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*** TRANSPORT PROTEIN 21-OCT-10 3APX ***elNémo ID: 240110225123556539Job options:ID = 240110225123556539 JOBID = TRANSPORT PROTEIN 21-OCT-10 3APX 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 TRANSPORT PROTEIN 21-OCT-10 3APX TITLE CRYSTAL STRUCTURE OF THE A VARIANT OF HUMAN ALPHA1-ACID GLYCOPROTEIN TITLE 2 AND CHLORPROMAZINE COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: ALPHA-1-ACID GLYCOPROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: AGP 2, OROSOMUCOID-2, OMD 2; COMPND 5 ENGINEERED: YES; COMPND 6 MUTATION: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: AGP2, ORM2; SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ORIGAMI B (DE3); SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET3C KEYWDS BETA BARREL, PLASMA PROTEIN, TRANSPORT PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR K.NISHI,T.ONO,T.NAKAMURA,N.FUKUNAGA,M.IZUMI,H.WATANABE,A.SUENAGA, AUTHOR 2 T.MARUYAMA,Y.YAMAGATA,S.CURRY,M.OTAGIRI REVDAT 4 08-NOV-23 3APX 1 REMARK REVDAT 3 12-OCT-22 3APX 1 REMARK SEQADV HETSYN REVDAT 2 07-NOV-18 3APX 1 JRNL REVDAT 1 23-FEB-11 3APX 0 JRNL AUTH K.NISHI,T.ONO,T.NAKAMURA,N.FUKUNAGA,M.IZUMI,H.WATANABE, JRNL AUTH 2 A.SUENAGA,T.MARUYAMA,Y.YAMAGATA,S.CURRY,M.OTAGIRI JRNL TITL STRUCTURAL INSIGHTS INTO DIFFERENCES IN DRUG-BINDING JRNL TITL 2 SELECTIVITY BETWEEN TWO FORMS OF HUMAN ALPHA1-ACID JRNL TITL 3 GLYCOPROTEIN GENETIC VARIANTS, THE A AND F1*S FORMS. JRNL REF J. BIOL. CHEM. V. 286 14427 2011 JRNL REFN ESSN 1083-351X JRNL PMID 21349832 JRNL DOI 10.1074/JBC.M110.208926 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.5.0099 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) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 28.88 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3 REMARK 3 NUMBER OF REFLECTIONS : 8671 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) : 0.206 REMARK 3 R VALUE (WORKING SET) : 0.202 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.400 REMARK 3 FREE R VALUE TEST SET COUNT : 494 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.20 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.26 REMARK 3 REFLECTION IN BIN (WORKING SET) : 600 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.77 REMARK 3 BIN R VALUE (WORKING SET) : 0.2040 REMARK 3 BIN FREE R VALUE SET COUNT : 34 REMARK 3 BIN FREE R VALUE : 0.3240 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1502 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 25 REMARK 3 SOLVENT ATOMS : 138 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 13.14 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.01000 REMARK 3 B22 (A**2) : -0.03000 REMARK 3 B33 (A**2) : 0.02000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 0.264 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.190 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 16.350 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.894 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1568 ; 0.008 ; 0.022 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2120 ; 1.100 ; 1.963 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 178 ; 5.588 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 86 ;38.381 ;24.186 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 273 ;15.631 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 11 ;21.895 ;15.000 REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 217 ; 0.080 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1221 ; 0.004 ; 0.021 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 895 ; 0.418 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1451 ; 0.819 ; 2.000 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 673 ; 1.225 ; 3.000 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 669 ; 2.051 ; 4.500 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 1 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 0 A 178 REMARK 3 ORIGIN FOR THE GROUP (A): -7.0140 -13.5210 17.5870 REMARK 3 T TENSOR REMARK 3 T11: 0.0301 T22: 0.0034 REMARK 3 T33: 0.0738 T12: 0.0066 REMARK 3 T13: 0.0005 T23: 0.0056 REMARK 3 L TENSOR REMARK 3 L11: 0.4180 L22: 0.2991 REMARK 3 L33: 0.9836 L12: -0.0198 REMARK 3 L13: 0.0025 L23: 0.1976 REMARK 3 S TENSOR REMARK 3 S11: 0.0149 S12: 0.0123 S13: 0.0428 REMARK 3 S21: -0.0307 S22: -0.0230 S23: 0.0025 REMARK 3 S31: -0.0431 S32: -0.0387 S33: 0.0081 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : 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 REMARK 4 REMARK 4 3APX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 09-NOV-10. REMARK 100 THE DEPOSITION ID IS D_1000029548. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 04-FEB-09 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 4.6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : PHOTON FACTORY REMARK 200 BEAMLINE : BL-5A REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000 REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9216 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 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 (%) : 99.2 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.07900 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 27.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.28 REMARK 200 COMPLETENESS FOR SHELL (%) : 95.2 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.16100 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 8.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: PDB ENTRY 3APU REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 35.32 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.90 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 0.2M AMMONIUM SULFATE, REMARK 280 0.1M SODIUM ACETATE, PH 4.6, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-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 21.06250 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 32.47850 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 31.53850 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 32.47850 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 21.06250 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 31.53850 REMARK 290 SMTRY3 4 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 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 GLU A 179 REMARK 465 GLU A 180 REMARK 465 GLY A 181 REMARK 465 GLU A 182 REMARK 465 SER A 183 REMARK 465 HIS A 184 REMARK 465 HIS A 185 REMARK 465 HIS A 186 REMARK 465 HIS A 187 REMARK 465 HIS A 188 REMARK 465 HIS A 189 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE Z80 A 190 REMARK 800 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 191 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 3APU RELATED DB: PDB REMARK 900 RELATED ID: 3APV RELATED DB: PDB REMARK 900 RELATED ID: 3APW RELATED DB: PDB DBREF 3APX A 1 183 UNP P19652 A1AG2_HUMAN 19 201 SEQADV 3APX MET A 0 UNP P19652 EXPRESSION TAG SEQADV 3APX ARG A 149 UNP P19652 CYS 167 ENGINEERED MUTATION SEQADV 3APX HIS A 184 UNP P19652 EXPRESSION TAG SEQADV 3APX HIS A 185 UNP P19652 EXPRESSION TAG SEQADV 3APX HIS A 186 UNP P19652 EXPRESSION TAG SEQADV 3APX HIS A 187 UNP P19652 EXPRESSION TAG SEQADV 3APX HIS A 188 UNP P19652 EXPRESSION TAG SEQADV 3APX HIS A 189 UNP P19652 EXPRESSION TAG SEQRES 1 A 190 MET GLN ILE PRO LEU CYS ALA ASN LEU VAL PRO VAL PRO SEQRES 2 A 190 ILE THR ASN ALA THR LEU ASP ARG ILE THR GLY LYS TRP SEQRES 3 A 190 PHE TYR ILE ALA SER ALA PHE ARG ASN GLU GLU TYR ASN SEQRES 4 A 190 LYS SER VAL GLN GLU ILE GLN ALA THR PHE PHE TYR PHE SEQRES 5 A 190 THR PRO ASN LYS THR GLU ASP THR ILE PHE LEU ARG GLU SEQRES 6 A 190 TYR GLN THR ARG GLN ASN GLN CYS PHE TYR ASN SER SER SEQRES 7 A 190 TYR LEU ASN VAL GLN ARG GLU ASN GLY THR VAL SER ARG SEQRES 8 A 190 TYR GLU GLY GLY ARG GLU HIS VAL ALA HIS LEU LEU PHE SEQRES 9 A 190 LEU ARG ASP THR LYS THR LEU MET PHE GLY SER TYR LEU SEQRES 10 A 190 ASP ASP GLU LYS ASN TRP GLY LEU SER PHE TYR ALA ASP SEQRES 11 A 190 LYS PRO GLU THR THR LYS GLU GLN LEU GLY GLU PHE TYR SEQRES 12 A 190 GLU ALA LEU ASP CYS LEU ARG ILE PRO ARG SER ASP VAL SEQRES 13 A 190 MET TYR THR ASP TRP LYS LYS ASP LYS CYS GLU PRO LEU SEQRES 14 A 190 GLU LYS GLN HIS GLU LYS GLU ARG LYS GLN GLU GLU GLY SEQRES 15 A 190 GLU SER HIS HIS HIS HIS HIS HIS HET Z80 A 190 21 HET ACY A 191 4 HETNAM Z80 3-(2-CHLORO-10H-PHENOTHIAZIN-10-YL)-N,N-DIMETHYLPROPAN- HETNAM 2 Z80 1-AMINE HETNAM ACY ACETIC ACID HETSYN Z80 CHLORPROMAZINE FORMUL 2 Z80 C17 H19 CL N2 S FORMUL 3 ACY C2 H4 O2 FORMUL 4 HOH *138(H2 O) HELIX 1 1 CYS A 5 VAL A 9 5 5 HELIX 2 2 THR A 14 THR A 22 1 9 HELIX 3 3 ASN A 34 GLN A 42 1 9 HELIX 4 4 THR A 134 LEU A 148 1 15 HELIX 5 5 PRO A 151 VAL A 155 5 5 HELIX 6 6 ASP A 159 ASP A 163 5 5 HELIX 7 7 CYS A 165 LYS A 177 1 13 SHEET 1 A10 MET A 156 TYR A 157 0 SHEET 2 A10 GLY A 23 PHE A 32 -1 N SER A 30 O MET A 156 SHEET 3 A10 GLY A 123 ALA A 128 -1 O PHE A 126 N ALA A 29 SHEET 4 A10 THR A 109 SER A 114 -1 N LEU A 110 O TYR A 127 SHEET 5 A10 ARG A 95 LEU A 102 -1 N LEU A 102 O MET A 111 SHEET 6 A10 THR A 87 GLU A 92 -1 N ARG A 90 O HIS A 97 SHEET 7 A10 GLN A 71 GLN A 82 -1 N GLN A 82 O THR A 87 SHEET 8 A10 THR A 59 ARG A 68 -1 N ILE A 60 O LEU A 79 SHEET 9 A10 ILE A 44 ASN A 54 -1 N ASN A 54 O THR A 59 SHEET 10 A10 GLY A 23 PHE A 32 -1 N TYR A 27 O THR A 47 SSBOND 1 CYS A 5 CYS A 147 1555 1555 2.03 SSBOND 2 CYS A 72 CYS A 165 1555 1555 2.03 CISPEP 1 ILE A 2 PRO A 3 0 4.85 SITE 1 AC1 9 PHE A 49 PHE A 51 VAL A 88 ARG A 90 SITE 2 AC1 9 GLU A 92 HIS A 97 ALA A 99 PHE A 112 SITE 3 AC1 9 TYR A 127 SITE 1 AC2 6 VAL A 11 ARG A 20 PHE A 103 ASP A 146 SITE 2 AC2 6 ARG A 152 HOH A 202 CRYST1 42.125 63.077 64.957 90.00 90.00 90.00 P 21 21 21 4 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 0.023739 0.000000 0.000000 0.00000 SCALE2 0.000000 0.015854 0.000000 0.00000 SCALE3 0.000000 0.000000 0.015395 0.00000 ATOM 1 N MET A 0 1.396 -6.174 40.396 1.00 16.67 N ANISOU 1 N MET A 0 1964 2023 2345 -132 -79 -318 N ATOM 2 CA MET A 0 0.496 -6.952 39.504 1.00 16.51 C ANISOU 2 CA MET A 0 1955 1979 2339 -106 -67 -277 C ATOM 3 C MET A 0 -0.035 -8.179 40.236 1.00 15.75 C ANISOU 3 C MET A 0 1857 1916 2209 -81 -70 -254 C ATOM 4 O MET A 0 0.744 -8.980 40.767 1.00 15.84 O ANISOU 4 O MET A 0 1855 1967 2195 -75 -87 -244 O ATOM 5 CB MET A 0 1.215 -7.351 38.210 1.00 16.76 C ANISOU 5 CB MET A 0 1976 1996 2395 -110 -67 -251 C ATOM 6 CG MET A 0 0.442 -8.359 37.371 1.00 18.67 C ANISOU 6 CG MET A 0 2226 2223 2644 -84 -58 -210 C ATOM 7 SD MET A 0 0.717 -8.224 35.600 1.00 24.33 S ANISOU 7 SD MET A 0 2945 2901 3399 -90 -48 -189 S ATOM 8 CE MET A 0 -0.081 -6.659 35.247 1.00 22.95 C ANISOU 8 CE MET A 0 2798 2674 3249 -102 -33 -212 C ATOM 9 N GLN A 1 -1.361 -8.309 40.252 1.00 14.82 N ANISOU 9 N GLN A 1 1755 1785 2090 -67 -55 -246 N ATOM 10 CA GLN A 1 -2.044 -9.334 41.026 1.00 14.09 C ANISOU 10 CA GLN A 1 1666 1723 1963 -53 -53 -228 C ATOM 11 C GLN A 1 -1.976 -10.708 40.361 1.00 12.92 C ANISOU 11 C GLN A 1 1522 1572 1815 -42 -55 -182 C ATOM 12 O GLN A 1 -2.455 -10.904 39.242 1.00 12.29 O ANISOU 12 O GLN A 1 1446 1461 1761 -38 -44 -164 O ATOM 13 CB GLN A 1 -3.497 -8.923 41.305 1.00 14.54 C ANISOU 13 CB GLN A 1 1732 1775 2017 -46 -33 -241 C ATOM 14 CG GLN A 1 -4.144 -9.720 42.436 1.00 15.65 C ANISOU 14 CG GLN A 1 1876 1957 2113 -42 -28 -233 C ATOM 15 CD GLN A 1 -5.649 -9.517 42.538 1.00 17.44 C ANISOU 15 CD GLN A 1 2104 2187 2335 -36 -6 -243 C ATOM 16 OE1 GLN A 1 -6.155 -8.396 42.407 1.00 19.07 O ANISOU 16 OE1 GLN A 1 2309 2378 2560 -29 2 -275 O ATOM 17 NE2 GLN A 1 -6.372 -10.606 42.781 1.00 17.16 N ANISOU 17 NE2 GLN A 1 2071 2173 2274 -39 5 -215 N ATOM 18 N ILE A 2 -1.368 -11.655 41.068 1.00 12.12 N ANISOU 18 N ILE A 2 1422 1503 1681 -34 -69 -166 N ATOM 19 CA ILE A 2 -1.209 -13.029 40.584 1.00 11.06 C ANISOU 19 CA ILE A 2 1299 1363 1540 -19 -74 -124 C ATOM 20 C ILE A 2 -1.779 -14.011 41.625 1.00 10.94 C ANISOU 20 C ILE A 2 1306 1371 1481 -14 -73 -103 C ATOM 21 O ILE A 2 -1.653 -13.760 42.824 1.00 11.13 O ANISOU 21 O ILE A 2 1329 1429 1472 -16 -79 -120 O ATOM 22 CB ILE A 2 0.287 -13.347 40.270 1.00 11.20 C ANISOU 22 CB ILE A 2 1301 1393 1561 -7 -96 -118 C ATOM 23 CG1 ILE A 2 1.180 -13.032 41.479 1.00 10.39 C ANISOU 23 CG1 ILE A 2 1184 1336 1426 -6 -117 -142 C ATOM 24 CG2 ILE A 2 0.748 -12.587 39.010 1.00 11.08 C ANISOU 24 CG2 ILE A 2 1269 1352 1590 -18 -91 -129 C ATOM 25 CD1 ILE A 2 2.669 -13.010 41.189 1.00 10.22 C ANISOU 25 CD1 ILE A 2 1135 1340 1410 1 -138 -150 C ATOM 26 N PRO A 3 -2.389 -15.138 41.184 1.00 10.29 N ANISOU 26 N PRO A 3 1246 1269 1394 -11 -63 -68 N ATOM 27 CA PRO A 3 -2.536 -15.667 39.823 1.00 9.57 C ANISOU 27 CA PRO A 3 1160 1141 1334 -8 -58 -46 C ATOM 28 C PRO A 3 -3.471 -14.902 38.881 1.00 8.80 C ANISOU 28 C PRO A 3 1051 1020 1273 -20 -38 -59 C ATOM 29 O PRO A 3 -3.409 -15.124 37.676 1.00 8.76 O ANISOU 29 O PRO A 3 1046 987 1297 -16 -36 -47 O ATOM 30 CB PRO A 3 -3.078 -17.093 40.053 1.00 10.04 C ANISOU 30 CB PRO A 3 1256 1193 1366 -8 -53 -9 C ATOM 31 CG PRO A 3 -3.763 -17.032 41.365 1.00 10.54 C ANISOU 31 CG PRO A 3 1328 1286 1389 -22 -44 -14 C ATOM 32 CD PRO A 3 -2.940 -16.072 42.188 1.00 10.51 C ANISOU 32 CD PRO A 3 1302 1315 1376 -14 -59 -45 C ATOM 33 N LEU A 4 -4.318 -14.017 39.403 1.00 8.47 N ANISOU 33 N LEU A 4 1000 990 1229 -30 -25 -86 N ATOM 34 CA LEU A 4 -5.309 -13.306 38.571 1.00 7.80 C ANISOU 34 CA LEU A 4 905 886 1173 -34 -9 -99 C ATOM 35 C LEU A 4 -4.783 -12.847 37.193 1.00 7.35 C ANISOU 35 C LEU A 4 841 794 1157 -27 -13 -97 C ATOM 36 O LEU A 4 -5.420 -13.100 36.166 1.00 7.22 O ANISOU 36 O LEU A 4 826 758 1158 -26 -5 -84 O ATOM 37 CB LEU A 4 -5.911 -12.111 39.327 1.00 7.52 C ANISOU 37 CB LEU A 4 858 866 1132 -34 -1 -137 C ATOM 38 CG LEU A 4 -6.879 -11.225 38.540 1.00 7.80 C ANISOU 38 CG LEU A 4 885 883 1196 -27 12 -154 C ATOM 39 CD1 LEU A 4 -8.147 -11.996 38.088 1.00 6.65 C ANISOU 39 CD1 LEU A 4 735 746 1046 -30 28 -137 C ATOM 40 CD2 LEU A 4 -7.243 -9.959 39.328 1.00 7.65 C ANISOU 40 CD2 LEU A 4 860 875 1171 -20 17 -196 C ATOM 41 N CYS A 5 -3.637 -12.173 37.190 1.00 6.92 N ANISOU 41 N CYS A 5 779 736 1113 -27 -26 -112 N ATOM 42 CA CYS A 5 -3.090 -11.567 35.976 1.00 6.70 C ANISOU 42 CA CYS A 5 746 680 1121 -27 -27 -113 C ATOM 43 C CYS A 5 -1.934 -12.346 35.358 1.00 6.10 C ANISOU 43 C CYS A 5 665 603 1048 -22 -39 -92 C ATOM 44 O CYS A 5 -1.294 -11.858 34.425 1.00 5.79 O ANISOU 44 O CYS A 5 618 548 1033 -27 -39 -94 O ATOM 45 CB CYS A 5 -2.670 -10.109 36.243 1.00 6.78 C ANISOU 45 CB CYS A 5 751 683 1143 -37 -28 -148 C ATOM 46 SG CYS A 5 -4.071 -9.001 36.538 1.00 6.98 S ANISOU 46 SG CYS A 5 785 695 1173 -31 -14 -175 S ATOM 47 N ALA A 6 -1.679 -13.557 35.854 1.00 6.13 N ANISOU 47 N ALA A 6 677 626 1027 -12 -47 -72 N ATOM 48 CA ALA A 6 -0.585 -14.407 35.331 1.00 6.07 C ANISOU 48 CA ALA A 6 667 621 1019 3 -60 -53 C ATOM 49 C ALA A 6 -0.494 -14.456 33.799 1.00 5.88 C ANISOU 49 C ALA A 6 640 569 1025 5 -53 -42 C ATOM 50 O ALA A 6 0.595 -14.298 33.233 1.00 6.20 O ANISOU 50 O ALA A 6 664 617 1077 8 -60 -46 O ATOM 51 CB ALA A 6 -0.664 -15.821 35.913 1.00 6.42 C ANISOU 51 CB ALA A 6 734 674 1032 19 -68 -27 C ATOM 52 N ASN A 7 -1.635 -14.627 33.132 1.00 6.02 N ANISOU 52 N ASN A 7 670 562 1053 2 -39 -32 N ATOM 53 CA ASN A 7 -1.670 -14.807 31.672 1.00 5.76 C ANISOU 53 CA ASN A 7 639 505 1043 5 -33 -20 C ATOM 54 C ASN A 7 -1.620 -13.514 30.857 1.00 5.95 C ANISOU 54 C ASN A 7 653 514 1094 -5 -25 -34 C ATOM 55 O ASN A 7 -1.513 -13.560 29.629 1.00 6.10 O ANISOU 55 O ASN A 7 672 516 1129 -2 -21 -24 O ATOM 56 CB ASN A 7 -2.891 -15.623 31.256 1.00 5.78 C ANISOU 56 CB ASN A 7 660 493 1044 5 -24 -3 C ATOM 57 CG ASN A 7 -2.841 -17.055 31.763 1.00 5.89 C ANISOU 57 CG ASN A 7 696 510 1032 12 -30 17 C ATOM 58 OD1 ASN A 7 -1.807 -17.729 31.683 1.00 4.40 O ANISOU 58 OD1 ASN A 7 513 323 837 30 -43 27 O ATOM 59 ND2 ASN A 7 -3.970 -17.531 32.280 1.00 4.84 N ANISOU 59 ND2 ASN A 7 578 377 883 -1 -22 23 N ATOM 60 N LEU A 8 -1.699 -12.371 31.530 1.00 5.80 N ANISOU 60 N LEU A 8 629 498 1078 -17 -24 -57 N ATOM 61 CA LEU A 8 -1.559 -11.074 30.864 1.00 6.14 C ANISOU 61 CA LEU A 8 671 518 1143 -28 -17 -70 C ATOM 62 C LEU A 8 -0.106 -10.644 30.752 1.00 6.44 C ANISOU 62 C LEU A 8 694 566 1186 -44 -22 -79 C ATOM 63 O LEU A 8 0.186 -9.582 30.207 1.00 7.09 O ANISOU 63 O LEU A 8 780 629 1285 -61 -15 -88 O ATOM 64 CB LEU A 8 -2.346 -9.982 31.603 1.00 6.00 C ANISOU 64 CB LEU A 8 661 492 1126 -32 -12 -94 C ATOM 65 CG LEU A 8 -3.829 -9.747 31.294 1.00 6.18 C ANISOU 65 CG LEU A 8 695 500 1154 -17 -3 -93 C ATOM 66 CD1 LEU A 8 -4.033 -9.195 29.881 1.00 5.26 C ANISOU 66 CD1 LEU A 8 589 350 1059 -12 2 -83 C ATOM 67 CD2 LEU A 8 -4.661 -10.999 31.522 1.00 5.28 C ANISOU 67 CD2 LEU A 8 578 407 1023 -9 -2 -78 C ATOM 68 N VAL A 9 0.801 -11.467 31.264 1.00 6.65 N ANISOU 68 N VAL A 9 705 626 1196 -38 -34 -76 N ATOM 69 CA VAL A 9 2.209 -11.091 31.332 1.00 6.95 C ANISOU 69 CA VAL A 9 719 689 1234 -53 -41 -90 C ATOM 70 C VAL A 9 2.965 -11.536 30.077 1.00 6.89 C ANISOU 70 C VAL A 9 699 685 1236 -49 -37 -76 C ATOM 71 O VAL A 9 3.085 -12.737 29.804 1.00 6.57 O ANISOU 71 O VAL A 9 657 654 1185 -22 -43 -58 O ATOM 72 CB VAL A 9 2.897 -11.607 32.629 1.00 6.98 C ANISOU 72 CB VAL A 9 706 737 1210 -45 -59 -101 C ATOM 73 CG1 VAL A 9 4.346 -11.169 32.672 1.00 6.90 C ANISOU 73 CG1 VAL A 9 661 761 1198 -62 -67 -121 C ATOM 74 CG2 VAL A 9 2.162 -11.099 33.864 1.00 7.15 C ANISOU 74 CG2 VAL A 9 740 759 1219 -51 -61 -118 C ATOM 75 N PRO A 10 3.476 -10.556 29.311 1.00 7.04 N ANISOU 75 N PRO A 10 711 693 1271 -77 -26 -84 N ATOM 76 CA PRO A 10 4.245 -10.839 28.092 1.00 7.14 C ANISOU 76 CA PRO A 10 709 713 1289 -79 -18 -72 C ATOM 77 C PRO A 10 5.541 -11.594 28.380 1.00 7.28 C ANISOU 77 C PRO A 10 689 786 1291 -67 -31 -79 C ATOM 78 O PRO A 10 6.156 -11.391 29.436 1.00 7.63 O ANISOU 78 O PRO A 10 713 863 1322 -75 -44 -100 O ATOM 79 CB PRO A 10 4.560 -9.438 27.539 1.00 7.38 C ANISOU 79 CB PRO A 10 744 724 1336 -121 -3 -83 C ATOM 80 CG PRO A 10 3.501 -8.532 28.146 1.00 7.40 C ANISOU 80 CG PRO A 10 779 688 1346 -129 -1 -93 C ATOM 81 CD PRO A 10 3.275 -9.107 29.521 1.00 7.12 C ANISOU 81 CD PRO A 10 734 677 1293 -110 -17 -103 C ATOM 82 N VAL A 11 5.929 -12.478 27.464 1.00 7.07 N ANISOU 82 N VAL A 11 654 771 1263 -43 -29 -65 N ATOM 83 CA VAL A 11 7.266 -13.113 27.493 1.00 7.48 C ANISOU 83 CA VAL A 11 665 878 1298 -27 -39 -74 C ATOM 84 C VAL A 11 7.840 -13.134 26.074 1.00 7.08 C ANISOU 84 C VAL A 11 600 836 1256 -32 -23 -68 C ATOM 85 O VAL A 11 7.074 -13.135 25.104 1.00 6.61 O ANISOU 85 O VAL A 11 568 736 1207 -32 -9 -50 O ATOM 86 CB VAL A 11 7.255 -14.555 28.105 1.00 7.46 C ANISOU 86 CB VAL A 11 669 890 1275 27 -60 -63 C ATOM 87 CG1 VAL A 11 6.843 -14.516 29.551 1.00 8.17 C ANISOU 87 CG1 VAL A 11 771 982 1352 29 -75 -69 C ATOM 88 CG2 VAL A 11 6.335 -15.490 27.327 1.00 7.98 C ANISOU 88 CG2 VAL A 11 772 915 1346 54 -55 -37 C ATOM 89 N PRO A 12 9.185 -13.134 25.937 1.00 7.39 N ANISOU 89 N PRO A 12 591 932 1284 -38 -24 -86 N ATOM 90 CA PRO A 12 9.736 -13.157 24.578 1.00 7.39 C ANISOU 90 CA PRO A 12 574 945 1287 -45 -5 -81 C ATOM 91 C PRO A 12 9.263 -14.355 23.742 1.00 7.42 C ANISOU 91 C PRO A 12 601 930 1289 4 -5 -60 C ATOM 92 O PRO A 12 9.047 -15.452 24.278 1.00 7.02 O ANISOU 92 O PRO A 12 563 878 1228 52 -24 -54 O ATOM 93 CB PRO A 12 11.250 -13.202 24.813 1.00 8.06 C ANISOU 93 CB PRO A 12 597 1110 1356 -48 -10 -107 C ATOM 94 CG PRO A 12 11.430 -12.546 26.151 1.00 8.20 C ANISOU 94 CG PRO A 12 603 1144 1370 -73 -25 -128 C ATOM 95 CD PRO A 12 10.246 -13.022 26.954 1.00 7.45 C ANISOU 95 CD PRO A 12 555 1000 1276 -42 -40 -112 C ATOM 96 N ILE A 13 9.084 -14.130 22.439 1.00 7.49 N ANISOU 96 N ILE A 13 620 921 1305 -10 16 -49 N ATOM 97 CA ILE A 13 8.559 -15.154 21.546 1.00 7.26 C ANISOU 97 CA ILE A 13 615 870 1273 30 17 -32 C ATOM 98 C ILE A 13 9.674 -16.069 21.050 1.00 7.90 C ANISOU 98 C ILE A 13 661 1003 1337 67 15 -43 C ATOM 99 O ILE A 13 10.636 -15.616 20.415 1.00 8.48 O ANISOU 99 O ILE A 13 695 1121 1406 46 31 -55 O ATOM 100 CB ILE A 13 7.770 -14.545 20.354 1.00 7.10 C ANISOU 100 CB ILE A 13 624 808 1264 4 38 -15 C ATOM 101 CG1 ILE A 13 6.438 -13.955 20.845 1.00 6.29 C ANISOU 101 CG1 ILE A 13 563 651 1177 -11 35 -4 C ATOM 102 CG2 ILE A 13 7.523 -15.609 19.282 1.00 6.65 C ANISOU 102 CG2 ILE A 13 582 744 1200 41 41 -4 C ATOM 103 CD1 ILE A 13 5.738 -13.038 19.863 1.00 4.46 C ANISOU 103 CD1 ILE A 13 358 382 954 -38 52 10 C ATOM 104 N THR A 14 9.539 -17.353 21.362 1.00 7.79 N ANISOU 104 N THR A 14 663 984 1313 123 -4 -39 N ATOM 105 CA THR A 14 10.484 -18.377 20.921 1.00 8.29 C ANISOU 105 CA THR A 14 702 1090 1359 174 -9 -50 C ATOM 106 C THR A 14 9.939 -19.122 19.705 1.00 8.19 C ANISOU 106 C THR A 14 722 1044 1347 197 1 -38 C ATOM 107 O THR A 14 8.766 -18.956 19.329 1.00 7.78 O ANISOU 107 O THR A 14 711 937 1306 177 8 -21 O ATOM 108 CB THR A 14 10.744 -19.393 22.036 1.00 8.48 C ANISOU 108 CB THR A 14 731 1123 1368 228 -38 -53 C ATOM 109 OG1 THR A 14 9.525 -20.080 22.343 1.00 8.69 O ANISOU 109 OG1 THR A 14 819 1084 1398 243 -48 -32 O ATOM 110 CG2 THR A 14 11.258 -18.691 23.302 1.00 8.47 C ANISOU 110 CG2 THR A 14 697 1158 1362 207 -51 -67 C ATOM 111 N ASN A 15 10.793 -19.936 19.091 1.00 8.64 N ANISOU 111 N ASN A 15 758 1138 1387 241 1 -51 N ATOM 112 CA ASN A 15 10.383 -20.811 17.995 1.00 8.61 C ANISOU 112 CA ASN A 15 786 1107 1379 271 7 -46 C ATOM 113 C ASN A 15 9.358 -21.864 18.394 1.00 8.39 C ANISOU 113 C ASN A 15 820 1016 1352 302 -11 -32 C ATOM 114 O ASN A 15 8.463 -22.176 17.602 1.00 8.13 O ANISOU 114 O ASN A 15 826 940 1325 296 -4 -22 O ATOM 115 CB ASN A 15 11.595 -21.446 17.314 1.00 9.03 C ANISOU 115 CB ASN A 15 800 1218 1412 317 10 -68 C ATOM 116 CG ASN A 15 12.360 -20.451 16.458 1.00 9.93 C ANISOU 116 CG ASN A 15 862 1387 1523 274 38 -79 C ATOM 117 OD1 ASN A 15 11.921 -19.310 16.274 1.00 10.79 O ANISOU 117 OD1 ASN A 15 975 1481 1646 211 55 -66 O ATOM 118 ND2 ASN A 15 13.504 -20.872 15.929 1.00 8.45 N ANISOU 118 ND2 ASN A 15 628 1266 1316 309 45 -102 N ATOM 119 N ALA A 16 9.486 -22.402 19.608 1.00 8.56 N ANISOU 119 N ALA A 16 852 1034 1368 332 -34 -31 N ATOM 120 CA ALA A 16 8.483 -23.315 20.166 1.00 8.85 C ANISOU 120 CA ALA A 16 951 1008 1402 349 -49 -14 C ATOM 121 C ALA A 16 7.111 -22.630 20.244 1.00 8.66 C ANISOU 121 C ALA A 16 954 939 1397 293 -40 3 C ATOM 122 O ALA A 16 6.083 -23.218 19.893 1.00 8.60 O ANISOU 122 O ALA A 16 993 883 1392 289 -39 14 O ATOM 123 CB ALA A 16 8.916 -23.809 21.550 1.00 9.07 C ANISOU 123 CB ALA A 16 984 1047 1417 384 -75 -13 C ATOM 124 N THR A 17 7.104 -21.377 20.696 1.00 8.83 N ANISOU 124 N THR A 17 947 979 1430 249 -33 2 N ATOM 125 CA THR A 17 5.887 -20.563 20.694 1.00 8.55 C ANISOU 125 CA THR A 17 930 907 1411 201 -23 14 C ATOM 126 C THR A 17 5.339 -20.319 19.279 1.00 7.99 C ANISOU 