HEADER TRANSFERASE 18-JAN-13 3W51
TITLE TANKYRASE IN COMPLEX WITH 2-HYDROXY-4-METHYLQUINOLINE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 952-1161;
COMPND 5 SYNONYM: TANK2, ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 6,
COMPND 6 ARTD6, POLY [ADP-RIBOSE] POLYMERASE 5B, TNKS-2, TRF1-INTERACTING
COMPND 7 ANKYRIN-RELATED ADP-RIBOSE POLYMERASE 2, TANKYRASE II, TANKYRASE-LIKE
COMPND 8 PROTEIN, TANKYRASE-RELATED PROTEIN;
COMPND 9 EC: 2.4.2.30;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PARP5B, TANK2, TNKL, TNKS2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ESCHERICHIA COLI BL21(DE3) R3 PRARE;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS RIBOSYLATION, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.E.JANSSON,E.A.LARSSON,P.L.NORDLUND
REVDAT 2 08-NOV-23 3W51 1 REMARK LINK
REVDAT 1 10-JUL-13 3W51 0
JRNL AUTH E.A.LARSSON,A.E.JANSSON,F.M.NG,S.W.THEN,R.PANICKER,B.LIU,
JRNL AUTH 2 K.SANGTHONGPITAG,V.PENDHARKAR,S.J.TAI,J.HILL,C.DAN,S.Y.HO,
JRNL AUTH 3 W.W.CHEONG,A.POULSEN,S.BLANCHARD,G.R.LIN,J.ALAM,T.H.KELLER,
JRNL AUTH 4 P.NORDLUND
JRNL TITL FRAGMENT-BASED LIGAND DESIGN OF NOVEL POTENT INHIBITORS OF
JRNL TITL 2 TANKYRASES.
JRNL REF J.MED.CHEM. V. 56 4497 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23672613
JRNL DOI 10.1021/JM400211F
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0109
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 35490
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) : 0.190
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.243
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1780
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.00
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.05
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2450
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.19
REMARK 3 BIN R VALUE (WORKING SET) : 0.2180
REMARK 3 BIN FREE R VALUE SET COUNT : 128
REMARK 3 BIN FREE R VALUE : 0.2980
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3354
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 46
REMARK 3 SOLVENT ATOMS : 315
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.56
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.62000
REMARK 3 B22 (A**2) : 0.20000
REMARK 3 B33 (A**2) : -0.82000
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): 0.171
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.166
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.113
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.962
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.927
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3502 ; 0.023 ; 0.021
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4722 ; 1.833 ; 1.942
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 422 ; 6.235 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;34.359 ;22.967
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 582 ;15.097 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 28 ;17.965 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 468 ; 0.133 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 2736 ; 0.010 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 2078 ; 1.185 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3330 ; 2.037 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1424 ; 3.314 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1388 ; 5.087 ; 4.500
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS U VALUES: REFINED INDIVIDUALLY
REMARK 4
REMARK 4 3W51 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 29-JAN-13.
REMARK 100 THE DEPOSITION ID IS D_1000095894.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-FEB-11
REMARK 200 TEMPERATURE (KELVIN) : 277
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : AUSTRALIAN SYNCHROTRON
REMARK 200 BEAMLINE : MX1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : NULL
