Browse entries in the PDBbind-CN Database
HEADER PROTEIN TRANSPORT 05-JAN-03 1J2J TITLE CRYSTAL STRUCTURE OF GGA1 GAT N-TERMINAL REGION IN COMPLEX TITLE 2 WITH ARF1 GTP FORM COMPND MOL_ID: 1; COMPND 2 MOLECULE: ADP-RIBOSYLATION FACTOR 1; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: RESIDUES 18-181; COMPND 5 SYNONYM: ARF1; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: ADP-RIBOSYLATION FACTOR BINDING PROTEIN GGA1; COMPND 10 CHAIN: B; COMPND 11 FRAGMENT: GAT N-TERMINAL REGION; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 3 ORGANISM_COMMON: HOUSE MOUSE; SOURCE 4 ORGANISM_TAXID: 10090; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPROEX HT; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_COMMON: HUMAN; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 511693; SOURCE 16 EXPRESSION_SYSTEM_STRAIN: BL21; SOURCE 17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 18 EXPRESSION_SYSTEM_PLASMID: PGEX4T-2 KEYWDS PROTEIN TRANSPORT EXPDTA X-RAY DIFFRACTION AUTHOR T.SHIBA,M.KAWASAKI,H.TAKATSU,T.NOGI,N.MATSUGAKI,N.IGARASHI, AUTHOR 2 M.SUZUKI,R.KATO,K.NAKAYAMA,S.WAKATSUKI REVDAT 2 24-FEB-09 1J2J 1 VERSN REVDAT 1 06-MAY-03 1J2J 0 JRNL AUTH T.SHIBA,M.KAWASAKI,H.TAKATSU,T.NOGI,N.MATSUGAKI, JRNL AUTH 2 N.IGARASHI,M.SUZUKI,R.KATO,K.NAKAYAMA,S.WAKATSUKI JRNL TITL MOLECULAR MECHANISM OF MEMBRANE RECRUITMENT OF GGA JRNL TITL 2 BY ARF IN LYSOSOMAL PROTEIN TRANSPORT JRNL REF NAT.STRUCT.BIOL. V. 10 386 2003 JRNL REFN ISSN 1072-8368 JRNL PMID 12679809 JRNL DOI 10.1038/NSB920 REMARK 1 REMARK 2 REMARK 2 RESOLUTION. 1.60 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5 REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON REMARK 3 REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.85 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0 REMARK 3 NUMBER OF REFLECTIONS : 29080 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) : 0.200 REMARK 3 R VALUE (WORKING SET) : 0.198 REMARK 3 FREE R VALUE : 0.227 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 1545 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 20 REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 1.60 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.64 REMARK 3 REFLECTION IN BIN (WORKING SET) : 1681 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL REMARK 3 BIN R VALUE (WORKING SET) : 0.2660 REMARK 3 BIN FREE R VALUE SET COUNT : 85 REMARK 3 BIN FREE R VALUE : 0.3670 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 1661 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 35 REMARK 3 SOLVENT ATOMS : 278 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 16.79 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 0.19000 REMARK 3 B22 (A**2) : 0.12000 REMARK 3 B33 (A**2) : -0.31000 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): 0.099 REMARK 3 ESU BASED ON FREE R VALUE (A): 0.096 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.062 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.752 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.943 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 1722 ; 0.012 ; 0.021 REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 2327 ; 1.559 ; 1.983 REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 204 ; 4.036 ; 3.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): NULL ; NULL ; NULL REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 327 ;12.109 ;15.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 259 ; 0.108 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 1272 ; 0.006 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 810 ; 0.213 ; 0.300 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): 234 ; 0.147 ; 0.500 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): 24 ; 0.184 ; 0.300 REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 24 ; 0.188 ; 0.500 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): 1022 ; 0.871 ; 1.500 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 1641 ; 1.612 ; 2.000 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 700 ; 2.571 ; 3.000 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 686 ; 4.283 ; 4.500 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 : NULL REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : BABINET MODEL WITH MASK REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.40 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 1J2J COMPLIES WITH FORMAT V. 3.15, 01-DEC-08 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 17-JAN-03. REMARK 100 THE RCSB ID CODE IS RCSB005549. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 14-MAR-02 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL 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-18B REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.0 REMARK 200 MONOCHROMATOR : SI (111) + GE (220) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : CCD REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4 REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM REMARK 200 DATA SCALING SOFTWARE : CCP4 (SCALA) REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 30625 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600 REMARK 200 RESOLUTION RANGE LOW (A) : 30.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 96.4 REMARK 200 DATA REDUNDANCY : NULL REMARK 200 R MERGE (I) : 0.04800 REMARK 200 R SYM (I) : NULL REMARK 200
FOR THE DATA SET : 11.0000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.69 REMARK 200 COMPLETENESS FOR SHELL (%) : 83.1 REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.24500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200
FOR SHELL : 3.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: SOLVE/RESOLVE REMARK 200 STARTING MODEL: PDB ENTRY 1J2I REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 41.71 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.13 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, KI, VAPOR DIFFUSION, REMARK 280 HANGING DROP, 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 24.70500 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.43700 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 30.94700 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.43700 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.70500 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 30.94700 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 2320 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 10860 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 181 REMARK 465 ASN B 166 REMARK 465 VAL B 167 REMARK 465 GLU B 209 REMARK 465 LYS B 210 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 ASN A 132 57.30 -104.85 REMARK 500 ASN A 179 31.68 -86.03 REMARK 500 ARG B 207 66.30 63.70 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MG A1002 MG REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GTP A1001 O2B REMARK 620 2 GTP A1001 O2G 92.7 REMARK 620 3 THR A 31 OG1 88.8 177.7 REMARK 620 4 THR A 48 OG1 179.1 88.2 90.4 REMARK 620 5 HOH A1022 O 90.4 91.9 89.8 89.7 REMARK 620 6 HOH A1021 O 91.3 88.1 90.2 88.6 178.3 REMARK 620 N 1 2 3 4 5 REMARK 800 REMARK 800 SITE REMARK 800 SITE_IDENTIFIER: AC1 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1002 REMARK 800 SITE_IDENTIFIER: AC2 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 1 REMARK 800 SITE_IDENTIFIER: AC3 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 2 REMARK 800 SITE_IDENTIFIER: AC4 REMARK 800 EVIDENCE_CODE: SOFTWARE REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GTP A 1001 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1J2H RELATED DB: PDB REMARK 900 HUMAN GGA1 GAT DOMAIN REMARK 900 RELATED ID: 1J2I RELATED DB: PDB REMARK 900 MOUSE ARF1 (DELTA17-Q71L), GTP FORM DBREF 1J2J A 18 181 UNP Q8BSL7 ARF2_MOUSE 18 181 DBREF 1J2J B 166 210 UNP Q9UJY5 GGA1_HUMAN 166 210 SEQADV 1J2J GLY A 16 UNP Q8BSL7 CLONING ARTIFACT SEQADV 1J2J SER A 17 UNP Q8BSL7 CLONING ARTIFACT SEQADV 1J2J LEU A 71 UNP Q8BSL7 GLN 71 ENGINEERED SEQRES 1 A 166 GLY SER MET ARG ILE LEU MET VAL GLY LEU ASP ALA ALA SEQRES 2 A 166 GLY LYS THR THR ILE LEU TYR LYS LEU LYS LEU GLY GLU SEQRES 3 A 166 ILE VAL THR THR ILE PRO THR ILE GLY PHE ASN VAL GLU SEQRES 4 A 166 THR VAL GLU TYR LYS ASN ILE SER PHE THR VAL TRP ASP SEQRES 5 A 166 VAL GLY GLY LEU ASP LYS ILE ARG PRO LEU TRP ARG HIS SEQRES 6 A 166 TYR PHE GLN ASN THR GLN GLY LEU ILE PHE VAL VAL ASP SEQRES 7 A 166 SER ASN ASP ARG GLU ARG VAL ASN GLU ALA ARG GLU GLU SEQRES 8 A 166 LEU MET ARG MET LEU ALA GLU ASP GLU LEU ARG ASP ALA SEQRES 9 A 166 VAL LEU LEU VAL PHE ALA ASN LYS GLN ASP LEU PRO ASN SEQRES 10 A 166 ALA MET ASN ALA ALA GLU ILE THR ASP LYS LEU GLY LEU SEQRES 11 A 166 HIS SER LEU ARG HIS ARG ASN TRP TYR ILE GLN ALA THR SEQRES 12 A 166 CYS ALA THR SER GLY ASP GLY LEU TYR GLU GLY LEU ASP SEQRES 13 A 166 TRP LEU SER ASN GLN LEU ARG ASN GLN LYS SEQRES 1 B 45 ASN VAL ILE PHE GLU ASP GLU GLU LYS SER LYS MET LEU SEQRES 2 B 45 ALA ARG LEU LEU LYS SER SER HIS PRO GLU ASP LEU ARG SEQRES 3 B 45 ALA ALA ASN LYS LEU ILE LYS GLU MET VAL GLN GLU ASP SEQRES 4 B 45 GLN LYS ARG MET GLU LYS HET MG A1002 1 HET IOD A 1 1 HET IOD B 2 1 HET GTP A1001 32 HETNAM MG MAGNESIUM ION HETNAM IOD IODIDE ION HETNAM GTP GUANOSINE-5'-TRIPHOSPHATE FORMUL 3 MG MG 2+ FORMUL 4 IOD 2(I 1-) FORMUL 6 GTP C10 H16 N5 O14 P3 FORMUL 7 HOH *278(H2 O) HELIX 1 1 GLY A 29 GLY A 40 1 12 HELIX 2 2 LEU A 71 PHE A 82 5 12 HELIX 3 3 ASP A 96 GLU A 98 5 3 HELIX 4 4 ARG A 99 ALA A 112 1 14 HELIX 5 5 GLU A 113 ARG A 117 5 5 HELIX 6 6 ASN A 135 GLY A 144 1 10 HELIX 7 7 LEU A 145 LEU A 148 5 4 HELIX 8 8 GLY A 165 ASN A 179 1 15 HELIX 9 9 ASP B 171 LYS B 183 1 13 HELIX 10 10 HIS B 186 LYS B 206 1 21 SHEET 1 A 6 PHE A 51 TYR A 58 0 SHEET 2 A 6 ILE A 61 VAL A 68 -1 O ASP A 67 N ASN A 52 SHEET 3 A 6 SER A 17 VAL A 23 1 N MET A 22 O TRP A 66 SHEET 4 A 6 GLY A 87 ASP A 93 1 O ILE A 89 N LEU A 21 SHEET 5 A 6 VAL A 120 ASN A 126 1 O LEU A 122 N LEU A 88 SHEET 6 A 6 TRP A 153 ALA A 157 1 O TYR A 154 N VAL A 123 LINK O2B GTP A1001 MG MG A1002 1555 1555 2.07 LINK O2G GTP A1001 MG MG A1002 1555 1555 2.00 LINK MG MG A1002 OG1 THR A 31 1555 1555 2.09 LINK MG MG A1002 OG1 THR A 48 1555 1555 2.10 LINK MG MG A1002 O HOH A1022 1555 1555 2.03 LINK MG MG A1002 O HOH A1021 1555 1555 2.09 SITE 1 AC1 5 THR A 31 THR A 48 GTP A1001 HOH A1021 SITE 2 AC1 5 HOH A1022 SITE 1 AC2 1 TRP A 66 SITE 1 AC3 1 ARG B 180 SITE 1 AC4 26 ASP A 26 ALA A 27 ALA A 28 GLY A 29 SITE 2 AC4 26 LYS A 30 THR A 31 THR A 32 THR A 45 SITE 3 AC4 26 THR A 48 GLY A 69 GLY A 70 ASN A 126 SITE 4 AC4 26 LYS A 127 ASP A 129 LEU A 130 ALA A 160 SITE 5 AC4 26 MG A1002 HOH A1015 HOH A1017 HOH A1018 SITE 6 AC4 26 HOH A1021 HOH A1022 HOH A1025 HOH A1093 SITE 7 AC4 26 HOH A1094 HOH A1095 CRYST1 49.410 61.894 76.874 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 0.020239 0.000000 0.000000 0.00000 SCALE2 0.000000 0.016157 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013008 0.00000 ATOM 1 N GLY A 16 7.211 7.461 16.727 1.00 16.70 N ATOM 2 CA GLY A 16 8.435 8.293 16.401 1.00 15.52 C ATOM 3 C GLY A 16 8.955 9.037 17.628 1.00 14.21 C ATOM 4 O GLY A 16 8.250 9.147 18.635 1.00 15.23 O ATOM 5 N SER A 17 10.186 9.545 17.549 1.00 13.97 N ATOM 6 CA SER A 17 10.798 10.272 18.658 1.00 12.61 C ATOM 7 C SER A 17 11.494 11.506 18.146 1.00 12.21 C ATOM 8 O SER A 17 11.902 11.557 16.999 1.00 12.23 O ATOM 9 CB SER A 17 11.867 9.471 19.396 1.00 13.31 C ATOM 10 OG SER A 17 12.889 9.043 18.517 1.00 14.74 O ATOM 11 N MET A 18 11.656 12.499 19.008 1.00 10.19 N ATOM 12 CA MET A 18 12.402 13.705 18.631 1.00 8.43 C ATOM 13 C MET A 18 13.060 14.254 19.870 1.00 7.86 C ATOM 14 O MET A 18 12.384 14.541 20.861 1.00 9.04 O ATOM 15 CB MET A 18 11.506 14.761 17.983 1.00 8.78 C ATOM 16 CG MET A 18 12.261 15.837 17.179 1.00 9.96 C ATOM 17 SD MET A 18 11.078 16.868 16.355 1.00 11.02 S ATOM 18 CE MET A 18 9.640 15.746 16.225 1.00 21.86 C ATOM 19 N ARG A 19 14.371 14.432 19.800 1.00 8.60 N ATOM 20 CA ARG A 19 15.131 15.005 20.905 1.00 9.01 C ATOM 21 C ARG A 19 15.159 16.526 20.744 1.00 7.63 C ATOM 22 O ARG A 19 15.660 17.056 19.728 1.00 7.84 O ATOM 23 CB ARG A 19 16.568 14.487 20.914 1.00 8.97 C ATOM 24 CG ARG A 19 17.414 15.136 22.008 1.00 8.55 C ATOM 25 CD ARG A 19 18.878 14.629 22.072 1.00 11.23 C ATOM 26 NE ARG A 19 19.697 15.543 22.893 1.00 12.89 N ATOM 27 CZ ARG A 19 20.160 15.274 24.096 1.00 13.62 C ATOM 28 NH1 ARG A 19 20.903 16.164 24.731 1.00 11.17 N ATOM 29 NH2 ARG A 19 19.888 14.113 24.697 1.00 14.93 N ATOM 30 N ILE A 20 14.608 17.220 21.741 1.00 7.50 N ATOM 31 CA ILE A 20 14.508 18.680 21.695 1.00 7.53 C ATOM 32 C ILE A 20 15.364 19.303 22.761 1.00 7.73 C ATOM 33 O ILE A 20 15.307 18.870 23.908 1.00 8.54 O ATOM 34 CB ILE A 20 13.044 19.072 21.965 1.00 7.85 C ATOM 35 CG1 ILE A 20 12.117 18.450 20.918 1.00 9.39 C ATOM 36 CG2 ILE A 20 12.870 20.625 21.946 1.00 9.25 C ATOM 37 CD1 ILE A 20 12.439 18.919 19.470 1.00 10.22 C ATOM 38 N LEU A 21 16.152 20.328 22.396 1.00 5.92 N ATOM 39 CA LEU A 21 16.933 21.059 23.396 1.00 6.99 C ATOM 40 C LEU A 21 16.264 22.428 23.546 1.00 6.77 C ATOM 41 O LEU A 21 16.167 23.178 22.567 1.00 7.34 O ATOM 42 CB LEU A 21 18.393 21.172 22.933 1.00 6.50 C ATOM 43 CG LEU A 21 19.264 22.082 23.831 1.00 7.00 C ATOM 44 CD1 LEU A 21 19.280 21.686 25.293 1.00 8.35 C ATOM 45 CD2 LEU A 21 20.687 22.101 23.226 1.00 7.05 C ATOM 46 N MET A 22 15.764 22.740 24.742 1.00 6.68 N ATOM 47 CA MET A 22 15.091 24.016 24.979 1.00 7.18 C ATOM 48 C MET A 22 16.014 24.897 25.836 1.00 7.35 C ATOM 49 O MET A 22 16.335 24.562 26.977 1.00 8.06 O ATOM 50 CB MET A 22 13.732 23.797 25.682 1.00 7.09 C ATOM 51 CG MET A 22 13.084 25.122 26.010 1.00 7.74 C ATOM 52 SD MET A 22 11.291 24.947 26.390 1.00 9.72 S ATOM 53 CE MET A 22 11.314 23.800 27.821 1.00 10.15 C ATOM 54 N VAL A 23 16.503 25.975 25.223 1.00 8.28 N ATOM 55 CA VAL A 23 17.425 26.912 25.859 1.00 8.64 C ATOM 56 C VAL A 23 16.959 28.340 25.640 1.00 9.00 C ATOM 57 O VAL A 23 15.949 28.596 24.972 1.00 9.08 O ATOM 58 CB VAL A 23 18.866 26.740 25.304 1.00 8.79 C ATOM 59 CG1 VAL A 23 19.536 25.445 25.848 1.00 9.14 C ATOM 60 CG2 VAL A 23 18.842 26.714 23.801 1.00 10.72 C ATOM 61 N GLY A 24 17.675 29.274 26.248 1.00 8.08 N ATOM 62 CA GLY A 24 17.273 30.672 26.217 1.00 8.24 C ATOM 63 C GLY A 24 17.832 31.276 27.493 1.00 8.28 C ATOM 64 O GLY A 24 18.288 30.534 28.366 1.00 8.09 O ATOM 65 N LEU A 25 17.784 32.602 27.624 1.00 8.39 N ATOM 66 CA LEU A 25 18.358 33.237 28.822 1.00 8.01 C ATOM 67 C LEU A 25 17.611 32.807 30.060 1.00 8.96 C ATOM 68 O LEU A 25 16.472 32.338 29.982 1.00 8.70 O ATOM 69 CB LEU A 25 18.247 34.770 28.733 1.00 9.48 C ATOM 70 CG LEU A 25 18.881 35.390 27.491 1.00 9.72 C ATOM 71 CD1 LEU A 25 18.837 36.895 27.711 1.00 10.84 C ATOM 72 CD2 LEU A 25 20.307 34.879 27.292 1.00 9.66 C ATOM 73 N ASP A 26 18.240 32.939 31.238 1.00 8.19 N ATOM 74 CA ASP A 26 17.473 32.714 32.452 1.00 9.32 C ATOM 75 C ASP A 26 16.254 33.614 32.453 1.00 9.58 C ATOM 76 O ASP A 26 16.264 34.703 31.851 1.00 9.14 O ATOM 77 CB ASP A 26 18.319 33.057 33.677 1.00 8.21 C ATOM 78 CG ASP A 26 18.857 34.470 33.623 1.00 10.10 C ATOM 79 OD1 ASP A 26 19.742 34.726 32.803 1.00 11.42 O ATOM 80 OD2 ASP A 26 18.458 35.373 34.373 1.00 14.02 O ATOM 81 N ALA A 27 15.220 33.139 33.133 1.00 8.90 N ATOM 82 CA ALA A 27 13.931 33.834 33.328 1.00 9.52 C ATOM 83 C ALA A 27 13.065 33.921 32.063 1.00 8.94 C ATOM 84 O ALA A 27 12.029 34.564 32.078 1.00 9.56 O ATOM 85 CB ALA A 27 14.138 35.217 33.957 1.00 10.42 C ATOM 86 N ALA A 28 13.436 33.212 31.002 