 C ASP A 66 4551 2596 3099 -314 1597 -522 C ATOM 218 O ASP A 66 37.325 46.421 30.670 1.00 28.68 O ANISOU 218 O ASP A 66 4725 2821 3348 -254 1847 -431 O ATOM 219 CB AASP A 66 37.716 47.917 33.357 0.50 24.78 C ANISOU 219 CB AASP A 66 4081 2259 3074 -639 1616 -536 C ATOM 220 CB BASP A 66 37.819 47.894 33.293 0.50 29.95 C ANISOU 220 CB BASP A 66 4447 2780 4151 -754 1428 -599 C ATOM 221 CG AASP A 66 37.165 49.271 32.957 0.50 25.21 C ANISOU 221 CG AASP A 66 4357 2193 3026 -659 1588 -514 C ATOM 222 CG BASP A 66 37.949 48.215 34.772 0.50 33.09 C ANISOU 222 CG BASP A 66 4704 3561 4305 -523 1272 -915 C ATOM 223 OD1AASP A 66 36.025 49.562 33.338 0.50 24.29 O ANISOU 223 OD1AASP A 66 4384 2136 2708 -473 1413 -526 O ATOM 224 OD1BASP A 66 37.407 47.456 35.586 0.50 35.70 O ANISOU 224 OD1BASP A 66 4795 3599 5168 -949 1292 -838 O ATOM 225 OD2AASP A 66 37.863 49.998 32.237 0.50 26.78 O ANISOU 225 OD2AASP A 66 4539 2372 3261 -524 1837 -325 O ATOM 226 OD2BASP A 66 38.578 49.235 35.097 0.50 37.11 O ANISOU 226 OD2BASP A 66 4657 3915 5528 -860 1318 -828 O ATOM 227 N MET A 67 35.251 47.160 31.128 1.00 27.77 N ANISOU 227 N MET A 67 4800 2731 3020 -298 1367 -543 N ATOM 228 CA MET A 67 34.897 47.445 29.750 1.00 30.13 C ANISOU 228 CA MET A 67 5570 2848 3030 -262 1363 -372 C ATOM 229 C MET A 67 34.581 48.935 29.734 1.00 32.69 C ANISOU 229 C MET A 67 6757 2815 2846 -246 1505 -21 C ATOM 230 O MET A 67 33.505 49.348 30.182 1.00 34.25 O ANISOU 230 O MET A 67 7576 2561 2875 -226 1622 -199 O ATOM 231 CB MET A 67 33.711 46.609 29.248 1.00 28.98 C ANISOU 231 CB MET A 67 5283 2677 3048 210 999 -410 C ATOM 232 CG MET A 67 34.081 45.157 29.080 1.00 27.33 C ANISOU 232 CG MET A 67 4951 2629 2802 34 659 -625 C ATOM 233 SD MET A 67 32.837 44.110 28.287 0.58 25.71 S ANISOU 233 SD MET A 67 4898 2108 2761 504 300 -585 S ATOM 234 CE MET A 67 32.872 44.673 26.586 1.00 29.11 C ANISOU 234 CE MET A 67 5726 2474 2860 501 131 -376 C ATOM 235 N PRO A 68 35.578 49.755 29.340 1.00 36.17 N ANISOU 235 N PRO A 68 7580 3528 2634 -719 1691 -87 N ATOM 236 CA PRO A 68 35.342 51.192 29.329 1.00 38.16 C ANISOU 236 CA PRO A 68 8218 3559 2722 -607 1385 14 C ATOM 237 C PRO A 68 33.938 51.467 28.764 1.00 40.34 C ANISOU 237 C PRO A 68 8842 3632 2851 -250 710 -275 C ATOM 238 O PRO A 68 33.605 50.937 27.702 1.00 47.11 O ANISOU 238 O PRO A 68 10285 4784 2830 -441 1098 166 O ATOM 239 CB PRO A 68 36.457 51.735 28.424 1.00 40.18 C ANISOU 239 CB PRO A 68 8469 3895 2902 -759 1831 103 C ATOM 240 CG PRO A 68 37.606 50.790 28.678 1.00 38.50 C ANISOU 240 CG PRO A 68 7920 3818 2891 -1096 2143 200 C ATOM 241 CD PRO A 68 36.933 49.444 28.842 1.00 37.01 C ANISOU 241 CD PRO A 68 7423 3695 2945 -943 1926 191 C ATOM 242 N GLY A 69 33.116 52.228 29.482 1.00 40.11 N ANISOU 242 N GLY A 69 8274 3861 3105 351 841 354 N ATOM 243 CA GLY A 69 31.750 52.543 29.039 1.00 42.43 C ANISOU 243 CA GLY A 69 8680 4073 3367 754 259 613 C ATOM 244 C GLY A 69 30.695 51.604 29.608 1.00 41.30 C ANISOU 244 C GLY A 69 7552 4020 4119 1044 -452 817 C ATOM 245 O GLY A 69 29.506 51.853 29.421 1.00 49.54 O ANISOU 245 O GLY A 69 7664 5368 5789 1277 -870 563 O ATOM 246 N PHE A 70 31.102 50.539 30.305 1.00 36.85 N ANISOU 246 N PHE A 70 6757 4056 3187 926 -380 552 N ATOM 247 CA PHE A 70 30.157 49.517 30.777 1.00 36.32 C ANISOU 247 CA PHE A 70 6191 4237 3370 818 -701 352 C ATOM 248 C PHE A 70 30.438 49.139 32.242 1.00 33.75 C ANISOU 248 C PHE A 70 5537 4027 3258 391 -368 394 C ATOM 249 O PHE A 70 29.623 48.487 32.882 1.00 34.95 O ANISOU 249 O PHE A 70 4808 4764 3706 240 -465 273 O ATOM 250 CB PHE A 70 30.246 48.283 29.873 1.00 40.42 C ANISOU 250 CB PHE A 70 6715 4738 3902 641 -708 -134 C ATOM 251 CG PHE A 70 28.944 47.551 29.662 1.00 48.10 C ANISOU 251 CG PHE A 70 6888 5566 5820 315 -706 -4 C ATOM 252 CD1 PHE A 70 27.945 48.095 28.868 1.00 53.15 C ANISOU 252 CD1 PHE A 70 7797 6300 6096 592 -1265 45 C ATOM 253 CD2 PHE A 70 28.719 46.313 30.250 1.00 50.59 C ANISOU 253 CD2 PHE A 70 7170 5765 6286 464 -676 260 C ATOM 254 CE1 PHE A 70 26.749 47.419 28.669 1.00 58.01 C ANISOU 254 CE1 PHE A 70 7615 6883 7542 481 -975 335 C ATOM 255 CE2 PHE A 70 27.523 45.639 30.051 1.00 54.35 C ANISOU 255 CE2 PHE A 70 7314 6406 6928 137 -545 129 C ATOM 256 CZ PHE A 70 26.540 46.192 29.261 1.00 57.38 C ANISOU 256 CZ PHE A 70 7462 6668 7672 406 -817 91 C ATOM 257 N GLY A 71 31.600 49.499 32.764 1.00 25.71 N ANISOU 257 N GLY A 71 4642 2940 2183 228 33 28 N ATOM 258 CA GLY A 71 31.961 49.121 34.116 1.00 22.46 C ANISOU 258 CA GLY A 71 3987 2603 1943 84 296 -237 C ATOM 259 C GLY A 71 32.753 47.831 34.166 1.00 20.44 C ANISOU 259 C GLY A 71 3674 2438 1652 -88 265 -450 C ATOM 260 O GLY A 71 33.322 47.386 33.179 1.00 20.94 O ANISOU 260 O GLY A 71 3782 2345 1826 -19 447 -403 O ATOM 261 N ALA A 72 32.862 47.300 35.379 1.00 19.20 N ANISOU 261 N ALA A 72 3427 2197 1668 -156 425 -447 N ATOM 262 CA ALA A 72 33.606 46.067 35.635 1.00 19.19 C ANISOU 262 CA ALA A 72 3325 2170 1796 -179 456 -532 C ATOM 263 C ALA A 72 32.691 44.865 35.407 1.00 19.33 C ANISOU 263 C ALA A 72 3148 2323 1871 -164 534 -594 C ATOM 264 O ALA A 72 31.823 44.610 36.205 1.00 22.62 O ANISOU 264 O ALA A 72 3831 2600 2163 -373 968 -602 O ATOM 265 CB ALA A 72 34.143 46.094 37.045 1.00 20.51 C ANISOU 265 CB ALA A 72 3535 2324 1934 -45 264 -568 C ATOM 266 N VAL A 73 32.928 44.158 34.326 1.00 17.55 N ANISOU 266 N VAL A 73 2594 2206 1866 -72 460 -564 N ATOM 267 CA VAL A 73 31.974 43.158 33.830 1.00 17.33 C ANISOU 267 CA VAL A 73 2454 2115 2014 62 490 -579 C ATOM 268 C VAL A 73 32.341 41.763 34.337 1.00 16.48 C ANISOU 268 C VAL A 73 2230 2036 1993 -52 653 -622 C ATOM 269 O VAL A 73 33.451 41.274 34.111 1.00 16.37 O ANISOU 269 O VAL A 73 2117 2111 1991 -55 597 -490 O ATOM 270 CB VAL A 73 31.934 43.198 32.295 1.00 18.61 C ANISOU 270 CB VAL A 73 2706 2353 2010 54 468 -539 C ATOM 271 CG1 VAL A 73 31.038 42.125 31.702 1.00 19.84 C ANISOU 271 CG1 VAL A 73 2768 2467 2301 60 370 -650 C ATOM 272 CG2 VAL A 73 31.539 44.571 31.781 1.00 21.26 C ANISOU 272 CG2 VAL A 73 3361 2522 2193 73 241 -341 C ATOM 273 N ALA A 74 31.378 41.110 34.967 1.00 16.47 N ANISOU 273 N ALA A 74 2044 2028 2184 -20 598 -593 N ATOM 274 CA ALA A 74 31.539 39.740 35.428 1.00 16.08 C ANISOU 274 CA ALA A 74 1872 2103 2133 120 592 -566 C ATOM 275 C ALA A 74 31.425 38.771 34.256 1.00 15.41 C ANISOU 275 C ALA A 74 1657 2100 2095 -8 425 -469 C ATOM 276 O ALA A 74 30.561 38.929 33.398 1.00 16.31 O ANISOU 276 O ALA A 74 1955 2017 2226 300 286 -491 O ATOM 277 CB ALA A 74 30.455 39.408 36.427 1.00 17.01 C ANISOU 277 CB ALA A 74 2051 2328 2082 66 704 -645 C ATOM 278 N SER A 75 32.245 37.710 34.299 1.00 13.85 N ANISOU 278 N SER A 75 1586 2071 1602 -27 375 -444 N ATOM 279 CA SER A 75 32.084 36.551 33.421 1.00 13.72 C ANISOU 279 CA SER A 75 1624 1962 1625 -9 380 -433 C ATOM 280 C SER A 75 32.173 35.276 34.249 1.00 13.41 C ANISOU 280 C SER A 75 1623 1953 1518 -8 457 -452 C ATOM 281 O SER A 75 33.086 35.170 35.081 1.00 13.83 O ANISOU 281 O SER A 75 1735 2012 1507 -108 365 -338 O ATOM 282 CB SER A 75 33.147 36.519 32.345 1.00 14.30 C ANISOU 282 CB SER A 75 1864 1993 1575 18 438 -359 C ATOM 283 OG SER A 75 32.938 35.410 31.475 1.00 14.69 O ANISOU 283 OG SER A 75 1927 2059 1594 102 372 -408 O ATOM 284 N ASN A 76 31.238 34.364 34.021 1.00 13.53 N ANISOU 284 N ASN A 76 1546 1962 1633 18 226 -381 N ATOM 285 CA ASN A 76 31.176 33.111 34.734 1.00 13.26 C ANISOU 285 CA ASN A 76 1489 1940 1608 -36 292 -402 C ATOM 286 C ASN A 76 31.592 31.929 33.851 1.00 12.41 C ANISOU 286 C ASN A 76 1329 1962 1422 -1 324 -373 C ATOM 287 O ASN A 76 31.212 31.868 32.676 1.00 13.03 O ANISOU 287 O ASN A 76 1470 1953 1528 43 222 -377 O ATOM 288 CB ASN A 76 29.738 32.834 35.183 1.00 14.12 C ANISOU 288 CB ASN A 76 1510 2141 1711 -26 319 -459 C ATOM 289 CG ASN A 76 29.130 33.951 35.998 1.00 14.73 C ANISOU 289 CG ASN A 76 1499 2251 1845 -146 521 -542 C ATOM 290 OD1 ASN A 76 29.780 34.526 36.878 1.00 16.14 O ANISOU 290 OD1 ASN A 76 1635 2511 1984 -4 410 -735 O ATOM 291 ND2 ASN A 76 27.872 34.261 35.721 1.00 17.27 N ANISOU 291 ND2 ASN A 76 1544 2623 2395 140 478 -774 N ATOM 292 N GLY A 77 32.274 30.985 34.492 1.00 12.44 N ANISOU 292 N GLY A 77 1432 1942 1351 -79 311 -346 N ATOM 293 CA GLY A 77 32.494 29.653 33.949 1.00 12.21 C ANISOU 293 CA GLY A 77 1389 1900 1349 -95 322 -248 C ATOM 294 C GLY A 77 32.247 28.607 35.029 1.00 12.12 C ANISOU 294 C GLY A 77 1376 1965 1263 -132 319 -271 C ATOM 295 O GLY A 77 31.712 28.927 36.097 1.00 12.90 O ANISOU 295 O GLY A 77 1465 2073 1362 -60 461 -277 O ATOM 296 N LEU A 78 32.658 27.364 34.749 1.00 11.91 N ANISOU 296 N LEU A 78 1336 1938 1251 -58 301 -179 N ATOM 297 CA LEU A 78 32.375 26.245 35.661 1.00 12.48 C ANISOU 297 CA LEU A 78 1393 2022 1327 -113 469 -115 C ATOM 298 C LEU A 78 33.635 25.449 35.972 1.00 12.22 C ANISOU 298 C LEU A 78 1359 2033 1248 -162 430 -108 C ATOM 299 O LEU A 78 34.595 25.403 35.196 1.00 12.55 O ANISOU 299 O LEU A 78 1362 2124 1281 -32 463 -18 O ATOM 300 CB LEU A 78 31.295 25.329 35.092 1.00 13.61 C ANISOU 300 CB LEU A 78 1521 2118 1530 -144 442 -205 C ATOM 301 CG LEU A 78 29.891 25.923 35.018 1.00 15.17 C ANISOU 301 CG LEU A 78 1535 2328 1900 -87 280 -140 C ATOM 302 CD1 LEU A 78 28.985 25.020 34.214 1.00 19.06 C ANISOU 302 CD1 LEU A 78 1651 3089 2501 -337 96 -292 C ATOM 303 CD2 LEU A 78 29.302 26.149 36.401 1.00 16.24 C ANISOU 303 CD2 LEU A 78 1477 2519 2172 -4 585 -179 C ATOM 304 N ILE A 79 33.559 24.802 37.139 1.00 12.79 N ANISOU 304 N ILE A 79 1460 2119 1278 -152 559 -55 N ATOM 305 CA ILE A 79 34.564 23.868 37.633 1.00 12.69 C ANISOU 305 CA ILE A 79 1544 2022 1254 -108 558 -101 C ATOM 306 C ILE A 79 33.807 22.612 38.050 1.00 12.94 C ANISOU 306 C ILE A 79 1526 2085 1304 -132 452 26 C ATOM 307 O ILE A 79 32.872 22.736 38.851 1.00 14.13 O ANISOU 307 O ILE A 79 1790 2137 1442 -260 648 -90 O ATOM 308 CB ILE A 79 35.371 24.446 38.797 1.00 13.00 C ANISOU 308 CB ILE A 79 1503 2143 1293 -202 458 -36 C ATOM 309 CG1 ILE A 79 36.018 25.782 38.413 1.00 14.00 C ANISOU 309 CG1 ILE A 79 1624 2163 1531 -250 395 13 C ATOM 310 CG2 ILE A 79 36.372 23.413 39.318 1.00 14.58 C ANISOU 310 CG2 ILE A 79 1712 2315 1512 -203 310 157 C ATOM 311 CD1 ILE A 79 36.637 26.509 39.586 1.00 15.10 C ANISOU 311 CD1 ILE A 79 1724 2327 1684 -182 297 -85 C ATOM 312 N VAL A 80 34.188 21.441 37.554 1.00 13.02 N ANISOU 312 N VAL A 80 1630 2037 1279 -113 519 58 N ATOM 313 CA VAL A 80 33.481 20.200 37.854 1.00 13.52 C ANISOU 313 CA VAL A 80 1738 2088 1308 -116 596 45 C ATOM 314 C VAL A 80 34.467 19.169 38.376 1.00 14.47 C ANISOU 314 C VAL A 80 1825 2099 1573 -107 569 186 C ATOM 315 O VAL A 80 35.463 18.905 37.709 1.00 14.75 O ANISOU 315 O VAL A 80 1791 2267 1544 70 542 374 O ATOM 316 CB VAL A 80 32.774 19.678 36.597 1.00 14.20 C ANISOU 316 CB VAL A 80 1841 2123 1430 -105 535 -1 C ATOM 317 CG1 VAL A 80 32.094 18.353 36.902 1.00 15.58 C ANISOU 317 CG1 VAL A 80 2072 2203 1642 -286 437 -23 C ATOM 318 CG2 VAL A 80 31.803 20.690 36.039 1.00 14.32 C ANISOU 318 CG2 VAL A 80 1842 2224 1372 -176 382 -19 C ATOM 319 N ARG A 81 34.187 18.568 39.538 1.00 14.75 N ANISOU 319 N ARG A 81 2026 2127 1451 -12 586 152 N ATOM 320 CA ARG A 81 34.972 17.410 39.974 1.00 15.57 C ANISOU 320 CA ARG A 81 2152 2195 1566 44 666 303 C ATOM 321 C ARG A 81 34.311 16.161 39.405 1.00 15.76 C ANISOU 321 C ARG A 81 2207 2221 1557 -11 640 333 C ATOM 322 O ARG A 81 33.123 15.915 39.639 1.00 16.55 O ANISOU 322 O ARG A 81 2181 2306 1800 -137 553 172 O ATOM 323 CB ARG A 81 35.115 17.305 41.494 1.00 16.28 C ANISOU 323 CB ARG A 81 2255 2356 1573 -135 596 367 C ATOM 324 CG ARG A 81 36.001 16.128 41.867 1.00 16.99 C ANISOU 324 CG ARG A 81 2407 2404 1641 -128 406 514 C ATOM 325 CD ARG A 81 36.222 15.974 43.358 1.00 17.88 C ANISOU 325 CD ARG A 81 2535 2620 1639 -58 424 524 C ATOM 326 NE ARG A 81 35.015 15.682 44.112 1.00 18.78 N ANISOU 326 NE ARG A 81 2692 2761 1680 0 552 416 N ATOM 327 CZ ARG A 81 34.381 14.509 44.114 1.00 18.16 C ANISOU 327 CZ ARG A 81 2480 2793 1627 18 512 588 C ATOM 328 NH1 ARG A 81 34.833 13.477 43.414 1.00 18.34 N ANISOU 328 NH1 ARG A 81 2502 2606 1858 100 312 632 N ATOM 329 NH2 ARG A 81 33.295 14.369 44.866 1.00 20.73 N ANISOU 329 NH2 ARG A 81 2702 3240 1932 -93 735 679 N ATOM 330 N ASP A 82 35.118 15.358 38.734 1.00 15.87 N ANISOU 330 N ASP A 82 2328 2242 1456 35 596 310 N ATOM 331 CA ASP A 82 34.679 14.060 38.236 1.00 16.67 C ANISOU 331 CA ASP A 82 2507 2317 1508 28 504 202 C ATOM 332 C ASP A 82 35.577 12.989 38.858 1.00 16.78 C ANISOU 332 C ASP A 82 2598 2298 1477 -4 434 258 C ATOM 333 O ASP A 82 36.665 12.736 38.347 1.00 17.40 O ANISOU 333 O ASP A 82 2746 2293 1572 136 509 357 O ATOM 334 CB ASP A 82 34.791 14.010 36.713 1.00 17.77 C ANISOU 334 CB ASP A 82 2783 2466 1499 149 488 273 C ATOM 335 CG ASP A 82 34.496 12.644 36.124 1.00 18.66 C ANISOU 335 CG ASP A 82 2869 2582 1636 206 483 82 C ATOM 336 OD1 ASP A 82 33.658 11.932 36.695 1.00 20.77 O ANISOU 336 OD1 ASP A 82 3451 2724 1715 -92 732 -30 O ATOM 337 OD2 ASP A 82 35.099 12.300 35.083 1.00 20.28 O ANISOU 337 OD2 ASP A 82 3129 2920 1655 273 580 23 O ATOM 338 N GLY A 83 35.157 12.404 39.976 1.00 16.86 N ANISOU 338 N GLY A 83 2479 2381 1546 -119 397 338 N ATOM 339 CA GLY A 83 35.994 11.470 40.697 1.00 18.00 C ANISOU 339 CA GLY A 83 2808 2430 1598 -137 394 562 C ATOM 340 C GLY A 83 37.300 12.114 41.141 1.00 17.36 C ANISOU 340 C GLY A 83 2664 2320 1612 1 366 577 C ATOM 341 O GLY A 83 37.292 13.082 41.929 1.00 17.76 O ANISOU 341 O GLY A 83 2565 2527 1656 -62 421 440 O ATOM 342 N GLY A 84 38.409 11.562 40.675 1.00 18.29 N ANISOU 342 N GLY A 84 2677 2452 1820 32 452 657 N ATOM 343 CA GLY A 84 39.746 12.035 41.050 1.00 18.21 C ANISOU 343 CA GLY A 84 2662 2493 1764 154 338 648 C ATOM 344 C GLY A 84 40.325 13.119 40.164 1.00 17.52 C ANISOU 344 C GLY A 84 2425 2422 1809 238 436 562 C ATOM 345 O GLY A 84 41.531 13.339 40.210 1.00 19.06 O ANISOU 345 O GLY A 84 2477 2717 2047 85 434 653 O ATOM 346 N ARG A 85 39.523 13.799 39.362 1.00 17.53 N ANISOU 346 N ARG A 85 2475 2310 1875 70 394 677 N ATOM 347 CA ARG A 85 40.066 14.852 38.511 1.00 17.44 C ANISOU 347 CA ARG A 85 2323 2348 1954 133 458 679 C ATOM 348 C ARG A 85 39.053 15.996 38.430 1.00 15.93 C ANISOU 348 C ARG A 85 2075 2325 1653 34 462 570 C ATOM 349 O ARG A 85 37.881 15.846 38.786 1.00 16.61 O ANISOU 349 O ARG A 85 2158 2290 1861 4 591 459 O ATOM 350 CB ARG A 85 40.374 14.301 37.123 1.00 18.53 C ANISOU 350 CB ARG A 85 2493 2551 1993 306 417 661 C ATOM 351 CG ARG A 85 39.110 14.008 36.343 1.00 18.71 C ANISOU 351 CG ARG A 85 2547 2679 1882 196 439 413 C ATOM 352 CD ARG A 85 39.347 12.946 35.290 1.00 20.81 C ANISOU 352 CD ARG A 85 3004 2943 1958 195 338 247 C ATOM 353 NE ARG A 85 38.126 12.674 34.562 1.00 19.80 N ANISOU 353 NE ARG A 85 3199 2651 1670 255 205 263 N ATOM 354 CZ ARG A 85 37.907 12.932 33.288 1.00 18.03 C ANISOU 354 CZ ARG A 85 3087 2261 1501 246 329 -89 C ATOM 355 NH1 ARG A 85 38.915 13.170 32.459 1.00 19.19 N ANISOU 355 NH1 ARG A 85 3277 2195 1818 269 565 -102 N ATOM 356 NH2 ARG A 85 36.655 12.955 32.862 1.00 18.20 N ANISOU 356 NH2 ARG A 85 2945 2286 1682 142 442 146 N ATOM 357 N VAL A 86 39.533 17.121 37.912 1.00 15.35 N ANISOU 357 N VAL A 86 2041 2226 1564 123 485 538 N ATOM 358 CA VAL A 86 38.747 18.336 37.779 1.00 14.24 C ANISOU 358 CA VAL A 86 1777 2164 1467 10 419 373 C ATOM 359 C VAL A 86 38.693 18.737 36.296 1.00 13.72 C ANISOU 359 C VAL A 86 1625 2114 1472 35 390 282 C ATOM 360 O VAL A 86 39.690 18.599 35.567 1.00 14.56 O ANISOU 360 O VAL A 86 1747 2235 1548 192 465 412 O ATOM 361 CB VAL A 86 39.344 19.457 38.650 1.00 14.68 C ANISOU 361 CB VAL A 86 1806 2287 1483 -103 312 417 C ATOM 362 CG1 VAL A 86 38.641 20.785 38.435 1.00 14.95 C ANISOU 362 CG1 VAL A 86 1733 2282 1664 -55 174 163 C ATOM 363 CG2 VAL A 86 39.287 19.061 40.119 1.00 16.67 C ANISOU 363 CG2 VAL A 86 2413 2478 1443 -138 160 367 C ATOM 364 N LEU A 87 37.534 19.247 35.887 1.00 13.45 N ANISOU 364 N LEU A 87 1708 2065 1337 106 394 233 N ATOM 365 CA LEU A 87 37.272 19.706 34.517 1.00 12.97 C ANISOU 365 CA LEU A 87 1608 2026 1291 26 462 197 C ATOM 366 C LEU A 87 36.856 21.160 34.584 1.00 12.86 C ANISOU 366 C LEU A 87 1580 2045 1261 61 392 189 C ATOM 367 O LEU A 87 36.070 21.532 35.478 1.00 14.21 O ANISOU 367 O LEU A 87 1828 2029 1543 177 660 207 O ATOM 368 CB LEU A 87 36.164 18.867 33.878 1.00 13.91 C ANISOU 368 CB LEU A 87 1765 2027 1492 31 367 98 C ATOM 369 CG LEU A 87 36.225 17.363 34.133 1.00 15.40 C ANISOU 369 CG LEU A 87 2076 2104 1670 0 337 274 C ATOM 370 CD1 LEU A 87 34.981 16.650 33.615 1.00 16.69 C ANISOU 370 CD1 LEU A 87 2255 2212 1873 -94 321 107 C ATOM 371 CD2 LEU A 87 37.476 16.738 33.574 1.00 17.09 C ANISOU 371 CD2 LEU A 87 2268 2271 1953 79 402 6 C ATOM 372 N VAL A 88 37.359 22.002 33.672 1.00 12.37 N ANISOU 372 N VAL A 88 1508 1923 1266 64 341 161 N ATOM 373 CA VAL A 88 37.036 23.423 33.683 1.00 12.06 C ANISOU 373 CA VAL A 88 1416 1949 1216 71 433 117 C ATOM 374 C VAL A 88 36.274 23.779 32.410 1.00 11.84 C ANISOU 374 C VAL A 88 1344 1953 1201 47 430 64 C ATOM 375 O VAL A 88 36.651 23.326 31.303 1.00 12.31 O ANISOU 375 O VAL A 88 1463 1987 1226 205 374 16 O ATOM 376 CB VAL A 88 38.318 24.249 33.835 1.00 13.06 C ANISOU 376 CB VAL A 88 1492 2078 1391 -16 264 157 C ATOM 377 CG1 VAL A 88 38.090 25.735 33.635 1.00 13.92 C ANISOU 377 CG1 VAL A 88 1414 2112 1760 -113 175 137 C ATOM 378 CG2 VAL A 88 38.967 23.980 35.189 1.00 14.32 C ANISOU 378 CG2 VAL A 88 1648 2251 1540 15 125 259 C ATOM 379 N VAL A 89 35.260 24.620 32.552 1.00 11.38 N ANISOU 379 N VAL A 89 1278 1816 1227 -23 348 41 N ATOM 380 CA VAL A 89 34.564 25.227 31.429 1.00 11.40 C ANISOU 380 CA VAL A 89 1292 1782 1258 61 313 -121 C ATOM 381 C VAL A 89 34.828 26.733 31.467 1.00 10.88 C ANISOU 381 C VAL A 89 1127 1754 1250 68 320 -144 C ATOM 382 O VAL A 89 34.436 27.406 32.430 1.00 11.33 O ANISOU 382 O VAL A 89 1296 1766 1244 10 334 -151 O ATOM 383 CB VAL A 89 33.051 24.957 31.480 1.00 12.49 C ANISOU 383 CB VAL A 89 1370 1838 1535 -63 267 -118 C ATOM 384 CG1 VAL A 89 32.382 25.600 30.270 1.00 13.19 C ANISOU 384 CG1 VAL A 89 1387 1876 1748 -15 175 -110 C ATOM 385 CG2 VAL A 89 32.739 23.483 31.543 1.00 13.29 C ANISOU 385 CG2 VAL A 89 1561 1913 1575 -161 283 -178 C ATOM 386 N ASP A 90 35.532 27.211 30.415 1.00 11.05 N ANISOU 386 N ASP A 90 1224 1710 1264 122 373 -116 N ATOM 387 CA ASP A 90 35.908 28.592 30.170 1.00 11.28 C ANISOU 387 CA ASP A 90 1304 1777 1203 60 302 -56 C ATOM 388 C ASP A 90 37.075 29.046 31.047 1.00 11.16 C ANISOU 388 C ASP A 90 1211 1773 1256 4 356 -75 C ATOM 389 O ASP A 90 37.193 28.659 32.220 1.00 12.15 O ANISOU 389 O ASP A 90 1373 1977 1266 30 248 -66 O ATOM 390 CB ASP A 90 34.718 29.548 30.279 1.00 11.87 C ANISOU 390 CB ASP A 90 1397 1847 1264 180 309 -152 C ATOM 391 CG ASP A 90 33.746 29.360 29.126 1.00 12.92 C ANISOU 391 CG ASP A 90 1503 1835 1569 82 155 -78 C ATOM 392 OD1 ASP A 90 34.203 28.876 28.059 1.00 14.42 O ANISOU 392 OD1 ASP A 90 2010 2039 1427 131 4 -177 O ATOM 393 OD2 ASP A 90 32.580 29.716 29.279 1.00 15.20 O ANISOU 393 OD2 ASP A 90 1463 2153 2160 63 219 30 O ATOM 394 N THR A 91 37.949 29.865 30.447 1.00 11.50 N ANISOU 394 N THR A 91 1334 1790 1243 -70 372 -95 N ATOM 395 CA THR A 91 38.934 30.559 31.245 1.00 11.60 C ANISOU 395 CA THR A 91 1201 1854 1352 -28 279 -66 C ATOM 396 C THR A 91 38.281 31.768 31.939 1.00 11.68 C ANISOU 396 C THR A 91 1279 1875 1283 -157 414 -108 C ATOM 397 O THR A 91 37.091 32.024 31.758 1.00 12.65 O ANISOU 397 O THR A 91 1360 1959 1487 -80 330 -163 O ATOM 398 CB THR A 91 40.128 31.008 30.393 1.00 12.43 C ANISOU 398 CB THR A 91 1271 1954 1498 -40 339 -100 C ATOM 399 OG1 THR A 91 39.801 32.113 29.542 1.00 12.50 O ANISOU 399 OG1 THR A 91 1390 1953 1407 -66 359 -84 O ATOM 400 CG2 THR A 91 40.674 29.913 29.503 1.00 12.76 C ANISOU 400 CG2 THR A 91 1332 1890 1625 94 329 -64 C ATOM 401 N ALA A 92 39.092 32.498 32.707 1.00 12.50 N ANISOU 401 N ALA A 92 1356 1959 1432 -128 312 -202 N ATOM 402 CA ALA A 92 38.759 33.851 33.116 1.00 12.84 C ANISOU 402 CA ALA A 92 1414 1975 1489 -163 349 -252 C ATOM 403 C ALA A 92 39.162 34.825 32.000 1.00 12.82 C ANISOU 403 C ALA A 92 1468 1922 1480 -152 277 -222 C ATOM 404 O ALA A 92 39.677 34.412 30.940 1.00 13.51 O ANISOU 404 O ALA A 92 1609 1943 1579 -66 433 -229 O ATOM 405 CB ALA A 92 39.463 34.189 34.413 1.00 13.43 C ANISOU 405 CB ALA A 92 1653 2064 1386 -294 412 -252 C ATOM 406 N TRP A 93 38.970 36.110 32.225 1.00 13.69 N ANISOU 406 N TRP A 93 1669 1886 1646 -203 333 -192 N ATOM 407 CA TRP A 93 39.318 37.094 31.203 1.00 13.72 C ANISOU 407 CA TRP A 93 1739 1786 1688 -168 339 -230 C ATOM 408 C TRP A 93 40.813 37.096 30.886 1.00 13.93 C ANISOU 408 C TRP A 93 1765 1888 1639 -139 412 -184 C ATOM 409 O TRP A 93 41.195 37.427 29.766 1.00 15.10 O ANISOU 409 O TRP A 93 1815 2309 1610 -230 342 -79 O ATOM 410 CB TRP A 93 38.931 38.496 31.677 1.00 14.52 C ANISOU 410 CB TRP A 93 1826 1858 1831 -124 196 -372 C ATOM 411 CG TRP A 93 37.481 38.785 31.849 1.00 14.39 C ANISOU 411 CG TRP A 93 1847 1869 1752 -165 386 -375 C ATOM 412 CD1 TRP A 93 36.797 38.706 33.027 1.00 14.70 C ANISOU 412 CD1 TRP A 93 2019 1957 1609 -166 298 -383 C ATOM 413 CD2 TRP A 93 36.586 39.354 30.893 1.00 14.66 C ANISOU 413 CD2 TRP A 93 1919 1826 1824 20 466 -414 C ATOM 414 NE1 TRP A 93 35.516 39.133 32.850 1.00 15.23 N ANISOU 414 NE1 TRP A 93 1917 2064 1804 -135 495 -507 N ATOM 415 CE2 TRP A 93 35.367 39.582 31.570 1.00 14.97 C ANISOU 415 CE2 TRP A 93 1857 1924 1906 30 424 -483 C ATOM 416 CE3 TRP A 93 36.696 39.764 29.570 1.00 15.85 C ANISOU 416 CE3 TRP A 93 2051 2098 1873 15 419 -382 C ATOM 417 CZ2 TRP A 93 34.275 40.148 30.938 1.00 16.00 C ANISOU 417 CZ2 TRP A 93 2012 2124 1944 107 292 -564 C ATOM 418 CZ3 TRP A 93 35.619 40.346 28.948 1.00 17.03 C ANISOU 418 CZ3 TRP A 93 2357 2126 1987 128 348 -194 C ATOM 419 CH2 TRP A 93 34.420 40.527 29.626 1.00 16.67 C ANISOU 419 CH2 TRP A 93 2252 2022 2059 241 221 -369 C ATOM 420 N THR A 94 41.656 36.868 31.885 1.00 14.59 N ANISOU 420 N THR A 94 1690 2116 1737 -242 331 -151 N ATOM 421 CA THR A 94 43.099 37.023 31.723 1.00 15.11 C ANISOU 421 CA THR A 94 1762 2179 1798 -374 351 43 C ATOM 422 C THR A 94 43.843 35.776 32.194 1.00 14.01 C ANISOU 422 C THR A 94 1478 2139 1706 -342 313 -149 C ATOM 423 O THR A 94 43.330 34.948 32.953 1.00 14.58 O ANISOU 423 O THR A 94 1485 2217 1837 -386 258 -89 O ATOM 424 CB THR A 94 43.651 38.243 32.479 1.00 16.17 C ANISOU 424 CB THR A 94 1900 2357 1887 -375 324 -122 C ATOM 425 OG1 THR A 94 43.614 37.940 33.880 1.00 16.22 O ANISOU 425 OG1 THR A 94 1980 2372 1808 -526 343 -163 O ATOM 426 CG2 THR A 94 42.880 39.515 32.201 1.00 17.11 C ANISOU 426 CG2 THR A 94 2158 2206 2136 -426 223 -217 C ATOM 427 N ASP A 95 45.104 35.675 31.757 1.00 15.31 N ANISOU 427 N ASP A 95 1539 2515 1763 -263 436 28 N ATOM 428 CA ASP A 95 45.985 34.632 32.228 1.00 15.67 C ANISOU 428 CA ASP A 95 1404 2540 2007 -379 302 56 C ATOM 429 C ASP A 95 46.139 34.680 33.751 1.00 16.39 C ANISOU 429 C ASP A 95 1542 2672 2013 -429 210 125 C ATOM 430 O ASP A 95 46.066 33.612 34.401 1.00 16.05 O ANISOU 430 O ASP A 95 1487 2668 1942 -390 251 106 O ATOM 431 CB ASP A 95 47.363 34.709 31.573 1.00 17.04 C ANISOU 431 CB ASP A 95 1492 2786 2193 -429 434 163 C ATOM 432 CG ASP A 95 47.327 34.432 30.082 1.00 17.82 C ANISOU 432 CG ASP A 95 1572 2934 2262 -371 637 -12 C ATOM 433 OD1 ASP A 95 46.564 33.572 29.643 1.00 18.22 O ANISOU 433 OD1 ASP A 95 1624 3084 2213 -151 470 -335 O ATOM 434 OD2 ASP A 95 48.098 35.102 29.382 1.00 22.71 O ANISOU 434 OD2 ASP A 95 2731 3392 2503 -757 1111 86 O ATOM 435 N ASP A 96 46.367 35.870 34.308 1.00 16.52 N ANISOU 435 N ASP A 96 1533 2774 1966 -637 401 115 N ATOM 436 CA ASP A 96 46.591 35.954 35.749 1.00 18.00 C ANISOU 436 CA ASP A 96 1637 3149 2053 -769 168 -18 C ATOM 437 C ASP A 96 45.343 35.480 36.504 1.00 16.70 C ANISOU 437 C ASP A 96 1654 2850 1841 -656 133 -13 C ATOM 438 O ASP A 96 45.439 34.771 37.505 1.00 18.06 O ANISOU 438 O ASP A 96 1893 3106 1862 -675 7 40 O ATOM 439 CB ASP A 96 46.968 37.367 36.185 1.00 19.98 C ANISOU 439 CB ASP A 96 2247 3240 2102 -942 83 -73 C ATOM 440 CG ASP A 96 48.387 37.786 35.836 1.00 25.51 C ANISOU 440 CG ASP A 96 2395 3966 3331 -1228 92 35 C ATOM 441 OD1 ASP A 96 49.194 36.921 35.438 1.00 28.51 O ANISOU 441 OD1 ASP A 96 2369 4614 3848 -1040 384 157 O ATOM 442 OD2 ASP A 96 48.672 38.982 35.975 1.00 31.09 O ANISOU 442 OD2 ASP A 96 3431 4094 4288 -1706 -163 237 O ATOM 443 N GLN A 97 44.165 35.874 36.045 1.00 15.85 N ANISOU 443 N GLN A 97 1661 2585 1774 -527 229 -222 N ATOM 444 CA GLN A 97 42.931 35.435 36.708 1.00 15.80 C ANISOU 444 CA GLN A 97 1733 2530 1737 -495 270 -201 C ATOM 445 C GLN A 97 42.756 33.919 36.577 1.00 15.19 C ANISOU 445 C GLN A 97 1768 2491 1511 -392 174 -88 C ATOM 446 O GLN A 97 42.269 33.245 37.494 1.00 15.37 O ANISOU 446 O GLN A 97 1763 2571 1506 -371 215 -122 O ATOM 447 CB GLN A 97 41.720 36.145 36.108 1.00 14.74 C ANISOU 447 CB GLN A 97 1697 2391 1512 -451 403 -278 C ATOM 448 CG GLN A 97 41.636 37.627 36.411 1.00 16.21 C ANISOU 448 CG GLN A 97 1875 2429 1855 -436 415 -354 C ATOM 449 CD GLN A 97 40.636 38.308 35.521 1.00 15.81 C ANISOU 449 CD GLN A 97 2031 2256 1719 -434 546 -199 C ATOM 450 OE1 GLN A 97 40.096 37.702 34.601 1.00 16.55 O ANISOU 450 OE1 GLN A 97 1995 2303 1989 -336 269 -270 O ATOM 451 NE2 GLN A 97 40.355 39.574 35.797 1.00 18.40 N ANISOU 451 NE2 GLN A 97 2485 2361 2143 -232 535 -289 N ATOM 452 N THR A 98 43.121 33.386 35.404 1.00 14.46 N ANISOU 452 N THR A 98 1429 2410 1653 -385 285 -156 N ATOM 453 CA THR A 98 42.984 31.965 35.161 1.00 14.48 C ANISOU 453 CA THR A 98 1448 2440 1614 -288 274 -133 C ATOM 454 C THR A 98 43.935 31.168 36.058 1.00 14.76 C ANISOU 454 C THR A 98 1491 2540 1575 -332 289 8 C ATOM 455 O THR A 98 43.555 30.122 36.589 1.00 15.17 O ANISOU 