HEADER TRANSFERASE 04-SEP-17 5OWS
TITLE CRYSTAL STRUCTURE OF TNKS2 IN COMPLEX WITH 2-[4-(4-METHYL-2-
TITLE 2 OXOIMIDAZOLIDIN-4-YL)PHENYL]-3,4-DIHYDROQUINAZOLIN-4-ONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: TANK2,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 6,ARTD6,
COMPND 5 POLY [ADP-RIBOSE] POLYMERASE 5B,TNKS-2,TRF1-INTERACTING ANKYRIN-
COMPND 6 RELATED ADP-RIBOSE POLYMERASE 2,TANKYRASE II,TANKYRASE-LIKE PROTEIN,
COMPND 7 TANKYRASE-RELATED PROTEIN;
COMPND 8 EC: 2.4.2.30;
COMPND 9 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: TNKS2, PARP5B, TANK2, TNKL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_VARIANT: ROSETTA 2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS TANKYRASE, INHIBITOR, ARTD6, PARP5B, ADP-RIBOSYLTRANSFERASE,
KEYWDS 2 TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR Y.NKIZINKIKO,T.HAIKARAINEN,L.LEHTIO
REVDAT 5 17-JAN-24 5OWS 1 REMARK
REVDAT 4 16-OCT-19 5OWS 1 REMARK
REVDAT 3 22-MAY-19 5OWS 1 COMPND REMARK HET HETNAM
REVDAT 3 2 1 HETSYN FORMUL ATOM
REVDAT 2 20-JUN-18 5OWS 1 REMARK
REVDAT 1 02-MAY-18 5OWS 0
JRNL AUTH Y.NKIZINKIKO,J.DESANTIS,J.KOIVUNEN,T.HAIKARAINEN,S.MURTHY,
JRNL AUTH 2 L.SANCINETO,S.MASSARI,F.IANNI,E.OBAJI,M.I.LOZA,
JRNL AUTH 3 T.PIHLAJANIEMI,J.BREA,O.TABARRINI,L.LEHTIO
JRNL TITL 2-PHENYLQUINAZOLINONES AS DUAL-ACTIVITY TANKYRASE-KINASE
JRNL TITL 2 INHIBITORS.
JRNL REF SCI REP V. 8 1680 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 29374194
JRNL DOI 10.1038/S41598-018-19872-3
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0135
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.38
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 47308
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) : 0.168
REMARK 3 R VALUE (WORKING SET) : 0.167
REMARK 3 FREE R VALUE : 0.194
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 2490
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) : 1.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.85
REMARK 3 REFLECTION IN BIN (WORKING SET) : 3451
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.97
REMARK 3 BIN R VALUE (WORKING SET) : 0.3110
REMARK 3 BIN FREE R VALUE SET COUNT : 181
REMARK 3 BIN FREE R VALUE : 0.3480
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3346
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 305
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 30.10
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.31000
REMARK 3 B22 (A**2) : -1.20000
REMARK 3 B33 (A**2) : 1.51000
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): 0.106
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.101
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.075
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.522
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.959
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3601 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3319 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4868 ; 1.435 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7628 ; 0.919 ; 3.003
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 437 ; 6.197 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 186 ;32.641 ;22.903
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 605 ;13.310 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;16.484 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 485 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4124 ; 0.007 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 940 ; 0.002 ; 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): 1691 ; 1.902 ; 2.754
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1690 ; 1.902 ; 2.753
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2114 ; 2.823 ; 4.104
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2115 ; 2.822 ; 4.106
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1910 ; 2.659 ; 3.102
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1910 ; 2.658 ; 3.103
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2744 ; 4.338 ; 4.525
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 4097 ; 6.391 ;22.597
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 4098 ; 6.390 ;22.602
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 : NULL
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 5OWS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-17.