126 C THR A 17 869 820 1348 184 -5 19 C ATOM 127 O THR A 17 4.119 -20.328 19.075 1.00 7.80 O ANISOU 127 O THR A 17 876 758 1330 167 -3 29 O ATOM 128 CB THR A 17 6.098 -19.239 21.475 1.00 9.02 C ANISOU 128 CB THR A 17 959 988 1479 163 -20 9 C ATOM 129 OG1 THR A 17 6.155 -19.544 22.876 1.00 10.57 O ANISOU 129 OG1 THR A 17 1161 1189 1667 176 -39 9 O ATOM 130 CG2 THR A 17 4.945 -18.239 21.231 1.00 9.07 C ANISOU 130 CG2 THR A 17 984 961 1503 120 -8 18 C ATOM 131 N LEU A 18 6.228 -20.120 18.307 1.00 7.48 N ANISOU 131 N LEU A 18 776 789 1278 188 7 10 N ATOM 132 CA LEU A 18 5.790 -19.946 16.919 1.00 7.17 C ANISOU 132 CA LEU A 18 746 738 1240 176 23 15 C ATOM 133 C LEU A 18 5.162 -21.233 16.364 1.00 7.40 C ANISOU 133 C LEU A 18 815 736 1261 207 17 16 C ATOM 134 O LEU A 18 4.119 -21.192 15.694 1.00 7.26 O ANISOU 134 O LEU A 18 823 690 1247 190 21 24 O ATOM 135 CB LEU A 18 6.930 -19.429 16.029 1.00 7.08 C ANISOU 135 CB LEU A 18 695 775 1220 169 41 5 C ATOM 136 CG LEU A 18 7.375 -17.977 16.308 1.00 7.41 C ANISOU 136 CG LEU A 18 706 839 1270 121 54 5 C ATOM 137 CD1 LEU A 18 8.657 -17.583 15.538 1.00 5.53 C ANISOU 137 CD1 LEU A 18 423 657 1020 110 74 -7 C ATOM 138 CD2 LEU A 18 6.241 -16.976 16.046 1.00 5.47 C ANISOU 138 CD2 LEU A 18 490 551 1038 82 62 23 C ATOM 139 N ASP A 19 5.782 -22.372 16.665 1.00 7.28 N ANISOU 139 N ASP A 19 806 727 1234 252 4 6 N ATOM 140 CA ASP A 19 5.216 -23.671 16.324 1.00 7.68 C ANISOU 140 CA ASP A 19 904 739 1277 280 -4 6 C ATOM 141 C ASP A 19 3.841 -23.849 16.953 1.00 7.76 C ANISOU 141 C ASP A 19 954 700 1294 254 -12 20 C ATOM 142 O ASP A 19 2.919 -24.350 16.317 1.00 7.74 O ANISOU 142 O ASP A 19 984 665 1290 245 -10 21 O ATOM 143 CB ASP A 19 6.133 -24.791 16.822 1.00 7.90 C ANISOU 143 CB ASP A 19 939 773 1289 338 -20 -5 C ATOM 144 CG ASP A 19 7.450 -24.845 16.076 1.00 9.21 C ANISOU 144 CG ASP A 19 1064 993 1443 372 -12 -24 C ATOM 145 OD1 ASP A 19 8.394 -25.454 16.616 1.00 11.09 O ANISOU 145 OD1 ASP A 19 1290 1254 1668 422 -26 -35 O ATOM 146 OD2 ASP A 19 7.546 -24.287 14.957 1.00 8.85 O ANISOU 146 OD2 ASP A 19 996 969 1397 352 7 -29 O ATOM 147 N ARG A 20 3.725 -23.440 18.217 1.00 7.98 N ANISOU 147 N ARG A 20 976 727 1327 241 -20 28 N ATOM 148 CA ARG A 20 2.499 -23.592 18.986 1.00 7.90 C ANISOU 148 CA ARG A 20 998 681 1321 216 -25 39 C ATOM 149 C ARG A 20 1.298 -22.875 18.323 1.00 7.46 C ANISOU 149 C ARG A 20 944 614 1278 176 -14 44 C ATOM 150 O ARG A 20 0.172 -23.350 18.394 1.00 7.22 O ANISOU 150 O ARG A 20 942 554 1246 159 -16 48 O ATOM 151 CB ARG A 20 2.745 -23.105 20.416 1.00 7.88 C ANISOU 151 CB ARG A 20 982 692 1320 210 -33 44 C ATOM 152 CG ARG A 20 1.538 -23.094 21.331 1.00 8.58 C ANISOU 152 CG ARG A 20 1096 754 1411 181 -36 55 C ATOM 153 CD ARG A 20 1.920 -22.573 22.703 1.00 9.08 C ANISOU 153 CD ARG A 20 1142 837 1470 179 -44 56 C ATOM 154 NE ARG A 20 0.741 -22.397 23.541 1.00 10.06 N ANISOU 154 NE ARG A 20 1285 944 1595 148 -42 64 N ATOM 155 CZ ARG A 20 0.759 -22.390 24.871 1.00 11.61 C ANISOU 155 CZ ARG A 20 1485 1146 1780 147 -50 69 C ATOM 156 NH1 ARG A 20 1.903 -22.552 25.532 1.00 12.16 N ANISOU 156 NH1 ARG A 20 1544 1239 1838 176 -64 66 N ATOM 157 NH2 ARG A 20 -0.376 -22.224 25.543 1.00 12.40 N ANISOU 157 NH2 ARG A 20 1598 1234 1878 117 -46 74 N ATOM 158 N ILE A 21 1.553 -21.753 17.656 1.00 7.04 N ANISOU 158 N ILE A 21 859 584 1232 161 -2 42 N ATOM 159 CA ILE A 21 0.472 -20.944 17.095 1.00 6.67 C ANISOU 159 CA ILE A 21 813 528 1194 131 5 48 C ATOM 160 C ILE A 21 0.238 -21.235 15.612 1.00 6.66 C ANISOU 160 C ILE A 21 821 525 1186 136 12 45 C ATOM 161 O ILE A 21 -0.668 -20.665 14.990 1.00 6.31 O ANISOU 161 O ILE A 21 779 477 1144 118 16 49 O ATOM 162 CB ILE A 21 0.690 -19.432 17.355 1.00 6.28 C ANISOU 162 CB ILE A 21 736 494 1155 109 13 51 C ATOM 163 CG1 ILE A 21 1.843 -18.882 16.502 1.00 6.81 C ANISOU 163 CG1 ILE A 21 779 589 1220 111 25 48 C ATOM 164 CG2 ILE A 21 0.948 -19.191 18.838 1.00 6.29 C ANISOU 164 CG2 ILE A 21 729 500 1161 105 5 50 C ATOM 165 CD1 ILE A 21 1.975 -17.344 16.537 1.00 6.44 C ANISOU 165 CD1 ILE A 21 716 548 1183 81 36 53 C ATOM 166 N THR A 22 1.054 -22.133 15.063 1.00 6.99 N ANISOU 166 N THR A 22 867 573 1215 164 12 36 N ATOM 167 CA THR A 22 0.941 -22.551 13.668 1.00 7.56 C ANISOU 167 CA THR A 22 950 647 1277 173 18 29 C ATOM 168 C THR A 22 -0.320 -23.385 13.466 1.00 7.57 C ANISOU 168 C THR A 22 986 615 1274 163 10 26 C ATOM 169 O THR A 22 -0.614 -24.276 14.263 1.00 7.60 O ANISOU 169 O THR A 22 1017 594 1278 165 0 25 O ATOM 170 CB THR A 22 2.168 -23.373 13.220 1.00 8.04 C ANISOU 170 CB THR A 22 1007 724 1325 212 19 15 C ATOM 171 OG1 THR A 22 3.359 -22.617 13.461 1.00 9.06 O ANISOU 171 OG1 THR A 22 1096 892 1455 216 27 15 O ATOM 172 CG2 THR A 22 2.082 -23.725 11.725 1.00 7.92 C ANISOU 172 CG2 THR A 22 1000 714 1294 220 27 6 C ATOM 173 N GLY A 23 -1.055 -23.078 12.400 1.00 7.56 N ANISOU 173 N GLY A 23 986 619 1268 149 14 25 N ATOM 174 CA GLY A 23 -2.253 -23.827 12.029 1.00 7.53 C ANISOU 174 CA GLY A 23 1009 594 1257 135 6 18 C ATOM 175 C GLY A 23 -3.484 -22.947 11.923 1.00 7.28 C ANISOU 175 C GLY A 23 966 571 1230 107 5 25 C ATOM 176 O GLY A 23 -3.382 -21.733 11.725 1.00 6.91 O ANISOU 176 O GLY A 23 896 541 1188 105 10 36 O ATOM 177 N LYS A 24 -4.652 -23.566 12.063 1.00 7.07 N ANISOU 177 N LYS A 24 955 532 1200 86 -3 17 N ATOM 178 CA LYS A 24 -5.920 -22.869 11.888 1.00 7.05 C ANISOU 178 CA LYS A 24 937 544 1197 66 -7 18 C ATOM 179 C LYS A 24 -6.522 -22.474 13.234 1.00 6.95 C ANISOU 179 C LYS A 24 914 529 1197 48 -9 24 C ATOM 180 O LYS A 24 -6.568 -23.283 14.161 1.00 6.83 O ANISOU 180 O LYS A 24 917 496 1184 36 -10 22 O ATOM 181 CB LYS A 24 -6.892 -23.749 11.101 1.00 7.25 C ANISOU 181 CB LYS A 24 978 570 1208 49 -14 1 C ATOM 182 CG LYS A 24 -8.249 -23.127 10.821 1.00 6.66 C ANISOU 182 CG LYS A 24 881 522 1129 32 -21 -3 C ATOM 183 CD LYS A 24 -9.162 -24.167 10.195 1.00 6.71 C ANISOU 183 CD LYS A 24 900 531 1118 8 -29 -25 C ATOM 184 CE LYS A 24 -10.463 -23.563 9.714 1.00 6.57 C ANISOU 184 CE LYS A 24 854 552 1092 -3 -38 -33 C ATOM 185 NZ LYS A 24 -11.328 -24.586 9.078 1.00 5.65 N ANISOU 185 NZ LYS A 24 746 444 957 -32 -46 -59 N ATOM 186 N TRP A 25 -6.989 -21.229 13.322 1.00 6.78 N ANISOU 186 N TRP A 25 869 525 1182 48 -8 31 N ATOM 187 CA TRP A 25 -7.603 -20.705 14.542 1.00 6.51 C ANISOU 187 CA TRP A 25 821 494 1158 35 -9 34 C ATOM 188 C TRP A 25 -8.989 -20.123 14.268 1.00 6.36 C ANISOU 188 C TRP A 25 782 499 1134 28 -15 27 C ATOM 189 O TRP A 25 -9.232 -19.607 13.188 1.00 6.49 O ANISOU 189 O TRP A 25 793 529 1143 41 -19 28 O ATOM 190 CB TRP A 25 -6.691 -19.637 15.153 1.00 6.76 C ANISOU 190 CB TRP A 25 843 523 1203 48 -3 46 C ATOM 191 CG TRP A 25 -5.380 -20.205 15.620 1.00 7.07 C ANISOU 191 CG TRP A 25 892 549 1244 57 0 49 C ATOM 192 CD1 TRP A 25 -4.184 -20.193 14.949 1.00 6.44 C ANISOU 192 CD1 TRP A 25 813 472 1164 74 5 52 C ATOM 193 CD2 TRP A 25 -5.145 -20.889 16.855 1.00 7.34 C ANISOU 193 CD2 TRP A 25 936 572 1280 51 -2 49 C ATOM 194 NE1 TRP A 25 -3.216 -20.828 15.703 1.00 8.03 N ANISOU 194 NE1 TRP A 25 1019 667 1366 84 4 51 N ATOM 195 CE2 TRP A 25 -3.783 -21.267 16.874 1.00 8.29 C ANISOU 195 CE2 TRP A 25 1061 688 1399 72 -1 51 C ATOM 196 CE3 TRP A 25 -5.958 -21.227 17.948 1.00 8.07 C ANISOU 196 CE3 TRP A 25 1034 660 1370 32 -4 47 C ATOM 197 CZ2 TRP A 25 -3.213 -21.959 17.950 1.00 8.80 C ANISOU 197 CZ2 TRP A 25 1139 743 1461 79 -5 53 C ATOM 198 CZ3 TRP A 25 -5.391 -21.919 19.019 1.00 8.88 C ANISOU 198 CZ3 TRP A 25 1154 750 1469 34 -6 51 C ATOM 199 CH2 TRP A 25 -4.027 -22.272 19.010 1.00 8.51 C ANISOU 199 CH2 TRP A 25 1114 697 1422 60 -8 55 C ATOM 200 N PHE A 26 -9.891 -20.211 15.247 1.00 6.20 N ANISOU 200 N PHE A 26 753 489 1115 9 -15 20 N ATOM 201 CA PHE A 26 -11.220 -19.601 15.139 1.00 6.03 C ANISOU 201 CA PHE A 26 704 499 1088 7 -21 10 C ATOM 202 C PHE A 26 -11.353 -18.488 16.168 1.00 5.65 C ANISOU 202 C PHE A 26 640 456 1051 18 -18 14 C ATOM 203 O PHE A 26 -11.025 -18.683 17.334 1.00 5.39 O ANISOU 203 O PHE A 26 612 413 1025 5 -11 16 O ATOM 204 CB PHE A 26 -12.331 -20.626 15.385 1.00 6.34 C ANISOU 204 CB PHE A 26 737 556 1115 -29 -22 -7 C ATOM 205 CG PHE A 26 -12.426 -21.707 14.339 1.00 6.45 C ANISOU 205 CG PHE A 26 769 567 1117 -45 -27 -17 C ATOM 206 CD1 PHE A 26 -11.603 -22.831 14.400 1.00 5.74 C ANISOU 206 CD1 PHE A 26 715 439 1025 -56 -22 -14 C ATOM 207 CD2 PHE A 26 -13.370 -21.619 13.321 1.00 6.38 C ANISOU 207 CD2 PHE A 26 739 592 1092 -45 -37 -32 C ATOM 208 CE1 PHE A 26 -11.709 -23.841 13.445 1.00 7.22 C ANISOU 208 CE1 PHE A 26 923 620 1200 -69 -26 -27 C ATOM 209 CE2 PHE A 26 -13.481 -22.616 12.368 1.00 8.38 C ANISOU 209 CE2 PHE A 26 1008 843 1332 -62 -42 -45 C ATOM 210 CZ PHE A 26 -12.648 -23.735 12.428 1.00 7.66 C ANISOU 210 CZ PHE A 26 958 710 1242 -75 -35 -44 C ATOM 211 N TYR A 27 -11.836 -17.327 15.735 1.00 5.79 N ANISOU 211 N TYR A 27 643 489 1069 43 -24 14 N ATOM 212 CA TYR A 27 -12.072 -16.209 16.645 1.00 6.00 C ANISOU 212 CA TYR A 27 656 518 1104 58 -22 13 C ATOM 213 C TYR A 27 -13.377 -16.450 17.410 1.00 6.09 C ANISOU 213 C TYR A 27 640 566 1107 44 -23 -7 C ATOM 214 O TYR A 27 -14.437 -16.664 16.803 1.00 6.38 O ANISOU 214 O TYR A 27 656 637 1130 43 -30 -20 O ATOM 215 CB TYR A 27 -12.057 -14.868 15.882 1.00 6.48 C ANISOU 215 CB TYR A 27 721 573 1167 95 -28 22 C ATOM 216 CG TYR A 27 -12.778 -13.738 16.579 1.00 7.60 C ANISOU 216 CG TYR A 27 850 725 1312 118 -31 13 C ATOM 217 CD1 TYR A 27 -13.778 -13.023 15.923 1.00 9.07 C ANISOU 217 CD1 TYR A 27 1025 935 1488 152 -44 7 C ATOM 218 CD2 TYR A 27 -12.475 -13.397 17.899 1.00 8.67 C ANISOU 218 CD2 TYR A 27 986 850 1460 111 -23 8 C ATOM 219 CE1 TYR A 27 -14.459 -11.997 16.557 1.00 10.78 C ANISOU 219 CE1 TYR A 27 1230 1159 1706 182 -47 -3 C ATOM 220 CE2 TYR A 27 -13.152 -12.378 18.543 1.00 10.92 C ANISOU 220 CE2 TYR A 27 1260 1143 1746 135 -25 -4 C ATOM 221 CZ TYR A 27 -14.143 -11.683 17.865 1.00 11.14 C ANISOU 221 CZ TYR A 27 1278 1191 1764 172 -37 -10 C ATOM 222 OH TYR A 27 -14.816 -10.675 18.497 1.00 13.68 O ANISOU 222 OH TYR A 27 1591 1521 2087 204 -40 -25 O ATOM 223 N ILE A 28 -13.279 -16.442 18.740 1.00 5.51 N ANISOU 223 N ILE A 28 565 489 1039 31 -14 -10 N ATOM 224 CA ILE A 28 -14.382 -16.840 19.620 1.00 5.57 C ANISOU 224 CA ILE A 28 547 533 1035 7 -9 -27 C ATOM 225 C ILE A 28 -15.098 -15.663 20.286 1.00 5.76 C ANISOU 225 C ILE A 28 546 583 1061 34 -9 -41 C ATOM 226 O ILE A 28 -16.325 -15.565 20.223 1.00 6.10 O ANISOU 226 O ILE A 28 555 673 1091 37 -12 -61 O ATOM 227 CB ILE A 28 -13.899 -17.834 20.719 1.00 5.63 C ANISOU 227 CB ILE A 28 573 525 1040 -30 3 -22 C ATOM 228 CG1 ILE A 28 -13.223 -19.071 20.095 1.00 5.13 C ANISOU 228 CG1 ILE A 28 540 433 975 -50 2 -11 C ATOM 229 CG2 ILE A 28 -15.041 -18.201 21.699 1.00 5.06 C ANISOU 229 CG2 ILE A 28 476 492 952 -60 12 -39 C ATOM 230 CD1 ILE A 28 -14.119 -19.945 19.240 1.00 5.43 C ANISOU 230 CD1 ILE A 28 572 491 999 -75 -1 -23 C ATOM 231 N ALA A 29 -14.326 -14.777 20.911 1.00 5.52 N ANISOU 231 N ALA A 29 530 524 1042 53 -6 -35 N ATOM 232 CA ALA A 29 -14.862 -13.711 21.736 1.00 5.76 C ANISOU 232 CA ALA A 29 544 570 1073 77 -5 -50 C ATOM 233 C ALA A 29 -13.832 -12.606 21.920 1.00 6.08 C ANISOU 233 C ALA A 29 613 568 1131 101 -6 -41 C ATOM 234 O ALA A 29 -12.625 -12.849 21.802 1.00 5.97 O ANISOU 234 O ALA A 29 624 520 1126 87 -3 -24 O ATOM 235 CB ALA A 29 -15.272 -14.272 23.094 1.00 5.87 C ANISOU 235 CB ALA A 29 543 610 1076 46 8 -63 C ATOM 236 N SER A 30 -14.311 -11.398 22.212 1.00 6.43 N ANISOU 236 N SER A 30 652 614 1177 136 -9 -54 N ATOM 237 CA SER A 30 -13.443 -10.262 22.536 1.00 6.85 C ANISOU 237 CA SER A 30 734 624 1244 153 -8 -51 C ATOM 238 C SER A 30 -14.167 -9.214 23.383 1.00 7.37 C ANISOU 238 C SER A 30 792 702 1308 184 -8 -75 C ATOM 239 O SER A 30 -15.402 -9.151 23.402 1.00 7.42 O ANISOU 239 O SER A 30 767 750 1301 207 -12 -94 O ATOM 240 CB SER A 30 -12.893 -9.601 21.266 1.00 6.68 C ANISOU 240 CB SER A 30 742 566 1231 173 -15 -31 C ATOM 241 OG SER A 30 -13.938 -8.965 20.545 1.00 7.60 O ANISOU 241 OG SER A 30 852 697 1340 216 -27 -37 O ATOM 242 N ALA A 31 -13.377 -8.403 24.084 1.00 7.62 N ANISOU 242 N ALA A 31 848 697 1350 185 -4 -79 N ATOM 243 CA ALA A 31 -13.877 -7.252 24.820 1.00 8.62 C ANISOU 243 CA ALA A 31 979 821 1476 219 -5 -103 C ATOM 244 C ALA A 31 -12.774 -6.207 24.951 1.00 9.31 C ANISOU 244 C ALA A 31 1109 849 1579 218 -4 -99 C ATOM 245 O ALA A 31 -11.595 -6.551 25.141 1.00 8.63 O ANISOU 245 O ALA A 31 1036 743 1501 180 1 -86 O ATOM 246 CB ALA A 31 -14.405 -7.658 26.189 1.00 8.38 C ANISOU 246 CB ALA A 31 917 833 1432 205 5 -127 C ATOM 247 N PHE A 32 -13.180 -4.939 24.858 1.00 10.09 N ANISOU 247 N PHE A 32 1231 920 1680 262 -10 -111 N ATOM 248 CA PHE A 32 -12.272 -3.796 24.824 1.00 10.95 C ANISOU 248 CA PHE A 32 1392 966 1804 261 -10 -108 C ATOM 249 C PHE A 32 -12.898 -2.606 25.534 1.00 11.90 C ANISOU 249 C PHE A 32 1529 1070 1921 304 -12 -139 C ATOM 250 O PHE A 32 -14.122 -2.422 25.517 1.00 11.81 O ANISOU 250 O PHE A 32 1498 1090 1899 353 -19 -156 O ATOM 251 CB PHE A 32 -11.999 -3.343 23.381 1.00 11.23 C ANISOU 251 CB PHE A 32 1462 961 1843 275 -16 -79 C ATOM 252 CG PHE A 32 -11.470 -4.415 22.475 1.00 11.84 C ANISOU 252 CG PHE A 32 1525 1053 1920 243 -14 -51 C ATOM 253 CD1 PHE A 32 -12.336 -5.152 21.670 1.00 13.05 C ANISOU 253 CD1 PHE A 32 1650 1245 2062 261 -21 -43 C ATOM 254 CD2 PHE A 32 -10.103 -4.661 22.390 1.00 12.05 C ANISOU 254 CD2 PHE A 32 1565 1057 1956 196 -5 -35 C ATOM 255 CE1 PHE A 32 -11.854 -6.142 20.817 1.00 11.11 C ANISOU 255 CE1 PHE A 32 1396 1011 1814 233 -20 -20 C ATOM 256 CE2 PHE A 32 -9.613 -5.638 21.542 1.00 11.45 C ANISOU 256 CE2 PHE A 32 1476 996 1878 173 -3 -12 C ATOM 257 CZ PHE A 32 -10.493 -6.378 20.750 1.00 11.82 C ANISOU 257 CZ PHE A 32 1501 1076 1914 192 -10 -5 C ATOM 258 N ARG A 33 -12.039 -1.775 26.113 1.00 12.82 N ANISOU 258 N ARG A 33 1683 1139 2048 287 -8 -148 N ATOM 259 CA ARG A 33 -12.440 -0.488 26.650 1.00 13.76 C ANISOU 259 CA ARG A 33 1836 1223 2168 327 -11 -177 C ATOM 260 C ARG A 33 -12.358 0.589 25.568 1.00 14.32 C ANISOU 260 C ARG A 33 1968 1227 2246 358 -18 -159 C ATOM 261 O ARG A 33 -13.001 1.632 25.675 1.00 14.37 O ANISOU 261 O ARG A 33 2008 1204 2250 412 -25 -178 O ATOM 262 CB ARG A 33 -11.594 -0.143 27.873 1.00 14.21 C ANISOU 262 CB ARG A 33 1905 1263 2229 289 -3 -200 C ATOM 263 CG ARG A 33 -12.035 -0.895 29.123 1.00 15.25 C ANISOU 263 CG ARG A 33 1987 1461 2346 281 3 -226 C ATOM 264 CD ARG A 33 -11.181 -0.540 30.333 1.00 17.91 C ANISOU 264 CD ARG A 33 2336 1785 2683 246 8 -250 C ATOM 265 NE ARG A 33 -11.660 -1.192 31.555 1.00 19.42 N ANISOU 265 NE ARG A 33 2484 2039 2855 241 14 -274 N ATOM 266 CZ ARG A 33 -11.172 -0.977 32.775 1.00 20.15 C ANISOU 266 CZ ARG A 33 2579 2138 2940 219 18 -301 C ATOM 267 NH1 ARG A 33 -10.179 -0.114 32.969 1.00 20.66 N ANISOU 267 NH1 ARG A 33 2684 2150 3016 196 16 -311 N ATOM 268 NH2 ARG A 33 -11.689 -1.620 33.812 1.00 20.20 N ANISOU 268 NH2 ARG A 33 2547 2205 2923 217 24 -318 N ATOM 269 N ASN A 34 -11.574 0.315 24.523 1.00 14.45 N ANISOU 269 N ASN A 34 2001 1221 2269 326 -16 -122 N ATOM 270 CA ASN A 34 -11.534 1.139 23.317 1.00 15.11 C ANISOU 270 CA ASN A 34 2140 1248 2354 351 -22 -96 C ATOM 271 C ASN A 34 -12.893 1.127 22.613 1.00 16.21 C ANISOU 271 C ASN A 34 2266 1416 2479 422 -38 -93 C ATOM 272 O ASN A 34 -13.382 0.062 22.227 1.00 15.97 O ANISOU 272 O ASN A 34 2182 1447 2439 422 -41 -85 O ATOM 273 CB ASN A 34 -10.451 0.618 22.363 1.00 14.43 C ANISOU 273 CB ASN A 34 2060 1151 2272 298 -14 -58 C ATOM 274 CG ASN A 34 -10.332 1.452 21.096 1.00 13.91 C ANISOU 274 CG ASN A 34 2056 1027 2203 316 -18 -27 C ATOM 275 OD1 ASN A 34 -10.617 0.974 19.996 1.00 13.22 O ANISOU 275 OD1 ASN A 34 1959 959 2105 331 -23 0 O ATOM 276 ND2 ASN A 34 -9.907 2.705 21.245 1.00 12.23 N ANISOU 276 ND2 ASN A 34 1910 741 1995 313 -14 -30 N ATOM 277 N GLU A 35 -13.495 2.306 22.450 1.00 17.80 N ANISOU 277 N GLU A 35 2516 1573 2675 484 -48 -102 N ATOM 278 CA GLU A 35 -14.849 2.405 21.891 1.00 19.51 C ANISOU 278 CA GLU A 35 2715 1823 2874 563 -67 -105 C ATOM 279 C GLU A 35 -14.934 2.125 20.395 1.00 19.67 C ANISOU 279 C GLU A 35 2745 1845 2884 576 -76 -66 C ATOM 280 O GLU A 35 -15.945 1.605 19.929 1.00 19.62 O ANISOU 280 O GLU A 35 2693 1900 2862 617 -90 -68 O ATOM 281 CB GLU A 35 -15.519 3.739 22.239 1.00 20.55 C ANISOU 281 CB GLU A 35 2896 1910 3001 638 -77 -130 C ATOM 282 CG GLU A 35 -16.472 3.649 23.445 1.00 22.98 C ANISOU 282 CG GLU A 35 3151 2277 3302 675 -78 -180 C ATOM 283 CD GLU A 35 -17.570 2.595 23.263 1.00 25.83 C ANISOU 283 CD GLU A 35 3426 2741 3647 697 -85 -188 C ATOM 284 OE1 GLU A 35 -17.637 1.651 24.090 1.00 26.31 O ANISOU 284 OE1 GLU A 35 3425 2866 3707 654 -73 -206 O ATOM 285 OE2 GLU A 35 -18.354 2.700 22.287 1.00 27.02 O ANISOU 285 OE2 GLU A 35 3573 2910 3782 755 -103 -176 O ATOM 286 N GLU A 36 -13.876 2.466 19.658 1.00 20.37 N ANISOU 286 N GLU A 36 2890 1872 2979 537 -69 -31 N ATOM 287 CA GLU A 36 -13.781 2.157 18.226 1.00 21.00 C ANISOU 287 CA GLU A 36 2980 1953 3046 538 -75 9 C ATOM 288 C GLU A 36 -13.857 0.651 17.953 1.00 20.91 C ANISOU 288 C GLU A 36 2893 2020 3031 504 -73 13 C ATOM 289 O GLU A 36 -14.610 0.208 17.074 1.00 21.08 O ANISOU 289 O GLU A 36 2890 2083 3035 538 -87 23 O ATOM 290 CB GLU A 36 -12.493 2.733 17.626 1.00 21.03 C ANISOU 290 CB GLU A 36 3052 1881 3056 488 -61 44 C ATOM 291 CG GLU A 36 -12.559 4.225 17.293 1.00 22.34 C ANISOU 291 CG GLU A 36 3311 1960 3216 530 -67 56 C ATOM 292 CD GLU A 36 -12.277 5.123 18.488 1.00 23.26 C ANISOU 292 CD GLU A 36 3465 2023 3349 521 -59 24 C ATOM 293 OE1 GLU A 36 -12.050 4.596 19.600 1.00 22.69 O ANISOU 293 OE1 GLU A 36 3342 1989 3291 485 -50 -7 O ATOM 294 OE2 GLU A 36 -12.279 6.366 18.312 1.00 24.94 O ANISOU 294 OE2 GLU A 36 3762 2154 3558 551 -63 31 O ATOM 295 N TYR A 37 -13.080 -0.126 18.707 1.00 20.71 N ANISOU 295 N TYR A 37 2835 2014 3021 438 -56 4 N ATOM 296 CA TYR A 37 -13.088 -1.582 18.563 1.00 20.83 C ANISOU 296 CA TYR A 37 2788 2095 3033 404 -53 6 C ATOM 297 C TYR A 37 -14.395 -2.211 19.037 1.00 21.01 C ANISOU 297 C TYR A 37 2749 2189 3045 436 -63 -22 C ATOM 298 O TYR A 37 -14.802 -3.246 18.522 1.00 20.87 O ANISOU 298 O TYR A 37 2689 2223 3017 427 -67 -18 O ATOM 299 CB TYR A 37 -11.884 -2.220 19.259 1.00 20.37 C ANISOU 299 CB TYR A 37 2716 2035 2990 332 -35 5 C ATOM 300 CG TYR A 37 -10.594 -2.158 18.458 1.00 21.04 C ANISOU 300 CG TYR A 37 2835 2081 3079 288 -24 36 C ATOM 301 CD1 TYR A 37 -10.611 -2.011 17.066 1.00 22.08 C ANISOU 301 CD1 TYR A 37 2992 2199 3197 304 -28 67 C ATOM 302 CD2 TYR A 37 -9.355 -2.281 19.090 1.00 21.41 C ANISOU 302 CD2 TYR A 37 2882 2113 3139 231 -8 34 C ATOM 303 CE1 TYR A 37 -9.423 -1.964 16.328 1.00 23.04 C ANISOU 303 CE1 TYR A 37 3142 2293 3320 260 -14 94 C ATOM 304 CE2 TYR A 37 -8.165 -2.241 18.362 1.00 22.32 C ANISOU 304 CE2 TYR A 37 3020 2204 3257 188 4 58 C ATOM 305 CZ TYR A 37 -8.204 -2.081 16.984 1.00 23.05 C ANISOU 305 CZ TYR A 37 3139 2283 3336 202 3 89 C ATOM 306 OH TYR A 37 -7.025 -2.046 16.266 1.00 23.71 O ANISOU 306 OH TYR A 37 3242 2349 3418 157 18 112 O ATOM 307 N ASN A 38 -15.055 -1.573 20.000 1.00 21.79 N ANISOU 307 N ASN A 38 2843 2291 3144 472 -66 -53 N ATOM 308 CA ASN A 38 -16.361 -2.028 20.477 1.00 22.61 C ANISOU 308 CA ASN A 38 2888 2469 3235 505 -73 -84 C ATOM 309 C ASN A 38 -17.469 -1.994 19.423 1.00 22.99 C ANISOU 309 C ASN A 38 2918 2554 3262 564 -94 -80 C ATOM 310 O ASN A 38 -18.272 -2.923 19.348 1.00 23.22 O ANISOU 310 O ASN A 38 2887 2658 3279 561 -98 -93 O ATOM 311 CB ASN A 38 -16.793 -1.261 21.729 1.00 23.12 C ANISOU 311 CB ASN A 38 2952 2531 3301 535 -71 -120 C ATOM 312 CG ASN A 38 -16.295 -1.905 23.008 1.00 23.51 C ANISOU 312 CG ASN A 38 2973 2600 3358 478 -52 -138 C ATOM 313 OD1 ASN A 38 -15.663 -2.963 22.980 1.00 25.36 O ANISOU 313 OD1 ASN A 38 3188 2851 3597 419 -43 -122 O ATOM 314 ND2 ASN A 38 -16.573 -1.270 24.137 1.00 24.49 N ANISOU 314 ND2 ASN A 38 3099 2723 3482 498 -48 -171 N ATOM 315 N LYS A 39 -17.503 -0.936 18.613 1.00 23.27 N ANISOU 315 N LYS A 39 3009 2540 3292 617 -107 -63 N ATOM 316 CA LYS A 39 -18.490 -0.817 17.537 1.00 23.42 C ANISOU 316 CA LYS A 39 3018 2592 3287 680 -131 -56 C ATOM 317 C LYS A 39 -18.097 -1.569 16.254 1.00 22.73 C ANISOU 317 C LYS A 39 2930 2513 3191 649 -134 -22 C ATOM 318 O LYS A 39 -18.968 -1.972 15.473 1.00 22.89 O ANISOU 318 O LYS A 39 2915 2590 3190 681 -152 -24 O ATOM 319 CB LYS A 39 -18.790 0.655 17.226 1.00 24.11 C ANISOU 319 CB LYS A 39 3171 2622 3368 760 -147 -51 C ATOM 320 CG LYS A 39 -20.036 1.216 17.933 1.00 25.71 C ANISOU 320 CG LYS A 39 3345 2865 3560 838 -161 -93 C ATOM 321 CD LYS A 39 -21.334 0.889 17.169 1.00 26.38 C ANISOU 321 CD LYS A 39 3374 3033 3615 900 -186 -103 C ATOM 322 CE LYS A 39 -22.552 1.517 17.833 1.00 27.23 C ANISOU 322 CE LYS A 39 3450 3186 3709 985 -199 -147 C ATOM 323 NZ LYS A 39 -23.719 1.565 16.907 1.00 27.36 N ANISOU 323 NZ LYS A 39 3431 3268 3694 1064 -230 -153 N ATOM 324 N SER A 40 -16.798 -1.751 16.033 1.00 21.62 N ANISOU 324 N SER A 40 2827 2322 3066 588 -117 6 N ATOM 325 CA SER A 40 -16.343 -2.398 14.806 1.00 20.90 C ANISOU 325 CA SER A 40 2740 2236 2964 561 -118 37 C ATOM 326 C SER A 40 -16.276 -3.920 14.925 1.00 19.87 C ANISOU 326 C SER A 40 2548 2164 2836 504 -110 27 C ATOM 327 O SER A 40 -16.625 -4.625 13.976 1.00 20.02 O ANISOU 327 O SER A 40 2545 2223 2839 504 -119 34 O ATOM 328 CB SER A 40 -15.003 -1.825 14.333 1.00 20.86 C ANISOU 328 CB SER A 40 2804 2154 2968 527 -104 72 C ATOM 329 OG SER A 40 -13.930 -2.349 15.085 1.00 20.44 O ANISOU 329 OG SER A 40 2741 2088 2937 456 -81 68 O ATOM 330 N VAL A 41 -15.829 -4.423 16.077 1.00 18.79 N ANISOU 330 N VAL A 41 2390 2032 2719 456 -92 10 N ATOM 331 CA VAL A 41 -15.732 -5.870 16.299 1.00 17.65 C ANISOU 331 CA VAL A 41 2197 1933 2575 403 -83 2 C ATOM 332 C VAL A 41 -17.141 -6.458 16.440 1.00 17.51 C ANISOU 332 C VAL A 41 2120 1992 2542 423 -95 -26 C ATOM 333 O VAL A 41 -17.379 -7.626 16.126 1.00 16.76 O ANISOU 333 O VAL A 41 1990 1940 2439 390 -94 -30 O ATOM 334 CB VAL A 41 -14.835 -6.227 17.527 1.00 17.47 C ANISOU 334 CB VAL A 41 2173 1892 2573 350 -63 -5 C ATOM 335 CG1 VAL A 41 -14.814 -7.719 17.771 1.00 16.49 C ANISOU 335 CG1 VAL A 41 2007 1810 2447 301 -56 -12 C ATOM 336 CG2 VAL A 41 -13.405 -5.737 17.322 1.00 17.22 C ANISOU 336 CG2 VAL A 41 2191 1797 2555 323 -52 20 C ATOM 337 N GLN A 42 -18.068 -5.615 16.891 1.00 17.54 N ANISOU 337 N GLN A 42 2114 2013 2539 478 -105 -48 N ATOM 338 CA GLN A 42 -19.488 -5.945 16.998 1.00 17.76 C ANISOU 338 CA GLN A 42 2080 2120 2547 507 -117 -78 C ATOM 339 C GLN A 42 -20.079 -6.455 15.673 1.00 17.20 C ANISOU 339 C GLN A 42 1988 2093 2455 521 -135 -71 C ATOM 340 O GLN A 42 -21.036 -7.233 15.672 1.00 17.29 O ANISOU 340 O GLN A 42 1940 2180 2451 511 -141 -96 O ATOM 341 CB GLN A 42 -20.245 -4.701 17.476 1.00 18.71 C ANISOU 341 CB GLN A 42 2205 2241 2662 581 -128 -99 C ATOM 342 CG GLN A 42 -21.679 -4.916 17.915 1.00 20.98 C ANISOU 342 CG GLN A 42 2421 2619 2931 612 -136 -139 C ATOM 343 CD GLN A 42 -22.210 -3.720 18.680 1.00 23.35 C ANISOU 343 CD GLN A 42 2729 2912 3230 680 -140 -164 C ATOM 344 OE1 GLN A 42 -22.933 -2.886 18.129 1.00 25.15 O ANISOU 344 OE1 GLN A 42 2964 3150 3442 760 -163 -170 O ATOM 345 NE2 GLN A 42 -21.829 -3.614 19.950 1.00 23.50 N ANISOU 345 NE2 GLN A 42 2752 2913 3263 652 -120 -180 N ATOM 346 N GLU A 43 -19.501 -6.025 14.554 1.00 16.29 N ANISOU 346 N GLU A 43 1921 1932 2335 538 -144 -39 N ATOM 347 CA GLU A 43 -19.969 -6.443 13.227 1.00 15.93 C ANISOU 347 CA GLU A 43 1862 1925 2265 554 -163 -30 C ATOM 348 C GLU A 43 -19.429 -7.803 12.751 1.00 14.57 C ANISOU 348 C GLU A 43 1676 1765 2093 484 -153 -23 C ATOM 349 O GLU A 43 -19.892 -8.338 11.754 1.00 14.47 O ANISOU 349 O GLU A 43 1643 1794 2059 488 -167 -24 O ATOM 350 CB GLU A 43 -19.676 -5.354 12.192 1.00 16.45 C ANISOU 350 CB GLU A 43 1990 1941 2319 609 -178 2 C ATOM 351 CG GLU A 43 -20.437 -4.059 12.452 1.00 18.49 C ANISOU 351 CG GLU A 43 2264 2192 2570 692 -195 -8 C ATOM 352 CD GLU A 43 -21.930 -4.290 12.637 1.00 20.40 C ANISOU 352 CD GLU A 43 2432 2527 2791 736 -214 -48 C ATOM 353 OE1 GLU A 43 -22.430 -4.064 13.762 1.00 19.93 O ANISOU 353 OE1 GLU A 43 2343 2490 2741 748 -208 -79 O ATOM 354 OE2 GLU A 43 -22.596 -4.718 11.663 1.00 22.49 O ANISOU 354 OE2 GLU A 43 2666 2850 3029 754 -235 -50 O ATOM 355 N ILE A 44 -18.461 -8.362 13.466 1.00 13.25 N ANISOU 355 N ILE A 44 1520 1564 1949 425 -129 -17 N ATOM 356 CA ILE A 44 -17.859 -9.631 13.051 1.00 12.35 C ANISOU 356 CA ILE A 44 1402 1454 1836 365 -120 -10 C ATOM 357 C ILE A 44 -18.708 -10.808 13.548 1.00 11.93 C ANISOU 357 C ILE A 44 1292 1463 1776 328 -118 -41 C ATOM 358 O ILE A 44 -18.882 -11.000 14.759 1.00 11.70 O ANISOU 358 O ILE A 44 1243 1444 1759 305 -105 -58 O ATOM 359 CB ILE A 44 -16.378 -9.749 13.501 1.00 11.85 C ANISOU 359 CB ILE A 44 1377 1328 1797 323 -98 10 C ATOM 360 CG1 ILE A 44 -15.566 -8.569 12.948 1.00 11.74 C ANISOU 360 CG1 ILE A 44 1419 1256 1786 351 -97 39 C ATOM 361 CG2 ILE A 44 -15.776 -11.094 13.056 1.00 11.39 C ANISOU 361 CG2 ILE A 44 1315 1274 1737 271 -89 15 C ATOM 362 CD1 ILE A 44 -14.149 -8.458 13.497 1.00 11.65 C ANISOU 362 CD1 ILE A 44 1439 1190 1796 312 -76 54 C ATOM 363 N GLN A 45 -19.244 -11.571 12.600 1.00 11.26 N ANISOU 363 N GLN A 45 1185 1422 1672 318 -130 -49 N ATOM 364 CA GLN A 45 -20.103 -12.712 12.905 1.00 11.18 C ANISOU 364 CA GLN A 45 1123 1472 1652 275 -128 -79 C ATOM 365 C GLN A 45 -19.286 -13.987 13.087 1.00 10.19 C ANISOU 365 C GLN A 45 1015 1319 1537 206 -110 -73 C ATOM 366 O GLN A 45 -19.666 -14.872 13.853 1.00 10.14 O ANISOU 366 O GLN A 45 984 1336 1531 159 -99 -91 O ATOM 367 CB GLN A 45 -21.149 -12.903 11.799 1.00 11.75 C ANISOU 367 CB GLN A 45 1161 1610 1695 296 -152 -95 C ATOM 368 CG GLN A 45 -22.257 -11.849 11.784 1.00 14.04 C ANISOU 368 CG GLN A 45 1417 1948 1968 366 -173 -111 C ATOM 369 CD GLN A 45 -22.739 -11.524 10.371 1.00 16.92 C ANISOU 369 CD GLN A 45 1780 2345 2304 415 -201 -107 C ATOM 370 OE1 GLN A 45 -21.943 -11.172 9.495 1.00 18.06 O ANISOU 370 OE1 GLN A 45 1975 2441 2446 433 -206 -75 O ATOM 371 NE2 GLN A 45 -24.044 -11.636 10.149 1.00 16.41 N ANISOU 371 NE2 GLN A 45 1654 2368 2214 436 -221 -140 N ATOM 372 N ALA A 46 -18.177 -14.079 12.357 1.00 9.47 N ANISOU 372 N ALA A 46 968 1179 1452 203 -107 -47 N ATOM 373 CA ALA A 46 -17.214 -15.164 12.509 1.00 8.84 C ANISOU 373 CA ALA A 46 911 1064 1382 152 -91 -39 C ATOM 374 C ALA A 46 -15.881 -14.760 11.902 1.00 8.54 C ANISOU 374 C ALA A 46 919 972 1353 165 -86 -10 C ATOM 375 O ALA A 46 -15.802 -13.762 11.181 1.00 8.26 O ANISOU 375 O ALA A 46 900 929 1312 207 -95 6 O ATOM 376 CB ALA A 46 -17.730 -16.449 11.858 1.00 8.76 C ANISOU 376 CB ALA A 46 885 1087 1355 114 -97 -58 C ATOM 377 N THR A 47 -14.836 -15.527 12.224 1.00 8.15 N ANISOU 377 N THR A 47 892 888 1317 131 -71 -2 N ATOM 378 CA THR A 47 -13.523 -15.444 11.561 1.00 7.63 C ANISOU 378 CA THR A 47 861 782 1255 134 -64 21 C ATOM 379 C THR A 47 -12.711 -16.682 11.891 1.00 7.26 C ANISOU 379 C THR A 47 828 716 1216 97 -52 18 C ATOM 380 O THR A 47 -12.660 -17.118 13.047 1.00 7.35 O ANISOU 380 O THR A 47 834 719 1239 74 -44 12 O ATOM 381 CB THR A 47 -12.700 -14.173 11.955 1.00 7.26 C ANISOU 381 CB THR A 47 836 698 1223 156 -56 42 C ATOM 382 OG1 THR A 47 -13.381 -13.004 11.510 1.00 7.55 O ANISOU 382 OG1 THR A 47 873 743 1251 197 -68 47 O ATOM 383 CG2 THR A 47 -11.330 -14.170 11.300 1.00 6.80 C ANISOU 383 CG2 THR A 47 808 609 1168 150 -45 62 C ATOM 384 N PHE A 48 -12.095 -17.261 10.869 1.00 7.18 N ANISOU 384 N PHE A 48 835 698 1196 94 -51 23 N ATOM 385 CA PHE A 48 -11.064 -18.268 11.081 1.00 7.14 C ANISOU 385 CA PHE A 48 849 667 1198 73 -40 24 C ATOM 386 C PHE A 48 -9.870 -17.904 10.214 1.00 7.66 C ANISOU 386 C PHE A 48 934 716 1261 89 -32 41 C ATOM 387 O PHE A 48 -10.034 -17.316 9.141 1.00 8.23 O ANISOU 387 O PHE A 48 1008 801 1317 109 -38 49 O ATOM 388 CB PHE A 48 -11.580 -19.686 10.797 1.00 7.04 C ANISOU 388 CB PHE A 48 838 664 1173 45 -44 3 C ATOM 389 CG PHE A 48 -12.027 -19.909 9.378 1.00 6.58 C ANISOU 389 CG PHE A 48 778 630 1092 52 -55 -6 C ATOM 390 CD1 PHE A 48 -13.367 -19.772 9.034 1.00 5.31 C ANISOU 390 CD1 PHE A 48 592 511 916 51 -69 -22 C ATOM 391 CD2 PHE A 48 -11.110 -20.281 8.392 1.00 5.32 C ANISOU 391 CD2 PHE A 48 641 458 923 61 -51 -2 C ATOM 392 CE1 PHE A 48 -13.795 -19.985 7.727 1.00 4.93 C ANISOU 392 CE1 PHE A 48 541 490 843 58 -82 -32 C ATOM 393 CE2 PHE A 48 -11.526 -20.494 7.076 1.00 5.66 C ANISOU 393 CE2 PHE A 48 684 525 940 68 -61 -11 C ATOM 394 CZ PHE A 48 -12.870 -20.345 6.746 1.00 6.38 C ANISOU 394 CZ PHE A 48 751 658 1016 66 -78 -26 C ATOM 395 N PHE A 49 -8.669 -18.222 10.688 1.00 7.77 N ANISOU 395 N PHE A 49 959 706 1286 83 -20 47 N ATOM 396 CA PHE A 49 -7.452 -17.827 9.979 1.00 7.82 C ANISOU 396 CA PHE A 49 977 705 1290 95 -10 61 C ATOM 397 C PHE A 49 -6.337 -18.841 10.114 1.00 7.94 C ANISOU 397 C PHE A 49 1001 709 1307 90 -1 55 C ATOM 398 O PHE A 49 -6.356 -19.679 11.011 1.00 8.71 O ANISOU 398 O PHE A 49 1102 795 1413 79 -3 46 O ATOM 399 CB PHE A 49 -6.968 -16.447 10.444 1.00 7.52 C ANISOU 399 CB PHE A 49 938 654 1264 101 -2 79 C ATOM 400 CG PHE A 49 -6.542 -16.392 11.895 1.00 7.27 C ANISOU 400 CG PHE A 49 901 609 1254 89 2 76 C ATOM 401 CD1 PHE A 49 -7.437 -15.995 12.882 1.00 7.00 C ANISOU 401 CD1 PHE A 49 857 574 1229 87 -4 70 C ATOM 402 CD2 PHE A 49 -5.235 -16.708 12.271 1.00 6.85 C ANISOU 402 CD2 PHE A 49 848 547 1207 83 13 78 C ATOM 403 CE1 PHE A 49 -7.043 -15.927 14.216 1.00 6.80 C ANISOU 403 CE1 PHE A 49 827 539 1219 77 0 67 C ATOM 404 CE2 PHE A 49 -4.836 -16.640 13.606 1.00 6.33 C ANISOU 404 CE2 PHE A 49 775 473 1156 75 14 75 C ATOM 405 CZ PHE A 49 -5.735 -16.249 14.577 1.00 6.78 C ANISOU 405 CZ PHE A 49 827 528 1222 71 8 70 C ATOM 406 N TYR A 50 -5.363 -18.739 9.217 1.00 8.26 N ANISOU 406 N TYR A 50 1046 754 1337 100 9 62 N ATOM 407 CA TYR A 50 -4.209 -19.611 9.206 1.00 8.37 C ANISOU 407 CA TYR A 50 1065 765 1350 105 17 54 C ATOM 408 C TYR A 50 -2.943 -18.819 9.549 1.00 8.29 C ANISOU 408 C TYR A 50 1043 757 1348 106 31 66 C ATOM 409 O TYR A 50 -2.727 -17.722 9.022 1.00 8.46 O ANISOU 409 O TYR A 50 1062 785 1366 103 40 81 O ATOM 410 CB TYR A 50 -4.066 -20.269 7.828 1.00 8.74 C ANISOU 410 CB TYR A 50 1122 825 1373 115 18 45 C ATOM 411 CG TYR A 50 -5.137 -21.292 7.500 1.00 8.52 C ANISOU 411 CG TYR A 50 1108 796 1336 109 5 26 C ATOM 412 CD1 TYR A 50 -6.390 -20.896 7.017 1.00 8.48 C ANISOU 412 CD1 TYR A 50 1098 805 1321 103 -7 25 C ATOM 413 CD2 TYR A 50 -4.893 -22.658 7.659 1.00 8.41 C ANISOU 413 CD2 TYR A 50 1111 765 1320 110 3 7 C ATOM 414 CE1 TYR A 50 -7.375 -21.835 6.708 1.00 9.11 C ANISOU 414 CE1 TYR A 50 1184 890 1389 90 -19 4 C ATOM 415 CE2 TYR A 50 -5.873 -23.611 7.352 1.00 9.22 C ANISOU 415 CE2 TYR A 50 1229 862 1411 96 -9 -13 C ATOM 416 CZ TYR A 50 -7.110 -23.190 6.877 1.00 9.76 C ANISOU 416 CZ TYR A 50 1287 951 1470 82 -19 -15 C ATOM 417 OH TYR A 50 -8.083 -24.119 6.572 1.00 10.03 O ANISOU 417 OH TYR A 50 1331 986 1492 61 -30 -38 O ATOM 418 N PHE A 51 -2.127 -19.370 10.447 1.00 7.97 N ANISOU 418 N PHE A 51 998 712 1319 109 33 60 N ATOM 419 CA PHE A 51 -0.796 -18.829 10.747 1.00 7.95 C ANISOU 419 CA PHE A 51 977 722 1321 109 46 64 C ATOM 420 C PHE A 51 0.299 -19.744 10.189 1.00 8.07 C ANISOU 420 C PHE A 51 988 755 1323 129 52 52 C ATOM 421 O PHE A 51 0.381 -20.916 10.573 1.00 8.02 O ANISOU 421 O PHE A 51 992 739 1315 147 44 38 O ATOM 422 CB PHE A 51 -0.594 -18.711 12.263 1.00 7.88 C ANISOU 422 CB PHE A 51 960 704 1331 103 40 63 C ATOM 423 CG PHE A 51 -1.078 -17.411 12.868 1.00 8.47 C ANISOU 423 CG PHE A 51 1031 770 1419 84 41 74 C ATOM 424 CD1 PHE A 51 -1.171 -17.283 14.256 1.00 9.28 C ANISOU 424 CD1 PHE A 51 1128 864 1535 78 34 71 C ATOM 425 CD2 PHE A 51 -1.432 -16.321 12.068 1.00 7.46 C ANISOU 425 CD2 PHE A 51 908 640 1286 76 47 87 C ATOM 426 CE1 PHE A 51 -1.597 -16.077 14.844 1.00 9.28 C ANISOU 426 CE1 PHE A 51 1126 853 1545 63 35 77 C ATOM 427 CE2 PHE A 51 -1.854 -15.124 12.642 1.00 9.02 C ANISOU 427 CE2 PHE A 51 1109 823 1496 64 46 95 C ATOM 428 CZ PHE A 51 -1.940 -15.003 14.038 1.00 8.58 C ANISOU 428 CZ PHE A 51 1046 758 1455 58 40 88 C ATOM 429 N THR A 52 1.124 -19.225 9.282 1.00 8.00 N ANISOU 429 N THR A 52 966 773 1302 128 69 56 N ATOM 430 CA THR A 52 2.374 -19.907 8.908 1.00 8.08 C ANISOU 430 CA THR A 52 961 811 1299 149 78 41 C ATOM 431 C THR A 52 3.550 -19.003 9.256 1.00 7.77 C ANISOU 431 C THR A 52 889 801 1264 134 94 45 C ATOM 432 O THR A 52 3.942 -18.156 8.454 1.00 7.67 O ANISOU 432 O THR A 52 867 808 1239 114 112 55 O ATOM 433 CB THR A 52 2.449 -20.297 7.411 1.00 8.24 C ANISOU 433 CB THR A 52 988 850 1293 161 88 35 C ATOM 434 OG1 THR A 52 1.242 -20.959 7.019 1.00 9.22 O ANISOU 434 OG1 THR A 52 1142 949 1412 166 73 29 O ATOM 435 CG2 THR A 52 3.641 -21.241 7.157 1.00 9.01 C ANISOU 435 CG2 THR A 52 1070 975 1377 193 95 12 C ATOM 436 N PRO A 53 4.105 -19.169 10.468 1.00 7.68 N ANISOU 436 N PRO A 53 861 793 1266 139 86 38 N ATOM 437 CA PRO A 53 5.243 -18.369 10.893 1.00 7.63 C ANISOU 437 CA PRO A 53 818 819 1262 121 99 37 C ATOM 438 C PRO A 53 6.495 -18.718 10.105 1.00 8.00 C ANISOU 438 C PRO A 53 834 916 1288 136 115 22 C ATOM 439 O PRO A 53 6.696 -19.874 9.723 1.00 8.27 O ANISOU 439 O PRO A 53 873 959 1311 176 110 7 O ATOM 440 CB PRO A 53 5.432 -18.771 12.367 1.00 7.77 C ANISOU 440 CB PRO A 53 828 830 1293 134 81 29 C ATOM 441 CG PRO A 53 4.168 -19.458 12.760 1.00 7.56 C ANISOU 441 CG PRO A 53 839 758 1274 146 63 33 C ATOM 442 CD PRO A 53 3.699 -20.127 11.509 1.00 7.39 C ANISOU 442 CD PRO A 53 839 730 1239 160 66 31 C ATOM 443 N ASN A 54 7.314 -17.712 9.845 1.00 7.94 N ANISOU 443 N ASN A 54 799 943 1275 102 136 26 N ATOM 444 CA ASN A 54 8.629 -17.929 9.291 1.00 8.52 C ANISOU 444 CA ASN A 54 830 1078 1329 110 154 9 C ATOM 445 C ASN A 54 9.637 -17.615 10.381 1.00 8.70 C ANISOU 445 C ASN A 54 810 1136 1360 100 153 -4 C ATOM 446 O ASN A 54 9.842 -16.451 10.751 1.00 8.45 O ANISOU 446 O ASN A 54 767 1108 1337 50 163 5 O ATOM 447 CB ASN A 54 8.860 -17.052 8.058 1.00 8.69 C ANISOU 447 CB ASN A 54 850 1121 1332 73 184 22 C ATOM 448 CG ASN A 54 10.178 -17.360 7.361 1.00 9.26 C ANISOU 448 CG ASN A 54 876 1265 1378 81 206 2 C ATOM 449 OD1 ASN A 54 11.190 -17.671 8.006 1.00 9.19 O ANISOU 449 OD1 ASN A 54 822 1301 1369 96 204 -20 O ATOM 450 ND2 ASN A 54 10.172 -17.274 6.036 1.00 9.26 N ANISOU 450 ND2 ASN A 54 886 1282 1353 74 227 8 N ATOM 451 N LYS A 55 10.252 -18.669 10.904 1.00 9.06 N ANISOU 451 N LYS A 55 834 1208 1402 149 138 -26 N ATOM 452 CA LYS A 55 11.097 -18.551 12.085 1.00 9.43 C ANISOU 452 CA LYS A 55 840 1288 1454 151 128 -41 C ATOM 453 C LYS A 55 12.451 -17.906 11.787 1.00 10.08 C ANISOU 453 C LYS A 55 861 1448 1522 122 151 -56 C ATOM 454 O LYS A 55 13.144 -17.429 12.697 1.00 10.57 O ANISOU 454 O LYS A 55 884 1544 1588 103 147 -68 O ATOM 455 CB LYS A 55 11.266 -19.930 12.736 1.00 9.44 C ANISOU 455 CB LYS A 55 845 1289 1452 221 101 -56 C ATOM 456 CG LYS A 55 9.971 -20.465 13.394 1.00 9.11 C ANISOU 456 CG LYS A 55 862 1173 1426 235 78 -41 C ATOM 457 CD LYS A 55 10.122 -21.911 13.879 1.00 9.11 C ANISOU 457 CD LYS A 55 880 1162 1418 302 54 -53 C ATOM 458 CE LYS A 55 9.762 -22.925 12.796 1.00 9.47 C ANISOU 458 CE LYS A 55 961 1187 1452 338 57 -58 C ATOM 459 NZ LYS A 55 9.797 -24.318 13.338 1.00 9.96 N ANISOU 459 NZ LYS A 55 1055 1223 1507 401 33 -68 N ATOM 460 N THR A 56 12.824 -17.892 10.512 1.00 10.37 N ANISOU 460 N THR A 56 886 1517 1538 117 177 -59 N ATOM 461 CA THR A 56 14.104 -17.350 10.094 1.00 11.44 C ANISOU 461 CA THR A 56 960 1733 1654 86 204 -75 C ATOM 462 C THR A 56 13.984 -15.853 9.784 1.00 11.69 C ANISOU 462 C THR A 56 1000 1752 1689 0 230 -53 C ATOM 463 O THR A 56 14.988 -15.150 9.711 1.00 12.55 O ANISOU 463 O THR A 56 1061 1920 1787 -47 253 -64 O ATOM 464 CB THR A 56 14.688 -18.118 8.875 1.00 11.71 C ANISOU 464 CB THR A 56 972 1818 1658 123 222 -93 C ATOM 465 OG1 THR A 56 13.921 -17.831 7.702 1.00 12.37 O ANISOU 465 OG1 THR A 56 1101 1866 1734 101 239 -70 O ATOM 466 CG2 THR A 56 14.668 -19.634 9.117 1.00 12.12 C ANISOU 466 CG2 THR A 56 1033 1865 1707 213 194 -113 C ATOM 467 N GLU A 57 12.754 -15.376 9.617 1.00 11.14 N ANISOU 467 N GLU A 57 993 1606 1634 -19 226 -24 N ATOM 468 CA GLU A 57 12.508 -13.999 9.196 1.00 11.37 C ANISOU 468 CA GLU A 57 1047 1610 1664 -91 249 1 C ATOM 469 C GLU A 57 11.720 -13.197 10.223 1.00 10.91 C ANISOU 469 C GLU A 57 1023 1487 1634 -118 232 16 C ATOM 470 O GLU A 57 11.591 -11.981 10.082 1.00 11.05 O ANISOU 470 O GLU A 57 1064 1479 1654 -176 248 34 O ATOM 471 CB GLU A 57 11.779 -13.964 7.849 1.00 11.42 C ANISOU 471 CB GLU A 57 1098 1587 1654 -89 262 25 C ATOM 472 CG GLU A 57 12.617 -14.402 6.651 1.00 12.46 C ANISOU 472 CG GLU A 57 1198 1786 1752 -81 289 13 C ATOM 473 CD GLU A 57 11.840 -14.316 5.347 1.00 13.99 C ANISOU 473 CD GLU A 57 1439 1950 1926 -81 300 38 C ATOM 474 OE1 GLU A 57 11.024 -13.386 5.192 1.00 13.85 O ANISOU 474 OE1 GLU A 57 1471 1877 1915 -115 302 69 O ATOM 475 OE2 GLU A 57 12.030 -15.193 4.477 1.00 15.93 O ANISOU 475 OE2 GLU A 57 1675 2229 2147 -42 306 25 O ATOM 476 N ASP A 58 11.213 -13.876 11.255 1.00 10.18 N ANISOU 476 N ASP A 58 938 1370 1560 -75 201 8 N ATOM 477 CA ASP A 58 10.370 -13.243 12.279 1.00 9.77 C ANISOU 477 CA ASP A 58 918 1260 1532 -92 183 18 C ATOM 478 C ASP A 58 9.109 -12.656 11.633 1.00 9.01 C ANISOU 478 C ASP A 58 884 1099 1442 -103 186 48 C ATOM 479 O ASP A 58 8.737 -11.501 11.874 1.00 8.73 O ANISOU 479 O ASP A 58 874 1025 1416 -145 191 62 O ATOM 480 CB ASP A 58 11.152 -12.186 13.082 1.00 10.26 C ANISOU 480 CB ASP A 58 953 1343 1601 -148 191 8 C ATOM 481 CG ASP A 58 12.246 -12.798 13.968 1.00 11.85 C ANISOU 481 CG ASP A 58 1093 1611 1799 -129 180 -24 C ATOM 482 OD1 ASP A 58 12.476 -14.026 13.913 1.00 12.51 O ANISOU 482 OD1 ASP A 58 1157 1723 1873 -68 166 -36 O ATOM 483 OD2 ASP A 58 12.878 -12.040 14.732 1.00 14.17 O ANISOU 483 OD2 ASP A 58 1360 1928 2098 -173 182 -38 O ATOM 484 N THR A 59 8.482 -13.462 10.778 1.00 8.21 N ANISOU 484 N THR A 59 803 986 1331 -64 182 56 N ATOM 485 CA THR A 59 7.211 -13.100 10.154 1.00 7.74 C ANISOU 485 CA THR A 59 795 872 1272 -63 179 81 C ATOM 486 C THR A 59 6.208 -14.212 10.356 1.00 7.04 C ANISOU 486 C THR A 59 726 759 1190 -13 153 77 C ATOM 487 O THR A 59 6.580 -15.345 10.652 1.00 6.82 O ANISOU 487 O THR A 59 677 754 1160 22 143 58 O ATOM 488 CB THR A 59 7.338 -12.840 8.629 1.00 8.04 C ANISOU 488 CB THR A 59 847 924 1284 -76 202 96 C ATOM 489 OG1 THR A 59 7.975 -13.957 8.001 1.00 7.56 O ANISOU 489 OG1 THR A 59 757 912 1204 -43 207 78 O ATOM 490 CG2 THR A 59 8.144 -11.566 8.349 1.00 8.63 C ANISOU 490 CG2 THR A 59 917 1011 1349 -138 231 107 C ATOM 491 N ILE A 60 4.931 -13.881 10.216 1.00 6.36 N ANISOU 491 N ILE A 60 679 627 1110 -10 143 93 N ATOM 492 CA ILE A 60 3.888 -14.896 10.146 1.00 6.04 C ANISOU 492 CA ILE A 60 657 567 1071 28 123 90 C ATOM 493 C ILE A 60 3.036 -14.593 8.919 1.00 6.04 C ANISOU 493 C ILE A 60 688 552 1056 29 126 108 C ATOM 494 O ILE A 60 2.585 -13.457 8.731 1.00 6.00 O ANISOU 494 O ILE A 60 705 522 1052 9 131 127 O ATOM 495 CB ILE A 60 3.000 -14.941 11.421 1.00 5.61 C ANISOU 495 CB ILE A 60 613 479 1038 34 101 88 C ATOM 496 CG1 ILE A 60 3.854 -15.019 12.688 1.00 5.34 C ANISOU 496 CG1 ILE A 60 551 461 1016 29 98 73 C ATOM 497 CG2 ILE A 60 2.019 -16.128 11.357 1.00 5.63 C ANISOU 497 CG2 ILE A 60 632 468 1040 65 84 82 C ATOM 498 CD1 ILE A 60 3.139 -14.572 13.943 1.00 5.64 C ANISOU 498 CD1 ILE A 60 600 471 1074 21 84 73 C ATOM 499 N PHE A 61 2.850 -15.598 8.069 1.00 5.87 N ANISOU 499 N PHE A 61 669 543 1017 55 123 100 N ATOM 500 CA PHE A 61 1.927 -15.465 6.958 1.00 6.18 C ANISOU 500 CA PHE A 61 736 572 1039 62 121 113 C ATOM 501 C PHE A 61 0.509 -15.748 7.448 1.00 6.53 C ANISOU 501 C PHE A 61 799 586 1096 76 96 112 C ATOM 502 O PHE A 61 0.216 -16.828 7.974 1.00 6.11 O ANISOU 502 O PHE A 61 742 529 1051 93 83 94 O ATOM 503 CB PHE A 61 2.308 -16.375 5.792 1.00 6.21 C ANISOU 503 CB PHE A 61 737 607 1017 81 128 102 C ATOM 504 CG PHE A 61 1.492 -16.137 4.542 1.00 6.00 C ANISOU 504 CG PHE A 61 736 578 965 85 127 116 C ATOM 505 CD1 PHE A 61 0.880 -17.202 3.880 1.00 5.16 C ANISOU 505 CD1 PHE A 61 640 478 844 110 115 100 C ATOM 506 CD2 PHE A 61 1.327 -14.844 4.033 1.00 4.79 C ANISOU 506 CD2 PHE A 61 603 416 802 64 137 144 C ATOM 507 CE1 PHE A 61 0.115 -16.982 2.720 1.00 5.90 C ANISOU 507 CE1 PHE A 61 755 575 911 115 111 110 C ATOM 508 CE2 PHE A 61 0.566 -14.616 2.870 1.00 5.16 C ANISOU 508 CE2 PHE A 61 676 464 821 74 134 158 C ATOM 509 CZ PHE A 61 -0.039 -15.681 2.218 1.00 4.99 C ANISOU 509 CZ PHE A 61 657 456 784 100 120 141 C ATOM 510 N LEU A 62 -0.355 -14.752 7.290 1.00 6.97 N ANISOU 510 N LEU A 62 875 621 1153 70 91 130 N ATOM 511 CA LEU A 62 -1.740 -14.847 7.719 1.00 7.30 C ANISOU 511 CA LEU A 62 928 643 1204 82 70 127 C ATOM 512 C LEU A 62 -2.655 -15.011 6.507 1.00 7.84 C ANISOU 512 C LEU A 62 1012 720 1248 99 61 132 C ATOM 513 O LEU A 62 -2.514 -14.299 5.521 1.00 8.15 O ANISOU 513 O LEU A 62 1066 764 1267 98 70 150 O ATOM 514 CB LEU A 62 -2.141 -13.591 8.515 1.00 7.12 C ANISOU 514 CB LEU A 62 914 593 1198 72 67 140 C ATOM 515 CG LEU A 62 -3.629 -13.403 8.845 1.00 6.60 C ANISOU 515 CG LEU A 62 857 514 1137 89 47 138 C ATOM 516 CD1 LEU A 62 -4.053 -14.342 9.939 1.00 6.49 C ANISOU 516 CD1 LEU A 62 825 502 1140 90 35 118 C ATOM 517 CD2 LEU A 62 -3.937 -11.965 9.239 1.00 6.98 C ANISOU 517 CD2 LEU A 62 922 535 1194 87 47 153 C ATOM 518 N ARG A 63 -3.571 -15.968 6.587 1.00 8.28 N ANISOU 518 N ARG A 63 1065 779 1304 110 44 114 N ATOM 519 CA ARG A 63 -4.679 -16.066 5.643 1.00 8.92 C ANISOU 519 CA ARG A 63 1155 871 1363 124 29 114 C ATOM 520 C ARG A 63 -5.972 -16.013 6.447 1.00 8.79 C ANISOU 520 C ARG A 63 1132 848 1361 128 10 106 C ATOM 521 O ARG A 63 -6.347 -16.990 7.097 1.00 8.65 O ANISOU 521 O ARG A 63 1104 829 1352 121 3 86 O ATOM 522 CB ARG A 63 -4.593 -17.351 4.818 1.00 9.30 C ANISOU 522 CB ARG A 63 1203 938 1392 130 27 94 C ATOM 523 CG ARG A 63 -3.201 -17.626 4.277 1.00 10.54 C ANISOU 523 CG ARG A 63 1359 1108 1538 129 48 94 C ATOM 524 CD ARG A 63 -3.185 -18.642 3.145 1.00 13.51 C ANISOU 524 CD ARG A 63 1742 1505 1887 141 47 76 C ATOM 525 NE ARG A 63 -3.756 -19.946 3.486 1.00 15.58 N ANISOU 525 NE ARG A 63 2007 1759 2155 143 32 48 N ATOM 526 CZ ARG A 63 -3.171 -20.877 4.241 1.00 18.01 C ANISOU 526 CZ ARG A 63 2313 2052 2478 145 34 32 C ATOM 527 NH1 ARG A 63 -1.977 -20.661 4.792 1.00 18.29 N ANISOU 527 NH1 ARG A 63 2337 2088 2526 148 49 38 N ATOM 528 NH2 ARG A 63 -3.801 -22.031 4.462 1.00 17.64 N ANISOU 528 NH2 ARG A 63 2278 1991 2433 143 21 9 N ATOM 529 N GLU A 64 -6.630 -14.857 6.406 1.00 8.93 N ANISOU 529 N GLU A 64 1157 859 1376 139 3 122 N ATOM 530 CA GLU A 64 -7.816 -14.580 7.221 1.00 9.25 C ANISOU 530 CA GLU A 64 1187 899 1429 147 -13 114 C ATOM 531 C GLU A 64 -9.124 -14.697 6.429 1.00 9.02 C ANISOU 531 C GLU A 64 1152 897 1377 166 -33 107 C ATOM 532 O GLU A 64 -9.218 -14.232 5.296 1.00 9.29 O ANISOU 532 O GLU A 64 1202 942 1387 184 -37 121 O ATOM 533 CB GLU A 64 -7.707 -13.181 7.852 1.00 9.42 C ANISOU 533 CB GLU A 64 1221 894 1465 153 -9 131 C ATOM 534 CG GLU A 64 -8.729 -12.912 8.970 1.00 11.18 C ANISOU 534 CG GLU A 64 1429 1116 1704 161 -21 118 C ATOM 535 CD GLU A 64 -8.628 -11.507 9.561 1.00 14.24 C ANISOU 535 CD GLU A 64 1834 1474 2104 170 -18 132 C ATOM 536 OE1 GLU A 64 -7.519 -10.929 9.585 1.00 14.53 O ANISOU 536 OE1 GLU A 64 1890 1485 2147 154 -1 147 O ATOM 537 OE2 GLU A 64 -9.669 -10.978 10.010 1.00 15.97 O ANISOU 537 OE2 GLU A 64 2047 1695 2325 193 -31 125 O ATOM 538 N TYR A 65 -10.124 -15.313 7.055 1.00 8.72 N ANISOU 538 N TYR A 65 1092 876 1346 161 -46 84 N ATOM 539 CA TYR A 65 -11.436 -15.529 6.467 1.00 8.62 C ANISOU 539 CA TYR A 65 1063 900 1312 174 -67 70 C ATOM 540 C TYR A 65 -12.480 -14.933 7.389 1.00 8.93 C ANISOU 540 C TYR A 65 1082 950 1363 186 -77 62 C ATOM 541 O TYR A 65 -12.983 -15.609 8.283 1.00 8.46 O ANISOU 541 O TYR A 65 999 900 1314 164 -78 41 O ATOM 542 CB TYR A 65 -11.700 -17.026 6.320 1.00 8.55 C ANISOU 542 CB TYR A 65 1043 909 1297 147 -70 43 C ATOM 543 CG TYR A 65 -10.866 -17.700 5.261 1.00 8.20 C ANISOU 543 CG TYR A 65 1017 862 1236 142 -63 43 C ATOM 544 CD1 TYR A 65 -9.571 -18.150 5.545 1.00 7.43 C ANISOU 544 CD1 TYR A 65 935 736 1152 130 -44 47 C ATOM 545 CD2 TYR A 65 -11.372 -17.907 3.977 1.00 7.87 C ANISOU 545 CD2 TYR A 65 976 852 1162 153 -76 36 C ATOM 546 CE1 TYR A 65 -8.800 -18.774 4.575 1.00 6.10 C ANISOU 546 CE1 TYR A 65 781 571 966 131 -36 44 C ATOM 547 CE2 TYR A 65 -10.602 -18.535 2.996 1.00 6.94 C ANISOU 547 CE2 TYR A 65 876 735 1026 151 -68 33 C ATOM 548 CZ TYR A 65 -9.320 -18.960 3.310 1.00 6.24 C ANISOU 548 CZ TYR A 65 802 618 952 140 -47 36 C ATOM 549 OH TYR A 65 -8.555 -19.565 2.358 1.00 6.27 O ANISOU 549 OH TYR A 65 819 626 936 143 -39 30 O ATOM 550 N GLN A 66 -12.814 -13.667 7.161 1.00 9.45 N ANISOU 550 N GLN A 66 1157 1012 1421 222 -85 78 N ATOM 551 CA GLN A 66 -13.695 -12.940 8.055 1.00 10.16 C ANISOU 551 CA GLN A 66 1230 1109 1521 243 -94 70 C ATOM 552 C GLN A 66 -15.133 -12.867 7.535 1.00 10.79 C ANISOU 552 C GLN A 66 1281 1241 1577 273 -119 54 C ATOM 553 O GLN A 66 -15.364 -12.518 6.367 1.00 10.80 O ANISOU 553 O GLN A 66 1295 1258 1552 303 -133 65 O ATOM 554 CB GLN A 66 -13.127 -11.537 8.278 1.00 10.71 C ANISOU 554 CB GLN A 66 1333 1135 1601 267 -88 96 C ATOM 555 CG GLN A 66 -13.931 -10.663 9.207 1.00 11.94 C ANISOU 555 CG GLN A 66 1479 1290 1767 295 -96 87 C ATOM 556 CD GLN A 66 -13.075 -9.603 9.849 1.00 14.81 C ANISOU 556 CD GLN A 66 1877 1599 2150 296 -82 105 C ATOM 557 OE1 GLN A 66 -13.037 -8.466 9.385 1.00 15.97 O ANISOU 557 OE1 GLN A 66 2060 1719 2289 329 -86 125 O ATOM 558 NE2 GLN A 66 -12.353 -9.977 10.912 1.00 15.17 N ANISOU 558 NE2 GLN A 66 1916 1627 2220 259 -65 97 N ATOM 559 N THR A 67 -16.092 -13.204 8.402 1.00 10.73 N ANISOU 559 N THR A 67 1235 1267 1577 265 -125 27 N ATOM 560 CA THR A 67 -17.507 -13.028 8.069 1.00 11.41 C ANISOU 560 CA THR A 67 1284 1412 1640 296 -149 7 C ATOM 561 C THR A 67 -18.058 -11.746 8.691 1.00 12.17 C ANISOU 561 C THR A 67 1376 1507 1741 347 -156 9 C ATOM 562 O THR A 67 -18.110 -11.590 9.915 1.00 11.84 O ANISOU 562 O THR A 67 1324 1456 1721 336 -145 -1 O ATOM 563 CB THR A 67 -18.397 -14.223 8.470 1.00 10.99 C ANISOU 563 CB THR A 67 1182 1412 1583 255 -151 -30 C ATOM 564 OG1 THR A 67 -17.930 -15.414 7.825 1.00 10.77 O ANISOU 564 OG1 THR A 67 1165 1380 1548 212 -146 -34 O ATOM 565 CG2 THR A 67 -19.837 -13.964 8.046 1.00 10.62 C ANISOU 565 CG2 THR A 67 1090 1437 1509 289 -177 -53 C ATOM 566 N ARG A 68 -18.477 -10.847 7.815 1.00 13.66 N ANISOU 566 N ARG A 68 1579 1705 1907 404 -176 22 N ATOM 567 CA ARG A 68 -19.002 -9.544 8.189 1.00 15.59 C ANISOU 567 CA ARG A 68 1830 1941 2150 465 -188 25 C ATOM 568 C ARG A 68 -19.961 -9.115 7.091 1.00 16.52 C ANISOU 568 C ARG A 68 1938 2106 2231 526 -219 25 C ATOM 569 O ARG A 68 -19.732 -9.417 5.916 1.00 16.47 O ANISOU 569 O ARG A 68 1948 2107 2202 524 -227 39 O ATOM 570 CB ARG A 68 -17.843 -8.559 8.281 1.00 15.87 C ANISOU 570 CB ARG A 68 1932 1896 2202 473 -173 61 C ATOM 571 CG ARG A 68 -18.197 -7.195 8.804 1.00 18.18 C ANISOU 571 CG ARG A 68 2247 2162 2500 531 -180 65 C ATOM 572 CD ARG A 68 -16.932 -6.380 9.021 1.00 20.67 C ANISOU 572 CD ARG A 68 2627 2392 2833 517 -160 96 C ATOM 573 NE ARG A 68 -16.371 -5.856 7.776 1.00 21.87 N ANISOU 573 NE ARG A 68 2833 2511 2965 533 -163 134 N ATOM 574 CZ ARG A 68 -15.337 -6.380 7.129 1.00 21.93 C ANISOU 574 CZ ARG A 68 2860 2502 2971 487 -147 154 C ATOM 575 NH1 ARG A 68 -14.732 -7.467 7.593 1.00 21.88 N ANISOU 575 NH1 ARG A 68 2825 2505 2984 427 -129 140 N ATOM 576 NH2 ARG A 68 -14.910 -5.810 6.009 1.00 23.13 N ANISOU 576 NH2 ARG A 68 3062 2627 3099 503 -148 188 N ATOM 577 N GLN A 69 -21.037 -8.424 7.470 1.00 17.69 N ANISOU 577 N GLN A 69 2058 2291 2370 582 -238 6 N ATOM 578 CA GLN A 69 -22.026 -7.925 6.507 1.00 18.51 C ANISOU 578 CA GLN A 69 2150 2447 2436 653 -272 4 C ATOM 579 C GLN A 69 -22.564 -9.040 5.607 1.00 18.36 C ANISOU 579 C GLN A 69 2085 2501 2390 626 -287 -16 C ATOM 580 O GLN A 69 -22.643 -8.887 4.383 1.00 18.73 O ANISOU 580 O GLN A 69 2151 2562 2405 658 -307 -1 O ATOM 581 CB GLN A 69 -21.430 -6.789 5.659 1.00 19.13 C ANISOU 581 CB GLN A 69 2306 2463 2501 705 -280 49 C ATOM 582 CG GLN A 69 -20.946 -5.581 6.466 1.00 20.71 C ANISOU 582 CG GLN A 69 2559 2586 2725 734 -268 68 C ATOM 583 CD GLN A 69 -20.343 -4.506 5.585 1.00 23.92 C ANISOU 583 CD GLN A 69 3049 2925 3115 775 -273 115 C ATOM 584 OE1 GLN A 69 -19.425 -4.769 4.800 1.00 24.99 O ANISOU 584 OE1 GLN A 69 3221 3030 3244 737 -261 144 O ATOM 585 NE2 GLN A 69 -20.857 -3.284 5.705 1.00 23.85 N ANISOU 585 NE2 GLN A 69 3073 2893 3096 853 -291 122 N ATOM 586 N ASN A 70 -22.910 -10.167 6.227 1.00 17.88 N ANISOU 586 N ASN A 70 1970 2484 2341 564 -276 -51 N ATOM 587 CA ASN A 70 -23.472 -11.333 5.528 1.00 17.76 C ANISOU 587 CA ASN A 70 1909 2537 2301 525 -287 -78 C ATOM 588 C ASN A 70 -22.595 -11.856 4.376 1.00 16.89 C ANISOU 588 C ASN A 70 1842 2396 2180 498 -284 -55 C ATOM 589 O ASN A 70 -23.091 -12.488 3.450 1.00 17.12 O ANISOU 589 O ASN A 70 1847 2481 2179 490 -302 -73 O ATOM 590 CB ASN A 70 -24.913 -11.028 5.062 1.00 18.71 C ANISOU 590 CB ASN A 70 1970 2752 2385 582 -323 -107 C ATOM 591 CG ASN A 70 -25.666 -12.271 4.582 1.00 19.47 C ANISOU 591 CG ASN A 70 2006 2932 2458 531 -333 -147 C ATOM 592 OD1 ASN A 70 -26.166 -12.315 3.452 1.00 20.78 O ANISOU 592 OD1 ASN A 70 2157 3150 2587 560 -362 -154 O ATOM 593 ND2 ASN A 70 -25.755 -13.277 5.441 1.00 19.49 N ANISOU 593 ND2 ASN A 70 1977 2948 2482 453 -310 -174 N ATOM 594 N GLN A 71 -21.292 -11.586 4.437 1.00 16.11 N ANISOU 594 N GLN A 71 1806 2215 2103 484 -261 -19 N ATOM 595 CA GLN A 71 -20.365 -12.021 3.378 1.00 15.53 C ANISOU 595 CA GLN A 71 1773 2112 2017 461 -255 3 C ATOM 596 C GLN A 71 -18.976 -12.410 3.878 1.00 14.52 C ANISOU 596 C GLN A 71 1683 1913 1921 408 -220 21 C ATOM 597 O GLN A 71 -18.617 -12.148 5.026 1.00 14.10 O ANISOU 597 O GLN A 71 1635 1823 1901 395 -202 24 O ATOM 598 CB GLN A 71 -20.271 -10.993 2.238 1.00 16.08 C ANISOU 598 CB GLN A 71 1885 2171 2054 525 -273 37 C ATOM 599 CG GLN A 71 -19.809 -9.610 2.639 1.00 16.95 C ANISOU 599 CG GLN A 71 2046 2217 2177 570 -266 72 C ATOM 600 CD GLN A 71 -20.126 -8.548 1.590 1.00 18.44 C ANISOU 600 CD GLN A 71 2272 2407 2326 645 -292 102 C ATOM 601 OE1 GLN A 71 -19.617 -8.588 0.469 1.00 18.85 O ANISOU 601 OE1 GLN A 71 2360 2451 2351 645 -293 126 O ATOM 602 NE2 GLN A 71 -20.958 -7.584 1.961 1.00 19.35 N ANISOU 602 NE2 GLN A 71 2382 2532 2437 712 -313 99 N ATOM 603 N CYS A 72 -18.203 -13.042 3.003 1.00 13.86 N ANISOU 603 N CYS A 72 1624 1816 1826 381 -212 31 N ATOM 604 CA CYS A 72 -16.840 -13.428 3.328 1.00 13.04 C ANISOU 604 CA CYS A 72 1553 1653 1748 338 -182 46 C ATOM 605 C CYS A 72 -15.853 -12.391 2.836 1.00 12.99 C ANISOU 605 C CYS A 72 1602 1597 1739 363 -171 89 C ATOM 606 O CYS A 72 -15.929 -11.950 1.695 1.00 13.12 O ANISOU 606 O CYS A 72 1639 1625 1721 395 -184 107 O ATOM 607 CB CYS A 72 -16.492 -14.785 2.717 1.00 12.54 C ANISOU 607 CB CYS A 72 1487 1604 1675 294 -176 28 C ATOM 608 SG CYS A 72 -14.848 -15.363 3.209 1.00 11.53 S ANISOU 608 SG CYS A 72 1391 1412 1577 249 -141 41 S ATOM 609 N PHE A 73 -14.924 -12.020 3.708 1.00 13.15 N ANISOU 609 N PHE A 73 1644 1563 1791 345 -148 104 N ATOM 610 CA PHE A 73 -13.825 -11.137 3.354 1.00 13.59 C ANISOU 610 CA PHE A 73 1749 1568 1845 351 -131 142 C ATOM 611 C PHE A 73 -12.503 -11.867 3.567 1.00 13.11 C ANISOU 611 C PHE A 73 1697 1481 1804 301 -103 143 C ATOM 612 O PHE A 73 -12.124 -12.180 4.695 1.00 12.47 O ANISOU 612 O PHE A 73 1602 1380 1754 273 -90 132 O ATOM 613 CB PHE A 73 -13.870 -9.854 4.186 1.00 13.90 C ANISOU 613 CB PHE A 73 1811 1568 1904 376 -129 157 C ATOM 614 CG PHE A 73 -14.974 -8.901 3.793 1.00 16.04 C ANISOU 614 CG PHE A 73 2088 1854 2151 440 -157 164 C ATOM 615 CD1 PHE A 73 -14.754 -7.920 2.827 1.00 17.01 C ANISOU 615 CD1 PHE A 73 2263 1953 2246 475 -162 200 C ATOM 616 CD2 PHE A 73 -16.224 -8.967 4.405 1.00 17.16 C ANISOU 616 CD2 PHE A 73 2186 2038 2296 466 -177 134 C ATOM 617 CE1 PHE A 73 -15.766 -7.031 2.466 1.00 18.20 C ANISOU 617 CE1 PHE A 73 2426 2116 2373 543 -190 208 C ATOM 618 CE2 PHE A 73 -17.240 -8.076 4.057 1.00 17.78 C ANISOU 618 CE2 PHE A 73 2267 2137 2350 534 -205 137 C ATOM 619 CZ PHE A 73 -17.012 -7.110 3.082 1.00 18.48 C ANISOU 619 CZ PHE A 73 2412 2197 2412 576 -213 175 C ATOM 620 N TYR A 74 -11.816 -12.147 2.466 1.00 13.67 N ANISOU 620 N TYR A 74 1787 1555 1851 293 -95 156 N ATOM 621 CA TYR A 74 -10.542 -12.851 2.504 1.00 13.82 C ANISOU 621 CA TYR A 74 1811 1558 1881 254 -69 155 C ATOM 622 C TYR A 74 -9.378 -11.896 2.323 1.00 14.18 C ANISOU 622 C TYR A 74 1893 1566 1927 247 -46 189 C ATOM 623 O TYR A 74 -9.356 -11.101 1.392 1.00 14.72 O ANISOU 623 O TYR A 74 1994 1632 1968 267 -47 216 O ATOM 624 CB TYR A 74 -10.477 -13.930 1.424 1.00 13.72 C ANISOU 624 CB TYR A 74 1792 1579 1841 246 -72 140 C ATOM 625 CG TYR A 74 -9.138 -14.635 1.359 1.00 13.68 C ANISOU 625 CG TYR A 74 1794 1562 1844 216 -46 137 C ATOM 626 CD1 TYR A 74 -8.200 -14.314 0.378 1.00 13.84 C ANISOU 626 CD1 TYR A 74 1837 1581 1839 215 -29 159 C ATOM 627 CD2 TYR A 74 -8.805 -15.615 2.295 1.00 12.85 C ANISOU 627 CD2 TYR A 74 1669 1446 1766 190 -38 114 C ATOM 628 CE1 TYR A 74 -6.958 -14.970 0.330 1.00 15.02 C ANISOU 628 CE1 TYR A 74 1985 1727 1993 192 -5 152 C ATOM 629 CE2 TYR A 74 -7.583 -16.267 2.261 1.00 12.50 C ANISOU 629 CE2 TYR A 74 1628 1394 1727 172 -18 109 C ATOM 630 CZ TYR A 74 -6.666 -15.952 1.283 1.00 13.79 C ANISOU 630 CZ TYR A 74 1809 1564 1868 175 -1 126 C ATOM 631 OH TYR A 74 -5.462 -16.621 1.266 1.00 14.63 O ANISOU 631 OH TYR A 74 1912 1669 1977 161 20 117 O ATOM 632 N ASN A 75 -8.405 -11.994 3.219 1.00 14.65 N ANISOU 632 N ASN A 75 1949 1600 2017 217 -25 187 N ATOM 633 CA ASN A 75 -7.169 -11.234 3.101 1.00 15.29 C ANISOU 633 CA ASN A 75 2057 1653 2100 198 0 212 C ATOM 634 C ASN A 75 -5.993 -12.035 3.605 1.00 14.64 C ANISOU 634 C ASN A 75 1955 1572 2036 164 21 198 C ATOM 635 O ASN A 75 -6.114 -12.772 4.580 1.00 14.08 O ANISOU 635 O ASN A 75 1858 1502 1990 156 17 174 O ATOM 636 CB ASN A 75 -7.264 -9.912 3.866 1.00 15.76 C ANISOU 636 CB ASN A 75 2139 1671 2177 203 1 230 C ATOM 637 CG ASN A 75 -8.273 -8.962 3.253 1.00 17.73 C ANISOU 637 CG ASN A 75 2420 1914 2404 245 -19 249 C ATOM 638 OD1 ASN A 75 -9.399 -8.843 3.741 1.00 20.26 O ANISOU 638 OD1 ASN A 75 2725 2241 2730 276 -41 236 O ATOM 639 ND2 ASN A 75 -7.890 -8.306 2.160 1.00 18.89 N ANISOU 639 ND2 ASN A 75 2607 2052 2520 250 -11 281 N ATOM 640 N SER A 76 -4.868 -11.899 2.908 1.00 14.84 N ANISOU 640 N SER A 76 1993 1601 2046 146 44 212 N ATOM 641 CA SER A 76 -3.600 -12.446 3.358 1.00 14.44 C ANISOU 641 CA SER A 76 1921 1555 2010 118 66 201 C ATOM 642 C SER A 76 -2.548 -11.345 3.470 1.00 14.51 C ANISOU 642 C SER A 76 1947 1545 2022 89 90 223 C ATOM 643 O SER A 76 -2.567 -10.367 2.721 1.00 14.72 O ANISOU 643 O SER A 76 2008 1559 2027 88 98 252 O ATOM 644 CB SER A 76 -3.120 -13.580 2.444 1.00 14.73 C ANISOU 644 CB SER A 76 1946 1628 2024 120 73 185 C ATOM 645 OG SER A 76 -2.842 -13.132 1.127 1.00 15.65 O ANISOU 645 OG SER A 76 2084 1759 2103 121 85 206 O ATOM 646 N SER A 77 -1.649 -11.505 4.434 1.00 14.01 N ANISOU 646 N SER A 77 1860 1479 1983 66 103 211 N ATOM 647 CA SER A 77 -0.559 -10.567 4.653 1.00 14.05 C ANISOU 647 CA SER A 77 1873 1473 1993 30 127 225 C ATOM 648 C SER A 77 0.557 -11.223 5.461 1.00 13.48 C ANISOU 648 C SER A 77 1760 1422 1939 10 139 201 C ATOM 649 O SER A 77 0.390 -12.324 5.997 1.00 13.23 O ANISOU 649 O SER A 77 1703 1404 1919 29 125 177 O ATOM 650 CB SER A 77 -1.062 -9.321 5.382 1.00 14.03 C ANISOU 650 CB SER A 77 1899 1424 2008 25 121 239 C ATOM 651 OG SER A 77 -1.548 -9.657 6.668 1.00 14.68 O ANISOU 651 OG SER A 77 1960 1496 2120 35 104 217 O ATOM 652 N TYR A 78 1.687 -10.530 5.538 1.00 13.28 N ANISOU 652 N TYR A 78 1730 1401 1912 -28 163 209 N ATOM 653 CA TYR A 78 2.809 -10.943 6.363 1.00 12.90 C ANISOU 653 CA TYR A 78 1642 1380 1881 -47 173 187 C ATOM 654 C TYR A 78 2.852 -10.110 7.631 1.00 12.48 C ANISOU 654 C TYR A 78 1590 1295 1854 -69 169 184 C ATOM 655 O TYR A 78 3.046 -8.901 7.590 1.00 13.14 O ANISOU 655 O TYR A 78 1702 1354 1938 -102 182 202 O ATOM 656 CB TYR A 78 4.128 -10.850 5.577 1.00 13.17 C ANISOU 656 CB TYR A 78 1657 1456 1891 -77 204 189 C ATOM 657 CG TYR A 78 4.208 -11.901 4.498 1.00 13.67 C ANISOU 657 CG TYR A 78 1709 1557 1928 -49 207 181 C ATOM 658 CD1 TYR A 78 3.725 -11.645 3.216 1.00 14.17 C ANISOU 658 CD1 TYR A 78 1805 1619 1960 -44 213 202 C ATOM 659 CD2 TYR A 78 4.723 -13.173 4.770 1.00 13.69 C ANISOU 659 CD2 TYR A 78 1672 1595 1933 -24 202 150 C ATOM 660 CE1 TYR A 78 3.768 -12.619 2.228 1.00 14.11 C ANISOU 660 CE1 TYR A 78 1788 1647 1926 -18 215 191 C ATOM 661 CE2 TYR A 78 4.781 -14.150 3.784 1.00 13.06 C ANISOU 661 CE2 TYR A 78 1587 1546 1829 4 205 139 C ATOM 662 CZ TYR A 78 4.296 -13.868 2.517 1.00 14.02 C ANISOU 662 CZ TYR A 78 1739 1669 1921 5 211 158 C ATOM 663 OH TYR A 78 4.339 -14.833 1.532 1.00 14.25 O ANISOU 663 OH TYR A 78 1763 1729 1922 33 213 143 O ATOM 664 N LEU A 79 2.627 -10.763 8.760 1.00 11.93 N ANISOU 664 N LEU A 79 1499 1226 1808 -52 151 163 N ATOM 665 CA LEU A 79 2.767 -10.108 10.046 1.00 11.46 C ANISOU 665 CA LEU A 79 1435 1146 1772 -72 147 155 C ATOM 666 C LEU A 79 4.238 -10.087 10.413 1.00 11.33 C ANISOU 666 C LEU A 79 1383 1167 1757 -105 164 141 C ATOM 667 O LEU A 79 5.006 -10.969 10.008 1.00 10.73 O ANISOU 667 O LEU A 79 1273 1136 1668 -96 172 129 O ATOM 668 CB LEU A 79 1.966 -10.839 11.130 1.00 11.02 C ANISOU 668 CB LEU A 79 1370 1082 1736 -41 122 138 C ATOM 669 CG LEU A 79 0.550 -11.297 10.771 1.00 11.53 C ANISOU 669 CG LEU A 79 1453 1130 1797 -5 103 143 C ATOM 670 CD1 LEU A 79 -0.144 -11.825 12.009 1.00 11.15 C ANISOU 670 CD1 LEU A 79 1395 1074 1767 11 84 127 C ATOM 671 CD2 LEU A 79 -0.274 -10.190 10.128 1.00 11.97 C ANISOU 671 CD2 LEU A 79 1550 1154 1846 -3 103 165 C ATOM 672 N ASN A 80 4.626 -9.061 11.164 1.00 11.23 N ANISOU 672 N ASN A 80 1374 1137 1756 -143 171 139 N ATOM 673 CA ASN A 80 5.954 -8.995 11.752 1.00 10.88 C ANISOU 673 CA ASN A 80 1288 1131 1714 -178 183 119 C ATOM 674 C ASN A 80 5.896 -9.367 13.225 1.00 10.04 C ANISOU 674 C ASN A 80 1159 1027 1628 -164 162 96 C ATOM 675 O ASN A 80 4.932 -9.025 13.924 1.00 9.30 O ANISOU 675 O ASN A 80 1092 892 1550 -152 146 98 O ATOM 676 CB ASN A 80 6.549 -7.607 11.548 1.00 11.88 C ANISOU 676 CB ASN A 80 1435 1242 1837 -240 207 130 C ATOM 677 CG ASN A 80 6.973 -7.374 10.108 1.00 14.18 C ANISOU 677 CG ASN A 80 1738 1548 2101 -262 234 151 C ATOM 678 OD1 ASN A 80 7.922 -7.994 9.616 1.00 18.25 O ANISOU 678 OD1 ASN A 80 2211 2123 2600 -268 249 140 O ATOM 679 ND2 ASN A 80 6.270 -6.489 9.423 1.00 15.85 N ANISOU 679 ND2 ASN A 80 2009 1708 2304 -270 239 181 N ATOM 680 N VAL A 81 6.921 -10.095 13.669 1.00 9.24 N ANISOU 680 N VAL A 81 1007 979 1523 -161 161 74 N ATOM 681 CA VAL A 81 7.051 -10.531 15.049 1.00 8.49 C ANISOU 681 CA VAL A 81 888 896 1441 -146 141 53 C ATOM 682 C VAL A 81 8.129 -9.712 15.746 1.00 8.76 C ANISOU 682 C VAL A 81 894 957 1478 -195 150 35 C ATOM 683 O VAL A 81 9.251 -9.608 15.246 1.00 9.37 O ANISOU 683 O VAL A 81 937 1082 1542 -224 169 28 O ATOM 684 CB VAL A 81 7.446 -12.039 15.145 1.00 8.41 C ANISOU 684 CB VAL A 81 844 928 1422 -98 128 39 C ATOM 685 CG1 VAL A 81 7.396 -12.514 16.591 1.00 7.50 C ANISOU 685 CG1 VAL A 81 715 817 1317 -77 105 23 C ATOM 686 CG2 VAL A 81 6.553 -12.895 14.259 1.00 7.29 C ANISOU 686 CG2 VAL A 81 729 767 1275 -58 123 53 C ATOM 687 N GLN A 82 7.787 -9.146 16.899 1.00 8.48 N ANISOU 687 N GLN A 82 870 895 1458 -207 137 26 N ATOM 688 CA GLN A 82 8.758 -8.461 17.757 1.00 9.06 C ANISOU 688 CA GLN A 82 914 995 1532 -253 141 3 C ATOM 689 C GLN A 82 9.034 -9.363 18.943 1.00 9.05 C ANISOU 689 C GLN A 82 876 1032 1532 -218 116 -19 C ATOM 690 O GLN A 82 8.350 -9.279 19.961 1.00 8.84 O ANISOU 690 O GLN A 82 867 977 1515 -205 99 -24 O ATOM 691 CB GLN A 82 8.241 -7.090 18.233 1.00 8.62 C ANISOU 691 CB GLN A 82 903 882 1491 -293 144 5 C ATOM 692 CG GLN A 82 7.929 -6.112 17.109 1.00 7.98 C ANISOU 692 CG GLN A 82 871 754 1407 -325 167 30 C ATOM 693 CD GLN A 82 6.640 -6.459 16.393 1.00 8.37 C ANISOU 693 CD GLN A 82 961 762 1458 -276 159 57 C ATOM 694 OE1 GLN A 82 5.671 -6.914 17.017 1.00 7.40 O ANISOU 694 OE1 GLN A 82 848 620 1345 -232 137 55 O ATOM 695 NE2 GLN A 82 6.622 -6.269 15.076 1.00 7.53 N ANISOU 695 NE2 GLN A 82 876 646 1337 -283 177 81 N ATOM 696 N ARG A 83 10.044 -10.217 18.802 1.00 9.83 N ANISOU 696 N ARG A 83 923 1194 1616 -200 116 -32 N ATOM 697 CA ARG A 83 10.293 -11.309 19.752 1.00 10.65 C ANISOU 697 CA ARG A 83 998 1334 1715 -151 90 -48 C ATOM 698 C ARG A 83 10.435 -10.870 21.214 1.00 11.00 C ANISOU 698 C ARG A 83 1032 1385 1764 -167 73 -67 C ATOM 699 O ARG A 83 9.797 -11.429 22.103 1.00 10.86 O ANISOU 699 O ARG A 83 1029 1350 1748 -131 51 -66 O ATOM 700 CB ARG A 83 11.505 -12.146 19.314 1.00 11.14 C ANISOU 700 CB ARG A 83 1006 1471 1758 -128 93 -62 C ATOM 701 CG ARG A 83 11.251 -13.086 18.121 1.00 11.65 C ANISOU 701 CG ARG A 83 1082 1530 1814 -86 99 -47 C ATOM 702 CD ARG A 83 12.443 -14.036 17.939 1.00 12.92 C ANISOU 702 CD ARG A 83 1188 1767 1955 -48 97 -68 C ATOM 703 NE ARG A 83 12.365 -14.829 16.709 1.00 12.69 N ANISOU 703 NE ARG A 83 1167 1740 1916 -13 107 -59 N ATOM 704 CZ ARG A 83 12.129 -16.139 16.671 1.00 12.08 C ANISOU 704 CZ ARG A 83 1102 1657 1832 54 90 -60 C ATOM 705 NH1 ARG A 83 11.940 -16.815 17.799 1.00 11.40 N ANISOU 705 NH1 ARG A 83 1024 1561 1748 93 61 -64 N ATOM 706 NH2 ARG A 83 12.079 -16.772 15.504 1.00 10.49 N ANISOU 706 NH2 ARG A 83 909 1457 1619 81 101 -56 N ATOM 707 N GLU A 84 11.258 -9.851 21.440 1.00 12.00 N ANISOU 707 N GLU A 84 1134 1537 1889 -226 84 -86 N ATOM 708 CA GLU A 84 11.575 -9.335 22.774 1.00 12.87 C ANISOU 708 CA GLU A 84 1227 1663 2000 -249 69 -111 C ATOM 709 C GLU A 84 10.325 -8.873 23.529 1.00 12.14 C ANISOU 709 C GLU A 84 1188 1502 1922 -245 59 -104 C ATOM 710 O GLU A 84 10.178 -9.140 24.718 1.00 12.40 O ANISOU 710 O GLU A 84 1216 1545 1951 -226 37 -117 O ATOM 711 CB GLU A 84 12.550 -8.153 22.665 1.00 13.70 C ANISOU 711 CB GLU A 84 1308 1796 2104 -328 89 -132 C ATOM 712 CG GLU A 84 13.367 -8.095 21.362 1.00 17.29 C ANISOU 712 CG GLU A 84 1735 2286 2548 -356 117 -127 C ATOM 713 CD GLU A 84 12.517 -7.799 20.118 1.00 20.52 C ANISOU 713 CD GLU A 84 2201 2630 2965 -360 139 -92 C ATOM 714 OE1 GLU A 84 12.877 -8.317 19.037 1.00 22.06 O ANISOU 714 OE1 GLU A 84 2380 2855 3149 -347 154 -82 O ATOM 715 OE2 GLU A 84 11.490 -7.071 20.219 1.00 21.50 O ANISOU 715 OE2 GLU A 84 2386 2678 3104 -371 139 -77 O ATOM 716 N ASN A 85 9.438 -8.176 22.825 1.00 11.37 N ANISOU 716 N ASN A 85 1142 1340 1838 -262 74 -83 N ATOM 717 CA ASN A 85 8.258 -7.567 23.430 1.00 10.85 C ANISOU 717 CA ASN A 85 1125 1212 1785 -260 68 -79 C ATOM 718 C ASN A 85 7.073 -8.515 23.469 1.00 10.15 C ANISOU 718 C ASN A 85 1060 1098 1698 -200 54 -60 C ATOM 719 O ASN A 85 6.006 -8.155 23.974 1.00 9.64 O ANISOU 719 O ASN A 85 1030 990 1642 -191 48 -57 O ATOM 720 CB ASN A 85 7.865 -6.300 22.665 1.00 10.55 C ANISOU 720 CB ASN A 85 1135 1116 1759 -301 89 -67 C ATOM 721 CG ASN A 85 8.964 -5.253 22.658 1.00 10.68 C ANISOU 721 CG ASN A 85 1137 1147 1772 -373 105 -86 C ATOM 722 OD1 ASN A 85 9.119 -4.509 21.688 1.00 11.19 O ANISOU 722 OD1 ASN A 85 1228 1186 1839 -412 128 -72 O ATOM 723 ND2 ASN A 85 9.723 -5.183 23.738 1.00 9.66 N ANISOU 723 ND2 ASN A 85 970 1062 1638 -394 94 -118 N ATOM 724 N GLY A 86 7.270 -9.718 22.928 1.00 9.94 N ANISOU 724 N GLY A 86 1015 1100 1663 -162 50 -49 N ATOM 725 CA GLY A 86 6.204 -10.712 22.806 1.00 9.28 C ANISOU 725 CA GLY A 86 954 993 1579 -113 40 -31 C ATOM 726 C GLY A 86 5.006 -10.165 22.048 1.00 9.07 C ANISOU 726 C GLY A 86 972 911 1564 -115 50 -12 C ATOM 727 O GLY A 86 3.861 -10.357 22.465 1.00 8.09 O ANISOU 727 O GLY A 86 872 759 1444 -92 41 -6 O ATOM 728 N THR A 87 5.271 -9.460 20.947 1.00 9.27 N ANISOU 728 N THR A 87 1007 923 1591 -141 69 -2 N ATOM 729 CA THR A 87 4.191 -8.881 20.139 1.00 9.53 C ANISOU 729 CA THR A 87 1084 906 1631 -138 76 18 C ATOM 730 C THR A 87 4.247 -9.268 18.674 1.00 10.10 C ANISOU 730 C THR A 87 1161 983 1695 -129 88 38 C ATOM 731 O THR A 87 5.275 -9.737 18.164 1.00 9.99 O ANISOU 731 O THR A 87 1116 1008 1670 -136 97 35 O ATOM 732 CB THR A 87 4.116 -7.331 20.202 1.00 9.30 C ANISOU 732 CB THR A 87 1086 837 1610 -178 87 16 C ATOM 733 OG1 THR A 87 5.301 -6.770 19.644 1.00 9.31 O ANISOU 733 OG1 THR A 87 1076 856 1607 -224 106 14 O ATOM 734 CG2 THR A 87 3.929 -6.826 21.617 1.00 10.03 C ANISOU 734 CG2 THR A 87 1181 920 1710 -185 75 -7 C ATOM 735 N VAL A 88 3.113 -9.019 18.023 1.00 10.56 N ANISOU 735 N VAL A 88 1255 1002 1755 -113 88 55 N ATOM 736 CA VAL A 88 2.891 -9.239 16.611 1.00 11.58 C ANISOU 736 CA VAL A 88 1398 1128 1874 -102 97 76 C ATOM 737 C VAL A 88 2.283 -7.953 16.031 1.00 12.61 C ANISOU 737 C VAL A 88 1574 1211 2005 -116 105 93 C ATOM 738 O VAL A 88 1.536 -7.248 16.717 1.00 12.35 O ANISOU 738 O VAL A 88 1565 1144 1984 -111 97 88 O ATOM 739 CB VAL A 88 1.923 -10.433 16.423 1.00 11.34 C ANISOU 739 CB VAL A 88 1368 1100 1840 -57 82 79 C ATOM 740 CG1 VAL A 88 1.360 -10.469 15.030 1.00 12.05 C ANISOU 740 CG1 VAL A 88 1481 1180 1919 -44 88 99 C ATOM 741 CG2 VAL A 88 2.628 -11.750 16.759 1.00 10.63 C ANISOU 741 CG2 VAL A 88 1245 1051 1745 -41 76 67 C ATOM 742 N SER A 89 2.613 -7.645 14.777 1.00 13.91 N ANISOU 742 N SER A 89 1754 1374 2157 -129 122 111 N ATOM 743 CA SER A 89 2.089 -6.448 14.115 1.00 15.31 C ANISOU 743 CA SER A 89 1982 1503 2330 -139 129 133 C ATOM 744 C SER A 89 1.659 -6.695 12.666 1.00 16.14 C ANISOU 744 C SER A 89 2107 1610 2416 -118 134 157 C ATOM 745 O SER A 89 2.229 -7.528 11.975 1.00 16.06 O ANISOU 745 O SER A 89 2070 1639 2392 -117 142 158 O ATOM 746 CB SER A 89 3.105 -5.305 14.182 1.00 15.59 C ANISOU 746 CB SER A 89 2031 1525 2366 -197 150 133 C ATOM 747 OG SER A 89 4.286 -5.634 13.474 1.00 16.11 O ANISOU 747 OG SER A 89 2069 1635 2418 -229 171 135 O ATOM 748 N ARG A 90 0.645 -5.958 12.223 1.00 17.90 N ANISOU 748 N ARG A 90 2376 1790 2636 -98 127 175 N ATOM 749 CA ARG A 90 0.138 -6.039 10.852 1.00 19.48 C ANISOU 749 CA ARG A 90 2600 1989 2813 -75 128 200 C ATOM 750 C ARG A 90 -0.389 -4.687 10.399 1.00 20.79 C ANISOU 750 C ARG A 90 2828 2100 2971 -74 130 225 C ATOM 751 O ARG A 90 -0.698 -3.821 11.218 1.00 20.75 O ANISOU 751 O ARG A 90 2848 2054 2981 -75 124 219 O ATOM 752 CB ARG A 90 -1.000 -7.054 10.748 1.00 19.32 C ANISOU 752 CB ARG A 90 2562 1987 2791 -25 105 193 C ATOM 753 CG ARG A 90 -2.076 -6.865 11.792 1.00 20.55 C ANISOU 753 CG ARG A 90 2720 2122 2964 2 85 179 C ATOM 754 CD ARG A 90 -3.477 -6.943 11.221 1.00 22.83 C ANISOU 754 CD ARG A 90 3023 2408 3242 49 66 186 C ATOM 755 NE ARG A 90 -4.052 -8.285 11.214 1.00 23.41 N ANISOU 755 NE ARG A 90 3061 2520 3313 70 53 172 N ATOM 756 CZ ARG A 90 -5.322 -8.555 11.513 1.00 24.07 C ANISOU 756 CZ ARG A 90 3136 2611 3398 102 33 161 C ATOM 757 NH1 ARG A 90 -6.157 -7.585 11.878 1.00 24.39 N ANISOU 757 NH1 ARG A 90 3198 2628 3443 125 23 161 N ATOM 758 NH2 ARG A 90 -5.761 -9.804 11.464 1.00 23.70 N ANISOU 758 NH2 ARG A 90 3060 2598 3348 110 25 147 N ATOM 759 N TYR A 91 -0.517 -4.522 9.089 1.00 22.28 N ANISOU 759 N TYR A 91 3046 2287 3134 -66 136 252 N ATOM 760 CA TYR A 91 -1.124 -3.325 8.543 1.00 24.10 C ANISOU 760 CA TYR A 91 3342 2463 3351 -53 134 280 C ATOM 761 C TYR A 91 -2.622 -3.511 8.330 1.00 24.61 C ANISOU 761 C TYR A 91 3416 2524 3410 14 105 282 C ATOM 762 O TYR A 91 -3.048 -4.391 7.586 1.00 25.02 O ANISOU 762 O TYR A 91 3446 2615 3447 41 96 284 O ATOM 763 CB TYR A 91 -0.419 -2.904 7.257 1.00 24.63 C ANISOU 763 CB TYR A 91 3443 2528 3388 -84 158 312 C ATOM 764 CG TYR A 91 0.903 -2.218 7.513 1.00 25.86 C ANISOU 764 CG TYR A 91 3607 2671 3547 -157 189 314 C ATOM 765 CD1 TYR A 91 2.079 -2.959 7.659 1.00 26.84 C ANISOU 765 CD1 TYR A 91 3673 2852 3674 -198 207 294 C ATOM 766 CD2 TYR A 91 0.979 -0.829 7.620 1.00 27.09 C ANISOU 766 CD2 TYR A 91 3830 2761 3703 -185 199 332 C ATOM 767 CE1 TYR A 91 3.305 -2.331 7.901 1.00 27.83 C ANISOU 767 CE1 TYR A 91 3798 2977 3801 -269 235 292 C ATOM 768 CE2 TYR A 91 2.197 -0.188 7.860 1.00 28.49 C ANISOU 768 CE2 TYR A 91 4014 2928 3882 -262 228 330 C ATOM 769 CZ TYR A 91 3.356 -0.946 7.999 1.00 28.90 C ANISOU 769 CZ TYR A 91 3999 3046 3936 -305 246 309 C ATOM 770 OH TYR A 91 4.563 -0.319 8.233 1.00 29.99 O ANISOU 770 OH TYR A 91 4136 3185 4074 -384 275 304 O ATOM 771 N GLU A 92 -3.406 -2.709 9.044 1.00 25.36 N ANISOU 771 N GLU A 92 3539 2578 3519 41 90 277 N ATOM 772 CA GLU A 92 -4.842 -2.585 8.818 1.00 25.99 C ANISOU 772 CA GLU A 92 3633 2651 3590 107 62 280 C ATOM 773 C GLU A 92 -5.047 -1.125 8.458 1.00 26.75 C ANISOU 773 C GLU A 92 3808 2682 3674 120 63 307 C ATOM 774 O GLU A 92 -4.422 -0.243 9.062 1.00 26.94 O ANISOU 774 O GLU A 92 3865 2658 3712 84 77 306 O ATOM 775 CB GLU A 92 -5.648 -2.898 10.085 1.00 25.95 C ANISOU 775 CB GLU A 92 3593 2659 3610 135 44 246 C ATOM 776 CG GLU A 92 -5.364 -4.249 10.769 1.00 26.63 C ANISOU 776 CG GLU A 92 3610 2796 3711 115 44 218 C ATOM 777 CD GLU A 92 -5.607 -4.218 12.289 1.00 27.67 C ANISOU 777 CD GLU A 92 3720 2925 3868 115 38 187 C ATOM 778 OE1 GLU A 92 -6.028 -3.160 12.809 1.00 29.81 O ANISOU 778 OE1 GLU A 92 4025 3155 4146 132 33 184 O ATOM 779 OE2 GLU A 92 -5.373 -5.241 12.973 1.00 26.59 O ANISOU 779 OE2 GLU A 92 3536 2825 3743 100 38 167 O ATOM 780 N GLY A 93 -5.902 -0.871 7.470 1.00 27.21 N ANISOU 780 N GLY A 93 3898 2735 3705 171 47 330 N ATOM 781 CA GLY A 93 -6.234 0.488 7.041 1.00 27.97 C ANISOU 781 CA GLY A 93 4077 2765 3785 197 43 360 C ATOM 782 C GLY A 93 -5.064 1.454 7.034 1.00 28.46 C ANISOU 782 C GLY A 93 4197 2768 3848 132 73 380 C ATOM 783 O GLY A 93 -5.136 2.513 7.649 1.00 28.90 O ANISOU 783 O GLY A 93 4305 2759 3915 134 73 379 O ATOM 784 N GLY A 94 -3.977 1.069 6.364 1.00 28.57 N ANISOU 784 N GLY A 94 4200 2806 3848 73 100 395 N ATOM 785 CA GLY A 94 -2.797 1.930 6.211 1.00 29.26 C ANISOU 785 CA GLY A 94 4337 2849 3931 1 133 416 C ATOM 786 C GLY A 94 -1.767 1.925 7.335 1.00 29.11 C ANISOU 786 C GLY A 94 4284 2831 3944 -67 153 386 C ATOM 787 O GLY A 94 -0.564 2.038 7.073 1.00 29.44 O ANISOU 787 O GLY A 94 4326 2881 3979 -140 184 393 O ATOM 788 N ARG A 95 -2.231 1.803 8.579 1.00 28.45 N ANISOU 788 N ARG A 95 4171 2747 3892 -44 135 350 N ATOM 789 CA ARG A 95 -1.361 1.880 9.761 1.00 28.06 C ANISOU 789 CA ARG A 95 4093 2698 3871 -101 148 318 C ATOM 790 C ARG A 95 -0.943 0.503 10.288 1.00 26.85 C ANISOU 790 C ARG A 95 3845 2623 3732 -112 147 287 C ATOM 791 O ARG A 95 -1.713 -0.461 10.229 1.00 25.87 O ANISOU 791 O ARG A 95 3679 2542 3608 -61 127 278 O ATOM 792 CB ARG A 95 -2.059 2.661 10.881 1.00 28.37 C ANISOU 792 CB ARG A 95 4163 2685 3932 -72 131 296 C ATOM 793 CG ARG A 95 -1.173 2.991 12.101 1.00 30.01 C ANISOU 793 CG ARG A 95 4356 2881 4165 -133 144 264 C ATOM 794 CD ARG A 95 -1.977 3.586 13.265 1.00 31.14 C ANISOU 794 CD ARG A 95 4520 2984 4329 -94 124 236 C ATOM 795 NE ARG A 95 -3.018 4.496 12.791 1.00 32.33 N ANISOU 795 NE ARG A 95 4747 3071 4467 -33 109 257 N ATOM 796 CZ ARG A 95 -4.309 4.410 13.109 1.00 32.54 C ANISOU 796 CZ ARG A 95 4766 3100 4496 49 81 244 C ATOM 797 NH1 ARG A 95 -4.737 3.465 13.937 1.00 31.34 N ANISOU 797 NH1 ARG A 95 4539 3010 4359 72 68 211 N ATOM 798 NH2 ARG A 95 -5.174 5.293 12.611 1.00 33.50 N ANISOU 798 NH2 ARG A 95 4959 3166 4603 108 67 264 N ATOM 799 N GLU A 96 0.281 0.425 10.803 1.00 26.20 N ANISOU 799 N GLU A 96 3733 2561 3660 -178 168 271 N ATOM 800 CA GLU A 96 0.726 -0.755 11.527 1.00 25.27 C ANISOU 800 CA GLU A 96 3534 2510 3558 -184 165 239 C ATOM 801 C GLU A 96 0.052 -0.775 12.893 1.00 24.11 C ANISOU 801 C GLU A 96 3372 2353 3436 -155 143 208 C ATOM 802 O GLU A 96 0.099 0.213 13.628 1.00 24.59 O ANISOU 802 O GLU A 96 3467 2366 3509 -173 144 197 O ATOM 803 CB GLU A 96 2.248 -0.758 11.686 1.00 25.70 C ANISOU 803 CB GLU A 96 3558 2595 3613 -260 191 229 C ATOM 804 CG GLU A 96 2.807 -2.061 12.253 1.00 26.53 C ANISOU 804 CG GLU A 96 3580 2773 3726 -258 187 200 C ATOM 805 CD GLU A 96 4.293 -1.984 12.566 1.00 29.29 C ANISOU 805 CD GLU A 96 3893 3158 4076 -328 210 183 C ATOM 806 OE1 GLU A 96 4.693 -1.125 13.389 1.00 30.33 O ANISOU 806 OE1 GLU A 96 4041 3263 4221 -370 215 168 O ATOM 807 OE2 GLU A 96 5.061 -2.794 11.998 1.00 30.17 O ANISOU 807 OE2 GLU A 96 3958 3330 4174 -338 222 182 O ATOM 808 N HIS A 97 -0.580 -1.901 13.213 1.00 22.36 N ANISOU 808 N HIS A 97 3100 2176 3220 -111 124 193 N ATOM 809 CA HIS A 97 -1.223 -2.124 14.512 1.00 21.06 C ANISOU 809 CA HIS A 97 2911 2015 3074 -84 105 163 C ATOM 810 C HIS A 97 -0.497 -3.249 15.242 1.00 19.45 C ANISOU 810 C HIS A 97 2642 1869 2879 -104 106 140 C ATOM 811 O HIS A 97 -0.119 -4.240 14.619 1.00 19.06 O ANISOU 811 O HIS A 97 2559 1862 2820 -103 110 146 O ATOM 812 CB HIS A 97 -2.692 -2.518 14.323 1.00 21.07 C ANISOU 812 CB HIS A 97 2912 2021 3072 -17 83 165 C ATOM 813 CG HIS A 97 -3.544 -1.435 13.737 1.00 23.00 C ANISOU 813 CG HIS A 97 3219 2213 3306 18 75 185 C ATOM 814 ND1 HIS A 97 -4.513 -0.775 14.463 1.00 23.96 N ANISOU 814 ND1 HIS A 97 3363 2305 3436 58 60 170 N ATOM 815 CD2 HIS A 97 -3.582 -0.905 12.491 1.00 23.95 C ANISOU 815 CD2 HIS A 97 3386 2308 3405 24 81 218 C ATOM 816 CE1 HIS A 97 -5.103 0.122 13.692 1.00 24.65 C ANISOU 816 CE1 HIS A 97 3509 2348 3510 92 54 193 C ATOM 817 NE2 HIS A 97 -4.558 0.061 12.490 1.00 24.75 N ANISOU 817 NE2 HIS A 97 3539 2360 3504 71 66 224 N ATOM 818 N VAL A 98 -0.317 -3.094 16.553 1.00 17.96 N ANISOU 818 N VAL A 98 2438 1680 2706 -116 101 112 N ATOM 819 CA VAL A 98 0.384 -4.088 17.376 1.00 16.30 C ANISOU 819 CA VAL A 98 2170 1521 2501 -130 99 90 C ATOM 820 C VAL A 98 -0.564 -4.830 18.337 1.00 15.00 C ANISOU 820 C VAL A 98 1982 1375 2343 -90 79 73 C ATOM 821 O VAL A 98 -1.517 -4.251 18.867 1.00 14.54 O ANISOU 821 O VAL A 98 1946 1288 2290 -65 69 65 O ATOM 822 CB VAL A 98 1.545 -3.447 18.174 1.00 16.66 C ANISOU 822 CB VAL A 98 2209 1568 2554 -185 109 71 C ATOM 823 CG1 VAL A 98 2.448 -4.512 18.762 1.00 16.78 C ANISOU 823 CG1 VAL A 98 2163 1645 2568 -197 107 53 C ATOM 824 CG2 VAL A 98 2.374 -2.528 17.278 1.00 17.45 C ANISOU 824 CG2 VAL A 98 2341 1644 2647 -235 132 87 C ATOM 825 N ALA A 99 -0.293 -6.117 18.534 1.00 13.47 N ANISOU 825 N ALA A 99 1745 1228 2147 -82 74 67 N ATOM 826 CA ALA A 99 -0.990 -6.938 19.526 1.00 12.17 C ANISOU 826 CA ALA A 99 1556 1084 1984 -55 58 52 C ATOM 827 C ALA A 99 -0.005 -7.809 20.308 1.00 11.21 C ANISOU 827 C ALA A 99 1395 1002 1861 -70 56 38 C ATOM 828 O ALA A 99 0.895 -8.414 19.721 1.00 10.95 O ANISOU 828 O ALA A 99 1343 996 1822 -80 62 44 O ATOM 829 CB ALA A 99 -2.040 -7.816 18.855 1.00 11.68 C ANISOU 829 CB ALA A 99 1491 1032 1915 -18 50 64 C ATOM 830 N HIS A 100 -0.184 -7.867 21.627 1.00 10.06 N ANISOU 830 N HIS A 100 1239 865 1719 -68 47 19 N ATOM 831 CA HIS A 100 0.540 -8.824 22.463 1.00 9.06 C ANISOU 831 CA HIS A 100 1079 778 1586 -70 39 7 C ATOM 832 C HIS A 100 -0.007 -10.233 22.292 1.00 8.42 C ANISOU 832 C HIS A 100 988 714 1497 -39 31 17 C ATOM 833 O HIS A 100 -1.205 -10.472 22.469 1.00 7.75 O ANISOU 833 O HIS A 100 913 619 1411 -20 26 19 O ATOM 834 CB HIS A 100 0.472 -8.428 23.934 1.00 8.57 C ANISOU 834 CB HIS A 100 1012 718 1525 -77 31 -15 C ATOM 835 CG HIS A 100 1.467 -7.380 24.314 1.00 8.63 C ANISOU 835 CG HIS A 100 1019 722 1536 -115 37 -32 C ATOM 836 ND1 HIS A 100 1.189 -6.030 24.238 1.00 6.90 N ANISOU 836 ND1 HIS A 100 833 461 1326 -133 45 -38 N ATOM 837 CD2 HIS A 100 2.747 -7.482 24.746 1.00 6.05 C ANISOU 837 CD2 HIS A 100 663 431 1205 -141 37 -45 C ATOM 838 CE1 HIS A 100 2.255 -5.347 24.620 1.00 8.19 C ANISOU 838 CE1 HIS A 100 990 630 1491 -175 50 -55 C ATOM 839 NE2 HIS A 100 3.214 -6.204 24.932 1.00 6.35 N ANISOU 839 NE2 HIS A 100 714 449 1249 -181 45 -61 N ATOM 840 N LEU A 101 0.887 -11.153 21.939 1.00 8.25 N ANISOU 840 N LEU A 101 947 721 1469 -36 31 21 N ATOM 841 CA LEU A 101 0.557 -12.564 21.838 1.00 7.81 C ANISOU 841 CA LEU A 101 887 678 1404 -10 23 28 C ATOM 842 C LEU A 101 0.543 -13.162 23.237 1.00 7.72 C ANISOU 842 C LEU A 101 867 680 1385 -2 11 18 C ATOM 843 O LEU A 101 1.569 -13.156 23.923 1.00 7.99 O ANISOU 843 O LEU A 101 882 738 1414 -8 6 8 O ATOM 844 CB LEU A 101 1.569 -13.285 20.944 1.00 7.93 C ANISOU 844 CB LEU A 101 888 714 1412 -3 28 33 C ATOM 845 CG LEU A 101 1.424 -14.803 20.740 1.00 8.17 C ANISOU 845 CG LEU A 101 921 753 1432 26 20 38 C ATOM 846 CD1 LEU A 101 0.126 -15.155 20.009 1.00 6.36 C ANISOU 846 CD1 LEU A 101 715 500 1203 35 20 48 C ATOM 847 CD2 LEU A 101 2.658 -15.379 20.002 1.00 6.05 C ANISOU 847 CD2 LEU A 101 632 511 1154 37 24 36 C ATOM 848 N LEU A 102 -0.625 -13.654 23.659 1.00 6.98 N ANISOU 848 N LEU A 102 788 576 1288 9 6 21 N ATOM 849 CA LEU A 102 -0.809 -14.189 25.007 1.00 7.02 C ANISOU 849 CA LEU A 102 792 593 1282 13 -3 15 C ATOM 850 C LEU A 102 -1.479 -15.572 24.993 1.00 7.50 C ANISOU 850 C LEU A 102 867 651 1331 27 -8 27 C ATOM 851 O LEU A 102 -2.070 -15.990 23.986 1.00 7.32 O ANISOU 851 O LEU A 102 854 615 1311 32 -4 35 O ATOM 852 CB LEU A 102 -1.599 -13.210 25.889 1.00 6.89 C ANISOU 852 CB LEU A 102 780 570 1269 3 -2 3 C ATOM 853 CG LEU A 102 -0.975 -11.828 26.190 1.00 6.50 C ANISOU 853 CG LEU A 102 725 517 1229 -16 1 -13 C ATOM 854 CD1 LEU A 102 -1.988 -10.907 26.826 1.00 5.38 C ANISOU 854 CD1 LEU A 102 593 359 1090 -17 3 -27 C ATOM 855 CD2 LEU A 102 0.270 -11.939 27.081 1.00 5.30 C ANISOU 855 CD2 LEU A 102 553 393 1068 -24 -7 -25 C ATOM 856 N PHE A 103 -1.379 -16.267 26.125 1.00 7.56 N ANISOU 856 N PHE A 103 880 669 1324 32 -16 27 N ATOM 857 CA PHE A 103 -1.800 -17.658 26.233 1.00 7.68 C ANISOU 857 CA PHE A 103 917 677 1325 41 -20 39 C ATOM 858 C PHE A 103 -2.577 -17.959 27.513 1.00 7.89 C ANISOU 858 C PHE A 103 956 708 1335 32 -22 40 C ATOM 859 O PHE A 103 -2.677 -17.124 28.404 1.00 7.24 O ANISOU 859 O PHE A 103 862 639 1252 23 -21 28 O ATOM 860 CB PHE A 103 -0.584 -18.577 26.104 1.00 7.54 C ANISOU 860 CB PHE A 103 901 665 1297 65 -30 45 C ATOM 861 CG PHE A 103 0.104 -18.463 24.780 1.00 7.57 C ANISOU 861 CG PHE A 103 893 671 1312 74 -25 44 C ATOM 862 CD1 PHE A 103 -0.389 -19.142 23.666 1.00 6.15 C ANISOU 862 CD1 PHE A 103 730 472 1134 80 -21 51 C ATOM 863 CD2 PHE A 103 1.225 -17.648 24.630 1.00 7.08 C ANISOU 863 CD2 PHE A 103 802 632 1257 73 -24 34 C ATOM 864 CE1 PHE A 103 0.241 -19.028 22.435 1.00 6.97 C ANISOU 864 CE1 PHE A 103 823 581 1244 88 -15 49 C ATOM 865 CE2 PHE A 103 1.854 -17.528 23.399 1.00 5.79 C ANISOU 865 CE2 PHE A 103 626 475 1100 77 -17 33 C ATOM 866 CZ PHE A 103 1.367 -18.212 22.306 1.00 6.26 C ANISOU 866 CZ PHE A 103 703 516 1160 87 -12 41 C ATOM 867 N LEU A 104 -3.132 -19.163 27.569 1.00 8.36 N ANISOU 867 N LEU A 104 1041 755 1381 31 -22 52 N ATOM 868 CA LEU A 104 -3.877 -19.646 28.717 1.00 9.50 C ANISOU 868 CA LEU A 104 1203 903 1505 17 -20 57 C ATOM 869 C LEU A 104 -3.402 -21.068 29.032 1.00 10.37 C ANISOU 869 C LEU A 104 1348 997 1594 30 -29 75 C ATOM 870 O LEU A 104 -2.532 -21.592 28.336 1.00 10.35 O ANISOU 870 O LEU A 104 1354 985 1596 54 -37 80 O ATOM 871 CB LEU A 104 -5.381 -19.619 28.414 1.00 9.25 C ANISOU 871 CB LEU A 104 1170 868 1474 -8 -7 54 C ATOM 872 CG LEU A 104 -5.966 -18.246 28.065 1.00 9.44 C ANISOU 872 CG LEU A 104 1165 905 1517 -12 -1 37 C ATOM 873 CD1 LEU A 104 -7.243 -18.384 27.252 1.00 9.63 C ANISOU 873 CD1 LEU A 104 1184 929 1544 -25 8 34 C ATOM 874 CD2 LEU A 104 -6.209 -17.425 29.324 1.00 9.68 C ANISOU 874 CD2 LEU A 104 1183 957 1540 -17 2 24 C ATOM 875 N ARG A 105 -3.954 -21.684 30.078 1.00 11.52 N ANISOU 875 N ARG A 105 1520 1143 1716 15 -27 85 N ATOM 876 CA ARG A 105 -3.601 -23.062 30.430 1.00 12.73 C ANISOU 876 CA ARG A 105 1719 1272 1845 28 -35 106 C ATOM 877 C ARG A 105 -3.776 -24.009 29.237 1.00 12.83 C ANISOU 877 C ARG A 105 1759 1251 1865 29 -33 113 C ATOM 878 O ARG A 105 -2.871 -24.776 28.906 1.00 12.88 O ANISOU 878 O ARG A 105 1789 1239 1867 62 -45 120 O ATOM 879 CB ARG A 105 -4.409 -23.553 31.632 1.00 13.46 C ANISOU 879 CB ARG A 105 1840 1365 1908 0 -28 118 C ATOM 880 CG ARG A 105 -3.972 -24.921 32.151 1.00 16.63 C ANISOU 880 CG ARG A 105 2300 1738 2280 15 -38 144 C ATOM 881 CD ARG A 105 -5.045 -25.606 32.989 1.00 21.26 C ANISOU 881 CD ARG A 105 2926 2315 2837 -26 -24 160 C ATOM 882 NE ARG A 105 -5.328 -24.931 34.258 1.00 24.70 N ANISOU 882 NE ARG A 105 3344 2789 3254 -41 -19 157 N ATOM 883 CZ ARG A 105 -6.518 -24.432 34.600 1.00 27.25 C ANISOU 883 CZ ARG A 105 3645 3136 3573 -83 1 146 C ATOM 884 NH1 ARG A 105 -7.554 -24.514 33.766 1.00 27.97 N ANISOU 884 NH1 ARG A 105 3726 3221 3679 -116 17 137 N ATOM 885 NH2 ARG A 105 -6.681 -23.848 35.784 1.00 28.05 N ANISOU 885 NH2 ARG A 105 3732 3273 3653 -91 5 140 N ATOM 886 N ASP A 106 -4.927 -23.934 28.577 1.00 13.12 N ANISOU 886 N ASP A 106 1790 1283 1912 -4 -19 106 N ATOM 887 CA ASP A 106 -5.180 -24.771 27.417 1.00 13.46 C ANISOU 887 CA ASP A 106 1857 1297 1961 -8 -17 108 C ATOM 888 C ASP A 106 -4.382 -24.306 26.206 1.00 13.09 C ANISOU 888 C ASP A 106 1784 1253 1936 22 -23 97 C ATOM 889 O ASP A 106 -4.509 -23.163 25.766 1.00 12.62 O ANISOU 889 O ASP A 106 1683 1216 1895 20 -19 85 O ATOM 890 CB ASP A 106 -6.676 -24.838 27.096 1.00 14.05 C ANISOU 890 CB ASP A 106 1928 1374 2036 -54 -2 101 C ATOM 891 CG ASP A 106 -7.006 -25.945 26.116 1.00 15.46 C ANISOU 891 CG ASP A 106 2142 1520 2213 -67 -1 102 C ATOM 892 OD1 ASP A 106 -6.135 -26.286 25.296 1.00 16.92 O ANISOU 892 OD1 ASP A 106 2338 1684 2405 -34 -10 102 O ATOM 893 OD2 ASP A 106 -8.125 -26.488 26.171 1.00 17.71 O ANISOU 893 OD2 ASP A 106 2443 1801 2487 -112 10 101 O ATOM 894 N THR A 107 -3.564 -25.212 25.675 1.00 13.14 N ANISOU 894 N THR A 107 1819 1235 1939 52 -32 102 N ATOM 895 CA THR A 107 -2.731 -24.939 24.499 1.00 12.86 C ANISOU 895 CA THR A 107 1761 1205 1918 81 -35 92 C ATOM 896 C THR A 107 -3.514 -24.909 23.182 1.00 12.24 C ANISOU 896 C THR A 107 1678 1121 1852 62 -26 83 C ATOM 897 O THR A 107 -2.971 -24.521 22.144 1.00 11.90 O ANISOU 897 O THR A 107 1614 1087 1820 80 -26 75 O ATOM 898 CB THR A 107 -1.589 -25.963 24.363 1.00 13.24 C ANISOU 898 CB THR A 107 1839 1235 1955 126 -48 97 C ATOM 899 OG1 THR A 107 -2.140 -27.287 24.357 1.00 15.02 O ANISOU 899 OG1 THR A 107 2125 1417 2166 118 -49 106 O ATOM 900 CG2 THR A 107 -0.609 -25.824 25.520 1.00 13.69 C ANISOU 900 CG2 THR A 107 1889 1312 2000 156 -61 103 C ATOM 901 N LYS A 108 -4.778 -25.326 23.220 1.00 11.66 N ANISOU 901 N LYS A 108 1623 1035 1773 24 -19 83 N ATOM 902 CA LYS A 108 -5.650 -25.209 22.053 1.00 11.71 C ANISOU 902 CA LYS A 108 1618 1044 1787 3 -13 72 C ATOM 903 C LYS A 108 -6.309 -23.832 21.979 1.00 10.56 C ANISOU 903 C LYS A 108 1424 933 1654 -10 -7 64 C ATOM 904 O LYS A 108 -7.278 -23.647 21.247 1.00 10.76 O ANISOU 904 O LYS A 108 1436 969 1682 -29 -3 55 O ATOM 905 CB LYS A 108 -6.725 -26.301 22.039 1.00 12.05 C ANISOU 905 CB LYS A 108 1697 1064 1816 -36 -8 71 C ATOM 906 CG LYS A 108 -6.307 -27.558 21.317 1.00 14.69 C ANISOU 906 CG LYS A 108 2080 1359 2143 -23 -13 70 C ATOM 907 CD LYS A 108 -6.001 -28.693 22.270 1.00 17.58 C ANISOU 907 CD LYS A 108 2505 1685 2491 -22 -17 85 C ATOM 908 CE LYS A 108 -5.732 -29.982 21.504 1.00 19.29 C ANISOU 908 CE LYS A 108 2777 1853 2698 -10 -21 81 C ATOM 909 NZ LYS A 108 -6.944 -30.437 20.761 1.00 21.66 N ANISOU 909 NZ LYS A 108 3089 2145 2996 -62 -13 66 N ATOM 910 N THR A 109 -5.794 -22.880 22.750 1.00 9.50 N ANISOU 910 N THR A 109 1266 816 1526 2 -8 66 N ATOM 911 CA THR A 109 -6.314 -21.514 22.729 1.00 8.93 C ANISOU 911 CA THR A 109 1157 771 1467 -3 -3 58 C ATOM 912 C THR A 109 -5.173 -20.491 22.700 1.00 8.29 C ANISOU 912 C THR A 109 1054 698 1397 20 -6 57 C ATOM 913 O THR A 109 -4.015 -20.823 22.990 1.00 7.89 O ANISOU 913 O THR A 109 1010 643 1343 39 -11 62 O ATOM 914 CB THR A 109 -7.238 -21.215 23.946 1.00 8.90 C ANISOU 914 CB THR A 109 1144 782 1454 -27 2 55 C ATOM 915 OG1 THR A 109 -6.464 -21.220 25.148 1.00 9.40 O ANISOU 915 OG1 THR A 109 1215 845 1510 -18 -1 62 O ATOM 916 CG2 THR A 109 -8.380 -22.238 24.068 1.00 9.01 C ANISOU 916 CG2 THR A 109 1177 793 1452 -61 8 55 C ATOM 917 N LEU A 110 -5.507 -19.258 22.339 1.00 7.68 N ANISOU 917 N LEU A 110 953 633 1332 20 -2 51 N ATOM 918 CA LEU A 110 -4.580 -18.132 22.463 1.00 7.83 C ANISOU 918 CA LEU A 110 955 658 1362 30 -2 49 C ATOM 919 C LEU A 110 -5.354 -16.819 22.523 1.00 7.39 C ANISOU 919 C LEU A 110 885 608 1316 25 2 42 C ATOM 920 O LEU A 110 -6.535 -16.769 22.159 1.00 7.13 O ANISOU 920 O LEU A 110 850 580 1281 21 4 38 O ATOM 921 CB LEU A 110 -3.531 -18.115 21.328 1.00 7.99 C ANISOU 921 CB LEU A 110 973 676 1388 44 -1 53 C ATOM 922 CG LEU A 110 -3.934 -17.879 19.859 1.00 8.61 C ANISOU 922 CG LEU A 110 1051 751 1469 47 3 55 C ATOM 923 CD1 LEU A 110 -4.326 -16.435 19.590 1.00 8.48 C ANISOU 923 CD1 LEU A 110 1024 735 1462 44 7 54 C ATOM 924 CD2 LEU A 110 -2.777 -18.262 18.930 1.00 9.38 C ANISOU 924 CD2 LEU A 110 1148 850 1564 61 6 58 C ATOM 925 N MET A 111 -4.676 -15.769 22.977 1.00 6.99 N ANISOU 925 N MET A 111 824 558 1273 26 3 37 N ATOM 926 CA MET A 111 -5.256 -14.429 23.048 1.00 6.94 C ANISOU 926 CA MET A 111 812 548 1275 27 6 29 C ATOM 927 C MET A 111 -4.372 -13.406 22.362 1.00 7.25 C ANISOU 927 C MET A 111 853 576 1326 27 10 31 C ATOM 928 O MET A 111 -3.148 -13.559 22.325 1.00 7.66 O ANISOU 928 O MET A 111 900 631 1378 22 11 34 O ATOM 929 CB MET A 111 -5.453 -13.997 24.505 1.00 6.38 C ANISOU 929 CB MET A 111 737 487 1202 21 6 16 C ATOM 930 CG MET A 111 -6.422 -14.850 25.303 1.00 6.03 C ANISOU 930 CG MET A 111 691 457 1142 14 6 13 C ATOM 931 SD MET A 111 -6.741 -14.174 26.938 1.00 6.64 S ANISOU 931 SD MET A 111 761 550 1211 9 8 -4 S ATOM 932 CE MET A 111 -5.089 -14.220 27.652 1.00 5.10 C ANISOU 932 CE MET A 111 569 355 1015 6 1 -3 C ATOM 933 N PHE A 112 -4.998 -12.371 21.814 1.00 7.39 N ANISOU 933 N PHE A 112 878 581 1351 34 12 31 N ATOM 934 CA PHE A 112 -4.284 -11.165 21.423 1.00 8.16 C ANISOU 934 CA PHE A 112 985 659 1457 28 18 33 C ATOM 935 C PHE A 112 -4.703 -10.022 22.335 1.00 8.22 C ANISOU 935 C PHE A 112 1000 654 1471 29 17 18 C ATOM 936 O PHE A 112 -5.898 -9.785 22.560 1.00 7.66 O ANISOU 936 O PHE A 112 930 584 1397 46 14 10 O ATOM 937 CB PHE A 112 -4.540 -10.795 19.962 1.00 8.38 C ANISOU 937 CB PHE A 112 1027 673 1484 38 21 47 C ATOM 938 CG PHE A 112 -3.975 -11.779 18.982 1.00 10.02 C ANISOU 938 CG PHE A 112 1230 894 1685 37 23 59 C ATOM 939 CD1 PHE A 112 -2.641 -12.170 19.056 1.00 11.47 C ANISOU 939 CD1 PHE A 112 1403 1087 1868 23 28 59 C ATOM 940 CD2 PHE A 112 -4.771 -12.304 17.973 1.00 10.96 C ANISOU 940 CD2 PHE A 112 1352 1017 1795 51 19 66 C ATOM 941 CE1 PHE A 112 -2.119 -13.081 18.148 1.00 11.80 C ANISOU 941 CE1 PHE A 112 1440 1142 1901 28 31 67 C ATOM 942 CE2 PHE A 112 -4.253 -13.220 17.060 1.00 11.49 C ANISOU 942 CE2 PHE A 112 1418 1095 1854 51 22 73 C ATOM 943 CZ PHE A 112 -2.931 -13.610 17.154 1.00 11.12 C ANISOU 943 CZ PHE A 112 1362 1056 1807 42 28 73 C ATOM 944 N GLY A 113 -3.711 -9.333 22.879 1.00 8.27 N ANISOU 944 N GLY A 113 1009 652 1483 9 21 10 N ATOM 945 CA GLY A 113 -3.980 -8.202 23.754 1.00 9.01 C ANISOU 945 CA GLY A 113 1115 729 1582 8 21 -8 C ATOM 946 C GLY A 113 -3.802 -6.901 23.005 1.00 9.55 C ANISOU 946 C GLY A 113 1213 757 1658 4 27 -3 C ATOM 947 O GLY A 113 -2.783 -6.702 22.342 1.00 9.41 O ANISOU 947 O GLY A 113 1201 733 1644 -20 35 7 O ATOM 948 N SER A 114 -4.798 -6.028 23.107 1.00 9.95 N ANISOU 948 N SER A 114 1285 785 1711 27 24 -11 N ATOM 949 CA SER A 114 -4.757 -4.725 22.454 1.00 10.99 C ANISOU 949 CA SER A 114 1457 869 1848 29 28 -5 C ATOM 950 C SER A 114 -4.669 -3.611 23.486 1.00 11.43 C ANISOU 950 C SER A 114 1536 898 1911 22 29 -30 C ATOM 951 O SER A 114 -5.396 -3.624 24.487 1.00 11.38 O ANISOU 951 O SER A 114 1518 904 1901 41 23 -52 O ATOM 952 CB SER A 114 -6.005 -4.520 21.589 1.00 11.12 C ANISOU 952 CB SER A 114 1489 875 1860 73 22 6 C ATOM 953 OG SER A 114 -6.132 -5.556 20.631 1.00 12.19 O ANISOU 953 OG SER A 114 1605 1038 1987 78 20 26 O ATOM 954 N TYR A 115 -3.789 -2.648 23.220 1.00 11.91 N ANISOU 954 N TYR A 115 1628 919 1978 -10 38 -28 N ATOM 955 CA TYR A 115 -3.565 -1.474 24.082 1.00 12.69 C ANISOU 955 CA TYR A 115 1757 981 2082 -25 39 -53 C ATOM 956 C TYR A 115 -3.404 -1.813 25.567 1.00 12.65 C ANISOU 956 C TYR A 115 1721 1010 2075 -36 34 -85 C ATOM 957 O TYR A 115 -3.945 -1.120 26.431 1.00 13.17 O ANISOU 957 O TYR A 115 1804 1060 2142 -20 30 -111 O ATOM 958 CB TYR A 115 -4.670 -0.418 23.905 1.00 13.09 C ANISOU 958 CB TYR A 115 1856 983 2134 19 35 -57 C ATOM 959 CG TYR A 115 -5.129 -0.144 22.481 1.00 14.05 C ANISOU 959 CG TYR A 115 2010 1076 2252 46 35 -25 C ATOM 960 CD1 TYR A 115 -6.466 -0.299 22.132 1.00 14.58 C ANISOU 960 CD1 TYR A 115 2074 1154 2313 107 23 -21 C ATOM 961 CD2 TYR A 115 -4.238 0.294 21.494 1.00 15.36 C ANISOU 961 CD2 TYR A 115 2208 1209 2418 10 46 0 C ATOM 962 CE1 TYR A 115 -6.914 -0.034 20.844 1.00 15.91 C ANISOU 962 CE1 TYR A 115 2272 1300 2473 136 19 7 C ATOM 963 CE2 TYR A 115 -4.678 0.556 20.188 1.00 16.08 C ANISOU 963 CE2 TYR A 115 2333 1275 2501 36 46 32 C ATOM 964 CZ TYR A 115 -6.023 0.389 19.877 1.00 16.40 C ANISOU 964 CZ TYR A 115 2371 1326 2534 102 31 35 C ATOM 965 OH TYR A 115 -6.495 0.639 18.605 1.00 17.55 O ANISOU 965 OH TYR A 115 2548 1452 2667 134 27 65 O ATOM 966 N LEU A 116 -2.641 -2.865 25.851 1.00 12.65 N ANISOU 966 N LEU A 116 1678 1058 2071 -59 34 -82 N ATOM 967 CA LEU A 116 -2.468 -3.379 27.209 1.00 12.84 C ANISOU 967 CA LEU A 116 1671 1122 2087 -65 27 -106 C ATOM 968 C LEU A 116 -1.743 -2.432 28.167 1.00 13.59 C ANISOU 968 C LEU A 116 1778 1203 2184 -99 27 -137 C ATOM 969 O LEU A 116 -1.775 -2.630 29.385 1.00 13.75 O ANISOU 969 O LEU A 116 1780 1251 2194 -98 21 -161 O ATOM 970 CB LEU A 116 -1.744 -4.732 27.182 1.00 12.60 C ANISOU 970 CB LEU A 116 1598 1142 2049 -76 24 -93 C ATOM 971 CG LEU A 116 -2.409 -5.946 26.516 1.00 12.11 C ANISOU 971 CG LEU A 116 1519 1101 1981 -47 22 -68 C ATOM 972 CD1 LEU A 116 -1.588 -7.193 26.822 1.00 11.46 C ANISOU 972 CD1 LEU A 116 1403 1062 1889 -56 17 -63 C ATOM 973 CD2 LEU A 116 -3.859 -6.141 26.958 1.00 11.64 C ANISOU 973 CD2 LEU A 116 1460 1047 1916 -12 17 -75 C ATOM 974 N ASP A 117 -1.085 -1.417 27.617 1.00 14.29 N ANISOU 974 N ASP A 117 1899 1249 2281 -131 36 -137 N ATOM 975 CA ASP A 117 -0.410 -0.398 28.428 1.00 15.19 C ANISOU 975 CA ASP A 117 2033 1342 2397 -171 38 -170 C ATOM 976 C ASP A 117 -1.394 0.650 28.934 1.00 15.25 C ANISOU 976 C ASP A 117 2086 1301 2408 -143 35 -192 C ATOM 977 O ASP A 117 -1.110 1.368 29.888 1.00 16.10 O ANISOU 977 O ASP A 117 2207 1396 2514 -164 34 -227 O ATOM 978 CB ASP A 117 0.734 0.272 27.644 1.00 15.55 C ANISOU 978 CB ASP A 117 2097 1361 2449 -228 51 -162 C ATOM 979 CG ASP A 117 0.310 0.769 26.247 1.00 17.62 C ANISOU 979 CG ASP A 117 2405 1570 2718 -216 61 -129 C ATOM 980 OD1 ASP A 117 -0.740 0.333 25.704 1.00 19.10 O ANISOU 980 OD1 ASP A 117 2596 1755 2905 -162 56 -108 O ATOM 981 OD2 ASP A 117 1.064 1.588 25.669 1.00 18.22 O ANISOU 981 OD2 ASP A 117 2514 1610 2798 -264 75 -123 O ATOM 982 N ASP A 118 -2.558 0.718 28.299 1.00 14.93 N ANISOU 982 N ASP A 118 2067 1237 2369 -91 34 -175 N ATOM 983 