455 O THR A 98 1504 2633 1625 -356 188 100 O ATOM 456 CB THR A 98 43.131 31.676 33.672 1.00 14.20 C ANISOU 456 CB THR A 98 1374 2375 1645 -110 253 -75 C ATOM 457 OG1 THR A 98 42.150 32.417 32.939 1.00 13.75 O ANISOU 457 OG1 THR A 98 1272 2334 1616 -145 290 -82 O ATOM 458 CG2 THR A 98 42.958 30.216 33.354 1.00 14.34 C ANISOU 458 CG2 THR A 98 1501 2388 1559 -72 312 -185 C ATOM 459 N ALA A 99 45.164 31.663 36.240 1.00 15.66 N ANISOU 459 N ALA A 99 1424 2812 1713 -317 187 217 N ATOM 460 CA ALA A 99 46.049 31.030 37.203 1.00 16.84 C ANISOU 460 CA ALA A 99 1489 3014 1894 -383 46 235 C ATOM 461 C ALA A 99 45.427 31.049 38.612 1.00 16.67 C ANISOU 461 C ALA A 99 1727 2880 1726 -491 -91 183 C ATOM 462 O ALA A 99 45.606 30.096 39.385 1.00 18.32 O ANISOU 462 O ALA A 99 1993 3174 1792 -498 -147 377 O ATOM 463 CB ALA A 99 47.407 31.681 37.166 1.00 18.87 C ANISOU 463 CB ALA A 99 1647 3297 2223 -570 74 424 C ATOM 464 N GLN A 100 44.692 32.100 38.953 1.00 17.73 N ANISOU 464 N GLN A 100 2073 2859 1804 -549 15 -17 N ATOM 465 CA GLN A 100 44.027 32.142 40.253 1.00 18.04 C ANISOU 465 CA GLN A 100 2247 2940 1666 -584 -37 31 C ATOM 466 C GLN A 100 42.913 31.085 40.338 1.00 16.40 C ANISOU 466 C GLN A 100 2070 2718 1443 -375 154 32 C ATOM 467 O GLN A 100 42.712 30.512 41.403 1.00 17.70 O ANISOU 467 O GLN A 100 2357 2834 1531 -481 -14 125 O ATOM 468 CB GLN A 100 43.507 33.552 40.528 1.00 19.81 C ANISOU 468 CB GLN A 100 2936 2850 1739 -727 198 -85 C ATOM 469 CG GLN A 100 44.599 34.504 40.972 1.00 24.42 C ANISOU 469 CG GLN A 100 3452 3200 2624 -1121 133 -187 C ATOM 470 CD GLN A 100 44.903 34.362 42.445 1.00 28.68 C ANISOU 470 CD GLN A 100 4174 3791 2931 -979 -558 -353 C ATOM 471 OE1 GLN A 100 45.312 33.309 42.934 1.00 29.39 O ANISOU 471 OE1 GLN A 100 4391 3932 2842 -862 -552 -329 O ATOM 472 NE2 GLN A 100 44.717 35.447 43.171 1.00 33.91 N ANISOU 472 NE2 GLN A 100 5115 4432 3336 -531 -465 -827 N ATOM 473 N ILE A 101 42.205 30.825 39.248 1.00 15.30 N ANISOU 473 N ILE A 101 1918 2411 1483 -387 217 135 N ATOM 474 CA ILE A 101 41.254 29.706 39.251 1.00 14.82 C ANISOU 474 CA ILE A 101 1740 2448 1439 -367 370 -24 C ATOM 475 C ILE A 101 41.982 28.416 39.614 1.00 15.41 C ANISOU 475 C ILE A 101 1786 2551 1516 -452 127 161 C ATOM 476 O ILE A 101 41.499 27.647 40.438 1.00 15.77 O ANISOU 476 O ILE A 101 1891 2603 1498 -477 121 228 O ATOM 477 CB ILE A 101 40.521 29.559 37.899 1.00 14.29 C ANISOU 477 CB ILE A 101 1638 2357 1432 -237 432 14 C ATOM 478 CG1 ILE A 101 39.621 30.760 37.615 1.00 15.27 C ANISOU 478 CG1 ILE A 101 1540 2483 1779 -185 436 25 C ATOM 479 CG2 ILE A 101 39.748 28.248 37.860 1.00 15.26 C ANISOU 479 CG2 ILE A 101 1855 2303 1637 -259 307 93 C ATOM 480 CD1 ILE A 101 39.035 30.757 36.236 1.00 15.46 C ANISOU 480 CD1 ILE A 101 1593 2365 1915 -237 255 123 C ATOM 481 N LEU A 102 43.125 28.172 38.971 1.00 15.50 N ANISOU 481 N LEU A 102 1708 2562 1619 -389 93 246 N ATOM 482 CA LEU A 102 43.864 26.951 39.256 1.00 16.05 C ANISOU 482 CA LEU A 102 1626 2667 1803 -328 45 194 C ATOM 483 C LEU A 102 44.360 26.936 40.709 1.00 16.64 C ANISOU 483 C LEU A 102 1718 2782 1818 -263 -6 370 C ATOM 484 O LEU A 102 44.358 25.858 41.334 1.00 17.35 O ANISOU 484 O LEU A 102 1856 2896 1838 -285 -8 465 O ATOM 485 CB LEU A 102 45.011 26.820 38.252 1.00 16.54 C ANISOU 485 CB LEU A 102 1521 2766 1995 -200 68 182 C ATOM 486 CG LEU A 102 44.590 26.797 36.787 1.00 16.23 C ANISOU 486 CG LEU A 102 1509 2761 1895 -221 266 289 C ATOM 487 CD1 LEU A 102 45.814 26.629 35.908 1.00 17.47 C ANISOU 487 CD1 LEU A 102 1610 2944 2081 -227 367 231 C ATOM 488 CD2 LEU A 102 43.590 25.694 36.503 1.00 16.49 C ANISOU 488 CD2 LEU A 102 1550 2866 1847 -267 400 244 C ATOM 489 N ASN A 103 44.725 28.086 41.262 1.00 17.78 N ANISOU 489 N ASN A 103 1917 2999 1837 -419 -103 307 N ATOM 490 CA ASN A 103 45.127 28.172 42.673 1.00 19.05 C ANISOU 490 CA ASN A 103 1980 3342 1916 -496 -182 211 C ATOM 491 C ASN A 103 43.961 27.820 43.593 1.00 18.87 C ANISOU 491 C ASN A 103 2167 3042 1959 -661 -178 426 C ATOM 492 O ASN A 103 44.132 27.101 44.582 1.00 19.85 O ANISOU 492 O ASN A 103 2437 3379 1726 -569 -222 399 O ATOM 493 CB ASN A 103 45.687 29.563 42.991 1.00 21.49 C ANISOU 493 CB ASN A 103 2630 3511 2021 -835 -434 315 C ATOM 494 CG ASN A 103 46.979 29.870 42.270 1.00 26.28 C ANISOU 494 CG ASN A 103 2768 4151 3067 -785 -85 479 C ATOM 495 OD1 ASN A 103 47.702 28.950 41.897 1.00 30.71 O ANISOU 495 OD1 ASN A 103 3001 4708 3956 -250 -89 417 O ATOM 496 ND2 ASN A 103 47.294 31.150 42.115 1.00 28.65 N ANISOU 496 ND2 ASN A 103 3147 4246 3492 -1070 3 326 N ATOM 497 N TRP A 104 42.790 28.353 43.274 1.00 17.94 N ANISOU 497 N TRP A 104 2171 2956 1688 -563 -81 174 N ATOM 498 CA TRP A 104 41.578 28.030 44.049 1.00 17.66 C ANISOU 498 CA TRP A 104 2322 2899 1486 -560 11 131 C ATOM 499 C TRP A 104 41.314 26.518 43.997 1.00 16.89 C ANISOU 499 C TRP A 104 2103 2846 1467 -430 -86 242 C ATOM 500 O TRP A 104 41.041 25.885 45.020 1.00 17.89 O ANISOU 500 O TRP A 104 2478 2827 1492 -363 0 231 O ATOM 501 CB TRP A 104 40.374 28.848 43.573 1.00 17.54 C ANISOU 501 CB TRP A 104 2388 2718 1558 -460 173 0 C ATOM 502 CG TRP A 104 39.117 28.568 44.346 1.00 18.54 C ANISOU 502 CG TRP A 104 2547 3049 1448 -541 288 10 C ATOM 503 CD1 TRP A 104 38.648 29.233 45.441 1.00 19.86 C ANISOU 503 CD1 TRP A 104 2928 3040 1576 -532 410 -35 C ATOM 504 CD2 TRP A 104 38.171 27.521 44.056 1.00 17.84 C ANISOU 504 CD2 TRP A 104 2346 3002 1430 -492 409 163 C ATOM 505 NE1 TRP A 104 37.462 28.683 45.835 1.00 20.20 N ANISOU 505 NE1 TRP A 104 3003 3031 1641 -360 663 114 N ATOM 506 CE2 TRP A 104 37.151 27.631 45.019 1.00 18.95 C ANISOU 506 CE2 TRP A 104 2564 2956 1679 -344 588 184 C ATOM 507 CE3 TRP A 104 38.074 26.502 43.099 1.00 17.63 C ANISOU 507 CE3 TRP A 104 2081 3085 1531 -374 244 77 C ATOM 508 CZ2 TRP A 104 36.066 26.760 45.066 1.00 19.46 C ANISOU 508 CZ2 TRP A 104 2460 3153 1782 -378 680 330 C ATOM 509 CZ3 TRP A 104 36.997 25.638 43.150 1.00 19.16 C ANISOU 509 CZ3 TRP A 104 2283 3101 1892 -420 327 86 C ATOM 510 CH2 TRP A 104 36.019 25.757 44.129 1.00 20.58 C ANISOU 510 CH2 TRP A 104 2391 3471 1955 -467 438 110 C ATOM 511 N ILE A 105 41.394 25.926 42.801 1.00 16.34 N ANISOU 511 N ILE A 105 2049 2647 1513 -397 -25 256 N ATOM 512 CA ILE A 105 41.163 24.485 42.666 1.00 16.46 C ANISOU 512 CA ILE A 105 2105 2623 1525 -325 63 286 C ATOM 513 C ILE A 105 42.163 23.723 43.545 1.00 17.37 C ANISOU 513 C ILE A 105 2254 2766 1579 -305 -35 397 C ATOM 514 O ILE A 105 41.773 22.760 44.235 1.00 18.26 O ANISOU 514 O ILE A 105 2422 2829 1688 -309 0 500 O ATOM 515 CB ILE A 105 41.253 24.071 41.189 1.00 15.70 C ANISOU 515 CB ILE A 105 1868 2604 1492 -225 135 381 C ATOM 516 CG1 ILE A 105 40.084 24.666 40.399 1.00 15.33 C ANISOU 516 CG1 ILE A 105 1828 2478 1516 -258 69 230 C ATOM 517 CG2 ILE A 105 41.318 22.554 41.059 1.00 16.93 C ANISOU 517 CG2 ILE A 105 2167 2643 1620 -186 123 344 C ATOM 518 CD1 ILE A 105 40.187 24.475 38.895 1.00 14.56 C ANISOU 518 CD1 ILE A 105 1586 2426 1517 -322 231 210 C ATOM 519 N LYS A 106 43.429 24.112 43.528 1.00 18.45 N ANISOU 519 N LYS A 106 2290 2987 1732 -382 -121 592 N ATOM 520 CA LYS A 106 44.431 23.432 44.339 1.00 20.45 C ANISOU 520 CA LYS A 106 2403 3458 1908 -394 -313 674 C ATOM 521 C LYS A 106 44.068 23.508 45.830 1.00 20.81 C ANISOU 521 C LYS A 106 2601 3482 1823 -351 -507 608 C ATOM 522 O LYS A 106 44.194 22.512 46.539 1.00 23.78 O ANISOU 522 O LYS A 106 3258 3680 2095 -500 -628 855 O ATOM 523 CB LYS A 106 45.805 24.054 44.090 1.00 21.85 C ANISOU 523 CB LYS A 106 2403 3632 2265 -414 -244 705 C ATOM 524 CG LYS A 106 46.916 23.543 44.987 1.00 25.92 C ANISOU 524 CG LYS A 106 2904 4308 2635 -329 -587 895 C ATOM 525 CD LYS A 106 47.234 22.082 44.835 1.00 31.43 C ANISOU 525 CD LYS A 106 3469 4477 3996 -95 -502 690 C ATOM 526 CE LYS A 106 48.366 21.669 45.760 1.00 35.88 C ANISOU 526 CE LYS A 106 4003 5155 4472 15 -905 861 C ATOM 527 NZ LYS A 106 48.589 20.203 45.784 1.00 39.24 N ANISOU 527 NZ LYS A 106 4665 5172 5072 24 -444 789 N ATOM 528 N GLN A 107 43.616 24.681 46.287 1.00 21.56 N ANISOU 528 N GLN A 107 2890 3512 1788 -390 -299 559 N ATOM 529 CA GLN A 107 43.272 24.885 47.706 1.00 23.04 C ANISOU 529 CA GLN A 107 3346 3751 1657 -430 -446 502 C ATOM 530 C GLN A 107 42.000 24.113 48.103 1.00 22.38 C ANISOU 530 C GLN A 107 3601 3420 1480 -444 -197 361 C ATOM 531 O GLN A 107 41.948 23.494 49.172 1.00 25.02 O ANISOU 531 O GLN A 107 3918 3826 1761 -405 -263 719 O ATOM 532 CB GLN A 107 43.105 26.382 47.989 1.00 25.10 C ANISOU 532 CB GLN A 107 3869 3746 1919 -760 -349 298 C ATOM 533 CG GLN A 107 42.574 26.712 49.386 1.00 28.31 C ANISOU 533 CG GLN A 107 4496 4407 1851 -520 -446 160 C ATOM 534 CD GLN A 107 42.505 28.203 49.627 1.00 30.75 C ANISOU 534 CD GLN A 107 4580 4437 2667 -856 -345 0 C ATOM 535 OE1 GLN A 107 43.523 28.898 49.648 1.00 34.19 O ANISOU 535 OE1 GLN A 107 5305 4380 3303 -1283 -629 275 O ATOM 536 NE2 GLN A 107 41.292 28.717 49.788 1.00 30.52 N ANISOU 536 NE2 GLN A 107 4713 4278 2605 -876 176 59 N ATOM 537 N GLU A 108 40.966 24.182 47.269 1.00 20.79 N ANISOU 537 N GLU A 108 3286 3118 1494 -394 23 406 N ATOM 538 CA GLU A 108 39.609 23.759 47.675 1.00 21.59 C ANISOU 538 CA GLU A 108 3539 3156 1507 -553 283 270 C ATOM 539 C GLU A 108 39.289 22.332 47.226 1.00 20.54 C ANISOU 539 C GLU A 108 3390 2972 1440 -438 268 478 C ATOM 540 O GLU A 108 38.419 21.700 47.821 1.00 21.95 O ANISOU 540 O GLU A 108 3553 2930 1854 -357 631 454 O ATOM 541 CB GLU A 108 38.594 24.758 47.127 1.00 21.81 C ANISOU 541 CB GLU A 108 3507 3117 1663 -399 468 105 C ATOM 542 CG GLU A 108 38.729 26.131 47.773 1.00 24.91 C ANISOU 542 CG GLU A 108 4093 3339 2032 -476 284 -151 C ATOM 543 CD GLU A 108 38.389 26.229 49.250 1.00 28.73 C ANISOU 543 CD GLU A 108 4900 3767 2246 -643 688 -485 C ATOM 544 OE1 GLU A 108 37.686 25.326 49.759 1.00 33.63 O ANISOU 544 OE1 GLU A 108 5494 4581 2699 -580 1360 176 O ATOM 545 OE2 GLU A 108 38.806 27.226 49.872 1.00 32.04 O ANISOU 545 OE2 GLU A 108 5618 3849 2706 -943 668 -564 O ATOM 546 N ILE A 109 39.974 21.823 46.200 1.00 18.52 N ANISOU 546 N ILE A 109 2562 2837 1634 -491 96 334 N ATOM 547 CA ILE A 109 39.701 20.481 45.667 1.00 18.41 C ANISOU 547 CA ILE A 109 2681 2696 1616 -389 166 449 C ATOM 548 C ILE A 109 40.964 19.616 45.735 1.00 19.23 C ANISOU 548 C ILE A 109 2766 2893 1646 -255 82 457 C ATOM 549 O ILE A 109 40.883 18.459 46.146 1.00 19.96 O ANISOU 549 O ILE A 109 2844 2997 1741 -228 167 640 O ATOM 550 CB ILE A 109 39.100 20.520 44.249 1.00 17.29 C ANISOU 550 CB ILE A 109 2419 2667 1481 -368 323 389 C ATOM 551 CG1 ILE A 109 37.838 21.385 44.202 1.00 18.31 C ANISOU 551 CG1 ILE A 109 2499 2768 1689 -322 189 338 C ATOM 552 CG2 ILE A 109 38.855 19.095 43.791 1.00 18.50 C ANISOU 552 CG2 ILE A 109 2657 2708 1663 -262 279 254 C ATOM 553 CD1 ILE A 109 37.358 21.679 42.802 1.00 18.01 C ANISOU 553 CD1 ILE A 109 2345 2759 1737 -374 187 327 C ATOM 554 N ASN A 110 42.107 20.154 45.313 1.00 19.68 N ANISOU 554 N ASN A 110 2626 3085 1766 -193 -34 580 N ATOM 555 CA ASN A 110 43.385 19.477 45.441 1.00 21.14 C ANISOU 555 CA ASN A 110 2623 3294 2114 -163 -238 667 C ATOM 556 C ASN A 110 43.380 18.177 44.636 1.00 20.29 C ANISOU 556 C ASN A 110 2450 3151 2108 51 -89 781 C ATOM 557 O ASN A 110 43.818 17.136 45.121 1.00 21.39 O ANISOU 557 O ASN A 110 2742 3266 2119 169 -37 848 O ATOM 558 CB ASN A 110 43.779 19.215 46.893 1.00 23.06 C ANISOU 558 CB ASN A 110 3149 3416 2197 -117 -343 782 C ATOM 559 CG ASN A 110 45.224 18.798 47.018 1.00 25.88 C ANISOU 559 CG ASN A 110 3238 3939 2654 -10 -407 924 C ATOM 560 OD1 ASN A 110 46.047 19.175 46.181 1.00 26.61 O ANISOU 560 OD1 ASN A 110 2972 4238 2897 -39 -480 1063 O ATOM 561 ND2 ASN A 110 45.534 18.053 48.067 1.00 27.77 N ANISOU 561 ND2 ASN A 110 3452 4315 2784 64 -765 1058 N ATOM 562 N LEU A 111 42.919 18.271 43.389 1.00 20.33 N ANISOU 562 N LEU A 111 2519 3106 2099 64 -101 605 N ATOM 563 CA LEU A 111 43.029 17.176 42.438 1.00 19.50 C ANISOU 563 CA LEU A 111 2293 3055 2058 204 51 677 C ATOM 564 C LEU A 111 43.458 17.765 41.096 1.00 20.32 C ANISOU 564 C LEU A 111 2265 3250 2206 208 174 773 C ATOM 565 O LEU A 111 43.237 18.949 40.851 1.00 19.96 O ANISOU 565 O LEU A 111 2584 3069 1932 3 173 654 O ATOM 566 CB LEU A 111 41.676 16.482 42.278 1.00 19.10 C ANISOU 566 CB LEU A 111 2295 3006 1956 204 242 467 C ATOM 567 CG LEU A 111 41.172 15.688 43.480 1.00 19.36 C ANISOU 567 CG LEU A 111 2498 2921 1937 118 158 523 C ATOM 568 CD1 LEU A 111 39.708 15.329 43.265 1.00 18.64 C ANISOU 568 CD1 LEU A 111 2456 2770 1856 191 358 96 C ATOM 569 CD2 LEU A 111 42.009 14.447 43.735 1.00 21.25 C ANISOU 569 CD2 LEU A 111 2807 3036 2229 266 169 683 C ATOM 570 N PRO A 112 44.059 16.936 40.222 1.00 20.50 N ANISOU 570 N PRO A 112 2402 3256 2131 408 135 857 N ATOM 571 CA PRO A 112 44.562 17.434 38.943 1.00 19.97 C ANISOU 571 CA PRO A 112 1901 3503 2184 323 314 645 C ATOM 572 C PRO A 112 43.417 17.946 38.062 1.00 18.83 C ANISOU 572 C PRO A 112 2048 2993 2113 140 243 612 C ATOM 573 O PRO A 112 42.373 17.336 38.014 1.00 18.56 O ANISOU 573 O PRO A 112 2079 2862 2110 149 274 718 O ATOM 574 CB PRO A 112 45.258 16.238 38.270 1.00 21.52 C ANISOU 574 CB PRO A 112 2137 3765 2272 751 390 800 C ATOM 575 CG PRO A 112 44.718 15.020 38.984 1.00 24.74 C ANISOU 575 CG PRO A 112 3032 3699 2665 505 547 676 C ATOM 576 CD PRO A 112 44.394 15.509 40.381 1.00 22.37 C ANISOU 576 CD PRO A 112 2724 3389 2386 647 298 892 C ATOM 577 N VAL A 113 43.697 19.004 37.298 1.00 17.23 N ANISOU 577 N VAL A 113 1624 2907 2014 21 336 499 N ATOM 578 CA VAL A 113 42.788 19.477 36.264 1.00 16.41 C ANISOU 578 CA VAL A 113 1607 2688 1939 250 538 426 C ATOM 579 C VAL A 113 43.085 18.715 34.975 1.00 16.57 C ANISOU 579 C VAL A 113 1735 2512 2047 365 591 456 C ATOM 580 O VAL A 113 44.118 18.955 34.345 1.00 18.51 O ANISOU 580 O VAL A 113 1887 3140 2003 325 741 383 O ATOM 581 CB VAL A 113 42.869 20.999 36.081 1.00 17.11 C ANISOU 581 CB VAL A 113 1619 2696 2185 0 453 413 C ATOM 582 CG1 VAL A 113 41.919 21.462 34.987 1.00 17.09 C ANISOU 582 CG1 VAL A 113 1592 2644 2256 190 568 549 C ATOM 583 CG2 VAL A 113 42.562 21.727 37.380 1.00 18.38 C ANISOU 583 CG2 VAL A 113 2030 2690 2263 -95 500 346 C ATOM 584 N ALA A 114 42.173 17.838 34.563 1.00 16.06 N ANISOU 584 N ALA A 114 2068 2344 1690 374 450 518 N ATOM 585 CA ALA A 114 42.396 16.963 33.409 1.00 16.60 C ANISOU 585 CA ALA A 114 2189 2371 1744 561 496 519 C ATOM 586 C ALA A 114 42.254 17.711 32.079 1.00 16.94 C ANISOU 586 C ALA A 114 2083 2602 1750 604 694 601 C ATOM 587 O ALA A 114 42.967 17.395 31.132 1.00 19.99 O ANISOU 587 O ALA A 114 2595 3248 1749 1199 726 624 O ATOM 588 CB ALA A 114 41.441 15.791 33.449 1.00 17.66 C ANISOU 588 CB ALA A 114 2507 2350 1851 476 501 515 C ATOM 589 N LEU A 115 41.324 18.646 31.992 1.00 14.28 N ANISOU 589 N LEU A 115 1753 2147 1524 257 492 381 N ATOM 590 CA LEU A 115 41.062 19.332 30.747 1.00 14.31 C ANISOU 590 CA LEU A 115 1800 2101 1536 302 565 391 C ATOM 591 C LEU A 115 40.228 20.570 31.015 1.00 13.29 C ANISOU 591 C LEU A 115 1603 2078 1365 248 458 239 C ATOM 592 O LEU A 115 39.571 20.694 32.056 1.00 13.40 O ANISOU 592 O LEU A 115 1535 2099 1455 168 491 245 O ATOM 593 CB LEU A 115 40.340 18.430 29.746 1.00 15.72 C ANISOU 593 CB LEU A 115 2169 1998 1806 321 507 225 C ATOM 594 CG LEU A 115 38.958 17.928 30.158 1.00 17.41 C ANISOU 594 CG LEU A 115 2333 2230 2050 -34 300 261 C ATOM 595 CD1 LEU A 115 37.830 18.830 29.675 1.00 16.93 C ANISOU 595 CD1 LEU A 115 2106 2243 2083 -71 440 68 C ATOM 596 CD2 LEU A 115 38.729 16.520 29.656 1.00 21.39 C ANISOU 596 CD2 LEU A 115 2962 2207 2956 89 0 170 C ATOM 597 N ALA A 116 40.245 21.446 30.014 1.00 12.78 N ANISOU 597 N ALA A 116 1507 1914 1434 120 510 223 N ATOM 598 CA ALA A 116 39.331 22.589 29.957 1.00 12.55 C ANISOU 598 CA ALA A 116 1525 2008 1235 203 547 144 C ATOM 599 C ALA A 116 38.703 22.643 28.572 1.00 12.27 C ANISOU 599 C ALA A 116 1509 1885 1268 138 444 145 C ATOM 600 O ALA A 116 39.357 22.345 27.562 1.00 13.36 O ANISOU 600 O ALA A 116 1724 2065 1283 270 498 135 O ATOM 601 CB ALA A 116 40.049 23.882 30.231 1.00 13.16 C ANISOU 601 CB ALA A 116 1655 2038 1305 158 503 43 C ATOM 602 N VAL A 117 37.424 23.037 28.547 1.00 12.05 N ANISOU 602 N VAL A 117 1538 1822 1217 133 432 69 N ATOM 603 CA VAL A 117 36.742 23.331 27.285 1.00 12.41 C ANISOU 603 CA VAL A 117 1721 1846 1148 210 397 -44 C ATOM 604 C VAL A 117 36.274 24.783 27.360 1.00 11.88 C ANISOU 604 C VAL A 117 1530 1768 1215 151 320 -67 C ATOM 605 O VAL A 117 35.789 25.229 28.413 1.00 12.17 O ANISOU 605 O VAL A 117 1583 1797 1243 135 371 -89 O ATOM 606 CB VAL A 117 35.582 22.353 27.036 1.00 13.47 C ANISOU 606 CB VAL A 117 1887 1785 1443 193 231 -161 C ATOM 607 CG1 VAL A 117 34.553 22.347 28.161 1.00 14.43 C ANISOU 607 CG1 VAL A 117 1859 1988 1635 117 282 -177 C ATOM 608 CG2 VAL A 117 34.908 22.618 25.708 1.00 15.17 C ANISOU 608 CG2 VAL A 117 2451 1860 1451 54 115 -121 C ATOM 609 N VAL A 118 36.439 25.517 26.250 1.00 12.08 N ANISOU 609 N VAL A 118 1642 1664 1281 174 303 -16 N ATOM 610 CA VAL A 118 36.111 26.934 26.206 1.00 11.92 C ANISOU 610 CA VAL A 118 1583 1656 1288 212 290 -61 C ATOM 611 C VAL A 118 35.043 27.139 25.143 1.00 12.31 C ANISOU 611 C VAL A 118 1798 1573 1306 212 194 -38 C ATOM 612 O VAL A 118 35.037 26.437 24.118 1.00 13.56 O ANISOU 612 O VAL A 118 2099 1743 1307 304 153 -120 O ATOM 613 CB VAL A 118 37.389 27.746 25.961 1.00 13.81 C ANISOU 613 CB VAL A 118 1799 1901 1547 17 440 -190 C ATOM 614 CG1 VAL A 118 38.379 27.537 27.086 1.00 15.10 C ANISOU 614 CG1 VAL A 118 1613 2267 1858 127 357 -477 C ATOM 615 CG2 VAL A 118 38.043 27.422 24.619 1.00 15.15 C ANISOU 615 CG2 VAL A 118 2066 1959 1729 -33 616 -297 C ATOM 616 N THR A 119 34.124 28.089 25.381 1.00 12.05 N ANISOU 616 N THR A 119 1557 1620 1399 144 122 -68 N ATOM 617 CA THR A 119 32.837 28.049 24.690 1.00 12.67 C ANISOU 617 CA THR A 119 1632 1752 1427 222 70 -146 C ATOM 618 C THR A 119 32.667 29.073 23.549 1.00 12.94 C ANISOU 618 C THR A 119 1792 1723 1400 195 -13 -173 C ATOM 619 O THR A 119 31.632 29.000 22.895 1.00 14.68 O ANISOU 619 O THR A 119 1916 2041 1621 161 -178 -11 O ATOM 620 CB THR A 119 31.691 28.089 25.708 1.00 13.25 C ANISOU 620 CB THR A 119 1618 1963 1451 169 86 -227 C ATOM 621 OG1 THR A 119 31.683 29.322 26.429 1.00 13.32 O ANISOU 621 OG1 THR A 119 1560 2008 1490 155 87 -271 O ATOM 622 CG2 THR A 119 31.709 26.889 26.628 1.00 13.58 C ANISOU 622 CG2 THR A 119 1720 1971 1467 54 192 -222 C ATOM 623 N HIS A 120 33.641 29.948 23.289 1.00 12.93 N ANISOU 623 N HIS A 120 1954 1653 1305 188 -6 -127 N ATOM 624 CA HIS A 120 33.796 30.656 22.014 1.00 13.60 C ANISOU 624 CA HIS A 120 2096 1756 1314 279 93 -111 C ATOM 625 C HIS A 120 35.046 31.534 22.111 1.00 13.13 C ANISOU 625 C HIS A 120 2000 1713 1274 363 175 -112 C ATOM 626 O HIS A 120 35.583 31.756 23.191 1.00 13.35 O ANISOU 626 O HIS A 120 1946 1826 1297 169 190 -23 O ATOM 627 CB HIS A 120 32.570 31.466 21.566 1.00 14.66 C ANISOU 627 CB HIS A 120 2231 1893 1444 293 -65 -38 C ATOM 628 CG HIS A 120 32.126 32.575 22.444 1.00 14.92 C ANISOU 628 CG HIS A 120 2186 1958 1522 383 -152 -94 C ATOM 629 ND1 HIS A 120 31.363 32.338 23.562 1.00 15.29 N ANISOU 629 ND1 HIS A 120 2099 2061 1646 483 -25 -192 N ATOM 630 CD2 HIS A 120 32.318 33.905 22.365 1.00 14.81 C ANISOU 630 CD2 HIS A 120 2210 1894 1522 435 -8 -227 C ATOM 631 CE1 HIS A 120 31.106 33.494 24.144 1.00 15.48 C ANISOU 631 CE1 HIS A 120 2133 2090 1657 613 79 -179 C ATOM 632 NE2 HIS A 120 31.654 34.474 23.437 1.00 15.24 N ANISOU 632 NE2 HIS A 120 2013 2119 1656 551 24 -229 N ATOM 633 N ALA A 121 35.406 32.093 20.965 1.00 14.47 N ANISOU 633 N ALA A 121 2433 1808 1256 278 195 -84 N ATOM 634 CA ALA A 121 36.623 32.927 20.834 1.00 14.84 C ANISOU 634 CA ALA A 121 2620 1668 1350 233 364 -21 C ATOM 635 C ALA A 121 36.352 34.402 21.153 1.00 15.01 C ANISOU 635 C ALA A 121 2681 1668 1352 265 292 11 C ATOM 636 O ALA A 121 36.493 35.258 20.314 1.00 18.11 O ANISOU 636 O ALA A 121 3525 1844 1509 348 578 157 O ATOM 637 CB ALA A 121 37.222 32.720 19.461 1.00 15.68 C ANISOU 637 CB ALA A 121 2763 1779 1413 119 443 -16 C ATOM 638 N HIS A 122 36.006 34.662 22.415 1.00 14.13 N ANISOU 638 N HIS A 122 2371 1664 1331 173 273 -15 N ATOM 639 CA HIS A 122 35.978 36.014 23.001 1.00 14.40 C ANISOU 639 CA HIS A 122 2456 1593 1421 248 235 0 C ATOM 640 C HIS A 122 36.821 35.945 24.274 1.00 13.64 C ANISOU 640 C HIS A 122 2147 1659 1375 202 324 -120 C ATOM 641 O HIS A 122 37.002 34.881 24.862 1.00 13.88 O ANISOU 641 O HIS A 122 2065 1683 1525 180 237 -133 O ATOM 642 CB HIS A 122 34.558 36.526 23.299 1.00 15.39 C ANISOU 642 CB HIS A 122 2463 1773 1608 346 -40 -101 C ATOM 643 CG HIS A 122 33.801 37.000 22.109 1.00 16.22 C ANISOU 643 CG HIS A 122 2933 1671 1556 440 -121 -68 C ATOM 644 ND1 HIS A 122 32.452 37.213 22.138 1.00 17.70 N ANISOU 644 ND1 HIS A 122 3056 1952 1716 626 -185 -55 N ATOM 645 CD2 HIS A 122 34.200 37.403 20.891 1.00 17.33 C ANISOU 645 CD2 HIS A 122 2925 1879 1780 293 34 74 C ATOM 646 CE1 HIS A 122 32.038 37.727 21.019 1.00 18.08 C ANISOU 646 CE1 HIS A 122 3193 1911 1765 558 -219 -68 C ATOM 647 NE2 HIS A 122 33.085 37.832 20.210 1.00 18.60 N ANISOU 647 NE2 HIS A 122 3342 1997 1728 406 -167 101 N ATOM 648 N GLN A 123 37.273 37.115 24.734 1.00 14.11 N ANISOU 648 N GLN A 123 2198 1640 1522 100 386 -105 N ATOM 649 CA GLN A 123 38.269 37.192 25.789 1.00 14.86 C ANISOU 649 CA GLN A 123 2166 1815 1664 4 350 -140 C ATOM 650 C GLN A 123 37.791 36.610 27.120 1.00 13.76 C ANISOU 650 C GLN A 123 1911 1725 1590 110 416 -259 C ATOM 651 O GLN A 123 38.593 36.072 27.880 1.00 14.19 O ANISOU 651 O GLN A 123 1801 1991 1597 34 338 -247 O ATOM 652 CB GLN A 123 38.705 38.634 26.021 1.00 15.66 C ANISOU 652 CB GLN A 123 2304 1887 1759 -111 561 -239 C ATOM 653 CG GLN A 123 39.869 38.723 26.992 1.00 16.85 C ANISOU 653 CG GLN A 123 2263 2297 1840 -351 582 -355 C ATOM 654 CD GLN A 123 40.251 40.107 27.414 1.00 20.38 C ANISOU 654 CD GLN A 123 3129 2386 2226 -638 593 -330 C ATOM 655 OE1 GLN A 123 39.809 41.083 26.833 1.00 21.90 O ANISOU 655 OE1 GLN A 123 4400 2013 1905 -611 1037 -272 O ATOM 656 NE2 GLN A 123 41.067 40.177 28.458 1.00 23.07 N ANISOU 656 NE2 GLN A 123 2878 3151 2736 -439 416 -842 N ATOM 657 N ASP A 124 36.508 36.799 27.438 1.00 13.61 N ANISOU 657 N ASP A 124 1863 1701 1607 196 340 -144 N ATOM 658 CA ASP A 124 35.993 36.295 28.700 1.00 13.27 C ANISOU 658 CA ASP A 124 1738 1798 1505 80 274 -193 C ATOM 659 C ASP A 124 36.037 34.770 28.798 1.00 12.22 C ANISOU 659 C ASP A 124 1366 1804 1471 77 301 -175 C ATOM 660 O ASP A 124 36.039 34.231 29.892 1.00 13.24 O ANISOU 660 O ASP A 124 1702 1959 1367 107 274 -231 O ATOM 661 CB ASP A 124 34.577 36.806 28.934 1.00 13.72 C ANISOU 661 CB ASP A 124 1764 1817 1632 220 216 -258 C ATOM 662 CG ASP A 124 33.556 36.641 27.821 1.00 14.27 C ANISOU 662 CG ASP A 124 1778 1906 1736 159 172 -135 C ATOM 663 OD1 ASP A 124 33.932 36.524 26.623 1.00 15.29 O ANISOU 663 OD1 ASP A 124 1967 2184 1656 254 116 -157 O ATOM 664 OD2 ASP A 124 32.347 36.690 28.180 1.00 15.92 O ANISOU 664 OD2 ASP A 124 1716 2417 1913 198 148 -165 O ATOM 665 N LYS A 125 36.056 34.095 27.634 1.00 12.57 N ANISOU 665 N LYS A 125 1662 1695 1417 54 237 -137 N ATOM 666 CA LYS A 125 36.001 32.634 27.578 1.00 12.15 C ANISOU 666 CA LYS A 125 1544 1685 1385 84 226 -157 C ATOM 667 C LYS A 125 37.361 31.996 27.273 1.00 11.88 C ANISOU 667 C LYS A 125 1494 1704 1316 52 183 -53 C ATOM 668 O LYS A 125 37.594 30.845 27.655 1.00 12.20 O ANISOU 668 O LYS A 125 1586 1702 1347 97 320 -83 O ATOM 669 CB LYS A 125 35.009 32.172 26.505 1.00 12.66 C ANISOU 669 CB LYS A 125 1665 1796 1346 55 235 -164 C ATOM 670 CG LYS A 125 33.641 32.850 26.514 1.00 13.30 C ANISOU 670 CG LYS A 125 1789 1857 1406 179 154 -242 C ATOM 671 CD LYS A 125 32.713 32.414 27.626 1.00 13.42 C ANISOU 671 CD LYS A 125 1593 1924 1582 144 164 -235 C ATOM 672 CE LYS A 125 32.979 33.030 28.988 1.00 13.59 C ANISOU 672 CE LYS A 125 1665 2045 1454 78 145 -103 C ATOM 673 NZ LYS A 125 32.197 32.341 30.052 1.00 13.80 N ANISOU 673 NZ LYS A 125 1390 2215 1637 73 246 -91 N ATOM 674 N MET A 126 38.223 32.718 26.543 1.00 12.64 N ANISOU 674 N MET A 126 1588 1731 1482 77 331 -39 N ATOM 675 CA AMET A 126 39.495 32.150 26.060 0.67 12.62 C ANISOU 675 CA AMET A 126 1636 1752 1407 160 314 12 C ATOM 676 CA BMET A 126 39.467 32.182 26.009 0.33 12.97 C ANISOU 676 CA BMET A 126 1634 1784 1507 146 351 41 C ATOM 677 C MET A 126 40.687 33.033 26.412 1.00 12.66 C ANISOU 677 C MET A 126 1591 1847 1370 84 470 116 C ATOM 678 O MET A 126 41.825 32.697 26.020 1.00 13.90 O ANISOU 678 O MET A 126 1544 2111 1627 10 544 -19 O ATOM 679 CB AMET A 126 39.498 31.898 24.541 0.67 12.83 C ANISOU 679 CB AMET A 126 1874 1648 1352 86 437 42 C ATOM 680 CB BMET A 126 39.338 32.127 24.482 0.33 14.28 C ANISOU 680 CB BMET A 126 2025 1899 1499 81 326 86 C ATOM 681 CG AMET A 126 38.587 30.801 24.143 0.67 12.52 C ANISOU 681 CG AMET A 126 1795 1683 1276 142 424 -81 C ATOM 682 CG BMET A 126 40.091 31.004 23.817 0.33 14.82 C ANISOU 682 CG BMET A 126 2170 1805 1656 163 219 99 C ATOM 683 SD AMET A 126 38.513 30.379 22.385 0.67 13.41 S ANISOU 683 SD AMET A 126 2001 1772 1321 210 350 -117 S ATOM 684 SD BMET A 126 39.392 30.716 22.180 0.33 16.35 S ANISOU 684 SD BMET A 126 2683 1885 1642 386 145 -109 S ATOM 685 CE AMET A 126 40.105 29.578 22.139 0.67 14.09 C ANISOU 685 CE AMET A 126 2048 1739 1566 195 490 -121 C ATOM 686 CE BMET A 126 40.285 29.239 21.698 0.33 15.48 C ANISOU 686 CE BMET A 126 2316 2152 1411 344 483 -196 C ATOM 687 N GLY A 127 40.491 34.123 27.153 1.00 13.00 N ANISOU 687 N GLY A 127 1600 1835 1503 45 431 -22 N ATOM 688 CA GLY A 127 41.590 35.049 27.424 1.00 14.25 C ANISOU 688 CA GLY A 127 1679 2020 1713 -72 494 -44 C ATOM 689 C GLY A 127 42.703 34.452 28.264 1.00 