HEADER TRANSFERASE 06-MAR-15 5AL4
TITLE CRYSTAL STRUCTURE OF TNKS2 IN COMPLEX WITH 2-(4-METHYLPIPERAZIN-1-YL)-
TITLE 2 3,4,5,6,7,8-HEXAHYDROQUINAZOLIN-4-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE 2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: CATALYTIC DOMAIN, RESIDUES 946-1162;
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, TANKYRASE 2;
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS TRANSFERASE, PROTEIN-LIGAND COMPLEX, DIPHTHERIA TOXIN LIKE FOLD, ADP-
KEYWDS 2 RIBOSYLATION, TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NKIZINKIKO,L.LEHTIO
REVDAT 3 10-JAN-24 5AL4 1 REMARK LINK
REVDAT 2 12-AUG-15 5AL4 1 JRNL
REVDAT 1 29-JUL-15 5AL4 0
JRNL AUTH Y.NKIZINKIKO,B.V.S.SUNEEL KUMAR,V.U.JEANKUMAR,T.HAIKARAINEN,
JRNL AUTH 2 J.KOIVUNEN,C.MADHURI,P.YOGEESWARI,H.VENKANNAGARI,E.OBAJI,
JRNL AUTH 3 T.PIHLAJANIEMI,D.SRIRAM,L.LEHTIO
JRNL TITL DISCOVERY OF POTENT AND SELECTIVE NONPLANAR TANKYRASE
JRNL TITL 2 INHIBITING NICOTINAMIDE MIMICS.
JRNL REF BIOORG.MED.CHEM. V. 23 4139 2015
JRNL REFN ISSN 0968-0896
JRNL PMID 26183543
JRNL DOI 10.1016/J.BMC.2015.06.063
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 39721
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) : 0.169
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.198
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2091
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.95
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2862
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 98.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.2470
REMARK 3 BIN FREE R VALUE SET COUNT : 151
REMARK 3 BIN FREE R VALUE : 0.2660
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3347
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 70
REMARK 3 SOLVENT ATOMS : 279
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 27.65
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.50000
REMARK 3 B22 (A**2) : -1.24000
REMARK 3 B33 (A**2) : 1.73000
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): 0.125
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.117
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.077
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.599
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.948
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3527 ; 0.013 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3257 ; 0.005 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4753 ; 1.537 ; 1.948
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7483 ; 1.104 ; 3.006
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 421 ; 6.144 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 183 ;33.542 ;22.787
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 583 ;13.558 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;15.643 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 473 ; 0.092 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4023 ; 0.008 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 909 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS.
REMARK 4
REMARK 4 5AL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1290063226.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 15-MAY-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I03
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.976250
REMARK 200 MONOCHROMATOR : WATER-COOLED SI(111) DOUBLE
REMARK 200 CRYSTAL MONOCHROMATOR
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 41813
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.08000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.4500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.95
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.60
REMARK 200 R MERGE FOR SHELL (I) : 0.80000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.370
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 3U9H
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 8.5
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 59.24500
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 59.24500
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 45.61000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 48.89000
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.61000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 48.89000
