HEADER TRANSFERASE 24-JUN-13 4BUU
TITLE CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH (4-(4-OXO-3,4-
TITLE 2 DIHYDROQUINAZOLIN-2-YL)PHENYL)METHANESULFONAMIDE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT, 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;
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: ROSETTA 2;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS TRANSFERASE, DIPHTHERIA TOXIN LIKE FOLD, ADP-RIBOSYLATION,
KEYWDS 2 TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HAIKARAINEN,M.NARWAL,L.LEHTIO
REVDAT 5 06-FEB-19 4BUU 1 REMARK
REVDAT 4 30-JAN-19 4BUU 1 REMARK
REVDAT 3 17-JAN-18 4BUU 1 REMARK
REVDAT 2 11-DEC-13 4BUU 1 JRNL
REVDAT 1 30-OCT-13 4BUU 0
JRNL AUTH T.HAIKARAINEN,J.KOIVUNEN,M.NARWAL,H.VENKANNAGARI,E.OBAJI,
JRNL AUTH 2 P.JOENSUU,T.PIHLAJANIEMI,L.LEHTIO
JRNL TITL PARA-SUBSTITUTED 2-PHENYL-3,4-DIHYDROQUINAZOLIN-4-ONES AS
JRNL TITL 2 POTENT AND SELECTIVE TANKYRASE INHIBITORS.
JRNL REF CHEMMEDCHEM V. 8 1978 2013
JRNL REFN ISSN 1860-7179
JRNL PMID 24130191
JRNL DOI 10.1002/CMDC.201300337
REMARK 2
REMARK 2 RESOLUTION. 1.60 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) : 1.60
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.14
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.9
REMARK 3 NUMBER OF REFLECTIONS : 61588
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) : 0.160
REMARK 3 R VALUE (WORKING SET) : 0.159
REMARK 3 FREE R VALUE : 0.188
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3242
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) : 4673
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.98
REMARK 3 BIN R VALUE (WORKING SET) : 0.2510
REMARK 3 BIN FREE R VALUE SET COUNT : 246
REMARK 3 BIN FREE R VALUE : 0.2880
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3353
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 91
REMARK 3 SOLVENT ATOMS : 505
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 20.44
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16000
REMARK 3 B22 (A**2) : -0.75000
REMARK 3 B33 (A**2) : 0.91000
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): 0.079
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.081
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.049
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.393
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.969
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.960
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3641 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 3333 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4920 ; 1.327 ; 1.970
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7649 ; 0.732 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 435 ; 5.992 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 185 ;31.399 ;22.865
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 599 ;12.087 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 30 ;15.427 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 487 ; 0.080 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4149 ; 0.006 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 961 ; 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 4BUU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-JUN-13.
REMARK 100 THE DEPOSITION ID IS D_1290057414.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 24-MAY-12
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 : MAX II
REMARK 200 BEAMLINE : I911-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.04088
REMARK 200 MONOCHROMATOR : BENT SI (111) CRYSTAL,
REMARK 200 HORIZONTALLY FOCUSING
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARRESEARCH
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 64830
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.600
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 (%) : 91.9
REMARK 200 DATA REDUNDANCY : 4.500
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.3400
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) : 1.64
REMARK 200 COMPLETENESS FOR SHELL (%) : 95.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.63000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.380
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NONE
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 49.59
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 59.37500
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 59.37500
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 45.72000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.07500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 45.72000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.07500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.37500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 45.72000
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 49.07500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.37500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 45.72000