13.68 C ANISOU 689 C GLY A 127 1562 2037 1596 -76 533 -152 C ATOM 690 O GLY A 127 43.820 34.985 28.268 1.00 16.02 O ANISOU 690 O GLY A 127 1650 2297 2139 -263 372 182 O ATOM 691 N GLY A 128 42.440 33.351 28.979 1.00 13.72 N ANISOU 691 N GLY A 128 1417 2188 1609 -143 424 13 N ATOM 692 CA GLY A 128 43.444 32.775 29.868 1.00 14.12 C ANISOU 692 CA GLY A 128 1209 2346 1810 -38 444 -38 C ATOM 693 C GLY A 128 44.034 31.467 29.360 1.00 12.90 C ANISOU 693 C GLY A 128 1101 2150 1650 -143 374 191 C ATOM 694 O GLY A 128 44.579 30.677 30.136 1.00 14.14 O ANISOU 694 O GLY A 128 1262 2364 1744 -73 270 245 O ATOM 695 N MET A 129 43.954 31.217 28.056 1.00 13.48 N ANISOU 695 N MET A 129 1413 2102 1604 -34 460 132 N ATOM 696 CA AMET A 129 44.446 29.941 27.494 0.57 13.81 C ANISOU 696 CA AMET A 129 1344 2125 1778 -7 492 142 C ATOM 697 CA BMET A 129 44.436 29.963 27.500 0.43 13.25 C ANISOU 697 CA BMET A 129 1361 2101 1571 -14 477 156 C ATOM 698 C MET A 129 45.918 29.703 27.845 1.00 14.68 C ANISOU 698 C MET A 129 1413 2304 1858 72 410 159 C ATOM 699 O MET A 129 46.280 28.564 28.185 1.00 15.84 O ANISOU 699 O MET A 129 1391 2395 2230 167 382 223 O ATOM 700 CB AMET A 129 44.321 29.863 25.971 0.57 14.91 C ANISOU 700 CB AMET A 129 1575 2314 1776 84 580 147 C ATOM 701 CB BMET A 129 44.210 29.983 25.987 0.43 13.02 C ANISOU 701 CB BMET A 129 1459 1975 1511 82 628 67 C ATOM 702 CG AMET A 129 42.925 29.935 25.409 0.57 15.13 C ANISOU 702 CG AMET A 129 1650 2329 1769 86 462 29 C ATOM 703 CG BMET A 129 44.469 28.665 25.313 0.43 12.66 C ANISOU 703 CG BMET A 129 1536 1916 1355 149 526 143 C ATOM 704 SD AMET A 129 41.738 28.771 26.131 0.57 15.67 S ANISOU 704 SD AMET A 129 1781 2316 1858 3 455 66 S ATOM 705 SD BMET A 129 43.274 27.416 25.786 0.43 13.50 S ANISOU 705 SD BMET A 129 1693 1886 1549 -39 289 58 S ATOM 706 CE AMET A 129 42.307 27.279 25.331 0.57 16.92 C ANISOU 706 CE AMET A 129 2007 1929 2492 18 471 261 C ATOM 707 CE BMET A 129 41.814 28.093 24.994 0.43 13.20 C ANISOU 707 CE BMET A 129 1682 1919 1411 -21 307 -65 C ATOM 708 N ASP A 130 46.774 30.720 27.754 1.00 15.16 N ANISOU 708 N ASP A 130 1351 2409 1998 29 533 205 N ATOM 709 CA ASP A 130 48.192 30.490 28.062 1.00 16.36 C ANISOU 709 CA ASP A 130 1359 2714 2140 86 528 268 C ATOM 710 C ASP A 130 48.402 30.000 29.499 1.00 16.14 C ANISOU 710 C ASP A 130 1303 2657 2172 4 498 278 C ATOM 711 O ASP A 130 49.312 29.236 29.750 1.00 17.61 O ANISOU 711 O ASP A 130 1253 2845 2593 17 487 470 O ATOM 712 CB ASP A 130 49.029 31.747 27.821 1.00 17.25 C ANISOU 712 CB ASP A 130 1261 2893 2398 -33 570 369 C ATOM 713 CG ASP A 130 49.496 32.018 26.397 1.00 19.15 C ANISOU 713 CG ASP A 130 1976 2900 2398 -64 702 305 C ATOM 714 OD1 ASP A 130 49.579 31.050 25.604 1.00 19.30 O ANISOU 714 OD1 ASP A 130 2033 3142 2157 243 532 271 O ATOM 715 OD2 ASP A 130 49.909 33.197 26.118 1.00 21.70 O ANISOU 715 OD2 ASP A 130 2506 3062 2676 -275 876 346 O ATOM 716 N ALA A 131 47.609 30.487 30.449 1.00 15.47 N ANISOU 716 N ALA A 131 1190 2578 2107 -19 373 217 N ATOM 717 CA ALA A 131 47.731 30.001 31.835 1.00 16.08 C ANISOU 717 CA ALA A 131 1169 2744 2194 -93 314 363 C ATOM 718 C ALA A 131 47.391 28.512 31.921 1.00 15.92 C ANISOU 718 C ALA A 131 1210 2703 2135 -54 235 238 C ATOM 719 O ALA A 131 48.045 27.777 32.656 1.00 16.75 O ANISOU 719 O ALA A 131 1270 2808 2285 2 273 381 O ATOM 720 CB ALA A 131 46.855 30.804 32.758 1.00 16.87 C ANISOU 720 CB ALA A 131 1254 2888 2265 -85 217 124 C ATOM 721 N LEU A 132 46.369 28.070 31.185 1.00 14.91 N ANISOU 721 N LEU A 132 1114 2515 2036 -58 378 151 N ATOM 722 CA LEU A 132 46.050 26.656 31.191 1.00 15.16 C ANISOU 722 CA LEU A 132 1348 2433 1979 60 435 210 C ATOM 723 C LEU A 132 47.209 25.840 30.600 1.00 15.70 C ANISOU 723 C LEU A 132 1363 2529 2071 86 449 294 C ATOM 724 O LEU A 132 47.590 24.786 31.122 1.00 16.86 O ANISOU 724 O LEU A 132 1477 2707 2220 214 500 433 O ATOM 725 CB LEU A 132 44.763 26.390 30.405 1.00 14.67 C ANISOU 725 CB LEU A 132 1312 2255 2007 49 464 185 C ATOM 726 CG LEU A 132 43.494 27.028 30.964 1.00 14.09 C ANISOU 726 CG LEU A 132 1252 2133 1967 97 354 233 C ATOM 727 CD1 LEU A 132 42.310 26.641 30.089 1.00 14.80 C ANISOU 727 CD1 LEU A 132 1251 2214 2159 172 333 -27 C ATOM 728 CD2 LEU A 132 43.216 26.613 32.397 1.00 15.33 C ANISOU 728 CD2 LEU A 132 1434 2399 1991 52 452 229 C ATOM 729 N HIS A 133 47.771 26.333 29.487 1.00 16.20 N ANISOU 729 N HIS A 133 1382 2542 2231 180 604 413 N ATOM 730 CA HIS A 133 48.871 25.631 28.829 1.00 16.93 C ANISOU 730 CA HIS A 133 1463 2707 2261 283 667 471 C ATOM 731 C HIS A 133 50.119 25.621 29.713 1.00 17.61 C ANISOU 731 C HIS A 133 1281 2907 2501 400 705 374 C ATOM 732 O HIS A 133 50.797 24.602 29.790 1.00 19.81 O ANISOU 732 O HIS A 133 1541 3077 2906 590 787 584 O ATOM 733 CB HIS A 133 49.143 26.235 27.448 1.00 17.21 C ANISOU 733 CB HIS A 133 1589 2710 2240 285 732 389 C ATOM 734 CG HIS A 133 47.984 26.041 26.527 1.00 16.64 C ANISOU 734 CG HIS A 133 1878 2373 2069 159 670 303 C ATOM 735 ND1 HIS A 133 47.852 26.743 25.360 1.00 17.26 N ANISOU 735 ND1 HIS A 133 2031 2436 2090 213 542 318 N ATOM 736 CD2 HIS A 133 46.921 25.216 26.600 1.00 16.97 C ANISOU 736 CD2 HIS A 133 2180 2258 2007 15 716 195 C ATOM 737 CE1 HIS A 133 46.732 26.365 24.755 1.00 17.62 C ANISOU 737 CE1 HIS A 133 2381 2440 1872 -104 462 268 C ATOM 738 NE2 HIS A 133 46.129 25.426 25.499 1.00 17.45 N ANISOU 738 NE2 HIS A 133 2306 2326 1996 -72 685 128 N ATOM 739 N ALA A 134 50.413 26.729 30.386 1.00 18.11 N ANISOU 739 N ALA A 134 1323 2895 2662 238 479 454 N ATOM 740 CA ALA A 134 51.550 26.764 31.299 1.00 19.81 C ANISOU 740 CA ALA A 134 1172 3381 2973 191 440 586 C ATOM 741 C ALA A 134 51.414 25.705 32.399 1.00 20.14 C ANISOU 741 C ALA A 134 1183 3480 2988 54 445 622 C ATOM 742 O ALA A 134 52.418 25.203 32.909 1.00 22.34 O ANISOU 742 O ALA A 134 1376 3861 3248 103 323 954 O ATOM 743 CB ALA A 134 51.685 28.131 31.903 1.00 20.39 C ANISOU 743 CB ALA A 134 1309 3440 2997 0 268 560 C ATOM 744 N ALA A 135 50.179 25.406 32.789 1.00 18.72 N ANISOU 744 N ALA A 135 1289 3289 2531 -25 475 666 N ATOM 745 CA ALA A 135 49.864 24.479 33.865 1.00 19.37 C ANISOU 745 CA ALA A 135 1384 3288 2685 104 337 833 C ATOM 746 C ALA A 135 49.841 23.031 33.358 1.00 20.04 C ANISOU 746 C ALA A 135 1432 3226 2955 184 386 883 C ATOM 747 O ALA A 135 49.651 22.127 34.152 1.00 22.49 O ANISOU 747 O ALA A 135 1744 3429 3370 317 344 1216 O ATOM 748 CB ALA A 135 48.544 24.861 34.496 1.00 19.54 C ANISOU 748 CB ALA A 135 1346 3326 2750 -210 446 641 C ATOM 749 N GLY A 136 49.954 22.818 32.050 1.00 19.62 N ANISOU 749 N GLY A 136 1383 3065 3003 275 479 772 N ATOM 750 CA GLY A 136 49.960 21.479 31.486 1.00 21.20 C ANISOU 750 CA GLY A 136 1606 3062 3384 525 403 706 C ATOM 751 C GLY A 136 48.573 20.890 31.280 1.00 20.05 C ANISOU 751 C GLY A 136 1735 2790 3090 502 506 762 C ATOM 752 O GLY A 136 48.447 19.669 31.146 1.00 22.74 O ANISOU 752 O GLY A 136 1908 2797 3935 603 313 618 O ATOM 753 N ILE A 137 47.543 21.735 31.196 1.00 17.47 N ANISOU 753 N ILE A 137 1537 2631 2469 373 529 722 N ATOM 754 CA ILE A 137 46.160 21.266 31.069 1.00 16.62 C ANISOU 754 CA ILE A 137 1672 2521 2121 243 530 498 C ATOM 755 C ILE A 137 45.799 21.138 29.578 1.00 16.32 C ANISOU 755 C ILE A 137 1679 2496 2025 230 708 449 C ATOM 756 O ILE A 137 46.045 22.048 28.800 1.00 18.14 O ANISOU 756 O ILE A 137 2149 2683 2059 46 672 535 O ATOM 757 CB ILE A 137 45.225 22.237 31.810 1.00 15.66 C ANISOU 757 CB ILE A 137 1423 2451 2075 116 540 542 C ATOM 758 CG1 ILE A 137 45.518 22.253 33.303 1.00 16.78 C ANISOU 758 CG1 ILE A 137 1575 2657 2143 129 397 586 C ATOM 759 CG2 ILE A 137 43.761 21.908 31.545 1.00 15.62 C ANISOU 759 CG2 ILE A 137 1416 2553 1963 151 545 436 C ATOM 760 CD1 ILE A 137 44.954 23.421 34.035 1.00 17.49 C ANISOU 760 CD1 ILE A 137 1638 2693 2311 58 414 363 C ATOM 761 N ALA A 138 45.189 20.018 29.200 1.00 16.64 N ANISOU 761 N ALA A 138 1745 2339 2236 406 449 486 N ATOM 762 CA ALA A 138 44.705 19.795 27.832 1.00 16.43 C ANISOU 762 CA ALA A 138 1829 2315 2096 493 649 400 C ATOM 763 C ALA A 138 43.500 20.689 27.566 1.00 14.55 C ANISOU 763 C ALA A 138 1770 2071 1687 433 735 272 C ATOM 764 O ALA A 138 42.568 20.700 28.373 1.00 15.17 O ANISOU 764 O ALA A 138 1670 2257 1836 414 729 470 O ATOM 765 CB ALA A 138 44.326 18.346 27.638 1.00 17.35 C ANISOU 765 CB ALA A 138 2066 2318 2205 581 612 262 C ATOM 766 N THR A 139 43.496 21.372 26.430 1.00 14.50 N ANISOU 766 N THR A 139 1708 2094 1704 370 723 252 N ATOM 767 CA THR A 139 42.451 22.341 26.142 1.00 14.14 C ANISOU 767 CA THR A 139 1724 1966 1683 248 601 257 C ATOM 768 C THR A 139 41.714 22.014 24.846 1.00 13.36 C ANISOU 768 C THR A 139 1795 1752 1529 285 708 205 C ATOM 769 O THR A 139 42.298 21.532 23.863 1.00 14.36 O ANISOU 769 O THR A 139 1955 1869 1631 247 804 137 O ATOM 770 CB THR A 139 43.016 23.764 26.084 1.00 14.94 C ANISOU 770 CB THR A 139 1860 1998 1819 175 640 103 C ATOM 771 OG1 THR A 139 44.013 23.812 25.056 1.00 15.33 O ANISOU 771 OG1 THR A 139 1997 2089 1736 131 700 248 O ATOM 772 CG2 THR A 139 43.593 24.186 27.420 1.00 16.35 C ANISOU 772 CG2 THR A 139 2112 2252 1847 124 556 105 C ATOM 773 N TYR A 140 40.415 22.328 24.873 1.00 13.09 N ANISOU 773 N TYR A 140 1823 1690 1458 306 630 137 N ATOM 774 CA TYR A 140 39.485 21.983 23.811 1.00 13.29 C ANISOU 774 CA TYR A 140 2040 1710 1299 273 663 82 C ATOM 775 C TYR A 140 38.597 23.177 23.489 1.00 13.15 C ANISOU 775 C TYR A 140 2099 1663 1232 202 541 44 C ATOM 776 O TYR A 140 38.140 23.862 24.395 1.00 13.78 O ANISOU 776 O TYR A 140 2065 1884 1284 394 551 -3 O ATOM 777 CB TYR A 140 38.588 20.818 24.246 1.00 14.11 C ANISOU 777 CB TYR A 140 2107 1763 1490 216 619 129 C ATOM 778 CG TYR A 140 39.345 19.541 24.516 1.00 14.82 C ANISOU 778 CG TYR A 140 2188 1866 1574 351 802 143 C ATOM 779 CD1 TYR A 140 40.003 19.335 25.720 1.00 14.41 C ANISOU 779 CD1 TYR A 140 1963 1781 1728 304 756 138 C ATOM 780 CD2 TYR A 140 39.430 18.554 23.558 1.00 15.01 C ANISOU 780 CD2 TYR A 140 2176 1860 1665 87 879 126 C ATOM 781 CE1 TYR A 140 40.802 18.222 25.922 1.00 16.08 C ANISOU 781 CE1 TYR A 140 2098 1940 2069 310 772 480 C ATOM 782 CE2 TYR A 140 40.203 17.423 23.758 1.00 17.05 C ANISOU 782 CE2 TYR A 140 2511 1810 2155 166 1099 182 C ATOM 783 CZ TYR A 140 40.916 17.265 24.931 1.00 17.05 C ANISOU 783 CZ TYR A 140 2291 1805 2382 314 1009 407 C ATOM 784 OH TYR A 140 41.691 16.161 25.140 1.00 19.86 O ANISOU 784 OH TYR A 140 2523 1994 3026 491 1137 557 O ATOM 785 N ALA A 141 38.298 23.347 22.209 1.00 13.21 N ANISOU 785 N ALA A 141 2028 1731 1257 261 606 -26 N ATOM 786 CA ALA A 141 37.346 24.356 21.755 1.00 13.72 C ANISOU 786 CA ALA A 141 2240 1770 1200 288 450 -2 C ATOM 787 C ALA A 141 36.701 23.866 20.459 1.00 13.83 C ANISOU 787 C ALA A 141 2235 1725 1291 210 490 -77 C ATOM 788 O ALA A 141 37.269 23.035 19.748 1.00 14.85 O ANISOU 788 O ALA A 141 2642 1768 1230 280 544 -81 O ATOM 789 CB ALA A 141 38.023 25.686 21.499 1.00 14.15 C ANISOU 789 CB ALA A 141 2410 1768 1197 299 458 121 C ATOM 790 N ASN A 142 35.531 24.422 20.131 1.00 13.80 N ANISOU 790 N ASN A 142 2257 1804 1179 219 440 -124 N ATOM 791 CA ASN A 142 35.013 24.271 18.770 1.00 14.76 C ANISOU 791 CA ASN A 142 2589 1763 1255 206 301 -125 C ATOM 792 C ASN A 142 36.146 24.521 17.762 1.00 15.08 C ANISOU 792 C ASN A 142 2631 1908 1189 159 274 -135 C ATOM 793 O ASN A 142 36.880 25.502 17.878 1.00 15.11 O ANISOU 793 O ASN A 142 2675 1779 1284 207 395 -106 O ATOM 794 CB ASN A 142 33.858 25.258 18.608 1.00 15.31 C ANISOU 794 CB ASN A 142 2591 1977 1249 291 175 -185 C ATOM 795 CG ASN A 142 33.082 25.182 17.310 1.00 16.34 C ANISOU 795 CG ASN A 142 2921 1926 1358 237 9 -248 C ATOM 796 OD1 ASN A 142 33.437 24.458 16.389 1.00 17.72 O ANISOU 796 OD1 ASN A 142 2960 2303 1468 400 74 -379 O ATOM 797 ND2 ASN A 142 32.012 25.944 17.225 1.00 18.09 N ANISOU 797 ND2 ASN A 142 3014 2249 1607 454 -15 -239 N ATOM 798 N ALA A 143 36.250 23.660 16.754 1.00 15.57 N ANISOU 798 N ALA A 143 2928 1773 1214 183 371 -65 N ATOM 799 CA ALA A 143 37.188 23.903 15.650 1.00 16.95 C ANISOU 799 CA ALA A 143 3235 1912 1292 256 539 -53 C ATOM 800 C ALA A 143 37.095 25.352 15.156 1.00 17.00 C ANISOU 800 C ALA A 143 3332 1844 1282 180 462 -160 C ATOM 801 O ALA A 143 38.121 25.991 14.879 1.00 17.41 O ANISOU 801 O ALA A 143 3329 1944 1341 156 517 -111 O ATOM 802 CB ALA A 143 36.900 22.963 14.508 1.00 18.12 C ANISOU 802 CB ALA A 143 3643 1868 1372 249 549 -97 C ATOM 803 N LEU A 144 35.878 25.869 15.023 1.00 17.12 N ANISOU 803 N LEU A 144 3401 1839 1264 211 273 -94 N ATOM 804 CA LEU A 144 35.707 27.233 14.513 1.00 17.92 C ANISOU 804 CA LEU A 144 3701 1904 1202 225 121 -16 C ATOM 805 C LEU A 144 36.280 28.250 15.505 1.00 16.70 C ANISOU 805 C LEU A 144 3336 1764 1245 285 278 -9 C ATOM 806 O LEU A 144 36.817 29.277 15.071 1.00 17.74 O ANISOU 806 O LEU A 144 3680 1859 1200 169 246 61 O ATOM 807 CB LEU A 144 34.228 27.510 14.218 1.00 18.95 C ANISOU 807 CB LEU A 144 3751 2185 1264 150 -65 -90 C ATOM 808 CG LEU A 144 33.896 28.877 13.620 1.00 19.93 C ANISOU 808 CG LEU A 144 3952 2266 1355 273 -90 -76 C ATOM 809 CD1 LEU A 144 34.666 29.158 12.336 1.00 21.71 C ANISOU 809 CD1 LEU A 144 4344 2541 1362 290 23 55 C ATOM 810 CD2 LEU A 144 32.394 29.005 13.385 1.00 21.74 C ANISOU 810 CD2 LEU A 144 4099 2561 1600 436 -425 15 C ATOM 811 N SER A 145 36.144 28.006 16.810 1.00 15.47 N ANISOU 811 N SER A 145 2973 1675 1228 150 249 -14 N ATOM 812 CA SER A 145 36.761 28.894 17.785 1.00 15.49 C ANISOU 812 CA SER A 145 2949 1668 1266 228 231 -73 C ATOM 813 C SER A 145 38.286 28.918 17.615 1.00 15.22 C ANISOU 813 C SER A 145 3004 1681 1094 272 417 27 C ATOM 814 O SER A 145 38.911 29.970 17.721 1.00 15.80 O ANISOU 814 O SER A 145 2914 1781 1307 233 517 -75 O ATOM 815 CB SER A 145 36.436 28.452 19.206 1.00 14.69 C ANISOU 815 CB SER A 145 2651 1665 1262 250 174 -61 C ATOM 816 OG SER A 145 35.035 28.409 19.441 1.00 14.94 O ANISOU 816 OG SER A 145 2616 1839 1222 288 106 -67 O ATOM 817 N ASN A 146 38.896 27.752 17.374 1.00 15.46 N ANISOU 817 N ASN A 146 2827 1727 1316 260 535 -1 N ATOM 818 CA ASN A 146 40.333 27.699 17.192 1.00 15.87 C ANISOU 818 CA ASN A 146 2872 1821 1335 326 565 82 C ATOM 819 C ASN A 146 40.735 28.422 15.905 1.00 16.58 C ANISOU 819 C ASN A 146 3112 1789 1398 82 676 8 C ATOM 820 O ASN A 146 41.751 29.093 15.881 1.00 17.28 O ANISOU 820 O ASN A 146 3056 1976 1532 60 672 38 O ATOM 821 CB ASN A 146 40.849 26.269 17.216 1.00 15.58 C ANISOU 821 CB ASN A 146 2786 1743 1389 205 693 -79 C ATOM 822 CG ASN A 146 40.768 25.678 18.605 1.00 15.37 C ANISOU 822 CG ASN A 146 2539 1814 1485 341 610 59 C ATOM 823 OD1 ASN A 146 40.864 26.409 19.598 1.00 15.85 O ANISOU 823 OD1 ASN A 146 2573 2017 1429 347 540 46 O ATOM 824 ND2 ASN A 146 40.630 24.367 18.670 1.00 16.22 N ANISOU 824 ND2 ASN A 146 2684 1826 1649 310 643 52 N ATOM 825 N GLN A 147 39.913 28.305 14.870 1.00 17.12 N ANISOU 825 N GLN A 147 3325 1833 1345 122 621 86 N ATOM 826 CA GLN A 147 40.182 29.021 13.614 1.00 18.63 C ANISOU 826 CA GLN A 147 3838 1892 1346 214 807 68 C ATOM 827 C GLN A 147 40.141 30.532 13.847 1.00 17.89 C ANISOU 827 C GLN A 147 3920 1833 1041 99 713 147 C ATOM 828 O GLN A 147 40.984 31.261 13.317 1.00 19.20 O ANISOU 828 O GLN A 147 3909 1921 1463 29 818 126 O ATOM 829 CB GLN A 147 39.154 28.592 12.574 1.00 20.67 C ANISOU 829 CB GLN A 147 4341 2053 1458 220 577 -126 C ATOM 830 CG GLN A 147 39.353 29.222 11.203 1.00 23.84 C ANISOU 830 CG GLN A 147 5119 2477 1459 302 436 34 C ATOM 831 CD GLN A 147 38.128 29.041 10.333 1.00 28.27 C ANISOU 831 CD GLN A 147 5671 3223 1846 58 -32 19 C ATOM 832 OE1 GLN A 147 37.620 27.937 10.147 1.00 31.95 O ANISOU 832 OE1 GLN A 147 6470 3345 2323 -130 -21 -122 O ATOM 833 NE2 GLN A 147 37.616 30.140 9.806 1.00 33.44 N ANISOU 833 NE2 GLN A 147 6470 3737 2497 452 -526 232 N ATOM 834 N LEU A 148 39.138 30.990 14.593 1.00 17.52 N ANISOU 834 N LEU A 148 3722 1845 1087 208 491 52 N ATOM 835 CA LEU A 148 38.911 32.416 14.835 1.00 17.89 C ANISOU 835 CA LEU A 148 3634 1837 1324 168 341 59 C ATOM 836 C LEU A 148 39.871 33.003 15.878 1.00 17.76 C ANISOU 836 C LEU A 148 3666 1821 1258 171 355 10 C ATOM 837 O LEU A 148 40.044 34.223 15.934 1.00 18.29 O ANISOU 837 O LEU A 148 3689 1819 1439 197 297 -3 O ATOM 838 CB LEU A 148 37.481 32.644 15.322 1.00 17.85 C ANISOU 838 CB LEU A 148 3585 1777 1420 214 312 34 C ATOM 839 CG LEU A 148 36.362 32.403 14.317 1.00 19.48 C ANISOU 839 CG LEU A 148 3727 2017 1655 159 138 124 C ATOM 840 CD1 LEU A 148 35.013 32.468 15.024 1.00 20.65 C ANISOU 840 CD1 LEU A 148 3592 2246 2006 290 42 -18 C ATOM 841 CD2 LEU A 148 36.444 33.405 13.177 1.00 22.52 C ANISOU 841 CD2 LEU A 148 3963 2394 2200 53 -106 596 C ATOM 842 N ALA A 149 40.489 32.156 16.699 1.00 17.91 N ANISOU 842 N ALA A 149 3638 1728 1437 38 367 134 N ATOM 843 CA ALA A 149 41.212 32.673 17.876 1.00 17.68 C ANISOU 843 CA ALA A 149 3383 1873 1461 5 392 152 C ATOM 844 C ALA A 149 42.245 33.749 17.498 1.00 17.50 C ANISOU 844 C ALA A 149 3390 1784 1475 81 437 199 C ATOM 845 O ALA A 149 42.241 34.831 18.080 1.00 17.57 O ANISOU 845 O ALA A 149 3266 1816 1593 112 507 105 O ATOM 846 CB ALA A 149 41.818 31.528 18.665 1.00 18.51 C ANISOU 846 CB ALA A 149 3272 1868 1891 -28 354 196 C ATOM 847 N PRO A 150 43.152 33.471 16.551 1.00 18.93 N ANISOU 847 N PRO A 150 3421 1945 1825 62 568 -4 N ATOM 848 CA PRO A 150 44.169 34.476 16.257 1.00 20.14 C ANISOU 848 CA PRO A 150 3658 2141 1850 -80 721 20 C ATOM 849 C PRO A 150 43.581 35.850 15.898 1.00 20.50 C ANISOU 849 C PRO A 150 3791 2196 1802 -98 814 126 C ATOM 850 O PRO A 150 44.033 36.845 16.448 1.00 21.55 O ANISOU 850 O PRO A 150 3872 2141 2174 -204 854 110 O ATOM 851 CB PRO A 150 44.975 33.853 15.110 1.00 22.12 C ANISOU 851 CB PRO A 150 3545 2487 2371 125 835 -192 C ATOM 852 CG PRO A 150 44.849 32.380 15.341 1.00 23.12 C ANISOU 852 CG PRO A 150 3726 2491 2565 216 809 -213 C ATOM 853 CD PRO A 150 43.432 32.211 15.839 1.00 20.40 C ANISOU 853 CD PRO A 150 3789 2074 1887 254 708 18 C ATOM 854 N GLN A 151 42.581 35.915 15.020 1.00 19.69 N ANISOU 854 N GLN A 151 4013 1807 1660 35 742 91 N ATOM 855 CA GLN A 151 42.030 37.219 14.616 1.00 20.37 C ANISOU 855 CA GLN A 151 4433 1864 1443 9 663 290 C ATOM 856 C GLN A 151 41.283 37.882 15.778 1.00 19.14 C ANISOU 856 C GLN A 151 3968 1800 1502 -80 508 206 C ATOM 857 O GLN A 151 41.147 39.107 15.811 1.00 21.22 O ANISOU 857 O GLN A 151 4650 1807 1603 39 448 249 O ATOM 858 CB GLN A 151 41.149 37.104 13.358 1.00 21.29 C ANISOU 858 CB GLN A 151 4723 1952 1413 65 582 282 C ATOM 859 CG GLN A 151 39.799 36.417 13.577 1.00 21.84 C ANISOU 859 CG GLN A 151 4549 2222 1525 130 457 93 C ATOM 860 CD GLN A 151 39.187 35.913 12.290 1.00 22.02 C ANISOU 860 CD GLN A 151 4646 2238 1479 4 626 -33 C ATOM 861 OE1 GLN A 151 39.651 34.952 11.694 1.00 22.90 O ANISOU 861 OE1 GLN A 151 4633 2431 1636 100 588 -152 O ATOM 862 NE2 GLN A 151 38.117 36.541 11.841 1.00 22.93 N ANISOU 862 NE2 GLN A 151 4485 2429 1797 -320 352 163 N ATOM 863 N GLU A 152 40.773 37.082 16.700 1.00 18.32 N ANISOU 863 N GLU A 152 3902 1768 1291 -1 428 189 N ATOM 864 CA GLU A 152 40.067 37.627 17.872 1.00 18.24 C ANISOU 864 CA GLU A 152 3806 1787 1337 123 363 146 C ATOM 865 C GLU A 152 41.056 38.019 18.977 1.00 18.74 C ANISOU 865 C GLU A 152 3691 1897 1532 90 371 64 C ATOM 866 O GLU A 152 40.604 38.488 20.036 1.00 20.75 O ANISOU 866 O GLU A 152 3911 2334 1637 40 376 -225 O ATOM 867 CB GLU A 152 39.036 36.627 18.393 1.00 18.25 C ANISOU 867 CB GLU A 152 3553 1863 1515 134 343 66 C ATOM 868 CG GLU A 152 37.945 36.291 17.402 1.00 19.15 C ANISOU 868 CG GLU A 152 3611 2030 1634 49 297 49 C ATOM 869 CD GLU A 152 37.090 37.489 17.052 1.00 22.35 C ANISOU 869 CD GLU A 152 3880 2418 2191 315 -100 14 C ATOM 870 OE1 GLU A 152 36.893 38.356 17.923 1.00 24.86 O ANISOU 870 OE1 GLU A 152 4424 2222 2797 355 97 -105 O ATOM 871 OE2 GLU A 152 36.699 37.602 15.870 1.00 28.32 O ANISOU 871 OE2 GLU A 152 4371 3730 2659 420 -694 9 O ATOM 872 N GLY A 153 42.355 37.784 18.783 1.00 18.85 N ANISOU 872 N GLY A 153 3702 1819 1641 90 386 112 N ATOM 873 CA GLY A 153 43.351 38.121 19.817 1.00 18.91 C ANISOU 873 CA GLY A 153 3632 1959 1592 -90 488 104 C ATOM 874 C GLY A 153 43.504 37.056 20.887 1.00 18.47 C ANISOU 874 C GLY A 153 3340 2021 1655 142 371 114 C ATOM 875 O GLY A 153 44.080 37.335 21.910 1.00 19.46 O ANISOU 875 O GLY A 153 3471 2294 1628 -14 417 187 O ATOM 876 N MET A 154 43.014 35.861 20.608 1.00 17.67 N ANISOU 876 N MET A 154 3293 1970 1449 138 608 121 N ATOM 877 CA MET A 154 43.066 34.730 21.538 1.00 17.49 C ANISOU 877 CA MET A 154 3143 2008 1493 205 514 175 C ATOM 878 C MET A 154 44.166 33.748 21.094 1.00 17.74 C ANISOU 878 C MET A 154 3186 1997 1555 225 498 126 C ATOM 879 O MET A 154 44.527 33.649 19.914 1.00 19.46 O ANISOU 879 O MET A 154 3339 2365 1687 655 667 198 O ATOM 880 CB MET A 154 41.733 33.963 21.572 1.00 18.21 C ANISOU 880 CB MET A 154 3140 2071 1706 215 726 26 C ATOM 881 CG MET A 154 40.531 34.785 21.927 1.00 18.15 C ANISOU 881 CG MET A 154 3150 2054 1691 195 560 -73 C ATOM 882 SD MET A 154 40.595 35.381 23.600 0.82 16.33 S ANISOU 882 SD MET A 154 2813 1895 1496 99 712 1 S ATOM 883 CE MET A 154 40.858 37.102 23.307 1.00 19.77 C ANISOU 883 CE MET A 154 3180 2304 2026 -30 1107 556 C ATOM 884 N VAL A 155 44.639 32.965 22.050 1.00 16.59 N ANISOU 884 N VAL A 155 2580 2030 1692 198 629 231 N ATOM 885 CA VAL A 155 45.434 31.775 21.810 1.00 16.53 C ANISOU 885 CA VAL A 155 2364 1973 1943 64 658 250 C ATOM 886 C VAL A 155 44.464 30.604 21.589 1.00 15.72 C ANISOU 886 C VAL A 155 2266 1891 1815 140 606 257 C ATOM 887 O VAL A 155 43.537 30.419 22.368 1.00 17.41 O ANISOU 887 O VAL A 155 2442 2234 1936 -14 752 126 O ATOM 888 CB VAL A 155 46.386 31.538 23.000 1.00 18.71 C ANISOU 888 CB VAL A 155 2537 2401 2171 -14 465 469 C ATOM 889 CG1 VAL A 155 47.108 30.203 22.890 1.00 20.07 C ANISOU 889 CG1 VAL A 155 2389 2546 2690 54 405 447 C ATOM 890 CG2 VAL A 155 47.365 32.699 23.136 1.00 20.00 C ANISOU 890 CG2 VAL A 155 2554 2372 2670 50 362 385 C ATOM 891 N ALA A 156 44.690 29.802 20.552 1.00 16.32 N ANISOU 891 N ALA A 156 2347 1949 1904 108 811 203 N ATOM 892 CA ALA A 156 43.827 28.650 20.252 1.00 15.95 C ANISOU 892 CA ALA A 156 2214 1968 1875 143 870 256 C ATOM 893 C ALA A 156 43.985 27.570 21.329 1.00 15.76 C ANISOU 893 C ALA A 156 2209 2070 1708 111 639 179 C ATOM 894 O ALA A 156 45.040 27.425 21.938 1.00 15.86 O ANISOU 894 O ALA A 156 2166 2010 1847 174 639 305 O ATOM 895 CB ALA A 156 44.131 28.059 18.899 1.00 17.31 C ANISOU 895 CB ALA A 156 2731 2117 1726 80 819 281 C ATOM 896 N ALA A 157 42.912 26.805 21.537 1.00 15.42 N ANISOU 896 N ALA A 157 2210 1967 1682 184 759 173 N ATOM 897 CA ALA A 157 43.009 25.561 22.310 1.00 15.21 C ANISOU 897 CA ALA A 157 2283 1935 1560 137 734 130 C ATOM 898 C ALA A 157 43.864 24.554 21.523 1.00 15.85 C ANISOU 898 C ALA A 157 2307 2001 1713 196 850 270 C ATOM 899 O ALA A 157 44.044 24.666 20.304 1.00 16.95 O ANISOU 899 O ALA A 157 2625 2064 1750 267 1023 207 O ATOM 900 CB ALA A 157 41.635 25.005 22.608 1.00 14.90 C ANISOU 900 CB ALA A 157 2239 1825 1595 206 696 138 C ATOM 901 N GLN A 158 44.342 23.550 22.243 1.00 15.66 N ANISOU 901 N GLN A 158 2144 1994 1811 372 928 265 N ATOM 902 CA GLN A 158 45.174 22.518 21.646 1.00 16.95 C ANISOU 902 CA GLN A 158 2143 2270 2027 417 1048 190 C ATOM 903 C GLN A 158 44.383 21.546 20.774 1.00 16.75 C ANISOU 903 C GLN A 158 2243 2177 1942 447 1114 193 C ATOM 904 O GLN A 158 44.955 20.959 19.842 1.00 20.43 O ANISOU 904 O GLN A 158 2694 2717 2349 200 1376 -327 O ATOM 905 CB GLN A 158 45.896 21.723 22.728 1.00 17.66 C ANISOU 905 CB GLN A 158 2128 2306 2275 493 997 253 C ATOM 906 CG GLN A 158 46.933 22.542 23.484 1.00 19.59 C ANISOU 906 CG GLN A 158 2161 2679 2602 395 860 206 C ATOM 907 CD GLN A 158 47.304 21.883 24.788 1.00 20.92 C ANISOU 907 CD GLN A 158 2181 3130 2638 456 949 360 C ATOM 908 OE1 GLN A 158 46.532 21.083 25.332 1.00 22.54 O ANISOU 908 OE1 GLN A 158 2493 3482 2587 229 925 437 O ATOM 909 NE2 GLN A 158 48.442 22.276 25.329 1.00 24.59 N ANISOU 909 NE2 GLN A 158 2305 3658 3377 380 800 113 N ATOM 910 N HIS A 159 43.117 21.348 21.056 1.00 15.64 N ANISOU 910 N HIS A 159 2233 1951 1755 366 1007 164 N ATOM 911 CA HIS A 159 42.304 20.346 20.417 1.00 15.96 C ANISOU 911 CA HIS A 159 2420 1923 1720 353 1098 39 C ATOM 912 C HIS A 159 41.005 20.972 19.919 1.00 15.52 C ANISOU 912 C HIS A 159 2484 1875 1534 272 991 0 C ATOM 913 O HIS A 159 40.485 21.888 20.540 1.00 15.02 O ANISOU 913 O HIS A 159 2342 1798 1566 328 731 5 O ATOM 914 CB HIS A 159 41.966 19.213 21.389 1.00 16.70 C ANISOU 914 CB HIS A 159 2414 1942 1989 327 977 163 C ATOM 915 CG HIS A 159 43.171 18.562 21.961 1.00 18.02 C ANISOU 915 CG HIS A 159 2540 1935 2368 518 1015 295 C ATOM 916 ND1 HIS A 159 43.957 17.701 21.220 1.00 21.09 N ANISOU 916 ND1 HIS A 159 2834 2428 2752 891 869 -22 N ATOM 917 CD2 HIS A 159 43.745 18.652 23.175 1.00 18.78 C ANISOU 917 CD2 HIS A 159 2224 2401 2510 514 983 350 C ATOM 918 CE1 HIS A 159 44.948 17.274 21.969 1.00 22.49 C ANISOU 918 CE1 HIS A 159 2795 2771 2977 1012 881 78 C ATOM 919 NE2 HIS A 159 44.856 17.848 23.162 1.00 21.19 N ANISOU 919 NE2 HIS A 159 2610 2615 2824 859 930 327 N ATOM 920 N SER A 160 40.517 20.455 18.786 1.00 16.38 N ANISOU 920 N SER A 160 2691 1841 1689 361 896 -111 N ATOM 921 CA SER A 160 39.319 20.984 18.137 1.00 16.60 C ANISOU 921 CA SER A 160 2909 1913 1483 355 745 -206 C ATOM 922 C SER A 160 38.167 19.989 18.238 1.00 16.68 C ANISOU 922 C SER A 160 3033 1858 1444 344 644 -139 C ATOM 923 O SER A 160 38.291 18.827 17.861 1.00 19.12 O ANISOU 923 O SER A 160 3314 1897 2054 271 891 -273 O ATOM 924 CB SER A 160 39.586 21.304 16.688 1.00 18.57 C ANISOU 924 CB SER A 160 3406 2090 1558 323 912 -102 C ATOM 925 OG SER A 160 40.473 22.404 