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.24500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.61000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 48.89000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.24500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.61000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 48.89000
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 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 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A2084 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B2064 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 923
REMARK 465 HIS A 924
REMARK 465 HIS A 925
REMARK 465 HIS A 926
REMARK 465 HIS A 927
REMARK 465 HIS A 928
REMARK 465 HIS A 929
REMARK 465 SER A 930
REMARK 465 SER A 931
REMARK 465 GLY A 932
REMARK 465 VAL A 933
REMARK 465 ASP A 934
REMARK 465 LEU A 935
REMARK 465 GLY A 936
REMARK 465 THR A 937
REMARK 465 GLU A 938
REMARK 465 ASN A 939
REMARK 465 LEU A 940
REMARK 465 TYR A 941
REMARK 465 PHE A 942
REMARK 465 GLN A 943
REMARK 465 SER A 944
REMARK 465 MET A 945
REMARK 465 LEU A 946
REMARK 465 ASN A 947
REMARK 465 THR A 948
REMARK 465 SER A 949
REMARK 465 GLY A 950
REMARK 465 SER A 951
REMARK 465 MET A 1113
REMARK 465 LYS A 1114
REMARK 465 GLY A 1162
REMARK 465 MET B 923
REMARK 465 HIS B 924
REMARK 465 HIS B 925
REMARK 465 HIS B 926
REMARK 465 HIS B 927
REMARK 465 HIS B 928
REMARK 465 HIS B 929
REMARK 465 SER B 930
REMARK 465 SER B 931
REMARK 465 GLY B 932
REMARK 465 VAL B 933
REMARK 465 ASP B 934
REMARK 465 LEU B 935
REMARK 465 GLY B 936
REMARK 465 THR B 937
REMARK 465 GLU B 938
REMARK 465 ASN B 939
REMARK 465 LEU B 940
REMARK 465 TYR B 941
REMARK 465 PHE B 942
REMARK 465 GLN B 943
REMARK 465 SER B 944
REMARK 465 MET B 945
REMARK 465 LEU B 946
REMARK 465 ASN B 947
REMARK 465 THR B 948
REMARK 465 SER B 949
REMARK 465 GLY B 950
REMARK 465 SER B 951
REMARK 465 GLY B 1162
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS B1114 CA C O CB CG CD CE
REMARK 470 LYS B1114 NZ
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 A1020 52.28 -145.96
REMARK 500 VAL A1131 -58.64 -133.04
REMARK 500 GLU B1046 2.67 -66.25
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 A2162 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1081 SG
REMARK 620 2 HIS A1084 ND1 106.9
REMARK 620 3 CYS A1089 SG 112.1 105.3
REMARK 620 4 CYS A1092 SG 115.5 101.6 114.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2162 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1081 SG
REMARK 620 2 HIS B1084 ND1 110.6
REMARK 620 3 CYS B1089 SG 110.6 100.8
REMARK 620 4 CYS B1092 SG 121.5 100.7 110.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WLH A 2165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE WLH B 2166
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2166
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5AKU RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TNKS2 IN COMPLEX WITH 2-(4-TERT -BUTYLPHENYL)-
REMARK 900 1,2,3,4-TETRAHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 5AKW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TNKS2 IN COMPLEX WITH 2-(4- CHLOROPHENYL)-1,2,
REMARK 900 3,4-TETRAHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 5AL1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TNKS2 IN COMPLEX WITH 2-(4-TERT -BUTYLPHENYL)-
REMARK 900 1H,2H,3H,4H-PYRIDO(2,3-D)PYRIMIDIN- 4-ONE
REMARK 900 RELATED ID: 5AL2 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TNKS2 IN COMPLEX WITH 2-(4-( PROPAN-2-YL)
REMARK 900 PHENYL)-1H,2H,3H,4H-PYRIDO(2,3-D) PYRIMIDIN-4-ONE
REMARK 900 RELATED ID: 5AL3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TNKS2 IN COMPLEX WITH 2-(2,4- DICHLOROPHENYL)-
REMARK 900 1-METHYL-1H,2H,3H,4H-PYRIDO(2,3-D )PYRIMIDIN-4-ONE
REMARK 900 RELATED ID: 5AL5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF TNKS2 IN COMPLEX WITH 2-(4-(( PYRIDIN-4-YL)
REMARK 900 METHYL)PIPERAZIN-1-YL)-3,4,5,6,7, 8-HEXAHYDROQUINAZOLIN-4-ONE
DBREF 5AL4 A 946 1162 UNP Q9H2K2 TNKS2_HUMAN 946 1162
DBREF 5AL4 B 946 1162 UNP Q9H2K2 TNKS2_HUMAN 946 1162