REMARK 100 THE DEPOSITION ID IS D_1200006493.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-15
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 : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.87260
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 : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 49798
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 7.520
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3100
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: MOLREP
REMARK 200 STARTING MODEL: 3U9H
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.65
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.44
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LISO4, 0.1 M TRIS HCL, 22%
REMARK 280 PEG3350, PH 8.5, VAPOR DIFFUSION, SITTING 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 59.22000
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 59.22000
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 45.78000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.19500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.78000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.19500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.22000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.78000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.19500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.22000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.78000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.19500
REMARK 290 SMTRY3 8 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2460 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 19640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -74.0 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 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 B1348 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 LYS B 1114
REMARK 465 GLY B 1162
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 NH1 ARG A 1128 O HOH A 1302 1.84
REMARK 500 O HOH A 1314 O HOH A 1440 2.02
REMARK 500 OE2 GLU A 971 O HOH A 1303 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 1384 O HOH A 1384 3555 1.13
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 ASN A1020 57.77 -142.60
REMARK 500 VAL A1131 -62.84 -135.44
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 A1203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1081 SG
REMARK 620 2 HIS A1084 ND1 106.7
REMARK 620 3 CYS A1089 SG 111.5 109.7
REMARK 620 4 CYS A1092 SG 116.2 97.2 114.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1203 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1081 SG
REMARK 620 2 HIS B1084 ND1 109.0
REMARK 620 3 CYS B1089 SG 109.1 103.8
REMARK 620 4 CYS B1092 SG 118.0 101.7 113.9
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 SO4 A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KC8 A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue KC8 B 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 1205
DBREF 5OWS A 946 1162 UNP Q9H2K2 TNKS2_HUMAN 946 1162
DBREF 5OWS B 946 1162 UNP Q9H2K2 TNKS2_HUMAN 946 1162
SEQADV 5OWS MET A 923 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 5OWS HIS A 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS A 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS A 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS A 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS A 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS A 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS SER A 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS SER A 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS GLY A 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS VAL A 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS ASP A 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS LEU A 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS GLY A 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS THR A 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS GLU A 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS ASN A 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS LEU A 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS TYR A 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS PHE A 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS GLN A 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS SER A 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS MET A 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS MET B 923 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 5OWS HIS B 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS B 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS B 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS B 