1.00 7.93 N ATOM 87 CA ALA A 28 12.667 33.325 29.738 1.00 7.19 C ATOM 88 C ALA A 28 11.338 32.626 29.817 1.00 7.12 C ATOM 89 O ALA A 28 10.417 32.967 29.090 1.00 7.70 O ATOM 90 CB ALA A 28 13.482 32.788 28.554 1.00 6.93 C ATOM 91 N GLY A 29 11.244 31.639 30.698 1.00 7.26 N ATOM 92 CA GLY A 29 10.042 30.856 30.889 1.00 6.80 C ATOM 93 C GLY A 29 10.114 29.389 30.455 1.00 7.45 C ATOM 94 O GLY A 29 9.089 28.751 30.267 1.00 8.18 O ATOM 95 N LYS A 30 11.325 28.845 30.274 1.00 6.47 N ATOM 96 CA LYS A 30 11.503 27.490 29.788 1.00 6.70 C ATOM 97 C LYS A 30 10.897 26.398 30.677 1.00 6.69 C ATOM 98 O LYS A 30 10.170 25.534 30.214 1.00 6.89 O ATOM 99 CB LYS A 30 13.003 27.219 29.631 1.00 7.17 C ATOM 100 CG LYS A 30 13.651 28.175 28.628 1.00 6.76 C ATOM 101 CD LYS A 30 15.142 27.899 28.373 1.00 6.66 C ATOM 102 CE LYS A 30 16.045 28.096 29.592 1.00 6.68 C ATOM 103 NZ LYS A 30 16.069 29.456 30.218 1.00 6.66 N ATOM 104 N THR A 31 11.252 26.404 31.956 1.00 6.17 N ATOM 105 CA THR A 31 10.740 25.383 32.855 1.00 7.86 C ATOM 106 C THR A 31 9.227 25.482 32.973 1.00 8.49 C ATOM 107 O THR A 31 8.530 24.478 33.020 1.00 9.56 O ATOM 108 CB THR A 31 11.410 25.523 34.210 1.00 6.90 C ATOM 109 OG1 THR A 31 12.846 25.373 34.020 1.00 8.05 O ATOM 110 CG2 THR A 31 10.978 24.409 35.173 1.00 8.94 C ATOM 111 N THR A 32 8.734 26.718 32.985 1.00 8.30 N ATOM 112 CA THR A 32 7.301 26.922 33.033 1.00 8.64 C ATOM 113 C THR A 32 6.649 26.250 31.843 1.00 7.28 C ATOM 114 O THR A 32 5.667 25.545 31.985 1.00 9.49 O ATOM 115 CB THR A 32 6.998 28.418 33.044 1.00 8.28 C ATOM 116 OG1 THR A 32 7.531 28.988 34.255 1.00 9.79 O ATOM 117 CG2 THR A 32 5.502 28.682 33.157 1.00 9.50 C ATOM 118 N ILE A 33 7.219 26.462 30.647 1.00 7.62 N ATOM 119 CA ILE A 33 6.696 25.831 29.439 1.00 7.73 C ATOM 120 C ILE A 33 6.773 24.299 29.501 1.00 7.66 C ATOM 121 O ILE A 33 5.821 23.611 29.135 1.00 8.31 O ATOM 122 CB ILE A 33 7.482 26.351 28.218 1.00 7.73 C ATOM 123 CG1 ILE A 33 7.017 27.767 27.926 1.00 7.86 C ATOM 124 CG2 ILE A 33 7.260 25.454 26.993 1.00 8.34 C ATOM 125 CD1 ILE A 33 7.827 28.510 26.846 1.00 10.27 C ATOM 126 N LEU A 34 7.902 23.768 29.995 1.00 7.70 N ATOM 127 CA LEU A 34 8.067 22.325 30.068 1.00 7.39 C ATOM 128 C LEU A 34 6.942 21.685 30.882 1.00 7.66 C ATOM 129 O LEU A 34 6.317 20.743 30.407 1.00 8.05 O ATOM 130 CB LEU A 34 9.427 21.981 30.704 1.00 7.66 C ATOM 131 CG LEU A 34 9.650 20.473 30.818 1.00 9.08 C ATOM 132 CD1 LEU A 34 9.854 19.814 29.452 1.00 13.91 C ATOM 133 CD2 LEU A 34 10.871 20.235 31.725 1.00 12.64 C ATOM 134 N TYR A 35 6.623 22.251 32.052 1.00 8.62 N ATOM 135 CA TYR A 35 5.626 21.596 32.901 1.00 9.30 C ATOM 136 C TYR A 35 4.210 21.950 32.478 1.00 9.52 C ATOM 137 O TYR A 35 3.265 21.213 32.749 1.00 10.23 O ATOM 138 CB TYR A 35 5.907 21.864 34.398 1.00 8.59 C ATOM 139 CG TYR A 35 7.127 21.118 34.846 1.00 10.49 C ATOM 140 CD1 TYR A 35 7.146 19.719 34.866 1.00 12.85 C ATOM 141 CD2 TYR A 35 8.261 21.798 35.233 1.00 15.41 C ATOM 142 CE1 TYR A 35 8.297 19.029 35.261 1.00 14.88 C ATOM 143 CE2 TYR A 35 9.388 21.133 35.647 1.00 18.98 C ATOM 144 CZ TYR A 35 9.413 19.764 35.646 1.00 21.35 C ATOM 145 OH TYR A 35 10.583 19.144 36.072 1.00 24.58 O ATOM 146 N LYS A 36 4.032 23.070 31.781 1.00 9.43 N ATOM 147 CA LYS A 36 2.728 23.325 31.204 1.00 10.05 C ATOM 148 C LYS A 36 2.450 22.260 30.142 1.00 10.22 C ATOM 149 O LYS A 36 1.329 21.762 30.040 1.00 9.86 O ATOM 150 CB LYS A 36 2.671 24.715 30.581 1.00 9.64 C ATOM 151 CG LYS A 36 1.302 25.039 29.939 1.00 11.75 C ATOM 152 CD LYS A 36 0.183 25.265 30.970 1.00 14.75 C ATOM 153 CE LYS A 36 -1.115 25.717 30.224 1.00 17.76 C ATOM 154 NZ LYS A 36 -2.288 25.405 31.107 1.00 21.30 N ATOM 155 N LEU A 37 3.454 21.915 29.330 1.00 10.73 N ATOM 156 CA LEU A 37 3.273 20.848 28.342 1.00 10.95 C ATOM 157 C LEU A 37 3.079 19.474 29.004 1.00 11.25 C ATOM 158 O LEU A 37 2.192 18.715 28.644 1.00 12.57 O ATOM 159 CB LEU A 37 4.468 20.779 27.373 1.00 11.18 C ATOM 160 CG LEU A 37 4.516 21.953 26.386 1.00 11.29 C ATOM 161 CD1 LEU A 37 5.795 21.897 25.583 1.00 13.26 C ATOM 162 CD2 LEU A 37 3.290 21.948 25.468 1.00 11.66 C ATOM 163 N LYS A 38 3.937 19.148 29.961 1.00 10.36 N ATOM 164 CA LYS A 38 3.972 17.812 30.524 1.00 10.45 C ATOM 165 C LYS A 38 2.797 17.575 31.449 1.00 10.95 C ATOM 166 O LYS A 38 2.197 16.501 31.414 1.00 11.66 O ATOM 167 CB LYS A 38 5.260 17.620 31.323 1.00 10.78 C ATOM 168 CG LYS A 38 5.387 16.299 31.993 1.00 9.23 C ATOM 169 CD LYS A 38 5.385 15.133 31.000 1.00 11.24 C ATOM 170 CE LYS A 38 5.904 13.852 31.663 1.00 11.91 C ATOM 171 NZ LYS A 38 5.763 12.685 30.764 1.00 10.21 N ATOM 172 N LEU A 39 2.501 18.564 32.288 1.00 10.50 N ATOM 173 CA LEU A 39 1.454 18.415 33.327 1.00 11.16 C ATOM 174 C LEU A 39 0.199 19.272 33.141 1.00 11.51 C ATOM 175 O LEU A 39 -0.756 19.150 33.937 1.00 12.20 O ATOM 176 CB LEU A 39 2.020 18.669 34.727 1.00 11.59 C ATOM 177 CG LEU A 39 3.286 17.890 35.077 1.00 9.94 C ATOM 178 CD1 LEU A 39 3.837 18.295 36.451 1.00 12.89 C ATOM 179 CD2 LEU A 39 3.099 16.374 34.960 1.00 12.42 C ATOM 180 N GLY A 40 0.202 20.170 32.163 1.00 10.20 N ATOM 181 CA GLY A 40 -0.978 20.966 31.863 1.00 10.57 C ATOM 182 C GLY A 40 -1.246 22.133 32.785 1.00 9.96 C ATOM 183 O GLY A 40 -2.298 22.779 32.680 1.00 11.45 O ATOM 184 N GLU A 41 -0.284 22.450 33.653 1.00 9.45 N ATOM 185 CA GLU A 41 -0.476 23.543 34.600 1.00 9.89 C ATOM 186 C GLU A 41 0.753 24.412 34.728 1.00 10.33 C ATOM 187 O GLU A 41 1.855 24.010 34.373 1.00 10.82 O ATOM 188 CB GLU A 41 -0.767 23.002 36.009 1.00 10.33 C ATOM 189 CG GLU A 41 -1.894 21.975 36.061 1.00 11.07 C ATOM 190 CD GLU A 41 -3.257 22.569 35.755 1.00 13.35 C ATOM 191 OE1 GLU A 41 -3.457 23.813 35.966 1.00 13.86 O ATOM 192 OE2 GLU A 41 -4.144 21.759 35.338 1.00 13.42 O ATOM 193 N ILE A 42 0.546 25.595 35.285 1.00 9.47 N ATOM 194 CA ILE A 42 1.649 26.459 35.667 1.00 10.40 C ATOM 195 C ILE A 42 2.067 26.061 37.074 1.00 10.50 C ATOM 196 O ILE A 42 1.244 26.102 38.006 1.00 11.54 O ATOM 197 CB ILE A 42 1.178 27.899 35.676 1.00 10.15 C ATOM 198 CG1 ILE A 42 0.799 28.343 34.267 1.00 12.38 C ATOM 199 CG2 ILE A 42 2.241 28.787 36.254 1.00 9.69 C ATOM 200 CD1 ILE A 42 1.913 28.169 33.215 1.00 13.25 C ATOM 201 N VAL A 43 3.316 25.637 37.232 1.00 10.41 N ATOM 202 CA VAL A 43 3.855 25.294 38.561 1.00 10.06 C ATOM 203 C VAL A 43 4.906 26.296 38.952 1.00 9.98 C ATOM 204 O VAL A 43 5.437 26.959 38.079 1.00 9.88 O ATOM 205 CB VAL A 43 4.418 23.868 38.595 1.00 11.36 C ATOM 206 CG1 VAL A 43 3.243 22.879 38.239 1.00 11.47 C ATOM 207 CG2 VAL A 43 5.557 23.737 37.646 1.00 11.61 C ATOM 208 N THR A 44 5.200 26.446 40.245 1.00 9.91 N ATOM 209 CA THR A 44 6.329 27.321 40.624 1.00 9.80 C ATOM 210 C THR A 44 7.658 26.763 40.129 1.00 9.82 C ATOM 211 O THR A 44 7.799 25.557 39.932 1.00 10.31 O ATOM 212 CB THR A 44 6.434 27.483 42.132 1.00 10.73 C ATOM 213 OG1 THR A 44 6.610 26.181 42.730 1.00 11.26 O ATOM 214 CG2 THR A 44 5.137 28.021 42.676 1.00 11.27 C ATOM 215 N THR A 45 8.661 27.636 39.965 1.00 9.51 N ATOM 216 CA THR A 45 9.990 27.219 39.559 1.00 9.33 C ATOM 217 C THR A 45 11.013 27.995 40.333 1.00 9.05 C ATOM 218 O THR A 45 10.695 28.999 40.988 1.00 9.95 O ATOM 219 CB THR A 45 10.289 27.554 38.084 1.00 9.12 C ATOM 220 OG1 THR A 45 10.232 28.977 37.897 1.00 9.99 O ATOM 221 CG2 THR A 45 9.200 26.979 37.169 1.00 9.31 C ATOM 222 N ILE A 46 12.260 27.521 40.245 1.00 10.06 N ATOM 223 CA ILE A 46 13.401 28.279 40.711 1.00 9.77 C ATOM 224 C ILE A 46 14.336 28.288 39.517 1.00 9.23 C ATOM 225 O ILE A 46 14.185 27.480 38.604 1.00 9.91 O ATOM 226 CB ILE A 46 14.116 27.606 41.894 1.00 10.06 C ATOM 227 CG1 ILE A 46 14.556 26.203 41.501 1.00 9.71 C ATOM 228 CG2 ILE A 46 13.205 27.546 43.103 1.00 12.78 C ATOM 229 CD1 ILE A 46 15.592 25.632 42.486 1.00 11.63 C ATOM 230 N PRO A 47 15.282 29.209 39.478 1.00 9.49 N ATOM 231 CA PRO A 47 16.235 29.198 38.375 1.00 8.81 C ATOM 232 C PRO A 47 16.883 27.812 38.335 1.00 9.18 C ATOM 233 O PRO A 47 17.362 27.319 39.362 1.00 9.55 O ATOM 234 CB PRO A 47 17.246 30.281 38.780 1.00 8.90 C ATOM 235 CG PRO A 47 16.399 31.227 39.626 1.00 9.67 C ATOM 236 CD PRO A 47 15.473 30.337 40.405 1.00 10.08 C ATOM 237 N THR A 48 16.891 27.191 37.158 1.00 8.17 N ATOM 238 CA THR A 48 17.337 25.808 36.963 1.00 7.94 C ATOM 239 C THR A 48 18.852 25.705 36.905 1.00 9.48 C ATOM 240 O THR A 48 19.478 26.224 35.990 1.00 9.18 O ATOM 241 CB THR A 48 16.775 25.338 35.626 1.00 7.61 C ATOM 242 OG1 THR A 48 15.339 25.452 35.636 1.00 7.94 O ATOM 243 CG2 THR A 48 17.101 23.824 35.393 1.00 9.39 C ATOM 244 N ILE A 49 19.431 25.031 37.900 1.00 9.63 N ATOM 245 CA ILE A 49 20.880 24.836 37.960 1.00 10.11 C ATOM 246 C ILE A 49 21.071 23.409 37.494 1.00 9.36 C ATOM 247 O ILE A 49 20.886 22.470 38.266 1.00 10.25 O ATOM 248 CB ILE A 49 21.359 25.009 39.405 1.00 10.79 C ATOM 249 CG1 ILE A 49 20.988 26.394 39.941 1.00 13.30 C ATOM 250 CG2 ILE A 49 22.878 24.834 39.493 1.00 10.68 C ATOM 251 CD1 ILE A 49 21.445 27.545 39.061 1.00 16.16 C ATOM 252 N GLY A 50 21.401 23.239 36.222 1.00 9.06 N ATOM 253 CA GLY A 50 21.405 21.919 35.597 1.00 8.63 C ATOM 254 C GLY A 50 20.295 21.881 34.550 1.00 8.21 C ATOM 255 O GLY A 50 20.226 22.746 33.668 1.00 7.84 O ATOM 256 N PHE A 51 19.395 20.922 34.665 1.00 7.72 N ATOM 257 CA PHE A 51 18.342 20.733 33.661 1.00 7.63 C ATOM 258 C PHE A 51 17.105 20.088 34.249 1.00 7.81 C ATOM 259 O PHE A 51 17.103 19.636 35.377 1.00 9.02 O ATOM 260 CB PHE A 51 18.871 19.851 32.509 1.00 7.91 C ATOM 261 CG PHE A 51 19.212 18.439 32.932 1.00 8.42 C ATOM 262 CD1 PHE A 51 18.244 17.443 32.891 1.00 10.34 C ATOM 263 CD2 PHE A 51 20.459 18.131 33.426 1.00 9.23 C ATOM 264 CE1 PHE A 51 18.519 16.146 33.285 1.00 10.22 C ATOM 265 CE2 PHE A 51 20.752 16.844 33.830 1.00 8.87 C ATOM 266 CZ PHE A 51 19.789 15.839 33.761 1.00 10.83 C ATOM 267 N ASN A 52 16.032 20.078 33.455 1.00 7.56 N ATOM 268 CA ASN A 52 14.880 19.233 33.702 1.00 7.76 C ATOM 269 C ASN A 52 14.668 18.530 32.388 1.00 8.45 C ATOM 270 O ASN A 52 14.940 19.112 31.347 1.00 9.30 O ATOM 271 CB ASN A 52 13.603 20.000 34.058 1.00 7.51 C ATOM 272 CG ASN A 52 13.761 20.874 35.275 1.00 9.07 C ATOM 273 OD1 ASN A 52 13.687 22.135 35.198 1.00 11.27 O ATOM 274 ND2 ASN A 52 13.998 20.231 36.421 1.00 8.73 N ATOM 275 N VAL A 53 14.230 17.280 32.424 1.00 8.67 N ATOM 276 CA VAL A 53 13.926 16.608 31.160 1.00 10.15 C ATOM 277 C VAL A 53 12.618 15.861 31.298 1.00 10.61 C ATOM 278 O VAL A 53 12.382 15.181 32.305 1.00 11.18 O ATOM 279 CB VAL A 53 15.059 15.670 30.710 1.00 10.27 C ATOM 280 CG1 VAL A 53 15.345 14.562 31.766 1.00 9.64 C ATOM 281 CG2 VAL A 53 14.688 15.035 29.380 1.00 12.71 C ATOM 282 N GLU A 54 11.713 16.065 30.339 1.00 10.00 N ATOM 283 CA GLU A 54 10.450 15.330 30.334 1.00 10.94 C ATOM 284 C GLU A 54 10.107 14.931 28.908 1.00 11.30 C ATOM 285 O GLU A 54 10.433 15.643 27.931 1.00 11.06 O ATOM 286 CB GLU A 54 9.273 16.146 30.898 1.00 10.92 C ATOM 287 CG GLU A 54 9.442 16.662 32.335 1.00 13.13 C ATOM 288 CD GLU A 54 9.416 15.559 33.378 1.00 15.52 C ATOM 289 OE1 GLU A 54 8.949 14.429 33.066 1.00 14.50 O ATOM 290 OE2 GLU A 54 9.856 15.855 34.532 1.00 17.37 O ATOM 291 N THR A 55 9.410 13.811 28.782 1.00 11.68 N ATOM 292 CA THR A 55 8.957 13.385 27.471 1.00 12.66 C ATOM 293 C THR A 55 7.510 13.767 27.354 1.00 12.90 C ATOM 294 O THR A 55 6.720 13.468 28.266 1.00 14.02 O ATOM 295 CB THR A 55 9.143 11.892 27.308 1.00 13.20 C ATOM 296 OG1 THR A 55 10.549 11.630 27.399 1.00 16.10 O ATOM 297 CG2 THR A 55 8.747 11.451 25.892 1.00 14.55 C ATOM 298 N VAL A 56 7.180 14.434 26.250 1.00 12.50 N ATOM 299 CA VAL A 56 5.827 14.875 25.961 1.00 13.84 C ATOM 300 C VAL A 56 5.329 14.098 24.744 1.00 14.29 C ATOM 301 O VAL A 56 5.955 14.125 23.687 1.00 13.58 O ATOM 302 CB VAL A 56 5.803 16.381 25.668 1.00 14.57 C ATOM 303 CG1 VAL A 56 4.430 16.822 25.197 1.00 15.69 C ATOM 304 CG2 VAL A 56 6.254 17.181 26.902 1.00 14.12 C ATOM 305 N GLU A 57 4.212 13.385 24.898 1.00 15.47 N ATOM 306 CA GLU A 57 3.637 12.629 23.790 1.00 16.94 C ATOM 307 C GLU A 57 2.644 13.513 23.049 1.00 16.52 C ATOM 308 O GLU A 57 1.686 14.019 23.651 1.00 17.48 O ATOM 309 CB GLU A 57 2.918 11.388 24.314 1.00 17.61 C ATOM 310 CG GLU A 57 3.736 10.505 25.242 1.00 21.48 C ATOM 311 CD GLU A 57 4.911 9.844 24.544 1.00 24.07 C ATOM 312 OE1 GLU A 57 4.744 9.378 23.400 1.00 26.74 O ATOM 313 OE2 GLU A 57 6.012 9.805 25.141 1.00 27.53 O ATOM 314 N TYR A 58 2.880 13.709 21.762 1.00 16.45 N ATOM 315 CA TYR A 58 2.041 14.578 20.945 1.00 17.46 C ATOM 316 C TYR A 58 2.079 14.151 19.488 1.00 17.58 C ATOM 317 O TYR A 58 3.147 13.986 18.912 1.00 17.57 O ATOM 318 CB TYR A 58 2.523 16.021 21.066 1.00 17.11 C ATOM 319 CG TYR A 58 1.625 17.012 20.390 1.00 17.41 C ATOM 320 CD1 TYR A 58 0.328 17.219 20.839 1.00 17.61 C ATOM 321 CD2 TYR A 58 2.053 17.710 19.282 1.00 18.08 C ATOM 322 CE1 TYR A 58 -0.501 18.124 20.210 1.00 18.46 C ATOM 323 CE2 TYR A 58 1.232 18.640 18.657 1.00 18.28 C ATOM 324 CZ TYR A 58 -0.047 18.830 19.125 1.00 18.78 C ATOM 325 OH TYR A 58 -0.878 19.732 18.504 1.00 20.42 O ATOM 326 N LYS A 59 0.905 13.961 18.892 1.00 19.15 N ATOM 327 CA LYS A 59 0.802 13.562 17.485 1.00 20.19 C ATOM 328 C LYS A 59 1.619 12.294 17.209 1.00 19.97 C ATOM 329 O LYS A 59 2.298 12.176 16.183 1.00 20.03 O ATOM 330 CB LYS A 59 1.219 14.695 16.548 1.00 21.27 C ATOM 331 CG LYS A 59 0.309 15.918 16.613 1.00 25.29 C ATOM 332 CD LYS A 59 -0.875 15.762 15.705 1.00 30.11 C ATOM 333 CE LYS A 59 -1.450 17.112 15.342 1.00 31.79 C ATOM 334 NZ LYS A 59 -1.804 17.880 16.561 1.00 33.58 N ATOM 335 N ASN A 60 1.576 11.378 18.158 1.00 19.97 N ATOM 336 CA ASN A 60 2.288 10.106 18.023 1.00 20.27 C ATOM 337 C ASN A 60 3.796 10.254 18.001 1.00 19.62 C ATOM 338 O ASN A 60 4.504 9.374 17.524 1.00 20.65 O ATOM 339 CB ASN A 60 1.825 9.363 16.776 1.00 20.13 C ATOM 340 CG ASN A 60 0.451 8.774 16.954 1.00 21.38 C ATOM 341 OD1 ASN A 60 0.070 8.399 18.059 1.00 25.54 O ATOM 342 ND2 ASN A 60 -0.320 8.749 15.898 1.00 20.26 N ATOM 343 N ILE A 61 4.288 11.384 18.491 1.00 17.92 N ATOM 344 CA ILE A 61 5.725 11.576 18.576 1.00 15.77 C ATOM 345 C ILE A 61 6.078 11.721 20.043 1.00 14.99 C ATOM 346 O ILE A 61 5.389 12.432 20.764 1.00 13.99 O ATOM 347 CB ILE A 61 6.174 12.839 17.835 1.00 15.47 C ATOM 348 CG1 ILE A 61 6.096 12.689 16.319 1.00 16.57 C ATOM 349 CG2 ILE A 61 7.601 13.182 18.195 1.00 15.17 C ATOM 350 CD1 ILE A 61 6.105 14.021 15.614 1.00 18.35 C ATOM 351 N SER A 62 7.114 11.012 20.488 1.00 13.76 N ATOM 352 CA SER A 62 7.592 11.198 21.858 1.00 14.26 C ATOM 353 C SER A 62 8.681 12.260 21.783 1.00 12.63 C ATOM 354 O SER A 62 9.769 11.980 21.284 1.00 11.35 O ATOM 355 CB SER A 62 8.158 9.909 22.458 1.00 15.21 C ATOM 356 OG SER A 62 7.153 8.887 22.532 1.00 18.94 O ATOM 357 N PHE A 63 8.362 13.468 22.244 1.00 11.72 N ATOM 358 CA PHE A 63 9.336 14.571 22.266 1.00 10.99 C ATOM 359 C PHE A 63 10.062 14.541 23.594 1.00 10.90 C ATOM 360 O PHE A 63 9.455 14.799 24.629 1.00 12.40 O ATOM 361 CB PHE A 63 8.614 15.917 22.185 1.00 10.34 C ATOM 362 CG PHE A 63 7.993 16.224 20.853 1.00 10.56 C ATOM 363 CD1 PHE A 63 6.667 15.878 20.589 1.00 12.39 C ATOM 364 CD2 PHE A 63 8.715 16.934 19.894 1.00 10.06 C ATOM 365 CE1 PHE A 63 6.092 16.205 19.355 1.00 12.01 C ATOM 366 CE2 PHE A 63 8.143 17.271 18.674 1.00 12.45 C ATOM 367 CZ PHE A 63 6.836 16.894 18.399 1.00 13.69 C ATOM 368 N THR A 64 11.357 14.219 23.596 1.00 9.57 N ATOM 369 CA THR A 64 12.092 14.302 24.839 1.00 9.13 C ATOM 370 C THR A 64 12.654 15.709 24.878 1.00 9.15 C ATOM 371 O THR A 64 13.509 16.094 24.061 1.00 9.24 O ATOM 372 CB THR A 64 13.180 13.304 24.867 1.00 8.98 C ATOM 373 OG1 THR A 64 12.589 11.990 24.961 