16.560 1.00 19.37 O ANISOU 925 OG SER A 160 3681 2130 1545 208 1005 -24 O ATOM 926 N LEU A 161 37.039 20.482 18.718 1.00 16.02 N ANISOU 926 N LEU A 161 2837 1803 1447 230 566 -71 N ATOM 927 CA LEU A 161 35.792 19.746 18.724 1.00 16.17 C ANISOU 927 CA LEU A 161 2942 1818 1382 133 477 -88 C ATOM 928 C LEU A 161 35.072 19.939 17.396 1.00 16.82 C ANISOU 928 C LEU A 161 3281 1816 1292 96 450 -64 C ATOM 929 O LEU A 161 35.060 21.040 16.843 1.00 17.90 O ANISOU 929 O LEU A 161 3473 1811 1515 90 296 8 O ATOM 930 CB LEU A 161 34.884 20.259 19.843 1.00 15.63 C ANISOU 930 CB LEU A 161 2764 1710 1464 177 477 -51 C ATOM 931 CG LEU A 161 35.466 20.239 21.247 1.00 17.20 C ANISOU 931 CG LEU A 161 2913 2172 1448 269 465 -114 C ATOM 932 CD1 LEU A 161 34.420 20.741 22.216 1.00 18.71 C ANISOU 932 CD1 LEU A 161 2957 2735 1413 499 423 -137 C ATOM 933 CD2 LEU A 161 35.925 18.859 21.642 1.00 19.30 C ANISOU 933 CD2 LEU A 161 3212 2284 1835 354 475 -16 C ATOM 934 N THR A 162 34.485 18.853 16.888 1.00 17.80 N ANISOU 934 N THR A 162 3555 1901 1304 31 355 -143 N ATOM 935 CA THR A 162 33.586 18.975 15.750 1.00 19.53 C ANISOU 935 CA THR A 162 3744 2201 1474 -2 178 -348 C ATOM 936 C THR A 162 32.235 18.386 16.155 1.00 18.41 C ANISOU 936 C THR A 162 3629 1906 1459 101 38 -330 C ATOM 937 O THR A 162 32.130 17.666 17.176 1.00 19.13 O ANISOU 937 O THR A 162 3495 2089 1682 -52 133 -114 O ATOM 938 CB THR A 162 34.189 18.340 14.490 1.00 20.27 C ANISOU 938 CB THR A 162 4039 2220 1442 -96 258 -323 C ATOM 939 OG1 THR A 162 34.352 16.947 14.723 1.00 20.54 O ANISOU 939 OG1 THR A 162 3713 2272 1817 101 465 -367 O ATOM 940 CG2 THR A 162 35.519 18.937 14.085 1.00 22.73 C ANISOU 940 CG2 THR A 162 4050 2828 1755 30 648 -244 C ATOM 941 N PHE A 163 31.213 18.725 15.387 1.00 20.03 N ANISOU 941 N PHE A 163 3960 2164 1485 114 -231 -323 N ATOM 942 CA PHE A 163 29.831 18.502 15.786 1.00 21.02 C ANISOU 942 CA PHE A 163 3848 2336 1803 172 -303 -370 C ATOM 943 C PHE A 163 29.058 17.804 14.674 1.00 23.74 C ANISOU 943 C PHE A 163 4313 2720 1986 -9 -351 -586 C ATOM 944 O PHE A 163 29.234 18.122 13.512 1.00 24.39 O ANISOU 944 O PHE A 163 4119 3240 1908 13 -247 -604 O ATOM 945 CB PHE A 163 29.164 19.828 16.168 1.00 21.25 C ANISOU 945 CB PHE A 163 3676 2414 1981 224 -404 -416 C ATOM 946 CG PHE A 163 29.837 20.456 17.358 1.00 19.42 C ANISOU 946 CG PHE A 163 3368 2025 1983 219 -247 -405 C ATOM 947 CD1 PHE A 163 30.925 21.293 17.195 1.00 19.28 C ANISOU 947 CD1 PHE A 163 3363 2052 1908 270 126 -462 C ATOM 948 CD2 PHE A 163 29.439 20.139 18.641 1.00 19.01 C ANISOU 948 CD2 PHE A 163 3151 2065 2007 51 -224 -456 C ATOM 949 CE1 PHE A 163 31.617 21.776 18.292 1.00 19.27 C ANISOU 949 CE1 PHE A 163 3187 1938 2195 124 68 -428 C ATOM 950 CE2 PHE A 163 30.113 20.641 19.739 1.00 18.18 C ANISOU 950 CE2 PHE A 163 3060 1937 1910 106 -162 -402 C ATOM 951 CZ PHE A 163 31.199 21.468 19.567 1.00 17.86 C ANISOU 951 CZ PHE A 163 2823 1993 1969 216 -141 -542 C ATOM 952 N ALA A 164 28.182 16.894 15.071 1.00 24.80 N ANISOU 952 N ALA A 164 4349 2800 2271 -225 -533 -772 N ATOM 953 CA ALA A 164 27.253 16.278 14.128 1.00 27.30 C ANISOU 953 CA ALA A 164 4765 3103 2504 -390 -617 -1047 C ATOM 954 C ALA A 164 26.246 17.328 13.637 1.00 28.34 C ANISOU 954 C ALA A 164 4620 3561 2584 -330 -872 -1038 C ATOM 955 O ALA A 164 26.088 18.376 14.232 1.00 27.50 O ANISOU 955 O ALA A 164 4317 3502 2627 -423 -851 -1019 O ATOM 956 CB ALA A 164 26.547 15.123 14.787 1.00 28.96 C ANISOU 956 CB ALA A 164 4839 3229 2933 -472 -600 -899 C ATOM 957 N ALA A 165 25.529 17.000 12.561 1.00 31.68 N ANISOU 957 N ALA A 165 5290 4084 2662 -490 -1078 -1194 N ATOM 958 CA ALA A 165 24.489 17.877 12.001 1.00 34.53 C ANISOU 958 CA ALA A 165 5508 4495 3117 -484 -1414 -959 C ATOM 959 C ALA A 165 23.449 18.256 13.064 1.00 32.24 C ANISOU 959 C ALA A 165 4818 4245 3185 -641 -1633 -811 C ATOM 960 O ALA A 165 22.916 19.366 13.044 1.00 35.13 O ANISOU 960 O ALA A 165 4964 4464 3919 -558 -1740 -270 O ATOM 961 CB ALA A 165 23.832 17.197 10.826 1.00 37.78 C ANISOU 961 CB ALA A 165 5844 5259 3251 -433 -1690 -1129 C ATOM 962 N ASN A 166 23.172 17.353 14.002 1.00 31.98 N ANISOU 962 N ASN A 166 4727 3926 3498 -999 -1311 -991 N ATOM 963 CA ASN A 166 22.168 17.615 15.036 1.00 31.95 C ANISOU 963 CA ASN A 166 4087 4128 3924 -939 -1401 -895 C ATOM 964 C ASN A 166 22.732 18.442 16.199 1.00 30.35 C ANISOU 964 C ASN A 166 3874 3979 3675 -860 -975 -961 C ATOM 965 O ASN A 166 21.982 18.769 17.114 1.00 30.96 O ANISOU 965 O ASN A 166 3632 4706 3426 -929 -1146 -991 O ATOM 966 CB ASN A 166 21.563 16.330 15.597 1.00 33.15 C ANISOU 966 CB ASN A 166 4103 4057 4436 -1224 -1419 -1101 C ATOM 967 CG ASN A 166 22.541 15.399 16.286 1.00 33.63 C ANISOU 967 CG ASN A 166 4134 4020 4622 -903 -1160 -1229 C ATOM 968 OD1 ASN A 166 23.674 15.763 16.594 1.00 31.79 O ANISOU 968 OD1 ASN A 166 4054 3943 4082 -826 -1107 -1031 O ATOM 969 ND2 ASN A 166 22.110 14.170 16.512 1.00 36.94 N ANISOU 969 ND2 ASN A 166 4486 4180 5370 -1150 -1127 -1143 N ATOM 970 N GLY A 167 24.017 18.778 16.184 1.00 26.75 N ANISOU 970 N GLY A 167 3619 3401 3143 -330 -952 -1093 N ATOM 971 CA GLY A 167 24.581 19.694 17.192 1.00 24.48 C ANISOU 971 CA GLY A 167 3185 3269 2845 -311 -754 -929 C ATOM 972 C GLY A 167 25.431 18.989 18.240 1.00 22.34 C ANISOU 972 C GLY A 167 3049 2662 2776 -192 -528 -1015 C ATOM 973 O GLY A 167 26.234 19.637 18.885 1.00 19.89 O ANISOU 973 O GLY A 167 2751 2424 2380 -82 -442 -711 O ATOM 974 N TRP A 168 25.266 17.676 18.438 1.00 23.20 N ANISOU 974 N TRP A 168 3073 2717 3023 -415 -617 -981 N ATOM 975 CA TRP A 168 26.038 16.993 19.495 1.00 22.27 C ANISOU 975 CA TRP A 168 3006 2622 2832 -315 -272 -889 C ATOM 976 C TRP A 168 27.500 16.864 19.069 1.00 20.57 C ANISOU 976 C TRP A 168 3064 2344 2405 -62 -248 -743 C ATOM 977 O TRP A 168 27.790 16.561 17.908 1.00 21.65 O ANISOU 977 O TRP A 168 3317 2579 2329 -218 -268 -758 O ATOM 978 CB TRP A 168 25.440 15.627 19.847 1.00 24.29 C ANISOU 978 CB TRP A 168 3330 2720 3176 -476 -113 -923 C ATOM 979 CG TRP A 168 24.179 15.768 20.637 1.00 25.26 C ANISOU 979 CG TRP A 168 3265 2777 3554 -679 -28 -1064 C ATOM 980 CD1 TRP A 168 22.911 15.526 20.205 1.00 27.63 C ANISOU 980 CD1 TRP A 168 3292 3325 3881 -590 -51 -1437 C ATOM 981 CD2 TRP A 168 24.064 16.264 21.984 1.00 24.84 C ANISOU 981 CD2 TRP A 168 3100 2832 3505 -682 37 -987 C ATOM 982 NE1 TRP A 168 22.015 15.806 21.201 1.00 28.58 N ANISOU 982 NE1 TRP A 168 3036 3747 4076 -582 13 -1299 N ATOM 983 CE2 TRP A 168 22.691 16.265 22.300 1.00 26.89 C ANISOU 983 CE2 TRP A 168 3040 3204 3972 -654 14 -1059 C ATOM 984 CE3 TRP A 168 24.976 16.722 22.946 1.00 24.39 C ANISOU 984 CE3 TRP A 168 3025 2790 3452 -670 -40 -798 C ATOM 985 CZ2 TRP A 168 22.213 16.697 23.537 1.00 27.92 C ANISOU 985 CZ2 TRP A 168 3043 3625 3939 -502 -39 -1054 C ATOM 986 CZ3 TRP A 168 24.498 17.139 24.172 1.00 24.88 C ANISOU 986 CZ3 TRP A 168 2916 2988 3550 -536 118 -678 C ATOM 987 CH2 TRP A 168 23.134 17.124 24.463 1.00 25.96 C ANISOU 987 CH2 TRP A 168 2942 3342 3578 -436 105 -846 C ATOM 988 N VAL A 169 28.400 17.029 20.021 1.00 19.04 N ANISOU 988 N VAL A 169 2867 2201 2166 -219 -59 -447 N ATOM 989 CA VAL A 169 29.810 16.864 19.744 1.00 17.77 C ANISOU 989 CA VAL A 169 2959 1979 1813 -100 51 -347 C ATOM 990 C VAL A 169 30.059 15.446 19.213 1.00 18.79 C ANISOU 990 C VAL A 169 3217 2001 1918 -155 45 -405 C ATOM 991 O VAL A 169 29.469 14.459 19.665 1.00 20.47 O ANISOU 991 O VAL A 169 3510 2046 2220 -291 158 -423 O ATOM 992 CB VAL A 169 30.684 17.165 20.973 1.00 16.80 C ANISOU 992 CB VAL A 169 2668 2048 1667 -31 199 -348 C ATOM 993 CG1 VAL A 169 30.513 16.137 22.085 1.00 18.59 C ANISOU 993 CG1 VAL A 169 2925 2195 1941 -134 90 -169 C ATOM 994 CG2 VAL A 169 32.155 17.327 20.602 1.00 16.77 C ANISOU 994 CG2 VAL A 169 2579 2182 1607 79 109 -318 C ATOM 995 N GLU A 170 30.936 15.363 18.234 1.00 19.29 N ANISOU 995 N GLU A 170 3588 1959 1780 -76 116 -421 N ATOM 996 CA GLU A 170 31.452 14.082 17.776 1.00 20.77 C ANISOU 996 CA GLU A 170 3869 1924 2095 -107 202 -510 C ATOM 997 C GLU A 170 32.313 13.505 18.911 1.00 20.23 C ANISOU 997 C GLU A 170 3683 1765 2237 113 410 -372 C ATOM 998 O GLU A 170 33.304 14.115 19.300 1.00 19.58 O ANISOU 998 O GLU A 170 3571 1792 2074 99 498 -236 O ATOM 999 CB GLU A 170 32.162 14.312 16.441 1.00 23.84 C ANISOU 999 CB GLU A 170 4532 2569 1956 115 364 -662 C ATOM 1000 CG GLU A 170 31.183 14.770 15.347 1.00 28.61 C ANISOU 1000 CG GLU A 170 4955 3451 2461 -79 -254 -816 C ATOM 1001 CD GLU A 170 31.613 14.821 13.891 1.00 32.71 C ANISOU 1001 CD GLU A 170 5496 4163 2767 -706 93 -586 C ATOM 1002 OE1 GLU A 170 32.607 15.511 13.563 1.00 38.40 O ANISOU 1002 OE1 GLU A 170 5991 4384 4214 -1101 238 -443 O ATOM 1003 OE2 GLU A 170 30.896 14.224 13.073 1.00 43.31 O ANISOU 1003 OE2 GLU A 170 7050 5606 3798 -932 -715 -1475 O ATOM 1004 N PRO A 171 31.878 12.377 19.511 1.00 21.37 N ANISOU 1004 N PRO A 171 3882 1958 2279 32 456 -266 N ATOM 1005 CA PRO A 171 32.529 11.908 20.725 1.00 22.18 C ANISOU 1005 CA PRO A 171 3876 2285 2267 154 634 -45 C ATOM 1006 C PRO A 171 34.049 11.694 20.647 1.00 20.31 C ANISOU 1006 C PRO A 171 3935 1847 1932 189 815 -27 C ATOM 1007 O PRO A 171 34.761 11.884 21.638 1.00 20.35 O ANISOU 1007 O PRO A 171 3897 2032 1800 148 936 0 O ATOM 1008 CB PRO A 171 31.870 10.555 21.008 1.00 25.80 C ANISOU 1008 CB PRO A 171 4103 2630 3069 -6 789 446 C ATOM 1009 CG PRO A 171 30.505 10.668 20.399 1.00 28.59 C ANISOU 1009 CG PRO A 171 4334 3067 3461 -227 462 148 C ATOM 1010 CD PRO A 171 30.691 11.564 19.199 1.00 24.53 C ANISOU 1010 CD PRO A 171 4031 2162 3125 -72 325 -260 C ATOM 1011 N ALA A 172 34.564 11.316 19.490 1.00 20.58 N ANISOU 1011 N ALA A 172 4109 1881 1829 112 714 -144 N ATOM 1012 CA ALA A 172 36.015 11.081 19.382 1.00 20.52 C ANISOU 1012 CA ALA A 172 4162 1882 1749 280 865 -106 C ATOM 1013 C ALA A 172 36.806 12.379 19.571 1.00 18.91 C ANISOU 1013 C ALA A 172 3827 1911 1445 320 829 122 C ATOM 1014 O ALA A 172 38.002 12.300 19.914 1.00 19.58 O ANISOU 1014 O ALA A 172 3832 1852 1755 436 804 123 O ATOM 1015 CB ALA A 172 36.362 10.515 18.038 1.00 22.48 C ANISOU 1015 CB ALA A 172 4278 2186 2076 311 1069 -408 C ATOM 1016 N THR A 173 36.161 13.534 19.370 1.00 18.11 N ANISOU 1016 N THR A 173 3751 1768 1359 225 729 -49 N ATOM 1017 CA THR A 173 36.869 14.805 19.500 1.00 17.47 C ANISOU 1017 CA THR A 173 3409 1755 1473 296 781 -45 C ATOM 1018 C THR A 173 36.837 15.334 20.928 1.00 16.68 C ANISOU 1018 C THR A 173 3191 1677 1466 250 689 -15 C ATOM 1019 O THR A 173 37.569 16.266 21.230 1.00 17.89 O ANISOU 1019 O THR A 173 3419 1840 1536 84 664 -19 O ATOM 1020 CB THR A 173 36.350 15.859 18.521 1.00 17.93 C ANISOU 1020 CB THR A 173 3494 1855 1463 310 807 29 C ATOM 1021 OG1 THR A 173 35.051 16.340 18.873 1.00 17.58 O ANISOU 1021 OG1 THR A 173 3353 1899 1424 249 641 -67 O ATOM 1022 CG2 THR A 173 36.394 15.383 17.085 1.00 20.23 C ANISOU 1022 CG2 THR A 173 4061 2166 1458 220 655 4 C ATOM 1023 N ALA A 174 36.024 14.711 21.789 1.00 16.82 N ANISOU 1023 N ALA A 174 3190 1861 1338 185 666 0 N ATOM 1024 CA ALA A 174 35.910 15.097 23.193 1.00 16.32 C ANISOU 1024 CA ALA A 174 2908 1941 1350 164 612 -49 C ATOM 1025 C ALA A 174 36.208 13.892 24.077 1.00 16.28 C ANISOU 1025 C ALA A 174 3045 1942 1197 130 695 -42 C ATOM 1026 O ALA A 174 35.376 13.484 24.907 1.00 16.76 O ANISOU 1026 O ALA A 174 2963 1941 1463 -113 690 -96 O ATOM 1027 CB ALA A 174 34.534 15.666 23.478 1.00 18.00 C ANISOU 1027 CB ALA A 174 2948 2531 1360 313 402 -44 C ATOM 1028 N PRO A 175 37.393 13.294 23.938 1.00 16.63 N ANISOU 1028 N PRO A 175 3124 1793 1399 206 720 29 N ATOM 1029 CA PRO A 175 37.714 12.133 24.750 1.00 16.69 C ANISOU 1029 CA PRO A 175 3134 1803 1405 141 627 -5 C ATOM 1030 C PRO A 175 37.830 12.493 26.239 1.00 15.46 C ANISOU 1030 C PRO A 175 2773 1682 1416 175 563 4 C ATOM 1031 O PRO A 175 38.315 13.551 26.604 1.00 15.49 O ANISOU 1031 O PRO A 175 2593 1765 1526 82 511 64 O ATOM 1032 CB PRO A 175 39.072 11.695 24.202 1.00 18.40 C ANISOU 1032 CB PRO A 175 3461 2025 1503 446 827 -36 C ATOM 1033 CG PRO A 175 39.700 12.987 23.729 1.00 18.77 C ANISOU 1033 CG PRO A 175 3251 2246 1632 327 687 54 C ATOM 1034 CD PRO A 175 38.535 13.730 23.121 1.00 17.65 C ANISOU 1034 CD PRO A 175 3243 1925 1537 159 747 159 C ATOM 1035 N ASN A 176 37.389 11.564 27.079 1.00 15.98 N ANISOU 1035 N ASN A 176 2957 1644 1469 83 551 5 N ATOM 1036 CA ASN A 176 37.570 11.694 28.550 1.00 16.25 C ANISOU 1036 CA ASN A 176 2779 1976 1417 24 679 72 C ATOM 1037 C ASN A 176 36.859 12.927 29.103 1.00 15.45 C ANISOU 1037 C ASN A 176 2705 1831 1334 -80 589 72 C ATOM 1038 O ASN A 176 37.257 13.466 30.126 1.00 16.54 O ANISOU 1038 O ASN A 176 2892 1921 1472 -12 391 -1 O ATOM 1039 CB ASN A 176 39.056 11.655 28.933 1.00 17.98 C ANISOU 1039 CB ASN A 176 2814 2345 1672 220 622 300 C ATOM 1040 CG ASN A 176 39.716 10.350 28.518 1.00 19.64 C ANISOU 1040 CG ASN A 176 3329 2593 1541 463 678 71 C ATOM 1041 OD1 ASN A 176 40.625 10.307 27.658 1.00 26.44 O ANISOU 1041 OD1 ASN A 176 3940 3906 2197 559 1236 18 O ATOM 1042 ND2 ASN A 176 39.151 9.256 28.975 1.00 19.48 N ANISOU 1042 ND2 ASN A 176 3451 2207 1741 575 443 65 N ATOM 1043 N PHE A 177 35.766 13.339 28.472 1.00 15.50 N ANISOU 1043 N PHE A 177 2527 1860 1501 -149 545 -219 N ATOM 1044 CA PHE A 177 35.011 14.491 28.976 1.00 15.07 C ANISOU 1044 CA PHE A 177 2298 1822 1605 -176 539 -174 C ATOM 1045 C PHE A 177 34.114 14.110 30.155 1.00 16.04 C ANISOU 1045 C PHE A 177 2506 1950 1636 -245 568 -169 C ATOM 1046 O PHE A 177 33.538 15.013 30.753 1.00 15.41 O ANISOU 1046 O PHE A 177 2274 2074 1504 -165 550 -143 O ATOM 1047 CB PHE A 177 34.222 15.142 27.835 1.00 15.20 C ANISOU 1047 CB PHE A 177 2158 1914 1702 -163 535 -151 C ATOM 1048 CG PHE A 177 34.933 16.282 27.154 1.00 14.61 C ANISOU 1048 CG PHE A 177 2111 1967 1472 -35 567 -56 C ATOM 1049 CD1 PHE A 177 36.249 16.170 26.737 1.00 14.41 C ANISOU 1049 CD1 PHE A 177 2118 1814 1543 94 608 -23 C ATOM 1050 CD2 PHE A 177 34.269 17.475 26.944 1.00 15.30 C ANISOU 1050 CD2 PHE A 177 2108 2012 1690 -45 521 24 C ATOM 1051 CE1 PHE A 177 36.885 17.229 26.112 1.00 14.45 C ANISOU 1051 CE1 PHE A 177 2097 1883 1510 41 506 16 C ATOM 1052 CE2 PHE A 177 34.918 18.527 26.316 1.00 15.00 C ANISOU 1052 CE2 PHE A 177 2021 1851 1826 100 515 35 C ATOM 1053 CZ PHE A 177 36.213 18.393 25.898 1.00 15.07 C ANISOU 1053 CZ PHE A 177 1996 2011 1716 80 541 81 C ATOM 1054 N GLY A 178 34.010 12.826 30.538 1.00 18.14 N ANISOU 1054 N GLY A 178 2772 2054 2066 -212 827 23 N ATOM 1055 CA GLY A 178 33.240 12.433 31.717 1.00 19.47 C ANISOU 1055 CA GLY A 178 2766 2268 2363 -300 989 128 C ATOM 1056 C GLY A 178 31.814 12.958 31.630 1.00 18.60 C ANISOU 1056 C GLY A 178 2663 2344 2059 -410 878 48 C ATOM 1057 O GLY A 178 31.100 12.715 30.646 1.00 21.28 O ANISOU 1057 O GLY A 178 2749 2936 2400 -454 647 -381 O ATOM 1058 N PRO A 179 31.373 13.713 32.633 1.00 17.97 N ANISOU 1058 N PRO A 179 2204 2672 1951 -304 744 22 N ATOM 1059 CA PRO A 179 29.994 14.163 32.642 1.00 18.66 C ANISOU 1059 CA PRO A 179 2215 2906 1967 -280 614 -63 C ATOM 1060 C PRO A 179 29.700 15.378 31.754 1.00 17.56 C ANISOU 1060 C PRO A 179 1942 2872 1857 -75 649 -230 C ATOM 1061 O PRO A 179 28.559 15.793 31.664 1.00 19.25 O ANISOU 1061 O PRO A 179 1952 3200 2160 -23 683 -38 O ATOM 1062 CB PRO A 179 29.792 14.534 34.112 1.00 20.52 C ANISOU 1062 CB PRO A 179 2480 3376 1939 -132 716 38 C ATOM 1063 CG PRO A 179 31.122 15.074 34.498 1.00 20.18 C ANISOU 1063 CG PRO A 179 2611 3251 1804 -69 451 5 C ATOM 1064 CD PRO A 179 32.077 14.097 33.854 1.00 19.61 C ANISOU 1064 CD PRO A 179 2604 2933 1915 -283 600 86 C ATOM 1065 N LEU A 180 30.710 15.952 31.108 1.00 16.24 N ANISOU 1065 N LEU A 180 1943 2541 1685 -38 555 -205 N ATOM 1066 CA LEU A 180 30.468 17.139 30.258 1.00 16.54 C ANISOU 1066 CA LEU A 180 2003 2600 1678 135 443 -255 C ATOM 1067 C LEU A 180 29.888 16.709 28.917 1.00 16.65 C ANISOU 1067 C LEU A 180 1923 2771 1630 -28 571 -231 C ATOM 1068 O LEU A 180 30.519 15.941 28.177 1.00 19.13 O ANISOU 1068 O LEU A 180 2424 3062 1780 459 259 -460 O ATOM 1069 CB LEU A 180 31.751 17.930 30.012 1.00 15.82 C ANISOU 1069 CB LEU A 180 1939 2415 1655 243 401 -113 C ATOM 1070 CG LEU A 180 32.478 18.438 31.249 1.00 16.93 C ANISOU 1070 CG LEU A 180 2094 2596 1741 181 183 85 C ATOM 1071 CD1 LEU A 180 33.630 19.324 30.801 1.00 17.78 C ANISOU 1071 CD1 LEU A 180 2154 2596 2005 -11 88 138 C ATOM 1072 CD2 LEU A 180 31.569 19.182 32.199 1.00 19.26 C ANISOU 1072 CD2 LEU A 180 2633 2779 1905 108 271 -294 C ATOM 1073 N LYS A 181 28.713 17.223 28.633 1.00 16.05 N ANISOU 1073 N LYS A 181 1886 2351 1858 -216 377 -341 N ATOM 1074 CA LYS A 181 28.006 16.898 27.398 1.00 16.84 C ANISOU 1074 CA LYS A 181 2006 2453 1938 -84 320 -429 C ATOM 1075 C LYS A 181 27.934 18.148 26.529 1.00 16.42 C ANISOU 1075 C LYS A 181 1965 2348 1926 -191 227 -506 C ATOM 1076 O LYS A 181 27.220 19.096 26.843 1.00 17.72 O ANISOU 1076 O LYS A 181 1954 2509 2267 -91 303 -436 O ATOM 1077 CB LYS A 181 26.617 16.367 27.748 1.00 18.86 C ANISOU 1077 CB LYS A 181 2074 2718 2374 -227 380 -404 C ATOM 1078 CG LYS A 181 26.621 15.072 28.549 1.00 23.89 C ANISOU 1078 CG LYS A 181 2920 3008 3146 -568 530 39 C ATOM 1079 CD LYS A 181 27.548 13.985 28.026 1.00 29.77 C ANISOU 1079 CD LYS A 181 3994 3237 4079 -76 401 -192 C ATOM 1080 CE LYS A 181 27.797 12.877 29.030 1.00 34.23 C ANISOU 1080 CE LYS A 181 4585 3987 4433 -100 68 263 C ATOM 1081 NZ LYS A 181 28.713 11.851 28.486 1.00 39.81 N ANISOU 1081 NZ LYS A 181 5408 4765 4953 568 -14 66 N ATOM 1082 N VAL A 182 28.715 18.163 25.463 1.00 16.42 N ANISOU 1082 N VAL A 182 2188 2090 1960 -14 325 -561 N ATOM 1083 CA VAL A 182 28.926 19.401 24.714 1.00 15.83 C ANISOU 1083 CA VAL A 182 2008 2055 1951 -76 137 -570 C ATOM 1084 C VAL A 182 28.011 19.435 23.484 1.00 16.52 C ANISOU 1084 C VAL A 182 2254 2099 1921 -125 109 -478 C ATOM 1085 O VAL A 182 27.946 18.463 22.712 1.00 17.79 O ANISOU 1085 O VAL A 182 2377 2283 2098 -168 51 -655 O ATOM 1086 CB VAL A 182 30.402 19.549 24.292 1.00 16.11 C ANISOU 1086 CB VAL A 182 2008 2178 1934 57 161 -532 C ATOM 1087 CG1 VAL A 182 30.645 20.885 23.602 1.00 16.49 C ANISOU 1087 CG1 VAL A 182 2150 2313 1800 -69 251 -498 C ATOM 1088 CG2 VAL A 182 31.332 19.372 25.472 1.00 17.66 C ANISOU 1088 CG2 VAL A 182 1848 2568 2291 109 95 -274 C ATOM 1089 N PHE A 183 27.362 20.579 23.299 1.00 15.92 N ANISOU 1089 N PHE A 183 1912 2146 1988 -181 13 -548 N ATOM 1090 CA PHE A 183 26.337 20.752 22.278 1.00 17.24 C ANISOU 1090 CA PHE A 183 2032 2304 2211 -44 -172 -708 C ATOM 1091 C PHE A 183 26.531 22.086 21.557 1.00 17.22 C ANISOU 1091 C PHE A 183 2082 2398 2062 90 -340 -599 C ATOM 1092 O PHE A 183 26.655 23.136 22.194 1.00 16.69 O ANISOU 1092 O PHE A 183 1969 2409 1962 128 -175 -568 O ATOM 1093 CB PHE A 183 24.956 20.707 22.941 1.00 18.66 C ANISOU 1093 CB PHE A 183 2029 2551 2510 -45 -137 -669 C ATOM 1094 CG PHE A 183 23.805 20.854 21.983 1.00 20.94 C ANISOU 1094 CG PHE A 183 2046 3127 2782 -61 -270 -844 C ATOM 1095 CD1 PHE A 183 23.460 19.805 21.146 1.00 23.12 C ANISOU 1095 CD1 PHE A 183 2452 3251 3081 -169 -470 -925 C ATOM 1096 CD2 PHE A 183 23.063 22.021 21.933 1.00 21.47 C ANISOU 1096 CD2 PHE A 183 2101 3121 2935 -114 -389 -720 C ATOM 1097 CE1 PHE A 183 22.400 19.926 20.265 1.00 23.91 C ANISOU 1097 CE1 PHE A 183 2342 3424 3317 -276 -503 -924 C ATOM 1098 CE2 PHE A 183 22.002 22.138 21.047 1.00 23.52 C ANISOU 1098 CE2 PHE A 183 2029 3648 3257 -55 -454 -829 C ATOM 1099 CZ PHE A 183 21.680 21.092 20.215 1.00 24.18 C ANISOU 1099 CZ PHE A 183 2244 3675 3266 -101 -600 -790 C ATOM 1100 N TYR A 184 26.580 22.031 20.227 1.00 17.47 N ANISOU 1100 N TYR A 184 2198 2363 2075 164 -276 -667 N ATOM 1101 CA TYR A 184 26.566 23.216 19.387 1.00 18.36 C ANISOU 1101 CA TYR A 184 2393 2416 2163 248 -431 -695 C ATOM 1102 C TYR A 184 25.118 23.526 18.994 1.00 20.23 C ANISOU 1102 C TYR A 184 2484 2798 2404 268 -691 -832 C ATOM 1103 O TYR A 184 24.527 22.768 18.248 1.00 21.47 O ANISOU 1103 O TYR A 184 2742 2943 2473 223 -756 -962 O ATOM 1104 CB TYR A 184 27.440 23.019 18.146 1.00 18.83 C ANISOU 1104 CB TYR A 184 2662 2398 2093 240 -398 -612 C ATOM 1105 CG TYR A 184 27.373 24.181 17.192 1.00 19.77 C ANISOU 1105 CG TYR A 184 2940 2649 1922 396 -436 -542 C ATOM 1106 CD1 TYR A 184 27.789 25.437 17.577 1.00 20.06 C ANISOU 1106 CD1 TYR A 184 3042 2587 1993 383 -551 -426 C ATOM 1107 CD2 TYR A 184 26.872 24.033 15.913 1.00 21.93 C ANISOU 1107 CD2 TYR A 184 3454 2858 2017 346 -613 -541 C ATOM 1108 CE1 TYR A 184 27.746 26.518 16.715 1.00 21.83 C ANISOU 1108 CE1 TYR A 184 3597 2572 2123 467 -686 -407 C ATOM 1109 CE2 TYR A 184 26.791 25.111 15.046 1.00 23.67 C ANISOU 1109 CE2 TYR A 184 3861 3072 2059 251 -901 -363 C ATOM 1110 CZ TYR A 184 27.234 26.361 15.443 1.00 22.90 C ANISOU 1110 CZ TYR A 184 3630 2815 2256 545 -929 -310 C ATOM 1111 OH TYR A 184 27.169 27.410 14.570 1.00 25.28 O ANISOU 1111 OH TYR A 184 4107 3035 2461 249 -1012 -112 O ATOM 1112 N PRO A 185 24.536 24.619 19.498 1.00 20.55 N ANISOU 1112 N PRO A 185 2456 2779 2572 333 -835 -818 N ATOM 1113 CA PRO A 185 23.104 24.854 19.295 1.00 22.29 C ANISOU 1113 CA PRO A 185 2406 3241 2822 229 -879 -762 C ATOM 1114 C PRO A 185 22.781 25.578 17.986 1.00 25.06 C ANISOU 1114 C PRO A 185 2894 3545 3082 501 -1100 -630 C ATOM 1115 O PRO A 185 21.598 25.792 17.686 1.00 26.50 O ANISOU 1115 O PRO A 185 2878 3999 3191 495 -1215 -866 O ATOM 1116 CB PRO A 185 22.721 25.753 20.473 1.00 23.08 C ANISOU 1116 CB PRO A 185 2526 3330 2911 510 -802 -724 C ATOM 1117 CG PRO A 185 23.974 26.559 20.711 1.00 21.11 C ANISOU 1117 CG PRO A 185 2545 2927 2548 598 -627 -894 C ATOM 1118 CD PRO A 185 25.094 25.579 20.468 1.00 19.93 C ANISOU 1118 CD PRO A 185 2361 2838 2372 450 -681 -874 C ATOM 1119 N GLY A 186 23.818 25.934 17.241 1.00 23.68 N ANISOU 1119 N GLY A 186 2995 3368 2632 507 -1177 -622 N ATOM 1120 CA GLY A 186 23.710 26.810 16.099 1.00 24.94 C ANISOU 1120 CA GLY A 186 3407 3472 2595 401 -1182 -604 C ATOM 1121 C GLY A 186 24.261 28.192 16.404 1.00 24.35 C ANISOU 1121 C GLY A 186 3402 3332 2517 607 -1188 -610 C ATOM 1122 O GLY A 186 24.497 28.568 17.558 1.00 23.99 O ANISOU 1122 O GLY A 186 3286 3324 2504 571 -1152 -593 O ATOM 1123 N PRO A 187 24.427 28.995 15.359 1.00 25.04 N ANISOU 1123 N PRO A 187 3725 3429 2360 703 -1249 -556 N ATOM 1124 CA PRO A 187 24.977 30.333 15.560 1.00 25.52 C ANISOU 1124 CA PRO A 187 3878 3410 2406 688 -1318 -382 C ATOM 1125 C PRO A 187 23.975 31.238 16.290 1.00 25.52 C ANISOU 1125 C PRO A 187 3763 3259 2673 760 -1409 -268 C ATOM 1126 O PRO A 187 22.776 31.157 16.048 1.00 28.05 O ANISOU 1126 O PRO A 187 3883 3578 3195 844 -1846 -538 O ATOM 1127 CB PRO A 187 25.289 30.824 14.141 1.00 27.92 C ANISOU 1127 CB PRO A 187 4510 3463 2635 705 -1027 -248 C ATOM 1128 CG PRO A 187 24.336 30.062 13.266 1.00 30.14 C ANISOU 1128 CG PRO A 187 4986 3903 2561 652 -1283 -365 C ATOM 1129 CD PRO A 187 24.098 28.735 13.949 1.00 27.84 C ANISOU 1129 CD PRO A 187 4358 3787 2430 717 -1529 -475 C ATOM 1130 N GLY A 188 24.469 32.090 17.170 1.00 24.33 N ANISOU 1130 N GLY A 188 3444 3082 2716 808 -1282 -299 N ATOM 1131 CA GLY A 188 23.608 32.968 17.937 1.00 25.00 C ANISOU 1131 CA GLY A 188 3346 3117 3033 942 -1419 -358 C ATOM 1132 C GLY A 188 24.392 34.167 18.443 1.00 24.22 C ANISOU 1132 C GLY A 188 3384 2814 3002 964 -1413 -91 C ATOM 1133 O GLY A 188 24.605 35.126 17.719 1.00 25.90 O ANISOU 1133 O GLY A 188 3789 3018 3033 826 -1398 73 O ATOM 1134 N HIS A 189 24.859 34.096 19.678 1.00 23.18 N ANISOU 1134 N HIS A 189 3276 2722 2809 913 -1172 -178 N ATOM 1135 CA HIS A 189 25.700 35.150 20.235 1.00 22.70 C ANISOU 1135 CA HIS A 189 3292 2542 2788 831 -870 -109 C ATOM 1136 C HIS A 189 26.953 35.334 19.364 1.00 21.28 C ANISOU 1136 C HIS A 189 3309 2394 2380 942 -947 -89 C ATOM 1137 O HIS A 189 27.399 36.442 19.066 1.00 22.34 O ANISOU 1137 O HIS A 189 3437 2372 2678 921 -1041 -68 O ATOM 1138 CB HIS A 189 26.064 34.799 21.680 1.00 20.53 C ANISOU 1138 CB HIS A 189 2715 2407 2678 714 -761 -204 C ATOM 1139 CG HIS A 189 27.224 35.581 22.206 1.00 19.90 C ANISOU 1139 CG HIS A 189 2752 2247 2561 694 -608 -434 C ATOM 1140 ND1 HIS A 189 27.094 36.891 22.605 1.00 21.16 N ANISOU 1140 ND1 HIS A 189 2964 2301 2774 678 -750 -476 N ATOM 1141 CD2 HIS A 189 28.534 35.260 22.381 1.00 18.47 C ANISOU 1141 CD2 HIS A 189 2753 2097 2167 627 -621 -252 C ATOM 1142 CE1 HIS A 189 28.265 37.333 23.018 1.00 19.47 C ANISOU 1142 CE1 HIS A 189 2798 2174 2424 659 -552 -437 C ATOM 1143 NE2 HIS A 189 29.179 36.363 22.887 1.00 18.52 N ANISOU 1143 NE2 HIS A 189 2789 2063 2183 591 -461 -276 N ATOM 1144 N THR A 190 27.533 34.208 18.964 1.00 21.26 N ANISOU 1144 N THR A 190 3433 2381 2263 797 -785 -189 N ATOM 1145 CA THR A 190 28.580 34.162 17.939 1.00 20.80 C ANISOU 1145 CA THR A 190 3522 2404 1975 617 -841 48 C ATOM 1146 C THR A 190 28.328 32.951 17.027 1.00 21.75 C ANISOU 1146 C THR A 190 3808 2617 1839 653 -966 -17 C ATOM 1147 O THR A 190 27.474 32.092 17.304 1.00 22.71 O ANISOU 1147 O THR A 190 3611 2602 2416 695 -900 -341 O ATOM 1148 CB THR A 190 30.009 34.037 18.504 1.00 19.36 C ANISOU 1148 CB THR A 190 3291 2175 1889 584 -488 14 C ATOM 1149 OG1 THR A 190 30.085 32.827 19.261 1.00 18.74 O ANISOU 1149 OG1 THR A 190 3075 2148 1895 546 -539 -20 O ATOM 1150 CG2 THR A 190 30.429 35.214 19.353 1.00 19.60 C ANISOU 1150 CG2 THR A 190 3341 2161 1943 526 -371 0 C ATOM 1151 N SER A 191 29.087 32.887 15.938 1.00 22.17 N ANISOU 1151 N SER A 191 3948 2572 1903 748 -880 -58 N ATOM 1152 CA ASER A 191 29.031 31.762 14.999 0.55 23.24 C ANISOU 1152 CA ASER A 191 4182 2673 1974 653 -991 -132 C ATOM 1153 CA BSER A 191 28.951 31.743 15.034 0.45 22.91 C ANISOU 1153 CA BSER A 191 4220 2719 1766 676 -929 -100 C ATOM 1154 C SER A 191 29.492 30.461 15.664 1.00 21.60 C ANISOU 1154 C SER A 191 3894 2441 