CA ASP A 118 -3.520 1.781 28.551 1.00 14.77 C ANISOU 983 CA ASP A 118 2093 1166 2351 -54 32 -195 C ATOM 984 C ASP A 118 -4.839 1.240 29.105 1.00 14.51 C ANISOU 984 C ASP A 118 2034 1170 2309 5 24 -205 C ATOM 985 O ASP A 118 -5.622 0.609 28.385 1.00 14.24 O ANISOU 985 O ASP A 118 1984 1155 2273 42 21 -181 O ATOM 986 CB ASP A 118 -3.742 2.574 27.260 1.00 14.75 C ANISOU 986 CB ASP A 118 2147 1099 2356 -42 37 -168 C ATOM 987 CG ASP A 118 -4.750 3.694 27.418 1.00 15.08 C ANISOU 987 CG ASP A 118 2246 1084 2400 8 33 -185 C ATOM 988 OD1 ASP A 118 -5.131 4.037 28.561 1.00 13.72 O ANISOU 988 OD1 ASP A 118 2074 916 2224 24 28 -224 O ATOM 989 OD2 ASP A 118 -5.167 4.230 26.373 1.00 14.92 O ANISOU 989 OD2 ASP A 118 2271 1017 2381 35 33 -161 O ATOM 990 N GLU A 119 -5.077 1.506 30.389 1.00 14.63 N ANISOU 990 N GLU A 119 2045 1199 2317 11 20 -243 N ATOM 991 CA GLU A 119 -6.286 1.054 31.074 1.00 14.66 C ANISOU 991 CA GLU A 119 2019 1244 2307 60 16 -258 C ATOM 992 C GLU A 119 -7.571 1.685 30.553 1.00 14.24 C ANISOU 992 C GLU A 119 1994 1162 2255 124 14 -260 C ATOM 993 O GLU A 119 -8.656 1.171 30.799 1.00 14.36 O ANISOU 993 O GLU A 119 1976 1220 2258 165 11 -265 O ATOM 994 CB GLU A 119 -6.168 1.229 32.597 1.00 15.28 C ANISOU 994 CB GLU A 119 2087 1347 2372 50 15 -301 C ATOM 995 CG GLU A 119 -5.948 2.660 33.100 1.00 18.51 C ANISOU 995 CG GLU A 119 2549 1698 2786 43 15 -338 C ATOM 996 CD GLU A 119 -5.241 2.698 34.460 1.00 22.13 C ANISOU 996 CD GLU A 119 2993 2186 3231 6 13 -375 C ATOM 997 OE1 GLU A 119 -5.212 3.782 35.088 1.00 23.26 O ANISOU 997 OE1 GLU A 119 3175 2290 3374 4 12 -415 O ATOM 998 OE2 GLU A 119 -4.703 1.643 34.894 1.00 23.33 O ANISOU 998 OE2 GLU A 119 3095 2397 3371 -20 10 -365 O ATOM 999 N LYS A 120 -7.452 2.790 29.827 1.00 13.84 N ANISOU 999 N LYS A 120 2003 1040 2216 131 14 -255 N ATOM 1000 CA LYS A 120 -8.625 3.421 29.222 1.00 13.12 C ANISOU 1000 CA LYS A 120 1943 918 2123 200 8 -253 C ATOM 1001 C LYS A 120 -9.040 2.716 27.923 1.00 11.77 C ANISOU 1001 C LYS A 120 1753 766 1952 220 5 -210 C ATOM 1002 O LYS A 120 -10.182 2.842 27.481 1.00 11.48 O ANISOU 1002 O LYS A 120 1717 735 1909 283 -3 -208 O ATOM 1003 CB LYS A 120 -8.373 4.910 28.962 1.00 13.75 C ANISOU 1003 CB LYS A 120 2105 906 2212 205 8 -262 C ATOM 1004 CG LYS A 120 -7.888 5.696 30.177 1.00 14.80 C ANISOU 1004 CG LYS A 120 2265 1013 2346 178 11 -307 C ATOM 1005 CD LYS A 120 -8.180 7.189 30.018 1.00 16.53 C ANISOU 1005 CD LYS A 120 2571 1140 2569 211 9 -324 C ATOM 1006 CE LYS A 120 -7.522 8.026 31.115 1.00 18.55 C ANISOU 1006 CE LYS A 120 2863 1359 2827 172 12 -370 C ATOM 1007 NZ LYS A 120 -6.044 8.222 30.922 1.00 19.66 N ANISOU 1007 NZ LYS A 120 3023 1468 2977 79 22 -360 N ATOM 1008 N ASN A 121 -8.118 1.973 27.313 1.00 10.03 N ANISOU 1008 N ASN A 121 1515 559 1738 170 10 -179 N ATOM 1009 CA ASN A 121 -8.400 1.383 26.008 1.00 9.00 C ANISOU 1009 CA ASN A 121 1374 440 1605 186 8 -141 C ATOM 1010 C ASN A 121 -8.157 -0.131 25.855 1.00 7.82 C ANISOU 1010 C ASN A 121 1164 356 1452 160 10 -122 C ATOM 1011 O ASN A 121 -8.444 -0.695 24.801 1.00 6.82 O ANISOU 1011 O ASN A 121 1027 243 1322 172 7 -94 O ATOM 1012 CB ASN A 121 -7.641 2.149 24.922 1.00 9.10 C ANISOU 1012 CB ASN A 121 1444 387 1625 163 13 -113 C ATOM 1013 CG ASN A 121 -8.220 3.524 24.674 1.00 9.83 C ANISOU 1013 CG ASN A 121 1607 410 1718 208 8 -119 C ATOM 1014 OD1 ASN A 121 -9.137 3.681 23.871 1.00 9.59 O ANISOU 1014 OD1 ASN A 121 1590 372 1680 265 -2 -103 O ATOM 1015 ND2 ASN A 121 -7.687 4.529 25.363 1.00 8.67 N ANISOU 1015 ND2 ASN A 121 1506 210 1578 184 13 -143 N ATOM 1016 N TRP A 122 -7.641 -0.782 26.892 1.00 7.22 N ANISOU 1016 N TRP A 122 1053 318 1373 126 13 -138 N ATOM 1017 CA TRP A 122 -7.208 -2.178 26.745 1.00 6.73 C ANISOU 1017 CA TRP A 122 945 306 1307 99 14 -119 C ATOM 1018 C TRP A 122 -8.324 -3.183 26.435 1.00 6.53 C ANISOU 1018 C TRP A 122 884 326 1272 130 10 -110 C ATOM 1019 O TRP A 122 -9.502 -2.948 26.731 1.00 6.41 O ANISOU 1019 O TRP A 122 861 325 1248 171 6 -127 O ATOM 1020 CB TRP A 122 -6.328 -2.646 27.915 1.00 6.59 C ANISOU 1020 CB TRP A 122 902 316 1285 59 16 -136 C ATOM 1021 CG TRP A 122 -6.948 -2.624 29.284 1.00 6.77 C ANISOU 1021 CG TRP A 122 910 367 1297 73 15 -168 C ATOM 1022 CD1 TRP A 122 -8.271 -2.814 29.610 1.00 7.52 C ANISOU 1022 CD1 TRP A 122 988 490 1381 113 13 -180 C ATOM 1023 CD2 TRP A 122 -6.255 -2.452 30.525 1.00 8.62 C ANISOU 1023 CD2 TRP A 122 1139 612 1524 45 14 -194 C ATOM 1024 NE1 TRP A 122 -8.440 -2.752 30.974 1.00 7.57 N ANISOU 1024 NE1 TRP A 122 981 522 1373 111 15 -210 N ATOM 1025 CE2 TRP A 122 -7.221 -2.531 31.561 1.00 8.36 C ANISOU 1025 CE2 TRP A 122 1090 610 1475 71 14 -219 C ATOM 1026 CE3 TRP A 122 -4.911 -2.228 30.865 1.00 9.87 C ANISOU 1026 CE3 TRP A 122 1302 763 1686 0 14 -200 C ATOM 1027 CZ2 TRP A 122 -6.888 -2.393 32.907 1.00 8.91 C ANISOU 1027 CZ2 TRP A 122 1153 701 1532 55 13 -249 C ATOM 1028 CZ3 TRP A 122 -4.576 -2.093 32.210 1.00 10.59 C ANISOU 1028 CZ3 TRP A 122 1383 876 1764 -16 11 -232 C ATOM 1029 CH2 TRP A 122 -5.564 -2.175 33.216 1.00 11.01 C ANISOU 1029 CH2 TRP A 122 1425 957 1801 13 11 -255 C ATOM 1030 N GLY A 123 -7.935 -4.288 25.801 1.00 6.19 N ANISOU 1030 N GLY A 123 818 307 1227 111 11 -85 N ATOM 1031 CA GLY A 123 -8.858 -5.364 25.490 1.00 5.86 C ANISOU 1031 CA GLY A 123 743 307 1174 127 8 -77 C ATOM 1032 C GLY A 123 -8.172 -6.660 25.121 1.00 5.72 C ANISOU 1032 C GLY A 123 706 313 1155 98 10 -56 C ATOM 1033 O GLY A 123 -6.955 -6.699 24.923 1.00 5.24 O ANISOU 1033 O GLY A 123 654 237 1101 70 13 -45 O ATOM 1034 N LEU A 124 -8.971 -7.720 25.024 1.00 6.06 N ANISOU 1034 N LEU A 124 722 392 1187 104 8 -52 N ATOM 1035 CA LEU A 124 -8.492 -9.054 24.690 1.00 6.13 C ANISOU 1035 CA LEU A 124 718 420 1192 81 9 -35 C ATOM 1036 C LEU A 124 -9.401 -9.718 23.676 1.00 6.45 C ANISOU 1036 C LEU A 124 748 477 1226 94 6 -24 C ATOM 1037 O LEU A 124 -10.634 -9.610 23.764 1.00 6.38 O ANISOU 1037 O LEU A 124 724 491 1209 114 3 -37 O ATOM 1038 CB LEU A 124 -8.429 -9.935 25.938 1.00 6.29 C ANISOU 1038 CB LEU A 124 721 468 1201 62 11 -43 C ATOM 1039 CG LEU A 124 -7.373 -9.615 26.989 1.00 6.79 C ANISOU 1039 CG LEU A 124 788 526 1264 45 12 -52 C ATOM 1040 CD1 LEU A 124 -7.796 -10.197 28.321 1.00 7.39 C ANISOU 1040 CD1 LEU A 124 851 633 1323 37 13 -65 C ATOM 1041 CD2 LEU A 124 -6.021 -10.157 26.567 1.00 7.54 C ANISOU 1041 CD2 LEU A 124 887 614 1364 26 10 -36 C ATOM 1042 N SER A 125 -8.781 -10.398 22.713 1.00 6.24 N ANISOU 1042 N SER A 125 726 445 1201 83 5 -5 N ATOM 1043 CA SER A 125 -9.498 -11.249 21.786 1.00 6.78 C ANISOU 1043 CA SER A 125 784 532 1261 88 2 3 C ATOM 1044 C SER A 125 -9.086 -12.706 22.027 1.00 6.61 C ANISOU 1044 C SER A 125 757 523 1233 62 4 9 C ATOM 1045 O SER A 125 -7.926 -12.988 22.311 1.00 6.49 O ANISOU 1045 O SER A 125 749 497 1222 49 6 15 O ATOM 1046 CB SER A 125 -9.250 -10.803 20.351 1.00 6.95 C ANISOU 1046 CB SER A 125 822 533 1284 102 -1 19 C ATOM 1047 OG SER A 125 -9.597 -9.435 20.196 1.00 8.53 O ANISOU 1047 OG SER A 125 1038 714 1489 128 -4 16 O ATOM 1048 N PHE A 126 -10.055 -13.609 21.918 1.00 6.78 N ANISOU 1048 N PHE A 126 765 570 1243 56 3 5 N ATOM 1049 CA PHE A 126 -9.940 -15.000 22.365 1.00 6.77 C ANISOU 1049 CA PHE A 126 764 575 1231 30 5 8 C ATOM 1050 C PHE A 126 -10.136 -15.949 21.183 1.00 6.75 C ANISOU 1050 C PHE A 126 767 574 1223 24 2 15 C ATOM 1051 O PHE A 126 -11.149 -15.870 20.479 1.00 6.95 O ANISOU 1051 O PHE A 126 779 619 1243 30 -2 8 O ATOM 1052 CB PHE A 126 -10.991 -15.259 23.471 1.00 7.10 C ANISOU 1052 CB PHE A 126 791 647 1262 16 10 -6 C ATOM 1053 CG PHE A 126 -11.053 -16.692 23.972 1.00 7.42 C ANISOU 1053 CG PHE A 126 839 692 1287 -15 15 -1 C ATOM 1054 CD1 PHE A 126 -9.900 -17.364 24.392 1.00 7.23 C ANISOU 1054 CD1 PHE A 126 839 646 1263 -22 14 13 C ATOM 1055 CD2 PHE A 126 -12.282 -17.351 24.065 1.00 6.48 C ANISOU 1055 CD2 PHE A 126 707 602 1154 -38 20 -10 C ATOM 1056 CE1 PHE A 126 -9.963 -18.690 24.863 1.00 8.17 C ANISOU 1056 CE1 PHE A 126 976 761 1366 -47 17 20 C ATOM 1057 CE2 PHE A 126 -12.352 -18.679 24.535 1.00 8.17 C ANISOU 1057 CE2 PHE A 126 938 813 1352 -73 26 -3 C ATOM 1058 CZ PHE A 126 -11.191 -19.348 24.933 1.00 7.53 C ANISOU 1058 CZ PHE A 126 890 700 1270 -75 24 14 C ATOM 1059 N TYR A 127 -9.166 -16.841 20.979 1.00 6.27 N ANISOU 1059 N TYR A 127 724 497 1163 16 3 26 N ATOM 1060 CA TYR A 127 -9.128 -17.726 19.809 1.00 6.05 C ANISOU 1060 CA TYR A 127 706 463 1129 13 0 30 C ATOM 1061 C TYR A 127 -8.917 -19.187 20.214 1.00 6.26 C ANISOU 1061 C TYR A 127 753 480 1146 -6 1 33 C ATOM 1062 O TYR A 127 -8.278 -19.460 21.225 1.00 5.62 O ANISOU 1062 O TYR A 127 682 389 1064 -9 3 38 O ATOM 1063 CB TYR A 127 -8.002 -17.293 18.869 1.00 5.62 C ANISOU 1063 CB TYR A 127 659 393 1082 32 -1 41 C ATOM 1064 CG TYR A 127 -8.086 -15.846 18.447 1.00 5.96 C ANISOU 1064 CG TYR A 127 696 436 1133 49 -1 43 C ATOM 1065 CD1 TYR A 127 -7.562 -14.826 19.251 1.00 5.92 C ANISOU 1065 CD1 TYR A 127 690 421 1138 52 3 42 C ATOM 1066 CD2 TYR A 127 -8.705 -15.490 17.255 1.00 4.88 C ANISOU 1066 CD2 TYR A 127 557 305 990 62 -5 44 C ATOM 1067 CE1 TYR A 127 -7.647 -13.492 18.861 1.00 6.61 C ANISOU 1067 CE1 TYR A 127 781 499 1232 66 3 45 C ATOM 1068 CE2 TYR A 127 -8.794 -14.165 16.862 1.00 5.70 C ANISOU 1068 CE2 TYR A 127 664 402 1098 81 -6 50 C ATOM 1069 CZ TYR A 127 -8.263 -13.174 17.659 1.00 5.87 C ANISOU 1069 CZ TYR A 127 691 408 1132 83 -1 50 C ATOM 1070 OH TYR A 127 -8.358 -11.865 17.250 1.00 8.06 O ANISOU 1070 OH TYR A 127 981 669 1412 101 -2 56 O ATOM 1071 N ALA A 128 -9.444 -20.118 19.419 1.00 6.79 N ANISOU 1071 N ALA A 128 829 547 1205 -19 -1 29 N ATOM 1072 CA ALA A 128 -9.324 -21.553 19.718 1.00 7.48 C ANISOU 1072 CA ALA A 128 946 615 1281 -40 0 31 C ATOM 1073 C ALA A 128 -9.233 -22.358 18.440 1.00 8.03 C ANISOU 1073 C ALA A 128 1032 673 1345 -39 -4 27 C ATOM 1074 O ALA A 128 -9.526 -21.839 17.365 1.00 8.45 O ANISOU 1074 O ALA A 128 1070 742 1400 -28 -7 22 O ATOM 1075 CB ALA A 128 -10.508 -22.032 20.562 1.00 7.79 C ANISOU 1075 CB ALA A 128 982 669 1307 -76 6 24 C ATOM 1076 N ASP A 129 -8.836 -23.626 18.557 1.00 8.71 N ANISOU 1076 N ASP A 129 1155 731 1423 -47 -4 30 N ATOM 1077 CA ASP A 129 -8.678 -24.493 17.383 1.00 9.42 C ANISOU 1077 CA ASP A 129 1268 804 1506 -45 -7 22 C ATOM 1078 C ASP A 129 -10.019 -25.018 16.844 1.00 9.63 C ANISOU 1078 C ASP A 129 1294 844 1522 -82 -8 6 C ATOM 1079 O ASP A 129 -10.059 -25.626 15.773 1.00 9.48 O ANISOU 1079 O ASP A 129 1289 817 1495 -84 -12 -5 O ATOM 1080 CB ASP A 129 -7.681 -25.637 17.657 1.00 9.58 C ANISOU 1080 CB ASP A 129 1333 785 1521 -32 -9 28 C ATOM 1081 CG ASP A 129 -8.259 -26.739 18.525 1.00 10.99 C ANISOU 1081 CG ASP A 129 1550 938 1687 -66 -7 31 C ATOM 1082 OD1 ASP A 129 -9.148 -26.472 19.358 1.00 10.06 O ANISOU 1082 OD1 ASP A 129 1418 838 1567 -98 -1 32 O ATOM 1083 OD2 ASP A 129 -7.798 -27.893 18.383 1.00 15.12 O ANISOU 1083 OD2 ASP A 129 2121 1422 2201 -61 -9 31 O ATOM 1084 N LYS A 130 -11.093 -24.785 17.604 1.00 9.56 N ANISOU 1084 N LYS A 130 1264 859 1509 -113 -3 2 N ATOM 1085 CA LYS A 130 -12.468 -25.123 17.205 1.00 10.10 C ANISOU 1085 CA LYS A 130 1318 955 1566 -153 -3 -17 C ATOM 1086 C LYS A 130 -13.325 -23.870 17.377 1.00 9.97 C ANISOU 1086 C LYS A 130 1248 989 1552 -146 -4 -24 C ATOM 1087 O LYS A 130 -12.968 -23.016 18.184 1.00 9.59 O ANISOU 1087 O LYS A 130 1187 943 1514 -125 -1 -13 O ATOM 1088 CB LYS A 130 -13.022 -26.243 18.081 1.00 9.94 C ANISOU 1088 CB LYS A 130 1327 919 1532 -205 6 -19 C ATOM 1089 CG LYS A 130 -12.267 -27.553 17.958 1.00 11.96 C ANISOU 1089 CG LYS A 130 1645 1116 1782 -210 5 -13 C ATOM 1090 CD LYS A 130 -12.772 -28.573 18.952 1.00 14.59 C ANISOU 1090 CD LYS A 130 2017 1427 2100 -262 16 -9 C ATOM 1091 CE LYS A 130 -11.952 -29.850 18.876 1.00 16.92 C ANISOU 1091 CE LYS A 130 2385 1655 2388 -257 13 -1 C ATOM 1092 NZ LYS A 130 -12.082 -30.623 20.149 1.00 18.74 N ANISOU 1092 NZ LYS A 130 2661 1854 2604 -292 23 16 N ATOM 1093 N PRO A 131 -14.455 -23.754 16.630 1.00 10.51 N ANISOU 1093 N PRO A 131 1285 1098 1610 -161 -9 -43 N ATOM 1094 CA PRO A 131 -15.329 -22.575 16.780 1.00 10.65 C ANISOU 1094 CA PRO A 131 1252 1166 1629 -145 -13 -52 C ATOM 1095 C PRO A 131 -16.156 -22.585 18.071 1.00 11.22 C ANISOU 1095 C PRO A 131 1303 1265 1694 -177 -1 -59 C ATOM 1096 O PRO A 131 -16.749 -21.567 18.428 1.00 11.77 O ANISOU 1096 O PRO A 131 1333 1373 1765 -156 -2 -66 O ATOM 1097 CB PRO A 131 -16.243 -22.659 15.556 1.00 10.91 C ANISOU 1097 CB PRO A 131 1259 1238 1647 -150 -24 -72 C ATOM 1098 CG PRO A 131 -16.321 -24.138 15.251 1.00 11.10 C ANISOU 1098 CG PRO A 131 1317 1241 1660 -199 -21 -82 C ATOM 1099 CD PRO A 131 -14.962 -24.685 15.597 1.00 10.92 C ANISOU 1099 CD PRO A 131 1347 1154 1649 -189 -15 -61 C ATOM 1100 N GLU A 132 -16.201 -23.727 18.754 1.00 11.52 N ANISOU 1100 N GLU A 132 1371 1284 1724 -225 10 -57 N ATOM 1101 CA GLU A 132 -16.896 -23.851 20.033 1.00 12.39 C ANISOU 1101 CA GLU A 132 1467 1417 1822 -262 25 -61 C ATOM 1102 C GLU A 132 -15.881 -24.150 21.141 1.00 11.85 C ANISOU 1102 C GLU A 132 1442 1302 1759 -260 33 -36 C ATOM 1103 O GLU A 132 -14.998 -24.983 20.954 1.00 12.01 O ANISOU 1103 O GLU A 132 1512 1270 1780 -260 31 -22 O ATOM 1104 CB GLU A 132 -17.944 -24.973 19.976 1.00 13.06 C ANISOU 1104 CB GLU A 132 1553 1523 1887 -332 34 -79 C ATOM 1105 CG GLU A 132 -19.338 -24.545 19.491 1.00 16.78 C ANISOU 1105 CG GLU A 132 1959 2071 2346 -346 30 -109 C ATOM 1106 CD GLU A 132 -19.547 -24.627 17.974 1.00 19.59 C ANISOU 1106 CD GLU A 132 2303 2439 2700 -333 12 -125 C ATOM 1107 OE1 GLU A 132 -19.283 -25.706 17.373 1.00 20.66 O ANISOU 1107 OE1 GLU A 132 2481 2538 2831 -365 11 -127 O ATOM 1108 OE2 GLU A 132 -20.013 -23.611 17.397 1.00 19.51 O ANISOU 1108 OE2 GLU A 132 2246 2477 2691 -291 -1 -137 O ATOM 1109 N THR A 133 -16.016 -23.485 22.288 1.00 11.47 N ANISOU 1109 N THR A 133 1374 1274 1709 -254 42 -34 N ATOM 1110 CA THR A 133 -15.109 -23.696 23.422 1.00 11.21 C ANISOU 1110 CA THR A 133 1379 1206 1676 -250 48 -12 C ATOM 1111 C THR A 133 -15.810 -24.298 24.632 1.00 11.63 C ANISOU 1111 C THR A 133 1437 1275 1705 -302 65 -11 C ATOM 1112 O THR A 133 -17.030 -24.187 24.777 1.00 11.58 O ANISOU 1112 O THR A 133 1393 1322 1686 -335 75 -31 O ATOM 1113 CB THR A 133 -14.405 -22.389 23.865 1.00 10.78 C ANISOU 1113 CB THR A 133 1304 1154 1636 -198 42 -7 C ATOM 1114 OG1 THR A 133 -15.364 -21.332 23.958 1.00 10.56 O ANISOU 1114 OG1 THR A 133 1225 1178 1609 -188 44 -27 O ATOM 1115 CG2 THR A 133 -13.325 -22.001 22.874 1.00 10.39 C ANISOU 1115 CG2 THR A 133 1267 1074 1607 -154 28 1 C ATOM 1116 N THR A 134 -15.026 -24.933 25.499 1.00 11.74 N ANISOU 1116 N THR A 134 1501 1249 1712 -309 69 11 N ATOM 1117 CA THR A 134 -15.550 -25.529 26.725 1.00 12.25 C ANISOU 1117 CA THR A 134 1582 1323 1749 -358 87 19 C ATOM 1118 C THR A 134 -15.584 -24.494 27.837 1.00 12.04 C ANISOU 1118 C THR A 134 1523 1333 1719 -337 93 16 C ATOM 1119 O THR A 134 -14.946 -23.438 27.730 1.00 11.20 O ANISOU 1119 O THR A 134 1395 1228 1632 -283 81 13 O ATOM 1120 CB THR A 134 -14.699 -26.719 27.188 1.00 12.52 C ANISOU 1120 CB THR A 134 1693 1294 1771 -369 87 47 C ATOM 1121 OG1 THR A 134 -13.361 -26.272 27.451 1.00 12.38 O ANISOU 1121 OG1 THR A 134 1690 1249 1767 -309 72 62 O ATOM 1122 CG2 THR A 134 -14.695 -27.836 26.119 1.00 13.30 C ANISOU 1122 CG2 THR A 134 1833 1350 1871 -391 82 46 C ATOM 1123 N LYS A 135 -16.320 -24.807 28.904 1.00 12.33 N ANISOU 1123 N LYS A 135 1558 1398 1728 -383 113 16 N ATOM 1124 CA LYS A 135 -16.364 -23.945 30.083 1.00 12.73 C ANISOU 1124 CA LYS A 135 1583 1484 1769 -367 120 12 C ATOM 1125 C LYS A 135 -14.984 -23.821 30.743 1.00 11.91 C ANISOU 1125 C LYS A 135 1518 1339 1669 -327 108 35 C ATOM 1126 O LYS A 135 -14.646 -22.762 31.285 1.00 11.94 O ANISOU 1126 O LYS A 135 1495 1361 1679 -290 104 27 O ATOM 1127 CB LYS A 135 -17.460 -24.392 31.073 1.00 13.47 C ANISOU 1127 CB LYS A 135 1667 1623 1827 -430 147 7 C ATOM 1128 CG LYS A 135 -17.021 -25.232 32.268 1.00 15.50 C ANISOU 1128 CG LYS A 135 1984 1852 2055 -459 158 37 C ATOM 1129 CD LYS A 135 -18.227 -25.605 33.150 1.00 18.84 C ANISOU 1129 CD LYS A 135 2391 2328 2439 -529 188 30 C ATOM 1130 CE LYS A 135 -18.666 -27.058 32.959 1.00 21.56 C ANISOU 1130 CE LYS A 135 2787 2642 2762 -604 202 46 C ATOM 1131 NZ LYS A 135 -19.034 -27.405 31.549 1.00 23.52 N ANISOU 1131 NZ LYS A 135 3024 2880 3032 -617 194 29 N ATOM 1132 N GLU A 136 -14.203 -24.899 30.680 1.00 11.47 N ANISOU 1132 N GLU A 136 1524 1227 1608 -332 102 61 N ATOM 1133 CA GLU A 136 -12.812 -24.903 31.133 1.00 11.26 C ANISOU 1133 CA GLU A 136 1531 1162 1583 -288 86 82 C ATOM 1134 C GLU A 136 -12.017 -23.815 30.410 1.00 10.13 C ANISOU 1134 C GLU A 136 1356 1020 1475 -231 68 70 C ATOM 1135 O GLU A 136 -11.357 -22.996 31.052 1.00 9.95 O ANISOU 1135 O GLU A 136 1319 1007 1455 -199 61 68 O ATOM 1136 CB GLU A 136 -12.162 -26.273 30.876 1.00 11.69 C ANISOU 1136 CB GLU A 136 1656 1156 1630 -294 79 108 C ATOM 1137 CG GLU A 136 -12.566 -27.393 31.832 1.00 13.80 C ANISOU 1137 CG GLU A 136 1979 1407 1859 -344 94 130 C ATOM 1138 CD GLU A 136 -13.942 -27.984 31.548 1.00 16.26 C ANISOU 1138 CD GLU A 136 2287 1734 2157 -417 116 119 C ATOM 1139 OE1 GLU A 136 -14.400 -27.960 30.384 1.00 16.56 O ANISOU 1139 OE1 GLU A 136 2301 1777 2216 -425 114 100 O ATOM 1140 OE2 GLU A 136 -14.572 -28.490 32.507 1.00 19.07 O ANISOU 1140 OE2 GLU A 136 2665 2101 2479 -469 136 131 O ATOM 1141 N GLN A 137 -12.101 -23.811 29.076 1.00 9.49 N ANISOU 1141 N GLN A 137 1263 927 1415 -223 62 61 N ATOM 1142 CA GLN A 137 -11.386 -22.851 28.223 1.00 8.80 C ANISOU 1142 CA GLN A 137 1150 836 1356 -175 47 53 C ATOM 1143 C GLN A 137 -11.878 -21.415 28.423 1.00 8.34 C ANISOU 1143 C GLN A 137 1041 819 1309 -159 50 32 C ATOM 1144 O GLN A 137 -11.079 -20.490 28.544 1.00 8.27 O ANISOU 1144 O GLN A 137 1021 807 1314 -124 42 29 O ATOM 1145 CB GLN A 137 -11.514 -23.229 26.742 1.00 8.81 C ANISOU 1145 CB GLN A 137 1154 821 1373 -174 42 48 C ATOM 1146 CG GLN A 137 -10.756 -24.501 26.346 1.00 9.04 C ANISOU 1146 CG GLN A 137 1236 801 1397 -173 35 65 C ATOM 1147 CD GLN A 137 -11.072 -24.966 24.934 1.00 9.40 C ANISOU 1147 CD GLN A 137 1285 835 1451 -180 32 56 C ATOM 1148 OE1 GLN A 137 -12.235 -24.996 24.519 1.00 8.83 O ANISOU 1148 OE1 GLN A 137 1191 788 1375 -213 39 40 O ATOM 1149 NE2 GLN A 137 -10.038 -25.359 24.194 1.00 7.71 N ANISOU 1149 NE2 GLN A 137 1096 587 1246 -148 21 62 N ATOM 1150 N LEU A 138 -13.199 -21.251 28.435 1.00 7.99 N ANISOU 1150 N LEU A 138 966 814 1256 -185 62 15 N ATOM 1151 CA LEU A 138 -13.859 -19.970 28.676 1.00 7.50 C ANISOU 1151 CA LEU A 138 858 794 1200 -167 65 -8 C ATOM 1152 C LEU A 138 -13.466 -19.338 30.015 1.00 7.16 C ANISOU 1152 C LEU A 138 813 760 1146 -155 69 -10 C ATOM 1153 O LEU A 138 -13.178 -18.136 30.090 1.00 7.15 O ANISOU 1153 O LEU A 138 793 764 1160 -120 63 -23 O ATOM 1154 CB LEU A 138 -15.372 -20.181 28.639 1.00 7.83 C ANISOU 1154 CB LEU A 138 866 884 1225 -201 79 -27 C ATOM 1155 CG LEU A 138 -16.274 -19.783 27.466 1.00 7.90 C ANISOU 1155 CG LEU A 138 837 921 1244 -192 74 -47 C ATOM 1156 CD1 LEU A 138 -15.556 -19.251 26.252 1.00 7.96 C ANISOU 1156 CD1 LEU A 138 850 896 1277 -149 56 -42 C ATOM 1157 CD2 LEU A 138 -17.201 -20.947 27.117 1.00 8.92 C ANISOU 1157 CD2 LEU A 138 964 1069 1355 -247 84 -51 C ATOM 1158 N GLY A 139 -13.456 -20.159 31.062 1.00 6.77 N ANISOU 1158 N GLY A 139 788 713 1070 -186 78 2 N ATOM 1159 CA GLY A 139 -13.105 -19.725 32.403 1.00 6.60 C ANISOU 1159 CA GLY A 139 769 706 1033 -179 82 1 C ATOM 1160 C GLY A 139 -11.784 -18.981 32.449 1.00 6.15 C ANISOU 1160 C GLY A 139 719 623 995 -138 64 3 C ATOM 1161 O GLY A 139 -11.665 -17.966 33.136 1.00 5.61 O ANISOU 1161 O GLY A 139 632 572 926 -120 64 -14 O ATOM 1162 N GLU A 140 -10.811 -19.493 31.698 1.00 5.79 N ANISOU 1162 N GLU A 140 698 537 963 -124 51 21 N ATOM 1163 CA GLU A 140 -9.462 -18.938 31.618 1.00 5.96 C ANISOU 1163 CA GLU A 140 725 539 1001 -90 35 23 C ATOM 1164 C GLU A 140 -9.477 -17.553 30.969 1.00 5.75 C ANISOU 1164 C GLU A 140 667 516 1001 -67 32 3 C ATOM 1165 O GLU A 140 -8.778 -16.641 31.430 1.00 5.39 O ANISOU 1165 O GLU A 140 614 471 962 -50 26 -7 O ATOM 1166 CB GLU A 140 -8.540 -19.909 30.861 1.00 6.07 C ANISOU 1166 CB GLU A 140 768 517 1021 -81 24 45 C ATOM 1167 CG GLU A 140 -8.460 -21.297 31.526 1.00 8.95 C ANISOU 1167 CG GLU A 140 1176 867 1357 -99 25 67 C ATOM 1168 CD GLU A 140 -7.809 -22.406 30.679 1.00 12.58 C ANISOU 1168 CD GLU A 140 1672 1288 1821 -89 16 85 C ATOM 1169 OE1 GLU A 140 -7.223 -22.138 29.602 1.00 11.58 O ANISOU 1169 OE1 GLU A 140 1534 1148 1718 -65 8 80 O ATOM 1170 OE2 GLU A 140 -7.888 -23.578 31.118 1.00 15.01 O ANISOU 1170 OE2 GLU A 140 2023 1575 2105 -105 18 104 O ATOM 1171 N PHE A 141 -10.289 -17.406 29.915 1.00 5.39 N ANISOU 1171 N PHE A 141 607 473 969 -67 35 -3 N ATOM 1172 CA PHE A 141 -10.468 -16.128 29.222 1.00 5.35 C ANISOU 1172 CA PHE A 141 579 467 985 -42 32 -19 C ATOM 1173 C PHE A 141 -11.206 -15.108 30.094 1.00 5.68 C ANISOU 1173 C PHE A 141 599 538 1020 -34 39 -44 C ATOM 1174 O PHE A 141 -10.745 -13.960 30.250 1.00 5.94 O ANISOU 1174 O PHE A 141 629 560 1066 -13 34 -56 O ATOM 1175 CB PHE A 141 -11.181 -16.332 27.873 1.00 5.26 C ANISOU 1175 CB PHE A 141 560 456 984 -41 32 -19 C ATOM 1176 CG PHE A 141 -11.584 -15.048 27.188 1.00 5.40 C ANISOU 1176 CG PHE A 141 558 476 1017 -12 28 -33 C ATOM 1177 CD1 PHE A 141 -12.912 -14.825 26.835 1.00 4.45 C ANISOU 1177 CD1 PHE A 141 412 387 892 -7 31 -48 C ATOM 1178 CD2 PHE A 141 -10.639 -14.061 26.897 1.00 4.86 C ANISOU 1178 CD2 PHE A 141 500 381 967 11 21 -32 C ATOM 1179 CE1 PHE A 141 -13.292 -13.639 26.207 1.00 5.88 C ANISOU 1179 CE1 PHE A 141 581 568 1084 29 25 -60 C ATOM 1180 CE2 PHE A 141 -11.011 -12.870 26.264 1.00 4.37 C ANISOU 1180 CE2 PHE A 141 431 312 917 38 18 -42 C ATOM 1181 CZ PHE A 141 -12.336 -12.655 25.920 1.00 4.79 C ANISOU 1181 CZ PHE A 141 463 392 964 52 18 -55 C ATOM 1182 N TYR A 142 -12.336 -15.528 30.669 1.00 5.59 N ANISOU 1182 N TYR A 142 572 563 988 -54 51 -52 N ATOM 1183 CA TYR A 142 -13.079 -14.697 31.618 1.00 5.50 C ANISOU 1183 CA TYR A 142 538 586 965 -46 60 -78 C ATOM 1184 C TYR A 142 -12.214 -14.225 32.790 1.00 5.66 C ANISOU 1184 C TYR A 142 572 602 978 -41 58 -83 C ATOM 1185 O TYR A 142 -12.345 -13.079 33.227 1.00 5.90 O ANISOU 1185 O TYR A 142 591 639 1012 -19 58 -108 O ATOM 1186 CB TYR A 142 -14.330 -15.410 32.138 1.00 5.84 C ANISOU 1186 CB TYR A 142 561 677 980 -77 77 -85 C ATOM 1187 CG TYR A 142 -15.407 -15.676 31.101 1.00 6.37 C ANISOU 1187 CG TYR A 142 604 767 1051 -83 79 -92 C ATOM 1188 CD1 TYR A 142 -16.353 -16.687 31.300 1.00 6.73 C ANISOU 1188 CD1 TYR A 142 636 847 1072 -127 94 -91 C ATOM 1189 CD2 TYR A 142 -15.483 -14.925 29.925 1.00 6.47 C ANISOU 1189 CD2 TYR A 142 606 766 1088 -47 67 -98 C ATOM 1190 CE1 TYR A 142 -17.347 -16.931 