1.00 13.12 O ATOM 374 CG2 THR A 64 13.944 13.441 26.151 1.00 10.45 C ATOM 375 N VAL A 65 12.144 16.486 25.809 1.00 8.27 N ATOM 376 CA VAL A 65 12.491 17.889 25.883 1.00 8.32 C ATOM 377 C VAL A 65 13.451 18.158 27.039 1.00 8.72 C ATOM 378 O VAL A 65 13.125 17.931 28.214 1.00 7.86 O ATOM 379 CB VAL A 65 11.225 18.752 26.072 1.00 8.80 C ATOM 380 CG1 VAL A 65 11.557 20.223 26.069 1.00 10.03 C ATOM 381 CG2 VAL A 65 10.217 18.470 24.970 1.00 10.04 C ATOM 382 N TRP A 66 14.637 18.641 26.692 1.00 7.20 N ATOM 383 CA TRP A 66 15.671 18.997 27.652 1.00 7.95 C ATOM 384 C TRP A 66 15.581 20.479 27.952 1.00 8.42 C ATOM 385 O TRP A 66 15.916 21.310 27.105 1.00 7.97 O ATOM 386 CB TRP A 66 17.049 18.665 27.065 1.00 8.15 C ATOM 387 CG TRP A 66 17.217 17.179 26.858 1.00 9.01 C ATOM 388 CD1 TRP A 66 16.817 16.442 25.786 1.00 10.37 C ATOM 389 CD2 TRP A 66 17.783 16.255 27.783 1.00 14.39 C ATOM 390 NE1 TRP A 66 17.132 15.117 25.968 1.00 13.57 N ATOM 391 CE2 TRP A 66 17.730 14.975 27.186 1.00 15.51 C ATOM 392 CE3 TRP A 66 18.364 16.386 29.045 1.00 17.95 C ATOM 393 CZ2 TRP A 66 18.200 13.831 27.820 1.00 20.32 C ATOM 394 CZ3 TRP A 66 18.839 15.240 29.673 1.00 20.53 C ATOM 395 CH2 TRP A 66 18.747 13.985 29.052 1.00 19.87 C ATOM 396 N ASP A 67 15.105 20.804 29.153 1.00 7.23 N ATOM 397 CA ASP A 67 14.983 22.177 29.596 1.00 7.38 C ATOM 398 C ASP A 67 16.289 22.505 30.321 1.00 7.67 C ATOM 399 O ASP A 67 16.528 22.031 31.429 1.00 9.13 O ATOM 400 CB ASP A 67 13.779 22.223 30.556 1.00 6.09 C ATOM 401 CG ASP A 67 13.799 23.421 31.450 1.00 7.84 C ATOM 402 OD1 ASP A 67 14.288 24.506 31.035 1.00 7.91 O ATOM 403 OD2 ASP A 67 13.310 23.348 32.584 1.00 7.68 O ATOM 404 N VAL A 68 17.136 23.321 29.696 1.00 7.21 N ATOM 405 CA VAL A 68 18.485 23.573 30.237 1.00 7.99 C ATOM 406 C VAL A 68 18.604 24.973 30.822 1.00 8.62 C ATOM 407 O VAL A 68 18.185 25.954 30.206 1.00 9.36 O ATOM 408 CB VAL A 68 19.548 23.267 29.155 1.00 8.24 C ATOM 409 CG1 VAL A 68 20.958 23.620 29.604 1.00 9.99 C ATOM 410 CG2 VAL A 68 19.511 21.755 28.813 1.00 7.36 C ATOM 411 N GLY A 69 19.173 25.080 32.030 1.00 8.46 N ATOM 412 CA GLY A 69 19.249 26.371 32.712 1.00 8.26 C ATOM 413 C GLY A 69 20.026 27.406 31.927 1.00 8.22 C ATOM 414 O GLY A 69 21.062 27.092 31.311 1.00 8.30 O ATOM 415 N GLY A 70 19.535 28.642 31.970 1.00 7.44 N ATOM 416 CA GLY A 70 20.130 29.735 31.220 1.00 8.18 C ATOM 417 C GLY A 70 20.852 30.824 32.005 1.00 9.92 C ATOM 418 O GLY A 70 21.211 31.825 31.400 1.00 10.37 O ATOM 419 N LEU A 71 21.035 30.657 33.317 1.00 10.51 N ATOM 420 CA LEU A 71 21.858 31.639 34.048 1.00 10.87 C ATOM 421 C LEU A 71 23.225 31.707 33.367 1.00 12.74 C ATOM 422 O LEU A 71 23.762 30.694 32.934 1.00 11.26 O ATOM 423 CB LEU A 71 22.036 31.225 35.493 1.00 11.07 C ATOM 424 CG LEU A 71 20.874 31.686 36.364 1.00 13.00 C ATOM 425 CD1 LEU A 71 20.965 31.083 37.750 1.00 15.17 C ATOM 426 CD2 LEU A 71 20.885 33.231 36.406 1.00 14.89 C ATOM 427 N ASP A 72 23.797 32.906 33.268 1.00 12.21 N ATOM 428 CA ASP A 72 25.037 33.077 32.522 1.00 14.66 C ATOM 429 C ASP A 72 26.140 32.126 33.011 1.00 14.18 C ATOM 430 O ASP A 72 26.874 31.558 32.188 1.00 13.91 O ATOM 431 CB ASP A 72 25.464 34.555 32.577 1.00 16.04 C ATOM 432 CG ASP A 72 26.725 34.829 31.788 1.00 20.17 C ATOM 433 OD1 ASP A 72 26.739 34.604 30.561 1.00 22.80 O ATOM 434 OD2 ASP A 72 27.775 35.260 32.330 1.00 25.30 O ATOM 435 N LYS A 73 26.204 31.920 34.324 1.00 14.67 N ATOM 436 CA LYS A 73 27.249 31.082 34.946 1.00 15.69 C ATOM 437 C LYS A 73 27.256 29.652 34.400 1.00 15.32 C ATOM 438 O LYS A 73 28.314 29.001 34.366 1.00 15.53 O ATOM 439 CB LYS A 73 27.120 31.076 36.483 1.00 16.99 C ATOM 440 CG LYS A 73 25.822 30.430 36.949 1.00 21.26 C ATOM 441 CD LYS A 73 25.165 31.061 38.210 1.00 28.43 C ATOM 442 CE LYS A 73 25.508 30.306 39.481 1.00 30.63 C ATOM 443 NZ LYS A 73 24.997 30.948 40.722 1.00 32.77 N ATOM 444 N ILE A 74 26.096 29.162 33.958 1.00 13.24 N ATOM 445 CA ILE A 74 26.026 27.808 33.422 1.00 12.01 C ATOM 446 C ILE A 74 25.799 27.726 31.921 1.00 11.74 C ATOM 447 O ILE A 74 25.645 26.639 31.389 1.00 11.23 O ATOM 448 CB ILE A 74 24.984 26.936 34.185 1.00 11.71 C ATOM 449 CG1 ILE A 74 23.598 27.586 34.137 1.00 10.03 C ATOM 450 CG2 ILE A 74 25.433 26.739 35.600 1.00 13.19 C ATOM 451 CD1 ILE A 74 22.474 26.719 34.678 1.00 12.01 C ATOM 452 N ARG A 75 25.823 28.846 31.200 1.00 12.35 N ATOM 453 CA ARG A 75 25.663 28.732 29.758 1.00 11.91 C ATOM 454 C ARG A 75 26.769 27.929 29.077 1.00 13.04 C ATOM 455 O ARG A 75 26.532 27.336 28.044 1.00 11.58 O ATOM 456 CB ARG A 75 25.503 30.096 29.074 1.00 13.32 C ATOM 457 CG ARG A 75 24.260 30.772 29.498 1.00 12.72 C ATOM 458 CD ARG A 75 24.051 32.146 28.811 1.00 13.47 C ATOM 459 NE ARG A 75 23.089 32.867 29.601 1.00 14.06 N ATOM 460 CZ ARG A 75 22.952 34.179 29.629 1.00 12.50 C ATOM 461 NH1 ARG A 75 23.687 34.950 28.823 1.00 11.32 N ATOM 462 NH2 ARG A 75 22.053 34.705 30.444 1.00 11.95 N ATOM 463 N PRO A 76 27.990 27.920 29.610 1.00 12.27 N ATOM 464 CA PRO A 76 29.022 27.077 28.997 1.00 13.54 C ATOM 465 C PRO A 76 28.606 25.614 28.961 1.00 13.33 C ATOM 466 O PRO A 76 29.135 24.859 28.164 1.00 15.25 O ATOM 467 CB PRO A 76 30.244 27.304 29.890 1.00 13.74 C ATOM 468 CG PRO A 76 30.012 28.730 30.424 1.00 15.10 C ATOM 469 CD PRO A 76 28.532 28.752 30.709 1.00 13.44 C ATOM 470 N LEU A 77 27.653 25.212 29.784 1.00 11.58 N ATOM 471 CA LEU A 77 27.239 23.802 29.768 1.00 11.05 C ATOM 472 C LEU A 77 26.296 23.469 28.617 1.00 10.28 C ATOM 473 O LEU A 77 26.024 22.293 28.363 1.00 10.61 O ATOM 474 CB LEU A 77 26.549 23.446 31.093 1.00 11.18 C ATOM 475 CG LEU A 77 27.374 23.712 32.344 1.00 9.68 C ATOM 476 CD1 LEU A 77 26.571 23.239 33.580 1.00 11.04 C ATOM 477 CD2 LEU A 77 28.715 22.971 32.191 1.00 11.72 C ATOM 478 N TRP A 78 25.759 24.478 27.927 1.00 10.66 N ATOM 479 CA TRP A 78 24.788 24.160 26.887 1.00 9.22 C ATOM 480 C TRP A 78 25.380 23.172 25.876 1.00 9.33 C ATOM 481 O TRP A 78 24.683 22.283 25.353 1.00 8.95 O ATOM 482 CB TRP A 78 24.389 25.446 26.138 1.00 8.17 C ATOM 483 CG TRP A 78 23.465 26.337 26.928 1.00 8.82 C ATOM 484 CD1 TRP A 78 23.043 26.159 28.239 1.00 8.53 C ATOM 485 CD2 TRP A 78 22.837 27.523 26.463 1.00 11.55 C ATOM 486 NE1 TRP A 78 22.195 27.182 28.590 1.00 9.88 N ATOM 487 CE2 TRP A 78 22.056 28.034 27.517 1.00 11.12 C ATOM 488 CE3 TRP A 78 22.844 28.206 25.246 1.00 12.96 C ATOM 489 CZ2 TRP A 78 21.297 29.203 27.393 1.00 12.17 C ATOM 490 CZ3 TRP A 78 22.101 29.390 25.126 1.00 13.44 C ATOM 491 CH2 TRP A 78 21.340 29.866 26.185 1.00 11.03 C ATOM 492 N ARG A 79 26.670 23.337 25.604 1.00 9.27 N ATOM 493 CA ARG A 79 27.337 22.496 24.606 1.00 10.70 C ATOM 494 C ARG A 79 27.291 21.001 24.883 1.00 10.59 C ATOM 495 O ARG A 79 27.346 20.201 23.936 1.00 11.15 O ATOM 496 CB ARG A 79 28.791 22.927 24.403 1.00 11.29 C ATOM 497 CG ARG A 79 29.740 22.540 25.518 1.00 16.33 C ATOM 498 CD ARG A 79 31.175 23.024 25.256 1.00 20.84 C ATOM 499 NE ARG A 79 32.167 22.387 26.113 1.00 26.07 N ATOM 500 CZ ARG A 79 32.386 22.721 27.371 1.00 25.33 C ATOM 501 NH1 ARG A 79 31.681 23.695 27.938 1.00 27.24 N ATOM 502 NH2 ARG A 79 33.313 22.083 28.077 1.00 27.45 N ATOM 503 N HIS A 80 27.157 20.614 26.151 1.00 9.49 N ATOM 504 CA HIS A 80 27.089 19.198 26.486 1.00 10.24 C ATOM 505 C HIS A 80 25.774 18.570 26.071 1.00 10.01 C ATOM 506 O HIS A 80 25.650 17.342 26.067 1.00 10.35 O ATOM 507 CB HIS A 80 27.235 18.988 27.988 1.00 10.56 C ATOM 508 CG HIS A 80 28.543 19.447 28.521 1.00 11.65 C ATOM 509 ND1 HIS A 80 29.744 19.084 27.943 1.00 15.12 N ATOM 510 CD2 HIS A 80 28.847 20.225 29.584 1.00 12.77 C ATOM 511 CE1 HIS A 80 30.733 19.634 28.627 1.00 15.01 C ATOM 512 NE2 HIS A 80 30.214 20.329 29.628 1.00 14.75 N ATOM 513 N TYR A 81 24.794 19.408 25.708 1.00 9.27 N ATOM 514 CA TYR A 81 23.488 18.894 25.308 1.00 8.58 C ATOM 515 C TYR A 81 23.231 18.905 23.814 1.00 8.74 C ATOM 516 O TYR A 81 22.169 18.440 23.341 1.00 8.67 O ATOM 517 CB TYR A 81 22.369 19.709 25.966 1.00 9.68 C ATOM 518 CG TYR A 81 22.419 19.811 27.470 1.00 8.06 C ATOM 519 CD1 TYR A 81 23.158 20.800 28.106 1.00 8.33 C ATOM 520 CD2 TYR A 81 21.681 18.936 28.266 1.00 8.14 C ATOM 521 CE1 TYR A 81 23.198 20.912 29.508 1.00 8.98 C ATOM 522 CE2 TYR A 81 21.691 19.057 29.685 1.00 8.93 C ATOM 523 CZ TYR A 81 22.454 20.038 30.294 1.00 7.59 C ATOM 524 OH TYR A 81 22.474 20.212 31.669 1.00 10.12 O ATOM 525 N PHE A 82 24.176 19.453 23.051 1.00 8.75 N ATOM 526 CA PHE A 82 23.946 19.552 21.597 1.00 9.18 C ATOM 527 C PHE A 82 23.878 18.222 20.867 1.00 8.94 C ATOM 528 O PHE A 82 23.074 18.049 19.963 1.00 8.96 O ATOM 529 CB PHE A 82 25.050 20.382 20.922 1.00 9.29 C ATOM 530 CG PHE A 82 25.121 21.817 21.380 1.00 10.29 C ATOM 531 CD1 PHE A 82 26.252 22.585 21.085 1.00 14.15 C ATOM 532 CD2 PHE A 82 24.106 22.404 22.095 1.00 10.21 C ATOM 533 CE1 PHE A 82 26.338 23.928 21.504 1.00 13.79 C ATOM 534 CE2 PHE A 82 24.173 23.748 22.484 1.00 10.23 C ATOM 535 CZ PHE A 82 25.293 24.497 22.215 1.00 12.45 C ATOM 536 N GLN A 83 24.689 17.260 21.284 1.00 9.53 N ATOM 537 CA GLN A 83 24.769 15.987 20.555 1.00 10.32 C ATOM 538 C GLN A 83 23.403 15.325 20.373 1.00 10.41 C ATOM 539 O GLN A 83 22.683 15.135 21.333 1.00 10.48 O ATOM 540 CB GLN A 83 25.716 15.058 21.319 1.00 10.19 C ATOM 541 CG GLN A 83 25.907 13.671 20.657 1.00 12.03 C ATOM 542 CD GLN A 83 27.105 12.951 21.236 1.00 14.33 C ATOM 543 OE1 GLN A 83 26.976 12.107 22.119 1.00 18.93 O ATOM 544 NE2 GLN A 83 28.265 13.313 20.754 1.00 16.26 N ATOM 545 N ASN A 84 23.074 14.993 19.127 1.00 10.33 N ATOM 546 CA ASN A 84 21.841 14.265 18.758 1.00 10.88 C ATOM 547 C ASN A 84 20.586 15.137 18.793 1.00 10.87 C ATOM 548 O ASN A 84 19.491 14.635 18.543 1.00 11.36 O ATOM 549 CB ASN A 84 21.633 12.980 19.567 1.00 11.68 C ATOM 550 CG ASN A 84 22.765 12.011 19.397 1.00 13.85 C ATOM 551 OD1 ASN A 84 23.302 11.851 18.302 1.00 16.24 O ATOM 552 ND2 ASN A 84 23.144 11.363 20.483 1.00 16.18 N ATOM 553 N THR A 85 20.732 16.408 19.104 1.00 10.36 N ATOM 554 CA THR A 85 19.575 17.276 19.084 1.00 9.78 C ATOM 555 C THR A 85 18.964 17.417 17.671 1.00 10.50 C ATOM 556 O THR A 85 19.658 17.703 16.676 1.00 10.94 O ATOM 557 CB THR A 85 19.954 18.640 19.700 1.00 10.29 C ATOM 558 OG1 THR A 85 20.286 18.398 21.073 1.00 13.89 O ATOM 559 CG2 THR A 85 18.759 19.559 19.752 1.00 11.11 C ATOM 560 N GLN A 86 17.652 17.215 17.598 1.00 9.12 N ATOM 561 CA GLN A 86 16.913 17.282 16.339 1.00 9.17 C ATOM 562 C GLN A 86 16.162 18.596 16.194 1.00 9.96 C ATOM 563 O GLN A 86 15.955 19.094 15.059 1.00 10.20 O ATOM 564 CB GLN A 86 15.953 16.110 16.260 1.00 9.10 C ATOM 565 CG GLN A 86 16.719 14.801 16.168 1.00 10.25 C ATOM 566 CD GLN A 86 15.813 13.627 16.279 1.00 11.18 C ATOM 567 OE1 GLN A 86 15.442 13.246 17.377 1.00 10.57 O ATOM 568 NE2 GLN A 86 15.447 13.028 15.119 1.00 12.29 N ATOM 569 N GLY A 87 15.713 19.145 17.322 1.00 8.70 N ATOM 570 CA GLY A 87 15.009 20.433 17.297 1.00 8.20 C ATOM 571 C GLY A 87 15.471 21.286 18.469 1.00 8.30 C ATOM 572 O GLY A 87 15.697 20.775 19.568 1.00 8.44 O ATOM 573 N LEU A 88 15.653 22.572 18.216 1.00 8.15 N ATOM 574 CA LEU A 88 16.034 23.535 19.247 1.00 8.98 C ATOM 575 C LEU A 88 14.817 24.391 19.507 1.00 9.38 C ATOM 576 O LEU A 88 14.179 24.847 18.556 1.00 11.14 O ATOM 577 CB LEU A 88 17.165 24.452 18.742 1.00 9.94 C ATOM 578 CG LEU A 88 18.533 23.790 18.534 1.00 12.94 C ATOM 579 CD1 LEU A 88 19.396 24.769 17.740 1.00 16.06 C ATOM 580 CD2 LEU A 88 19.171 23.518 19.871 1.00 16.29 C ATOM 581 N ILE A 89 14.467 24.612 20.775 1.00 8.37 N ATOM 582 CA ILE A 89 13.434 25.589 21.082 1.00 7.74 C ATOM 583 C ILE A 89 14.178 26.694 21.801 1.00 7.92 C ATOM 584 O ILE A 89 14.757 26.457 22.858 1.00 9.03 O ATOM 585 CB ILE A 89 12.345 25.027 21.961 1.00 7.97 C ATOM 586 CG1 ILE A 89 11.533 23.976 21.190 1.00 8.04 C ATOM 587 CG2 ILE A 89 11.393 26.163 22.414 1.00 8.92 C ATOM 588 CD1 ILE A 89 10.408 23.314 21.995 1.00 7.90 C ATOM 589 N PHE A 90 14.230 27.872 21.201 1.00 7.03 N ATOM 590 CA PHE A 90 14.924 28.973 21.852 1.00 7.28 C ATOM 591 C PHE A 90 13.840 29.891 22.389 1.00 6.99 C ATOM 592 O PHE A 90 13.073 30.485 21.615 1.00 7.80 O ATOM 593 CB PHE A 90 15.852 29.687 20.860 1.00 7.49 C ATOM 594 CG PHE A 90 16.752 30.694 21.511 1.00 8.78 C ATOM 595 CD1 PHE A 90 17.912 30.279 22.155 1.00 8.00 C ATOM 596 CD2 PHE A 90 16.447 32.041 21.488 1.00 11.01 C ATOM 597 CE1 PHE A 90 18.766 31.204 22.792 1.00 10.75 C ATOM 598 CE2 PHE A 90 17.301 32.966 22.105 1.00 11.86 C ATOM 599 CZ PHE A 90 18.462 32.530 22.757 1.00 9.91 C ATOM 600 N VAL A 91 13.752 29.990 23.711 1.00 6.37 N ATOM 601 CA VAL A 91 12.693 30.763 24.364 1.00 7.17 C ATOM 602 C VAL A 91 13.181 32.140 24.723 1.00 7.36 C ATOM 603 O VAL A 91 14.250 32.263 25.362 1.00 7.65 O ATOM 604 CB VAL A 91 12.197 30.030 25.637 1.00 6.78 C ATOM 605 CG1 VAL A 91 11.016 30.797 26.256 1.00 6.38 C ATOM 606 CG2 VAL A 91 11.739 28.609 25.314 1.00 6.83 C ATOM 607 N VAL A 92 12.434 33.163 24.309 1.00 8.26 N ATOM 608 CA VAL A 92 12.759 34.555 24.590 1.00 8.72 C ATOM 609 C VAL A 92 11.687 35.254 25.430 1.00 8.90 C ATOM 610 O VAL A 92 10.495 35.120 25.150 1.00 9.45 O ATOM 611 CB VAL A 92 12.921 35.341 23.249 1.00 9.94 C ATOM 612 CG1 VAL A 92 13.231 36.793 23.494 1.00 10.70 C ATOM 613 CG2 VAL A 92 14.053 34.727 22.435 1.00 11.69 C ATOM 614 N ASP A 93 12.124 36.000 26.439 1.00 8.72 N ATOM 615 CA ASP A 93 11.206 36.852 27.184 1.00 9.59 C ATOM 616 C ASP A 93 10.907 38.053 26.295 1.00 9.63 C ATOM 617 O ASP A 93 11.765 38.948 26.138 1.00 9.86 O ATOM 618 CB ASP A 93 11.818 37.280 28.512 1.00 9.29 C ATOM 619 CG ASP A 93 10.883 38.139 29.302 1.00 10.63 C ATOM 620 OD1 ASP A 93 11.134 38.304 30.514 1.00 12.68 O ATOM 621 OD2 ASP A 93 9.911 38.711 28.764 1.00 11.34 O ATOM 622 N SER A 94 9.700 38.075 25.722 1.00 10.77 N ATOM 623 CA SER A 94 9.326 39.128 24.769 1.00 11.39 C ATOM 624 C SER A 94 9.266 40.510 25.420 1.00 12.78 C ATOM 625 O SER A 94 9.307 41.530 24.699 1.00 12.59 O ATOM 626 CB SER A 94 8.011 38.809 24.059 1.00 11.96 C ATOM 627 OG SER A 94 8.095 37.588 23.363 1.00 10.88 O ATOM 628 N ASN A 95 9.219 40.549 26.755 1.00 13.71 N ATOM 629 CA ASN A 95 9.105 41.816 27.495 1.00 15.68 C ATOM 630 C ASN A 95 10.465 42.356 27.913 1.00 16.63 C ATOM 631 O ASN A 95 10.575 43.474 28.437 1.00 17.83 O ATOM 632 CB ASN A 95 8.251 41.585 28.751 1.00 16.09 C ATOM 633 CG ASN A 95 8.035 42.858 29.578 1.00 18.55 C ATOM 634 OD1 ASN A 95 8.415 42.925 30.757 1.00 22.35 O ATOM 635 ND2 ASN A 95 7.413 43.845 28.979 1.00 19.72 N ATOM 636 N ASP A 96 11.508 41.558 27.699 1.00 15.88 N ATOM 637 CA ASP A 96 12.835 41.931 28.155 1.00 15.68 C ATOM 638 C ASP A 96 13.627 42.606 27.034 1.00 16.07 C ATOM 639 O ASP A 96 14.472 42.005 26.367 1.00 14.97 O ATOM 640 CB ASP A 96 13.550 40.713 28.770 1.00 16.14 C ATOM 641 CG ASP A 96 14.781 41.090 29.562 1.00 16.40 C ATOM 642 OD1 ASP A 96 15.334 40.218 30.289 1.00 18.20 O ATOM 643 OD2 ASP A 96 15.298 42.227 29.490 1.00 18.83 O ATOM 644 N ARG A 97 13.343 43.880 26.823 1.00 16.26 N ATOM 645 CA ARG A 97 14.029 44.619 25.774 1.00 16.52 C ATOM 646 C ARG A 97 15.508 44.810 26.085 1.00 16.74 C ATOM 647 O ARG A 97 16.343 44.839 25.173 1.00 17.70 O ATOM 648 CB ARG A 97 13.331 45.954 25.531 1.00 16.74 C ATOM 649 CG ARG A 97 11.883 45.758 25.087 1.00 19.20 C ATOM 650 CD ARG A 97 10.999 46.954 25.422 1.00 22.98 C ATOM 651 NE ARG A 97 9.602 46.716 25.094 1.00 26.56 N ATOM 652 CZ ARG A 97 9.141 46.730 23.860 1.00 24.86 C ATOM 653 NH1 ARG A 97 9.973 46.961 22.869 1.00 28.38 N ATOM 654 NH2 ARG A 97 7.859 46.516 23.605 1.00 21.67 N ATOM 655 N GLU A 98 15.838 44.912 27.363 1.00 16.13 N ATOM 656 CA GLU A 98 17.218 45.120 27.769 1.00 16.97 