1872 560 -853 -289 C ATOM 1155 O SER A 191 29.048 29.377 15.285 1.00 22.92 O ANISOU 1155 O SER A 191 3981 2594 2133 529 -1125 -377 O ATOM 1156 CB ASER A 191 29.864 32.039 13.766 0.55 25.21 C ANISOU 1156 CB ASER A 191 4624 2863 2092 746 -773 -57 C ATOM 1157 CB BSER A 191 29.617 31.987 13.719 0.45 23.63 C ANISOU 1157 CB BSER A 191 4644 2665 1668 904 -895 -38 C ATOM 1158 OG ASER A 191 31.244 32.186 14.093 0.55 24.86 O ANISOU 1158 OG ASER A 191 4459 2718 2269 665 -349 7 O ATOM 1159 OG BSER A 191 28.897 32.963 13.001 0.45 25.67 O ANISOU 1159 OG BSER A 191 5114 2908 1731 1075 -892 180 O ATOM 1160 N ASP A 192 30.434 30.598 16.607 1.00 19.31 N ANISOU 1160 N ASP A 192 3681 2154 1503 498 -626 -190 N ATOM 1161 CA ASP A 192 31.133 29.444 17.161 1.00 17.93 C ANISOU 1161 CA ASP A 192 3209 2167 1435 470 -400 -159 C ATOM 1162 C ASP A 192 30.639 29.024 18.556 1.00 16.95 C ANISOU 1162 C ASP A 192 2848 2118 1474 430 -393 -202 C ATOM 1163 O ASP A 192 31.178 28.055 19.118 1.00 16.63 O ANISOU 1163 O ASP A 192 2678 2130 1509 475 -160 -166 O ATOM 1164 CB ASP A 192 32.644 29.687 17.213 1.00 17.19 C ANISOU 1164 CB ASP A 192 3151 2029 1351 487 -182 -23 C ATOM 1165 CG ASP A 192 33.082 30.883 18.057 1.00 16.97 C ANISOU 1165 CG ASP A 192 3021 2112 1314 465 -112 -19 C ATOM 1166 OD1 ASP A 192 32.365 31.912 18.040 1.00 18.65 O ANISOU 1166 OD1 ASP A 192 3342 2084 1659 591 -306 -121 O ATOM 1167 OD2 ASP A 192 34.148 30.768 18.706 1.00 16.17 O ANISOU 1167 OD2 ASP A 192 2846 1909 1389 464 -12 -115 O ATOM 1168 N ASN A 193 29.652 29.704 19.137 1.00 17.31 N ANISOU 1168 N ASN A 193 2553 2244 1777 465 -469 -172 N ATOM 1169 CA ASN A 193 29.250 29.445 20.519 1.00 16.56 C ANISOU 1169 CA ASN A 193 2497 2120 1673 394 -617 -181 C ATOM 1170 C ASN A 193 28.828 27.988 20.739 1.00 16.45 C ANISOU 1170 C ASN A 193 2462 2114 1672 386 -411 -375 C ATOM 1171 O ASN A 193 28.051 27.424 19.974 1.00 17.02 O ANISOU 1171 O ASN A 193 2332 2225 1908 321 -534 -298 O ATOM 1172 CB ASN A 193 28.169 30.440 20.996 1.00 17.53 C ANISOU 1172 CB ASN A 193 2454 2327 1879 463 -573 -285 C ATOM 1173 CG ASN A 193 26.913 30.639 20.161 1.00 18.84 C ANISOU 1173 CG ASN A 193 2458 2540 2157 683 -622 -325 C ATOM 1174 OD1 ASN A 193 26.295 31.708 20.254 1.00 21.21 O ANISOU 1174 OD1 ASN A 193 2844 2663 2551 898 -887 -396 O ATOM 1175 ND2 ASN A 193 26.478 29.624 19.436 1.00 20.34 N ANISOU 1175 ND2 ASN A 193 2732 2589 2407 510 -815 -305 N ATOM 1176 N ILE A 194 29.342 27.411 21.833 1.00 14.63 N ANISOU 1176 N ILE A 194 1889 2141 1528 290 -189 -337 N ATOM 1177 CA ILE A 194 28.938 26.056 22.237 1.00 14.83 C ANISOU 1177 CA ILE A 194 1867 2053 1713 248 -260 -414 C ATOM 1178 C ILE A 194 28.427 26.095 23.684 1.00 14.22 C ANISOU 1178 C ILE A 194 1644 2011 1747 153 -225 -380 C ATOM 1179 O ILE A 194 28.584 27.079 24.408 1.00 14.49 O ANISOU 1179 O ILE A 194 1754 2003 1746 177 -152 -379 O ATOM 1180 CB ILE A 194 30.053 25.019 22.020 1.00 14.51 C ANISOU 1180 CB ILE A 194 2005 1925 1581 204 -80 -358 C ATOM 1181 CG1 ILE A 194 31.289 25.370 22.845 1.00 14.39 C ANISOU 1181 CG1 ILE A 194 1815 2046 1604 194 89 -379 C ATOM 1182 CG2 ILE A 194 30.363 24.875 20.531 1.00 15.58 C ANISOU 1182 CG2 ILE A 194 2304 2053 1561 330 -93 -267 C ATOM 1183 CD1 ILE A 194 32.335 24.276 22.896 1.00 14.90 C ANISOU 1183 CD1 ILE A 194 1878 2045 1739 170 66 -189 C ATOM 1184 N THR A 195 27.780 24.998 24.073 1.00 14.55 N ANISOU 1184 N THR A 195 1701 2055 1771 43 -61 -476 N ATOM 1185 CA THR A 195 27.107 24.889 25.366 1.00 14.67 C ANISOU 1185 CA THR A 195 1489 2252 1833 155 -1 -554 C ATOM 1186 C THR A 195 27.449 23.539 25.994 1.00 14.50 C ANISOU 1186 C THR A 195 1506 2151 1851 -87 22 -518 C ATOM 1187 O THR A 195 27.890 22.626 25.292 1.00 15.22 O ANISOU 1187 O THR A 195 1774 2185 1823 -69 87 -515 O ATOM 1188 CB THR A 195 25.589 25.031 25.194 1.00 16.46 C ANISOU 1188 CB THR A 195 1528 2462 2263 69 -90 -567 C ATOM 1189 OG1 THR A 195 25.035 23.942 24.447 1.00 17.69 O ANISOU 1189 OG1 THR A 195 1660 2632 2428 21 -150 -745 O ATOM 1190 CG2 THR A 195 25.242 26.356 24.553 1.00 17.18 C ANISOU 1190 CG2 THR A 195 1668 2535 2323 176 -244 -556 C ATOM 1191 N VAL A 196 27.261 23.430 27.310 1.00 14.28 N ANISOU 1191 N VAL A 196 1497 2107 1821 114 168 -530 N ATOM 1192 CA VAL A 196 27.727 22.246 28.039 1.00 14.76 C ANISOU 1192 CA VAL A 196 1467 2228 1910 86 237 -378 C ATOM 1193 C VAL A 196 26.713 21.861 29.115 1.00 15.42 C ANISOU 1193 C VAL A 196 1472 2321 2063 -33 309 -447 C ATOM 1194 O VAL A 196 26.418 22.668 29.990 1.00 16.40 O ANISOU 1194 O VAL A 196 1802 2326 2102 -159 412 -481 O ATOM 1195 CB VAL A 196 29.114 22.486 28.670 1.00 14.93 C ANISOU 1195 CB VAL A 196 1408 2329 1934 120 213 -256 C ATOM 1196 CG1 VAL A 196 29.616 21.207 29.310 1.00 15.98 C ANISOU 1196 CG1 VAL A 196 1591 2214 2264 60 290 -199 C ATOM 1197 CG2 VAL A 196 30.130 23.057 27.679 1.00 15.24 C ANISOU 1197 CG2 VAL A 196 1554 2299 1934 -22 244 -338 C ATOM 1198 N GLY A 197 26.233 20.628 29.054 1.00 16.18 N ANISOU 1198 N GLY A 197 1618 2438 2089 -184 406 -430 N ATOM 1199 CA GLY A 197 25.459 20.062 30.156 1.00 17.33 C ANISOU 1199 CA GLY A 197 1676 2638 2268 -200 600 -460 C ATOM 1200 C GLY A 197 26.332 19.266 31.095 1.00 17.41 C ANISOU 1200 C GLY A 197 1732 2683 2197 -291 550 -449 C ATOM 1201 O GLY A 197 27.337 18.725 30.646 1.00 17.22 O ANISOU 1201 O GLY A 197 1960 2528 2054 -70 446 -427 O ATOM 1202 N ILE A 198 25.948 19.151 32.361 1.00 17.93 N ANISOU 1202 N ILE A 198 1630 2865 2315 -380 663 -325 N ATOM 1203 CA AILE A 198 26.744 18.345 33.298 0.74 18.25 C ANISOU 1203 CA AILE A 198 1731 2974 2228 -460 592 -285 C ATOM 1204 CA BILE A 198 26.725 18.398 33.335 0.26 17.98 C ANISOU 1204 CA BILE A 198 1722 2935 2173 -432 678 -313 C ATOM 1205 C ILE A 198 25.897 17.168 33.754 1.00 18.77 C ANISOU 1205 C ILE A 198 1864 2985 2280 -504 751 -293 C ATOM 1206 O ILE A 198 24.954 17.292 34.532 1.00 20.08 O ANISOU 1206 O ILE A 198 2063 3119 2445 -623 965 -222 O ATOM 1207 CB AILE A 198 27.247 19.130 34.519 0.74 19.23 C ANISOU 1207 CB AILE A 198 1958 3123 2223 -533 620 -328 C ATOM 1208 CB BILE A 198 27.114 19.311 34.524 0.26 18.21 C ANISOU 1208 CB BILE A 198 1714 3092 2112 -466 766 -361 C ATOM 1209 CG1AILE A 198 28.022 20.370 34.088 0.74 18.57 C ANISOU 1209 CG1AILE A 198 1822 3087 2145 -536 446 -200 C ATOM 1210 CG1BILE A 198 27.521 20.727 34.087 0.26 17.45 C ANISOU 1210 CG1BILE A 198 1528 3073 2027 -408 620 -325 C ATOM 1211 CG2AILE A 198 28.073 18.214 35.406 0.74 21.02 C ANISOU 1211 CG2AILE A 198 2213 3526 2245 -535 594 -39 C ATOM 1212 CG2BILE A 198 28.193 18.661 35.371 0.26 17.71 C ANISOU 1212 CG2BILE A 198 1697 3070 1961 -564 888 -168 C ATOM 1213 CD1AILE A 198 28.216 21.323 35.207 0.74 19.86 C ANISOU 1213 CD1AILE A 198 2083 3090 2372 -504 611 -365 C ATOM 1214 CD1BILE A 198 28.806 20.808 33.274 0.26 16.69 C ANISOU 1214 CD1BILE A 198 1553 2936 1850 -235 597 -366 C ATOM 1215 N ASP A 199 26.217 16.000 33.228 1.00 20.37 N ANISOU 1215 N ASP A 199 2143 2959 2634 -501 870 -385 N ATOM 1216 CA AASP A 199 25.499 14.795 33.596 0.58 22.95 C ANISOU 1216 CA AASP A 199 2722 2978 3018 -656 1062 -458 C ATOM 1217 CA BASP A 199 25.553 14.749 33.586 0.42 23.36 C ANISOU 1217 CA BASP A 199 2778 3029 3067 -687 968 -308 C ATOM 1218 C ASP A 199 25.590 14.576 35.109 1.00 23.78 C ANISOU 1218 C ASP A 199 2922 3039 3074 -689 1134 -250 C ATOM 1219 O ASP A 199 26.573 14.894 35.743 1.00 24.22 O ANISOU 1219 O ASP A 199 2912 3411 2878 -401 1086 -17 O ATOM 1220 CB AASP A 199 26.040 13.601 32.816 0.58 25.80 C ANISOU 1220 CB AASP A 199 3255 3171 3375 -544 1139 -682 C ATOM 1221 CB BASP A 199 26.233 13.575 32.876 0.42 24.79 C ANISOU 1221 CB BASP A 199 3166 2953 3301 -675 1066 -319 C ATOM 1222 CG AASP A 199 25.390 13.447 31.455 0.58 28.56 C ANISOU 1222 CG AASP A 199 3742 3803 3304 -499 1141 -764 C ATOM 1223 CG BASP A 199 25.343 12.364 32.644 0.42 28.20 C ANISOU 1223 CG BASP A 199 3888 3110 3717 -1079 968 -128 C ATOM 1224 OD1AASP A 199 24.715 14.392 31.013 0.58 29.19 O ANISOU 1224 OD1AASP A 199 4250 3591 3248 -575 1106 -719 O ATOM 1225 OD1BASP A 199 24.114 12.502 32.769 0.42 30.44 O ANISOU 1225 OD1BASP A 199 3866 3530 4167 -1163 836 -302 O ATOM 1226 OD2AASP A 199 25.555 12.375 30.855 0.58 35.43 O ANISOU 1226 OD2AASP A 199 5462 4382 3618 118 877 -1274 O ATOM 1227 OD2BASP A 199 25.893 11.296 32.322 0.42 31.26 O ANISOU 1227 OD2BASP A 199 4559 3081 4235 -746 864 221 O ATOM 1228 N GLY A 200 24.515 14.043 35.671 1.00 25.28 N ANISOU 1228 N GLY A 200 3313 2961 3331 -761 1484 -283 N ATOM 1229 CA GLY A 200 24.461 13.775 37.106 1.00 27.14 C ANISOU 1229 CA GLY A 200 3713 3210 3387 -637 1460 -16 C ATOM 1230 C GLY A 200 24.044 14.986 37.924 1.00 25.86 C ANISOU 1230 C GLY A 200 3357 3225 3241 -571 1489 147 C ATOM 1231 O GLY A 200 24.010 14.908 39.155 1.00 29.77 O ANISOU 1231 O GLY A 200 3871 4218 3220 -66 1587 591 O ATOM 1232 N THR A 201 23.699 16.080 37.246 1.00 23.52 N ANISOU 1232 N THR A 201 2883 2961 3091 -715 1312 -121 N ATOM 1233 CA THR A 201 23.277 17.295 37.881 1.00 23.08 C ANISOU 1233 CA THR A 201 2341 3207 3221 -630 1294 -199 C ATOM 1234 C THR A 201 22.094 17.868 37.117 1.00 23.26 C ANISOU 1234 C THR A 201 2313 3255 3268 -653 1361 -86 C ATOM 1235 O THR A 201 21.716 17.392 36.047 1.00 26.12 O ANISOU 1235 O THR A 201 2489 3737 3698 -757 942 -276 O ATOM 1236 CB THR A 201 24.358 18.379 37.886 1.00 21.31 C ANISOU 1236 CB THR A 201 2263 3303 2528 -593 1190 -286 C ATOM 1237 OG1 THR A 201 24.410 19.026 36.609 1.00 20.95 O ANISOU 1237 OG1 THR A 201 2227 3078 2655 -489 1009 -232 O ATOM 1238 CG2 THR A 201 25.715 17.852 38.289 1.00 22.89 C ANISOU 1238 CG2 THR A 201 2254 3591 2850 -735 920 -86 C ATOM 1239 N ASP A 202 21.538 18.914 37.691 1.00 23.94 N ANISOU 1239 N ASP A 202 1896 3639 3561 -435 1305 -271 N ATOM 1240 CA ASP A 202 20.456 19.591 37.042 1.00 24.52 C ANISOU 1240 CA ASP A 202 1604 3645 4067 -651 1164 -256 C ATOM 1241 C ASP A 202 20.935 20.800 36.240 1.00 22.04 C ANISOU 1241 C ASP A 202 1707 3205 3461 -157 1073 -452 C ATOM 1242 O ASP A 202 20.114 21.659 35.921 1.00 22.45 O ANISOU 1242 O ASP A 202 1547 3218 3765 -256 726 -555 O ATOM 1243 CB ASP A 202 19.440 20.063 38.087 1.00 32.45 C ANISOU 1243 CB ASP A 202 2461 5244 4623 -296 1793 -289 C ATOM 1244 CG ASP A 202 18.947 18.991 39.044 1.00 38.04 C ANISOU 1244 CG ASP A 202 3417 5711 5324 -472 1989 105 C ATOM 1245 OD1 ASP A 202 18.739 17.848 38.589 1.00 44.35 O ANISOU 1245 OD1 ASP A 202 3755 5968 7128 -1549 1317 250 O ATOM 1246 OD2 ASP A 202 18.742 19.318 40.235 1.00 47.79 O ANISOU 1246 OD2 ASP A 202 4520 8077 5560 -296 2137 -297 O ATOM 1247 N ILE A 203 22.222 20.849 35.908 1.00 20.24 N ANISOU 1247 N ILE A 203 1600 2907 3182 -417 796 -558 N ATOM 1248 CA ILE A 203 22.854 22.073 35.412 1.00 19.28 C ANISOU 1248 CA ILE A 203 1643 2883 2800 -393 714 -569 C ATOM 1249 C ILE A 203 23.129 21.946 33.911 1.00 17.74 C ANISOU 1249 C ILE A 203 1380 2639 2721 -256 354 -582 C ATOM 1250 O ILE A 203 23.685 20.955 33.443 1.00 18.37 O ANISOU 1250 O ILE A 203 1765 2535 2679 -312 606 -506 O ATOM 1251 CB ILE A 203 24.149 22.352 36.191 1.00 19.47 C ANISOU 1251 CB ILE A 203 1861 2928 2607 -186 483 -487 C ATOM 1252 CG1 ILE A 203 23.876 22.592 37.677 1.00 21.01 C ANISOU 1252 CG1 ILE A 203 2091 3269 2622 -213 657 -326 C ATOM 1253 CG2 ILE A 203 24.931 23.506 35.563 1.00 20.66 C ANISOU 1253 CG2 ILE A 203 2011 2824 3012 -351 227 -478 C ATOM 1254 CD1 ILE A 203 25.111 22.552 38.542 1.00 22.44 C ANISOU 1254 CD1 ILE A 203 2452 3295 2780 -315 350 -363 C ATOM 1255 N ALA A 204 22.812 23.028 33.193 1.00 17.35 N ANISOU 1255 N ALA A 204 1294 2716 2579 -133 624 -528 N ATOM 1256 CA ALA A 204 23.281 23.217 31.828 1.00 17.65 C ANISOU 1256 CA ALA A 204 1696 2569 2441 -205 425 -440 C ATOM 1257 C ALA A 204 23.830 24.638 31.685 1.00 16.84 C ANISOU 1257 C ALA A 204 1330 2513 2556 -116 473 -647 C ATOM 1258 O ALA A 204 23.281 25.597 32.227 1.00 18.49 O ANISOU 1258 O ALA A 204 1468 2539 3019 -104 595 -711 O ATOM 1259 CB ALA A 204 22.185 22.943 30.820 1.00 20.18 C ANISOU 1259 CB ALA A 204 1882 2966 2818 -490 260 -404 C ATOM 1260 N PHE A 205 24.944 24.751 30.953 1.00 15.43 N ANISOU 1260 N PHE A 205 1340 2369 2152 -124 349 -617 N ATOM 1261 CA PHE A 205 25.685 25.999 30.811 1.00 14.76 C ANISOU 1261 CA PHE A 205 1352 2291 1965 -42 226 -629 C ATOM 1262 C PHE A 205 25.496 26.551 29.402 1.00 14.93 C ANISOU 1262 C PHE A 205 1207 2373 2091 -38 161 -487 C ATOM 1263 O PHE A 205 25.913 25.947 28.411 1.00 15.82 O ANISOU 1263 O PHE A 205 1462 2484 2063 45 78 -570 O ATOM 1264 CB PHE A 205 27.175 25.780 31.055 1.00 14.87 C ANISOU 1264 CB PHE A 205 1376 2320 1955 -64 142 -399 C ATOM 1265 CG PHE A 205 28.041 27.019 30.967 1.00 14.22 C ANISOU 1265 CG PHE A 205 1324 2319 1757 -6 231 -406 C ATOM 1266 CD1 PHE A 205 27.897 28.038 31.898 1.00 15.70 C ANISOU 1266 CD1 PHE A 205 1512 2460 1991 -183 346 -594 C ATOM 1267 CD2 PHE A 205 28.952 27.200 29.941 1.00 13.81 C ANISOU 1267 CD2 PHE A 205 1305 2178 1765 40 241 -447 C ATOM 1268 CE1 PHE A 205 28.714 29.159 31.862 1.00 15.41 C ANISOU 1268 CE1 PHE A 205 1610 2285 1960 -120 284 -576 C ATOM 1269 CE2 PHE A 205 29.754 28.327 29.885 1.00 14.38 C ANISOU 1269 CE2 PHE A 205 1385 2134 1943 50 256 -349 C ATOM 1270 CZ PHE A 205 29.651 29.292 30.860 1.00 14.23 C ANISOU 1270 CZ PHE A 205 1365 2075 1966 28 174 -380 C ATOM 1271 N GLY A 206 24.888 27.720 29.318 1.00 16.15 N ANISOU 1271 N GLY A 206 1447 2553 2135 200 -29 -621 N ATOM 1272 CA GLY A 206 24.612 28.362 28.072 1.00 16.59 C ANISOU 1272 CA GLY A 206 1450 2565 2287 296 -137 -589 C ATOM 1273 C GLY A 206 25.694 29.342 27.646 1.00 16.34 C ANISOU 1273 C GLY A 206 1548 2527 2134 330 -111 -533 C ATOM 1274 O GLY A 206 25.628 29.894 26.544 1.00 17.12 O ANISOU 1274 O GLY A 206 1849 2387 2266 323 -205 -422 O ATOM 1275 N GLY A 207 26.672 29.616 28.479 1.00 15.86 N ANISOU 1275 N GLY A 207 1485 2389 2151 276 -87 -450 N ATOM 1276 CA GLY A 207 27.705 30.582 28.107 1.00 15.16 C ANISOU 1276 CA GLY A 207 1599 2275 1886 327 -104 -414 C ATOM 1277 C GLY A 207 27.119 31.936 27.790 1.00 16.45 C ANISOU 1277 C GLY A 207 1752 2376 2121 478 -101 -435 C ATOM 1278 O GLY A 207 26.220 32.390 28.457 1.00 17.24 O ANISOU 1278 O GLY A 207 1639 2454 2456 429 -55 -608 O ATOM 1279 N CYS A 208 27.620 32.582 26.758 1.00 16.13 N ANISOU 1279 N CYS A 208 1863 2159 2105 451 -314 -308 N ATOM 1280 CA CYS A 208 27.144 33.915 26.468 1.00 17.85 C ANISOU 1280 CA CYS A 208 2133 2205 2443 388 -403 -214 C ATOM 1281 C CYS A 208 25.937 33.900 25.536 1.00 18.30 C ANISOU 1281 C CYS A 208 1917 2337 2698 486 -391 -331 C ATOM 1282 O CYS A 208 25.386 34.949 25.226 1.00 20.27 O ANISOU 1282 O CYS A 208 2343 2349 3008 594 -665 -405 O ATOM 1283 CB CYS A 208 28.236 34.817 25.934 1.00 17.43 C ANISOU 1283 CB CYS A 208 1876 2488 2255 512 -245 -307 C ATOM 1284 SG CYS A 208 29.762 34.754 26.898 0.87 14.60 S ANISOU 1284 SG CYS A 208 1701 2019 1828 431 -65 -285 S ATOM 1285 N LEU A 209 25.486 32.722 25.148 1.00 17.83 N ANISOU 1285 N LEU A 209 2014 2392 2367 534 -394 -477 N ATOM 1286 CA LEU A 209 24.265 32.640 24.343 1.00 18.02 C ANISOU 1286 CA LEU A 209 1926 2473 2447 468 -378 -448 C ATOM 1287 C LEU A 209 23.007 32.994 25.159 1.00 18.70 C ANISOU 1287 C LEU A 209 1878 2618 2609 611 -379 -394 C ATOM 1288 O LEU A 209 22.052 33.575 24.608 1.00 20.99 O ANISOU 1288 O LEU A 209 1965 3136 2872 745 -598 -479 O ATOM 1289 CB LEU A 209 24.148 31.217 23.804 1.00 18.49 C ANISOU 1289 CB LEU A 209 2023 2485 2515 443 -583 -479 C ATOM 1290 CG LEU A 209 22.906 30.905 22.973 1.00 20.38 C ANISOU 1290 CG LEU A 209 2070 2819 2851 467 -717 -513 C ATOM 1291 CD1 LEU A 209 22.956 31.635 21.644 1.00 21.32 C ANISOU 1291 CD1 LEU A 209 2306 3014 2780 476 -693 -535 C ATOM 1292 CD2 LEU A 209 22.781 29.411 22.773 1.00 20.98 C ANISOU 1292 CD2 LEU A 209 2165 2851 2954 309 -694 -555 C ATOM 1293 N ILE A 210 22.964 32.584 26.430 1.00 18.84 N ANISOU 1293 N ILE A 210 1578 2903 2676 561 -229 -274 N ATOM 1294 CA ILE A 210 21.773 32.677 27.268 1.00 20.19 C ANISOU 1294 CA ILE A 210 1446 2971 3251 680 -91 -279 C ATOM 1295 C ILE A 210 21.997 33.813 28.267 1.00 19.95 C ANISOU 1295 C ILE A 210 1409 2769 3401 935 141 -186 C ATOM 1296 O ILE A 210 23.041 33.965 28.849 1.00 19.91 O ANISOU 1296 O ILE A 210 1724 2851 2988 692 -115 -328 O ATOM 1297 CB ILE A 210 21.459 31.339 27.966 1.00 20.79 C ANISOU 1297 CB ILE A 210 1641 2973 3282 490 -59 -369 C ATOM 1298 CG1 ILE A 210 21.298 30.186 26.969 1.00 20.67 C ANISOU 1298 CG1 ILE A 210 1492 3237 3125 413 -12 -492 C ATOM 1299 CG2 ILE A 210 20.262 31.475 28.891 1.00 21.78 C ANISOU 1299 CG2 ILE A 210 1627 3170 3475 359 44 -383 C ATOM 1300 CD1 ILE A 210 20.206 30.391 25.931 1.00 22.94 C ANISOU 1300 CD1 ILE A 210 1886 3388 3440 429 -373 -657 C ATOM 1301 N LYS A 211 20.940 34.625 28.401 1.00 35.21 N ANISOU 1301 N LYS A 211 4583 4715 4078 -1951 1589 -2133 N ATOM 1302 CA LYS A 211 20.835 35.708 29.402 1.00 35.13 C ANISOU 1302 CA LYS A 211 4425 4512 4410 -1508 1338 -2091 C ATOM 1303 C LYS A 211 19.709 35.358 30.382 1.00 35.09 C ANISOU 1303 C LYS A 211 4156 4669 4506 -1278 1372 -2292 C ATOM 1304 O LYS A 211 18.861 34.513 30.084 1.00 34.61 O ANISOU 1304 O LYS A 211 4049 4754 4344 -1225 1474 -2335 O ATOM 1305 CB LYS A 211 20.555 37.062 28.738 1.00 37.66 C ANISOU 1305 CB LYS A 211 5014 4567 4728 -1426 1019 -2049 C ATOM 1306 CG LYS A 211 21.179 37.244 27.359 1.00 38.94 C ANISOU 1306 CG LYS A 211 5506 4530 4758 -1675 1057 -1783 C ATOM 1307 CD LYS A 211 22.694 37.213 27.397 1.00 39.00 C ANISOU 1307 CD LYS A 211 5502 4473 4841 -1876 1361 -1592 C ATOM 1308 CE LYS A 211 23.340 37.599 26.084 1.00 41.12 C ANISOU 1308 CE LYS A 211 6177 4443 5001 -2146 1495 -1394 C ATOM 1309 NZ LYS A 211 24.822 37.553 26.167 1.00 41.91 N ANISOU 1309 NZ LYS A 211 6156 4454 5312 -2360 1865 -1245 N ATOM 1310 N ASP A 212 19.697 35.989 31.550 1.00 36.16 N ANISOU 1310 N ASP A 212 4164 4862 4711 -1147 1275 -2396 N ATOM 1311 CA ASP A 212 18.756 35.583 32.596 1.00 37.48 C ANISOU 1311 CA ASP A 212 4073 5286 4879 -870 1515 -2480 C ATOM 1312 C ASP A 212 17.334 36.066 32.259 1.00 39.55 C ANISOU 1312 C ASP A 212 4276 5557 5194 -572 1405 -2672 C ATOM 1313 O ASP A 212 17.140 36.846 31.326 1.00 40.73 O ANISOU 1313 O ASP A 212 4598 5433 5443 -520 1136 -2644 O ATOM 1314 CB ASP A 212 19.194 36.134 33.944 1.00 38.83 C ANISOU 1314 CB ASP A 212 4263 5459 5030 -874 1450 -2568 C ATOM 1315 CG ASP A 212 19.147 37.656 33.974 1.00 41.93 C ANISOU 1315 CG ASP A 212 4855 5472 5601 -755 1041 -2685 C ATOM 1316 OD1 ASP A 212 20.170 38.288 33.658 1.00 44.16 O ANISOU 1316 OD1 ASP A 212 5168 5556 6052 -890 892 -2112 O ATOM 1317 OD2 ASP A 212 18.079 38.191 34.220 1.00 45.12 O ANISOU 1317 OD2 ASP A 212 5033 5927 6181 -515 970 -2744 O ATOM 1318 N SER A 213 16.374 35.620 33.079 1.00 40.53 N ANISOU 1318 N SER A 213 4122 5930 5346 -439 1587 -2858 N ATOM 1319 CA SER A 213 14.936 35.808 32.808 1.00 43.57 C ANISOU 1319 CA SER A 213 4150 6357 6048 -212 1519 -2882 C ATOM 1320 C SER A 213 14.523 37.284 32.900 1.00 47.37 C ANISOU 1320 C SER A 213 4710 6608 6681 183 1349 -3054 C ATOM 1321 O SER A 213 13.441 37.632 32.421 1.00 50.60 O ANISOU 1321 O SER A 213 4798 6917 7509 379 1180 -3002 O ATOM 1322 CB SER A 213 14.104 34.932 33.715 1.00 44.47 C ANISOU 1322 CB SER A 213 3895 6850 6148 -180 1844 -2979 C ATOM 1323 OG SER A 213 14.386 35.174 35.085 1.00 45.62 O ANISOU 1323 OG SER A 213 4053 7116 6163 -184 2038 -3160 O ATOM 1324 N LYS A 214 15.352 38.145 33.490 1.00 47.66 N ANISOU 1324 N LYS A 214 5144 6428 6534 253 1346 -3223 N ATOM 1325 CA LYS A 214 15.017 39.570 33.643 1.00 51.91 C ANISOU 1325 CA LYS A 214 5778 6572 7372 572 1177 -3372 C ATOM 1326 C LYS A 214 15.986 40.450 32.838 1.00 50.83 C ANISOU 1326 C LYS A 214 6128 6065 7118 417 740 -3280 C ATOM 1327 O LYS A 214 16.055 41.651 33.063 1.00 53.92 O ANISOU 1327 O LYS A 214 6766 6156 7565 634 530 -3388 O ATOM 1328 CB LYS A 214 15.038 39.943 35.128 1.00 54.78 C ANISOU 1328 CB LYS A 214 6225 7113 7474 791 1453 -3598 C ATOM 1329 CG LYS A 214 14.300 38.974 36.044 1.00 56.57 C ANISOU 1329 CG LYS A 214 5920 7820 7754 799 1925 -3508 C ATOM 1330 CD LYS A 214 13.381 39.644 37.026 1.00 62.69 C ANISOU 1330 CD LYS A 214 6692 8605 8522 1261 2286 -3853 C ATOM 1331 CE LYS A 214 12.745 38.677 38.002 1.00 65.50 C ANISOU 1331 CE LYS A 214 6796 9397 8694 1118 2777 -3792 C ATOM 1332 NZ LYS A 214 13.436 38.690 39.313 1.00 67.19 N ANISOU 1332 NZ LYS A 214 7552 9661 8315 912 2947 -3875 N ATOM 1333 N ALA A 215 16.721 39.868 31.889 1.00 47.71 N ANISOU 1333 N ALA A 215 5842 5627 6658 64 698 -2982 N ATOM 1334 CA ALA A 215 17.695 40.636 31.107 1.00 47.33 C ANISOU 1334 CA ALA A 215 6208 5197 6577 -178 388 -2839 C ATOM 1335 C ALA A 215 16.979 41.591 30.144 1.00 50.39 C ANISOU 1335 C ALA A 215 6756 5188 7201 -27 -14 -2829 C ATOM 1336 O ALA A 215 15.963 41.230 29.545 1.00 51.37 O ANISOU 1336 O ALA A 215 6647 5278 7591 29 -87 -2801 O ATOM 1337 CB ALA A 215 18.588 39.687 30.348 1.00 44.14 C ANISOU 1337 CB ALA A 215 5842 4930 5997 -563 543 -2539 C ATOM 1338 N LYS A 216 17.553 42.779 29.955 1.00 52.52 N ANISOU 1338 N LYS A 216 7387 5028 7538 -55 -301 -2771 N ATOM 1339 CA LYS A 216 16.900 43.834 29.175 1.00 56.54 C ANISOU 1339 CA LYS A 216 8068 5140 8274 144 -760 -2695 C ATOM 1340 C LYS A 216 17.235 43.699 27.686 1.00 56.02 C ANISOU 1340 C LYS A 216 8382 4847 8054 -225 -928 -2395 C ATOM 1341 O LYS A 216 16.415 44.057 26.846 1.00 59.19 O ANISOU 1341 O LYS A 216 8841 4934 8714 -146 -1256 -2258 O ATOM 1342 CB LYS A 216 17.300 45.220 29.685 1.00 59.48 C ANISOU 1342 CB LYS A 216 8778 5118 8701 267 -1078 -2832 C ATOM 1343 CG LYS A 216 16.457 45.735 30.842 1.00 63.23 C ANISOU 1343 CG LYS A 216 9106 5545 9371 845 -933 -3183 C ATOM 1344 CD LYS A 216 16.869 47.107 31.323 1.00 66.70 C ANISOU 1344 CD LYS A 216 10017 5533 9790 967 -1288 -3352 C ATOM 1345 CE LYS A 216 16.606 48.198 30.307 1.00 70.15 C ANISOU 1345 CE LYS A 216 10673 5504 10475 1001 -1946 -3177 C ATOM 1346 NZ LYS A 216 16.789 49.546 30.893 1.00 74.56 N ANISOU 1346 NZ LYS A 216 11699 5571 11059 1234 -2289 -3413 N ATOM 1347 N SER A 217 18.425 43.192 27.360 1.00 53.72 N ANISOU 1347 N SER A 217 8279 4719 7411 -553 -628 -2118 N ATOM 1348 CA SER A 217 18.828 43.018 25.960 1.00 53.70 C ANISOU 1348 CA SER A 217 8645 4547 7212 -992 -726 -1842 C ATOM 1349 C SER A 217 19.650 41.730 25.816 1.00 50.65 C ANISOU 1349 C SER A 217 8175 4483 6587 -1238 -118 -1684 C ATOM 1350 O SER A 217 20.007 41.105 26.815 1.00 49.34 O ANISOU 1350 O SER A 217 7692 4603 6451 -997 390 -1666 O ATOM 1351 CB SER A 217 19.586 44.205 25.448 1.00 55.98 C ANISOU 1351 CB SER A 217 9415 4460 7394 -1234 -1094 -1701 C ATOM 1352 OG SER A 217 20.921 44.200 25.923 1.00 55.03 O ANISOU 1352 OG SER A 217 9274 4564 7070 -1346 -766 -1506 O ATOM 1353 N LEU A 218 19.916 41.350 24.570 1.00 50.59 N ANISOU 1353 N LEU A 218 8481 4298 6442 -1721 -118 -1543 N ATOM 1354 CA LEU A 218 20.854 40.266 24.256 1.00 48.68 C ANISOU 1354 CA LEU A 218 8257 4212 6027 -2010 476 -1435 C ATOM 1355 C LEU A 218 22.283 40.829 24.211 1.00 49.16 C ANISOU 1355 C LEU A 218 8475 4226 5977 -2276 598 -1301 C ATOM 1356 O LEU A 218 23.220 40.109 23.901 1.00 49.29 O ANISOU 1356 O LEU A 218 8464 4375 5888 -2420 1170 -1074 O ATOM 1357 CB LEU A 218 20.466 39.620 22.919 1.00 50.00 C ANISOU 1357 CB LEU A 218 8833 4258 5905 -2289 502 -1281 C ATOM 1358 CG LEU A 218 19.137 38.867 22.905 1.00 49.92 C ANISOU 1358 CG LEU A 218 8632 4329 6007 -2109 342 -1339 C ATOM 1359 CD1 LEU A 218 18.734 38.491 21.488 1.00 52.90 C ANISOU 1359 CD1 LEU A 218 9557 4524 6017 -2412 153 -1146 C ATOM 1360 CD2 LEU A 218 19.198 37.625 23.782 1.00 46.84 C ANISOU 1360 CD2 LEU A 218 7767 4316 5712 -1927 822 -1446 C ATOM 1361 N GLY A 219 22.447 42.115 24.509 1.00 51.60 N ANISOU 1361 N GLY A 219 9015 4209 6381 -2200 78 -1360 N ATOM 1362 CA GLY A 219 23.772 42.715 24.629 1.00 52.78 C ANISOU 1362 CA GLY A 219 9271 4180 6600 -2476 -48 -1401 C ATOM 1363 C GLY A 219 24.386 42.995 23.269 1.00 56.23 C ANISOU 1363 C GLY A 219 10250 4478 6636 -2920 36 -1224 C ATOM 1364 O GLY A 219 23.672 43.122 22.276 1.00 58.10 O ANISOU 1364 O GLY A 219 10849 4578 6647 -2957 -190 -1187 O ATOM 1365 N ASN A 220 25.713 43.080 23.232 1.00 59.04 N ANISOU 1365 N ASN A 220 10327 4917 7188 -3379 111 -1305 N ATOM 1366 CA ASN A 220 26.460 43.292 21.993 1.00 63.76 C ANISOU 1366 CA ASN A 220 11494 5425 7305 -3912 426 -1192 C ATOM 1367 C ASN A 220 26.249 42.101 21.047 1.00 66.35 C ANISOU 1367 C ASN A 220 12031 5915 7262 -4181 978 -1534 C ATOM 1368 O ASN A 220 26.635 40.968 21.341 1.00 65.37 O ANISOU 1368 O ASN A 220 11470 6125 7240 -3721 1374 -1753 O ATOM 1369 CB ASN A 220 27.949 43.530 22.263 1.00 66.41 C ANISOU 1369 CB ASN A 220 11442 5796 7992 -4088 631 -932 C ATOM 1370 CG ASN A 220 28.728 43.945 21.031 1.00 71.15 C ANISOU 1370 CG ASN A 220 12480 6215 8339 -4529 948 -617 C ATOM 1371 OD1 ASN A 220 28.241 43.833 19.907 1.00 73.47 O ANISOU 1371 OD1 ASN A 220 13283 6431 8199 -4646 973 -638 O ATOM 1372 ND2 ASN A 220 29.943 44.428 21.229 1.00 74.17 N ANISOU 1372 ND2 ASN A 220 12541 6589 9050 -4748 992 -288 N ATOM 1373 N LEU A 221 25.645 42.404 19.902 1.00 36.03 N ANISOU 1373 N LEU A 221 3734 3660 6294 583 141 677 N ATOM 1374 CA LEU A 221 25.292 41.446 18.862 1.00 34.46 C ANISOU 1374 CA LEU A 221 3460 3877 5754 454 -259 1043 C ATOM 1375 C LEU A 221 26.214 41.647 17.650 1.00 33.14 C ANISOU 1375 C LEU A 221 3712 3458 5421 305 -461 1280 C ATOM 1376 O LEU A 221 25.900 41.213 16.544 1.00 35.19 O ANISOU 1376 O LEU A 221 4173 3730 5465 577 -1055 1469 O ATOM 1377 CB LEU A 221 23.823 41.672 18.484 1.00 35.63 C ANISOU 1377 CB LEU A 221 3545 3999 5993 483 -402 1175 C ATOM 1378 CG LEU A 221 22.801 41.241 19.534 1.00 36.65 C ANISOU 1378 CG LEU A 221 3518 4326 6078 412 -386 1090 C ATOM 1379 CD1 LEU A 221 21.413 41.758 19.192 1.00 38.49 C ANISOU 1379 CD1 LEU A 221 3589 4637 6398 512 -455 1412 C ATOM 1380 CD2 LEU A 221 22.792 39.730 19.677 1.00 35.69 C ANISOU 1380 CD2 LEU A 221 3621 4284 5655 418 -347 942 C ATOM 1381 N GLY A 222 27.376 42.261 17.859 1.00 33.49 N ANISOU 1381 N GLY A 222 3942 3092 5688 211 -385 974 N ATOM 1382 CA GLY A 222 28.289 42.594 16.757 1.00 32.83 C ANISOU 1382 CA GLY A 222 4164 2890 5419 475 -481 1325 C ATOM 1383 C GLY A 222 28.869 41.367 16.055 1.00 32.42 C ANISOU 1383 C GLY A 222 4304 3108 4905 540 -754 1182 C ATOM 1384 O GLY A 222 29.214 41.445 14.869 1.00 34.24 O ANISOU 1384 O GLY A 222 4892 3252 4864 765 -782 1570 O ATOM 1385 N ASP A 223 28.999 40.242 16.754 1.00 30.34 N ANISOU 1385 N ASP A 223 4130 3061 4334 602 -988 942 N ATOM 1386 CA ASP A 223 29.486 38.994 16.140 1.00 29.57 C ANISOU 1386 CA ASP A 223 4335 3134 3765 658 -1111 1029 C ATOM 1387 C ASP A 223 28.316 38.005 16.024 1.00 29.87 C ANISOU 1387 C ASP A 223 4384 3409 3554 612 -1245 874 C ATOM 1388 O ASP A 223 28.540 36.839 15.755 1.00 28.93 O ANISOU 1388 O ASP A 223 4319 3432 3241 497 -1153 738 O ATOM 1389 CB ASP A 223 30.659 38.396 16.935 1.00 28.91 C ANISOU 1389 CB ASP A 223 4534 3150 3299 599 -1042 1012 C ATOM 1390 CG ASP A 223 31.988 39.124 16.793 1.00 29.82 C ANISOU 1390 CG ASP A 223 4717 3218 3393 419 -962 1301 C ATOM 1391 OD1 ASP A 223 32.170 39.847 15.816 1.00 32.92 O ANISOU 1391 OD1 ASP A 223 5015 4008 3484 12 -627 1594 O ATOM 1392 OD2 ASP A 223 32.857 38.959 17.665 1.00 31.63 O ANISOU 1392 OD2 ASP A 223 4940 3871 3206 -105 -781 1359 O ATOM 1393 N ALA A 224 27.082 38.465 16.218 1.00 29.85 N ANISOU 1393 N ALA A 224 4406 3240 3696 650 -1217 979 N ATOM 1394 CA ALA A 224 25.927 37.584 16.386 1.00 30.66 C ANISOU 1394 CA ALA A 224 4309 3661 3680 447 -1333 675 C ATOM 1395 C ALA A 224 25.336 37.176 15.033 1.00 29.31 C ANISOU 1395 C ALA A 224 4059 3648 3428 394 -1386 1112 C ATOM 1396 O ALA A 224 25.518 37.865 14.030 1.00 32.34 O ANISOU 1396 O ALA A 224 4802 3817 3669 164 -1240 1285 O ATOM 1397 CB ALA A 224 24.871 38.280 17.213 1.00 30.50 C ANISOU 1397 CB ALA A 224 4022 3469 4098 401 -1417 623 C ATOM 1398 N ASP A 225 24.561 36.097 15.080 1.00 29.07 N ANISOU 1398 N ASP A 225 4009 3813 3220 300 -1045 865 N ATOM 1399 CA ASP A 225 23.692 35.666 13.990 1.00 30.29 C ANISOU 1399 CA ASP A 225 4097 4317 3092 139 -944 899 C ATOM 1400 C ASP A 225 22.239 35.935 14.397 1.00 28.39 C ANISOU 1400 C ASP A 225 3633 4113 3037 -306 -965 1379 C ATOM 1401 O ASP A 225 21.601 35.138 15.121 1.00 28.17 O ANISOU 1401 O ASP A 225 3653 4011 3039 -499 -752 1078 O ATOM 1402 CB ASP A 225 23.958 34.196 13.666 1.00 30.92 C ANISOU 1402 CB ASP A 225 4442 4378 2925 123 -965 671 C ATOM 1403 CG ASP A 225 23.342 33.735 12.363 1.00 34.94 C ANISOU 1403 CG ASP A 225 5190 5008 3077 310 -1156 422 C ATOM 1404 OD1 ASP A 225 22.195 34.142 12.076 1.00 38.15 O ANISOU 1404 OD1 ASP A 225 5536 5619 3338 521 -1383 336 O ATOM 1405 OD2 ASP A 225 24.022 32.985 11.640 1.00 37.07 O ANISOU 1405 OD2 ASP A 225 5458 5434 3192 836 -1304 292 O ATOM 1406 N THR A 226 21.700 37.060 13.927 1.00 31.20 N ANISOU 1406 N THR A 226 3722 4406 3726 137 -756 1250 N ATOM 1407 CA THR A 226 20.410 37.577 14.387 1.00 32.35 C ANISOU 1407 CA THR A 226 3613 4599 4079 7 -636 1307 C ATOM 1408 C THR A 226 19.251 36.717 13.869 1.00 33.32 C ANISOU 1408 C THR A 226 3363 5232 4063 111 -869 1208 C ATOM 1409 O THR A 226 18.236 36.562 14.565 1.00 35.12 O ANISOU 1409 O THR A 226 3149 5375 4817 -143 -765 853 O ATOM 1410 CB THR A 226 20.267 39.057 14.018 1.00 34.77 C ANISOU 1410 CB THR A 226 3874 4673 4662 -12 -340 1554 C ATOM 1411 OG1 THR A 226 20.543 39.244 12.627 1.00 36.65 O ANISOU 1411 OG1 THR A 226 4454 4691 4778 229 -205 1925 O ATOM 1412 CG2 THR A 226 21.179 39.911 14.869 1.00 34.65 C ANISOU 1412 CG2 THR A 226 3641 4427 5094 -183 -17 1431 C ATOM 1413 N GLU A 227 19.416 36.125 12.696 1.00 33.69 N ANISOU 1413 N GLU A 227 3454 5693 3653 264 -962 1492 N ATOM 1414 CA GLU A 227 18.384 35.278 12.092 1.00 35.86 C ANISOU 1414 CA GLU A 227 3801 6318 3506 259 -1358 1229 C ATOM 1415 C GLU A 227 18.194 33.983 12.890 1.00 33.34 C ANISOU 1415 C GLU A 227 3282 5793 3591 232 -1258 776 C ATOM 1416 O GLU A 227 17.055 33.523 13.086 1.00 34.69 O ANISOU 1416 O GLU A 227 3246 6099 3834 179 -1188 429 O ATOM 1417 CB GLU A 227 18.754 34.969 10.638 1.00 39.24 C ANISOU 1417 CB GLU A 227 4528 6992 3387 352 -1306 1413 C ATOM 1418 CG GLU A 227 17.783 34.016 9.970 1.00 44.13 C ANISOU 1418 CG GLU A 227 5160 7710 3894 123 -1807 1138 C ATOM 1419 CD GLU A 227 16.339 34.496 9.974 1.00 48.94 C ANISOU 1419 CD GLU A 227 5261 8276 5058 196 -2038 1364 C ATOM 1420 OE1 GLU A 227 16.126 35.708 9.787 1.00 55.63 O ANISOU 1420 OE1 GLU A 227 6588 8421 6129 401 -2391 1424 O ATOM 1421 OE2 GLU A 227 15.433 33.663 10.175 1.00 52.80 O ANISOU 1421 OE2 GLU A 227 6058 8501 5501 -338 -1914 1369 O ATOM 1422 N HIS A 228 19.307 33.407 13.356 1.00 31.85 N ANISOU 1422 N HIS A 228 3607 5462 3031 243 -1449 857 N ATOM 1423 CA HIS A 228 19.316 32.039 13.875 1.00 31.04 C ANISOU 1423 CA HIS A 228 3695 5151 2945 268 -1262 466 C ATOM 1424 C HIS A 228 19.319 32.009 15.419 1.00 27.23 C ANISOU 1424 C HIS A 228 3177 4280 2889 214 -1111 562 C ATOM 1425 O HIS A 228 19.105 30.953 16.019 1.00 26.07 O ANISOU 1425 O HIS A 228 2866 4035 3004 532 -870 415 O ATOM 1426 CB HIS A 228 20.521 31.279 13.296 1.00 33.32 C ANISOU 1426 CB HIS A 228 3999 5361 3299 407 -1158 102 C ATOM 1427 CG HIS A 228 20.449 31.059 11.822 1.00 37.06 C ANISOU 1427 CG HIS A 228 4617 6113 3349 386 -1370 -39 C ATOM 1428 ND1 HIS A 228 21.263 31.728 10.914 1.00 38.49 N ANISOU 1428 ND1 HIS A 228 4956 6420 3245 385 -1152 -82 N ATOM 1429 CD2 HIS A 228 19.639 30.272 11.081 1.00 40.64 C ANISOU 1429 CD2 HIS A 228 5291 6601 3548 165 -1465 -422 C ATOM 1430 CE1 HIS A 228 20.963 31.348 9.689 1.00 41.59 C ANISOU 1430 CE1 HIS A 228 5469 6909 3425 426 -1365 -333 C ATOM 1431 NE2 HIS A 228 19.964 30.464 9.764 1.00 42.61 N ANISOU 1431 NE2 HIS A 228 5733 6942 3514 307 -1382 -489 N ATOM 1432 N TYR A 229 19.442 33.163 16.080 1.00 27.28 N ANISOU 1432 N TYR A 229 3080 4193 3093 369 -888 595 N ATOM 1433 CA TYR A 229 19.621 33.221 17.536 1.00 24.44 C ANISOU 1433 CA TYR A 229 2442 3740 3101 309 -737 543 C ATOM 1434 C TYR A 229 18.464 32.540 18.269 1.00 25.08 C ANISOU 1434 C TYR A 229 2696 3678 3154 264 -688 596 C ATOM 1435 O TYR A 229 18.726 31.702 19.134 1.00 24.13 O ANISOU 1435 O TYR A 229 2681 3517 2969 267 -760 401 O ATOM 1436 CB TYR A 229 19.766 34.665 18.027 1.00 24.78 C ANISOU 1436 CB TYR A 229 2542 3561 3311 282 -524 748 C ATOM 1437 CG TYR A 229 20.479 34.864 19.344 1.00 23.85 C ANISOU 1437 CG TYR A 229 2490 3294 3278 330 -348 632 C ATOM 1438 CD1 TYR A 229 20.082 34.214 20.511 1.00 23.51 C ANISOU 1438 CD1 TYR A 229 2445 3356 3129 75 -393 554 C ATOM 1439 CD2 TYR A 229 21.471 35.821 19.441 1.00 23.23 C ANISOU 1439 CD2 TYR A 229 2344 3155 3327 540 -397 609 C ATOM 1440 CE1 TYR A 229 20.726 34.444 21.718 1.00 22.33 C ANISOU 1440 CE1 TYR A 229 2306 3073 3103 176 -277 396 C ATOM 1441 CE2 TYR A 229 22.152 36.037 20.637 1.00 22.73 C ANISOU 1441 CE2 TYR A 229 2319 3010 3308 386 -217 469 C ATOM 1442 CZ TYR A 229 21.761 35.359 21.778 1.00 21.38 C ANISOU 1442 CZ TYR A 229 2241 2759 3121 340 -357 351 C ATOM 1443 OH TYR A 229 22.438 35.600 22.950 1.00 22.21 O ANISOU 1443 OH TYR A 229 2382 2953 3102 455 -424 79 O ATOM 1444 N ALA A 230 17.211 32.899 17.929 1.00 25.93 N ANISOU 1444 N ALA A 230 2459 4029 3362 112 -846 796 N ATOM 1445 CA ALA A 230 16.134 32.360 18.720 1.00 26.24 C ANISOU 1445 CA ALA A 230 2382 4006 3582 49 -723 635 C ATOM 1446 C ALA A 230 16.160 30.829 18.652 1.00 26.11 C ANISOU 1446 C ALA A 230 2570 3984 3366 271 -855 580 C ATOM 1447 O ALA A 230 15.910 30.128 19.660 1.00 25.51 O ANISOU 1447 O ALA A 230 2249 3959 3485 226 -697 549 O ATOM 1448 CB ALA A 230 14.827 32.934 18.241 1.00 27.81 C ANISOU 1448 CB ALA A 230 2519 4195 3851 223 -834 778 C ATOM 1449 N ALA A 231 16.306 30.297 17.430 1.00 27.15 N ANISOU 1449 N ALA A 231 2745 4202 3367 434 -973 358 N ATOM 1450 CA ALA A 231 16.283 28.838 17.245 1.00 27.06 C ANISOU 1450 CA ALA A 231 2747 4276 3259 302 -1146 124 C ATOM 1451 C ALA A 231 17.456 28.189 17.988 1.00 25.20 C ANISOU 1451 C ALA A 231 2752 3877 2945 242 -1147 41 C ATOM 1452 O ALA A 231 17.304 27.107 18.573 1.00 25.61 O ANISOU 1452 O ALA A 231 2785 3817 3126 13 -1004 -58 O ATOM 1453 CB ALA A 231 16.309 28.504 15.774 1.00 29.78 C ANISOU 1453 CB ALA A 231 3251 4796 3267 350 -1204 101 C ATOM 1454 N SER A 232 18.593 28.875 18.009 1.00 25.19 N ANISOU 1454 N SER A 232 2755 3927 2888 318 -886 45 N ATOM 1455 CA SER A 232 19.783 28.376 18.679 1.00 24.51 C ANISOU 1455 CA SER A 232 2797 3732 2782 486 -836 -217 C ATOM 1456 C SER A 232 19.561 28.327 20.204 1.00 23.22 C ANISOU 1456 C SER A 232 2595 3425 2801 265 -872 -370 C ATOM 1457 O SER A 232 19.855 27.320 20.844 1.00 23.07 O ANISOU 1457 O SER A 232 2267 3463 3033 434 -859 -470 O ATOM 1458 CB SER A 232 21.002 29.185 18.283 1.00 24.66 C ANISOU 1458 CB SER A 232 2867 3629 2873 408 -1065 -274 C ATOM 1459 OG SER A 232 21.264 29.031 16.885 1.00 27.24 O ANISOU 1459 OG SER A 232 3215 4188 2946 831 -1158 -594 O ATOM 1460 N ALA A 233 18.953 29.378 20.776 1.00 22.59 N ANISOU 1460 N ALA A 233 2073 3611 2897 436 -703 -58 N ATOM 1461 CA ALA A 233 18.577 29.374 22.198 1.00 22.76 C ANISOU 1461 CA ALA A 233 2290 3382 2974 349 -618 -210 C ATOM 1462 C ALA A 233 17.650 28.201 22.519 1.00 22.95 C ANISOU 1462 C ALA A 233 2201 3448 3071 290 -552 -117 C ATOM 1463 O ALA A 233 17.807 27.524 23.530 1.00 21.95 O ANISOU 1463 O ALA A 233 1837 3397 3105 110 -376 -98 O ATOM 1464 CB ALA A 233 17.962 30.699 22.570 1.00 23.31 C ANISOU 1464 CB ALA A 233 2364 3331 3162 488 -602 -116 C ATOM 1465 N ARG A 234 16.592 28.018 21.709 1.00 23.60 N ANISOU 1465 N ARG A 234 2010 3574 3383 -84 -469 102 N ATOM 1466 CA ARG A 234 15.606 26.960 21.963 1.00 24.20 C ANISOU 1466 CA ARG A 234 2139 3570 3484 -204 -571 8 C ATOM 1467 C ARG A 234 16.236 25.582 21.767 1.00 22.75 C ANISOU 1467 C ARG A 234 1749 3539 3353 -234 -743 -19 C ATOM 1468 O ARG A 234 15.929 24.638 22.512 1.00 25.12 O ANISOU 1468 O ARG A 234 2335 3547 3662 -331 -352 -97 O ATOM 1469 CB ARG A 234 14.376 27.165 21.082 1.00 25.31 C ANISOU 1469 CB ARG A 234 2044 3781 3788 -140 -701 108 C ATOM 1470 CG ARG A 234 13.562 28.371 21.524 1.00 25.91 C ANISOU 1470 CG ARG A 234 2050 3864 3929 20 -669 238 C ATOM 1471 CD ARG A 234 12.317 28.572 20.692 1.00 27.46 C ANISOU 1471 CD ARG A 234 2206 4051 4177 26 -801 361 C ATOM 1472 NE ARG A 234 11.488 29.644 21.217 1.00 27.60 N ANISOU 1472 NE ARG A 234 2112 3948 4425 63 -709 571 N ATOM 1473 CZ ARG A 234 11.371 30.859 20.679 1.00 28.99 C ANISOU 1473 CZ ARG A 234 2287 4103 4623 256 -584 772 C ATOM 1474 NH1 ARG A 234 11.803 31.109 19.449 1.00 30.38 N ANISOU 1474 NH1 ARG A 234 2201 4645 4697 87 -630 745 N ATOM 1475 NH2 ARG A 234 10.785 31.826 21.367 1.00 29.32 N ANISOU 1475 NH2 ARG A 234 1911 4171 5056 331 -419 943 N ATOM 1476 N ALA A 235 17.184 25.479 20.827 1.00 24.86 N ANISOU 1476 N ALA A 235 2266 3885 3293 -153 -661 -403 N ATOM 1477 CA ALA A 235 17.887 24.209 20.603 1.00 25.12 C ANISOU 1477 CA ALA A 235 2373 3966 3204 -37 -689 -471 C ATOM 1478 C ALA A 235 18.725 23.836 21.837 1.00 22.42 C ANISOU 1478 C ALA A 235 1868 3493 3156 -131 -548 -403 C ATOM 1479 O ALA A 235 18.785 22.673 22.227 1.00 23.52 O ANISOU 1479 O ALA A 235 2340 3449 3147 -116 -546 -611 O ATOM 1480 CB ALA A 235 18.733 24.310 19.360 1.00 25.16 C ANISOU 1480 CB ALA A 235 2603 4054 2902 -178 -870 -551 C ATOM 1481 N PHE A 236 19.351 24.834 22.469 1.00 23.31 N ANISOU 1481 N PHE A 236 2201 3429 3226 37 -701 -448 N ATOM 1482 CA PHE A 236 20.063 24.615 23.732 1.00 22.34 C ANISOU 1482 CA PHE A 236 2063 3426 2998 -77 -498 -552 C ATOM 1483 C PHE A 236 19.101 24.017 24.773 1.00 21.30 C ANISOU 1483 C PHE A 236 1561 3329 3202 -153 -670 -498 C ATOM 1484 O PHE A 236 19.406 23.023 25.409 1.00 22.34 O ANISOU 1484 O PHE A 236 2017 3285 3186 -92 -270 -527 O ATOM 1485 CB PHE A 236 20.725 25.914 24.205 1.00 21.20 C ANISOU 1485 CB PHE A 236 1610 3409 3036 19 -484 -552 C ATOM 1486 CG PHE A 236 21.109 25.902 25.660 1.00 19.70 C ANISOU 1486 CG PHE A 236 1440 3119 2923 -16 -303 -640 C ATOM 1487 CD1 PHE A 236 22.194 25.150 26.087 1.00 19.80 C ANISOU 1487 CD1 PHE A 236 1443 3172 2907 85 -166 -732 C ATOM 1488 CD2 PHE A 236 20.411 26.646 26.599 1.00 21.26 C ANISOU 1488 CD2 PHE A 236 1418 3347 3309 30 -80 -718 C ATOM 1489 CE1 PHE A 236 22.548 25.106 27.429 1.00 18.97 C ANISOU 1489 CE1 PHE A 236 1221 3088 2896 -14 -97 -724 C ATOM 1490 CE2 PHE A 236 20.771 26.610 27.940 1.00 22.27 C ANISOU 1490 CE2 PHE A 236 1644 3517 3301 276 -75 -802 C ATOM 1491 CZ PHE A 236 21.832 25.840 28.351 1.00 20.45 C ANISOU 1491 CZ PHE A 236 1569 3223 2978 120 -184 -939 C ATOM 1492 N GLY A 237 17.903 24.600 24.906 1.00 22.30 N ANISOU 1492 N GLY A 237 1705 3431 3336 -99 -388 -560 N ATOM 1493 CA GLY A 237 16.913 24.123 25.897 1.00 23.37 C ANISOU 1493 CA GLY A 237 1581 3717 3580 -118 -289 -619 C ATOM 1494 C GLY A 237 16.460 22.702 25.607 1.00 23.30 C ANISOU 1494 C GLY A 237 1594 3583 3676 -142 -392 -451 C ATOM 1495 O GLY A 237 16.331 21.848 26.521 1.00 25.21 O ANISOU 1495 O GLY A 237 2183 3461 3934 -20 -54 -406 O ATOM 1496 N ALA A 238 16.256 22.424 24.325 1.00 25.24 N ANISOU 1496 N ALA A 238 2031 3795 3762 -200 -550 -759 N ATOM 1497 CA ALA A 238 15.777 21.125 23.889 1.00 27.40 C ANISOU 1497 CA ALA A 238 2384 4103 3924 -444 -694 -963 C ATOM 1498 C ALA A 238 16.857 20.054 24.046 1.00 27.08 C ANISOU 1498 C ALA A 238 2322 3978 3987 -506 -485 -1035 C ATOM 1499 O ALA A 238 16.523 18.887 24.201 1.00 28.71 O ANISOU 1499 O ALA A 238 2376 3929 4601 -473 -370 -1239 O ATOM 1500 CB ALA A 238 15.286 21.193 22.464 1.00 28.88 C ANISOU 1500 CB ALA A 238 2422 4494 4055 -336 -859 -1027 C ATOM 1501 N ALA A 239 18.143 20.449 23.986 1.00 25.10 N ANISOU 1501 N ALA A 239 2194 3781 3560 -306 -507 -883 N ATOM 1502 CA ALA A 239 19.279 19.522 24.132 1.00 24.81 C ANISOU 1502 CA ALA A 239 2198 3571 3656 -363 -360 -1049 C ATOM 1503 C ALA A 239 19.398 19.053 25.584 1.00 22.83 C ANISOU 1503 C ALA A 239 1775 3178 3721 -495 -277 -887 C ATOM 1504 O ALA A 239 19.841 17.928 25.820 1.00 25.47 O ANISOU 1504 O ALA A 239 2509 3202 3964 -399 -299 -954 O ATOM 1505 CB ALA A 239 20.575 20.168 23.674 1.00 24.71 C ANISOU 1505 CB ALA A 239 2141 3654 3593 -218 -253 -988 C ATOM 1506 N PHE A 240 19.007 19.922 26.526 1.00 23.24 N ANISOU 1506 N PHE A 240 1827 3154 3846 -381 -186 -860 N ATOM 1507 CA PHE A 240 19.140 19.664 27.970 1.00 23.61 C ANISOU 1507 CA PHE A 240 1789 3354 3827 -344 -28 -977 C ATOM 1508 C PHE A 240 17.777 19.849 28.652 1.00 24.59 C ANISOU 1508 C PHE A 240 1884 3336 4123 -612 158 -918 C ATOM 1509 O PHE A 240 17.621 20.708 29.527 1.00 24.04 O ANISOU 1509 O PHE A 240 1899 3279 3953 -354 114 -832 O ATOM 1510 CB PHE A 240 20.216 20.582 28.548 1.00 21.77 C ANISOU 1510 CB PHE A 240 1708 3132 3430 -353 12 -760 C ATOM 1511 CG PHE A 240 21.544 20.486 27.842 1.00 21.06 C ANISOU 1511 CG PHE A 240 1670 3036 3294 -371 -68 -892 C ATOM 1512 CD1 PHE A 240 22.339 19.372 28.010 1.00 21.91 C ANISOU 1512 CD1 PHE A 240 1685 3143 3496 -282 -49 -809 C ATOM 1513 CD2 PHE A 240 21.993 21.508 27.018 1.00 20.65 C ANISOU 1513 CD2 PHE A 240 1593 3012 3240 -182 -135 -815 C ATOM 1514 CE1 PHE A 240 23.562 19.284 27.367 1.00 20.93 C ANISOU 1514 CE1 PHE A 240 1817 2904 3230 -86 -26 -884 C ATOM 1515 CE2 PHE A 240 23.229 21.430 26.394 1.00 20.05 C ANISOU 1515 CE2 PHE A 240 1679 3043 2893 -215 -119 -707 C ATOM 1516 CZ PHE A 240 23.998 20.305 26.555 1.00 20.46 C ANISOU 1516 CZ PHE A 240 1675 3086 3013 -88 -76 -817 C ATOM 1517 N PRO A 241 16.781 19.051 28.238 1.00 26.93 N ANISOU 1517 N PRO A 241 1815 3560 4856 -728 253 -1053 N ATOM 1518 CA PRO A 241 15.419 19.295 28.708 1.00 28.47 C ANISOU 1518 CA PRO A 241 1842 3566 5406 -839 475 -996 C ATOM 1519 C PRO A 241 15.168 19.151 30.220 1.00 29.72 C ANISOU 1519 C PRO A 241 2188 3584 5519 -820 674 -798 C ATOM 1520 O PRO A 241 14.167 19.678 30.703 1.00 33.84 O ANISOU 1520 O PRO A 241 2236 4540 6081 -724 1153 -564 O ATOM 1521 CB PRO A 241 14.593 18.256 27.933 1.00 31.43 C ANISOU 1521 CB PRO A 241 2227 3993 5721 -909 93 -1108 C ATOM 1522 CG PRO A 241 15.573 17.153 27.615 1.00 30.89 C ANISOU 1522 CG PRO A 241 2357 3725 5652 -1043 182 -1132 C ATOM 1523 CD PRO A 241 16.889 17.862 27.398 1.00 28.35 C ANISOU 1523 CD PRO A 241 2025 3622 5121 -784 105 -1234 C ATOM 1524 N LYS A 242 15.994 18.391 30.923 1.00 30.24 N ANISOU 1524 N LYS A 242 2724 3514 5252 -990 725 -497 N ATOM 1525 CA LYS A 242 15.830 18.113 32.352 1.00 31.82 C ANISOU 1525 CA LYS A 242 3147 3597 5345 -1099 1000 -436 C ATOM 1526 C LYS A 242 16.580 19.156 33.195 1.00 30.96 C ANISOU 1526 C LYS A 242 3082 3558 5124 -1051 1015 -450 C ATOM 1527 O LYS A 242 16.435 19.158 34.415 1.00 35.28 O ANISOU 1527 O LYS A 242 4181 4110 5113 -900 1005 -215 O ATOM 1528 CB LYS A 242 16.357 16.710 32.684 1.00 37.06 C ANISOU 1528 CB LYS A 242 4530 3673 5877 -849 945 -372 C ATOM 1529 CG LYS A 242 15.561 15.549 32.100 1.00 41.03 C ANISOU 1529 CG LYS A 242 4859 4111 6619 -1285 946 -492 C ATOM 1530 CD LYS A 242 15.852 14.203 32.757 1.00 46.50 C ANISOU 1530 CD LYS A 242 5606 4927 7133 -957 1043 255 C ATOM 1531 CE LYS A 242 17.009 13.436 32.146 1.00 48.42 C ANISOU 1531 CE LYS A 242 5724 5452 7221 -646 862 112 C ATOM 1532 NZ LYS A 242 18.309 13.792 32.768 1.00 48.84 N ANISOU 1532 NZ LYS A 242 5942 5779 6833 -809 827 427 N ATOM 1533 N ALA A 243 17.390 20.019 32.575 1.00 26.37 N ANISOU 1533 N ALA A 243 2192 3388 4437 -707 836 -742 N ATOM 1534 CA ALA A 243 18.223 20.970 33.331 1.00 24.98 C ANISOU 1534 CA ALA A 243 1969 3540 3982 -484 622 -665 C ATOM 1535 C ALA A 243 17.323 22.051 33.948 1.00 25.44 C ANISOU 1535 C ALA A 243 2088 3596 3981 -448 564 -773 C ATOM 1536 O ALA A 243 16.627 22.786 33.238 1.00 28.39 O ANISOU 1536 O ALA A 243 2508 3815 4462 283 529 -914 O ATOM 1537 CB ALA A 243 19.285 21.566 32.435 1.00 23.96 C ANISOU 1537 CB ALA A 243 1876 3369 3857 -503 551 -777 C ATOM 1538 N SER A 244 17.314 22.141 35.279 1.00 24.32 N ANISOU 1538 N SER A 244 1655 3608 3976 -339 758 -698 N ATOM 1539 CA SER A 244 16.493 23.114 35.985 1.00 25.46 C ANISOU 1539 CA SER A 244 1812 3596 4265 -103 778 -608 C ATOM 1540 C SER A 244 17.321 24.332 36.411 1.00 24.45 C ANISOU 1540 C SER A 244 1519 3589 4179 -144 1036 -571 C ATOM 1541 O SER A 244 16.763 25.386 36.743 1.00 27.59 O ANISOU 1541 O SER A 244 1641 4073 4768 42 910 -1171 O ATOM 1542 CB SER A 244 15.810 22.486 37.160 1.00 27.58 C ANISOU 1542 CB SER A 244 1846 4066 4564 -71 1116 -487 C ATOM 1543 OG SER A 244 16.747 21.912 38.053 1.00 27.69 O ANISOU 1543 OG SER A 244 2445 3820 4254 -276 1259 -62 O ATOM 1544 N MET A 245 18.652 24.198 36.417 1.00 22.36 N ANISOU 1544 N MET A 245 1495 3302 3697 -148 890 -604 N ATOM 1545 CA MET A 245 19.552 25.325 36.720 1.00 21.74 C ANISOU 1545 CA MET A 245 1534 3284 3440 -87 1037 -718 C ATOM 1546 C MET A 245 20.336 25.657 35.459 1.00 20.51 C ANISOU 1546 C MET A 245 1405 3233 3154 12 768 -674 C ATOM 1547 O MET A 245 21.165 24.873 35.003 1.00 20.80 O ANISOU 1547 O MET A 245 1706 3107 3087 136 900 -467 O ATOM 1548 CB MET A 245 20.535 25.013 37.854 1.00 23.39 C ANISOU 1548 CB MET A 245 1674 3765 3446 -356 987 -666 C ATOM 1549 CG MET A 245 21.413 26.203 38.213 1.00 23.39 C ANISOU 1549 CG MET A 245 2049 3620 3218 -322 1016 -835 C ATOM 1550 SD MET A 245 22.647 25.826 39.454 0.79 24.74 S ANISOU 1550 SD MET A 245 2102 3824 3474 -221 675 -1180 S ATOM 1551 CE MET A 245 21.699 25.015 40.736 1.00 33.43 C ANISOU 1551 CE MET A 245 3620 5202 3877 -400 622 -118 C ATOM 1552 N ILE A 246 20.074 26.853 34.951 1.00 19.74 N ANISOU 1552 N ILE A 246 1147 3036 3317 -14 649 -737 N ATOM 1553 CA ILE A 246 20.740 27.352 33.769 1.00 19.63 C ANISOU 1553 CA ILE A 246 1421 2877 3161 -17 484 -677 C ATOM 1554 C ILE A 246 21.820 28.343 34.201 1.00 19.43 C ANISOU 1554 C ILE A 246 1511 2918 2952 -14 608 -956 C ATOM 1555 O ILE A 246 21.548 29.355 34.847 1.00 20.40 O ANISOU 1555 O ILE A 246 1374 2958 3418 -11 486 -1155 O ATOM 1556 CB ILE A 246 19.742 27.984 32.776 1.00 21.24 C ANISOU 1556 CB ILE A 246 1673 2981 3415 27 198 -790 C ATOM 1557 CG1 ILE A 246 18.588 27.029 32.446 1.00 22.28 C ANISOU 1557 CG1 ILE A 246 1622 3098 3746 1 163 -686 C ATOM 1558 CG2 ILE A 246 20.476 28.438 31.516 1.00 21.31 C ANISOU 1558 CG2 ILE A 246 2047 2839 3210 -95 1 -708 C ATOM 1559 CD1 ILE A 246 19.022 25.661 31.943 1.00 21.75 C ANISOU 1559 CD1 ILE A 246 1687 3126 3450 21 131 -700 C ATOM 1560 N VAL A 247 23.053 28.002 33.857 1.00 17.89 N ANISOU 1560 N VAL A 247 1454 2737 2605 -44 463 -876 N ATOM 1561 CA VAL A 247 24.222 28.815 34.183 1.00 16.91 C ANISOU 1561 CA VAL A 247 1355 2689 2380 35 454 -764 C ATOM 1562 C VAL A 247 24.632 29.564 32.915 1.00 16.08 C ANISOU 1562 C VAL A 247 1302 2408 2399 187 229 -720 C ATOM 1563 O VAL A 247 24.552 29.018 31.807 1.00 16.58 O ANISOU 1563 O VAL A 247 1479 2463 2358 17 229 -674 O ATOM 1564 CB VAL A 247 25.338 27.941 34.777 1.00 16.34 C ANISOU 1564 CB VAL A 247 1484 2557 2164 -19 528 -623 C ATOM 1565 CG1 VAL A 247 26.579 28.748 35.139 1.00 17.38 C ANISOU 1565 CG1 VAL A 247 1475 2720 2408 42 441 -765 C ATOM 1566 CG2 VAL A 247 24.827 27.180 35.985 1.00 17.37 C ANISOU 1566 CG2 VAL A 247 1493 2831 2275 -26 529 -447 C ATOM 1567 N MET A 248 25.099 30.793 33.082 1.00 16.10 N ANISOU 1567 N MET A 248 1385 2507 2222 102 375 -659 N ATOM 1568 CA AMET A 248 25.444 31.560 31.893 0.55 15.55 C ANISOU 1568 CA AMET A 248 1298 2351 2260 212 229 -612 C ATOM 1569 CA BMET A 248 25.300 31.730 31.979 0.45 16.38 C ANISOU 1569 CA BMET A 248 1357 2360 2505 159 205 -498 C ATOM 1570 C MET A 248 26.551 32.564 32.238 1.00 15.46 C ANISOU 1570 C MET A 248 1207 2410 2255 202 420 -667 C ATOM 1571 O MET A 248 26.946 32.728 33.380 1.00 16.57 O ANISOU 1571 O MET A 248 1457 2576 2261 21 340 -756 O ATOM 1572 CB AMET A 248 24.200 32.254 31.317 0.55 17.52 C ANISOU 1572 CB AMET A 248 1266 2708 2680 379 279 -596 C ATOM 1573 CB BMET A 248 24.128 32.711 31.881 0.45 18.28 C ANISOU 1573 CB BMET A 248 1623 2531 2790 353 360 -228 C ATOM 1574 CG AMET A 248 23.672 33.362 32.204 0.55 19.04 C ANISOU 1574 CG AMET A 248 1473 2870 2889 418 310 -769 C ATOM 1575 CG BMET A 248 22.832 32.070 31.515 0.45 19.09 C ANISOU 1575 CG BMET A 248 1735 2759 2757 145 477 -65 C ATOM 1576 SD AMET A 248 21.894 33.667 32.016 0.55 25.84 S ANISOU 1576 SD AMET A 248 1589 3938 4289 879 496 -687 S ATOM 1577 SD BMET A 248 21.501 33.088 32.141 0.45 20.54 S ANISOU 1577 SD BMET A 248 1892 2683 3227 260 728 398 S ATOM 1578 CE AMET A 248 21.231 32.274 32.927 0.55 27.52 C ANISOU 1578 CE AMET A 248 2210 3692 4554 150 75 -975 C ATOM 1579 CE BMET A 248 21.334 32.467 33.811 0.45 21.79 C ANISOU 1579 CE BMET A 248 1740 3137 3403 16 1026 202 C ATOM 1580 N SER A 249 27.129 33.153 31.205 1.00 15.28 N ANISOU 1580 N SER A 249 1241 2386 2179 182 271 -563 N ATOM 1581 CA SER A 249 28.359 33.939 31.415 1.00 15.15 C ANISOU 1581 CA SER A 249 1320 2251 2185 224 288 -594 C ATOM 1582 C SER A 249 28.128 35.229 32.182 1.00 16.42 C ANISOU 1582 C SER A 249 1489 2227 2520 134 457 -643 C ATOM 1583 O SER A 249 29.018 35.655 32.911 1.00 16.94 O ANISOU 1583 O SER A 249 1748 2239 2448 93 330 -673 O ATOM 1584 CB SER A 249 29.026 34.283 30.107 1.00 15.49 C ANISOU 1584 CB SER A 249 1552 2154 2177 264 245 -471 C ATOM 1585 OG SER A 249 29.448 33.102 29.448 1.00 14.76 O ANISOU 1585 OG SER A 249 1521 2038 2047 213 167 -448 O ATOM 1586 N HIS A 250 27.012 35.901 31.923 1.00 17.44 N ANISOU 1586 N HIS A 250 1594 2263 2769 262 499 -636 N ATOM 1587 CA HIS A 250 26.908 37.281 32.357 1.00 19.41 C ANISOU 1587 CA HIS A 250 1921 2334 3117 411 585 -765 C ATOM 1588 C HIS A 250 25.661 37.510 33.218 1.00 21.36 C ANISOU 1588 C HIS A 250 2210 2403 3500 313 976 -808 C ATOM 1589 O HIS A 250 25.248 38.668 33.374 1.00 26.74 O ANISOU 1589 O HIS A 250 3160 2529 4469 569 1518 -543 O ATOM 1590 CB HIS A 250 26.977 38.246 31.162 1.00 19.84 C ANISOU 1590 CB HIS A 250 1982 2282 3275 492 391 -675 C ATOM 1591 CG HIS A 250 28.221 38.071 30.344 1.00 18.77 C ANISOU 1591 CG HIS A 250 1792 2183 3154 549 175 -750 C ATOM 1592 ND1 HIS A 250 29.500 38.231 30.856 1.00 18.94 N ANISOU 1592 ND1 HIS A 250 1807 2318 3071 432 216 -785 N ATOM 1593 CD2 HIS A 250 28.386 37.718 29.050 1.00 18.95 C ANISOU 1593 CD2 HIS A 250 1889 2260 3049 579 -83 -686 C ATOM 1594 CE1 HIS A 250 30.398 37.955 29.914 1.00 18.94 C ANISOU 1594 CE1 HIS A 250 1764 2461 2970 455 75 -804 C ATOM 1595 NE2 HIS A 250 29.733 37.634 28.788 1.00 18.44 N ANISOU 1595 NE2 HIS A 250 1853 2323 2828 395 -130 -415 N ATOM 1596 N SER A 251 25.096 36.442 33.779 1.00 20.89 N ANISOU 1596 N SER A 251 2030 2573 3332 335 847 -671 N ATOM 1597 CA SER A 251 24.032 36.540 34.783 1.00 22.81 C ANISOU 1597 CA SER A 251 2068 2833 3763 462 1056 -699 C ATOM 1598 C SER A 251 24.284 35.437 35.808 1.00 20.91 C ANISOU 1598 C SER A 251 1869 2748 3326 299 853 -970 C ATOM 1599 O SER A 251 24.913 34.443 35.463 1.00 19.58 O ANISOU 1599 O SER A 251 1775 2588 3075 269 796 -809 O ATOM 1600 CB SER A 251 22.661 36.346 34.180 1.00 25.44 C ANISOU 1600 CB SER A 251 1970 3297 4396 665 1066 -188 C ATOM 1601 OG SER A 251 22.358 37.327 33.207 1.00 29.57 O ANISOU 1601 OG SER A 251 2589 3541 5104 938 1174 253 O ATOM 1602 N ALA A 252 23.719 35.586 37.003 1.00 21.89 N ANISOU 1602 N ALA A 252 2018 2880 3420 375 948 -1099 N ATOM 1603 CA ALA A 252 23.714 34.521 37.982 1.00 21.54 C ANISOU 1603 CA ALA A 252 1931 3091 3162 199 811 -1091 C ATOM 1604 C ALA A 252 22.847 33.361 37.484 1.00 21.09 C ANISOU 1604 C ALA A 252 1932 3088 2993 238 745 -1025 C ATOM 1605 O ALA A 252 21.991 33.556 36.624 1.00 22.23 O ANISOU 1605 O ALA A 252 1836 3265 3343 434 638 -998 O ATOM 1606 CB ALA A 252 23.215 35.076 39.299 1.00 23.98 C ANISOU 1606 CB ALA A 252 2269 3540 3302 44 1008 -1295 C ATOM 1607 N PRO A 253 23.027 32.160 38.062 1.00 19.87 N ANISOU 1607 N PRO A 253 1561 3148 2840 95 789 -926 N ATOM 1608 CA PRO A 253 