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 49.07500
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 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 A3133 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B3114 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 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: 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 O ALA A 1049 N10 F38 A 2162 2.05
REMARK 500 O ALA B 1049 N10 F38 B 2162 2.19
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 B 3222 O HOH B 3222 4545 1.98
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 55.78 -145.58
REMARK 500 VAL A1131 -58.29 -129.21
REMARK 500 SER B1033 141.98 -170.39
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 A2163 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1081 SG
REMARK 620 2 CYS A1089 SG 109.6
REMARK 620 3 HIS A1084 ND1 108.8 108.1
REMARK 620 4 CYS A1092 SG 116.9 112.6 100.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B2163 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B1084 ND1
REMARK 620 2 CYS B1089 SG 108.0
REMARK 620 3 CYS B1092 SG 100.5 112.1
REMARK 620 4 CYS B1081 SG 107.9 108.8 118.7
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 F38 B 2162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE F38 A 2162
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 2163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2163
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2164
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 2165
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2166
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2165
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2167
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 2166
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 2168
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4BU3 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-PHENYL-3,4-
REMARK 900 DIHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 4BU5 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-
REMARK 900 HYDROXYPHENYL)-3,4-DIHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 4BU6 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-
REMARK 900 AMINOPHENYL)-3,4-DIHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 4BU7 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-
REMARK 900 BROMOPHENYL)-3,4-DIHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 4BU8 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 4-(4-OXO-1,4-
REMARK 900 DIHYDROQUINAZOLIN-2-YL)BENZONITRILE
REMARK 900 RELATED ID: 4BU9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-
REMARK 900 METHOXYPHENYL)-3,4-DIHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 4BUA RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-
REMARK 900 (METHYLSULFANYL)PHENYL)-3,4-DIHYDROQUINAZOLIN-4- ONE
REMARK 900 RELATED ID: 4BUD RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-TERT-
REMARK 900 BUTYLPHENYL)-1,4-DIHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 4BUE RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 3-METHYL-N-
REMARK 900 (4-(4-OXO-3,4-DIHYDROQUINAZOLIN-2-YL) PHENYL)BUTANAMIDE
REMARK 900 RELATED ID: 4BUF RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-
REMARK 900 ACETYLPHENYL)-3,4-DIHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 4BUI RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH METHYL 4-(4-
REMARK 900 OXO-3,4-DIHYDROQUINAZOLIN-2- YL) BENZOATE
REMARK 900 RELATED ID: 4BUS RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-(4-OXO-
REMARK 900 3,4-DIHYDROQUINAZOLIN-2- YL)PHENOXY) ACETIC ACID
REMARK 900 RELATED ID: 4BUT RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 4-(4-OXO-3,4-
REMARK 900 DIHYDROQUINAZOLIN-2-YL)BENZENE-1- SULFONAMIDE
REMARK 900 RELATED ID: 4BUV RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH N-(4-(4-OXO-
REMARK 900 3,4-DIHYDROQUINAZOLIN-2- YL)PHENYL) THIOPHENE-2-CARBOXAMIDE
REMARK 900 RELATED ID: 4BUW RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 2-(4-(2-OXO-
REMARK 900 1,3-OXAZOLIDIN-3-YL)PHENYL)-3,4- DIHYDROQUINAZOLIN-4-ONE
REMARK 900 RELATED ID: 4BUX RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 3-((4-(4-OXO-
REMARK 900 3,4-DIHYDROQUINAZOLIN-2- YL)PHENYL) METHYL)IMIDAZOLIDINE-2,4-DIONE
REMARK 900 RELATED ID: 4BUY RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH 5-METHYL-5-
REMARK 900 (4-(4-OXO-3,4-DIHYDROQUINAZOLIN-2-YL) PHENYL)IMIDAZOLIDINE-2,4-DIONE
DBREF 4BUU A 946 1162 UNP Q9H2K2 TNKS2_HUMAN 946 1162
DBREF 4BUU B 946 1162 UNP Q9H2K2 TNKS2_HUMAN 946 1162