C ATOM 657 C GLU A 98 18.127 43.947 27.415 1.00 16.08 C ATOM 658 O GLU A 98 19.332 44.125 27.191 1.00 15.50 O ATOM 659 CB GLU A 98 17.277 45.451 29.249 1.00 17.98 C ATOM 660 CG GLU A 98 16.631 46.807 29.511 1.00 23.91 C ATOM 661 CD GLU A 98 16.556 47.163 30.981 1.00 32.19 C ATOM 662 OE1 GLU A 98 16.051 48.266 31.300 1.00 36.44 O ATOM 663 OE2 GLU A 98 17.000 46.345 31.816 1.00 37.70 O ATOM 664 N ARG A 99 17.547 42.750 27.320 1.00 14.58 N ATOM 665 CA ARG A 99 18.384 41.572 27.076 1.00 13.54 C ATOM 666 C ARG A 99 18.124 40.856 25.753 1.00 12.93 C ATOM 667 O ARG A 99 18.626 39.748 25.536 1.00 12.11 O ATOM 668 CB ARG A 99 18.234 40.584 28.236 1.00 13.50 C ATOM 669 CG ARG A 99 18.867 41.124 29.534 1.00 14.00 C ATOM 670 CD ARG A 99 19.325 39.984 30.474 1.00 16.13 C ATOM 671 NE ARG A 99 18.157 39.260 30.928 1.00 14.70 N ATOM 672 CZ ARG A 99 18.185 38.050 31.510 1.00 14.57 C ATOM 673 NH1 ARG A 99 19.331 37.400 31.676 1.00 12.93 N ATOM 674 NH2 ARG A 99 17.042 37.478 31.887 1.00 13.44 N ATOM 675 N VAL A 100 17.388 41.499 24.845 1.00 11.78 N ATOM 676 CA VAL A 100 17.045 40.831 23.603 1.00 11.94 C ATOM 677 C VAL A 100 18.299 40.618 22.755 1.00 10.98 C ATOM 678 O VAL A 100 18.442 39.586 22.095 1.00 11.41 O ATOM 679 CB VAL A 100 15.900 41.547 22.849 1.00 11.73 C ATOM 680 CG1 VAL A 100 16.356 42.836 22.197 1.00 13.14 C ATOM 681 CG2 VAL A 100 15.228 40.576 21.872 1.00 14.32 C ATOM 682 N ASN A 101 19.237 41.558 22.823 1.00 10.92 N ATOM 683 CA ASN A 101 20.450 41.393 22.026 1.00 10.29 C ATOM 684 C ASN A 101 21.337 40.327 22.608 1.00 11.23 C ATOM 685 O ASN A 101 22.020 39.603 21.863 1.00 11.45 O ATOM 686 CB ASN A 101 21.252 42.700 21.895 1.00 10.74 C ATOM 687 CG ASN A 101 22.357 42.563 20.911 1.00 12.99 C ATOM 688 OD1 ASN A 101 22.125 42.214 19.753 1.00 12.75 O ATOM 689 ND2 ASN A 101 23.577 42.829 21.352 1.00 13.29 N ATOM 690 N GLU A 102 21.351 40.247 23.939 1.00 10.71 N ATOM 691 CA GLU A 102 22.092 39.195 24.637 1.00 10.54 C ATOM 692 C GLU A 102 21.533 37.831 24.225 1.00 10.01 C ATOM 693 O GLU A 102 22.292 36.880 23.999 1.00 10.60 O ATOM 694 CB GLU A 102 21.992 39.410 26.145 1.00 11.11 C ATOM 695 CG GLU A 102 22.655 38.311 26.967 1.00 11.77 C ATOM 696 CD GLU A 102 22.677 38.607 28.444 1.00 19.70 C ATOM 697 OE1 GLU A 102 23.243 37.755 29.181 1.00 22.11 O ATOM 698 OE2 GLU A 102 22.127 39.664 28.875 1.00 18.24 O ATOM 699 N ALA A 103 20.214 37.747 24.080 1.00 9.68 N ATOM 700 CA ALA A 103 19.595 36.499 23.615 1.00 9.84 C ATOM 701 C ALA A 103 20.095 36.184 22.204 1.00 10.22 C ATOM 702 O ALA A 103 20.481 35.034 21.903 1.00 10.25 O ATOM 703 CB ALA A 103 18.067 36.599 23.656 1.00 10.58 C ATOM 704 N ARG A 104 20.113 37.205 21.337 1.00 9.50 N ATOM 705 CA ARG A 104 20.620 37.007 19.985 1.00 9.48 C ATOM 706 C ARG A 104 22.054 36.501 20.004 1.00 10.41 C ATOM 707 O ARG A 104 22.399 35.563 19.299 1.00 9.67 O ATOM 708 CB ARG A 104 20.572 38.305 19.179 1.00 9.48 C ATOM 709 CG ARG A 104 20.983 38.084 17.714 1.00 10.96 C ATOM 710 CD ARG A 104 21.054 39.402 16.881 1.00 14.17 C ATOM 711 NE ARG A 104 21.381 39.134 15.474 1.00 22.07 N ATOM 712 CZ ARG A 104 22.583 39.324 14.936 1.00 23.31 C ATOM 713 NH1 ARG A 104 23.575 39.771 15.691 1.00 25.90 N ATOM 714 NH2 ARG A 104 22.801 39.049 13.651 1.00 25.01 N ATOM 715 N GLU A 105 22.898 37.124 20.824 1.00 10.78 N ATOM 716 CA GLU A 105 24.279 36.683 20.889 1.00 11.43 C ATOM 717 C GLU A 105 24.392 35.211 21.283 1.00 11.07 C ATOM 718 O GLU A 105 25.151 34.471 20.686 1.00 11.10 O ATOM 719 CB GLU A 105 25.096 37.556 21.844 1.00 12.52 C ATOM 720 CG GLU A 105 25.307 38.972 21.315 1.00 17.09 C ATOM 721 CD GLU A 105 26.286 39.016 20.155 1.00 21.39 C ATOM 722 OE1 GLU A 105 25.843 39.099 18.989 1.00 21.37 O ATOM 723 OE2 GLU A 105 27.504 38.934 20.414 1.00 25.78 O ATOM 724 N GLU A 106 23.616 34.785 22.271 1.00 10.28 N ATOM 725 CA GLU A 106 23.668 33.384 22.670 1.00 9.50 C ATOM 726 C GLU A 106 23.112 32.463 21.590 1.00 9.38 C ATOM 727 O GLU A 106 23.681 31.405 21.304 1.00 9.77 O ATOM 728 CB GLU A 106 22.897 33.161 23.970 1.00 9.32 C ATOM 729 CG GLU A 106 23.456 33.946 25.155 1.00 11.09 C ATOM 730 CD GLU A 106 24.779 33.435 25.665 1.00 12.64 C ATOM 731 OE1 GLU A 106 25.362 34.136 26.553 1.00 14.35 O ATOM 732 OE2 GLU A 106 25.241 32.363 25.203 1.00 14.20 O ATOM 733 N LEU A 107 22.030 32.891 20.948 1.00 9.35 N ATOM 734 CA LEU A 107 21.449 32.087 19.885 1.00 9.49 C ATOM 735 C LEU A 107 22.424 31.876 18.724 1.00 10.73 C ATOM 736 O LEU A 107 22.585 30.762 18.250 1.00 10.58 O ATOM 737 CB LEU A 107 20.152 32.729 19.359 1.00 9.83 C ATOM 738 CG LEU A 107 19.489 31.982 18.192 1.00 10.05 C ATOM 739 CD1 LEU A 107 19.131 30.489 18.510 1.00 8.38 C ATOM 740 CD2 LEU A 107 18.278 32.793 17.713 1.00 11.27 C ATOM 741 N MET A 108 23.086 32.929 18.274 1.00 11.68 N ATOM 742 CA MET A 108 24.002 32.814 17.141 1.00 12.84 C ATOM 743 C MET A 108 25.264 32.017 17.479 1.00 13.77 C ATOM 744 O MET A 108 25.783 31.278 16.628 1.00 15.04 O ATOM 745 CB MET A 108 24.347 34.199 16.579 1.00 12.96 C ATOM 746 CG MET A 108 23.141 34.969 16.079 1.00 15.24 C ATOM 747 SD MET A 108 22.157 34.076 14.858 1.00 19.52 S ATOM 748 CE MET A 108 23.367 33.967 13.542 1.00 23.61 C ATOM 749 N ARG A 109 25.722 32.129 18.728 1.00 14.85 N ATOM 750 CA ARG A 109 26.895 31.398 19.216 1.00 16.49 C ATOM 751 C ARG A 109 26.612 29.904 19.218 1.00 16.04 C ATOM 752 O ARG A 109 27.474 29.070 18.891 1.00 16.55 O ATOM 753 CB ARG A 109 27.224 31.857 20.632 1.00 17.69 C ATOM 754 CG ARG A 109 28.425 31.192 21.249 1.00 23.58 C ATOM 755 CD ARG A 109 28.611 31.550 22.701 1.00 30.67 C ATOM 756 NE ARG A 109 28.612 32.994 22.905 1.00 34.87 N ATOM 757 CZ ARG A 109 28.438 33.564 24.091 1.00 39.00 C ATOM 758 NH1 ARG A 109 28.452 34.885 24.204 1.00 40.33 N ATOM 759 NH2 ARG A 109 28.260 32.802 25.170 1.00 40.77 N ATOM 760 N MET A 110 25.401 29.550 19.627 1.00 14.37 N ATOM 761 CA MET A 110 24.977 28.151 19.607 1.00 13.89 C ATOM 762 C MET A 110 24.795 27.637 18.175 1.00 13.50 C ATOM 763 O MET A 110 25.179 26.494 17.881 1.00 14.51 O ATOM 764 CB MET A 110 23.678 27.978 20.425 1.00 13.55 C ATOM 765 CG MET A 110 23.041 26.650 20.252 1.00 15.50 C ATOM 766 SD MET A 110 21.593 26.432 21.354 1.00 17.11 S ATOM 767 CE MET A 110 20.461 27.403 20.463 1.00 16.24 C ATOM 768 N LEU A 111 24.206 28.435 17.287 1.00 12.55 N ATOM 769 CA LEU A 111 23.983 27.997 15.930 1.00 12.47 C ATOM 770 C LEU A 111 25.271 27.800 15.122 1.00 13.70 C ATOM 771 O LEU A 111 25.242 27.172 14.076 1.00 14.76 O ATOM 772 CB LEU A 111 23.024 28.919 15.211 1.00 12.01 C ATOM 773 CG LEU A 111 21.618 28.959 15.836 1.00 12.25 C ATOM 774 CD1 LEU A 111 20.755 29.898 15.031 1.00 10.67 C ATOM 775 CD2 LEU A 111 20.994 27.563 15.885 1.00 14.09 C ATOM 776 N ALA A 112 26.378 28.352 15.604 1.00 13.76 N ATOM 777 CA ALA A 112 27.650 28.201 14.884 1.00 14.78 C ATOM 778 C ALA A 112 28.192 26.793 15.054 1.00 15.31 C ATOM 779 O ALA A 112 29.092 26.364 14.310 1.00 15.48 O ATOM 780 CB ALA A 112 28.669 29.226 15.379 1.00 15.57 C ATOM 781 N GLU A 113 27.616 26.036 15.985 1.00 14.91 N ATOM 782 CA GLU A 113 28.160 24.715 16.317 1.00 15.24 C ATOM 783 C GLU A 113 27.824 23.607 15.339 1.00 15.29 C ATOM 784 O GLU A 113 26.666 23.390 14.991 1.00 15.50 O ATOM 785 CB GLU A 113 27.640 24.313 17.696 1.00 15.40 C ATOM 786 CG GLU A 113 28.145 25.196 18.815 1.00 18.45 C ATOM 787 CD GLU A 113 29.622 25.009 19.027 1.00 25.71 C ATOM 788 OE1 GLU A 113 30.091 23.851 18.951 1.00 25.67 O ATOM 789 OE2 GLU A 113 30.304 26.028 19.235 1.00 29.49 O ATOM 790 N ASP A 114 28.844 22.849 14.924 1.00 15.18 N ATOM 791 CA ASP A 114 28.615 21.784 13.950 1.00 16.04 C ATOM 792 C ASP A 114 27.632 20.730 14.412 1.00 14.67 C ATOM 793 O ASP A 114 26.875 20.177 13.599 1.00 14.28 O ATOM 794 CB ASP A 114 29.928 21.085 13.604 1.00 16.10 C ATOM 795 CG ASP A 114 30.923 22.012 12.959 1.00 21.47 C ATOM 796 OD1 ASP A 114 30.499 22.906 12.212 1.00 24.59 O ATOM 797 OD2 ASP A 114 32.156 21.904 13.142 1.00 28.59 O ATOM 798 N GLU A 115 27.630 20.457 15.711 1.00 14.89 N ATOM 799 CA GLU A 115 26.751 19.431 16.223 1.00 15.16 C ATOM 800 C GLU A 115 25.284 19.751 16.030 1.00 14.79 C ATOM 801 O GLU A 115 24.447 18.862 16.104 1.00 16.02 O ATOM 802 CB GLU A 115 27.021 19.178 17.697 1.00 15.84 C ATOM 803 CG GLU A 115 28.287 18.398 17.961 1.00 18.09 C ATOM 804 CD GLU A 115 28.580 18.336 19.434 1.00 22.54 C ATOM 805 OE1 GLU A 115 28.247 17.312 20.051 1.00 24.94 O ATOM 806 OE2 GLU A 115 29.120 19.330 19.962 1.00 25.91 O ATOM 807 N LEU A 116 24.966 21.023 15.805 1.00 14.13 N ATOM 808 CA LEU A 116 23.582 21.416 15.611 1.00 13.12 C ATOM 809 C LEU A 116 23.267 21.724 14.160 1.00 13.49 C ATOM 810 O LEU A 116 22.225 22.264 13.867 1.00 12.98 O ATOM 811 CB LEU A 116 23.247 22.655 16.457 1.00 11.98 C ATOM 812 CG LEU A 116 23.400 22.480 17.971 1.00 12.77 C ATOM 813 CD1 LEU A 116 23.158 23.826 18.689 1.00 9.95 C ATOM 814 CD2 LEU A 116 22.488 21.363 18.505 1.00 13.00 C ATOM 815 N ARG A 117 24.139 21.320 13.239 1.00 15.05 N ATOM 816 CA ARG A 117 23.967 21.720 11.853 1.00 16.11 C ATOM 817 C ARG A 117 22.625 21.321 11.253 1.00 15.67 C ATOM 818 O ARG A 117 22.030 22.077 10.492 1.00 15.56 O ATOM 819 CB ARG A 117 25.143 21.214 10.999 1.00 17.80 C ATOM 820 CG ARG A 117 25.325 19.739 11.007 1.00 23.27 C ATOM 821 CD ARG A 117 26.498 19.287 10.128 1.00 31.72 C ATOM 822 NE ARG A 117 26.291 19.658 8.731 1.00 36.01 N ATOM 823 CZ ARG A 117 25.553 18.959 7.875 1.00 41.39 C ATOM 824 NH1 ARG A 117 24.943 17.847 8.267 1.00 43.33 N ATOM 825 NH2 ARG A 117 25.419 19.368 6.614 1.00 44.13 N ATOM 826 N ASP A 118 22.127 20.160 11.658 1.00 14.85 N ATOM 827 CA ASP A 118 20.903 19.627 11.077 1.00 15.39 C ATOM 828 C ASP A 118 19.679 19.816 11.964 1.00 14.33 C ATOM 829 O ASP A 118 18.589 19.334 11.616 1.00 15.57 O ATOM 830 CB ASP A 118 21.084 18.154 10.783 1.00 15.84 C ATOM 831 CG ASP A 118 22.091 17.920 9.681 1.00 19.90 C ATOM 832 OD1 ASP A 118 22.782 16.885 9.733 1.00 25.02 O ATOM 833 OD2 ASP A 118 22.255 18.732 8.758 1.00 22.05 O ATOM 834 N ALA A 119 19.854 20.513 13.088 1.00 11.94 N ATOM 835 CA ALA A 119 18.732 20.768 13.991 1.00 10.76 C ATOM 836 C ALA A 119 17.820 21.853 13.420 1.00 11.11 C ATOM 837 O ALA A 119 18.301 22.859 12.837 1.00 11.71 O ATOM 838 CB ALA A 119 19.236 21.233 15.366 1.00 10.68 C ATOM 839 N VAL A 120 16.519 21.691 13.599 1.00 9.86 N ATOM 840 CA VAL A 120 15.611 22.718 13.166 1.00 10.05 C ATOM 841 C VAL A 120 15.439 23.662 14.349 1.00 9.72 C ATOM 842 O VAL A 120 15.686 23.274 15.481 1.00 10.73 O ATOM 843 CB VAL A 120 14.261 22.154 12.681 1.00 9.97 C ATOM 844 CG1 VAL A 120 14.464 21.243 11.504 1.00 10.28 C ATOM 845 CG2 VAL A 120 13.477 21.438 13.799 1.00 10.75 C ATOM 846 N LEU A 121 15.021 24.893 14.081 1.00 9.61 N ATOM 847 CA LEU A 121 14.891 25.938 15.123 1.00 8.41 C ATOM 848 C LEU A 121 13.511 26.519 15.285 1.00 8.91 C ATOM 849 O LEU A 121 12.947 27.125 14.358 1.00 9.13 O ATOM 850 CB LEU A 121 15.871 27.095 14.808 1.00 8.27 C ATOM 851 CG LEU A 121 15.720 28.321 15.715 1.00 8.14 C ATOM 852 CD1 LEU A 121 16.124 27.993 17.171 1.00 10.07 C ATOM 853 CD2 LEU A 121 16.573 29.451 15.187 1.00 10.29 C ATOM 854 N LEU A 122 12.952 26.352 16.489 1.00 7.52 N ATOM 855 CA LEU A 122 11.664 26.945 16.836 1.00 8.09 C ATOM 856 C LEU A 122 11.926 27.993 17.890 1.00 8.80 C ATOM 857 O LEU A 122 12.453 27.682 18.959 1.00 9.22 O ATOM 858 CB LEU A 122 10.687 25.888 17.400 1.00 7.64 C ATOM 859 CG LEU A 122 9.372 26.449 17.956 1.00 8.09 C ATOM 860 CD1 LEU A 122 8.503 27.175 16.902 1.00 9.45 C ATOM 861 CD2 LEU A 122 8.654 25.193 18.532 1.00 9.89 C ATOM 862 N VAL A 123 11.584 29.239 17.582 1.00 8.14 N ATOM 863 CA VAL A 123 11.737 30.309 18.546 1.00 8.22 C ATOM 864 C VAL A 123 10.391 30.600 19.184 1.00 9.07 C ATOM 865 O VAL A 123 9.384 30.741 18.489 1.00 9.30 O ATOM 866 CB VAL A 123 12.295 31.625 17.892 1.00 7.74 C ATOM 867 CG1 VAL A 123 12.343 32.787 18.906 1.00 7.61 C ATOM 868 CG2 VAL A 123 13.664 31.343 17.283 1.00 9.23 C ATOM 869 N PHE A 124 10.356 30.625 20.510 1.00 8.98 N ATOM 870 CA PHE A 124 9.146 31.029 21.218 1.00 8.73 C ATOM 871 C PHE A 124 9.308 32.467 21.719 1.00 9.35 C ATOM 872 O PHE A 124 10.184 32.763 22.553 1.00 9.37 O ATOM 873 CB PHE A 124 8.846 30.108 22.408 1.00 8.96 C ATOM 874 CG PHE A 124 8.131 28.824 22.062 1.00 7.70 C ATOM 875 CD1 PHE A 124 8.203 27.750 22.940 1.00 8.31 C ATOM 876 CD2 PHE A 124 7.324 28.693 20.933 1.00 9.27 C ATOM 877 CE1 PHE A 124 7.527 26.583 22.729 1.00 9.23 C ATOM 878 CE2 PHE A 124 6.661 27.489 20.700 1.00 10.94 C ATOM 879 CZ PHE A 124 6.742 26.436 21.635 1.00 9.28 C ATOM 880 N ALA A 125 8.449 33.365 21.209 1.00 8.41 N ATOM 881 CA ALA A 125 8.420 34.750 21.656 1.00 9.47 C ATOM 882 C ALA A 125 7.432 34.712 22.804 1.00 9.85 C ATOM 883 O ALA A 125 6.235 34.919 22.620 1.00 9.61 O ATOM 884 CB ALA A 125 7.912 35.673 20.534 1.00 10.06 C ATOM 885 N ASN A 126 7.963 34.431 23.986 1.00 9.72 N ATOM 886 CA ASN A 126 7.157 34.140 25.178 1.00 9.61 C ATOM 887 C ASN A 126 6.749 35.361 25.994 1.00 10.56 C ATOM 888 O ASN A 126 7.292 36.446 25.807 1.00 10.63 O ATOM 889 CB ASN A 126 7.932 33.131 26.052 1.00 9.49 C ATOM 890 CG ASN A 126 7.058 32.471 27.098 1.00 11.67 C ATOM 891 OD1 ASN A 126 5.921 32.090 26.806 1.00 12.73 O ATOM 892 ND2 ASN A 126 7.597 32.303 28.335 1.00 11.01 N ATOM 893 N LYS A 127 5.825 35.143 26.924 1.00 9.88 N ATOM 894 CA LYS A 127 5.294 36.192 27.806 1.00 11.68 C ATOM 895 C LYS A 127 4.485 37.248 27.059 1.00 12.50 C ATOM 896 O LYS A 127 4.522 38.421 27.401 1.00 14.61 O ATOM 897 CB LYS A 127 6.363 36.852 28.689 1.00 11.19 C ATOM 898 CG LYS A 127 7.314 35.874 29.396 1.00 9.62 C ATOM 899 CD LYS A 127 8.006 36.539 30.571 1.00 8.46 C ATOM 900 CE LYS A 127 9.104 35.650 31.137 1.00 8.07 C ATOM 901 NZ LYS A 127 9.869 36.316 32.272 1.00 8.43 N ATOM 902 N GLN A 128 3.733 36.794 26.072 1.00 13.54 N ATOM 903 CA GLN A 128 2.904 37.691 25.254 1.00 14.73 C ATOM 904 C GLN A 128 1.778 38.332 26.067 1.00 16.36 C ATOM 905 O GLN A 128 1.171 39.321 25.628 1.00 17.64 O ATOM 906 CB GLN A 128 2.336 36.919 24.073 1.00 14.24 C ATOM 907 CG GLN A 128 3.357 36.680 22.949 1.00 14.97 C ATOM 908 CD GLN A 128 3.934 37.957 22.375 1.00 18.06 C ATOM 909 OE1 GLN A 128 3.206 38.919 22.105 1.00 18.55 O ATOM 910 NE2 GLN A 128 5.238 37.981 22.184 1.00 15.05 N ATOM 911 N ASP A 129 1.497 37.777 27.237 1.00 17.39 N ATOM 912 CA ASP A 129 0.487 38.366 28.120 1.00 18.68 C ATOM 913 C ASP A 129 0.875 39.724 28.687 1.00 19.85 C ATOM 914 O ASP A 129 -0.006 40.492 29.104 1.00 20.27 O ATOM 915 CB ASP A 129 0.198 37.432 29.278 1.00 18.47 C ATOM 916 CG ASP A 129 1.445 37.095 30.049 1.00 19.35 C ATOM 917 OD1 ASP A 129 1.550 37.520 31.222 1.00 19.79 O ATOM 918 OD2 ASP A 129 2.393 36.444 29.533 1.00 19.13 O ATOM 919 N LEU A 130 2.167 40.026 28.728 1.00 19.85 N ATOM 920 CA LEU A 130 2.661 41.251 29.343 1.00 20.67 C ATOM 921 C LEU A 130 2.344 42.462 28.475 1.00 22.64 C ATOM 922 O LEU A 130 2.498 42.399 27.264 1.00 22.37 O ATOM 923 CB LEU A 130 4.164 41.151 29.647 1.00 20.00 C ATOM 924 CG LEU A 130 4.456 40.165 30.778 1.00 20.32 C ATOM 925 CD1 LEU A 130 5.965 40.029 31.003 1.00 18.87 C ATOM 926 CD2 LEU A 130 3.764 40.674 32.057 1.00 19.46 C ATOM 927 N PRO A 131 1.886 43.541 29.109 1.00 24.15 N ATOM 928 CA PRO A 131 1.458 44.763 28.412 1.00 26.10 C ATOM 929 C PRO A 131 2.386 45.220 27.299 1.00 27.36 C ATOM 930 O PRO A 131 1.927 45.399 26.169 1.00 28.75 O ATOM 931 CB PRO A 131 1.411 45.813 29.533 1.00 25.98 C ATOM 932 CG PRO A 131 1.134 45.031 30.767 1.00 26.09 C ATOM 933 CD PRO A 131 1.708 43.645 30.570 1.00 24.60 C ATOM 934 N ASN A 132 3.658 45.430 27.605 1.00 28.27 N ATOM 935 CA ASN A 132 4.567 45.858 26.566 1.00 29.21 C ATOM 