30.363 1.00 7.20 C ANISOU 1190 CE1 TYR A 142 668 935 1133 -136 95 -102 C ATOM 1191 CE2 TYR A 142 -16.461 -15.171 28.976 1.00 7.14 C ANISOU 1191 CE2 TYR A 142 666 876 1172 -49 66 -105 C ATOM 1192 CZ TYR A 142 -17.395 -16.167 29.203 1.00 7.98 C ANISOU 1192 CZ TYR A 142 754 1024 1255 -94 80 -109 C ATOM 1193 OH TYR A 142 -18.369 -16.406 28.262 1.00 8.69 O ANISOU 1193 OH TYR A 142 813 1146 1342 -99 77 -121 O ATOM 1194 N GLU A 143 -11.335 -15.092 33.295 1.00 5.48 N ANISOU 1194 N GLU A 143 574 566 943 -59 54 -62 N ATOM 1195 CA GLU A 143 -10.349 -14.679 34.313 1.00 5.96 C ANISOU 1195 CA GLU A 143 645 623 996 -52 47 -66 C ATOM 1196 C GLU A 143 -9.446 -13.543 33.814 1.00 5.87 C ANISOU 1196 C GLU A 143 633 584 1012 -28 35 -77 C ATOM 1197 O GLU A 143 -9.161 -12.598 34.560 1.00 6.24 O ANISOU 1197 O GLU A 143 677 636 1058 -19 33 -99 O ATOM 1198 CB GLU A 143 -9.482 -15.854 34.783 1.00 5.40 C ANISOU 1198 CB GLU A 143 602 542 906 -67 41 -39 C ATOM 1199 CG GLU A 143 -8.432 -15.450 35.845 1.00 7.16 C ANISOU 1199 CG GLU A 143 833 771 1118 -57 30 -45 C ATOM 1200 CD GLU A 143 -7.561 -16.614 36.319 1.00 8.29 C ANISOU 1200 CD GLU A 143 1004 907 1238 -62 20 -17 C ATOM 1201 OE1 GLU A 143 -7.410 -16.777 37.551 1.00 9.58 O ANISOU 1201 OE1 GLU A 143 1176 1093 1370 -67 20 -17 O ATOM 1202 OE2 GLU A 143 -7.035 -17.363 35.467 1.00 7.08 O ANISOU 1202 OE2 GLU A 143 867 728 1097 -56 13 3 O ATOM 1203 N ALA A 144 -8.990 -13.650 32.565 1.00 5.88 N ANISOU 1203 N ALA A 144 641 556 1038 -20 28 -63 N ATOM 1204 CA ALA A 144 -8.099 -12.644 31.978 1.00 6.05 C ANISOU 1204 CA ALA A 144 665 551 1085 -5 19 -69 C ATOM 1205 C ALA A 144 -8.814 -11.302 31.885 1.00 6.41 C ANISOU 1205 C ALA A 144 703 593 1141 13 23 -95 C ATOM 1206 O ALA A 144 -8.200 -10.245 32.077 1.00 6.46 O ANISOU 1206 O ALA A 144 716 581 1158 19 19 -110 O ATOM 1207 CB ALA A 144 -7.608 -13.096 30.608 1.00 5.73 C ANISOU 1207 CB ALA A 144 631 484 1061 -3 15 -48 C ATOM 1208 N LEU A 145 -10.120 -11.361 31.614 1.00 6.75 N ANISOU 1208 N LEU A 145 732 654 1180 21 31 -101 N ATOM 1209 CA LEU A 145 -10.977 -10.178 31.608 1.00 7.14 C ANISOU 1209 CA LEU A 145 772 707 1234 48 34 -127 C ATOM 1210 C LEU A 145 -11.136 -9.604 33.007 1.00 7.79 C ANISOU 1210 C LEU A 145 850 810 1299 50 39 -155 C ATOM 1211 O LEU A 145 -11.161 -8.379 33.178 1.00 8.48 O ANISOU 1211 O LEU A 145 945 881 1396 73 37 -179 O ATOM 1212 CB LEU A 145 -12.351 -10.496 31.017 1.00 7.14 C ANISOU 1212 CB LEU A 145 750 736 1229 58 39 -130 C ATOM 1213 CG LEU A 145 -12.440 -10.815 29.525 1.00 6.81 C ANISOU 1213 CG LEU A 145 710 676 1201 64 33 -110 C ATOM 1214 CD1 LEU A 145 -13.890 -11.026 29.172 1.00 5.87 C ANISOU 1214 CD1 LEU A 145 560 597 1071 74 37 -121 C ATOM 1215 CD2 LEU A 145 -11.841 -9.680 28.683 1.00 6.18 C ANISOU 1215 CD2 LEU A 145 652 553 1145 90 23 -108 C ATOM 1216 N ASP A 146 -11.244 -10.479 34.005 1.00 7.62 N ANISOU 1216 N ASP A 146 821 822 1252 27 46 -151 N ATOM 1217 CA ASP A 146 -11.249 -10.030 35.397 1.00 8.18 C ANISOU 1217 CA ASP A 146 890 917 1301 26 50 -176 C ATOM 1218 C ASP A 146 -9.985 -9.245 35.752 1.00 8.23 C ANISOU 1218 C ASP A 146 915 893 1318 27 39 -186 C ATOM 1219 O ASP A 146 -10.060 -8.227 36.443 1.00 8.56 O ANISOU 1219 O ASP A 146 961 936 1357 40 40 -217 O ATOM 1220 CB ASP A 146 -11.443 -11.198 36.365 1.00 8.22 C ANISOU 1220 CB ASP A 146 891 960 1273 -3 59 -164 C ATOM 1221 CG ASP A 146 -12.879 -11.682 36.410 1.00 8.66 C ANISOU 1221 CG ASP A 146 923 1059 1310 -11 76 -169 C ATOM 1222 OD1 ASP A 146 -13.151 -12.740 37.024 1.00 8.89 O ANISOU 1222 OD1 ASP A 146 952 1115 1310 -42 86 -154 O ATOM 1223 OD2 ASP A 146 -13.735 -11.006 35.811 1.00 8.70 O ANISOU 1223 OD2 ASP A 146 908 1071 1328 14 79 -188 O ATOM 1224 N CYS A 147 -8.836 -9.719 35.272 1.00 7.93 N ANISOU 1224 N CYS A 147 890 832 1292 13 28 -162 N ATOM 1225 CA CYS A 147 -7.569 -9.039 35.506 1.00 7.98 C ANISOU 1225 CA CYS A 147 908 816 1307 7 18 -171 C ATOM 1226 C CYS A 147 -7.666 -7.589 35.036 1.00 7.89 C ANISOU 1226 C CYS A 147 908 770 1319 23 18 -194 C ATOM 1227 O CYS A 147 -7.266 -6.679 35.750 1.00 8.05 O ANISOU 1227 O CYS A 147 938 783 1338 21 15 -222 O ATOM 1228 CB CYS A 147 -6.426 -9.770 34.799 1.00 7.56 C ANISOU 1228 CB CYS A 147 859 748 1264 -5 8 -142 C ATOM 1229 SG CYS A 147 -4.889 -8.821 34.692 1.00 8.89 S ANISOU 1229 SG CYS A 147 1034 893 1450 -17 -3 -155 S ATOM 1230 N LEU A 148 -8.245 -7.391 33.853 1.00 8.14 N ANISOU 1230 N LEU A 148 943 779 1370 40 20 -184 N ATOM 1231 CA LEU A 148 -8.362 -6.068 33.242 1.00 8.43 C ANISOU 1231 CA LEU A 148 1000 775 1428 60 19 -199 C ATOM 1232 C LEU A 148 -9.597 -5.312 33.727 1.00 9.13 C ANISOU 1232 C LEU A 148 1086 874 1508 93 25 -229 C ATOM 1233 O LEU A 148 -9.863 -4.201 33.274 1.00 9.20 O ANISOU 1233 O LEU A 148 1118 846 1532 119 23 -243 O ATOM 1234 CB LEU A 148 -8.365 -6.178 31.715 1.00 7.66 C ANISOU 1234 CB LEU A 148 911 650 1351 67 17 -171 C ATOM 1235 CG LEU A 148 -7.157 -6.799 31.001 1.00 7.45 C ANISOU 1235 CG LEU A 148 886 611 1334 41 13 -143 C ATOM 1236 CD1 LEU A 148 -7.366 -6.716 29.502 1.00 6.15 C ANISOU 1236 CD1 LEU A 148 731 421 1185 54 14 -121 C ATOM 1237 CD2 LEU A 148 -5.827 -6.131 31.398 1.00 7.20 C ANISOU 1237 CD2 LEU A 148 867 560 1308 15 10 -154 C ATOM 1238 N ARG A 149 -10.336 -5.925 34.653 1.00 9.88 N ANISOU 1238 N ARG A 149 1157 1019 1578 93 32 -240 N ATOM 1239 CA ARG A 149 -11.572 -5.357 35.200 1.00 10.49 C ANISOU 1239 CA ARG A 149 1222 1123 1642 126 40 -272 C ATOM 1240 C ARG A 149 -12.559 -4.988 34.082 1.00 10.09 C ANISOU 1240 C ARG A 149 1168 1063 1605 164 38 -270 C ATOM 1241 O ARG A 149 -13.094 -3.884 34.045 1.00 10.17 O ANISOU 1241 O ARG A 149 1189 1055 1619 205 37 -296 O ATOM 1242 CB ARG A 149 -11.259 -4.159 36.110 1.00 11.26 C ANISOU 1242 CB ARG A 149 1341 1201 1737 136 38 -310 C ATOM 1243 CG ARG A 149 -10.374 -4.519 37.303 1.00 13.65 C ANISOU 1243 CG ARG A 149 1642 1525 2020 101 37 -317 C ATOM 1244 CD ARG A 149 -9.906 -3.294 38.079 1.00 17.23 C ANISOU 1244 CD ARG A 149 2121 1954 2473 105 33 -357 C ATOM 1245 NE ARG A 149 -8.972 -2.459 37.318 1.00 21.25 N ANISOU 1245 NE ARG A 149 2664 2399 3012 96 24 -354 N ATOM 1246 CZ ARG A 149 -7.655 -2.658 37.248 1.00 23.01 C ANISOU 1246 CZ ARG A 149 2893 2608 3242 56 17 -340 C ATOM 1247 NH1 ARG A 149 -7.086 -3.677 37.889 1.00 24.09 N ANISOU 1247 NH1 ARG A 149 3007 2789 3359 30 13 -327 N ATOM 1248 NH2 ARG A 149 -6.898 -1.835 36.535 1.00 23.53 N ANISOU 1248 NH2 ARG A 149 2988 2619 3332 43 12 -340 N ATOM 1249 N ILE A 150 -12.760 -5.926 33.157 1.00 9.56 N ANISOU 1249 N ILE A 150 1085 1006 1541 154 38 -239 N ATOM 1250 CA ILE A 150 -13.737 -5.782 32.078 1.00 8.90 C ANISOU 1250 CA ILE A 150 991 927 1465 188 35 -235 C ATOM 1251 C ILE A 150 -14.874 -6.764 32.334 1.00 8.80 C ANISOU 1251 C ILE A 150 934 981 1429 180 45 -238 C ATOM 1252 O ILE A 150 -14.637 -7.974 32.397 1.00 8.35 O ANISOU 1252 O ILE A 150 866 943 1363 139 49 -215 O ATOM 1253 CB ILE A 150 -13.123 -6.067 30.680 1.00 8.57 C ANISOU 1253 CB ILE A 150 966 846 1443 179 26 -199 C ATOM 1254 CG1 ILE A 150 -11.979 -5.091 30.373 1.00 8.88 C ANISOU 1254 CG1 ILE A 150 1049 822 1503 178 20 -195 C ATOM 1255 CG2 ILE A 150 -14.195 -5.978 29.593 1.00 7.89 C ANISOU 1255 CG2 ILE A 150 867 774 1359 215 21 -196 C ATOM 1256 CD1 ILE A 150 -11.152 -5.466 29.131 1.00 8.49 C ANISOU 1256 CD1 ILE A 150 1014 741 1469 159 15 -159 C ATOM 1257 N PRO A 151 -16.110 -6.241 32.503 1.00 9.22 N ANISOU 1257 N PRO A 151 961 1072 1470 220 48 -268 N ATOM 1258 CA PRO A 151 -17.312 -7.057 32.711 1.00 9.00 C ANISOU 1258 CA PRO A 151 884 1119 1419 211 60 -276 C ATOM 1259 C PRO A 151 -17.507 -8.092 31.618 1.00 8.45 C ANISOU 1259 C PRO A 151 800 1057 1352 187 56 -247 C ATOM 1260 O PRO A 151 -17.357 -7.779 30.433 1.00 8.49 O ANISOU 1260 O PRO A 151 821 1029 1377 210 43 -233 O ATOM 1261 CB PRO A 151 -18.450 -6.034 32.644 1.00 9.54 C ANISOU 1261 CB PRO A 151 931 1214 1481 274 57 -313 C ATOM 1262 CG PRO A 151 -17.840 -4.769 33.086 1.00 10.27 C ANISOU 1262 CG PRO A 151 1065 1253 1585 306 51 -332 C ATOM 1263 CD PRO A 151 -16.399 -4.799 32.633 1.00 9.28 C ANISOU 1263 CD PRO A 151 986 1056 1483 275 43 -299 C ATOM 1264 N ARG A 152 -17.852 -9.311 32.024 1.00 7.76 N ANISOU 1264 N ARG A 152 689 1014 1245 140 70 -239 N ATOM 1265 CA ARG A 152 -18.192 -10.389 31.096 1.00 7.50 C ANISOU 1265 CA ARG A 152 642 997 1212 111 69 -217 C ATOM 1266 C ARG A 152 -19.336 -9.976 30.167 1.00 7.26 C ANISOU 1266 C ARG A 152 576 1001 1180 151 61 -235 C ATOM 1267 O ARG A 152 -19.422 -10.433 29.027 1.00 6.58 O ANISOU 1267 O ARG A 152 489 908 1102 146 51 -218 O ATOM 1268 CB ARG A 152 -18.586 -11.639 31.886 1.00 7.48 C ANISOU 1268 CB ARG A 152 621 1040 1181 53 87 -213 C ATOM 1269 CG ARG A 152 -18.594 -12.936 31.103 1.00 8.43 C ANISOU 1269 CG ARG A 152 744 1157 1300 9 88 -186 C ATOM 1270 CD ARG A 152 -18.964 -14.128 32.015 1.00 9.21 C ANISOU 1270 CD ARG A 152 837 1294 1370 -53 109 -181 C ATOM 1271 NE ARG A 152 -18.078 -14.214 33.185 1.00 9.85 N ANISOU 1271 NE ARG A 152 949 1352 1441 -67 114 -170 N ATOM 1272 CZ ARG A 152 -18.030 -15.232 34.043 1.00 9.44 C ANISOU 1272 CZ ARG A 152 912 1314 1363 -117 129 -155 C ATOM 1273 NH1 ARG A 152 -18.821 -16.286 33.889 1.00 9.33 N ANISOU 1273 NH1 ARG A 152 884 1330 1329 -166 143 -149 N ATOM 1274 NH2 ARG A 152 -17.185 -15.192 35.066 1.00 8.63 N ANISOU 1274 NH2 ARG A 152 838 1192 1250 -120 130 -146 N ATOM 1275 N SER A 153 -20.214 -9.112 30.675 1.00 7.50 N ANISOU 1275 N SER A 153 579 1073 1200 194 64 -270 N ATOM 1276 CA SER A 153 -21.348 -8.587 29.909 1.00 7.82 C ANISOU 1276 CA SER A 153 582 1154 1235 245 54 -292 C ATOM 1277 C SER A 153 -20.922 -7.782 28.674 1.00 7.50 C ANISOU 1277 C SER A 153 576 1054 1219 294 30 -277 C ATOM 1278 O SER A 153 -21.701 -7.637 27.731 1.00 7.33 O ANISOU 1278 O SER A 153 531 1060 1194 329 18 -283 O ATOM 1279 CB SER A 153 -22.243 -7.732 30.810 1.00 8.24 C ANISOU 1279 CB SER A 153 602 1258 1270 290 62 -337 C ATOM 1280 OG SER A 153 -21.506 -6.646 31.369 1.00 9.12 O ANISOU 1280 OG SER A 153 758 1312 1394 325 57 -345 O ATOM 1281 N ASP A 154 -19.694 -7.260 28.690 1.00 7.06 N ANISOU 1281 N ASP A 154 577 920 1185 295 25 -258 N ATOM 1282 CA ASP A 154 -19.151 -6.504 27.553 1.00 7.06 C ANISOU 1282 CA ASP A 154 619 857 1206 332 7 -238 C ATOM 1283 C ASP A 154 -18.573 -7.356 26.419 1.00 6.44 C ANISOU 1283 C ASP A 154 553 755 1137 297 1 -202 C ATOM 1284 O ASP A 154 -18.120 -6.816 25.404 1.00 6.32 O ANISOU 1284 O ASP A 154 572 693 1136 322 -12 -183 O ATOM 1285 CB ASP A 154 -18.091 -5.507 28.034 1.00 7.52 C ANISOU 1285 CB ASP A 154 732 845 1282 342 6 -237 C ATOM 1286 CG ASP A 154 -18.697 -4.321 28.745 1.00 8.19 C ANISOU 1286 CG ASP A 154 817 934 1359 398 5 -275 C ATOM 1287 OD1 ASP A 154 -19.888 -4.035 28.524 1.00 8.89 O ANISOU 1287 OD1 ASP A 154 872 1071 1434 448 0 -298 O ATOM 1288 OD2 ASP A 154 -17.978 -3.675 29.526 1.00 10.74 O ANISOU 1288 OD2 ASP A 154 1174 1216 1690 394 10 -285 O ATOM 1289 N VAL A 155 -18.583 -8.677 26.584 1.00 5.78 N ANISOU 1289 N VAL A 155 448 703 1045 241 11 -192 N ATOM 1290 CA VAL A 155 -18.035 -9.570 25.565 1.00 4.99 C ANISOU 1290 CA VAL A 155 361 581 952 208 6 -161 C ATOM 1291 C VAL A 155 -18.904 -9.646 24.302 1.00 5.59 C ANISOU 1291 C VAL A 155 415 688 1022 234 -8 -162 C ATOM 1292 O VAL A 155 -20.130 -9.756 24.378 1.00 5.43 O ANISOU 1292 O VAL A 155 347 733 983 246 -8 -187 O ATOM 1293 CB VAL A 155 -17.753 -10.993 26.130 1.00 4.97 C ANISOU 1293 CB VAL A 155 352 594 941 142 20 -150 C ATOM 1294 CG1 VAL A 155 -17.191 -11.892 25.052 1.00 2.96 C ANISOU 1294 CG1 VAL A 155 115 315 694 115 14 -123 C ATOM 1295 CG2 VAL A 155 -16.771 -10.918 27.310 1.00 4.04 C ANISOU 1295 CG2 VAL A 155 260 447 827 121 30 -146 C ATOM 1296 N MET A 156 -18.243 -9.575 23.148 1.00 5.98 N ANISOU 1296 N MET A 156 495 693 1083 242 -19 -137 N ATOM 1297 CA MET A 156 -18.862 -9.830 21.847 1.00 6.80 C ANISOU 1297 CA MET A 156 584 822 1179 258 -34 -132 C ATOM 1298 C MET A 156 -18.439 -11.222 21.399 1.00 6.74 C ANISOU 1298 C MET A 156 577 813 1170 200 -29 -115 C ATOM 1299 O MET A 156 -17.253 -11.568 21.470 1.00 6.06 O ANISOU 1299 O MET A 156 527 679 1097 171 -22 -93 O ATOM 1300 CB MET A 156 -18.428 -8.774 20.828 1.00 7.16 C ANISOU 1300 CB MET A 156 669 818 1233 307 -49 -114 C ATOM 1301 CG MET A 156 -18.831 -7.331 21.231 1.00 8.91 C ANISOU 1301 CG MET A 156 901 1027 1455 371 -56 -131 C ATOM 1302 SD MET A 156 -17.839 -6.024 20.457 1.00 13.22 S ANISOU 1302 SD MET A 156 1521 1485 2017 408 -65 -103 S ATOM 1303 CE MET A 156 -16.210 -6.280 21.155 1.00 9.81 C ANISOU 1303 CE MET A 156 1125 996 1607 345 -46 -85 C ATOM 1304 N TYR A 157 -19.418 -12.023 20.975 1.00 7.08 N ANISOU 1304 N TYR A 157 581 913 1196 182 -31 -128 N ATOM 1305 CA TYR A 157 -19.207 -13.422 20.621 1.00 7.09 C ANISOU 1305 CA TYR A 157 585 918 1193 124 -26 -118 C ATOM 1306 C TYR A 157 -19.451 -13.673 19.140 1.00 7.69 C ANISOU 1306 C TYR A 157 657 1002 1261 135 -42 -113 C ATOM 1307 O TYR A 157 -20.322 -13.054 18.523 1.00 7.99 O ANISOU 1307 O TYR A 157 669 1079 1289 178 -58 -127 O ATOM 1308 CB TYR A 157 -20.154 -14.323 21.421 1.00 7.47 C ANISOU 1308 CB TYR A 157 591 1024 1222 77 -12 -141 C ATOM 1309 CG TYR A 157 -19.928 -14.302 22.914 1.00 7.24 C ANISOU 1309 CG TYR A 157 567 991 1194 57 6 -145 C ATOM 1310 CD1 TYR A 157 -20.719 -13.512 23.745 1.00 6.47 C ANISOU 1310 CD1 TYR A 157 435 937 1087 84 11 -171 C ATOM 1311 CD2 TYR A 157 -18.922 -15.077 23.496 1.00 6.46 C ANISOU 1311 CD2 TYR A 157 505 848 1102 14 18 -124 C ATOM 1312 CE1 TYR A 157 -20.517 -13.486 25.117 1.00 6.31 C ANISOU 1312 CE1 TYR A 157 418 917 1063 66 28 -176 C ATOM 1313 CE2 TYR A 157 -18.710 -15.058 24.878 1.00 6.97 C ANISOU 1313 CE2 TYR A 157 574 912 1162 -3 33 -126 C ATOM 1314 CZ TYR A 157 -19.513 -14.262 25.679 1.00 5.66 C ANISOU 1314 CZ TYR A 157 375 791 986 21 39 -152 C ATOM 1315 OH TYR A 157 -19.310 -14.234 27.039 1.00 4.70 O ANISOU 1315 OH TYR A 157 258 673 856 4 54 -156 O ATOM 1316 N THR A 158 -18.697 -14.607 18.572 1.00 7.62 N ANISOU 1316 N THR A 158 677 962 1257 99 -40 -95 N ATOM 1317 CA THR A 158 -18.987 -15.066 17.223 1.00 7.88 C ANISOU 1317 CA THR A 158 705 1011 1279 99 -54 -95 C ATOM 1318 C THR A 158 -20.106 -16.115 17.255 1.00 8.70 C ANISOU 1318 C THR A 158 768 1176 1363 54 -52 -121 C ATOM 1319 O THR A 158 -20.451 -16.638 18.318 1.00 8.10 O ANISOU 1319 O THR A 158 675 1118 1283 14 -36 -132 O ATOM 1320 CB THR A 158 -17.726 -15.612 16.525 1.00 7.35 C ANISOU 1320 CB THR A 158 684 887 1222 83 -52 -69 C ATOM 1321 OG1 THR A 158 -17.108 -16.601 17.352 1.00 7.31 O ANISOU 1321 OG1 THR A 158 698 857 1224 35 -36 -64 O ATOM 1322 CG2 THR A 158 -16.749 -14.496 16.280 1.00 6.89 C ANISOU 1322 CG2 THR A 158 659 781 1178 125 -55 -47 C ATOM 1323 N ASP A 159 -20.684 -16.386 16.086 1.00 9.70 N ANISOU 1323 N ASP A 159 876 1336 1474 59 -68 -130 N ATOM 1324 CA ASP A 159 -21.697 -17.423 15.923 1.00 10.48 C ANISOU 1324 CA ASP A 159 937 1492 1552 8 -67 -157 C ATOM 1325 C ASP A 159 -21.324 -18.179 14.671 1.00 10.92 C ANISOU 1325 C ASP A 159 1017 1529 1602 -9 -77 -151 C ATOM 1326 O ASP A 159 -21.560 -17.700 13.559 1.00 11.19 O ANISOU 1326 O ASP A 159 1043 1584 1626 32 -98 -152 O ATOM 1327 CB ASP A 159 -23.095 -16.810 15.776 1.00 10.91 C ANISOU 1327 CB ASP A 159 926 1632 1587 40 -81 -188 C ATOM 1328 CG ASP A 159 -24.194 -17.860 15.614 1.00 11.66 C ANISOU 1328 CG ASP A 159 974 1799 1659 -20 -80 -220 C ATOM 1329 OD1 ASP A 159 -25.367 -17.532 15.895 1.00 12.83 O ANISOU 1329 OD1 ASP A 159 1059 2027 1789 -10 -83 -251 O ATOM 1330 OD2 ASP A 159 -23.905 -19.009 15.208 1.00 11.27 O ANISOU 1330 OD2 ASP A 159 948 1726 1606 -77 -75 -218 O ATOM 1331 N TRP A 160 -20.749 -19.366 14.855 1.00 11.41 N ANISOU 1331 N TRP A 160 1113 1554 1669 -66 -64 -145 N ATOM 1332 CA TRP A 160 -20.220 -20.156 13.747 1.00 12.04 C ANISOU 1332 CA TRP A 160 1225 1605 1745 -81 -71 -139 C ATOM 1333 C TRP A 160 -21.232 -20.422 12.629 1.00 12.65 C ANISOU 1333 C TRP A 160 1266 1743 1797 -87 -89 -166 C ATOM 1334 O TRP A 160 -20.855 -20.506 11.462 1.00 12.80 O ANISOU 1334 O TRP A 160 1305 1750 1810 -69 -102 -161 O ATOM 1335 CB TRP A 160 -19.621 -21.477 14.247 1.00 11.99 C ANISOU 1335 CB TRP A 160 1260 1551 1744 -141 -54 -134 C ATOM 1336 CG TRP A 160 -19.037 -22.297 13.131 1.00 13.51 C ANISOU 1336 CG TRP A 160 1489 1711 1931 -152 -60 -132 C ATOM 1337 CD1 TRP A 160 -19.405 -23.560 12.759 1.00 14.30 C ANISOU 1337 CD1 TRP A 160 1602 1814 2018 -208 -59 -152 C ATOM 1338 CD2 TRP A 160 -18.002 -21.893 12.216 1.00 14.15 C ANISOU 1338 CD2 TRP A 160 1601 1756 2020 -106 -68 -113 C ATOM 1339 NE1 TRP A 160 -18.656 -23.974 11.681 1.00 15.46 N ANISOU 1339 NE1 TRP A 160 1784 1926 2162 -195 -66 -147 N ATOM 1340 CE2 TRP A 160 -17.787 -22.972 11.328 1.00 15.31 C ANISOU 1340 CE2 TRP A 160 1774 1887 2155 -133 -71 -123 C ATOM 1341 CE3 TRP A 160 -17.234 -20.726 12.065 1.00 14.36 C ANISOU 1341 CE3 TRP A 160 1635 1762 2058 -50 -71 -88 C ATOM 1342 CZ2 TRP A 160 -16.833 -22.923 10.300 1.00 15.23 C ANISOU 1342 CZ2 TRP A 160 1795 1847 2145 -101 -76 -110 C ATOM 1343 CZ3 TRP A 160 -16.288 -20.674 11.040 1.00 14.86 C ANISOU 1343 CZ3 TRP A 160 1728 1795 2121 -25 -75 -74 C ATOM 1344 CH2 TRP A 160 -16.096 -21.767 10.173 1.00 15.72 C ANISOU 1344 CH2 TRP A 160 1859 1895 2217 -48 -77 -85 C ATOM 1345 N LYS A 161 -22.508 -20.556 12.985 1.00 13.70 N ANISOU 1345 N LYS A 161 1345 1948 1914 -113 -90 -196 N ATOM 1346 CA LYS A 161 -23.564 -20.833 11.999 1.00 14.70 C ANISOU 1346 CA LYS A 161 1427 2145 2013 -123 -109 -228 C ATOM 1347 C LYS A 161 -23.716 -19.710 10.985 1.00 14.58 C ANISOU 1347 C LYS A 161 1395 2156 1988 -43 -136 -223 C ATOM 1348 O LYS A 161 -24.258 -19.927 9.899 1.00 15.36 O ANISOU 1348 O LYS A 161 1473 2300 2063 -40 -156 -241 O ATOM 1349 CB LYS A 161 -24.913 -21.106 12.681 1.00 15.37 C ANISOU 1349 CB LYS A 161 1447 2312 2081 -166 -103 -264 C ATOM 1350 CG LYS A 161 -25.000 -22.452 13.380 1.00 16.97 C ANISOU 1350 CG LYS A 161 1667 2499 2282 -262 -79 -274 C ATOM 1351 CD LYS A 161 -24.462 -22.379 14.811 1.00 19.18 C ANISOU 1351 CD LYS A 161 1973 2734 2581 -274 -53 -252 C ATOM 1352 CE LYS A 161 -23.596 -23.596 15.131 1.00 19.66 C ANISOU 1352 CE LYS A 161 2104 2715 2651 -333 -36 -234 C ATOM 1353 NZ LYS A 161 -22.691 -23.341 16.287 1.00 19.42 N ANISOU 1353 NZ LYS A 161 2112 2627 2641 -319 -19 -203 N ATOM 1354 N LYS A 162 -23.230 -18.520 11.344 1.00 14.28 N ANISOU 1354 N LYS A 162 1371 2090 1966 20 -136 -198 N ATOM 1355 CA LYS A 162 -23.321 -17.326 10.497 1.00 13.98 C ANISOU 1355 CA LYS A 162 1329 2064 1917 101 -160 -187 C ATOM 1356 C LYS A 162 -22.124 -17.152 9.556 1.00 13.61 C ANISOU 1356 C LYS A 162 1343 1952 1877 125 -163 -154 C ATOM 1357 O LYS A 162 -22.078 -16.187 8.779 1.00 13.46 O ANISOU 1357 O LYS A 162 1334 1935 1848 188 -181 -138 O ATOM 1358 CB LYS A 162 -23.487 -16.070 11.361 1.00 14.02 C ANISOU 1358 CB LYS A 162 1323 2070 1934 156 -158 -180 C ATOM 1359 CG LYS A 162 -24.841 -15.987 12.061 1.00 15.07 C ANISOU 1359 CG LYS A 162 1385 2289 2053 154 -160 -217 C ATOM 1360 CD LYS A 162 -25.009 -14.690 12.834 1.00 15.26 C ANISOU 1360 CD LYS A 162 1401 2312 2086 219 -160 -214 C ATOM 1361 CE LYS A 162 -26.423 -14.577 13.367 1.00 15.46 C ANISOU 1361 CE LYS A 162 1348 2436 2091 226 -165 -256 C ATOM 1362 NZ LYS A 162 -26.626 -13.286 14.061 1.00 17.86 N ANISOU 1362 NZ LYS A 162 1646 2740 2401 299 -167 -257 N ATOM 1363 N ASP A 163 -21.158 -18.069 9.639 1.00 12.96 N ANISOU 1363 N ASP A 163 1302 1814 1808 77 -146 -142 N ATOM 1364 CA ASP A 163 -19.953 -18.004 8.803 1.00 12.51 C ANISOU 1364 CA ASP A 163 1298 1699 1755 95 -145 -114 C ATOM 1365 C ASP A 163 -20.306 -18.057 7.328 1.00 12.69 C ANISOU 1365 C ASP A 163 1316 1758 1749 115 -167 -121 C ATOM 1366 O ASP A 163 -21.193 -18.814 6.918 1.00 13.30 O ANISOU 1366 O ASP A 163 1360 1889 1805 85 -178 -152 O ATOM 1367 CB ASP A 163 -18.975 -19.137 9.134 1.00 11.84 C ANISOU 1367 CB ASP A 163 1252 1560 1687 42 -124 -108 C ATOM 1368 CG ASP A 163 -17.950 -19.376 8.022 1.00 11.41 C ANISOU 1368 CG ASP A 163 1240 1470 1627 53 -125 -92 C ATOM 1369 OD1 ASP A 163 -17.102 -18.493 7.777 1.00 9.28 O ANISOU 1369 OD1 ASP A 163 994 1166 1364 93 -122 -63 O ATOM 1370 OD2 ASP A 163 -17.994 -20.453 7.393 1.00 11.58 O ANISOU 1370 OD2 ASP A 163 1269 1495 1635 19 -127 -109 O ATOM 1371 N LYS A 164 -19.603 -17.251 6.537 1.00 12.58 N ANISOU 1371 N LYS A 164 1335 1715 1730 163 -173 -92 N ATOM 1372 CA LYS A 164 -19.806 -17.223 5.090 1.00 12.71 C ANISOU 1372 CA LYS A 164 1353 1761 1713 188 -193 -93 C ATOM 1373 C LYS A 164 -18.555 -17.644 4.316 1.00 11.92 C ANISOU 1373 C LYS A 164 1303 1612 1613 178 -182 -73 C ATOM 1374 O LYS A 164 -18.588 -17.748 3.091 1.00 12.12 O ANISOU 1374 O LYS A 164 1337 1660 1610 192 -196 -74 O ATOM 1375 CB LYS A 164 -20.300 -15.835 4.653 1.00 13.19 C ANISOU 1375 CB LYS A 164 1408 1847 1758 262 -214 -77 C ATOM 1376 CG LYS A 164 -21.788 -15.597 4.938 1.00 14.35 C ANISOU 1376 CG LYS A 164 1493 2071 1889 281 -236 -108 C ATOM 1377 CD LYS A 164 -22.665 -16.011 3.757 1.00 16.82 C ANISOU 1377 CD LYS A 164 1773 2457 2161 288 -264 -133 C ATOM 1378 CE LYS A 164 -23.920 -16.741 4.195 1.00 18.47 C ANISOU 1378 CE LYS A 164 1913 2744 2360 249 -271 -181 C ATOM 1379 NZ LYS A 164 -24.777 -15.935 5.103 1.00 20.56 N ANISOU 1379 NZ LYS A 164 2133 3047 2630 285 -277 -192 N ATOM 1380 N CYS A 165 -17.475 -17.923 5.045 1.00 11.03 N ANISOU 1380 N CYS A 165 1221 1440 1529 153 -157 -59 N ATOM 1381 CA CYS A 165 -16.151 -18.139 4.453 1.00 10.60 C ANISOU 1381 CA CYS A 165 1211 1340 1477 151 -143 -38 C ATOM 1382 C CYS A 165 -15.772 -19.593 4.143 1.00 11.01 C ANISOU 1382 C CYS A 165 1277 1382 1525 107 -135 -59 C ATOM 1383 O CYS A 165 -14.898 -19.840 3.299 1.00 10.86 O ANISOU 1383 O CYS A 165 1286 1344 1495 113 -129 -51 O ATOM 1384 CB CYS A 165 -15.073 -17.489 5.322 1.00 9.84 C ANISOU 1384 CB CYS A 165 1140 1189 1411 158 -122 -10 C ATOM 1385 SG CYS A 165 -15.049 -15.681 5.205 1.00 8.85 S ANISOU 1385 SG CYS A 165 1026 1054 1284 215 -128 23 S ATOM 1386 N GLU A 166 -16.420 -20.541 4.821 1.00 11.40 N ANISOU 1386 N GLU A 166 1309 1443 1582 63 -135 -87 N ATOM 1387 CA GLU A 166 -16.172 -21.973 4.605 1.00 12.47 C ANISOU 1387 CA GLU A 166 1464 1561 1713 18 -129 -110 C ATOM 1388 C GLU A 166 -16.163 -22.378 3.118 1.00 12.42 C ANISOU 1388 C GLU A 166 1469 1577 1675 25 -141 -124 C ATOM 1389 O GLU A 166 -15.228 -23.054 2.690 1.00 12.15 O ANISOU 1389 O GLU A 166 1470 1508 1639 20 -130 -124 O ATOM 1390 CB GLU A 166 -17.160 -22.836 5.400 1.00 13.16 C ANISOU 1390 CB GLU A 166 1529 1666 1804 -35 -129 -140 C ATOM 1391 CG GLU A 166 -17.157 -24.323 5.034 1.00 16.92 C ANISOU 1391 CG GLU A 166 2031 2127 2270 -85 -127 -168 C ATOM 1392 CD GLU A 166 -16.581 -25.198 6.125 1.00 20.88 C ANISOU 1392 CD GLU A 166 2567 2572 2795 -121 -107 -165 C ATOM 1393 OE1 GLU A 166 -15.679 -24.728 6.850 1.00 23.55 O ANISOU 1393 OE1 GLU A 166 2921 2872 3156 -97 -94 -137 O ATOM 1394 OE2 GLU A 166 -17.033 -26.359 6.259 1.00 22.64 O ANISOU 1394 OE2 GLU A 166 2803 2786 3011 -175 -105 -191 O ATOM 1395 N PRO A 167 -17.194 -21.972 2.335 1.00 12.79 N ANISOU 1395 N PRO A 167 1484 1685 1693 41 -164 -137 N ATOM 1396 CA PRO A 167 -17.170 -22.297 0.903 1.00 13.14 C ANISOU 1396 CA PRO A 167 1538 1753 1701 50 -177 -150 C ATOM 1397 C PRO A 167 -15.960 -21.745 0.139 1.00 13.25 C ANISOU 1397 C PRO A 167 1588 1739 1708 90 -167 -118 C ATOM 1398 O PRO A 167 -15.493 -22.402 -0.790 1.00 13.38 O ANISOU 1398 O PRO A 167 1627 1753 1703 85 -166 -130 O ATOM 1399 CB PRO A 167 -18.473 -21.682 0.377 1.00 13.14 C ANISOU 1399 CB PRO A 167 1493 1828 1673 73 -206 -163 C ATOM 1400 CG PRO A 167 -19.380 -21.705 1.548 1.00 13.63 C ANISOU 1400 CG PRO A 167 1516 1910 1754 47 -206 -178 C ATOM 1401 CD PRO A 167 -18.495 -21.388 2.725 1.00 12.96 C ANISOU 1401 CD PRO A 167 1454 1761 1708 48 -181 -148 C ATOM 1402 N LEU A 168 -15.462 -20.564 0.521 1.00 13.48 N ANISOU 1402 N LEU A 168 1623 1747 1752 126 -159 -80 N ATOM 1403 CA LEU A 168 -14.267 -19.982 -0.116 1.00 13.79 C ANISOU 1403 CA LEU A 168 1695 1759 1784 155 -145 -48 C ATOM 1404 C LEU A 168 -12.977 -20.690 0.300 1.00 13.77 C ANISOU 1404 C LEU A 168 1720 1706 1804 134 -119 -46 C ATOM 1405 O LEU A 168 -12.114 -20.943 -0.542 1.00 13.87 O ANISOU 1405 O LEU A 168 1755 1713 1800 141 -109 -43 O ATOM 1406 CB LEU A 168 -14.143 -18.472 0.153 1.00 13.79 C ANISOU 1406 CB LEU A 168 1699 1749 1792 194 -144 -9 C ATOM 1407 CG LEU A 168 -12.955 -17.749 -0.508 1.00 13.81 C ANISOU 1407 CG LEU A 168 1736 1726 1784 216 -127 27 C ATOM 1408 CD1 LEU A 168 -13.058 -17.798 -2.029 1.00 14.46 C ANISOU 1408 CD1 LEU A 168 1831 1845 1819 234 -139 27 C ATOM 1409 CD2 LEU A 168 -12.833 -16.295 -0.045 1.00 14.57 C ANISOU 1409 CD2 LEU A 168 1843 1800 1893 244 -124 63 C ATOM 1410 N GLU A 169 -12.846 -20.979 1.595 1.00 13.89 N ANISOU 1410 N GLU A 169 1731 1690 1855 112 -108 -48 N ATOM 1411 CA GLU A 169 -11.743 -21.790 2.120 1.00 14.19 C ANISOU 1411 CA GLU A 169 1793 1684 1914 94 -88 -51 C ATOM 1412 C GLU A 169 -11.679 -23.123 1.374 1.00 14.78 C ANISOU 1412 C GLU A 169 1886 1761 1970 76 -91 -83 C ATOM 1413 O GLU A 169 -10.590 -23.570 0.988 1.00 14.75 O ANISOU 1413 O GLU A 169 1907 1736 1963 85 -77 -83 O ATOM 1414 CB GLU A 169 -11.910 -22.017 3.631 1.00 14.16 C ANISOU 1414 CB GLU A 169 1782 1655 1944 71 -82 -52 C ATOM 1415 CG GLU A 169 -10.878 -22.957 4.279 1.00 14.35 C ANISOU 1415 CG GLU A 169 1832 1633 1986 57 -66 -56 C ATOM 1416 CD GLU A 169 -11.353 -23.563 5.604 1.00 15.93 C ANISOU 1416 CD GLU A 169 2031 1815 2208 24 -65 -65 C ATOM 1417 OE1 GLU A 169 -12.501 -24.052 5.684 1.00 16.37 O ANISOU 1417 OE1 GLU A 169 2074 1890 2256 -5 -75 -87 O ATOM 1418 OE2 GLU A 169 -10.558 -23.578 6.569 1.00 17.22 O ANISOU 1418 OE2 GLU A 169 2205 1945 2393 27 -52 -51 O ATOM 1419 N LYS A 170 -12.853 -23.723 1.156 1.00 15.35 N ANISOU 1419 N LYS A 170 1944 1860 2027 51 -108 -112 N ATOM 1420 CA LYS A 170 -13.004 -24.974 0.407 1.00 16.47 C ANISOU 1420 CA LYS A 170 2105 2005 2148 27 -114 -149 C ATOM 1421 C LYS A 170 -12.456 -24.819 -1.009 1.00 16.63 C ANISOU 1421 C LYS A 170 2138 2046 2135 57 -115 -148 C ATOM 1422 O LYS A 170 -11.713 -25.675 -1.500 1.00 16.33 O ANISOU 1422 O LYS A 170 2129 1987 2088 56 -105 -165 O ATOM 1423 CB LYS A 170 -14.484 -25.382 0.355 1.00 17.19 C ANISOU 1423 CB LYS A 170 2170 2136 2225 -8 -134 -181 C ATOM 1424 CG LYS A 170 -14.748 -26.881 0.164 1.00 19.63 C ANISOU 1424 CG LYS A 170 2503 2430 2525 -55 -136 -223 C ATOM 1425 CD LYS A 170 -14.136 -27.737 1.285 1.00 22.70 C ANISOU 1425 CD LYS A 170 2927 2753 2945 -80 -118 -222 C ATOM 1426 CE LYS A 170 -14.894 -27.600 2.612 1.00 24.36 C ANISOU 1426 CE LYS A 170 3115 2963 3178 -113 -115 -216 C ATOM 1427 NZ LYS A 170 -14.751 -26.228 3.189 1.00 24.84 N ANISOU 1427 NZ LYS A 170 3145 3038 3256 -76 -112 -179 N ATOM 1428 N GLN A 171 -12.819 -23.710 -1.648 1.00 16.88 N ANISOU 1428 N GLN A 171 2151 2118 2147 86 -125 -128 N ATOM 1429 CA GLN A 171 -12.313 -23.374 -2.973 1.00 17.56 C ANISOU 1429 CA GLN A 171 2249 2227 2196 116 -125 -120 C ATOM 1430 C GLN A 171 -10.787 -23.188 -2.982 1.00 17.30 C ANISOU 1430 C GLN A 171 2241 2160 2173 134 -97 -96 C ATOM 1431 O GLN A 171 -10.113 -23.669 -3.887 1.00 17.48 O ANISOU 1431 O GLN A 171 2283 2189 2172 142 -89 -107 O ATOM 1432 CB GLN A 171 -13.052 -22.149 -3.537 1.00 17.82 C ANISOU 1432 CB GLN A 171 2262 2304 2204 146 -143 -97 C ATOM 1433 CG GLN A 171 -12.664 -21.757 -4.966 1.00 19.35 C ANISOU 1433 CG GLN A 171 2472 2527 2352 176 -145 -85 C ATOM 1434 CD GLN A 171 -12.827 -22.890 -5.977 1.00 21.18 C ANISOU 1434 CD GLN A 171 2712 2784 2549 161 -154 -127 C ATOM 1435 OE1 GLN A 171 -13.808 -23.646 -5.946 1.00 20.81 O ANISOU 1435 OE1 GLN A 171 2650 2760 2499 134 -173 -165 O ATOM 1436 NE2 GLN A 171 -11.860 -23.005 -6.887 1.00 21.72 N ANISOU 1436 NE2 GLN A 171 2806 2853 2592 176 -138 -123 N ATOM 1437 N HIS A 172 -10.246 -22.510 -1.971 1.00 17.34 N ANISOU 1437 N HIS A 172 2243 2135 2212 139 -83 -67 N ATOM 1438 CA HIS A 172 -8.790 -22.350 -1.852 1.00 17.54 C ANISOU 1438 CA HIS A 172 2283 2135 2248 150 -56 -48 C ATOM 1439 C HIS A 172 -8.044 -23.678 -1.651 1.00 18.34 C ANISOU 1439 C HIS A 172 2402 2209 2358 141 -45 -76 C ATOM 1440 O HIS A 172 -6.985 -23.881 -2.246 1.00 18.29 O ANISOU 1440 O HIS A 172 2407 2204 2337 157 -29 -78 O ATOM 1441 CB HIS A 172 -8.414 -21.332 -0.767 1.00 16.56 C ANISOU 1441 CB HIS A 172 2149 1986 2156 153 -46 -15 C ATOM 1442 CG HIS A 172 -8.742 -19.915 -1.130 1.00 16.05 C ANISOU 1442 CG HIS A 172 2081 1938 2079 172 -50 19 C ATOM 1443 ND1 HIS A 172 -8.704 -18.884 -0.216 1.00 14.64 N ANISOU 1443 ND1 HIS A 172 1897 1739 1927 175 -46 45 N ATOM 1444 CD2 HIS A 172 -9.128 -19.361 -2.303 1.00 14.91 C ANISOU 1444 CD2 HIS A 172 1942 1826 1896 191 -60 29 C ATOM 1445 CE1 HIS A 172 -9.039 -17.754 -0.813 1.00 14.03 C ANISOU 1445 CE1 HIS A 172 1827 1675 1829 196 -53 71 C ATOM 1446 NE2 HIS A 172 -9.305 -18.017 -2.079 1.00 14.40 N ANISOU 1446 NE2 HIS A 172 1881 1755 1836 207 -62 64 N ATOM 1447 N GLU A 173 -8.602 -24.574 -0.833 1.00 19.46 N ANISOU 1447 N GLU A 173 2547 2326 2520 116 -54 -99 N ATOM 1448 CA GLU A 173 -8.031 -25.920 -0.631 1.00 21.02 C ANISOU 1448 CA GLU A 173 2772 2490 2724 110 -47 -128 C ATOM 1449 C GLU A 173 -7.870 -26.664 -1.957 1.00 21.82 C ANISOU 1449 C GLU A 173 2892 2608 2788 118 -49 -158 C ATOM 1450 O GLU A 173 -6.836 -27.278 -2.213 1.00 22.11 O ANISOU 1450 O GLU A 173 2950 2631 2821 138 -35 -170 O ATOM 1451 CB GLU A 173 -8.896 -26.755 0.318 1.00 21.32 C ANISOU 1451 CB GLU A 173 2819 2501 2782 74 -58 -147 C ATOM 1452 CG GLU A 173 -8.867 -26.337 1.788 1.00 22.35 C ANISOU 1452 CG GLU A 173 2937 2606 2948 65 -53 -123 C ATOM 1453 CD GLU A 173 -9.808 -27.178 2.655 1.00 24.12 C ANISOU 1453 CD GLU A 173 3171 2809 3186 23 -61 -142 C ATOM 1454 OE1 GLU A 173 -10.389 -28.160 2.140 1.00 24.87 O ANISOU 1454 OE1 GLU A 173 3285 2902 3263 -2 -70 -174 O ATOM 1455 OE2 GLU A 173 -9.966 -26.855 3.855 1.00 24.64 O ANISOU 1455 OE2 GLU A 173 3226 2860 3276 12 -58 -125 O ATOM 1456 N LYS A 174 -8.903 -26.587 -2.792 1.00 22.96 N ANISOU 1456 N LYS A 174 3028 2789 2905 107 -67 -172 N ATOM 1457 CA LYS A 174 -8.896 -27.168 -4.129 1.00 24.25 C ANISOU 1457 CA LYS A 174 3208 2979 3029 114 -72 -201 C ATOM 1458 C LYS A 174 -7.769 -26.590 -4.995 1.00 24.75 C ANISOU 1458 C LYS A 174 3272 3064 3068 151 -53 -183 C ATOM 1459 O LYS A 174 -7.063 -27.339 -5.680 1.00 24.87 O ANISOU 1459 O LYS A 174 3308 3079 3063 165 -43 -208 O ATOM 1460 CB LYS A 174 -10.252 -26.940 -4.795 1.00 24.67 C ANISOU 1460 CB LYS A 174 3242 3079 3054 98 -97 -214 C ATOM 1461 CG LYS A 174 -10.551 -27.866 -5.966 1.00 26.48 C ANISOU 1461 CG LYS A 174 3489 3329 3243 90 -109 -259 C ATOM 1462 CD LYS A 174 -11.918 -27.556 -6.582 1.00 29.27 C ANISOU 1462 CD LYS A 174 3815 3739 3567 75 -137 -272 C ATOM 1463 CE LYS A 174 -11.858 -26.412 -7.604 1.00 30.02 C ANISOU 1463 CE LYS A 174 3896 3886 3625 113 -142 -243 C ATOM 1464 NZ LYS A 174 -11.317 -26.838 -8.936 1.00 30.91 N ANISOU 1464 NZ LYS A 174 4030 4022 3692 130 -138 -263 N ATOM 1465 N GLU A 175 -7.603 -25.267 -4.946 1.00 24.89 N ANISOU 1465 N GLU A 175 3269 3100 3087 164 -47 -140 N ATOM 1466 CA GLU A 175 -6.572 -24.560 -5.716 1.00 25.67 C ANISOU 1466 CA GLU A 175 3369 3223 3163 190 -26 -116 C ATOM 1467 C GLU A 175 -5.147 -24.911 -5.287 1.00 26.22 C ANISOU 1467 C GLU A 175 3443 3269 3250 202 1 -117 C ATOM 1468 O GLU A 175 -4.285 -25.148 -6.125 1.00 26.63 O ANISOU 1468 O GLU A 175 3502 3342 3274 220 18 -127 O ATOM 1469 CB GLU A 175 -6.763 -23.040 -5.616 1.00 25.19 C ANISOU 1469 CB GLU A 175 3294 3175 3103 195 -25 -69 C ATOM 1470 CG GLU A 175 -8.051 -22.528 -6.232 1.00 25.01 C ANISOU 1470 CG GLU A 175 3265 3186 3053 198 -52 -64 C ATOM 1471 CD GLU A 175 -8.368 -21.086 -5.858 1.00 24.45 C ANISOU 1471 CD GLU A 175 3185 3113 2991 207 -55 -19 C ATOM 1472 OE1 GLU A 175 -7.509 -20.398 -5.268 1.00 25.03 O ANISOU 1472 OE1 GLU A 175 3261 3163 3088 208 -34 10 O ATOM 1473 OE2 GLU A 175 -9.484 -20.633 -6.167 1.00 24.25 O ANISOU 1473 OE2 GLU A 175 3152 3114 2948 216 -80 -16 O ATOM 1474 N ARG A 176 -4.905 -24.932 -3.980 1.00 26.88 N ANISOU 1474 N ARG A 176 3522 3316 3377 195 4 -108 N ATOM 1475 CA ARG A 176 -3.551 -25.078 -3.453 1.00 27.82 C ANISOU 1475 CA ARG A 176 3637 3420 3513 210 27 -104 C ATOM 1476 C ARG A 176 -3.081 -26.532 -3.365 1.00 28.59 C ANISOU 1476 C ARG A 176 3758 3494 3613 224 28 -144 C ATOM 1477 O ARG A 176 -1.900 -26.793 -3.117 1.00 28.63 O ANISOU 1477 O ARG A 176 3758 3495 3624 247 45 -148 O ATOM 1478 CB ARG A 176 -3.412 -24.349 -2.108 1.00 27.40 C ANISOU 1478 CB ARG A 176 3567 3342 3501 199 30 -74 C ATOM 1479 CG ARG A 176 -4.037 -25.052 -0.903 1.00 28.36 C ANISOU 1479 CG ARG A 176 3697 3422 3656 184 15 -86 C ATOM 1480 CD ARG A 176 -4.451 -24.054 0.197 1.00 29.37 C ANISOU 1480 CD ARG A 176 3807 3538 3814 168 11 -56 C ATOM 1481 NE ARG A 176 -3.579 -22.876 0.272 1.00 29.74 N ANISOU 1481 NE ARG A 176 3836 3598 3865 175 29 -24 N ATOM 1482 CZ ARG A 176 -2.421 -22.820 0.935 1.00 29.91 C ANISOU 1482 CZ ARG A 176 3848 3611 3903 183 45 -18 C ATOM 1483 NH1 ARG A 176 -1.959 -23.880 1.588 1.00 29.92 N ANISOU 1483 NH1 ARG A 176 3857 3591 3919 193 44 -39 N ATOM 1484 NH2 ARG A 176 -1.713 -21.697 0.937 1.00 29.26 N ANISOU 1484 NH2 ARG A 176 3750 3544 3822 180 62 8 N ATOM 1485 N LYS A 177 -4.009 -27.464 -3.578 1.00 29.64 N ANISOU 1485 N LYS A 177 3914 3611 3739 210 9 -175 N ATOM 1486 CA LYS A 177 -3.707 -28.894 -3.568 1.00 30.85 C ANISOU 1486 CA LYS A 177 4100 3731 3890 221 7 -216 C ATOM 1487 C LYS A 177 -3.691 -29.494 -4.970 1.00 31.60 C ANISOU 1487 C LYS A 177 4213 3852 3942 234 7 -251 C ATOM 1488 O LYS A 177 -3.374 -30.669 -5.132 1.00 32.04 O ANISOU 1488 O LYS A 177 4301 3881 3991 249 6 -289 O ATOM 1489 CB LYS A 177 -4.701 -29.661 -2.686 1.00 30.92 C ANISOU 1489 CB LYS A 177 4132 3693 3924 189 -12 -230 C ATOM 1490 CG LYS A 177 -4.323 -29.707 -1.209 1.00 31.87 C ANISOU 1490 CG LYS A 177 4254 3772 4084 188 -8 -211 C ATOM 1491 CD LYS A 177 -5.064 -30.820 -0.469 1.00 33.55 C ANISOU 1491 CD LYS A 177 4503 3931 4311 160 -22 -232 C ATOM 1492 CE LYS A 177 -4.259 -31.295 0.748 1.00 34.54 C ANISOU 1492 CE LYS A 177 4648 4011 4464 179 -16 -223 C ATOM 1493 NZ LYS A 177 -5.024 -32.221 1.637 1.00 34.76 N ANISOU 1493 NZ LYS A 177 4716 3984 4507 144 -28 -233 N ATOM 1494 N GLN A 178 -4.021 -28.687 -5.977 1.00 32.24 N ANISOU 1494 N GLN A 178 4276 3983 3991 231 6 -239 N ATOM 1495 CA GLN A 178 -4.133 -29.173 -7.358 1.00 33.39 C ANISOU 1495 CA GLN A 178 4437 4161 4090 240 4 -272 C ATOM 1496 C GLN A 178 -2.802 -29.696 -7.907 1.00 33.85 C ANISOU 1496 C GLN A 178 4504 4230 4128 280 27 -293 C ATOM 1497 O GLN A 178 -2.735 -30.787 -8.494 1.00 34.36 O ANISOU 1497 O GLN A 178 4599 4286 4172 293 24 -339 O ATOM 1498 CB GLN A 178 -4.682 -28.080 -8.281 1.00 33.65 C ANISOU 1498 CB GLN A 178 4449 4249 4089 234 -1 -247 C ATOM 1499 CG GLN A 178 -5.165 -28.604 -9.637 1.00 35.61 C ANISOU 1499 CG GLN A 178 4713 4533 4286 236 -12 -283 C ATOM 1500 CD GLN A 178 -4.665 -27.768 -10.805 1.00 37.57 C ANISOU 1500 CD GLN A 178 4949 4838 4486 256 3 -263 C ATOM 1501 OE1 GLN A 178 -4.431 -26.565 -10.671 1.00 38.46 O ANISOU 1501 OE1 GLN A 178 5043 4968 4602 258 14 -214 O ATOM 1502 NE2 GLN A 178 -4.495 -28.406 -11.962 1.00 38.49 N ANISOU 1502 NE2 GLN A 178 5083 4986 4557 270 5 -299 N TER 1503 GLN A 178 HETATM 1504 C1 Z80 A 190 -3.891 -8.358 15.315 1.00 30.91 C HETATM 1505 N1 Z80 A 190 -5.147 -9.023 15.344 1.00 31.26 N HETATM 1506 S1 Z80 A 190 -2.555 -10.619 14.651 1.00 30.21 S HETATM 1507 C2 Z80 A 190 -2.676 -8.968 15.007 1.00 30.23 C HETATM 1508 N2 Z80 A 190 -8.783 -6.859 15.987 1.00 31.58 N HETATM 1509 C3 Z80 A 190 -4.153 -11.082 14.316 1.00 30.47 C HETATM 1510 C4 Z80 A 190 -5.244 -10.289 14.688 1.00 30.77 C HETATM 1511 C5 Z80 A 190 -2.729 -6.228 15.576 1.00 31.11 C HETATM 1512 C6 Z80 A 190 -1.522 -6.858 15.283 1.00 30.77 C HETATM 1513 C7 Z80 A 190 -1.501 -8.219 15.000 1.00 30.04 C HETATM 1514 C8 Z80 A 190 -4.366 -12.299 13.661 1.00 30.21 C HETATM 1515 C9 Z80 A 190 -5.657 -12.739 13.359 1.00 30.70 C HETATM 1516 C10 Z80 A 190 -6.744 -11.950 13.720 1.00 30.89 C HETATM 1517 C11 Z80 A 190 -6.527 -10.742 14.370 1.00 30.84 C HETATM 1518 C12 Z80 A 190 -5.721 -9.046 16.707 1.00 31.72 C HETATM 1519 C13 Z80 A 190 -7.199 -8.630 16.640 1.00 32.43 C HETATM 1520 C14 Z80 A 190 -7.432 -7.122 16.519 1.00 31.56 C HETATM 1521 C15 Z80 A 190 -9.634 -6.232 17.010 1.00 31.03 C HETATM 1522 C16 Z80 A 190 -8.694 -5.954 14.828 1.00 31.65 C HETATM 1523 CL1 Z80 A 190 -8.435 -12.449 13.369 1.00 31.87 CL HETATM 1524 C17 Z80 A 190 -3.901 -6.981 15.589 1.00 31.38 C HETATM 1525 C ACY A 191 4.538 -19.216 27.402 1.00 26.60 C HETATM 1526 O ACY A 191 4.942 -19.321 28.580 1.00 26.32 O HETATM 1527 OXT ACY A 191 5.267 -18.780 26.481 1.00 25.80 O HETATM 1528 CH3 ACY A 191 3.126 -19.619 27.098 1.00 26.37 C HETATM 1529 O HOH A 192 -15.389 -17.389 14.192 1.00 4.76 O HETATM 1530 O HOH A 193 -15.638 -16.268 8.831 1.00 12.74 O HETATM 1531 O HOH A 194 0.321 -15.251 28.378 1.00 9.81 O HETATM 1532 O HOH A 195 -8.480 -15.268 39.449 1.00 10.41 O HETATM 1533 O HOH A 196 -4.033 -17.154 36.045 1.00 10.85 O HETATM 1534 O HOH A 197 0.352 -17.903 29.978 1.00 8.03 O HETATM 1535 O HOH A 198 -18.544 -17.602 20.156 1.00 3.02 O HETATM 1536 O HOH A 199 -6.406 -16.442 33.045 1.00 10.42 O HETATM 1537 O HOH A 200 -2.972 -21.045 25.303 1.00 7.52 O HETATM 1538 O HOH A 201 10.404 -21.250 9.515 1.00 7.21 O HETATM 1539 O HOH A 202 -17.762 -10.041 35.111 1.00 11.53 O HETATM 1540 O HOH A 203 -5.266 -13.266 42.326 1.00 8.78 O HETATM 1541 O HOH A 204 1.753 -8.106 3.626 1.00 7.47 O HETATM 1542 O HOH A 205 -4.561 -14.396 33.785 1.00 9.43 O HETATM 1543 O HOH A 206 -14.750 -11.929 32.976 1.00 14.26 O HETATM 1544 O HOH A 207 -6.259 -20.747 2.895 1.00 21.71 O HETATM 1545 O HOH A 208 5.533 -15.026 23.999 1.00 10.38 O HETATM 1546 O HOH A 209 -12.736 -26.198 22.105 1.00 9.60 O HETATM 1547 O HOH A 210 -11.929 5.921 21.551 1.00 5.20 O HETATM 1548 O HOH A 211 5.563 -18.213 6.358 1.00 4.22 O HETATM 1549 O HOH A 212 6.420 -4.317 20.098 1.00 3.52 O HETATM 1550 O HOH A 213 3.284 -11.081 24.894 1.00 12.99 O HETATM 1551 O HOH A 214 -22.060 -10.818 21.063 1.00 6.57 O HETATM 1552 O HOH A 215 -2.120 -30.876 -10.857 1.00 15.14 O HETATM 1553 O HOH A 216 -0.327 -10.704 43.812 1.00 7.27 O HETATM 1554 O HOH A 217 -8.853 0.559 35.223 1.00 21.80 O HETATM 1555 O HOH A 218 13.540 -10.524 9.275 1.00 12.99 O HETATM 1556 O HOH A 219 -16.397 -4.764 24.840 1.00 11.82 O HETATM 1557 O HOH A 220 -8.036 -25.741 14.085 1.00 3.40 O HETATM 1558 O HOH A 221 -8.571 -21.499 27.411 1.00 9.30 O HETATM 1559 O HOH A 222 8.529 -9.575 26.670 1.00 14.58 O HETATM 1560 O HOH A 223 -1.821 -22.085 22.259 1.00 12.43 O HETATM 1561 O HOH A 224 -27.241 -18.766 14.404 1.00 13.50 O HETATM 1562 O HOH A 225 -7.192 -7.986 20.782 1.00 13.27 O HETATM 1563 O HOH A 226 -8.742 -9.131 43.676 1.00 8.38 O HETATM 1564 O HOH A 227 -18.686 -20.312 20.429 1.00 11.85 O HETATM 1565 O HOH A 228 -2.968 -6.362 38.978 1.00 14.42 O HETATM 1566 O HOH A 229 -3.653 -15.245 -0.416 1.00 23.32 O HETATM 1567 O HOH A 230 -19.633 -14.230 0.722 1.00 11.50 O HETATM 1568 O HOH A 231 -17.977 -21.670 22.993 1.00 10.34 O HETATM 1569 O HOH A 232 -21.710 -4.157 30.500 1.00 15.81 O HETATM 1570 O HOH A 233 -17.389 -10.131 17.146 1.00 14.52 O HETATM 1571 O HOH A 234 -16.924 -24.145 -2.444 1.00 10.60 O HETATM 1572 O HOH A 235 2.475 -3.909 39.470 1.00 18.97 O HETATM 1573 O HOH A 236 -14.297 -2.085 31.276 1.00 22.39 O HETATM 1574 O HOH A 237 -13.781 -23.775 8.436 1.00 25.88 O HETATM 1575 O HOH A 238 -2.821 2.633 31.779 1.00 14.96 O HETATM 1576 O HOH A 239 -10.073 -10.546 5.810 1.00 17.98 O HETATM 1577 O HOH A 240 -19.506 -22.533 7.767 1.00 9.75 O HETATM 1578 O HOH A 241 -9.041 1.559 18.176 1.00 6.20 O HETATM 1579 O HOH A 242 -11.751 -27.334 14.193 1.00 14.50 O HETATM 1580 O HOH A 243 -12.829 -11.476 -0.193 1.00 17.64 O HETATM 1581 O HOH A 244 8.233 -13.769 5.326 1.00 17.18 O HETATM 1582 O HOH A 245 -24.121 -19.282 7.454 1.00 18.70 O HETATM 1583 O HOH A 246 -3.396 -20.100 -0.536 1.00 24.67 O HETATM 1584 O HOH A 247 -22.794 -16.924 19.414 1.00 2.32 O HETATM 1585 O HOH A 248 10.127 -9.099 10.707 1.00 13.35 O HETATM 1586 O HOH A 249 2.819 -14.583 27.884 1.00 6.73 O HETATM 1587 O HOH A 250 3.287 -6.345 8.473 1.00 12.77 O HETATM 1588 O HOH A 251 -3.893 -23.748 -8.377 1.00 13.38 O HETATM 1589 O HOH A 252 -19.635 -10.647 17.432 1.00 17.13 O HETATM 1590 O HOH A 253 7.048 -17.295 24.138 1.00 13.35 O HETATM 1591 O HOH A 254 -2.315 -28.974 21.661 1.00 16.26 O HETATM 1592 O HOH A 255 -7.460 -19.999 35.733 1.00 19.82 O HETATM 1593 O HOH A 256 0.204 -22.288 31.286 1.00 15.06 O HETATM 1594 O HOH A 257 -21.263 -20.530 4.765 1.00 17.50 O HETATM 1595 O HOH A 258 -0.967 -4.349 23.952 1.00 15.62 O HETATM 1596 O HOH A 259 -6.157 -9.325 7.208 1.00 15.20 O HETATM 1597 O HOH A 260 -20.899 -12.549 28.264 1.00 4.79 O HETATM 1598 O HOH A 261 -26.111 -15.040 16.713 1.00 13.50 O HETATM 1599 O HOH A 262 -4.985 6.829 26.212 1.00 14.29 O HETATM 1600 O HOH A 263 -9.059 -8.666 11.185 1.00 22.55 O HETATM 1601 O HOH A 264 0.510 -20.859 29.073 1.00 22.60 O HETATM 1602 O HOH A 265 -23.389 -13.948 7.923 1.00 18.85 O HETATM 1603 O HOH A 266 0.519 -6.749 7.592 1.00 15.11 O HETATM 1604 O HOH A 267 -16.679 -4.112 11.307 1.00 24.30 O HETATM 1605 O HOH A 268 -16.351 -26.863 17.667 1.00 16.12 O HETATM 1606 O HOH A 269 8.020 -16.275 4.774 1.00 17.22 O HETATM 1607 O HOH A 270 -17.903 -27.345 28.503 1.00 10.03 O HETATM 1608 O HOH A 271 -0.783 -19.331 6.951 1.00 18.99 O HETATM 1609 O HOH A 272 -0.008 -6.819 30.094 1.00 9.87 O HETATM 1610 O HOH A 273 -8.421 7.094 25.399 1.00 17.46 O HETATM 1611 O HOH A 274 -3.169 -7.997 8.017 1.00 33.63 O HETATM 1612 O HOH A 275 3.346 -14.676 25.411 1.00 8.79 O HETATM 1613 O HOH A 276 -10.455 -27.004 21.422 1.00 18.57 O HETATM 1614 O HOH A 277 -22.405 -13.702 0.956 1.00 13.48 O HETATM 1615 O HOH A 278 -7.540 -6.278 38.543 1.00 25.83 O HETATM 1616 O HOH A 279 -14.396 -8.512 35.425 1.00 28.58 O HETATM 1617 O HOH A 280 -5.244 -8.566 1.443 1.00 30.74 O HETATM 1618 O HOH A 281 -1.503 -0.841 17.977 1.00 13.42 O HETATM 1619 O HOH A 282 -0.858 -2.429 31.918 1.00 24.50 O HETATM 1620 O HOH A 283 1.729 -5.524 28.539 1.00 18.88 O HETATM 1621 O HOH A 284 -9.109 4.181 18.348 1.00 14.59 O HETATM 1622 O HOH A 285 4.244 -18.930 4.594 1.00 5.43 O HETATM 1623 O HOH A 286 -11.705 4.620 23.968 1.00 9.25 O HETATM 1624 O HOH A 287 -1.646 -33.521 -12.809 1.00 28.78 O HETATM 1625 O HOH A 288 -20.146 -20.705 17.471 1.00 9.89 O HETATM 1626 O HOH A 289 -15.592 -28.513 15.439 1.00 16.96 O HETATM 1627 O HOH A 290 -24.252 -10.931 23.922 1.00 21.66 O HETATM 1628 O HOH A 291 10.554 -8.507 13.175 1.00 19.05 O HETATM 1629 O HOH A 292 2.136 -23.584 28.678 1.00 28.11 O HETATM 1630 O HOH A 293 -4.440 -24.650 15.757 1.00 14.47 O HETATM 1631 O HOH A 294 7.962 -17.821 2.505 1.00 7.98 O HETATM 1632 O HOH A 295 -1.224 -2.628 21.330 1.00 12.54 O HETATM 1633 O HOH A 296 7.233 -20.179 6.540 1.00 19.15 O HETATM 1634 O HOH A 297 4.319 -24.259 8.966 1.00 12.56 O HETATM 1635 O HOH A 298 5.686 -2.917 22.214 1.00 19.70 O HETATM 1636 O HOH A 299 -19.249 -26.735 14.016 1.00 24.88 O HETATM 1637 O HOH A 300 6.848 -8.981 30.490 1.00 8.95 O HETATM 1638 O HOH A 301 6.044 -22.329 10.072 1.00 18.32 O HETATM 1639 O HOH A 302 6.298 -2.444 17.840 1.00 18.50 O HETATM 1640 O HOH A 303 -0.729 -8.147 44.181 1.00 15.36 O HETATM 1641 O HOH A 304 0.602 -5.784 42.787 1.00 21.79 O HETATM 1642 O HOH A 305 -2.134 -5.300 30.621 1.00 28.04 O HETATM 1643 O HOH A 306 -11.305 -22.787 33.681 1.00 22.03 O HETATM 1644 O HOH A 307 -3.366 -27.912 26.466 1.00 24.41 O HETATM 1645 O HOH A 308 -1.241 -23.056 8.601 1.00 26.28 O HETATM 1646 O HOH A 309 -1.703 -4.712 33.130 1.00 28.94 O HETATM 1647 O HOH A 310 5.729 -5.706 25.621 1.00 14.55 O HETATM 1648 O HOH A 311 -11.993 -7.596 6.527 1.00 23.75 O HETATM 1649 O HOH A 312 4.206 -17.137 1.867 1.00 19.18 O HETATM 1650 O HOH A 313 -11.977 -28.625 -1.479 1.00 21.98 O HETATM 1651 O HOH A 314 -11.467 -28.064 27.742 1.00 14.61 O HETATM 1652 O HOH A 315 -1.987 -11.556 46.122 1.00 26.06 O HETATM 1653 O HOH A 316 13.160 -14.954 21.412 1.00 16.80 O HETATM 1654 O HOH A 317 -5.623 -20.575 32.436 1.00 21.75 O HETATM 1655 O HOH A 318 -1.915 -20.445 32.259 1.00 13.08 O HETATM 1656 O HOH A 319 4.698 -27.196 10.043 1.00 24.55 O HETATM 1657 O HOH A 320 -4.125 -26.561 12.051 1.00 19.66 O HETATM 1658 O HOH A 321 -15.965 5.341 19.018 1.00 18.20 O HETATM 1659 O HOH A 322 -22.539 -13.257 15.961 1.00 18.95 O HETATM 1660 O HOH A 323 -8.026 -26.053 30.541 1.00 30.21 O HETATM 1661 O HOH A 324 -3.128 -5.133 35.297 1.00 35.23 O HETATM 1662 O HOH A 325 9.620 -17.512 26.397 1.00 24.26 O HETATM 1663 O HOH A 326 -11.319 -8.492 1.659 1.00 25.21 O HETATM 1664 O HOH A 327 8.867 -2.398 18.377 1.00 13.87 O HETATM 1665 O HOH A 328 -4.705 -27.692 29.769 1.00 30.77 O HETATM 1666 O HOH A 329 -28.045 -22.184 12.133 1.00 29.33 O CONECT 46 1229 CONECT 608 1385 CONECT 1229 46 CONECT 1385 608 CONECT 1504 1505 1507 1524 CONECT 1505 1504 1510 1518 CONECT 1506 1507 1509 CONECT 1507 1504 1506 1513 CONECT 1508 1520 1521 1522 CONECT 1509 1506 1510 1514 CONECT 1510 1505 1509 1517 CONECT 1511 1512 1524 CONECT 1512 1511 1513 CONECT 1513 1507 1512 CONECT 1514 1509 1515 CONECT 1515 1514 1516 CONECT 1516 1515 1517 1523 CONECT 1517 1510 1516 CONECT 1518 1505 1519 CONECT 1519 1518 1520 CONECT 1520 1508 1519 CONECT 1521 1508 CONECT 1522 1508 CONECT 1523 1516 CONECT 1524 1504 1511 CONECT 1525 1526 1527 1528 CONECT 1526 1525 CONECT 1527 1525 CONECT 1528 1525 MASTER 287 0 2 7 10 0 5 6 1665 1 29 15 END If you find results from this site helpful for your research, please cite one of our papers:
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