22.214 31.002 37.659 1.00 19.65 C ANISOU 1608 CA PRO A 253 1463 3284 2719 56 581 -812 C ATOM 1609 C PRO A 253 20.720 31.314 37.782 1.00 20.62 C ANISOU 1609 C PRO A 253 1474 3317 3041 54 761 -889 C ATOM 1610 O PRO A 253 20.283 31.996 38.706 1.00 22.75 O ANISOU 1610 O PRO A 253 1794 3737 3110 64 823 -1086 O ATOM 1611 CB PRO A 253 22.647 29.880 38.599 1.00 21.44 C ANISOU 1611 CB PRO A 253 1897 3303 2946 104 594 -695 C ATOM 1612 CG PRO A 253 24.080 30.243 38.891 1.00 20.60 C ANISOU 1612 CG PRO A 253 1831 3364 2630 58 719 -695 C ATOM 1613 CD PRO A 253 24.084 31.751 38.999 1.00 20.48 C ANISOU 1613 CD PRO A 253 1684 3415 2681 46 783 -836 C ATOM 1614 N ASP A 254 19.943 30.781 36.856 1.00 20.91 N ANISOU 1614 N ASP A 254 1579 3205 3160 289 582 -988 N ATOM 1615 CA ASP A 254 18.514 31.035 36.808 1.00 22.01 C ANISOU 1615 CA ASP A 254 1533 3356 3471 224 620 -725 C ATOM 1616 C ASP A 254 17.755 29.749 36.481 1.00 21.57 C ANISOU 1616 C ASP A 254 1498 3546 3152 135 570 -732 C ATOM 1617 O ASP A 254 18.360 28.729 36.163 1.00 22.94 O ANISOU 1617 O ASP A 254 1359 3554 3801 174 529 -697 O ATOM 1618 CB ASP A 254 18.250 32.110 35.763 1.00 22.80 C ANISOU 1618 CB ASP A 254 1491 3412 3760 264 599 -532 C ATOM 1619 CG ASP A 254 16.953 32.890 35.948 1.00 24.49 C ANISOU 1619 CG ASP A 254 1729 3276 4298 400 488 -345 C ATOM 1620 OD1 ASP A 254 16.171 32.595 36.895 1.00 26.82 O ANISOU 1620 OD1 ASP A 254 1900 3624 4666 419 813 -364 O ATOM 1621 OD2 ASP A 254 16.702 33.792 35.134 1.00 28.47 O ANISOU 1621 OD2 ASP A 254 2406 3538 4871 950 89 -149 O ATOM 1622 N SER A 255 16.434 29.848 36.498 1.00 22.62 N ANISOU 1622 N SER A 255 1460 3671 3462 76 697 -640 N ATOM 1623 CA SER A 255 15.572 28.770 36.069 1.00 22.62 C ANISOU 1623 CA SER A 255 1549 3668 3377 28 458 -372 C ATOM 1624 C SER A 255 15.572 28.706 34.533 1.00 22.13 C ANISOU 1624 C SER A 255 1226 3671 3510 -95 592 -221 C ATOM 1625 O SER A 255 16.203 29.521 33.853 1.00 21.50 O ANISOU 1625 O SER A 255 1585 3206 3375 -108 434 -202 O ATOM 1626 CB SER A 255 14.191 28.992 36.571 1.00 23.69 C ANISOU 1626 CB SER A 255 1608 3788 3603 199 543 -218 C ATOM 1627 OG SER A 255 13.592 30.004 35.789 1.00 24.85 O ANISOU 1627 OG SER A 255 1762 3911 3766 24 265 3 O ATOM 1628 N ARG A 256 14.803 27.780 33.980 1.00 22.95 N ANISOU 1628 N ARG A 256 1469 3719 3532 -200 469 -110 N ATOM 1629 CA ARG A 256 14.669 27.655 32.538 1.00 22.21 C ANISOU 1629 CA ARG A 256 1140 3681 3617 39 295 -17 C ATOM 1630 C ARG A 256 13.981 28.863 31.905 1.00 23.59 C ANISOU 1630 C ARG A 256 1837 3382 3744 37 327 -81 C ATOM 1631 O ARG A 256 14.004 29.004 30.672 1.00 22.00 O ANISOU 1631 O ARG A 256 1336 3345 3676 -109 64 11 O ATOM 1632 CB ARG A 256 13.934 26.374 32.160 1.00 23.56 C ANISOU 1632 CB ARG A 256 1663 3607 3679 39 176 -15 C ATOM 1633 CG ARG A 256 14.657 25.098 32.553 1.00 23.30 C ANISOU 1633 CG ARG A 256 1489 3599 3763 54 358 -49 C ATOM 1634 CD ARG A 256 13.914 23.878 32.065 1.00 24.10 C ANISOU 1634 CD ARG A 256 1695 3530 3931 -108 296 61 C ATOM 1635 NE ARG A 256 13.922 23.764 30.610 1.00 23.76 N ANISOU 1635 NE ARG A 256 1549 3519 3959 -338 143 11 N ATOM 1636 CZ ARG A 256 14.904 23.193 29.903 1.00 24.09 C ANISOU 1636 CZ ARG A 256 1858 3462 3833 -53 -77 -311 C ATOM 1637 NH1 ARG A 256 15.991 22.743 30.510 1.00 23.95 N ANISOU 1637 NH1 ARG A 256 1593 3462 4042 -17 42 -292 N ATOM 1638 NH2 ARG A 256 14.817 23.109 28.582 1.00 25.64 N ANISOU 1638 NH2 ARG A 256 2063 3754 3925 -326 63 -292 N ATOM 1639 N ALA A 257 13.373 29.737 32.699 1.00 22.89 N ANISOU 1639 N ALA A 257 1289 3445 3963 176 413 27 N ATOM 1640 CA ALA A 257 12.878 31.006 32.185 1.00 23.65 C ANISOU 1640 CA ALA A 257 1544 3460 3980 166 270 138 C ATOM 1641 C ALA A 257 13.987 31.835 31.539 1.00 22.44 C ANISOU 1641 C ALA A 257 1519 3196 3808 270 194 188 C ATOM 1642 O ALA A 257 13.693 32.668 30.685 1.00 23.12 O ANISOU 1642 O ALA A 257 1576 3194 4012 191 51 301 O ATOM 1643 CB ALA A 257 12.155 31.789 33.270 1.00 25.23 C ANISOU 1643 CB ALA A 257 1508 3768 4307 359 543 136 C ATOM 1644 N ALA A 258 15.248 31.611 31.897 1.00 21.53 N ANISOU 1644 N ALA A 258 1449 3165 3564 96 225 197 N ATOM 1645 CA ALA A 258 16.329 32.259 31.170 1.00 21.53 C ANISOU 1645 CA ALA A 258 1552 3181 3446 -68 233 -3 C ATOM 1646 C ALA A 258 16.288 31.864 29.679 1.00 20.99 C ANISOU 1646 C ALA A 258 1385 3159 3429 -3 81 129 C ATOM 1647 O ALA A 258 16.529 32.700 28.788 1.00 21.35 O ANISOU 1647 O ALA A 258 1185 3389 3536 307 48 326 O ATOM 1648 CB ALA A 258 17.656 31.889 31.792 1.00 21.75 C ANISOU 1648 CB ALA A 258 1619 3188 3456 6 189 -202 C ATOM 1649 N ILE A 259 16.010 30.597 29.392 1.00 21.31 N ANISOU 1649 N ILE A 259 1564 3146 3388 -107 71 209 N ATOM 1650 CA ILE A 259 16.007 30.106 28.006 1.00 21.10 C ANISOU 1650 CA ILE A 259 1537 3195 3286 27 -189 345 C ATOM 1651 C ILE A 259 14.795 30.692 27.290 1.00 21.73 C ANISOU 1651 C ILE A 259 1528 3008 3719 30 -129 586 C ATOM 1652 O ILE A 259 14.958 31.260 26.186 1.00 22.82 O ANISOU 1652 O ILE A 259 2022 3074 3572 94 -350 577 O ATOM 1653 CB ILE A 259 15.978 28.567 27.932 1.00 21.57 C ANISOU 1653 CB ILE A 259 1734 3246 3216 -4 -188 221 C ATOM 1654 CG1 ILE A 259 17.158 27.937 28.670 1.00 20.56 C ANISOU 1654 CG1 ILE A 259 1512 3011 3289 55 -19 169 C ATOM 1655 CG2 ILE A 259 15.964 28.112 26.482 1.00 23.62 C ANISOU 1655 CG2 ILE A 259 2056 3651 3266 178 -212 189 C ATOM 1656 CD1 ILE A 259 17.009 26.467 28.985 1.00 21.62 C ANISOU 1656 CD1 ILE A 259 2048 2894 3271 185 108 -117 C ATOM 1657 N THR A 260 13.597 30.585 27.870 1.00 23.00 N ANISOU 1657 N THR A 260 1559 3172 4006 -151 -44 566 N ATOM 1658 CA THR A 260 12.412 31.105 27.195 1.00 24.00 C ANISOU 1658 CA THR A 260 1772 3140 4208 -97 -155 598 C ATOM 1659 C THR A 260 12.544 32.622 26.990 1.00 23.89 C ANISOU 1659 C THR A 260 1509 3143 4423 -68 -95 654 C ATOM 1660 O THR A 260 12.141 33.132 25.950 1.00 26.06 O ANISOU 1660 O THR A 260 1937 3404 4558 -138 -154 789 O ATOM 1661 CB THR A 260 11.135 30.744 27.955 1.00 25.01 C ANISOU 1661 CB THR A 260 1616 3503 4382 -38 -159 498 C ATOM 1662 OG1 THR A 260 11.249 31.149 29.322 1.00 25.76 O ANISOU 1662 OG1 THR A 260 1555 3837 4394 -185 26 344 O ATOM 1663 CG2 THR A 260 10.832 29.262 27.909 1.00 26.45 C ANISOU 1663 CG2 THR A 260 2123 3531 4396 -151 -106 471 C ATOM 1664 N HIS A 261 13.019 33.340 28.001 1.00 23.58 N ANISOU 1664 N HIS A 261 1432 3112 4413 -34 29 604 N ATOM 1665 CA HIS A 261 13.096 34.782 27.900 1.00 24.10 C ANISOU 1665 CA HIS A 261 1644 3072 4439 16 -98 661 C ATOM 1666 C HIS A 261 14.117 35.176 26.843 1.00 23.43 C ANISOU 1666 C HIS A 261 1547 3029 4326 162 -162 762 C ATOM 1667 O HIS A 261 13.923 36.123 26.102 1.00 25.21 O ANISOU 1667 O HIS A 261 2002 2965 4610 179 -65 885 O ATOM 1668 CB HIS A 261 13.476 35.434 29.234 1.00 24.28 C ANISOU 1668 CB HIS A 261 1746 3057 4421 170 96 476 C ATOM 1669 CG HIS A 261 13.635 36.915 29.137 1.00 26.40 C ANISOU 1669 CG HIS A 261 2077 3046 4908 252 -139 556 C ATOM 1670 ND1 HIS A 261 12.632 37.777 28.703 1.00 28.34 N ANISOU 1670 ND1 HIS A 261 2149 3112 5506 415 -93 502 N ATOM 1671 CD2 HIS A 261 14.673 37.699 29.456 1.00 26.87 C ANISOU 1671 CD2 HIS A 261 2111 3149 4949 130 141 408 C ATOM 1672 CE1 HIS A 261 13.086 39.014 28.723 1.00 29.46 C ANISOU 1672 CE1 HIS A 261 2402 2951 5837 608 -160 365 C ATOM 1673 NE2 HIS A 261 14.323 38.992 29.209 1.00 29.82 N ANISOU 1673 NE2 HIS A 261 2540 3248 5539 408 -231 299 N ATOM 1674 N THR A 262 15.267 34.493 26.825 1.00 22.84 N ANISOU 1674 N THR A 262 1289 3130 4259 -18 26 657 N ATOM 1675 CA THR A 262 16.274 34.776 25.846 1.00 23.27 C ANISOU 1675 CA THR A 262 1416 3160 4264 -137 14 788 C ATOM 1676 C THR A 262 15.748 34.526 24.426 1.00 22.97 C ANISOU 1676 C THR A 262 1369 3035 4322 48 -143 927 C ATOM 1677 O THR A 262 15.981 35.326 23.522 1.00 25.12 O ANISOU 1677 O THR A 262 1933 3308 4302 235 -15 988 O ATOM 1678 CB THR A 262 17.523 33.926 26.092 1.00 21.88 C ANISOU 1678 CB THR A 262 1318 3106 3890 -217 14 651 C ATOM 1679 OG1 THR A 262 18.233 34.303 27.270 1.00 21.24 O ANISOU 1679 OG1 THR A 262 1490 2923 3656 17 134 454 O ATOM 1680 CG2 THR A 262 18.496 34.075 24.961 1.00 23.22 C ANISOU 1680 CG2 THR A 262 1566 3339 3915 -202 41 930 C ATOM 1681 N ALA A 263 15.082 33.401 24.225 1.00 23.66 N ANISOU 1681 N ALA A 263 1710 3119 4161 -63 -149 779 N ATOM 1682 CA ALA A 263 14.524 33.071 22.913 1.00 24.43 C ANISOU 1682 CA ALA A 263 1664 3349 4267 43 -260 815 C ATOM 1683 C ALA A 263 13.495 34.126 22.517 1.00 26.16 C ANISOU 1683 C ALA A 263 1631 3643 4665 153 -270 972 C ATOM 1684 O ALA A 263 13.447 34.567 21.383 1.00 28.48 O ANISOU 1684 O ALA A 263 1934 4093 4793 377 -259 1281 O ATOM 1685 CB ALA A 263 13.953 31.678 22.942 1.00 24.78 C ANISOU 1685 CB ALA A 263 1704 3380 4329 30 -233 734 C ATOM 1686 N ARG A 264 12.645 34.539 23.463 1.00 27.40 N ANISOU 1686 N ARG A 264 1563 3738 5107 74 -51 859 N ATOM 1687 CA ARG A 264 11.591 35.477 23.138 1.00 28.39 C ANISOU 1687 CA ARG A 264 1701 3797 5288 77 -164 972 C ATOM 1688 C ARG A 264 12.177 36.837 22.737 1.00 28.44 C ANISOU 1688 C ARG A 264 1777 3623 5405 438 -134 1298 C ATOM 1689 O ARG A 264 11.704 37.453 21.798 1.00 31.64 O ANISOU 1689 O ARG A 264 2226 4193 5599 238 -232 1554 O ATOM 1690 CB ARG A 264 10.602 35.580 24.308 1.00 28.81 C ANISOU 1690 CB ARG A 264 1777 3697 5470 93 -3 814 C ATOM 1691 CG ARG A 264 9.278 36.236 23.960 1.00 30.17 C ANISOU 1691 CG ARG A 264 1838 3809 5816 118 -51 807 C ATOM 1692 CD ARG A 264 8.426 35.302 23.121 1.00 31.15 C ANISOU 1692 CD ARG A 264 2130 3920 5783 -7 -204 843 C ATOM 1693 NE ARG A 264 7.179 35.937 22.728 1.00 32.22 N ANISOU 1693 NE ARG A 264 2343 3883 6015 114 -352 983 N ATOM 1694 CZ ARG A 264 6.763 36.146 21.476 1.00 33.55 C ANISOU 1694 CZ ARG A 264 2506 4137 6104 89 -525 1070 C ATOM 1695 NH1 ARG A 264 7.516 35.772 20.452 1.00 34.49 N ANISOU 1695 NH1 ARG A 264 3049 4244 5809 140 -592 952 N ATOM 1696 NH2 ARG A 264 5.597 36.735 21.259 1.00 35.41 N ANISOU 1696 NH2 ARG A 264 2683 4373 6396 242 -642 1109 N ATOM 1697 N MET A 265 13.243 37.266 23.404 1.00 28.69 N ANISOU 1697 N MET A 265 1929 3555 5416 119 38 1212 N ATOM 1698 CA MET A 265 13.932 38.497 22.973 1.00 29.62 C ANISOU 1698 CA MET A 265 2072 3412 5769 222 238 1316 C ATOM 1699 C MET A 265 14.580 38.288 21.604 1.00 30.20 C ANISOU 1699 C MET A 265 1907 3901 5666 373 27 1708 C ATOM 1700 O MET A 265 14.580 39.203 20.761 1.00 32.92 O ANISOU 1700 O MET A 265 2410 3920 6177 250 187 1913 O ATOM 1701 CB MET A 265 15.006 38.946 23.967 1.00 28.91 C ANISOU 1701 CB MET A 265 2276 3241 5465 264 491 889 C ATOM 1702 CG MET A 265 14.421 39.539 25.227 1.00 29.76 C ANISOU 1702 CG MET A 265 2344 3382 5578 81 560 605 C ATOM 1703 SD MET A 265 15.584 40.408 26.294 0.54 29.77 S ANISOU 1703 SD MET A 265 3057 2892 5359 -119 566 561 S ATOM 1704 CE MET A 265 16.876 40.871 25.158 1.00 32.63 C ANISOU 1704 CE MET A 265 3323 3505 5570 471 876 1028 C ATOM 1705 N ALA A 266 15.136 37.115 21.372 1.00 26.14 N ANISOU 1705 N ALA A 266 3428 3380 3122 877 718 1158 N ATOM 1706 CA ALA A 266 15.765 36.868 20.073 1.00 27.27 C ANISOU 1706 CA ALA A 266 3383 4041 2936 984 533 1392 C ATOM 1707 C ALA A 266 14.728 36.823 18.938 1.00 29.45 C ANISOU 1707 C ALA A 266 3397 4336 3454 732 258 1619 C ATOM 1708 O ALA A 266 15.070 37.103 17.811 1.00 31.51 O ANISOU 1708 O ALA A 266 3474 4886 3612 873 103 2115 O ATOM 1709 CB ALA A 266 16.545 35.585 20.146 1.00 28.06 C ANISOU 1709 CB ALA A 266 3332 4158 3169 1076 414 1100 C ATOM 1710 N ASP A 267 13.482 36.456 19.225 1.00 29.33 N ANISOU 1710 N ASP A 267 3404 4430 3308 633 99 1707 N ATOM 1711 CA ASP A 267 12.422 36.423 18.217 1.00 33.51 C ANISOU 1711 CA ASP A 267 3599 5611 3521 501 -93 2034 C ATOM 1712 C ASP A 267 12.299 37.800 17.562 1.00 38.01 C ANISOU 1712 C ASP A 267 3706 5995 4738 591 90 2577 C ATOM 1713 O ASP A 267 11.963 37.886 16.391 1.00 41.69 O ANISOU 1713 O ASP A 267 4101 6780 4956 456 -142 3293 O ATOM 1714 CB ASP A 267 11.069 36.060 18.834 1.00 33.09 C ANISOU 1714 CB ASP A 267 3515 5486 3571 658 -77 1920 C ATOM 1715 CG ASP A 267 10.867 34.588 19.119 1.00 31.98 C ANISOU 1715 CG ASP A 267 3600 5350 3201 680 -300 1482 C ATOM 1716 OD1 ASP A 267 11.504 33.764 18.442 1.00 34.13 O ANISOU 1716 OD1 ASP A 267 4056 5461 3451 361 -207 1172 O ATOM 1717 OD2 ASP A 267 10.049 34.275 20.023 1.00 32.35 O ANISOU 1717 OD2 ASP A 267 3540 5282 3470 1001 -300 1220 O ATOM 1718 N LYS A 268 12.568 38.867 18.319 1.00 37.62 N ANISOU 1718 N LYS A 268 3535 5533 5227 1000 506 2579 N ATOM 1719 CA LYS A 268 12.416 40.250 17.808 1.00 42.47 C ANISOU 1719 CA LYS A 268 3846 5973 6318 1130 716 3248 C ATOM 1720 C LYS A 268 13.575 40.633 16.872 1.00 44.43 C ANISOU 1720 C LYS A 268 4133 6193 6553 962 770 3434 C ATOM 1721 O LYS A 268 13.470 41.660 16.192 1.00 50.81 O ANISOU 1721 O LYS A 268 5091 6127 8087 723 1481 3733 O ATOM 1722 CB LYS A 268 12.303 41.243 18.972 1.00 47.92 C ANISOU 1722 CB LYS A 268 4604 6271 7331 1176 824 2611 C ATOM 1723 CG LYS A 268 10.888 41.425 19.507 1.00 52.45 C ANISOU 1723 CG LYS A 268 4626 7099 8203 1058 1057 2649 C ATOM 1724 CD LYS A 268 10.776 41.523 21.017 1.00 53.50 C ANISOU 1724 CD LYS A 268 5343 6750 8235 881 1087 2319 C ATOM 1725 CE LYS A 268 9.385 41.192 21.522 1.00 54.94 C ANISOU 1725 CE LYS A 268 5172 7082 8619 1269 1156 2441 C ATOM 1726 NZ LYS A 268 9.233 39.750 21.845 1.00 52.60 N ANISOU 1726 NZ LYS A 268 5248 7223 7512 641 338 2299 N ATOM 1727 N LEU A 269 14.658 39.851 16.818 1.00 41.16 N ANISOU 1727 N LEU A 269 4064 5699 5875 854 812 3144 N ATOM 1728 CA LEU A 269 15.810 40.170 15.906 1.00 42.81 C ANISOU 1728 CA LEU A 269 4256 6194 5815 1000 933 3333 C ATOM 1729 C LEU A 269 15.509 39.726 14.468 1.00 46.49 C ANISOU 1729 C LEU A 269 5000 7055 5610 607 866 3785 C ATOM 1730 O LEU A 269 16.220 40.136 13.533 1.00 47.78 O ANISOU 1730 O LEU A 269 5339 7366 5448 603 907 3917 O ATOM 1731 CB LEU A 269 17.080 39.453 16.380 1.00 41.36 C ANISOU 1731 CB LEU A 269 3974 6204 5533 956 1020 2680 C ATOM 1732 CG LEU A 269 17.774 40.007 17.624 1.00 41.26 C ANISOU 1732 CG LEU A 269 3760 6169 5746 1206 926 2390 C ATOM 1733 CD1 LEU A 269 18.722 38.968 18.207 1.00 41.62 C ANISOU 1733 CD1 LEU A 269 3821 6082 5911 1410 901 2049 C ATOM 1734 CD2 LEU A 269 18.528 41.290 17.298 1.00 45.33 C ANISOU 1734 CD2 LEU A 269 4647 6410 6166 826 1205 2418 C ATOM 1735 N ARG A 270 14.514 38.857 14.289 1.00 49.63 N ANISOU 1735 N ARG A 270 4929 7600 6326 414 -208 3548 N ATOM 1736 CA ARG A 270 14.248 38.251 12.981 1.00 56.36 C ANISOU 1736 CA ARG A 270 5899 8935 6577 273 -645 3231 C ATOM 1737 C ARG A 270 13.414 39.218 12.130 1.00 62.42 C ANISOU 1737 C ARG A 270 6066 10028 7621 602 -1149 3647 C ATOM 1738 O ARG A 270 12.438 39.790 12.607 1.00 66.69 O ANISOU 1738 O ARG A 270 6197 10347 8795 1227 -1376 3597 O ATOM 1739 CB ARG A 270 13.544 36.901 13.157 1.00 57.44 C ANISOU 1739 CB ARG A 270 6202 8944 6676 90 -1234 3043 C ATOM 1740 CG ARG A 270 14.391 35.854 13.866 1.00 55.59 C ANISOU 1740 CG ARG A 270 5701 8575 6842 353 -1216 2327 C ATOM 1741 CD ARG A 270 13.848 34.440 13.752 1.00 58.05 C ANISOU 1741 CD ARG A 270 6157 8863 7037 -13 -1156 1975 C ATOM 1742 NE ARG A 270 12.691 34.202 14.611 1.00 57.40 N ANISOU 1742 NE ARG A 270 5822 9102 6883 3 -1483 2091 N ATOM 1743 CZ ARG A 270 12.432 33.060 15.252 1.00 56.05 C ANISOU 1743 CZ ARG A 270 5506 8669 7121 -119 -1407 1650 C ATOM 1744 NH1 ARG A 270 13.302 32.060 15.242 1.00 56.81 N ANISOU 1744 NH1 ARG A 270 6747 9308 5527 -56 -2262 1104 N ATOM 1745 NH2 ARG A 270 11.298 32.928 15.915 1.00 51.81 N ANISOU 1745 NH2 ARG A 270 5503 8364 5818 -314 -2253 1875 N TER 1746 ARG A 270 HETATM 1747 ZN ZN A 301 30.720 36.819 27.177 1.00 16.13 ZN ANISOU 1747 ZN ZN A 301 1981 2159 1987 444 -21 -342 ZN HETATM 1748 ZN ZN A 302 31.113 36.450 23.521 1.00 16.59 ZN ANISOU 1748 ZN ZN A 302 2471 1987 1842 568 -140 -207 ZN HETATM 1749 O2 MCO A 303 27.333 42.896 25.250 1.00 39.47 O ANISOU 1749 O2 MCO A 303 4995 3395 6607 1868 -1956 -747 O HETATM 1750 C9 MCO A 303 28.083 42.021 25.715 1.00 34.42 C ANISOU 1750 C9 MCO A 303 4239 3194 5643 1449 -1622 -815 C HETATM 1751 O3 MCO A 303 27.975 40.791 25.492 1.00 37.62 O ANISOU 1751 O3 MCO A 303 4158 3239 6897 1376 -1625 -908 O HETATM 1752 C8 MCO A 303 29.113 42.354 26.678 1.00 28.06 C ANISOU 1752 C8 MCO A 303 3146 2874 4641 810 -518 -734 C HETATM 1753 C7 MCO A 303 28.888 43.022 27.961 1.00 30.01 C ANISOU 1753 C7 MCO A 303 3455 3115 4832 1077 -108 -929 C HETATM 1754 C6 MCO A 303 29.040 41.778 28.815 1.00 27.22 C ANISOU 1754 C6 MCO A 303 2799 3855 3685 557 237 -835 C HETATM 1755 C5 MCO A 303 30.219 41.026 28.199 1.00 24.71 C ANISOU 1755 C5 MCO A 303 3081 3332 2974 648 1 -856 C HETATM 1756 N MCO A 303 30.246 41.476 26.801 1.00 23.40 N ANISOU 1756 N MCO A 303 3307 2407 3176 861 -294 -768 N HETATM 1757 C4 MCO A 303 31.078 41.150 25.789 1.00 22.48 C ANISOU 1757 C4 MCO A 303 3785 2166 2587 819 -187 -273 C HETATM 1758 O1 MCO A 303 30.922 41.570 24.646 1.00 26.42 O ANISOU 1758 O1 MCO A 303 4992 2259 2787 1175 -635 -212 O HETATM 1759 C2 MCO A 303 32.263 40.286 25.897 1.00 20.33 C ANISOU 1759 C2 MCO A 303 3182 2372 2171 495 -12 -614 C HETATM 1760 C3 MCO A 303 33.585 40.902 26.091 1.00 22.06 C ANISOU 1760 C3 MCO A 303 3282 2501 2598 363 -269 -294 C HETATM 1761 C1 MCO A 303 32.270 38.967 25.178 1.00 18.17 C ANISOU 1761 C1 MCO A 303 2973 2304 1624 734 -85 -396 C HETATM 1762 S MCO A 303 30.777 38.026 25.196 1.00 17.34 S ANISOU 1762 S MCO A 303 2576 2031 1979 627 -109 -266 S HETATM 1763 O HOH A 401 30.533 37.879 41.969 1.00 44.97 O ANISOU 1763 O HOH A 401 3754 7877 5455 102 841 -1360 O HETATM 1764 O HOH A 402 31.018 35.534 51.186 1.00 39.15 O ANISOU 1764 O HOH A 402 5940 6053 2880 -364 -396 -1883 O HETATM 1765 O HOH A 403 48.169 28.669 39.450 1.00 29.57 O ANISOU 1765 O HOH A 403 2783 4537 3915 192 -296 44 O HETATM 1766 O HOH A 404 8.895 32.265 16.282 1.00 51.66 O ANISOU 1766 O HOH A 404 4885 10037 4703 654 -655 -992 O HETATM 1767 O HOH A 405 25.983 39.461 27.381 1.00 41.37 O ANISOU 1767 O HOH A 405 3707 3738 8273 488 1 -2040 O HETATM 1768 O HOH A 406 8.205 32.624 19.401 1.00 39.47 O ANISOU 1768 O HOH A 406 2672 4385 7938 277 -823 268 O HETATM 1769 O HOH A 407 30.062 28.672 47.576 1.00 33.86 O ANISOU 1769 O HOH A 407 6729 4215 1921 -817 1159 -753 O HETATM 1770 O HOH A 408 32.960 9.758 35.521 1.00 35.51 O ANISOU 1770 O HOH A 408 7235 3595 2660 638 -403 23 O HETATM 1771 O HOH A 409 26.263 39.478 24.097 1.00 30.69 O ANISOU 1771 O HOH A 409 4041 3852 3765 1100 -537 -240 O HETATM 1772 O HOH A 410 23.383 37.402 30.837 1.00 31.38 O ANISOU 1772 O HOH A 410 3427 4383 4113 76 -399 162 O HETATM 1773 O HOH A 411 28.532 46.407 34.002 1.00 34.02 O ANISOU 1773 O HOH A 411 5092 4341 3493 -17 -1043 -591 O HETATM 1774 O HOH A 412 27.388 45.423 25.871 1.00 41.99 O ANISOU 1774 O HOH A 412 5132 4111 6708 478 467 189 O HETATM 1775 O HOH A 413 15.843 31.668 14.830 1.00 30.49 O ANISOU 1775 O HOH A 413 2524 5920 3137 350 -636 732 O HETATM 1776 O HOH A 414 19.322 40.622 34.452 1.00 46.52 O ANISOU 1776 O HOH A 414 5880 4988 6807 404 -594 -260 O HETATM 1777 O HOH A 415 42.643 14.999 23.006 1.00 29.52 O ANISOU 1777 O HOH A 415 4275 2520 4418 401 2022 -460 O HETATM 1778 O HOH A 416 13.555 32.521 36.924 1.00 40.82 O ANISOU 1778 O HOH A 416 2752 5599 7159 498 1484 -1387 O HETATM 1779 O HOH A 417 46.936 18.500 25.207 1.00 35.71 O ANISOU 1779 O HOH A 417 4235 5050 4280 640 1954 80 O HETATM 1780 O HOH A 418 49.869 28.623 24.658 1.00 21.43 O ANISOU 1780 O HOH A 418 2155 2745 3239 -189 631 334 O HETATM 1781 O HOH A 419 21.386 44.348 21.893 1.00 42.28 O ANISOU 1781 O HOH A 419 4641 4499 6922 962 -1420 990 O HETATM 1782 O HOH A 420 29.326 45.406 36.360 1.00 25.08 O ANISOU 1782 O HOH A 420 3838 3109 2578 -118 -318 -656 O HETATM 1783 O HOH A 421 10.132 33.407 30.064 1.00 34.56 O ANISOU 1783 O HOH A 421 3619 3996 5516 291 -322 -983 O HETATM 1784 O HOH A 422 35.183 40.311 17.503 1.00 24.25 O ANISOU 1784 O HOH A 422 4304 2440 2467 418 -13 133 O HETATM 1785 O HOH A 423 48.120 35.072 26.634 1.00 25.75 O ANISOU 1785 O HOH A 423 2854 3321 3608 -710 745 130 O HETATM 1786 O HOH A 424 34.265 51.499 32.953 1.00 37.48 O ANISOU 1786 O HOH A 424 6129 4727 3385 546 1874 460 O HETATM 1787 O HOH A 425 48.300 26.371 41.915 1.00 39.33 O ANISOU 1787 O HOH A 425 3002 5381 6558 -672 -416 102 O HETATM 1788 O HOH A 426 24.500 42.201 14.521 1.00 48.68 O ANISOU 1788 O HOH A 426 7558 4607 6329 1694 -2482 -634 O HETATM 1789 O HOH A 427 47.457 20.205 19.392 1.00 47.82 O ANISOU 1789 O HOH A 427 3802 8505 5861 1443 1434 -1702 O HETATM 1790 O HOH A 428 39.707 17.031 19.848 1.00 24.50 O ANISOU 1790 O HOH A 428 3801 3049 2459 -389 1016 -271 O HETATM 1791 O HOH A 429 31.299 13.015 28.004 1.00 37.75 O ANISOU 1791 O HOH A 429 5849 4365 4127 -625 -645 480 O HETATM 1792 O HOH A 430 30.651 32.560 41.061 1.00 16.89 O ANISOU 1792 O HOH A 430 2060 2579 1776 -247 575 -387 O HETATM 1793 O HOH A 431 37.361 52.626 32.157 1.00 41.92 O ANISOU 1793 O HOH A 431 6344 3581 6000 -392 1086 376 O HETATM 1794 O HOH A 432 46.490 18.090 33.455 1.00 28.34 O ANISOU 1794 O HOH A 432 2699 4094 3975 867 1121 1018 O HETATM 1795 O HOH A 433 20.708 16.003 27.479 1.00 42.28 O ANISOU 1795 O HOH A 433 4073 3882 8109 -325 1224 -883 O HETATM 1796 O HOH A 434 28.023 35.478 13.359 1.00 44.02 O ANISOU 1796 O HOH A 434 5768 5443 5513 1272 -2242 19 O HETATM 1797 O HOH A 435 22.608 40.905 27.457 1.00 45.91 O ANISOU 1797 O HOH A 435 4802 5391 7251 1788 -1648 284 O HETATM 1798 O HOH A 436 18.071 39.681 11.639 1.00 53.95 O ANISOU 1798 O HOH A 436 7546 5966 6984 877 -3317 1049 O HETATM 1799 O HOH A 437 40.959 40.562 38.366 1.00 24.53 O ANISOU 1799 O HOH A 437 2975 4031 2313 -53 468 -1003 O HETATM 1800 O HOH A 438 43.069 21.747 16.812 1.00 36.52 O ANISOU 1800 O HOH A 438 4817 4917 4140 179 1069 204 O HETATM 1801 O HOH A 439 34.456 33.266 32.072 1.00 13.53 O ANISOU 1801 O HOH A 439 1589 2064 1487 80 430 -305 O HETATM 1802 O HOH A 440 44.231 28.839 14.850 1.00 30.14 O ANISOU 1802 O HOH A 440 3529 3583 4339 21 1425 -1146 O HETATM 1803 O HOH A 441 35.566 23.929 48.846 1.00 54.84 O ANISOU 1803 O HOH A 441 8154 9198 3483 371 485 -1164 O HETATM 1804 O HOH A 442 49.392 20.392 43.209 1.00 43.83 O ANISOU 1804 O HOH A 442 3221 6364 7069 -322 343 1136 O HETATM 1805 O HOH A 443 45.647 17.635 30.844 1.00 26.19 O ANISOU 1805 O HOH A 443 3089 3265 3595 499 654 1046 O HETATM 1806 O HOH A 444 32.824 23.181 14.083 1.00 39.06 O ANISOU 1806 O HOH A 444 7313 5029 2498 -1438 -452 -1022 O HETATM 1807 O HOH A 445 47.538 26.939 21.012 1.00 26.17 O ANISOU 1807 O HOH A 445 2450 4322 3170 292 1155 79 O HETATM 1808 O HOH A 446 43.851 16.932 18.624 1.00 33.53 O ANISOU 1808 O HOH A 446 5028 4658 3052 1448 470 -1146 O HETATM 1809 O HOH A 447 20.173 15.552 38.771 1.00 56.98 O ANISOU 1809 O HOH A 447 6381 6938 8328 -1914 2870 781 O HETATM 1810 O HOH A 448 10.173 37.163 27.734 1.00 32.81 O ANISOU 1810 O HOH A 448 2801 4061 5604 700 -425 -547 O HETATM 1811 O HOH A 449 29.114 40.273 40.178 1.00 37.82 O ANISOU 1811 O HOH A 449 3447 6264 4657 -1429 1701 -2489 O HETATM 1812 O HOH A 450 35.525 49.450 36.006 1.00 27.64 O ANISOU 1812 O HOH A 450 4091 3310 3098 546 965 -283 O HETATM 1813 O HOH A 451 19.882 25.442 15.609 1.00 44.45 O ANISOU 1813 O HOH A 451 4813 7707 4370 430 -2369 -1395 O HETATM 1814 O HOH A 452 42.215 12.155 26.455 1.00 26.01 O ANISOU 1814 O HOH A 452 3966 2855 3059 72 143 79 O HETATM 1815 O HOH A 453 27.599 29.614 24.352 1.00 16.89 O ANISOU 1815 O HOH A 453 2020 2380 2016 373 -267 -370 O HETATM 1816 O HOH A 454 15.381 25.377 17.727 1.00 30.01 O ANISOU 1816 O HOH A 454 2876 5210 3315 -334 -911 -577 O HETATM 1817 O HOH A 455 28.216 14.916 37.915 1.00 36.88 O ANISOU 1817 O HOH A 455 4923 5215 3874 287 193 216 O HETATM 1818 O HOH A 456 25.014 44.955 19.178 1.00 39.30 O ANISOU 1818 O HOH A 456 4923 4826 5183 420 345 -73 O HETATM 1819 O HOH A 457 30.085 13.855 45.420 1.00 26.62 O ANISOU 1819 O HOH A 457 3217 3720 3176 -198 991 839 O HETATM 1820 O HOH A 458 25.150 31.741 35.779 1.00 17.06 O ANISOU 1820 O HOH A 458 1464 2564 2452 185 506 -644 O HETATM 1821 O HOH A 459 38.199 32.355 49.772 1.00 42.03 O ANISOU 1821 O HOH A 459 6350 4770 4848 760 1467 1635 O HETATM 1822 O HOH A 460 40.810 14.511 27.163 1.00 20.99 O ANISOU 1822 O HOH A 460 2957 2601 2416 83 538 431 O HETATM 1823 O HOH A 461 44.592 21.094 41.864 1.00 22.01 O ANISOU 1823 O HOH A 461 2472 3332 2558 -11 0 694 O HETATM 1824 O HOH A 462 44.400 24.197 17.636 1.00 36.93 O ANISOU 1824 O HOH A 462 6234 5520 2278 92 1397 -278 O HETATM 1825 O HOH A 463 40.363 42.173 45.003 1.00 19.62 O ANISOU 1825 O HOH A 463 2778 2598 2078 -216 242 -190 O HETATM 1826 O HOH A 464 22.459 21.724 42.291 1.00 37.84 O ANISOU 1826 O HOH A 464 2959 4437 6979 -921 784 -622 O HETATM 1827 O HOH A 465 26.220 21.101 14.055 1.00 36.59 O ANISOU 1827 O HOH A 465 7014 3198 3690 27 -1506 -678 O HETATM 1828 O HOH A 466 43.575 11.860 41.267 1.00 31.75 O ANISOU 1828 O HOH A 466 3355 4269 4438 1024 448 1338 O HETATM 1829 O HOH A 467 37.480 39.940 49.818 1.00 31.30 O ANISOU 1829 O HOH A 467 4534 3651 3706 -662 271 -951 O HETATM 1830 O HOH A 468 21.352 32.317 41.204 1.00 33.30 O ANISOU 1830 O HOH A 468 3720 5510 3420 379 370 -895 O HETATM 1831 O HOH A 469 34.364 26.591 21.469 1.00 13.72 O ANISOU 1831 O HOH A 469 2088 1836 1289 250 194 -97 O HETATM 1832 O HOH A 470 53.710 24.007 35.008 1.00 47.97 O ANISOU 1832 O HOH A 470 5032 7973 5219 -2843 -1323 2731 O HETATM 1833 O HOH A 471 11.706 42.355 13.248 1.00 57.89 O ANISOU 1833 O HOH A 471 5887 7143 8964 1709 -2273 1709 O HETATM 1834 O HOH A 472 20.074 35.445 37.158 1.00 32.50 O ANISOU 1834 O HOH A 472 3571 4452 4324 1760 -412 -1055 O HETATM 1835 O HOH A 473 13.855 18.278 23.996 1.00 43.71 O ANISOU 1835 O HOH A 473 3031 5158 8418 -1262 -1115 -137 O HETATM 1836 O HOH A 474 29.772 30.981 25.341 1.00 15.78 O ANISOU 1836 O HOH A 474 2040 2021 1932 305 -19 -289 O HETATM 1837 O HOH