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 36841
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 66.930
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : 0.05600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.4000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASES
REMARK 200 STARTING MODEL: 3KR7
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.76
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.72
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 17% PEG 3350, 0.2M AMMONIUMSULPHATE,
REMARK 280 0.1M TRIS PH 8.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.24850
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.24850
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 47.13800
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.51900
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 47.13800
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.51900
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 58.24850
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 47.13800
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.51900
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 58.24850
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 47.13800
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.51900
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 1114
REMARK 465 LYS B 1114
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 TYR B1009 CE2 TYR B1009 CD2 0.096
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 ALA B1057 85.41 -69.55
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 ZN A1202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1081 SG
REMARK 620 2 HIS A1084 ND1 110.2
REMARK 620 3 CYS A1089 SG 113.2 108.8
REMARK 620 4 CYS A1092 SG 115.0 98.1 110.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1202 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1081 SG
REMARK 620 2 HIS B1084 ND1 112.5
REMARK 620 3 CYS B1089 SG 111.0 99.7
REMARK 620 4 CYS B1092 SG 118.3 102.0 111.5
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AJ2 A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AJ2 B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4IUE RELATED DB: PDB
DBREF 3W51 A 952 1161 UNP Q9H2K2 TNKS2_HUMAN 952 1161
DBREF 3W51 B 952 1161 UNP Q9H2K2 TNKS2_HUMAN 952 1161
SEQRES 1 A 210 GLY THR ILE LEU ILE ASP LEU SER PRO ASP ASP LYS GLU
SEQRES 2 A 210 PHE GLN SER VAL GLU GLU GLU MET GLN SER THR VAL ARG
SEQRES 3 A 210 GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY ILE PHE ASN
SEQRES 4 A 210 ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL CYS ASN LYS
SEQRES 5 A 210 LYS LEU TRP GLU ARG TYR THR HIS ARG ARG LYS GLU VAL
SEQRES 6 A 210 SER GLU GLU ASN HIS ASN HIS ALA ASN GLU ARG MET LEU
SEQRES 7 A 210 PHE HIS GLY SER PRO PHE VAL ASN ALA ILE ILE HIS LYS
SEQRES 8 A 210 GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY GLY MET PHE
SEQRES 9 A 210 GLY ALA GLY ILE TYR PHE ALA GLU ASN SER SER LYS SER
SEQRES 10 A 210 ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY THR GLY CYS
SEQRES 11 A 210 PRO VAL HIS LYS ASP ARG SER CYS TYR ILE CYS HIS ARG
SEQRES 12 A 210 GLN LEU LEU PHE CYS ARG VAL THR LEU GLY LYS SER PHE
SEQRES 13 A 210 LEU GLN PHE SER ALA MET LYS MET ALA HIS SER PRO PRO
SEQRES 14 A 210 GLY HIS HIS SER VAL THR GLY ARG PRO SER VAL ASN GLY
SEQRES 15 A 210 LEU ALA LEU ALA GLU TYR VAL ILE TYR ARG GLY GLU GLN
SEQRES 16 A 210 ALA TYR PRO GLU TYR LEU ILE THR TYR GLN ILE MET ARG
SEQRES 17 A 210 PRO GLU
SEQRES 1 B 210 GLY THR ILE LEU ILE ASP LEU SER PRO ASP ASP LYS GLU
SEQRES 2 B 210 PHE GLN SER VAL GLU GLU GLU MET GLN SER THR VAL ARG
SEQRES 3 B 210 GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY ILE PHE ASN
SEQRES 4 B 210 ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL CYS ASN LYS
SEQRES 5 B 210 LYS LEU TRP GLU ARG TYR THR HIS ARG ARG LYS GLU VAL
SEQRES 6 B 210 SER GLU GLU ASN HIS ASN HIS ALA ASN GLU ARG MET LEU