936 C ASN A 132 5.488 44.741 26.097 1.00 28.31 C ATOM 937 O ASN A 132 6.705 44.871 26.155 1.00 30.03 O ATOM 938 CB ASN A 132 5.371 47.098 26.968 1.00 30.58 C ATOM 939 CG ASN A 132 5.626 48.026 25.780 1.00 33.19 C ATOM 940 OD1 ASN A 132 6.273 49.068 25.907 1.00 36.63 O ATOM 941 ND2 ASN A 132 5.102 47.645 24.613 1.00 36.50 N ATOM 942 N ALA A 133 4.901 43.643 25.638 1.00 26.15 N ATOM 943 CA ALA A 133 5.702 42.566 25.073 1.00 23.54 C ATOM 944 C ALA A 133 5.895 42.854 23.603 1.00 22.41 C ATOM 945 O ALA A 133 4.973 43.301 22.907 1.00 22.36 O ATOM 946 CB ALA A 133 5.004 41.245 25.220 1.00 23.61 C ATOM 947 N MET A 134 7.099 42.594 23.125 1.00 20.26 N ATOM 948 CA MET A 134 7.371 42.719 21.710 1.00 18.84 C ATOM 949 C MET A 134 6.637 41.585 20.991 1.00 18.11 C ATOM 950 O MET A 134 6.485 40.469 21.530 1.00 17.05 O ATOM 951 CB MET A 134 8.871 42.611 21.459 1.00 18.56 C ATOM 952 CG MET A 134 9.685 43.739 22.039 1.00 17.43 C ATOM 953 SD MET A 134 11.469 43.568 21.823 1.00 18.90 S ATOM 954 CE MET A 134 11.869 42.390 23.053 1.00 17.39 C ATOM 955 N ASN A 135 6.141 41.857 19.786 1.00 17.67 N ATOM 956 CA ASN A 135 5.486 40.814 19.016 1.00 17.45 C ATOM 957 C ASN A 135 6.492 39.936 18.289 1.00 16.54 C ATOM 958 O ASN A 135 7.692 40.214 18.287 1.00 17.69 O ATOM 959 CB ASN A 135 4.493 41.366 18.001 1.00 19.17 C ATOM 960 CG ASN A 135 5.129 42.334 17.032 1.00 20.83 C ATOM 961 OD1 ASN A 135 6.177 42.078 16.441 1.00 21.08 O ATOM 962 ND2 ASN A 135 4.504 43.496 16.890 1.00 27.10 N ATOM 963 N ALA A 136 5.976 38.927 17.612 1.00 15.63 N ATOM 964 CA ALA A 136 6.829 37.912 16.977 1.00 14.92 C ATOM 965 C ALA A 136 7.644 38.522 15.863 1.00 15.41 C ATOM 966 O ALA A 136 8.807 38.163 15.669 1.00 13.56 O ATOM 967 CB ALA A 136 6.017 36.748 16.448 1.00 16.56 C ATOM 968 N ALA A 137 7.028 39.441 15.128 1.00 15.15 N ATOM 969 CA ALA A 137 7.768 40.078 14.035 1.00 15.42 C ATOM 970 C ALA A 137 8.917 40.917 14.559 1.00 15.00 C ATOM 971 O ALA A 137 9.995 40.927 13.971 1.00 14.74 O ATOM 972 CB ALA A 137 6.844 40.925 13.200 1.00 15.83 C ATOM 973 N GLU A 138 8.700 41.641 15.652 1.00 14.79 N ATOM 974 CA GLU A 138 9.782 42.435 16.217 1.00 14.37 C ATOM 975 C GLU A 138 10.919 41.558 16.741 1.00 13.63 C ATOM 976 O GLU A 138 12.085 41.857 16.554 1.00 13.39 O ATOM 977 CB GLU A 138 9.258 43.328 17.338 1.00 15.12 C ATOM 978 CG GLU A 138 10.348 44.100 18.062 1.00 17.44 C ATOM 979 CD GLU A 138 9.813 45.315 18.776 1.00 21.67 C ATOM 980 OE1 GLU A 138 8.621 45.304 19.162 1.00 21.47 O ATOM 981 OE2 GLU A 138 10.584 46.269 18.934 1.00 25.29 O ATOM 982 N ILE A 139 10.571 40.461 17.403 1.00 12.74 N ATOM 983 CA ILE A 139 11.591 39.547 17.903 1.00 11.93 C ATOM 984 C ILE A 139 12.359 38.947 16.720 1.00 11.80 C ATOM 985 O ILE A 139 13.586 38.774 16.789 1.00 10.86 O ATOM 986 CB ILE A 139 10.961 38.442 18.795 1.00 12.00 C ATOM 987 CG1 ILE A 139 10.370 39.055 20.069 1.00 14.23 C ATOM 988 CG2 ILE A 139 11.977 37.387 19.187 1.00 11.47 C ATOM 989 CD1 ILE A 139 11.396 39.604 20.986 1.00 17.18 C ATOM 990 N THR A 140 11.642 38.616 15.648 1.00 10.42 N ATOM 991 CA THR A 140 12.322 38.122 14.439 1.00 10.63 C ATOM 992 C THR A 140 13.387 39.112 13.976 1.00 10.54 C ATOM 993 O THR A 140 14.524 38.732 13.691 1.00 10.00 O ATOM 994 CB THR A 140 11.304 37.961 13.334 1.00 10.11 C ATOM 995 OG1 THR A 140 10.393 36.912 13.697 1.00 12.91 O ATOM 996 CG2 THR A 140 11.961 37.432 12.072 1.00 12.72 C ATOM 997 N ASP A 141 13.007 40.383 13.918 1.00 10.80 N ATOM 998 CA ASP A 141 13.918 41.428 13.467 1.00 11.01 C ATOM 999 C ASP A 141 15.094 41.575 14.432 1.00 11.40 C ATOM 1000 O ASP A 141 16.241 41.617 14.035 1.00 11.06 O ATOM 1001 CB ASP A 141 13.186 42.764 13.369 1.00 12.12 C ATOM 1002 CG ASP A 141 12.139 42.773 12.300 1.00 13.80 C ATOM 1003 OD1 ASP A 141 11.257 43.671 12.346 1.00 16.60 O ATOM 1004 OD2 ASP A 141 12.113 41.920 11.399 1.00 13.64 O ATOM 1005 N LYS A 142 14.796 41.643 15.723 1.00 11.13 N ATOM 1006 CA LYS A 142 15.835 41.876 16.710 1.00 11.21 C ATOM 1007 C LYS A 142 16.845 40.726 16.791 1.00 10.96 C ATOM 1008 O LYS A 142 18.032 40.946 17.024 1.00 11.53 O ATOM 1009 CB LYS A 142 15.187 42.182 18.088 1.00 12.58 C ATOM 1010 CG LYS A 142 14.360 43.531 18.213 1.00 18.12 C ATOM 1011 CD LYS A 142 15.189 44.618 18.801 1.00 25.42 C ATOM 1012 CE LYS A 142 14.360 45.823 19.306 1.00 26.53 C ATOM 1013 NZ LYS A 142 13.368 46.396 18.353 1.00 28.38 N ATOM 1014 N LEU A 143 16.360 39.489 16.625 1.00 10.02 N ATOM 1015 CA LEU A 143 17.239 38.332 16.649 1.00 9.23 C ATOM 1016 C LEU A 143 17.940 38.110 15.316 1.00 9.99 C ATOM 1017 O LEU A 143 18.860 37.311 15.257 1.00 10.07 O ATOM 1018 CB LEU A 143 16.489 37.027 17.036 1.00 9.27 C ATOM 1019 CG LEU A 143 15.796 36.967 18.398 1.00 9.40 C ATOM 1020 CD1 LEU A 143 15.069 35.609 18.562 1.00 8.87 C ATOM 1021 CD2 LEU A 143 16.794 37.146 19.530 1.00 10.43 C ATOM 1022 N GLY A 144 17.478 38.775 14.256 1.00 9.25 N ATOM 1023 CA GLY A 144 18.089 38.585 12.948 1.00 10.93 C ATOM 1024 C GLY A 144 17.841 37.199 12.385 1.00 10.50 C ATOM 1025 O GLY A 144 18.686 36.648 11.661 1.00 10.42 O ATOM 1026 N LEU A 145 16.692 36.605 12.702 1.00 10.28 N ATOM 1027 CA LEU A 145 16.397 35.265 12.191 1.00 10.29 C ATOM 1028 C LEU A 145 16.413 35.167 10.651 1.00 10.28 C ATOM 1029 O LEU A 145 16.795 34.144 10.108 1.00 10.30 O ATOM 1030 CB LEU A 145 15.024 34.799 12.693 1.00 10.42 C ATOM 1031 CG LEU A 145 14.899 34.752 14.224 1.00 9.37 C ATOM 1032 CD1 LEU A 145 13.485 34.247 14.551 1.00 9.21 C ATOM 1033 CD2 LEU A 145 15.977 33.844 14.838 1.00 8.94 C ATOM 1034 N HIS A 146 15.982 36.221 9.958 1.00 10.46 N ATOM 1035 CA HIS A 146 15.963 36.189 8.493 1.00 11.70 C ATOM 1036 C HIS A 146 17.346 35.991 7.896 1.00 11.06 C ATOM 1037 O HIS A 146 17.460 35.557 6.743 1.00 13.65 O ATOM 1038 CB HIS A 146 15.230 37.394 7.893 1.00 10.99 C ATOM 1039 CG HIS A 146 13.741 37.308 8.026 1.00 12.50 C ATOM 1040 ND1 HIS A 146 13.027 36.218 7.574 1.00 12.07 N ATOM 1041 CD2 HIS A 146 12.842 38.131 8.620 1.00 11.96 C ATOM 1042 CE1 HIS A 146 11.743 36.397 7.837 1.00 12.91 C ATOM 1043 NE2 HIS A 146 11.599 37.550 8.468 1.00 13.81 N ATOM 1044 N SER A 147 18.399 36.276 8.664 1.00 11.23 N ATOM 1045 CA SER A 147 19.770 36.076 8.166 1.00 11.60 C ATOM 1046 C SER A 147 20.315 34.656 8.335 1.00 10.48 C ATOM 1047 O SER A 147 21.388 34.328 7.814 1.00 11.08 O ATOM 1048 CB SER A 147 20.727 37.064 8.844 1.00 12.18 C ATOM 1049 OG SER A 147 20.274 38.380 8.604 1.00 16.55 O ATOM 1050 N LEU A 148 19.591 33.783 9.028 1.00 10.22 N ATOM 1051 CA LEU A 148 20.052 32.420 9.171 1.00 10.86 C ATOM 1052 C LEU A 148 20.089 31.692 7.847 1.00 10.95 C ATOM 1053 O LEU A 148 19.142 31.734 7.075 1.00 10.79 O ATOM 1054 CB LEU A 148 19.105 31.670 10.117 1.00 10.84 C ATOM 1055 CG LEU A 148 19.076 32.230 11.533 1.00 11.36 C ATOM 1056 CD1 LEU A 148 18.027 31.480 12.373 1.00 10.54 C ATOM 1057 CD2 LEU A 148 20.443 32.137 12.186 1.00 14.11 C ATOM 1058 N ARG A 149 21.189 31.002 7.592 1.00 11.78 N ATOM 1059 CA ARG A 149 21.333 30.230 6.363 1.00 12.89 C ATOM 1060 C ARG A 149 21.297 28.730 6.627 1.00 12.85 C ATOM 1061 O ARG A 149 21.695 28.264 7.692 1.00 13.86 O ATOM 1062 CB ARG A 149 22.631 30.616 5.630 1.00 12.61 C ATOM 1063 CG ARG A 149 22.662 32.072 5.237 1.00 13.79 C ATOM 1064 CD ARG A 149 23.595 32.387 4.091 1.00 17.59 C ATOM 1065 NE ARG A 149 23.528 33.799 3.727 1.00 15.98 N ATOM 1066 CZ ARG A 149 23.806 34.262 2.510 1.00 15.47 C ATOM 1067 NH1 ARG A 149 23.753 35.559 2.248 1.00 14.31 N ATOM 1068 NH2 ARG A 149 24.172 33.420 1.554 1.00 15.42 N ATOM 1069 N HIS A 150 20.832 27.993 5.630 1.00 14.42 N ATOM 1070 CA HIS A 150 20.785 26.530 5.653 1.00 16.37 C ATOM 1071 C HIS A 150 20.122 25.995 6.903 1.00 15.86 C ATOM 1072 O HIS A 150 20.581 25.019 7.483 1.00 16.11 O ATOM 1073 CB HIS A 150 22.207 25.967 5.552 1.00 17.51 C ATOM 1074 CG HIS A 150 22.948 26.411 4.323 1.00 22.60 C ATOM 1075 ND1 HIS A 150 24.318 26.542 4.288 1.00 30.44 N ATOM 1076 CD2 HIS A 150 22.508 26.744 3.086 1.00 27.54 C ATOM 1077 CE1 HIS A 150 24.693 26.943 3.086 1.00 30.36 C ATOM 1078 NE2 HIS A 150 23.614 27.076 2.338 1.00 29.79 N ATOM 1079 N ARG A 151 19.046 26.649 7.317 1.00 15.04 N ATOM 1080 CA ARG A 151 18.375 26.273 8.553 1.00 15.38 C ATOM 1081 C ARG A 151 16.873 26.458 8.415 1.00 14.25 C ATOM 1082 O ARG A 151 16.391 27.524 8.029 1.00 15.09 O ATOM 1083 CB ARG A 151 18.921 27.160 9.652 1.00 15.62 C ATOM 1084 CG ARG A 151 18.194 27.120 10.975 1.00 17.80 C ATOM 1085 CD ARG A 151 18.901 26.308 12.017 1.00 14.75 C ATOM 1086 NE ARG A 151 20.353 26.520 12.081 1.00 14.79 N ATOM 1087 CZ ARG A 151 21.189 25.605 12.563 1.00 17.01 C ATOM 1088 NH1 ARG A 151 20.700 24.458 13.030 1.00 14.67 N ATOM 1089 NH2 ARG A 151 22.501 25.819 12.586 1.00 17.37 N ATOM 1090 N ASN A 152 16.112 25.408 8.715 1.00 13.09 N ATOM 1091 CA ASN A 152 14.666 25.542 8.765 1.00 12.60 C ATOM 1092 C ASN A 152 14.307 26.110 10.146 1.00 11.48 C ATOM 1093 O ASN A 152 14.710 25.556 11.163 1.00 11.37 O ATOM 1094 CB ASN A 152 13.971 24.182 8.626 1.00 12.79 C ATOM 1095 CG ASN A 152 13.866 23.705 7.184 1.00 15.38 C ATOM 1096 OD1 ASN A 152 13.333 22.614 6.912 1.00 18.87 O ATOM 1097 ND2 ASN A 152 14.368 24.512 6.253 1.00 16.18 N ATOM 1098 N TRP A 153 13.573 27.206 10.162 1.00 11.06 N ATOM 1099 CA TRP A 153 13.219 27.873 11.431 1.00 10.79 C ATOM 1100 C TRP A 153 11.827 28.449 11.393 1.00 11.07 C ATOM 1101 O TRP A 153 11.231 28.617 10.320 1.00 10.85 O ATOM 1102 CB TRP A 153 14.249 28.951 11.834 1.00 10.25 C ATOM 1103 CG TRP A 153 14.320 30.126 10.924 1.00 9.38 C ATOM 1104 CD1 TRP A 153 15.169 30.282 9.875 1.00 10.25 C ATOM 1105 CD2 TRP A 153 13.490 31.296 10.948 1.00 7.90 C ATOM 1106 NE1 TRP A 153 14.936 31.480 9.242 1.00 10.52 N ATOM 1107 CE2 TRP A 153 13.922 32.136 9.897 1.00 10.75 C ATOM 1108 CE3 TRP A 153 12.459 31.747 11.787 1.00 9.38 C ATOM 1109 CZ2 TRP A 153 13.335 33.370 9.638 1.00 10.21 C ATOM 1110 CZ3 TRP A 153 11.867 32.975 11.527 1.00 9.90 C ATOM 1111 CH2 TRP A 153 12.320 33.779 10.466 1.00 11.51 C ATOM 1112 N TYR A 154 11.281 28.690 12.588 1.00 10.64 N ATOM 1113 CA TYR A 154 9.922 29.198 12.745 1.00 10.66 C ATOM 1114 C TYR A 154 9.871 29.938 14.056 1.00 10.98 C ATOM 1115 O TYR A 154 10.606 29.560 14.999 1.00 11.09 O ATOM 1116 CB TYR A 154 8.954 28.003 12.812 1.00 11.52 C ATOM 1117 CG TYR A 154 7.493 28.346 12.650 1.00 13.60 C ATOM 1118 CD1 TYR A 154 6.985 28.660 11.397 1.00 16.54 C ATOM 1119 CD2 TYR A 154 6.610 28.313 13.733 1.00 16.27 C ATOM 1120 CE1 TYR A 154 5.657 28.956 11.213 1.00 19.24 C ATOM 1121 CE2 TYR A 154 5.261 28.621 13.559 1.00 19.43 C ATOM 1122 CZ TYR A 154 4.798 28.934 12.297 1.00 21.10 C ATOM 1123 OH TYR A 154 3.469 29.238 12.084 1.00 23.57 O ATOM 1124 N ILE A 155 9.034 30.978 14.121 1.00 9.94 N ATOM 1125 CA ILE A 155 8.833 31.714 15.356 1.00 10.62 C ATOM 1126 C ILE A 155 7.358 31.710 15.678 1.00 10.68 C ATOM 1127 O ILE A 155 6.490 31.925 14.793 1.00 11.22 O ATOM 1128 CB ILE A 155 9.418 33.144 15.302 1.00 9.68 C ATOM 1129 CG1 ILE A 155 9.234 33.852 16.648 1.00 10.11 C ATOM 1130 CG2 ILE A 155 8.733 33.989 14.213 1.00 10.15 C ATOM 1131 CD1 ILE A 155 10.121 35.040 16.843 1.00 9.66 C ATOM 1132 N GLN A 156 7.071 31.456 16.957 1.00 10.47 N ATOM 1133 CA GLN A 156 5.715 31.382 17.453 1.00 10.68 C ATOM 1134 C GLN A 156 5.582 32.237 18.708 1.00 10.84 C ATOM 1135 O GLN A 156 6.363 32.081 19.657 1.00 10.08 O ATOM 1136 CB GLN A 156 5.336 29.920 17.773 1.00 11.87 C ATOM 1137 CG GLN A 156 3.981 29.802 18.445 1.00 13.49 C ATOM 1138 CD GLN A 156 2.845 30.048 17.481 1.00 16.52 C ATOM 1139 OE1 GLN A 156 1.893 30.775 17.800 1.00 22.67 O ATOM 1140 NE2 GLN A 156 2.957 29.489 16.282 1.00 16.59 N ATOM 1141 N ALA A 157 4.586 33.118 18.720 1.00 11.24 N ATOM 1142 CA ALA A 157 4.255 33.882 19.903 1.00 11.10 C ATOM 1143 C ALA A 157 3.609 32.955 20.929 1.00 11.23 C ATOM 1144 O ALA A 157 2.768 32.159 20.572 1.00 11.19 O ATOM 1145 CB ALA A 157 3.282 35.017 19.534 1.00 11.87 C ATOM 1146 N THR A 158 4.021 33.044 22.195 1.00 11.19 N ATOM 1147 CA THR A 158 3.437 32.137 23.191 1.00 11.53 C ATOM 1148 C THR A 158 3.128 32.867 24.488 1.00 11.99 C ATOM 1149 O THR A 158 3.717 33.902 24.799 1.00 11.29 O ATOM 1150 CB THR A 158 4.417 30.978 23.519 1.00 11.50 C ATOM 1151 OG1 THR A 158 5.643 31.530 24.022 1.00 10.49 O ATOM 1152 CG2 THR A 158 4.824 30.182 22.288 1.00 11.27 C ATOM 1153 N CYS A 159 2.191 32.296 25.233 1.00 13.41 N ATOM 1154 CA CYS A 159 1.916 32.686 26.614 1.00 16.67 C ATOM 1155 C CYS A 159 1.806 31.365 27.371 1.00 17.36 C ATOM 1156 O CYS A 159 0.886 30.607 27.140 1.00 17.50 O ATOM 1157 CB CYS A 159 0.616 33.488 26.738 1.00 16.52 C ATOM 1158 SG CYS A 159 0.258 33.877 28.474 1.00 22.26 S ATOM 1159 N ALA A 160 2.769 31.088 28.241 1.00 19.99 N ATOM 1160 CA ALA A 160 2.755 29.821 28.988 1.00 22.02 C ATOM 1161 C ALA A 160 1.473 29.619 29.812 1.00 23.59 C ATOM 1162 O ALA A 160 0.879 28.548 29.783 1.00 23.52 O ATOM 1163 CB ALA A 160 4.000 29.697 29.852 1.00 22.61 C ATOM 1164 N THR A 161 1.036 30.653 30.530 1.00 25.06 N ATOM 1165 CA THR A 161 -0.191 30.557 31.335 1.00 26.27 C ATOM 1166 C THR A 161 -1.418 30.009 30.595 1.00 26.37 C ATOM 1167 O THR A 161 -2.098 29.071 31.041 1.00 27.34 O ATOM 1168 CB THR A 161 -0.523 31.953 31.899 1.00 26.63 C ATOM 1169 OG1 THR A 161 0.670 32.541 32.437 1.00 27.97 O ATOM 1170 CG2 THR A 161 -1.478 31.860 33.078 1.00 28.05 C ATOM 1171 N SER A 162 -1.751 30.611 29.471 1.00 25.32 N ATOM 1172 CA SER A 162 -2.896 30.147 28.732 1.00 24.75 C ATOM 1173 C SER A 162 -2.542 28.919 27.900 1.00 24.29 C ATOM 1174 O SER A 162 -3.407 28.111 27.568 1.00 25.66 O ATOM 1175 CB SER A 162 -3.394 31.265 27.824 1.00 25.66 C ATOM 1176 OG SER A 162 -2.314 31.680 27.012 1.00 24.34 O ATOM 1177 N GLY A 163 -1.259 28.772 27.587 1.00 23.29 N ATOM 1178 CA GLY A 163 -0.801 27.695 26.727 1.00 21.51 C ATOM 1179 C GLY A 163 -0.837 28.105 25.260 1.00 20.75 C ATOM 1180 O GLY A 163 -0.455 27.335 24.366 1.00 19.42 O ATOM 1181 N ASP A 164 -1.301 29.320 24.991 1.00 19.52 N ATOM 1182 CA ASP A 164 -1.414 29.745 23.590 1.00 19.04 C ATOM 1183 C ASP A 164 -0.040 29.695 22.905 1.00 17.18 C ATOM 1184 O ASP A 164 0.956 30.163 23.471 1.00 16.27 O ATOM 1185 CB ASP A 164 -2.015 31.156 23.467 1.00 20.42 C ATOM 1186 CG ASP A 164 -3.508 31.187 23.770 1.00 24.41 C ATOM 1187 OD1 ASP A 164 -3.944 30.526 24.731 1.00 29.70 O ATOM 1188 OD2 ASP A 164 -4.332 31.831 23.082 1.00 30.34 O ATOM 1189 N GLY A 165 -0.006 29.086 21.722 1.00 16.06 N ATOM 1190 CA GLY A 165 1.201 29.034 20.909 1.00 14.24 C ATOM 1191 C GLY A 165 2.060 27.807 21.154 1.00 12.76 C ATOM 1192 O GLY A 165 2.824 27.388 20.289 1.00 12.82 O ATOM 1193 N LEU A 166 1.907 27.190 22.320 1.00 11.97 N ATOM 1194 CA LEU A 166 2.762 26.052 22.648 1.00 11.64 C ATOM 1195 C LEU A 166 2.544 24.863 21.722 1.00 12.53 C ATOM 1196 O LEU A 166 3.508 24.310 21.172 1.00 11.88 O ATOM 1197 CB LEU A 166 2.622 25.617 24.120 1.00 11.54 C ATOM 1198 CG LEU A 166 2.927 26.704 25.162 1.00 11.05 C ATOM 1199 CD1 LEU A 166 2.838 26.116 26.581 1.00 12.07 C ATOM 1200 CD2 LEU A 166 4.319 27.363 24.962 1.00 12.87 C ATOM 1201 N TYR A 167 1.292 24.452 21.537 1.00 12.64 N ATOM 1202 CA TYR A 167 1.064 23.316 20.659 1.00 13.11 C ATOM 1203 C TYR A 167 1.264 23.633 19.183 1.00 13.14 C ATOM 1204 O TYR A 167 1.576 22.739 18.390 1.00 13.51 O ATOM 1205 CB TYR A 167 -0.303 22.678 20.935 1.00 13.58 C ATOM 1206 CG TYR A 167 -0.286 22.017 22.281 1.00 13.99 C ATOM 1207 CD1 TYR A 167 0.312 20.783 22.447 1.00 14.85 C ATOM 1208 CD2 TYR A 167 -0.808 22.650 23.396 1.00 15.26 C ATOM 1209 CE1 TYR A 167 0.345 20.159 23.676 1.00 14.61 C ATOM 1210 CE2 TYR A 167 -0.760 22.041 24.643 1.00 17.41 C ATOM 1211 CZ TYR A 167 -0.177 20.801 24.771 1.00 