SEQADV 5AL4 MET A 923 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS A 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS A 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS A 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS A 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS A 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS A 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 SER A 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 SER A 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 GLY A 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 VAL A 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 ASP A 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 LEU A 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 GLY A 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 THR A 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 GLU A 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 ASN A 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 LEU A 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 TYR A 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 PHE A 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 GLN A 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 SER A 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 MET A 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 MET B 923 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS B 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS B 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS B 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS B 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS B 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 HIS B 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 SER B 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 SER B 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 GLY B 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 VAL B 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 ASP B 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 LEU B 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 GLY B 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 THR B 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 GLU B 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 ASN B 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 LEU B 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 TYR B 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 PHE B 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 GLN B 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 SER B 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5AL4 MET B 945 UNP Q9H2K2 EXPRESSION TAG
SEQRES 1 A 240 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 240 GLY THR GLU ASN LEU TYR PHE GLN SER MET LEU ASN THR
SEQRES 3 A 240 SER GLY SER GLY THR ILE LEU ILE ASP LEU SER PRO ASP
SEQRES 4 A 240 ASP LYS GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER
SEQRES 5 A 240 THR VAL ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY
SEQRES 6 A 240 ILE PHE ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL
SEQRES 7 A 240 CYS ASN LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG
SEQRES 8 A 240 LYS GLU VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU
SEQRES 9 A 240 ARG MET LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE
SEQRES 10 A 240 ILE HIS LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY
SEQRES 11 A 240 GLY MET PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER
SEQRES 12 A 240 SER LYS SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY
SEQRES 13 A 240 THR GLY CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE
SEQRES 14 A 240 CYS HIS ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY
SEQRES 15 A 240 LYS SER PHE LEU GLN PHE SER ALA MET LYS MET ALA HIS
SEQRES 16 A 240 SER PRO PRO GLY HIS HIS SER VAL THR GLY ARG PRO SER
SEQRES 17 A 240 VAL ASN GLY LEU ALA LEU ALA GLU TYR VAL ILE TYR ARG
SEQRES 18 A 240 GLY GLU GLN ALA TYR PRO GLU TYR LEU ILE THR TYR GLN
SEQRES 19 A 240 ILE MET ARG PRO GLU GLY
SEQRES 1 B 240 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 240 GLY THR GLU ASN LEU TYR PHE GLN SER MET LEU ASN THR
SEQRES 3 B 240 SER GLY SER GLY THR ILE LEU ILE ASP LEU SER PRO ASP
SEQRES 4 B 240 ASP LYS GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER
SEQRES 5 B 240 THR VAL ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY
SEQRES 6 B 240 ILE PHE ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL
SEQRES 7 B 240 CYS ASN LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG
SEQRES 8 B 240 LYS GLU VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU
SEQRES 9 B 240 ARG MET LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE
SEQRES 10 B 240 ILE HIS LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY
SEQRES 11 B 240 GLY MET PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER
SEQRES 12 B 240 SER LYS SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY
SEQRES 13 B 240 THR GLY CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE
SEQRES 14 B 240 CYS HIS ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY
SEQRES 15 B 240 LYS SER PHE LEU GLN PHE SER ALA MET LYS MET ALA HIS
SEQRES 16 B 240 SER PRO PRO GLY HIS HIS SER VAL THR GLY ARG PRO SER
SEQRES 17 B 240 VAL ASN GLY LEU ALA LEU ALA GLU TYR VAL ILE TYR ARG
SEQRES 18 B 240 GLY GLU GLN ALA TYR PRO GLU TYR LEU ILE THR TYR GLN
SEQRES 19 B 240 ILE MET ARG PRO GLU GLY
HET ZN A2162 1
HET SO4 A2163 5
HET SO4 A2164 5
HET WLH A2165 18
HET GOL A2166 6
HET ZN B2162 1
HET SO4 B2163 5
HET SO4 B2164 5
HET GOL B2165 6
HET WLH B2166 18
HETNAM ZN ZINC ION
HETNAM SO4 SULFATE ION
HETNAM WLH 2-(4-METHYLPIPERAZIN-1-YL)-3,4,5,6,7,8-
HETNAM 2 WLH HEXAHYDROQUINAZOLIN-4-ONE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 ZN 2(ZN 2+)
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 6 WLH 2(C13 H20 N4 O)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 13 HOH *279(H2 O)
HELIX 1 1 ASP A 962 THR A 975 1 14
HELIX 2 2 ASN A 1002 GLU A 1019 1 18
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 ASN B 1064 GLN B 1070 1 7
HELIX 12 12 GLY B 1074 GLY B 1078 5 5
HELIX 13 13 ARG B 1143 GLU B 1145 5 3
SHEET 1 AA 5 ILE A 954 ASP A 957 0
SHEET 2 AA 5 TYR A 992 CYS A1001 -1 O LYS A 999 N ILE A 956
SHEET 3 AA 5 ALA A1147 ILE A1157 -1 O GLU A1150 N VAL A1000
SHEET 4 AA 5 ARG A1094 THR A1102 -1 O ARG A1094 N TYR A1155
SHEET 5 AA 5 GLU A1026 HIS A1031 -1 O ARG A1027 N VAL A1101
SHEET 1 AB 4 ILE A1059 ALA A1062 0
SHEET 2 AB 4 GLU A1138 ILE A1141 -1 O TYR A1139 N PHE A1061
SHEET 3 AB 4 SER A1124 PRO A1129 -1 O VAL A1125 N VAL A1140
SHEET 4 AB 4 SER A1106 SER A1111 1 O PHE A1107 N THR A1126
SHEET 1 BA 5 ILE B 954 ASP B 957 0
SHEET 2 BA 5 TYR B 992 CYS B1001 -1 O LYS B 999 N ILE B 956
SHEET 3 BA 5 ALA B1147 ILE B1157 -1 O GLU B1150 N VAL B1000
SHEET 4 BA 5 ARG B1094 THR B1102 -1 O ARG B1094 N TYR B1155
SHEET 5 BA 5 GLU B1026 HIS B1031 -1 O ARG B1027 N VAL B1101
SHEET 1 BB 4 ILE B1059 ALA B1062 0
SHEET 2 BB 4 GLU B1138 ILE B1141 -1 O TYR B1139 N PHE B1061
SHEET 3 BB 4 SER B1124 PRO B1129 -1 O VAL B1125 N VAL B1140
SHEET 4 BB 4 SER B1106 SER B1111 1 O PHE B1107 N THR B1126
LINK SG CYS A1081 ZN ZN A2162 1555 1555 2.11
LINK ND1 HIS A1084 ZN ZN A2162 1555 1555 2.26
LINK SG CYS A1089 ZN ZN A2162 1555 1555 2.29
LINK SG CYS A1092 ZN ZN A2162 1555 1555 2.32
LINK SG CYS B1081 ZN ZN B2162 1555 1555 2.30
LINK ND1 HIS B1084 ZN ZN B2162 1555 1555 2.14
LINK SG CYS B1089 ZN ZN B2162 1555 1555 2.24
LINK SG CYS B1092 ZN ZN B2162 1555 1555 2.30
SITE 1 AC1 4 CYS B1081 HIS B1084 CYS B1089 CYS B1092
SITE 1 AC2 4 CYS A1081 HIS A1084 CYS A1089 CYS A1092
SITE 1 AC3 8 ARG A 977 HIS A 979 ARG A 980 LYS A1067
SITE 2 AC3 8 GLN A1070 HOH A2038 HOH A2112 HOH A2150
SITE 1 AC4 8 ARG B 977 HIS B 979 ARG B 980 LYS B1067
SITE 2 AC4 8 GLN B1070 HOH B2027 HOH B2029 HOH B2112
SITE 1 AC5 5 ASN B 990 ARG B 991 PRO B1160 GLU B1161
SITE 2 AC5 5 HOH B2040
SITE 1 AC6 7 ASN A 990 ARG A 991 PRO A1160 GLU A1161
SITE 2 AC6 7 HOH A2049 HOH A2051 HOH A2156
SITE 1 AC7 9 ARG B 977 GLU B 978 HIS B 979 GLY B 983
SITE 2 AC7 9 GLY B 987 ILE B 988 PHE B 989 HOH B2038
SITE 3 AC7 9 HOH B2039
SITE 1 AC8 9 HIS A1031 GLY A1032 SER A1033 TYR A1050
SITE 2 AC8 9 TYR A1060 SER A1068 TYR A1071 ILE A1075
SITE 3 AC8 9 GLU A1138
SITE 1 AC9 7 HIS B1031 GLY B1032 SER B1033 TYR B1050
SITE 2 AC9 7 TYR B1060 SER B1068 TYR B1071
SITE 1 BC1 4 PRO A1129 SER A1130 VAL A1131 GLY A1133
CRYST1 91.220 97.780 118.490 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 0.010963 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010227 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008440 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