A 475 26.453 28.030 47.246 1.00 45.58 O ANISOU 1837 O HOH A 475 6773 5811 4733 418 2131 -2200 O HETATM 1838 O HOH A 476 39.277 10.009 20.739 1.00 21.18 O ANISOU 1838 O HOH A 476 3756 2345 1945 313 744 -51 O HETATM 1839 O HOH A 477 41.809 33.869 13.008 1.00 21.24 O ANISOU 1839 O HOH A 477 4224 2206 1637 -88 1038 -92 O HETATM 1840 O HOH A 478 44.499 36.409 24.465 1.00 22.55 O ANISOU 1840 O HOH A 478 3179 2998 2390 -317 519 288 O HETATM 1841 O HOH A 479 28.162 13.583 21.921 1.00 32.87 O ANISOU 1841 O HOH A 479 5072 3969 3447 -1411 635 239 O HETATM 1842 O HOH A 480 44.038 22.772 50.810 1.00 48.80 O ANISOU 1842 O HOH A 480 5113 9025 4402 -348 -1344 2196 O HETATM 1843 O HOH A 481 48.747 21.833 28.028 1.00 27.61 O ANISOU 1843 O HOH A 481 2749 4043 3697 144 1316 761 O HETATM 1844 O HOH A 482 28.697 34.163 42.326 1.00 27.79 O ANISOU 1844 O HOH A 482 3174 4607 2775 653 752 -1059 O HETATM 1845 O HOH A 483 43.265 38.530 28.244 1.00 42.71 O ANISOU 1845 O HOH A 483 5716 7243 3267 -2658 1570 -487 O HETATM 1846 O HOH A 484 16.615 35.130 16.274 1.00 31.53 O ANISOU 1846 O HOH A 484 3151 4710 4116 -243 -284 1944 O HETATM 1847 O HOH A 485 35.397 33.687 34.835 1.00 13.44 O ANISOU 1847 O HOH A 485 1546 2091 1468 -41 452 -299 O HETATM 1848 O HOH A 486 30.583 15.793 25.422 1.00 21.69 O ANISOU 1848 O HOH A 486 3335 2870 2036 163 261 -384 O HETATM 1849 O HOH A 487 31.748 40.942 22.085 1.00 48.37 O ANISOU 1849 O HOH A 487 8268 3791 6320 2494 22 295 O HETATM 1850 O HOH A 488 44.218 40.186 35.378 1.00 20.84 O ANISOU 1850 O HOH A 488 2653 2871 2393 -750 295 -482 O HETATM 1851 O HOH A 489 27.864 39.156 19.342 1.00 33.92 O ANISOU 1851 O HOH A 489 5137 2942 4807 208 -1036 192 O HETATM 1852 O HOH A 490 40.364 43.011 35.898 1.00 23.82 O ANISOU 1852 O HOH A 490 2682 3292 3076 -580 721 -1088 O HETATM 1853 O HOH A 491 44.093 33.729 24.812 1.00 16.83 O ANISOU 1853 O HOH A 491 2104 2623 1666 -87 593 214 O HETATM 1854 O HOH A 492 38.448 39.040 38.540 1.00 19.20 O ANISOU 1854 O HOH A 492 2335 2706 2252 -241 180 -471 O HETATM 1855 O HOH A 493 39.473 17.543 15.704 1.00 33.05 O ANISOU 1855 O HOH A 493 5043 3911 3603 88 1858 -1209 O HETATM 1856 O HOH A 494 28.050 18.748 11.078 1.00 49.54 O ANISOU 1856 O HOH A 494 6954 8090 3780 -45 -861 -610 O HETATM 1857 O HOH A 495 27.481 35.251 49.406 1.00 36.69 O ANISOU 1857 O HOH A 495 5524 4320 4095 339 1604 91 O HETATM 1858 O HOH A 496 37.745 10.177 38.125 1.00 19.18 O ANISOU 1858 O HOH A 496 2903 2576 1808 312 427 346 O HETATM 1859 O HOH A 497 36.384 15.531 13.443 1.00 30.34 O ANISOU 1859 O HOH A 497 4819 4046 2663 1206 1186 150 O HETATM 1860 O HOH A 498 50.286 17.774 32.041 1.00 41.77 O ANISOU 1860 O HOH A 498 2921 3721 9228 476 -12 1082 O HETATM 1861 O HOH A 499 47.719 34.994 39.095 1.00 27.09 O ANISOU 1861 O HOH A 499 2826 4652 2813 -678 -231 -111 O HETATM 1862 O HOH A 500 29.160 40.319 22.348 1.00 40.88 O ANISOU 1862 O HOH A 500 7478 3877 4178 1253 -367 -280 O HETATM 1863 O HOH A 501 46.463 27.296 46.113 1.00 40.95 O ANISOU 1863 O HOH A 501 3497 7145 4916 -385 -1188 -1162 O HETATM 1864 O HOH A 502 34.563 35.465 50.752 1.00 32.42 O ANISOU 1864 O HOH A 502 6220 4315 1781 -1557 985 -608 O HETATM 1865 O HOH A 503 36.773 39.410 23.209 1.00 20.66 O ANISOU 1865 O HOH A 503 3233 2129 2488 213 518 462 O HETATM 1866 O HOH A 504 22.697 25.448 44.056 1.00 46.55 O ANISOU 1866 O HOH A 504 4362 7238 6083 1757 2195 -1259 O HETATM 1867 O HOH A 505 40.232 24.997 13.325 1.00 35.72 O ANISOU 1867 O HOH A 505 5894 3604 4072 947 2336 -112 O HETATM 1868 O HOH A 506 25.315 35.463 29.533 1.00 23.90 O ANISOU 1868 O HOH A 506 2221 2886 3972 131 -596 -239 O HETATM 1869 O HOH A 507 45.177 23.353 40.361 1.00 20.92 O ANISOU 1869 O HOH A 507 2286 3275 2386 -283 138 411 O HETATM 1870 O HOH A 508 45.874 37.458 29.727 1.00 32.47 O ANISOU 1870 O HOH A 508 4283 4339 3714 438 1770 1701 O HETATM 1871 O HOH A 509 36.639 38.704 45.054 1.00 19.75 O ANISOU 1871 O HOH A 509 3011 2652 1841 -12 290 -195 O HETATM 1872 O HOH A 510 22.884 22.691 15.967 1.00 40.90 O ANISOU 1872 O HOH A 510 6164 4259 5116 866 -2799 -1463 O HETATM 1873 O HOH A 511 20.036 27.926 14.609 1.00 39.80 O ANISOU 1873 O HOH A 511 5002 5799 4317 797 -1577 -1524 O HETATM 1874 O HOH A 512 46.918 33.051 18.556 1.00 26.28 O ANISOU 1874 O HOH A 512 3767 3471 2744 317 1164 702 O HETATM 1875 O HOH A 513 32.832 42.581 15.927 1.00 56.62 O ANISOU 1875 O HOH A 513 9851 4525 7135 -110 -134 727 O HETATM 1876 O HOH A 514 32.565 13.677 24.876 1.00 28.58 O ANISOU 1876 O HOH A 514 3608 4006 3244 -306 604 -417 O HETATM 1877 O HOH A 515 10.362 31.715 24.281 1.00 23.52 O ANISOU 1877 O HOH A 515 2173 3629 3133 -157 418 765 O HETATM 1878 O HOH A 516 46.061 21.826 48.542 1.00 41.34 O ANISOU 1878 O HOH A 516 6208 5400 4097 -315 -2315 895 O HETATM 1879 O HOH A 517 28.162 36.192 38.484 1.00 39.68 O ANISOU 1879 O HOH A 517 3485 5437 6153 986 1463 -2002 O HETATM 1880 O HOH A 518 40.139 46.631 30.497 1.00 34.06 O ANISOU 1880 O HOH A 518 6518 3007 3414 -325 2483 -114 O HETATM 1881 O HOH A 519 38.925 32.657 10.210 1.00 31.15 O ANISOU 1881 O HOH A 519 6143 3287 2404 -808 470 -400 O HETATM 1882 O HOH A 520 24.383 37.751 22.855 1.00 26.89 O ANISOU 1882 O HOH A 520 3184 3004 4027 1061 -140 -195 O HETATM 1883 O HOH A 521 18.489 17.112 35.868 1.00 58.37 O ANISOU 1883 O HOH A 521 5055 6633 10489 -2402 453 -1708 O HETATM 1884 O HOH A 522 18.944 15.386 24.958 1.00 43.04 O ANISOU 1884 O HOH A 522 6295 3878 6177 -194 682 -1022 O HETATM 1885 O HOH A 523 30.769 35.032 15.170 1.00 29.22 O ANISOU 1885 O HOH A 523 5470 3246 2385 -149 38 400 O HETATM 1886 O HOH A 524 38.771 43.721 26.774 1.00 44.71 O ANISOU 1886 O HOH A 524 10028 3772 3186 1484 1851 260 O HETATM 1887 O HOH A 525 18.203 20.625 20.345 1.00 34.34 O ANISOU 1887 O HOH A 525 2681 5376 4991 151 -783 -2285 O HETATM 1888 O HOH A 526 30.303 39.110 52.318 1.00 35.55 O ANISOU 1888 O HOH A 526 3331 6647 3525 346 492 -782 O HETATM 1889 O HOH A 527 45.978 15.383 44.510 1.00 43.07 O ANISOU 1889 O HOH A 527 4602 5380 6380 1281 55 1067 O HETATM 1890 O HOH A 528 50.151 22.655 36.913 1.00 30.33 O ANISOU 1890 O HOH A 528 2767 4723 4031 -185 50 1243 O HETATM 1891 O HOH A 529 30.972 14.922 38.042 1.00 22.02 O ANISOU 1891 O HOH A 529 2567 3232 2566 55 359 426 O HETATM 1892 O HOH A 530 31.688 20.761 13.439 1.00 26.13 O ANISOU 1892 O HOH A 530 5264 2721 1940 71 -323 -54 O HETATM 1893 O HOH A 531 5.520 36.787 24.894 1.00 35.45 O ANISOU 1893 O HOH A 531 3756 5415 4298 213 627 1160 O HETATM 1894 O HOH A 532 48.694 28.858 35.222 1.00 21.75 O ANISOU 1894 O HOH A 532 2122 3539 2604 -360 137 275 O HETATM 1895 O HOH A 533 33.815 34.271 18.760 1.00 23.40 O ANISOU 1895 O HOH A 533 3416 2551 2921 481 -534 -523 O HETATM 1896 O HOH A 534 22.459 18.404 33.010 1.00 37.18 O ANISOU 1896 O HOH A 534 4401 4028 5696 -921 1038 -1280 O HETATM 1897 O HOH A 535 48.097 19.860 34.966 1.00 27.52 O ANISOU 1897 O HOH A 535 2260 4191 4004 235 728 1151 O HETATM 1898 O HOH A 536 22.711 38.187 37.700 1.00 44.82 O ANISOU 1898 O HOH A 536 6398 4953 5678 1072 2087 238 O HETATM 1899 O HOH A 537 28.104 40.414 33.561 1.00 27.30 O ANISOU 1899 O HOH A 537 2756 3419 4196 695 213 -865 O HETATM 1900 O HOH A 538 14.019 25.734 35.952 1.00 27.74 O ANISOU 1900 O HOH A 538 2512 3946 4079 43 572 154 O HETATM 1901 O HOH A 539 43.094 37.738 42.152 1.00 27.11 O ANISOU 1901 O HOH A 539 3114 4279 2907 -135 94 -325 O HETATM 1902 O HOH A 540 42.066 18.520 17.321 1.00 32.82 O ANISOU 1902 O HOH A 540 5282 3735 3450 1833 1037 -1004 O HETATM 1903 O HOH A 541 33.177 10.762 17.024 1.00 29.50 O ANISOU 1903 O HOH A 541 5509 3251 2448 328 276 -1079 O HETATM 1904 O HOH A 542 34.839 10.248 29.526 1.00 32.43 O ANISOU 1904 O HOH A 542 3586 2390 6345 -447 1742 -818 O HETATM 1905 O HOH A 543 26.126 14.453 11.314 1.00 42.07 O ANISOU 1905 O HOH A 543 5460 6113 4412 300 -586 -3328 O HETATM 1906 O HOH A 544 23.679 17.057 30.516 1.00 34.85 O ANISOU 1906 O HOH A 544 3109 4379 5754 -616 62 -981 O HETATM 1907 O HOH A 545 12.530 29.335 17.269 1.00 29.55 O ANISOU 1907 O HOH A 545 3310 4878 3038 -48 -231 352 O HETATM 1908 O HOH A 546 32.587 17.003 46.092 1.00 37.85 O ANISOU 1908 O HOH A 546 5161 4185 5034 546 -153 -936 O HETATM 1909 O HOH A 547 43.334 30.484 11.778 1.00 42.82 O ANISOU 1909 O HOH A 547 7782 4013 4474 -892 2969 141 O HETATM 1910 O HOH A 548 34.253 10.703 24.258 1.00 34.03 O ANISOU 1910 O HOH A 548 5488 4243 3198 -1292 336 -742 O HETATM 1911 O HOH A 549 51.069 22.927 27.413 1.00 46.42 O ANISOU 1911 O HOH A 549 5701 4912 7023 -238 1849 -1146 O HETATM 1912 O HOH A 550 22.461 19.596 40.377 1.00 35.12 O ANISOU 1912 O HOH A 550 3561 5932 3851 -357 1469 -1396 O HETATM 1913 O HOH A 551 47.228 38.225 32.807 1.00 21.50 O ANISOU 1913 O HOH A 551 2301 3157 2711 -682 372 53 O HETATM 1914 O HOH A 552 30.585 26.077 14.676 1.00 42.27 O ANISOU 1914 O HOH A 552 4206 7582 4271 -680 -1376 2265 O HETATM 1915 O HOH A 553 18.034 23.513 40.136 1.00 47.09 O ANISOU 1915 O HOH A 553 6173 7064 4653 -2841 1180 475 O HETATM 1916 O HOH A 554 37.642 36.081 51.265 1.00 32.51 O ANISOU 1916 O HOH A 554 5550 3867 2932 213 300 306 O HETATM 1917 O HOH A 555 46.039 33.375 26.764 1.00 17.20 O ANISOU 1917 O HOH A 555 1968 2418 2149 -212 350 256 O HETATM 1918 O HOH A 556 10.972 28.801 35.280 1.00 32.87 O ANISOU 1918 O HOH A 556 2273 5396 4817 -458 -34 947 O HETATM 1919 O HOH A 557 29.040 42.594 35.924 1.00 25.91 O ANISOU 1919 O HOH A 557 2736 3613 3494 539 630 -1024 O HETATM 1920 O HOH A 558 41.236 36.342 49.006 1.00 37.53 O ANISOU 1920 O HOH A 558 5855 4765 3637 16 -1561 -643 O HETATM 1921 O HOH A 559 46.335 20.282 37.265 1.00 22.47 O ANISOU 1921 O HOH A 559 1949 3631 2957 89 325 618 O HETATM 1922 O HOH A 560 27.363 17.524 41.624 1.00 27.64 O ANISOU 1922 O HOH A 560 3637 3675 3190 -192 635 26 O HETATM 1923 O HOH A 561 23.905 40.392 35.335 1.00 52.16 O ANISOU 1923 O HOH A 561 6278 5079 8459 2613 829 -2260 O HETATM 1924 O HOH A 562 11.159 29.098 24.084 1.00 29.77 O ANISOU 1924 O HOH A 562 3185 5192 2934 18 188 -23 O HETATM 1925 O HOH A 563 11.808 24.632 28.763 1.00 36.92 O ANISOU 1925 O HOH A 563 1829 6896 5299 428 123 -375 O HETATM 1926 O HOH A 564 31.273 37.824 48.468 1.00 40.75 O ANISOU 1926 O HOH A 564 5795 5648 4038 1130 -824 -2085 O HETATM 1927 O HOH A 565 18.706 17.433 30.298 1.00 32.08 O ANISOU 1927 O HOH A 565 2664 4890 4634 -284 31 82 O HETATM 1928 O HOH A 566 36.674 25.608 11.697 1.00 38.80 O ANISOU 1928 O HOH A 566 7998 3619 3123 -567 434 -424 O HETATM 1929 O HOH A 567 46.952 30.277 18.712 1.00 22.12 O ANISOU 1929 O HOH A 567 2851 2935 2617 83 1171 168 O HETATM 1930 O HOH A 568 33.172 25.264 48.027 1.00 36.02 O ANISOU 1930 O HOH A 568 6013 5116 2554 -1487 543 -415 O HETATM 1931 O HOH A 569 26.362 34.114 40.707 1.00 49.88 O ANISOU 1931 O HOH A 569 3746 7800 7404 2675 -935 -5067 O HETATM 1932 O HOH A 570 13.394 24.468 24.051 1.00 54.38 O ANISOU 1932 O HOH A 570 3045 5933 11682 1142 -656 -1373 O HETATM 1933 O HOH A 571 42.824 42.378 29.430 1.00 34.39 O ANISOU 1933 O HOH A 571 4487 5194 3385 -1929 868 -1482 O HETATM 1934 O HOH A 572 32.564 17.160 11.072 1.00 53.31 O ANISOU 1934 O HOH A 572 6826 7535 5894 1125 1273 -1683 O HETATM 1935 O HOH A 573 33.960 11.416 27.065 1.00 31.72 O ANISOU 1935 O HOH A 573 4908 4279 2864 -1318 463 -507 O HETATM 1936 O HOH A 574 31.908 20.757 48.797 1.00 51.39 O ANISOU 1936 O HOH A 574 4479 9151 5896 238 586 2930 O HETATM 1937 O HOH A 575 28.289 12.995 12.271 1.00 55.21 O ANISOU 1937 O HOH A 575 5566 7659 7751 -1849 3289 -3326 O HETATM 1938 O HOH A 576 28.831 10.849 32.697 1.00 52.80 O ANISOU 1938 O HOH A 576 4653 4630 10776 -1349 -602 830 O HETATM 1939 O HOH A 577 23.392 14.458 13.261 1.00 47.10 O ANISOU 1939 O HOH A 577 6403 5599 5894 -1828 -237 -2724 O HETATM 1940 O HOH A 578 35.002 18.028 45.977 1.00 30.94 O ANISOU 1940 O HOH A 578 4191 4316 3248 330 742 -888 O HETATM 1941 O HOH A 579 46.505 19.552 43.240 1.00 41.35 O ANISOU 1941 O HOH A 579 3595 6769 5346 550 -413 1892 O HETATM 1942 O HOH A 580 47.985 17.779 28.856 1.00 56.84 O ANISOU 1942 O HOH A 580 2888 7114 11594 744 -331 -2900 O HETATM 1943 O HOH A 581 41.674 12.187 33.137 1.00 30.18 O ANISOU 1943 O HOH A 581 3311 3248 4907 373 541 -172 O HETATM 1944 O HOH A 582 25.074 13.131 17.131 1.00 49.11 O ANISOU 1944 O HOH A 582 5506 7781 5372 -1473 -153 -2422 O HETATM 1945 O HOH A 583 32.699 32.359 11.433 1.00 43.93 O ANISOU 1945 O HOH A 583 8537 4446 3707 547 286 -609 O HETATM 1946 O HOH A 584 41.920 43.197 27.412 1.00 45.73 O ANISOU 1946 O HOH A 584 5967 5065 6341 -1802 130 2514 O HETATM 1947 O HOH A 585 50.416 24.258 24.127 1.00 39.49 O ANISOU 1947 O HOH A 585 4346 4776 5882 338 2260 847 O HETATM 1948 O HOH A 586 19.941 18.353 32.555 1.00 44.47 O ANISOU 1948 O HOH A 586 3812 5229 7854 -625 -993 -1095 O HETATM 1949 O HOH A 587 39.984 45.343 34.836 1.00 26.94 O ANISOU 1949 O HOH A 587 3714 3276 3245 -1233 705 -433 O HETATM 1950 O HOH A 588 19.160 42.791 21.965 1.00 45.76 O ANISOU 1950 O HOH A 588 5290 4611 7484 1657 -912 -105 O HETATM 1951 O HOH A 589 11.605 34.061 35.800 1.00 58.49 O ANISOU 1951 O HOH A 589 3693 9053 9478 -2234 1460 -2629 O HETATM 1952 O HOH A 590 37.314 41.550 25.071 1.00 30.21 O ANISOU 1952 O HOH A 590 4872 2819 3787 -156 1235 -51 O HETATM 1953 O HOH A 591 23.451 38.306 11.706 1.00 46.80 O ANISOU 1953 O HOH A 591 6030 5735 6015 694 -1011 2949 O HETATM 1954 O HOH A 592 26.822 37.007 36.712 1.00 37.63 O ANISOU 1954 O HOH A 592 4171 4343 5782 -197 1833 -2147 O HETATM 1955 O HOH A 593 19.084 15.361 22.122 1.00 48.79 O ANISOU 1955 O HOH A 593 3387 6924 8225 -189 -930 -3238 O HETATM 1956 O HOH A 594 26.782 39.799 35.828 1.00 41.40 O ANISOU 1956 O HOH A 594 3299 6821 5608 -31 521 -2395 O HETATM 1957 O HOH A 595 49.799 34.638 37.493 1.00 50.31 O ANISOU 1957 O HOH A 595 4359 8661 6094 -2581 -420 -1728 O HETATM 1958 O HOH A 596 30.176 19.042 48.317 1.00 52.90 O ANISOU 1958 O HOH A 596 7930 4989 7181 1170 -1991 1333 O HETATM 1959 O HOH A 597 40.686 31.719 50.488 1.00 35.31 O ANISOU 1959 O HOH A 597 5750 4727 2936 -398 1334 -247 O HETATM 1960 O HOH A 598 6.618 35.187 17.490 1.00 51.53 O ANISOU 1960 O HOH A 598 5010 7094 7473 1855 -915 -1226 O HETATM 1961 O HOH A 599 11.017 35.676 31.872 1.00 40.34 O ANISOU 1961 O HOH A 599 5935 5098 4292 207 191 -532 O HETATM 1962 O HOH A 600 38.805 45.860 27.898 1.00 46.77 O ANISOU 1962 O HOH A 600 9886 4106 3777 -1400 -158 1254 O HETATM 1963 O HOH A 601 49.967 37.909 32.452 1.00 44.99 O ANISOU 1963 O HOH A 601 4050 6971 6071 -1104 887 -426 O HETATM 1964 O HOH A 602 33.178 35.896 16.597 1.00 28.90 O ANISOU 1964 O HOH A 602 4838 3067 3076 897 281 373 O HETATM 1965 O HOH A 603 29.790 38.917 44.184 1.00 32.25 O ANISOU 1965 O HOH A 603 3509 5207 3536 -466 317 -1102 O HETATM 1966 O HOH A 604 27.614 11.799 36.239 1.00 52.64 O ANISOU 1966 O HOH A 604 4816 8746 6435 -463 2277 -118 O HETATM 1967 O HOH A 605 31.226 10.583 33.681 1.00 49.43 O ANISOU 1967 O HOH A 605 7260 5237 6282 -1859 1473 1210 O HETATM 1968 O HOH A 606 19.946 22.194 41.383 1.00 55.37 O ANISOU 1968 O HOH A 606 4926 8211 7898 -1659 1 -321 O HETATM 1969 O HOH A 607 24.371 17.339 41.493 1.00 43.09 O ANISOU 1969 O HOH A 607 6666 4988 4718 -1796 1176 -322 O HETATM 1970 O HOH A 608 41.266 31.771 9.974 1.00 49.71 O ANISOU 1970 O HOH A 608 8867 4599 5421 605 -1303 112 O HETATM 1971 O HOH A 609 46.565 40.745 33.967 1.00 42.76 O ANISOU 1971 O HOH A 609 3200 4409 8638 -1045 1614 156 O HETATM 1972 O HOH A 610 24.070 22.491 13.831 1.00 52.59 O ANISOU 1972 O HOH A 610 5685 9800 4496 -1692 -1692 -1228 O HETATM 1973 O HOH A 611 25.869 21.854 46.665 1.00 44.59 O ANISOU 1973 O HOH A 611 6185 6506 4248 -1628 2528 -1254 O HETATM 1974 O HOH A 612 45.722 36.847 13.405 1.00 51.41 O ANISOU 1974 O HOH A 612 7299 5205 7030 -1114 3053 1125 O HETATM 1975 O HOH A 613 14.745 23.457 19.325 1.00 40.61 O ANISOU 1975 O HOH A 613 3326 7041 5062 -616 -1476 -35 O HETATM 1976 O HOH A 614 35.814 40.926 20.080 1.00 26.27 O ANISOU 1976 O HOH A 614 3814 3766 2401 -132 325 651 O HETATM 1977 O HOH A 615 8.199 28.349 21.785 1.00 25.55 O ANISOU 1977 O HOH A 615 2817 3751 3137 498 780 179 O HETATM 1978 O HOH A 616 41.737 14.294 29.813 1.00 35.17 O ANISOU 1978 O HOH A 616 5212 5162 2989 1389 -939 -60 O HETATM 1979 O HOH A 617 42.711 40.698 45.472 1.00 34.33 O ANISOU 1979 O HOH A 617 3312 5244 4489 -22 -805 -349 O HETATM 1980 O HOH A 618 28.638 12.994 41.944 1.00 54.43 O ANISOU 1980 O HOH A 618 3884 8695 8100 478 1668 -1057 O HETATM 1981 O HOH A 619 16.229 29.998 12.710 1.00 36.94 O ANISOU 1981 O HOH A 619 3708 7062 3263 563 209 244 O HETATM 1982 O HOH A 620 50.033 30.598 39.625 1.00 56.16 O ANISOU 1982 O HOH A 620 5521 8994 6820 1925 -2590 -370 O HETATM 1983 O HOH A 621 49.882 19.417 27.798 1.00 46.89 O ANISOU 1983 O HOH A 621 5796 4877 7142 1808 -430 -959 O HETATM 1984 O HOH A 622 34.591 37.468 12.086 1.00 51.05 O ANISOU 1984 O HOH A 622 5816 9929 3649 81 416 243 O HETATM 1985 O HOH A 623 8.120 30.022 19.632 1.00 27.12 O ANISOU 1985 O HOH A 623 2544 4213 3546 -63 140 385 O HETATM 1986 O HOH A 624 27.451 14.852 40.423 1.00 49.71 O ANISOU 1986 O HOH A 624 5074 8020 5790 -195 1767 -2120 O HETATM 1987 O HOH A 625 24.722 42.973 27.825 1.00 58.15 O ANISOU 1987 O HOH A 625 4862 11076 6157 1839 -400 3517 O HETATM 1988 O HOH A 626 18.904 14.797 29.282 1.00 42.19 O ANISOU 1988 O HOH A 626 4360 4518 7150 -323 661 -306 O HETATM 1989 O HOH A 627 10.592 39.043 25.236 1.00 52.14 O ANISOU 1989 O HOH A 627 4277 8662 6871 2703 -520 -84 O HETATM 1990 O HOH A 628 28.424 14.610 24.540 1.00 43.58 O ANISOU 1990 O HOH A 628 4919 8367 3270 -1281 245 -318 O HETATM 1991 O HOH A 629 46.570 25.522 48.327 1.00 54.10 O ANISOU 1991 O HOH A 629 8769 7193 4592 -1651 -214 -697 O HETATM 1992 O HOH A 630 31.440 11.496 15.499 1.00 36.42 O ANISOU 1992 O HOH A 630 4778 5554 3505 64 208 -71 O HETATM 1993 O HOH A 631 9.597 28.772 17.623 1.00 35.72 O ANISOU 1993 O HOH A 631 3468 5898 4205 0 86 -473 O HETATM 1994 O HOH A 632 34.678 27.237 8.021 1.00 48.99 O ANISOU 1994 O HOH A 632 6009 6059 6544 328 2920 2340 O HETATM 1995 O HOH A 633 9.854 26.285 21.275 1.00 47.44 O ANISOU 1995 O HOH A 633 2893 7354 7776 384 583 -507 O HETATM 1996 O HOH A 634 50.013 18.554 35.182 1.00 56.30 O ANISOU 1996 O HOH A 634 3865 9811 7714 -1840 1806 -1267 O HETATM 1997 O HOH A 635 44.201 39.727 43.477 1.00 39.94 O ANISOU 1997 O HOH A 635 3526 5462 6187 -741 42 -2224 O HETATM 1998 O HOH A 636 27.027 20.399 48.513 1.00 55.58 O ANISOU 1998 O HOH A 636 7061 9682 4374 -1780 2665 -920 O HETATM 1999 O HOH A 637 34.409 40.705 22.319 1.00 31.90 O ANISOU 1999 O HOH A 637 4952 3980 3186 269 578 -40 O HETATM 2000 O HOH A 638 43.837 37.638 39.437 1.00 32.15 O ANISOU 2000 O HOH A 638 4765 4325 3124 -1301 104 -456 O HETATM 2001 O HOH A 639 18.254 18.033 20.906 1.00 55.13 O ANISOU 2001 O HOH A 639 7857 9048 4040 -2549 -588 -583 O HETATM 2002 O HOH A 640 43.127 38.328 25.806 1.00 27.41 O ANISOU 2002 O HOH A 640 3606 3243 3565 238 274 536 O HETATM 2003 O HOH A 641 8.001 34.802 15.280 1.00 60.76 O ANISOU 2003 O HOH A 641 6981 9040 7062 862 -333 1164 O HETATM 2004 O HOH A 642 44.246 14.569 35.219 1.00 48.13 O ANISOU 2004 O HOH A 642 5827 6777 5682 2173 -1678 193 O HETATM 2005 O HOH A 643 47.830 24.139 40.689 1.00 26.03 O ANISOU 2005 O HOH A 643 2422 4602 2864 -246 -217 465 O HETATM 2006 O HOH A 644 24.543 11.451 15.019 1.00 41.15 O ANISOU 2006 O HOH A 644 4427 5818 5387 -1164 -986 -876 O HETATM 2007 O HOH A 645 29.100 37.458 50.229 1.00 52.75 O ANISOU 2007 O HOH A 645 6420 5834 7786 406 -1311 -1133 O HETATM 2008 O HOH A 646 50.080 32.549 32.765 1.00 31.52 O ANISOU 2008 O HOH A 646 2432 4719 4823 -598 -69 246 O HETATM 2009 O HOH A 647 42.834 42.433 34.610 1.00 23.12 O ANISOU 2009 O HOH A 647 2842 3039 2900 -404 818 -793 O HETATM 2010 O HOH A 648 51.799 26.341 25.192 1.00 48.92 O ANISOU 2010 O HOH A 648 3399 9947 5240 1182 1542 -1077 O HETATM 2011 O HOH A 649 46.773 37.408 40.365 1.00 42.88 O ANISOU 2011 O HOH A 649 4076 5029 7185 -181 -675 -160 O HETATM 2012 O HOH A 650 19.149 13.032 20.978 1.00 53.31 O ANISOU 2012 O HOH A 650 3413 8321 8522 164 -984 -1041 O HETATM 2013 O HOH A 651 8.479 43.083 23.938 1.00 36.09 O ANISOU 2013 O HOH A 651 4988 3854 4871 1080 189 1678 O HETATM 2014 O HOH A 652 12.985 27.298 25.645 1.00 46.31 O ANISOU 2014 O HOH A 652 4550 6467 6577 307 179 -99 O HETATM 2015 O HOH A 653 43.635 40.055 38.104 1.00 30.13 O ANISOU 2015 O HOH A 653 4741 3708 2998 -731 16 -590 O HETATM 2016 O HOH A 654 22.877 39.907 30.106 1.00 34.41 O ANISOU 2016 O HOH A 654 4816 3827 4428 1725 -270 -905 O HETATM 2017 O HOH A 655 44.185 34.432 11.564 1.00 31.91 O ANISOU 2017 O HOH A 655 4399 5353 2373 135 755 541 O HETATM 2018 O HOH A 656 40.425 9.838 37.516 1.00 28.86 O ANISOU 2018 O HOH A 656 3036 4515 3413 64 86 1093 O HETATM 2019 O HOH A 657 12.538 22.965 20.782 1.00 59.17 O ANISOU 2019 O HOH A 657 3301 14027 5153 1100 717 2304 O HETATM 2020 O HOH A 658 52.317 24.192 37.078 1.00 44.15 O ANISOU 2020 O HOH A 658 4288 7972 4513 -1398 1006 -183 O HETATM 2021 O HOH A 659 46.967 15.763 34.872 1.00 42.16 O ANISOU 2021 O HOH A 659 5031 4957 6028 614 14 707 O HETATM 2022 O HOH A 660 18.037 27.905 12.670 1.00 47.53 O ANISOU 2022 O HOH A 660 6556 6537 4966 1206 -2751 -823 O HETATM 2023 O HOH A 661 27.116 42.170 31.622 1.00 45.16 O ANISOU 2023 O HOH A 661 4567 3571 9021 971 -160 -168 O HETATM 2024 O HOH A 662 51.917 26.902 36.873 1.00 48.02 O ANISOU 2024 O HOH A 662 3156 9044 6046 1584 250 1587 O HETATM 2025 O HOH A 663 50.532 30.736 34.678 1.00 28.23 O ANISOU 2025 O HOH A 663 2207 4191 4328 -915 399 -327 O HETATM 2026 O HOH A 664 38.925 53.804 30.380 1.00 51.30 O ANISOU 2026 O HOH A 664 9207 4725 5557 -993 3099 -655 O HETATM 2027 O HOH A 665 13.227 26.840 16.812 1.00 45.18 O ANISOU 2027 O HOH A 665 3430 7336 6398 1018 -2182 -1693 O HETATM 2028 O HOH A 666 44.339 12.284 36.899 1.00 48.80 O ANISOU 2028 O HOH A 666 5676 5947 6918 -1574 2193 -2251 O HETATM 2029 O HOH A 667 46.566 15.485 29.130 1.00 55.26 O ANISOU 2029 O HOH A 667 6156 6728 8109 3801 823 -693 O HETATM 2030 O HOH A 668 32.766 19.769 11.150 1.00 49.79 O ANISOU 2030 O HOH A 668 10102 6082 2731 1657 632 -690 O HETATM 2031 O HOH A 669 47.941 19.100 39.175 1.00 33.52 O ANISOU 2031 O HOH A 669 3076 5337 4321 335 -462 1371 O HETATM 2032 O HOH A 670 21.635 26.834 12.454 1.00 51.21 O ANISOU 2032 O HOH A 670 6902 6885 5670 -2640 -741 -413 O HETATM 2033 O HOH A 671 45.954 22.961 37.710 1.00 21.14 O ANISOU 2033 O HOH A 671 2234 3360 2438 58 219 507 O HETATM 2034 O HOH A 672 27.982 41.261 38.073 1.00 35.33 O ANISOU 2034 O HOH A 672 4588 3666 5168 68 2248 -1059 O HETATM 2035 O HOH A 673 25.509 41.112 29.468 1.00 38.80 O ANISOU 2035 O HOH A 673 4110 3980 6650 1454 323 -672 O HETATM 2036 O HOH A 674 29.634 40.679 47.626 1.00 58.19 O ANISOU 2036 O HOH A 674 9402 7128 5578 -3899 3738 -2053 O HETATM 2037 O HOH A 675 47.682 26.488 18.046 1.00 47.63 O ANISOU 2037 O HOH A 675 5507 6264 6325 292 1964 -818 O HETATM 2038 O HOH A 676 48.377 24.450 37.998 1.00 25.94 O ANISOU 2038 O HOH A 676 2571 4404 2880 -557 157 592 O HETATM 2039 O HOH A 677 16.090 21.324 18.657 1.00 43.11 O ANISOU 2039 O HOH A 677 3490 7685 5203 -552 -662 -1641 O HETATM 2040 O HOH A 678 10.783 25.980 18.379 1.00 44.52 O ANISOU 2040 O HOH A 678 3437 7339 6136 689 897 -201 O HETATM 2041 O HOH A 679 46.604 29.147 16.258 1.00 28.63 O ANISOU 2041 O HOH A 679 3739 4131 3007 137 1317 33 O HETATM 2042 O HOH A 680 30.359 24.666 12.358 1.00 60.49 O ANISOU 2042 O HOH A 680 9501 6157 7323 2906 808 1448 O HETATM 2043 O HOH A 681 41.994 45.634 32.708 1.00 39.69 O ANISOU 2043 O HOH A 681 4679 4301 6100 -862 1184 -201 O HETATM 2044 O HOH A 682 27.945 14.410 47.388 1.00 31.68 O ANISOU 2044 O HOH A 682 4130 3729 4178 498 505 1459 O HETATM 2045 O HOH A 683 12.368 19.115 21.664 1.00 55.20 O ANISOU 2045 O HOH A 683 4836 6813 9326 -1136 -1217 -489 O HETATM 2046 O HOH A 684 26.895 11.479 13.712 1.00 41.86 O ANISOU 2046 O HOH A 684 4303 5468 6134 1076 -185 -1238 O HETATM 2047 O HOH A 685 49.070 27.204 37.416 1.00 24.79 O ANISOU 2047 O HOH A 685 2295 4232 2890 -272 -34 539 O HETATM 2048 O HOH A 686 50.138 20.734 38.854 1.00 37.25 O ANISOU 2048 O HOH A 686 4518 5349 4287 48 -270 1676 O HETATM 2049 O HOH A 687 43.072 27.529 10.822 1.00 54.06 O ANISOU 2049 O HOH A 687 8964 8035 3538 229 -968 -568 O HETATM 2050 O HOH A 688 51.060 32.480 36.666 1.00 41.72 O ANISOU 2050 O HOH A 688 3042 6907 5899 -337 757 -1315 O HETATM 2051 O HOH A 689 46.273 12.762 41.950 1.00 46.67 O ANISOU 2051 O HOH A 689 6189 6935 4608 835 222 1730 O HETATM 2052 O HOH A 690 29.276 9.291 16.472 1.00 43.85 O ANISOU 2052 O HOH A 690 5010 3942 7708 -31 -874 -423 O HETATM 2053 O HOH A 691 49.857 22.259 41.164 1.00 46.65 O ANISOU 2053 O HOH A 691 5190 6620 5914 1120 -1359 1523 O HETATM 2054 O HOH A 692 43.456 43.221 31.997 1.00 29.29 O ANISOU 2054 O HOH A 692 4062 3763 3303 -548 534 -106 O HETATM 2055 O HOH A 693 36.245 21.460 11.292 1.00 46.67 O ANISOU 2055 O HOH A 693 7856 5249 4624 -504 882 -578 O HETATM 2056 O HOH A 694 48.462 30.742 14.828 1.00 48.12 O ANISOU 2056 O HOH A 694 3750 9598 4934 80 1711 1175 O CONECT 632 1748 CONECT 644 1748 CONECT 664 1747 CONECT 1143 1748 CONECT 1284 1747 CONECT 1595 1747 CONECT 1747 664 1284 1595 1762 CONECT 1748 632 644 1143 1762 CONECT 1749 1750 CONECT 1750 1749 1751 1752 CONECT 1751 1750 CONECT 1752 1750 1753 1756 CONECT 1753 1752 1754 CONECT 1754 1753 1755 CONECT 1755 1754 1756 CONECT 1756 1752 1755 1757 CONECT 1757 1756 1758 1759 CONECT 1758 1757 CONECT 1759 1757 1760 1761 CONECT 1760 1759 CONECT 1761 1759 1762 CONECT 1762 1747 1748 1761 MASTER 468 0 3 8 12 0 8 6 2011 1 22 19 END If you find results from this site helpful for your research, please cite one of our papers:
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