17.69 C ATOM 1212 OH TYR A 167 -0.118 20.174 25.994 1.00 20.98 O ATOM 1213 N GLU A 168 1.099 24.901 18.823 1.00 13.44 N ATOM 1214 CA GLU A 168 1.340 25.335 17.455 1.00 13.88 C ATOM 1215 C GLU A 168 2.826 25.135 17.175 1.00 13.39 C ATOM 1216 O GLU A 168 3.232 24.719 16.099 1.00 12.79 O ATOM 1217 CB GLU A 168 0.899 26.774 17.263 1.00 15.06 C ATOM 1218 CG GLU A 168 -0.616 26.931 17.207 1.00 16.29 C ATOM 1219 CD GLU A 168 -1.311 26.954 18.560 1.00 19.34 C ATOM 1220 OE1 GLU A 168 -2.548 27.140 18.558 1.00 21.97 O ATOM 1221 OE2 GLU A 168 -0.647 26.866 19.618 1.00 17.61 O ATOM 1222 N GLY A 169 3.636 25.408 18.194 1.00 12.73 N ATOM 1223 CA GLY A 169 5.060 25.135 18.126 1.00 12.61 C ATOM 1224 C GLY A 169 5.348 23.650 17.950 1.00 12.06 C ATOM 1225 O GLY A 169 6.145 23.258 17.103 1.00 12.32 O ATOM 1226 N LEU A 170 4.703 22.798 18.739 1.00 11.29 N ATOM 1227 CA LEU A 170 4.946 21.395 18.577 1.00 11.32 C ATOM 1228 C LEU A 170 4.456 20.904 17.216 1.00 12.19 C ATOM 1229 O LEU A 170 5.031 19.991 16.636 1.00 12.07 O ATOM 1230 CB LEU A 170 4.303 20.573 19.705 1.00 11.75 C ATOM 1231 CG LEU A 170 4.885 20.809 21.101 1.00 12.25 C ATOM 1232 CD1 LEU A 170 4.184 19.922 22.108 1.00 13.61 C ATOM 1233 CD2 LEU A 170 6.398 20.501 21.126 1.00 14.67 C ATOM 1234 N ASP A 171 3.404 21.534 16.707 1.00 12.79 N ATOM 1235 CA ASP A 171 2.882 21.145 15.392 1.00 13.52 C ATOM 1236 C ASP A 171 3.939 21.387 14.335 1.00 12.87 C ATOM 1237 O ASP A 171 4.140 20.563 13.449 1.00 13.77 O ATOM 1238 CB ASP A 171 1.651 21.982 15.015 1.00 13.79 C ATOM 1239 CG ASP A 171 0.410 21.570 15.765 1.00 15.88 C ATOM 1240 OD1 ASP A 171 -0.479 22.436 15.916 1.00 19.83 O ATOM 1241 OD2 ASP A 171 0.246 20.438 16.261 1.00 20.57 O ATOM 1242 N TRP A 172 4.636 22.508 14.437 1.00 12.22 N ATOM 1243 CA TRP A 172 5.647 22.817 13.430 1.00 12.35 C ATOM 1244 C TRP A 172 6.769 21.787 13.510 1.00 11.87 C ATOM 1245 O TRP A 172 7.227 21.266 12.482 1.00 12.06 O ATOM 1246 CB TRP A 172 6.189 24.232 13.623 1.00 12.35 C ATOM 1247 CG TRP A 172 7.196 24.611 12.602 1.00 13.39 C ATOM 1248 CD1 TRP A 172 6.949 25.089 11.345 1.00 12.95 C ATOM 1249 CD2 TRP A 172 8.621 24.538 12.733 1.00 10.95 C ATOM 1250 NE1 TRP A 172 8.133 25.310 10.681 1.00 13.21 N ATOM 1251 CE2 TRP A 172 9.178 24.977 11.506 1.00 12.62 C ATOM 1252 CE3 TRP A 172 9.489 24.151 13.767 1.00 13.35 C ATOM 1253 CZ2 TRP A 172 10.570 25.065 11.287 1.00 12.33 C ATOM 1254 CZ3 TRP A 172 10.860 24.230 13.561 1.00 12.19 C ATOM 1255 CH2 TRP A 172 11.396 24.686 12.314 1.00 12.78 C ATOM 1256 N LEU A 173 7.232 21.511 14.728 1.00 12.17 N ATOM 1257 CA LEU A 173 8.289 20.526 14.931 1.00 12.29 C ATOM 1258 C LEU A 173 7.868 19.191 14.358 1.00 13.04 C ATOM 1259 O LEU A 173 8.663 18.530 13.726 1.00 12.06 O ATOM 1260 CB LEU A 173 8.583 20.343 16.416 1.00 12.98 C ATOM 1261 CG LEU A 173 9.817 20.976 17.064 1.00 16.24 C ATOM 1262 CD1 LEU A 173 10.752 21.847 16.256 1.00 14.81 C ATOM 1263 CD2 LEU A 173 9.521 21.494 18.465 1.00 12.64 C ATOM 1264 N SER A 174 6.620 18.802 14.622 1.00 13.79 N ATOM 1265 CA SER A 174 6.078 17.536 14.151 1.00 15.58 C ATOM 1266 C SER A 174 6.139 17.445 12.615 1.00 15.64 C ATOM 1267 O SER A 174 6.597 16.449 12.063 1.00 16.54 O ATOM 1268 CB SER A 174 4.639 17.369 14.659 1.00 16.17 C ATOM 1269 OG SER A 174 4.009 16.272 14.034 1.00 20.06 O ATOM 1270 N ASN A 175 5.686 18.488 11.930 1.00 16.21 N ATOM 1271 CA ASN A 175 5.734 18.526 10.471 1.00 16.86 C ATOM 1272 C ASN A 175 7.172 18.489 9.939 1.00 16.68 C ATOM 1273 O ASN A 175 7.468 17.851 8.945 1.00 16.54 O ATOM 1274 CB ASN A 175 4.925 19.716 9.959 1.00 17.51 C ATOM 1275 CG ASN A 175 3.431 19.544 10.240 1.00 21.01 C ATOM 1276 OD1 ASN A 175 2.928 18.415 10.216 1.00 25.34 O ATOM 1277 ND2 ASN A 175 2.724 20.640 10.531 1.00 27.27 N ATOM 1278 N GLN A 176 8.093 19.148 10.640 1.00 16.02 N ATOM 1279 CA GLN A 176 9.480 19.055 10.232 1.00 16.01 C ATOM 1280 C GLN A 176 9.974 17.613 10.293 1.00 17.04 C ATOM 1281 O GLN A 176 10.628 17.143 9.372 1.00 17.13 O ATOM 1282 CB GLN A 176 10.363 19.965 11.104 1.00 15.23 C ATOM 1283 CG GLN A 176 10.140 21.452 10.875 1.00 13.90 C ATOM 1284 CD GLN A 176 10.596 21.904 9.489 1.00 14.84 C ATOM 1285 OE1 GLN A 176 9.843 22.540 8.747 1.00 18.84 O ATOM 1286 NE2 GLN A 176 11.792 21.534 9.129 1.00 12.63 N ATOM 1287 N LEU A 177 9.651 16.894 11.365 1.00 17.14 N ATOM 1288 CA LEU A 177 10.147 15.542 11.528 1.00 18.46 C ATOM 1289 C LEU A 177 9.542 14.638 10.463 1.00 20.29 C ATOM 1290 O LEU A 177 10.221 13.808 9.876 1.00 20.41 O ATOM 1291 CB LEU A 177 9.753 15.009 12.906 1.00 17.97 C ATOM 1292 CG LEU A 177 10.384 13.657 13.245 1.00 16.51 C ATOM 1293 CD1 LEU A 177 11.896 13.758 13.539 1.00 17.22 C ATOM 1294 CD2 LEU A 177 9.653 13.021 14.424 1.00 16.81 C ATOM 1295 N ARG A 178 8.254 14.817 10.230 1.00 22.77 N ATOM 1296 CA ARG A 178 7.529 13.984 9.277 1.00 26.37 C ATOM 1297 C ARG A 178 8.096 14.084 7.878 1.00 28.30 C ATOM 1298 O ARG A 178 8.143 13.085 7.144 1.00 28.78 O ATOM 1299 CB ARG A 178 6.080 14.415 9.218 1.00 26.63 C ATOM 1300 CG ARG A 178 5.249 14.060 10.406 1.00 30.66 C ATOM 1301 CD ARG A 178 3.844 14.563 10.225 1.00 37.46 C ATOM 1302 NE ARG A 178 3.429 14.373 8.833 1.00 42.16 N ATOM 1303 CZ ARG A 178 2.554 15.146 8.203 1.00 45.02 C ATOM 1304 NH1 ARG A 178 1.986 16.162 8.848 1.00 46.55 N ATOM 1305 NH2 ARG A 178 2.237 14.901 6.934 1.00 45.58 N ATOM 1306 N ASN A 179 8.487 15.291 7.484 1.00 30.74 N ATOM 1307 CA ASN A 179 9.037 15.513 6.145 1.00 33.97 C ATOM 1308 C ASN A 179 10.540 15.237 6.119 1.00 35.73 C ATOM 1309 O ASN A 179 11.288 15.855 5.358 1.00 37.12 O ATOM 1310 CB ASN A 179 8.734 16.939 5.655 1.00 34.21 C ATOM 1311 CG ASN A 179 7.243 17.182 5.414 1.00 35.49 C ATOM 1312 OD1 ASN A 179 6.600 16.483 4.625 1.00 37.52 O ATOM 1313 ND2 ASN A 179 6.689 18.181 6.096 1.00 37.23 N ATOM 1314 N GLN A 180 10.957 14.293 6.959 1.00 37.85 N ATOM 1315 CA GLN A 180 12.349 13.859 7.096 1.00 39.86 C ATOM 1316 C GLN A 180 13.215 14.855 7.857 1.00 40.33 C ATOM 1317 O GLN A 180 12.822 15.968 8.212 1.00 40.43 O ATOM 1318 CB GLN A 180 12.985 13.514 5.740 1.00 40.31 C ATOM 1319 CG GLN A 180 12.423 12.272 5.061 1.00 43.41 C ATOM 1320 CD GLN A 180 13.182 11.904 3.784 1.00 47.21 C ATOM 1321 OE1 GLN A 180 12.739 11.043 3.016 1.00 49.71 O ATOM 1322 NE2 GLN A 180 14.327 12.551 3.561 1.00 47.52 N TER 1323 GLN A 180 ATOM 1324 N ILE B 168 34.153 28.268 37.030 1.00 28.54 N ATOM 1325 CA ILE B 168 33.468 27.132 37.716 1.00 27.94 C ATOM 1326 C ILE B 168 33.785 25.787 37.068 1.00 27.80 C ATOM 1327 O ILE B 168 33.984 24.782 37.761 1.00 27.85 O ATOM 1328 CB ILE B 168 31.928 27.288 37.686 1.00 27.55 C ATOM 1329 CG1 ILE B 168 31.451 28.624 38.270 1.00 29.05 C ATOM 1330 CG2 ILE B 168 31.276 26.154 38.444 1.00 26.58 C ATOM 1331 CD1 ILE B 168 29.881 28.747 38.310 1.00 29.08 C ATOM 1332 N PHE B 169 33.792 25.755 35.739 1.00 27.71 N ATOM 1333 CA PHE B 169 33.952 24.491 35.024 1.00 27.36 C ATOM 1334 C PHE B 169 35.272 24.438 34.259 1.00 27.96 C ATOM 1335 O PHE B 169 35.322 23.928 33.140 1.00 29.04 O ATOM 1336 CB PHE B 169 32.767 24.270 34.064 1.00 27.36 C ATOM 1337 CG PHE B 169 31.414 24.452 34.717 1.00 24.58 C ATOM 1338 CD1 PHE B 169 30.722 25.645 34.589 1.00 24.99 C ATOM 1339 CD2 PHE B 169 30.840 23.430 35.454 1.00 25.20 C ATOM 1340 CE1 PHE B 169 29.487 25.825 35.201 1.00 24.13 C ATOM 1341 CE2 PHE B 169 29.601 23.596 36.076 1.00 23.94 C ATOM 1342 CZ PHE B 169 28.927 24.806 35.952 1.00 23.91 C ATOM 1343 N GLU B 170 36.333 24.957 34.866 1.00 27.56 N ATOM 1344 CA GLU B 170 37.638 25.007 34.190 1.00 27.52 C ATOM 1345 C GLU B 170 38.383 23.677 34.208 1.00 25.65 C ATOM 1346 O GLU B 170 39.298 23.447 33.401 1.00 25.34 O ATOM 1347 CB GLU B 170 38.522 26.110 34.796 1.00 28.55 C ATOM 1348 CG GLU B 170 38.967 25.878 36.234 1.00 32.50 C ATOM 1349 CD GLU B 170 39.692 27.091 36.793 1.00 38.65 C ATOM 1350 OE1 GLU B 170 39.041 28.156 36.932 1.00 39.96 O ATOM 1351 OE2 GLU B 170 40.909 26.983 37.072 1.00 39.35 O ATOM 1352 N ASP B 171 38.010 22.815 35.146 1.00 23.51 N ATOM 1353 CA ASP B 171 38.679 21.542 35.309 1.00 21.83 C ATOM 1354 C ASP B 171 38.212 20.649 34.171 1.00 21.18 C ATOM 1355 O ASP B 171 37.061 20.202 34.177 1.00 20.43 O ATOM 1356 CB ASP B 171 38.317 20.948 36.670 1.00 21.60 C ATOM 1357 CG ASP B 171 39.017 19.646 36.950 1.00 22.47 C ATOM 1358 OD1 ASP B 171 39.188 18.839 36.011 1.00 23.01 O ATOM 1359 OD2 ASP B 171 39.428 19.324 38.087 1.00 20.87 O ATOM 1360 N GLU B 172 39.108 20.398 33.213 1.00 20.13 N ATOM 1361 CA GLU B 172 38.804 19.603 32.023 1.00 20.25 C ATOM 1362 C GLU B 172 38.350 18.193 32.343 1.00 18.62 C ATOM 1363 O GLU B 172 37.467 17.642 31.669 1.00 17.39 O ATOM 1364 CB GLU B 172 40.023 19.529 31.104 1.00 21.25 C ATOM 1365 CG GLU B 172 40.335 20.821 30.368 1.00 26.11 C ATOM 1366 CD GLU B 172 41.568 20.706 29.475 1.00 32.40 C ATOM 1367 OE1 GLU B 172 41.910 21.704 28.804 1.00 35.36 O ATOM 1368 OE2 GLU B 172 42.195 19.615 29.446 1.00 35.13 O ATOM 1369 N GLU B 173 38.965 17.585 33.351 1.00 17.64 N ATOM 1370 CA GLU B 173 38.582 16.230 33.721 1.00 17.33 C ATOM 1371 C GLU B 173 37.173 16.188 34.301 1.00 17.26 C ATOM 1372 O GLU B 173 36.402 15.297 33.975 1.00 16.26 O ATOM 1373 CB GLU B 173 39.602 15.595 34.661 1.00 17.31 C ATOM 1374 CG GLU B 173 40.954 15.342 33.979 1.00 19.86 C ATOM 1375 CD GLU B 173 40.861 14.451 32.750 1.00 23.06 C ATOM 1376 OE1 GLU B 173 40.269 13.353 32.837 1.00 26.38 O ATOM 1377 OE2 GLU B 173 41.388 14.844 31.692 1.00 21.99 O ATOM 1378 N LYS B 174 36.816 17.140 35.158 1.00 17.01 N ATOM 1379 CA LYS B 174 35.457 17.147 35.683 1.00 17.50 C ATOM 1380 C LYS B 174 34.480 17.416 34.537 1.00 16.82 C ATOM 1381 O LYS B 174 33.363 16.869 34.511 1.00 17.60 O ATOM 1382 CB LYS B 174 35.278 18.190 36.790 1.00 17.95 C ATOM 1383 CG LYS B 174 36.058 17.918 38.044 1.00 21.00 C ATOM 1384 CD LYS B 174 35.765 19.007 39.075 1.00 25.76 C ATOM 1385 CE LYS B 174 36.889 19.101 40.103 1.00 26.92 C ATOM 1386 NZ LYS B 174 36.647 20.203 41.074 1.00 30.62 N ATOM 1387 N SER B 175 34.903 18.222 33.564 1.00 16.66 N ATOM 1388 CA SER B 175 34.036 18.497 32.409 1.00 15.98 C ATOM 1389 C SER B 175 33.775 17.235 31.607 1.00 15.81 C ATOM 1390 O SER B 175 32.666 17.021 31.113 1.00 15.33 O ATOM 1391 CB SER B 175 34.618 19.576 31.501 1.00 16.61 C ATOM 1392 OG SER B 175 34.487 20.843 32.088 1.00 21.39 O ATOM 1393 N LYS B 176 34.809 16.407 31.447 1.00 13.71 N ATOM 1394 CA LYS B 176 34.639 15.154 30.719 1.00 13.93 C ATOM 1395 C LYS B 176 33.652 14.231 31.424 1.00 12.68 C ATOM 1396 O LYS B 176 32.898 13.486 30.775 1.00 12.15 O ATOM 1397 CB LYS B 176 35.973 14.404 30.607 1.00 14.17 C ATOM 1398 CG LYS B 176 36.919 15.011 29.591 1.00 17.18 C ATOM 1399 CD LYS B 176 38.175 14.182 29.519 1.00 20.32 C ATOM 1400 CE LYS B 176 39.194 14.794 28.575 1.00 25.81 C ATOM 1401 NZ LYS B 176 40.372 13.893 28.473 1.00 30.53 N ATOM 1402 N MET B 177 33.694 14.232 32.760 1.00 12.95 N ATOM 1403 CA MET B 177 32.790 13.380 33.519 1.00 12.70 C ATOM 1404 C MET B 177 31.365 13.908 33.279 1.00 12.67 C ATOM 1405 O MET B 177 30.468 13.156 32.954 1.00 11.86 O ATOM 1406 CB MET B 177 33.126 13.397 35.023 1.00 13.75 C ATOM 1407 CG MET B 177 32.149 12.544 35.824 1.00 15.53 C ATOM 1408 SD MET B 177 32.655 12.385 37.560 1.00 18.70 S ATOM 1409 CE MET B 177 31.552 11.067 38.128 1.00 17.43 C ATOM 1410 N LEU B 178 31.191 15.216 33.398 1.00 12.55 N ATOM 1411 CA LEU B 178 29.882 15.825 33.206 1.00 12.43 C ATOM 1412 C LEU B 178 29.365 15.542 31.820 1.00 12.24 C ATOM 1413 O LEU B 178 28.231 15.126 31.678 1.00 12.28 O ATOM 1414 CB LEU B 178 29.931 17.326 33.472 1.00 13.22 C ATOM 1415 CG LEU B 178 28.592 18.042 33.345 1.00 14.32 C ATOM 1416 CD1 LEU B 178 27.586 17.405 34.281 1.00 14.29 C ATOM 1417 CD2 LEU B 178 28.761 19.525 33.694 1.00 12.80 C ATOM 1418 N ALA B 179 30.217 15.716 30.809 1.00 11.27 N ATOM 1419 CA ALA B 179 29.794 15.470 29.434 1.00 12.09 C ATOM 1420 C ALA B 179 29.342 14.037 29.234 1.00 11.74 C ATOM 1421 O ALA B 179 28.313 13.791 28.593 1.00 12.72 O ATOM 1422 CB ALA B 179 30.924 15.830 28.436 1.00 12.37 C ATOM 1423 N ARG B 180 30.080 13.057 29.758 1.00 11.54 N ATOM 1424 CA ARG B 180 29.650 11.689 29.517 1.00 12.00 C ATOM 1425 C ARG B 180 28.372 11.353 30.258 1.00 12.30 C ATOM 1426 O ARG B 180 27.567 10.552 29.775 1.00 13.41 O ATOM 1427 CB ARG B 180 30.755 10.641 29.819 1.00 11.63 C ATOM 1428 CG ARG B 180 30.994 10.338 31.274 1.00 12.95 C ATOM 1429 CD ARG B 180 31.981 9.198 31.471 1.00 14.43 C ATOM 1430 NE ARG B 180 32.292 8.875 32.869 1.00 13.57 N ATOM 1431 CZ ARG B 180 31.583 8.049 33.637 1.00 14.24 C ATOM 1432 NH1 ARG B 180 30.466 7.501 33.152 1.00 13.95 N ATOM 1433 NH2 ARG B 180 31.985 7.793 34.894 1.00 14.92 N ATOM 1434 N LEU B 181 28.160 11.959 31.423 1.00 10.95 N ATOM 1435 CA LEU B 181 26.944 11.652 32.151 1.00 11.30 C ATOM 1436 C LEU B 181 25.752 12.261 31.441 1.00 10.78 C ATOM 1437 O LEU B 181 24.701 11.641 31.385 1.00 11.21 O ATOM 1438 CB LEU B 181 27.008 12.174 33.588 1.00 11.17 C ATOM 1439 CG LEU B 181 28.111 11.533 34.439 1.00 10.41 C ATOM 1440 CD1 LEU B 181 28.191 12.299 35.775 1.00 9.70 C ATOM 1441 CD2 LEU B 181 27.850 10.001 34.675 1.00 10.94 C ATOM 1442 N LEU B 182 25.926 13.480 30.916 1.00 10.21 N ATOM 1443 CA LEU B 182 24.820 14.164 30.240 1.00 10.74 C ATOM 1444 C LEU B 182 24.438 13.522 28.911 1.00 10.47 C ATOM 1445 O LEU B 182 23.325 13.743 28.405 1.00 11.35 O ATOM 1446 CB LEU B 182 25.140 15.642 30.011 1.00 11.50 C ATOM 1447 CG LEU B 182 25.062 16.534 31.253 1.00 10.53 C ATOM 1448 CD1 LEU B 182 25.582 17.923 30.973 1.00 10.92 C ATOM 1449 CD2 LEU B 182 23.619 16.602 31.819 1.00 10.29 C ATOM 1450 N LYS B 183 25.360 12.769 28.323 1.00 10.77 N ATOM 1451 CA LYS B 183 25.136 12.150 27.011 1.00 10.84 C ATOM 1452 C LYS B 183 24.784 10.659 27.119 1.00 11.68 C ATOM 1453 O LYS B 183 24.614 9.949 26.123 1.00 11.56 O ATOM 1454 CB LYS B 183 26.387 12.351 26.138 1.00 11.09 C ATOM 1455 CG LYS B 183 26.673 13.808 25.790 1.00 11.63 C ATOM 1456 CD LYS B 183 28.035 14.010 25.127 1.00 12.47 C ATOM 1457 CE LYS B 183 28.298 15.533 24.986 1.00 12.77 C ATOM 1458 NZ LYS B 183 29.638 15.756 24.335 1.00 15.57 N ATOM 1459 N SER B 184 24.646 10.200 28.354 1.00 10.78 N ATOM 1460 CA SER B 184 24.353 8.815 28.635 1.00 12.69 C ATOM 1461 C SER B 184 22.883 8.479 28.487 1.00 13.73 C ATOM 1462 O SER B 184 22.029 9.333 28.697 1.00 15.51 O ATOM 1463 CB SER B 184 24.805 8.505 30.064 1.00 12.34 C ATOM 1464 OG SER B 184 24.495 7.164 30.373 1.00 11.32 O ATOM 1465 N SER B 185 22.594 7.226 28.152 1.00 15.58 N ATOM 1466 CA SER B 185 21.213 6.771 28.113 1.00 17.24 C ATOM 1467 C SER B 185 20.743 6.258 29.468 1.00 16.26 C ATOM 1468 O SER B 185 19.526 6.011 29.653 1.00 18.52 O ATOM 1469 CB SER B 185 21.062 5.654 27.083 1.00 17.32 C ATOM 1470 OG SER B 185 21.863 4.545 27.445 1.00 21.73 O ATOM 1471 N HIS B 186 21.659 6.133 30.432 1.00 14.34 N ATOM 1472 CA HIS B 186 21.309 5.535 31.722 1.00 13.77 C ATOM 1473 C HIS B 186 20.700 6.611 32.596 1.00 12.67 C ATOM 1474 O HIS B 186 21.328 7.623 32.834 1.00 12.19 O ATOM 1475 CB HIS B 186 22.552 4.973 32.429 1.00 12.70 C ATOM 1476 CG HIS B 186 23.198 3.847 31.686 1.00 14.93 C ATOM 1477 ND1 HIS B 186 22.718 2.553 31.742 1.00 17.16 N ATOM 1478 CD2 HIS B 186 24.257 3.824 30.847 1.00 17.25 C ATOM 1479 CE1 HIS B 186 23.465 1.778 30.969 1.00 17.74 C ATOM 1480 NE2 HIS B 186 24.404 2.525 30.417 1.00 16.73 N ATOM 1481 N PRO B 187 19.495 6.389 33.092 1.00 13.27 N ATOM 1482 CA PRO B 187 18.855 7.396 33.945 1.00 13.37 C ATOM 1483 C PRO B 187 19.687 7.769 35.176 1.00 12.16 C ATOM 1484 O PRO B 187 19.636 8.929 35.598 1.00 12.08 O ATOM 1485 CB PRO B 187 17.549 6.722 34.371 1.00 13.47 C ATOM 1486 CG PRO B 187 17.782 5.276 