SEQRES 7 B 210 PHE HIS GLY SER PRO PHE VAL ASN ALA ILE ILE HIS LYS
SEQRES 8 B 210 GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY GLY MET PHE
SEQRES 9 B 210 GLY ALA GLY ILE TYR PHE ALA GLU ASN SER SER LYS SER
SEQRES 10 B 210 ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY THR GLY CYS
SEQRES 11 B 210 PRO VAL HIS LYS ASP ARG SER CYS TYR ILE CYS HIS ARG
SEQRES 12 B 210 GLN LEU LEU PHE CYS ARG VAL THR LEU GLY LYS SER PHE
SEQRES 13 B 210 LEU GLN PHE SER ALA MET LYS MET ALA HIS SER PRO PRO
SEQRES 14 B 210 GLY HIS HIS SER VAL THR GLY ARG PRO SER VAL ASN GLY
SEQRES 15 B 210 LEU ALA LEU ALA GLU TYR VAL ILE TYR ARG GLY GLU GLN
SEQRES 16 B 210 ALA TYR PRO GLU TYR LEU ILE THR TYR GLN ILE MET ARG
SEQRES 17 B 210 PRO GLU
HET AJ2 A1201 12
HET ZN A1202 1
HET SO4 A1203 5
HET SO4 A1204 5
HET AJ2 B1201 12
HET ZN B1202 1
HET SO4 B1203 5
HET SO4 B1204 5
HETNAM AJ2 4-METHYLQUINOLIN-2-OL
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
FORMUL 3 AJ2 2(C10 H9 N O)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 11 HOH *315(H2 O)
HELIX 1 1 ASP A 962 THR A 975 1 14
HELIX 2 2 ASN A 1002 ASN A 1020 1 19
HELIX 3 3 PHE A 1035 GLY A 1043 1 9
HELIX 4 4 ASP A 1045 ALA A 1049 5 5
HELIX 5 5 ASN A 1064 GLN A 1070 1 7
HELIX 6 6 GLY A 1074 GLY A 1078 5 5
HELIX 7 7 ARG A 1143 GLU A 1145 5 3
HELIX 8 8 ASP B 962 THR B 975 1 14
HELIX 9 9 ASN B 1002 ASN B 1020 1 19
HELIX 10 10 PHE B 1035 GLY B 1043 1 9
HELIX 11 11 ASP B 1045 ALA B 1049 5 5
HELIX 12 12 ASN B 1064 GLN B 1070 1 7
HELIX 13 13 GLY B 1074 GLY B 1078 5 5
HELIX 14 14 ARG B 1143 GLU B 1145 5 3
SHEET 1 A 5 ILE A 954 ASP A 957 0
SHEET 2 A 5 TYR A 992 CYS A1001 -1 O CYS A1001 N ILE A 954
SHEET 3 A 5 ALA A1147 ILE A1157 -1 O THR A1154 N LEU A 995
SHEET 4 A 5 ARG A1094 THR A1102 -1 N ARG A1094 O TYR A1155
SHEET 5 A 5 GLU A1026 HIS A1031 -1 N LEU A1029 O CYS A1099
SHEET 1 B 4 ILE A1059 ALA A1062 0
SHEET 2 B 4 GLU A1138 ILE A1141 -1 O ILE A1141 N ILE A1059
SHEET 3 B 4 SER A1124 PRO A1129 -1 N GLY A1127 O GLU A1138
SHEET 4 B 4 SER A1106 SER A1111 1 N GLN A1109 O THR A1126
SHEET 1 C 5 ILE B 954 ASP B 957 0
SHEET 2 C 5 TYR B 992 CYS B1001 -1 O CYS B1001 N ILE B 954
SHEET 3 C 5 ALA B1147 ILE B1157 -1 O THR B1154 N LEU B 995
SHEET 4 C 5 ARG B1094 THR B1102 -1 N ARG B1094 O TYR B1155
SHEET 5 C 5 GLU B1026 HIS B1031 -1 N LEU B1029 O CYS B1099
SHEET 1 D 4 ILE B1059 ALA B1062 0
SHEET 2 D 4 GLU B1138 ILE B1141 -1 O ILE B1141 N ILE B1059
SHEET 3 D 4 SER B1124 PRO B1129 -1 N GLY B1127 O GLU B1138
SHEET 4 D 4 SER B1106 SER B1111 1 N GLN B1109 O THR B1126
LINK SG CYS A1081 ZN ZN A1202 1555 1555 2.29
LINK ND1 HIS A1084 ZN ZN A1202 1555 1555 2.19
LINK SG CYS A1089 ZN ZN A1202 1555 1555 2.26
LINK SG CYS A1092 ZN ZN A1202 1555 1555 2.42
LINK SG CYS B1081 ZN ZN B1202 1555 1555 2.27
LINK ND1 HIS B1084 ZN ZN B1202 1555 1555 2.18
LINK SG CYS B1089 ZN ZN B1202 1555 1555 2.37
LINK SG CYS B1092 ZN ZN B1202 1555 1555 2.28
SITE 1 AC1 8 PHE A1030 HIS A1031 GLY A1032 TYR A1050
SITE 2 AC1 8 TYR A1060 SER A1068 TYR A1071 GLU A1138
SITE 1 AC2 4 CYS A1081 HIS A1084 CYS A1089 CYS A1092
SITE 1 AC3 7 ARG A 977 HIS A 979 ARG A 980 LYS A1067
SITE 2 AC3 7 GLN A1070 HOH A1391 HOH A1428
SITE 1 AC4 7 ASN A 990 ARG A 991 PRO A1160 GLU A1161
SITE 2 AC4 7 HOH A1314 HOH A1399 HOH A1400
SITE 1 AC5 8 PHE B1030 HIS B1031 GLY B1032 TYR B1050
SITE 2 AC5 8 TYR B1060 SER B1068 TYR B1071 GLU B1138
SITE 1 AC6 4 CYS B1081 HIS B1084 CYS B1089 CYS B1092
SITE 1 AC7 6 ARG B 977 HIS B 979 ARG B 980 LYS B1067
SITE 2 AC7 6 GLN B1070 HOH B1401
SITE 1 AC8 6 ASN B 990 ARG B 991 PRO B1160 GLU B1161
SITE 2 AC8 6 HOH B1316 HOH B1374
CRYST1 94.276 95.038 116.497 90.00 90.00 90.00 C 2 2 21 16
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 0.010607 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010522 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008584 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