SEQADV 4BUU MET A 923 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS A 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS A 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS A 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS A 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS A 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS A 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU SER A 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU SER A 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU GLY A 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU VAL A 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU ASP A 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU LEU A 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU GLY A 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU THR A 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU GLU A 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU ASN A 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU LEU A 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU TYR A 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU PHE A 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU GLN A 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU SER A 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU MET A 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU MET B 923 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS B 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS B 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS B 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS B 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS B 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU HIS B 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU SER B 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU SER B 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU GLY B 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU VAL B 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU ASP B 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU LEU B 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU GLY B 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU THR B 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU GLU B 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU ASN B 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU LEU B 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU TYR B 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU PHE B 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU GLN B 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU SER B 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4BUU 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 F38 A2162 44
HET ZN A2163 1
HET GOL A2164 6
HET GOL A2165 6
HET SO4 A2166 5
HET SO4 A2167 5
HET PEG A2168 7
HET F38 B2162 44
HET ZN B2163 1
HET GOL B2164 6
HET SO4 B2165 5
HET SO4 B2166 5
HETNAM F38 [4-(4-OXO-3,4-DIHYDROQUINAZOLIN-2- YL)
HETNAM 2 F38 PHENYL]METHANESULFONAMIDE
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETNAM SO4 SULFATE ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 F38 2(C15 H13 N3 O3 S)
FORMUL 4 ZN 2(ZN 2+)
FORMUL 5 GOL 3(C3 H8 O3)
FORMUL 7 SO4 4(O4 S 2-)
FORMUL 9 PEG C4 H10 O3
FORMUL 15 HOH *505(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 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 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 ZN ZN A2163 SG CYS A1081 1555 1555 2.24
LINK ZN ZN A2163 SG CYS A1089 1555 1555 2.30
LINK ZN ZN A2163 ND1 HIS A1084 1555 1555 2.15
LINK ZN ZN A2163 SG CYS A1092 1555 1555 2.30
LINK ZN ZN B2163 ND1 HIS B1084 1555 1555 2.08
LINK ZN ZN B2163 SG CYS B1089 1555 1555 2.35
LINK ZN ZN B2163 SG CYS B1092 1555 1555 2.30
LINK ZN ZN B2163 SG CYS B1081 1555 1555 2.31
SITE 1 AC1 14 HIS B1031 GLY B1032 PHE B1035 HIS B1048
SITE 2 AC1 14 ALA B1049 TYR B1050 TYR B1060 PHE B1061
SITE 3 AC1 14 LYS B1067 SER B1068 TYR B1071 ILE B1075
SITE 4 AC1 14 GLU B1138 HOH B3132
SITE 1 AC2 12 HIS A1031 GLY A1032 PHE A1035 HIS A1048
SITE 2 AC2 12 ALA A1049 TYR A1050 TYR A1060 PHE A1061
SITE 3 AC2 12 SER A1068 TYR A1071 ILE A1075 GLU A1138
SITE 1 AC3 4 CYS B1081 HIS B1084 CYS B1089 CYS B1092
SITE 1 AC4 4 CYS A1081 HIS A1084 CYS A1089 CYS A1092
SITE 1 AC5 8 GLU B 978 HIS B 979 GLY B 982 GLY B 983
SITE 2 AC5 8 ILE B 988 PHE B 989 HOH B3042 HOH B3065
SITE 1 AC6 7 TYR A1050 GLY A1053 MET A1054 PHE A1055
SITE 2 AC6 7 TYR A1060 GLU A1138 HOH A3267
SITE 1 AC7 6 PRO A1129 SER A1130 VAL A1131 ASN A1132
SITE 2 AC7 6 GLY A1133 HOH A3257
SITE 1 AC8 9 ARG A 977 HIS A 979 ARG A 980 LYS A1067
SITE 2 AC8 9 GLN A1070 HOH A3053 HOH A3057 HOH A3188
SITE 3 AC8 9 HOH A3258
SITE 1 AC9 10 HOH A3009 ARG B 977 HIS B 979 ARG B 980
SITE 2 AC9 10 LYS B1067 GLN B1070 HOH B3044 HOH B3049
SITE 3 AC9 10 HOH B3053 HOH B3155
SITE 1 BC1 6 ASN A 990 ARG A 991 PRO A1160 GLU A1161
SITE 2 BC1 6 HOH A3073 HOH A3075
SITE 1 BC2 5 ASN B 990 ARG B 991 GLU B1161 HOH B3066
SITE 2 BC2 5 HOH B3234
SITE 1 BC3 5 LYS A 999 ASN A1002 TYR A1148 HOH A3180
SITE 2 BC3 5 HOH A3263
CRYST1 91.440 98.150 118.750 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 0.010936 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010188 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008421 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