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS B 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS HIS B 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS SER B 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS SER B 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS GLY B 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS VAL B 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS ASP B 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS LEU B 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS GLY B 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS THR B 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS GLU B 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS ASN B 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS LEU B 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS TYR B 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS PHE B 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS GLN B 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS SER B 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 5OWS 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 SO4 A1201 10
HET SO4 A1202 5
HET ZN A1203 1
HET KC8 A1204 24
HET GOL A1205 6
HET SO4 B1201 5
HET SO4 B1202 5
HET ZN B1203 1
HET KC8 B1204 24
HET GOL B1205 6
HETNAM SO4 SULFATE ION
HETNAM ZN ZINC ION
HETNAM KC8 2-[4-[(4~{S})-4-METHYL-2-OXIDANYLIDENE-IMIDAZOLIDIN-4-
HETNAM 2 KC8 YL]PHENYL]-3~{H}-QUINAZOLIN-4-ONE
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 4(O4 S 2-)
FORMUL 5 ZN 2(ZN 2+)
FORMUL 6 KC8 2(C18 H16 N4 O2)
FORMUL 7 GOL 2(C3 H8 O3)
FORMUL 13 HOH *305(H2 O)
HELIX 1 AA1 ASP A 962 THR A 975 1 14
HELIX 2 AA2 ASN A 1002 GLU A 1019 1 18
HELIX 3 AA3 PHE A 1035 GLY A 1043 1 9
HELIX 4 AA4 ASP A 1045 ALA A 1049 5 5
HELIX 5 AA5 ASN A 1064 GLN A 1070 1 7
HELIX 6 AA6 GLY A 1074 GLY A 1078 5 5
HELIX 7 AA7 ARG A 1143 GLU A 1145 5 3
HELIX 8 AA8 ASP B 962 THR B 975 1 14
HELIX 9 AA9 ASN B 1002 ASN B 1020 1 19
HELIX 10 AB1 PHE B 1035 GLY B 1043 1 9
HELIX 11 AB2 ASP B 1045 ALA B 1049 5 5
HELIX 12 AB3 ASN B 1064 GLN B 1070 1 7
HELIX 13 AB4 GLY B 1074 GLY B 1078 5 5
HELIX 14 AB5 ARG B 1143 GLU B 1145 5 3
SHEET 1 AA1 5 ILE A 954 ASP A 957 0
SHEET 2 AA1 5 TYR A 992 CYS A1001 -1 O LYS A 999 N ILE A 956
SHEET 3 AA1 5 ALA A1147 ILE A1157 -1 O LEU A1152 N GLN A 998
SHEET 4 AA1 5 ARG A1094 THR A1102 -1 N ARG A1094 O TYR A1155
SHEET 5 AA1 5 GLU A1026 HIS A1031 -1 N LEU A1029 O CYS A1099
SHEET 1 AA2 4 ILE A1059 ALA A1062 0
SHEET 2 AA2 4 GLU A1138 ILE A1141 -1 O ILE A1141 N ILE A1059
SHEET 3 AA2 4 SER A1124 PRO A1129 -1 N GLY A1127 O GLU A1138
SHEET 4 AA2 4 SER A1106 SER A1111 1 N PHE A1107 O THR A1126
SHEET 1 AA3 5 ILE B 954 ASP B 957 0
SHEET 2 AA3 5 TYR B 992 CYS B1001 -1 O CYS B1001 N ILE B 954
SHEET 3 AA3 5 ALA B1147 ILE B1157 -1 O THR B1154 N LYS B 996
SHEET 4 AA3 5 ARG B1094 THR B1102 -1 N ARG B1094 O TYR B1155
SHEET 5 AA3 5 GLU B1026 HIS B1031 -1 N LEU B1029 O CYS B1099
SHEET 1 AA4 4 ILE B1059 ALA B1062 0
SHEET 2 AA4 4 GLU B1138 ILE B1141 -1 O ILE B1141 N ILE B1059
SHEET 3 AA4 4 SER B1124 PRO B1129 -1 N GLY B1127 O GLU B1138
SHEET 4 AA4 4 SER B1106 SER B1111 1 N GLN B1109 O THR B1126
LINK SG CYS A1081 ZN ZN A1203 1555 1555 2.25
LINK ND1 HIS A1084 ZN ZN A1203 1555 1555 2.31
LINK SG CYS A1089 ZN ZN A1203 1555 1555 2.33
LINK SG CYS A1092 ZN ZN A1203 1555 1555 2.34
LINK SG CYS B1081 ZN ZN B1203 1555 1555 2.33
LINK ND1 HIS B1084 ZN ZN B1203 1555 1555 2.20
LINK SG CYS B1089 ZN ZN B1203 1555 1555 2.23
LINK SG CYS B1092 ZN ZN B1203 1555 1555 2.35
SITE 1 AC1 7 ARG A 977 HIS A 979 ARG A 980 LYS A1067
SITE 2 AC1 7 HOH A1301 HOH A1321 HOH A1341
SITE 1 AC2 5 ASN A 990 ARG A 991 PRO A1160 GLU A1161
SITE 2 AC2 5 HOH A1338
SITE 1 AC3 4 CYS A1081 HIS A1084 CYS A1089 CYS A1092
SITE 1 AC4 13 HIS A1031 GLY A1032 SER A1033 HIS A1048
SITE 2 AC4 13 ALA A1049 TYR A1050 TYR A1060 LYS A1067
SITE 3 AC4 13 SER A1068 TYR A1071 ILE A1075 GLU A1138
SITE 4 AC4 13 HOH A1312
SITE 1 AC5 6 PRO A1129 SER A1130 VAL A1131 ASN A1132
SITE 2 AC5 6 GLY A1133 HOH A1302
SITE 1 AC6 6 ARG B 977 HIS B 979 ARG B 980 LYS B1067
SITE 2 AC6 6 GLN B1070 HOH B1346
SITE 1 AC7 5 ASN B 990 ARG B 991 PRO B1160 GLU B1161
SITE 2 AC7 5 HOH B1317
SITE 1 AC8 4 CYS B1081 HIS B1084 CYS B1089 CYS B1092
SITE 1 AC9 11 HIS B1031 GLY B1032 ALA B1049 TYR B1050
SITE 2 AC9 11 TYR B1060 LYS B1067 SER B1068 TYR B1071
SITE 3 AC9 11 ILE B1075 GLU B1138 HOH B1340
SITE 1 AD1 9 ARG B 977 HIS B 979 GLY B 983 GLY B 987
SITE 2 AD1 9 ILE B 988 PHE B 989 HOH B1315 HOH B1359
SITE 3 AD1 9 HOH B1396
CRYST1 91.560 98.390 118.440 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 0.010922 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010164 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008443 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