34.110 1.00 17.24 C ATOM 1487 CD PRO B 187 18.627 5.214 32.865 1.00 12.87 C ATOM 1488 N GLU B 188 20.442 6.831 35.760 1.00 12.18 N ATOM 1489 CA GLU B 188 21.229 7.206 36.941 1.00 12.58 C ATOM 1490 C GLU B 188 22.327 8.193 36.587 1.00 11.51 C ATOM 1491 O GLU B 188 22.716 9.032 37.402 1.00 10.98 O ATOM 1492 CB GLU B 188 21.898 5.984 37.555 1.00 13.51 C ATOM 1493 CG GLU B 188 20.999 4.771 37.668 1.00 19.15 C ATOM 1494 CD GLU B 188 21.197 3.836 36.477 1.00 22.51 C ATOM 1495 OE1 GLU B 188 20.827 4.209 35.355 1.00 18.29 O ATOM 1496 OE2 GLU B 188 21.737 2.714 36.666 1.00 27.74 O ATOM 1497 N ASP B 189 22.850 8.077 35.369 1.00 10.14 N ATOM 1498 CA ASP B 189 23.897 8.993 34.948 1.00 9.90 C ATOM 1499 C ASP B 189 23.351 10.406 34.810 1.00 8.43 C ATOM 1500 O ASP B 189 24.015 11.373 35.162 1.00 8.20 O ATOM 1501 CB ASP B 189 24.455 8.592 33.592 1.00 9.04 C ATOM 1502 CG ASP B 189 25.334 7.386 33.667 1.00 10.83 C ATOM 1503 OD1 ASP B 189 25.821 7.074 34.790 1.00 11.55 O ATOM 1504 OD2 ASP B 189 25.640 6.741 32.626 1.00 11.59 O ATOM 1505 N LEU B 190 22.137 10.512 34.278 1.00 9.14 N ATOM 1506 CA LEU B 190 21.527 11.813 34.118 1.00 9.23 C ATOM 1507 C LEU B 190 21.236 12.439 35.493 1.00 9.68 C ATOM 1508 O LEU B 190 21.441 13.638 35.687 1.00 9.86 O ATOM 1509 CB LEU B 190 20.257 11.701 33.287 1.00 9.37 C ATOM 1510 CG LEU B 190 20.463 11.145 31.898 1.00 11.08 C ATOM 1511 CD1 LEU B 190 19.095 10.933 31.217 1.00 12.52 C ATOM 1512 CD2 LEU B 190 21.307 12.099 31.094 1.00 13.40 C ATOM 1513 N ARG B 191 20.772 11.623 36.454 1.00 9.57 N ATOM 1514 CA ARG B 191 20.539 12.168 37.787 1.00 9.38 C ATOM 1515 C ARG B 191 21.848 12.617 38.387 1.00 8.53 C ATOM 1516 O ARG B 191 21.900 13.639 39.067 1.00 8.46 O ATOM 1517 CB ARG B 191 19.895 11.155 38.713 1.00 8.82 C ATOM 1518 CG ARG B 191 18.468 10.783 38.288 1.00 9.72 C ATOM 1519 CD ARG B 191 17.735 10.011 39.365 1.00 10.90 C ATOM 1520 NE ARG B 191 18.376 8.740 39.675 1.00 13.35 N ATOM 1521 CZ ARG B 191 18.019 7.562 39.176 1.00 15.52 C ATOM 1522 NH1 ARG B 191 16.996 7.458 38.317 1.00 15.26 N ATOM 1523 NH2 ARG B 191 18.704 6.478 39.531 1.00 16.58 N ATOM 1524 N ALA B 192 22.905 11.831 38.178 1.00 9.13 N ATOM 1525 CA ALA B 192 24.204 12.192 38.680 1.00 8.89 C ATOM 1526 C ALA B 192 24.715 13.502 38.104 1.00 8.92 C ATOM 1527 O ALA B 192 25.303 14.294 38.820 1.00 8.99 O ATOM 1528 CB ALA B 192 25.258 11.072 38.362 1.00 8.88 C ATOM 1529 N ALA B 193 24.476 13.715 36.809 1.00 8.58 N ATOM 1530 CA ALA B 193 24.954 14.922 36.145 1.00 8.35 C ATOM 1531 C ALA B 193 24.279 16.140 36.734 1.00 8.40 C ATOM 1532 O ALA B 193 24.914 17.171 36.938 1.00 8.43 O ATOM 1533 CB ALA B 193 24.643 14.842 34.664 1.00 8.89 C ATOM 1534 N ASN B 194 22.976 16.015 36.912 1.00 7.45 N ATOM 1535 CA ASN B 194 22.148 17.134 37.407 1.00 8.06 C ATOM 1536 C ASN B 194 22.614 17.555 38.801 1.00 8.35 C ATOM 1537 O ASN B 194 22.773 18.744 39.087 1.00 9.23 O ATOM 1538 CB ASN B 194 20.661 16.733 37.384 1.00 7.35 C ATOM 1539 CG ASN B 194 19.734 17.867 36.951 1.00 9.44 C ATOM 1540 OD1 ASN B 194 20.148 18.997 36.757 1.00 9.15 O ATOM 1541 ND2 ASN B 194 18.472 17.517 36.751 1.00 9.27 N ATOM 1542 N LYS B 195 22.887 16.575 39.657 1.00 8.81 N ATOM 1543 CA LYS B 195 23.431 16.853 40.988 1.00 10.18 C ATOM 1544 C LYS B 195 24.853 17.397 40.909 1.00 10.80 C ATOM 1545 O LYS B 195 25.211 18.294 41.676 1.00 10.59 O ATOM 1546 CB LYS B 195 23.372 15.599 41.855 1.00 10.55 C ATOM 1547 CG LYS B 195 23.678 15.903 43.323 1.00 18.03 C ATOM 1548 CD LYS B 195 23.268 14.730 44.230 1.00 23.46 C ATOM 1549 CE LYS B 195 23.294 15.128 45.683 1.00 28.37 C ATOM 1550 NZ LYS B 195 24.613 15.716 46.001 1.00 29.03 N ATOM 1551 N LEU B 196 25.664 16.862 39.997 1.00 10.11 N ATOM 1552 CA LEU B 196 27.034 17.325 39.818 1.00 11.48 C ATOM 1553 C LEU B 196 27.055 18.817 39.499 1.00 11.21 C ATOM 1554 O LEU B 196 27.809 19.577 40.093 1.00 11.58 O ATOM 1555 CB LEU B 196 27.731 16.520 38.712 1.00 10.74 C ATOM 1556 CG LEU B 196 29.182 16.873 38.394 1.00 11.96 C ATOM 1557 CD1 LEU B 196 30.018 16.919 39.671 1.00 15.38 C ATOM 1558 CD2 LEU B 196 29.794 15.881 37.406 1.00 13.57 C ATOM 1559 N ILE B 197 26.160 19.248 38.610 1.00 10.39 N ATOM 1560 CA ILE B 197 26.136 20.654 38.227 1.00 10.33 C ATOM 1561 C ILE B 197 25.771 21.525 39.426 1.00 9.94 C ATOM 1562 O ILE B 197 26.439 22.541 39.668 1.00 11.76 O ATOM 1563 CB ILE B 197 25.145 20.880 37.093 1.00 9.09 C ATOM 1564 CG1 ILE B 197 25.670 20.196 35.840 1.00 8.67 C ATOM 1565 CG2 ILE B 197 24.996 22.393 36.832 1.00 10.09 C ATOM 1566 CD1 ILE B 197 24.602 20.127 34.711 1.00 8.23 C ATOM 1567 N LYS B 198 24.774 21.105 40.201 1.00 10.04 N ATOM 1568 CA LYS B 198 24.395 21.852 41.397 1.00 10.19 C ATOM 1569 C LYS B 198 25.555 21.896 42.410 1.00 11.01 C ATOM 1570 O LYS B 198 25.799 22.924 43.030 1.00 12.03 O ATOM 1571 CB LYS B 198 23.155 21.236 42.023 1.00 9.53 C ATOM 1572 CG LYS B 198 21.930 21.414 41.110 1.00 8.79 C ATOM 1573 CD LYS B 198 20.714 20.679 41.664 1.00 9.28 C ATOM 1574 CE LYS B 198 19.487 20.866 40.757 1.00 9.51 C ATOM 1575 NZ LYS B 198 19.772 20.233 39.430 1.00 9.98 N ATOM 1576 N GLU B 199 26.255 20.786 42.570 1.00 11.56 N ATOM 1577 CA GLU B 199 27.363 20.781 43.529 1.00 13.45 C ATOM 1578 C GLU B 199 28.432 21.750 43.121 1.00 14.36 C ATOM 1579 O GLU B 199 28.972 22.476 43.967 1.00 16.71 O ATOM 1580 CB GLU B 199 27.969 19.368 43.687 1.00 12.91 C ATOM 1581 CG GLU B 199 27.032 18.388 44.360 1.00 14.14 C ATOM 1582 CD GLU B 199 26.771 18.716 45.815 1.00 18.37 C ATOM 1583 OE1 GLU B 199 25.595 18.772 46.257 1.00 20.87 O ATOM 1584 OE2 GLU B 199 27.771 18.872 46.543 1.00 19.32 O ATOM 1585 N MET B 200 28.765 21.753 41.840 1.00 14.75 N ATOM 1586 CA MET B 200 29.837 22.586 41.320 1.00 16.16 C ATOM 1587 C MET B 200 29.472 24.047 41.470 1.00 17.10 C ATOM 1588 O MET B 200 30.298 24.855 41.874 1.00 17.85 O ATOM 1589 CB MET B 200 30.182 22.214 39.888 1.00 16.56 C ATOM 1590 CG MET B 200 30.868 20.873 39.813 1.00 19.28 C ATOM 1591 SD MET B 200 31.319 20.468 38.152 1.00 23.74 S ATOM 1592 CE MET B 200 32.667 21.582 37.892 1.00 24.04 C ATOM 1593 N VAL B 201 28.229 24.381 41.172 1.00 16.03 N ATOM 1594 CA VAL B 201 27.775 25.751 41.343 1.00 17.02 C ATOM 1595 C VAL B 201 27.777 26.149 42.821 1.00 17.61 C ATOM 1596 O VAL B 201 28.221 27.252 43.178 1.00 18.08 O ATOM 1597 CB VAL B 201 26.391 25.928 40.728 1.00 16.40 C ATOM 1598 CG1 VAL B 201 25.829 27.309 41.028 1.00 17.48 C ATOM 1599 CG2 VAL B 201 26.484 25.716 39.221 1.00 15.88 C ATOM 1600 N GLN B 202 27.285 25.259 43.675 1.00 18.26 N ATOM 1601 CA GLN B 202 27.222 25.534 45.109 1.00 20.67 C ATOM 1602 C GLN B 202 28.630 25.690 45.678 1.00 21.80 C ATOM 1603 O GLN B 202 28.900 26.611 46.467 1.00 21.66 O ATOM 1604 CB GLN B 202 26.419 24.440 45.824 1.00 20.70 C ATOM 1605 CG GLN B 202 26.257 24.579 47.333 1.00 26.05 C ATOM 1606 CD GLN B 202 25.518 23.388 47.938 1.00 32.37 C ATOM 1607 OE1 GLN B 202 24.422 23.029 47.481 1.00 36.43 O ATOM 1608 NE2 GLN B 202 26.124 22.754 48.949 1.00 36.84 N ATOM 1609 N GLU B 203 29.557 24.841 45.253 1.00 23.01 N ATOM 1610 CA GLU B 203 30.911 24.965 45.800 1.00 25.83 C ATOM 1611 C GLU B 203 31.525 26.287 45.373 1.00 26.95 C ATOM 1612 O GLU B 203 32.273 26.915 46.145 1.00 26.56 O ATOM 1613 CB GLU B 203 31.796 23.797 45.386 1.00 26.07 C ATOM 1614 CG GLU B 203 31.378 22.477 45.996 1.00 30.56 C ATOM 1615 CD GLU B 203 32.478 21.442 45.875 1.00 35.45 C ATOM 1616 OE1 GLU B 203 32.730 20.978 44.746 1.00 37.36 O ATOM 1617 OE2 GLU B 203 33.111 21.130 46.908 1.00 38.30 O ATOM 1618 N ASP B 204 31.200 26.713 44.155 1.00 28.64 N ATOM 1619 CA ASP B 204 31.693 27.979 43.629 1.00 31.07 C ATOM 1620 C ASP B 204 31.028 29.137 44.349 1.00 32.61 C ATOM 1621 O ASP B 204 31.636 30.195 44.494 1.00 33.35 O ATOM 1622 CB ASP B 204 31.469 28.089 42.123 1.00 30.95 C ATOM 1623 CG ASP B 204 31.938 29.416 41.559 1.00 30.90 C ATOM 1624 OD1 ASP B 204 33.157 29.584 41.343 1.00 32.64 O ATOM 1625 OD2 ASP B 204 31.163 30.346 41.277 1.00 33.17 O ATOM 1626 N GLN B 205 29.799 28.936 44.812 1.00 34.76 N ATOM 1627 CA GLN B 205 29.106 29.967 45.573 1.00 37.37 C ATOM 1628 C GLN B 205 29.873 30.138 46.889 1.00 39.15 C ATOM 1629 O GLN B 205 30.080 31.263 47.369 1.00 38.67 O ATOM 1630 CB GLN B 205 27.646 29.592 45.806 1.00 37.45 C ATOM 1631 CG GLN B 205 26.782 30.731 46.331 1.00 39.22 C ATOM 1632 CD GLN B 205 26.425 31.731 45.252 1.00 42.07 C ATOM 1633 OE1 GLN B 205 25.837 31.368 44.224 1.00 43.99 O ATOM 1634 NE2 GLN B 205 26.777 32.992 45.474 1.00 43.51 N ATOM 1635 N LYS B 206 30.292 29.011 47.463 1.00 41.27 N ATOM 1636 CA LYS B 206 31.190 29.023 48.608 1.00 44.19 C ATOM 1637 C LYS B 206 32.457 29.555 47.988 1.00 45.42 C ATOM 1638 O LYS B 206 32.558 29.569 46.771 1.00 46.44 O ATOM 1639 CB LYS B 206 31.449 27.609 49.100 1.00 44.17 C ATOM 1640 CG LYS B 206 30.240 26.932 49.667 1.00 46.10 C ATOM 1641 CD LYS B 206 29.925 27.492 51.030 1.00 49.17 C ATOM 1642 CE LYS B 206 31.121 27.342 51.957 1.00 50.52 C ATOM 1643 NZ LYS B 206 31.531 25.918 52.120 1.00 50.83 N ATOM 1644 N ARG B 207 33.436 29.967 48.775 1.00 47.33 N ATOM 1645 CA ARG B 207 34.628 30.504 48.144 1.00 49.04 C ATOM 1646 C ARG B 207 34.158 31.748 47.417 1.00 49.79 C ATOM 1647 O ARG B 207 34.155 31.802 46.186 1.00 50.11 O ATOM 1648 CB ARG B 207 35.175 29.481 47.141 1.00 49.08 C ATOM 1649 CG ARG B 207 36.360 29.944 46.308 1.00 50.44 C ATOM 1650 CD ARG B 207 36.853 28.892 45.334 1.00 52.12 C ATOM 1651 NE ARG B 207 37.750 29.432 44.312 1.00 53.92 N ATOM 1652 CZ ARG B 207 37.363 30.209 43.302 1.00 54.75 C ATOM 1653 NH1 ARG B 207 36.087 30.555 43.172 1.00 54.24 N ATOM 1654 NH2 ARG B 207 38.255 30.646 42.416 1.00 55.23 N ATOM 1655 N MET B 208 33.733 32.745 48.185 1.00 50.84 N ATOM 1656 CA MET B 208 33.168 33.960 47.615 1.00 51.59 C ATOM 1657 C MET B 208 33.862 35.227 48.105 1.00 51.93 C ATOM 1658 O MET B 208 34.761 35.199 48.951 1.00 52.44 O ATOM 1659 CB MET B 208 31.687 34.034 47.961 1.00 51.83 C ATOM 1660 CG MET B 208 31.409 33.846 49.443 1.00 52.65 C ATOM 1661 SD MET B 208 29.648 33.695 49.809 1.00 55.52 S ATOM 1662 CE MET B 208 29.118 35.444 49.736 1.00 55.42 C TER 1663 MET B 208 HETATM 1664 MG MG A1002 14.301 26.819 34.431 1.00 8.17 MG HETATM 1665 I IOD A 1 16.778 12.078 24.003 1.00 35.47 I HETATM 1666 PG GTP A1001 16.170 29.372 34.012 1.00 8.55 P HETATM 1667 O1G GTP A1001 17.003 30.307 34.788 1.00 10.14 O HETATM 1668 O2G GTP A1001 15.748 28.149 34.805 1.00 10.00 O HETATM 1669 O3G GTP A1001 16.805 28.973 32.683 1.00 9.85 O HETATM 1670 O3B GTP A1001 14.792 30.202 33.722 1.00 7.70 O HETATM 1671 PB GTP A1001 13.536 29.615 32.927 1.00 8.80 P HETATM 1672 O1B GTP A1001 13.614 30.030 31.515 1.00 7.75 O HETATM 1673 O2B GTP A1001 13.257 28.145 33.233 1.00 7.22 O HETATM 1674 O3A GTP A1001 12.341 30.547 33.512 1.00 8.27 O HETATM 1675 PA GTP A1001 11.100 30.102 34.443 1.00 8.51 P HETATM 1676 O1A GTP A1001 10.249 29.074 33.793 1.00 8.55 O HETATM 1677 O2A GTP A1001 11.696 29.741 35.800 1.00 7.92 O HETATM 1678 O5' GTP A1001 10.268 31.469 34.528 1.00 12.36 O HETATM 1679 C5' GTP A1001 10.889 32.645 34.951 1.00 12.43 C HETATM 1680 C4' GTP A1001 9.771 33.602 35.394 1.00 16.21 C HETATM 1681 O4' GTP A1001 8.957 33.982 34.306 1.00 15.80 O HETATM 1682 C3' GTP A1001 8.821 32.946 36.383 1.00 18.08 C HETATM 1683 O3' GTP A1001 8.492 33.919 37.353 1.00 24.43 O HETATM 1684 C2' GTP A1001 7.572 32.605 35.625 1.00 19.76 C HETATM 1685 O2' GTP A1001 6.483 32.815 36.506 1.00 26.82 O HETATM 1686 C1' GTP A1001 7.594 33.706 34.585 1.00 15.49 C HETATM 1687 N9 GTP A1001 6.915 33.295 33.378 1.00 16.05 N HETATM 1688 C8 GTP A1001 7.066 32.144 32.643 1.00 13.54 C HETATM 1689 N7 GTP A1001 6.244 32.222 31.577 1.00 17.61 N HETATM 1690 C5 GTP A1001 5.550 33.393 31.627 1.00 16.32 C HETATM 1691 C6 GTP A1001 4.581 33.973 30.810 1.00 16.83 C HETATM 1692 O6 GTP A1001 4.137 33.458 29.762 1.00 18.58 O HETATM 1693 N1 GTP A1001 4.125 35.225 31.177 1.00 14.29 N HETATM 1694 C2 GTP A1001 4.587 35.862 32.306 1.00 13.78 C HETATM 1695 N2 GTP A1001 4.106 37.065 32.640 1.00 13.62 N HETATM 1696 N3 GTP A1001 5.551 35.296 33.109 1.00 14.42 N HETATM 1697 C4 GTP A1001 6.010 34.073 32.747 1.00 14.01 C HETATM 1698 I IOD B 2 35.503 10.507 32.127 1.00 30.96 I HETATM 1699 O HOH A1003 6.317 7.676 20.225 1.00 27.03 O HETATM 1700 O HOH A1004 13.707 10.586 15.200 1.00 16.29 O HETATM 1701 O HOH A1005 11.279 8.764 14.893 1.00 31.65 O HETATM 1702 O HOH A1006 14.278 11.592 21.413 1.00 16.16 O HETATM 1703 O HOH A1007 14.922 10.876 18.626 1.00 15.50 O HETATM 1704 O HOH A1008 18.885 10.771 21.145 1.00 28.52 O HETATM 1705 O HOH A1009 23.224 14.008 23.734 1.00 14.33 O HETATM 1706 O HOH A1010 23.541 15.537 26.133 1.00 14.16 O HETATM 1707 O HOH A1011 16.300 34.028 25.715 1.00 8.07 O HETATM 1708 O HOH A1012 14.759 35.917 29.793 1.00 12.81 O HETATM 1709 O HOH A1013 14.990 36.194 27.104 1.00 10.34 O HETATM 1710 O HOH A1014 13.858 38.201 31.101 1.00 13.43 O HETATM 1711 O HOH A1015 19.517 28.925 35.162 1.00 9.54 O HETATM 1712 O HOH A1016 16.896 34.550 36.658 1.00 17.11 O HETATM 1713 O HOH A1017 15.568 32.180 36.096 1.00 12.11 O HETATM 1714 O HOH A1018 13.374 31.222 37.378 1.00 15.30 O HETATM 1715 O HOH A1019 14.191 23.967 37.509 1.00 10.37 O HETATM 1716 O HOH A1020 15.956 22.664 39.284 1.00 11.19 O HETATM 1717 O HOH A1021 15.429 26.157 32.798 1.00 9.64 O HETATM 1718 O HOH A1022 13.239 27.420 36.048 1.00 7.42 O HETATM 1719 O HOH A1023 12.090 24.637 39.186 1.00 10.54 O HETATM 1720 O HOH A1024 9.548 23.848 38.502 1.00 13.73 O HETATM 1721 O HOH A1025 6.807 30.494 30.051 1.00 20.25 O HETATM 1722 O HOH A1026 6.223 29.286 36.758 1.00 12.55 O HETATM 1723 O HOH A1027 4.417 25.025 34.465 1.00 9.40 O HETATM 1724 O HOH A1028 13.595 16.182 34.974 1.00 21.38 O HETATM 1725 O HOH A1029 12.752 20.532 38.962 1.00 22.68 O HETATM 1726 O HOH A1030 -0.586 21.837 28.208 1.00 22.99 O HETATM 1727 O HOH A1031 0.626 17.635 26.640 1.00 32.13 O HETATM 1728 O HOH A1032 2.938 13.556 27.567 1.00 21.53 O HETATM 1729 O HOH A1033 1.709 15.656 28.296 1.00 28.03 O HETATM 1730 O HOH A1034 -3.591 19.392 34.164 1.00 15.76 O HETATM 1731 O HOH A1035 -2.185 26.242 35.843 1.00 14.86 O HETATM 1732 O HOH A1036 -4.359 26.276 29.687 1.00 30.72 O HETATM 1733 O HOH A1037 3.861 24.831 42.176 1.00 12.85 O HETATM 1734 O HOH A1038 9.598 25.982 42.737 1.00 15.41 O HETATM 1735 O HOH A1039 10.297 27.791 44.596 1.00 15.71 O HETATM 1736 O HOH A1040 2.398 26.244 43.978 1.00 11.15 O HETATM 1737 O HOH A1041 3.975 30.606 39.580 1.00 20.36 O HETATM 1738 O HOH A1042 4.589 32.108 41.308 1.00 19.73 O HETATM 1739 O HOH A1043 7.884 30.378 38.830 1.00 14.38 O HETATM 1740 O HOH A1044 18.038 28.348 41.850 1.00 15.61 O HETATM 1741 O HOH A1045 17.758 24.520 40.174 1.00 10.17 O HETATM 1742 O HOH A1046 23.197 25.190 31.471 1.00 8.74 O HETATM 1743 O HOH A1047 22.785 22.734 32.656 1.00 8.90 O HETATM 1744 O HOH A1048 17.197 20.495 38.114 1.00 11.23 O HETATM 1745 O HOH A1049 9.061 12.314 31.237 1.00 14.35 O HETATM 1746 O HOH A1050 8.012 12.538 34.720 1.00 29.74 O HETATM 1747 O HOH A1051 0.155 10.986 21.127 1.00 25.38 O HETATM 1748 O HOH A1052 3.212 13.661 13.729 1.00 25.42 O HETATM 1749 O HOH A1053 12.001 10.853 22.596 1.00 13.50 O HETATM 1750 O HOH A1054 22.302 35.396 33.767 1.00 17.30 O HETATM 1751 O HOH A1055 24.957 33.988 36.573 1.00 14.62 O HETATM 1752 O HOH A1056 27.623 26.301 25.620 1.00 20.81 O HETATM 1753 O HOH A1057 26.319 27.628 23.357 1.00 15.68 O HETATM 1754 O HOH A1058 25.279 30.277 23.281 1.00 17.76 O HETATM 1755 O HOH A1059 31.073 22.792 21.422 1.00 35.62 O HETATM 1756 O HOH A1060 27.197 17.786 22.712 1.00 11.06 O HETATM 1757 O HOH A1061 30.479 18.054 25.540 1.00 17.25 O HETATM 1758 O HOH A1062 24.558 16.024 16.845 1.00 17.17 O HETATM 1759 O HOH A1063 30.361 11.594 19.302 1.00 15.85 O HETATM 1760 O HOH A1064 29.727 11.313 23.197 1.00 12.58 O HETATM 1761 O HOH A1065 25.596 9.721 20.229 1.00 19.35 O HETATM 1762 O HOH A1066 16.471 14.451 12.824 1.00 30.68 O HETATM 1763 O HOH A1067 16.355 17.774 12.672 1.00 19.37 O HETATM 1764 O HOH A1068 15.918 38.365 26.315 1.00 21.01 O HETATM 1765 O HOH A1069 10.234 40.636 31.656 1.00 17.30 O HETATM 1766 O HOH A1070 13.714 45.405 29.523 1.00 30.90 O HETATM 1767 O HOH A1071 16.405 42.685 31.922 1.00 26.10 O HETATM 1768 O HOH A1072 21.966 42.289 28.061 1.00 17.74 O HETATM 1769 O HOH A1073 21.239 42.796 25.528 1.00 13.92 O HETATM 1770 O HOH A1074 19.050 44.362 24.082 1.00 15.45 O HETATM 1771 O HOH A1075 13.734 38.734 33.837 1.00 22.95 O HETATM 1772 O HOH A1076 15.475 38.225 35.990 1.00 27.14 O HETATM 1773 O HOH A1077 19.947 41.214 12.608 1.00 12.94 O HETATM 1774 O HOH A1078 17.636 42.598 12.001 1.00 17.12 O HETATM 1775 O HOH A1079 21.467 39.933 10.849 1.00 13.39 O HETATM 1776 O HOH A1080 14.341 41.366 9.870 1.00 13.70 O HETATM 1777 O HOH A1081 15.922 43.671 10.147 1.00 17.39 O HETATM 1778 O HOH A1082 27.194 35.493 18.857 1.00 22.24 O HETATM 1779 O HOH A1083 26.169 36.579 26.123 1.00 40.03 O HETATM 1780 O HOH A1084 26.086 31.648 14.047 1.00 25.82 O HETATM 1781 O HOH A1085 28.238 27.465 21.472 1.00 19.78 O HETATM 1782 O HOH A1086 24.895 24.588 13.388 1.00 16.98 O HETATM 1783 O HOH A1087 21.713 28.725 10.665 1.00 16.87 O HETATM 1784 O HOH A1088 23.490 31.323 9.777 1.00 16.95 O HETATM 1785 O HOH A1089 29.571 21.422 17.824 1.00 15.53 O HETATM 1786 O HOH A1090 31.594 23.595 15.545 1.00 20.94 O HETATM 1787 O HOH A1091 21.773 15.798 6.823 1.00 47.28 O HETATM 1788 O HOH A1092 13.446 19.450 8.696 1.00 17.68 O HETATM 1789 O HOH A1093 7.702 37.141 34.056 1.00 17.16 O HETATM 1790 O HOH A1094 8.376 36.812 36.734 1.00 23.73 O HETATM 1791 O HOH A1095 4.507 38.471 35.232 1.00 24.48 O HETATM 1792 O HOH A1096 11.136 37.406 34.824 1.00 22.31 O HETATM 1793 O HOH A1097 0.188 34.384 22.322 1.00 15.97 O HETATM 1794 O HOH A1098 3.120 32.477 34.392 1.00 31.57 O HETATM 1795 O HOH A1099 0.602 35.271 32.842 1.00 34.59 O HETATM 1796 O HOH A1100 4.091 39.812 14.907 1.00 21.75 O HETATM 1797 O HOH A1101 7.869 31.836 11.411 1.00 14.83 O HETATM 1798 O HOH A1102 3.045 33.690 16.219 1.00 17.22 O HETATM 1799 O HOH A1103 2.885 31.873 14.430 1.00 35.77 O HETATM 1800 O HOH A1104 5.366 32.159 12.443 1.00 22.95 O HETATM 1801 O HOH A1105 8.317 34.248 10.174 1.00 22.73 O HETATM 1802 O HOH A1106 0.550 32.806 13.075 1.00 38.42 O HETATM 1803 O HOH A1107 8.382 36.681 11.708 1.00 15.35 O HETATM 1804 O HOH A1108 9.987 40.845 10.262 1.00 38.12 O HETATM 1805 O HOH A1109 9.116 38.627 9.722 1.00 27.21 O HETATM 1806 O HOH A1110 15.552 39.012 10.923 1.00 10.89 O HETATM 1807 O HOH A1111 13.686 49.047 19.230 1.00 39.99 O HETATM 1808 O HOH A1112 13.324 37.868 3.592 1.00 18.58 O HETATM 1809 O HOH A1113 23.688 35.313 10.966 1.00 13.64 O HETATM 1810 O HOH A1114 17.789 29.238 6.339 1.00 19.42 O HETATM 1811 O HOH A1115 17.586 27.652 4.312 1.00 35.79 O HETATM 1812 O HOH A1116 10.986 26.283 7.194 1.00 44.78 O HETATM 1813 O HOH A1117 9.383 30.406 9.319 1.00 19.62 O HETATM 1814 O HOH A1118 12.868 28.371 7.484 1.00 23.36 O HETATM 1815 O HOH A1119 1.917 28.325 13.988 1.00 25.15 O HETATM 1816 O HOH A1120 2.072 25.425 13.765 1.00 23.57 O HETATM 1817 O HOH A1121 2.132 36.123 16.022 1.00 33.01 O HETATM 1818 O HOH A1122 -1.263 25.781 22.062 1.00 18.08 O HETATM 1819 O HOH A1123 -0.423 24.547 14.066 1.00 23.72 O HETATM 1820 O HOH A1124 7.091 22.389 9.822 1.00 20.17 O HETATM 1821 O HOH A1125 4.338 23.222 9.569 1.00 36.70 O HETATM 1822 O HOH A1126 3.403 25.065 11.262 1.00 31.07 O HETATM 1823 O HOH A1127 6.522 11.505 12.197 1.00 19.27 O HETATM 1824 O HOH A1128 13.642 6.509 17.806 1.00 41.31 O HETATM 1825 O HOH A1129 24.512 11.499 23.481 1.00 19.18 O HETATM 1826 O HOH A1130 14.857 36.132 37.493 1.00 24.02 O HETATM 1827 O HOH A1131 22.089 37.574 31.603 1.00 24.95 O HETATM 1828 O HOH A1132 10.156 21.156 39.168 1.00 26.59 O HETATM 1829 O HOH A1133 14.358 21.466 41.158 1.00 20.26 O HETATM 1830 O HOH A1134 -2.671 27.230 33.118 1.00 33.61 O HETATM 1831 O HOH A1135 0.541 16.530 24.423 1.00 22.01 O HETATM 1832 O HOH A1136 -0.713 18.543 29.626 1.00 28.22 O HETATM 1833 O HOH A1137 -1.729 28.117 38.137 1.00 31.15 O HETATM 1834 O HOH A1138 7.294 30.892 41.239 1.00 32.12 O HETATM 1835 O HOH A1139 9.015 30.380 42.818 1.00 21.55 O HETATM 1836 O HOH A1140 11.819 31.293 39.756 1.00 25.47 O HETATM 1837 O HOH A1141 11.930 30.399 44.818 1.00 26.26 O HETATM 1838 O HOH A1142 16.756 29.526 44.051 1.00 22.22 O HETATM 1839 O HOH A1143 19.721 32.888 40.729 1.00 23.95 O HETATM 1840 O HOH A1144 20.280 30.313 41.562 1.00 24.35 O HETATM 1841 O HOH A1145 19.261 24.075 42.393 1.00 18.46 O HETATM 1842 O HOH A1146 19.049 26.592 43.726 1.00 23.31 O HETATM 1843 O HOH A1147 14.879 17.653 37.201 1.00 19.46 O HETATM 1844 O HOH A1148 23.552 35.929 35.818 1.00 29.27 O HETATM 1845 O HOH A1149 27.564 33.656 27.811 1.00 28.24 O HETATM 1846 O HOH A1150 30.855 30.051 33.859 1.00 28.36 O HETATM 1847 O HOH A1151 30.046 26.804 24.937 1.00 30.49 O HETATM 1848 O HOH A1152 29.597 20.380 22.126 1.00 26.07 O HETATM 1849 O HOH A1153 18.937 12.296 17.256 1.00 32.65 O HETATM 1850 O HOH A1154 22.391 11.870 15.763 1.00 26.83 O HETATM 1851 O HOH A1155 14.094 39.659 24.956 1.00 18.87 O HETATM 1852 O HOH A1156 5.045 44.739 30.354 1.00 26.72 O HETATM 1853 O HOH A1157 12.397 42.273 31.772 1.00 25.55 O HETATM 1854 O HOH A1158 7.703 49.978 24.173 1.00 36.48 O HETATM 1855 O HOH A1159 20.207 46.552 22.984 1.00 35.47 O HETATM 1856 O HOH A1160 22.706 40.626 31.373 1.00 30.78 O HETATM 1857 O HOH A1161 26.337 38.992 25.055 1.00 29.04 O HETATM 1858 O HOH A1162 28.195 15.186 18.569 1.00 33.41 O HETATM 1859 O HOH A1163 22.850 18.324 13.694 1.00 20.32 O HETATM 1860 O HOH A1164 0.772 41.934 25.048 1.00 30.94 O HETATM 1861 O HOH A1165 -2.848 34.365 30.494 1.00 41.46 O HETATM 1862 O HOH A1166 6.247 44.479 18.857 1.00 22.10 O HETATM 1863 O HOH A1167 3.070 41.411 21.158 1.00 24.61 O HETATM 1864 O HOH A1168 3.216 38.345 17.855 1.00 28.09 O HETATM 1865 O HOH A1169 5.990 36.566 12.492 1.00 30.68 O HETATM 1866 O HOH A1170 7.508 47.263 20.773 1.00 24.85 O HETATM 1867 O HOH A1171 10.246 47.860 20.787 1.00 39.04 O HETATM 1868 O HOH A1172 13.550 46.171 15.627 1.00 34.52 O HETATM 1869 O HOH A1173 15.160 46.100 22.737 1.00 23.83 O HETATM 1870 O HOH A1174 17.095 46.253 20.601 1.00 34.88 O HETATM 1871 O HOH A1175 16.418 32.557 6.860 1.00 13.98 O HETATM 1872 O HOH A1176 22.635 24.303 9.022 1.00 33.00 O HETATM 1873 O HOH A1177 14.745 29.428 6.225 1.00 30.77 O HETATM 1874 O HOH A1178 10.020 23.372 5.717 1.00 30.30 O HETATM 1875 O HOH A1179 8.244 26.493 7.978 1.00 29.56 O HETATM 1876 O HOH A1180 7.562 29.074 7.831 1.00 26.84 O HETATM 1877 O HOH A1181 -2.303 31.164 19.779 1.00 36.35 O HETATM 1878 O HOH A1182 -3.203 24.386 25.990 1.00 30.90 O HETATM 1879 O HOH A1183 -2.925 28.816 20.855 1.00 24.34 O HETATM 1880 O HOH A1184 10.030 9.955 12.324 1.00 31.41 O HETATM 1881 O HOH A1185 11.426 18.482 7.009 1.00 32.31 O HETATM 1882 O HOH A1186 32.354 24.120 30.401 1.00 35.35 O HETATM 1883 O HOH A1187 18.254 34.596 39.216 1.00 23.22 O HETATM 1884 O HOH A1188 -4.748 25.173 33.098 1.00 39.78 O HETATM 1885 O HOH A1189 -5.860 23.015 33.352 1.00 29.33 O HETATM 1886 O HOH A1190 11.786 8.196 23.341 1.00 23.01 O HETATM 1887 O HOH A1191 29.495 29.916 26.461 1.00 39.88 O HETATM 1888 O HOH A1192 31.371 19.854 23.895 1.00 32.00 O HETATM 1889 O HOH A1193 30.118 28.680 19.338 1.00 41.59 O HETATM 1890 O HOH A1194 4.351 35.777 36.734 1.00 36.46 O HETATM 1891 O HOH A1195 -0.092 39.224 32.715 1.00 25.78 O HETATM 1892 O HOH A1196 5.835 10.504 28.439 1.00 27.74 O HETATM 1893 O HOH A1197 12.580 31.606 42.196 1.00 29.73 O HETATM 1894 O HOH A1198 16.404 32.096 43.716 1.00 38.65 O HETATM 1895 O HOH A1199 1.618 43.268 23.119 1.00 27.92 O HETATM 1896 O HOH A1200 1.994 16.932 12.177 1.00 37.42 O HETATM 1897 O HOH A1201 3.182 9.372 21.369 1.00 39.27 O HETATM 1898 O HOH A1202 -1.712 14.028 20.386 1.00 36.51 O HETATM 1899 O HOH A1203 13.550 9.795 26.350 1.00 26.29 O HETATM 1900 O HOH A1204 27.421 34.888 36.831 1.00 36.45 O HETATM 1901 O HOH A1205 22.475 14.481 15.060 1.00 29.16 O HETATM 1902 O HOH A1206 11.932 44.397 31.297 1.00 39.31 O HETATM 1903 O HOH A1207 20.882 46.249 27.197 1.00 34.26 O HETATM 1904 O HOH A1208 21.636 43.716 30.352 1.00 34.83 O HETATM 1905 O HOH A1209 23.549 43.479 24.310 1.00 20.12 O HETATM 1906 O HOH A1210 31.594 19.805 16.819 1.00 30.53 O HETATM 1907 O HOH A1211 26.409 17.206 12.590 1.00 38.47 O HETATM 1908 O HOH A1212 17.902 18.898 9.070 1.00 28.36 O HETATM 1909 O HOH A1213 19.381 22.545 10.243 1.00 29.00 O HETATM 1910 O HOH A1214 15.971 20.261 8.069 1.00 24.00 O HETATM 1911 O HOH A1215 13.380 21.249 4.292 1.00 33.13 O HETATM 1912 O HOH A1216 -2.918 39.303 29.184 1.00 44.05 O HETATM 1913 O HOH A1217 -3.133 35.974 28.736 1.00 31.29 O HETATM 1914 O HOH A1218 -2.873 38.084 32.123 1.00 41.76 O HETATM 1915 O HOH A1219 15.643 45.124 14.800 1.00 30.82 O HETATM 1916 O HOH A1220 15.123 45.744 11.877 1.00 20.51 O HETATM 1917 O HOH A1221 25.192 29.021 8.141 1.00 33.38 O HETATM 1918 O HOH A1222 17.707 23.582 5.562 1.00 38.05 O HETATM 1919 O HOH A1223 9.797 20.655 5.934 1.00 34.93 O HETATM 1920 O HOH A1224 19.114 37.748 35.250 1.00 30.72 O HETATM 1921 O HOH A1225 -5.544 28.589 30.816 1.00 43.80 O HETATM 1922 O HOH A1226 14.330 33.584 42.167 1.00 46.06 O HETATM 1923 O HOH A1227 6.774 8.325 26.837 1.00 38.06 O HETATM 1924 O HOH A1228 28.857 32.271 30.059 1.00 38.11 O HETATM 1925 O HOH A1229 32.054 26.876 26.430 1.00 35.41 O HETATM 1926 O HOH A1230 29.863 15.826 21.445 1.00 27.00 O HETATM 1927 O HOH A1231 20.271 17.036 14.342 1.00 30.53 O HETATM 1928 O HOH A1232 20.066 20.115 7.333 1.00 34.08 O HETATM 1929 O HOH A1233 3.965 37.687 13.381 1.00 38.32 O HETATM 1930 O HOH A1234 17.006 48.896 19.741 1.00 31.61 O HETATM 1931 O HOH A1235 11.239 39.184 5.127 1.00 26.64 O HETATM 1932 O HOH A1236 17.660 21.988 43.777 1.00 25.94 O HETATM 1933 O HOH A1237 15.752 22.985 45.037 1.00 30.61 O HETATM 1934 O HOH A1238 8.243 45.252 33.011 1.00 41.38 O HETATM 1935 O HOH A1239 25.180 40.994 24.848 1.00 44.83 O HETATM 1936 O HOH A1240 19.560 17.462 5.809 1.00 43.97 O HETATM 1937 O HOH A1241 8.884 34.642 7.752 1.00 31.81 O HETATM 1938 O HOH A1242 13.389 47.930 22.400 1.00 34.09 O HETATM 1939 O HOH A1243 -4.268 32.939 20.457 1.00 43.79 O HETATM 1940 O HOH B 211 28.348 29.518 41.394 1.00 22.39 O HETATM 1941 O HOH B 212 32.009 21.717 31.509 1.00 21.13 O HETATM 1942 O HOH B 213 31.300 13.518 24.266 1.00 22.39 O HETATM 1943 O HOH B 214 44.202 16.182 36.854 1.00 13.36 O HETATM 1944 O HOH B 215 43.992 13.387 36.242 1.00 11.88 O HETATM 1945 O HOH B 216 41.250 12.766 37.064 1.00 17.11 O HETATM 1946 O HOH B 217 39.170 14.514 37.849 1.00 26.07 O HETATM 1947 O HOH B 218 40.358 11.459 34.726 1.00 24.88 O HETATM 1948 O HOH B 219 17.201 10.476 35.034 1.00 16.64 O HETATM 1949 O HOH B 220 15.443 9.630 36.941 1.00 14.97 O HETATM 1950 O HOH B 221 15.803 9.527 32.788 1.00 26.08 O HETATM 1951 O HOH B 222 17.453 13.398 35.344 1.00 17.68 O HETATM 1952 O HOH B 223 17.902 14.719 37.640 1.00 15.32 O HETATM 1953 O HOH B 224 21.544 11.691 27.411 1.00 23.24 O HETATM 1954 O HOH B 225 14.791 13.697 35.256 1.00 22.17 O HETATM 1955 O HOH B 226 34.571 21.296 35.127 1.00 25.33 O HETATM 1956 O HOH B 227 34.657 8.932 35.473 1.00 22.74 O HETATM 1957 O HOH B 228 20.430 2.840 28.551 1.00 34.88 O HETATM 1958 O HOH B 229 20.563 2.213 33.138 1.00 28.59 O HETATM 1959 O HOH B 230 46.037 12.087 32.019 1.00 25.52 O HETATM 1960 O HOH B 231 28.450 21.797 47.150 1.00 27.49 O HETATM 1961 O HOH B 232 29.276 23.584 48.795 1.00 27.71 O HETATM 1962 O HOH B 233 37.117 18.494 28.926 1.00 30.37 O HETATM 1963 O HOH B 234 43.968 12.946 33.633 1.00 27.70 O HETATM 1964 O HOH B 235 36.968 12.663 34.314 1.00 25.76 O HETATM 1965 O HOH B 236 43.826 17.693 34.497 1.00 24.49 O HETATM 1966 O HOH B 237 23.453 24.688 43.119 1.00 25.36 O HETATM 1967 O HOH B 238 39.854 16.994 38.781 1.00 24.20 O HETATM 1968 O HOH B 239 34.099 25.804 48.064 1.00 27.48 O HETATM 1969 O HOH B 240 34.498 17.924 27.883 1.00 29.64 O HETATM 1970 O HOH B 241 35.934 22.892 37.488 1.00 29.97 O HETATM 1971 O HOH B 242 32.357 20.783 34.754 1.00 28.49 O HETATM 1972 O HOH B 243 17.189 7.058 28.730 1.00 37.29 O HETATM 1973 O HOH B 244 17.365 9.748 27.858 1.00 34.67 O HETATM 1974 O HOH B 245 26.998 27.590 48.295 1.00 38.34 O HETATM 1975 O HOH B 246 27.747 24.759 50.727 1.00 41.53 O HETATM 1976 O HOH B 247 13.591 11.456 33.947 1.00 26.51 O CONECT 109 1664 CONECT 242 1664 CONECT 1664 109 242 1668 1673 CONECT 1664 1717 1718 CONECT 1666 1667 1668 1669 1670 CONECT 1667 1666 CONECT 1668 1664 1666 CONECT 1669 1666 CONECT 1670 1666 1671 CONECT 1671 1670 1672 1673 1674 CONECT 1672 1671 CONECT 1673 1664 1671 CONECT 1674 1671 1675 CONECT 1675 1674 1676 1677 1678 CONECT 1676 1675 CONECT 1677 1675 CONECT 1678 1675 1679 CONECT 1679 1678 1680 CONECT 1680 1679 1681 1682 CONECT 1681 1680 1686 CONECT 1682 1680 1683 1684 CONECT 1683 1682 CONECT 1684 1682 1685 1686 CONECT 1685 1684 CONECT 1686 1681 1684 1687 CONECT 1687 1686 1688 1697 CONECT 1688 1687 1689 CONECT 1689 1688 1690 CONECT 1690 1689 1691 1697 CONECT 1691 1690 1692 1693 CONECT 1692 1691 CONECT 1693 1691 1694 CONECT 1694 1693 1695 1696 CONECT 1695 1694 CONECT 1696 1694 1697 CONECT 1697 1687 1690 1696 CONECT 1717 1664 CONECT 1718 1664 MASTER 300 0 4 10 6 0 11 6 1974 2 38 17 END
Display Options:
Goto PDB code:
3D presentation of molecule is powered by
3Dmol
, which supports all modern browsers and mobile devices via WebGL.
Hold mouse button:
left to rotate,middle to shift,right to zoom
Related entries of code: 1j2j
Entries with 90% protein sequence similarity cutoff in PDBbind
PDB Code
Check Database
Protein Sequence Similarity
No similar entries are found!
Complexes with the same small molecule ligand
PDB Code
Check Database
Ligand Name
1e96
RCSB PDB
PDBbind
protein
1efx
RCSB PDB
PDBbind
protein
1ffx
RCSB PDB
PDBbind
protein
1gua
RCSB PDB
PDBbind
protein
1i4d
RCSB PDB
PDBbind
protein
1kxp
RCSB PDB
PDBbind
protein
1mi5
RCSB PDB
PDBbind
protein
1nf3
RCSB PDB
PDBbind
protein
1p1z
RCSB PDB
PDBbind
protein
1p4l
RCSB PDB
PDBbind
protein
1rv6
RCSB PDB
PDBbind
protein
1shz
RCSB PDB
PDBbind
protein
1t44
RCSB PDB
PDBbind
protein
1uad
RCSB PDB
PDBbind
protein
1vg0
RCSB PDB
PDBbind
protein
1w1w
RCSB PDB
PDBbind
protein
1w72
RCSB PDB
PDBbind
protein
1y4a
RCSB PDB
PDBbind
protein
1zc3
RCSB PDB
PDBbind
protein
1zc4
RCSB PDB
PDBbind
protein
2a78
RCSB PDB
PDBbind
protein
Entry Information
PDB ID
1j2j
Complex Type
Protein-Protein
PDBbind Subset
general set
Protein Name
adp-ribosylation factor 1
Ligand Name
protein
EC.Number
E.C.-.-.-.-
Resolution
1.6(Å)
Affinity (Kd/Ki/IC50)
Kd=1.4uM
Release Year
2003
Protein/NA Sequence
Check fasta file
Primary Reference
NAT.STRUCT.BIOL. v10 pp. 386-93, 2003
Links to External Databases
RCSB PDB
The mother database
PDBsum
Enhanced annotations on PDB entries
Pubchem
Comprehensive collection of chemical and biological data
UniProtKB AC
UniProt accession number (AC):
Q8BSL7
Q9UJY5
Entrez Gene ID
NCBI Entrez Gene ID:
11841
26088
ASD
Information of known allosteric effects of PDB entries
This site has been visited
times since Nov 2007.
Copyright ©2007-2024 涓婃捣鐩堣禌鎬濅俊鎭鎶鏈夐檺鍏徃 缃戠珯澶囨鍙凤細
娌狪CP澶2021015625鍙-3
娌叕缃戝畨澶囷細
姝e湪鐢宠涓
Technical Support锛堟妧鏈敮鎸侊級:
yingsaisi@foxmail.com