HEADER TRANSFERASE 17-OCT-12 4HLK
TITLE CRYSTAL STRUCTURE OF TANKYRASE 2 IN COMPLEX WITH 4'-METHYLFLAVONE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: C-TERMINAL FRAGMENT, UNP RESIDUES 946-1113;
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;
COMPND 11 MOL_ID: 2;
COMPND 12 MOLECULE: TANKYRASE-2;
COMPND 13 CHAIN: C, D;
COMPND 14 FRAGMENT: C-TERMINAL FRAGMENT, UNP RESIDUES 1114-1162;
COMPND 15 EC: 2.4.2.30;
COMPND 16 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;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: TNKS2, PARP5B, TANK2, TNKL;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PNIC-BSA4
KEYWDS PROTEIN-LIGAND COMPLEX, DIPHTHERIA TOXIN LIKE FOLD, TRANSFERASE, ADP-
KEYWDS 2 RIBOSYLATION
EXPDTA X-RAY DIFFRACTION
AUTHOR M.NARWAL,T.HAIKARAINEN,L.LEHTIO
REVDAT 5 20-SEP-23 4HLK 1 REMARK LINK
REVDAT 4 29-JAN-20 4HLK 1 REMARK SEQADV
REVDAT 3 22-MAY-13 4HLK 1 JRNL
REVDAT 2 08-MAY-13 4HLK 1 JRNL
REVDAT 1 31-OCT-12 4HLK 0
JRNL AUTH M.NARWAL,T.HAIKARAINEN,A.FALLARERO,P.M.VUORELA,L.LEHTIO
JRNL TITL SCREENING AND STRUCTURAL ANALYSIS OF FLAVONES INHIBITING
JRNL TITL 2 TANKYRASES.
JRNL REF J.MED.CHEM. V. 56 3507 2013
JRNL REFN ISSN 0022-2623
JRNL PMID 23574272
JRNL DOI 10.1021/JM3018783
REMARK 2
REMARK 2 RESOLUTION. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
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) : 44.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 3 NUMBER OF REFLECTIONS : 33862
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) : 0.186
REMARK 3 R VALUE (WORKING SET) : 0.184
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1783
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) : 1858
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 77.13
REMARK 3 BIN R VALUE (WORKING SET) : 0.2620
REMARK 3 BIN FREE R VALUE SET COUNT : 98
REMARK 3 BIN FREE R VALUE : 0.3220
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 : 71
REMARK 3 SOLVENT ATOMS : 239
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 19.77
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.33000
REMARK 3 B22 (A**2) : -1.04000
REMARK 3 B33 (A**2) : 0.71000
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): 0.165
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.145
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.103
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.783
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.935
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3519 ; 0.012 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2444 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4740 ; 1.507 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 5874 ; 0.856 ; 3.002
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 419 ; 6.214 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 182 ;33.313 ;22.857
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 580 ;13.945 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 29 ;17.835 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 471 ; 0.084 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3955 ; 0.007 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 794 ; 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 4HLK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-OCT-12.
REMARK 100 THE DEPOSITION ID IS D_1000075617.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 19-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 : 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 : SI (111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 225 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 35646
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 44.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.2
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.12600
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 10.4700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.05
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.1
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 0.84100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.880
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 (%): 49.38
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LISO4, 0.1 M TRIS HCL 24 %
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 59.12500
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 59.12500
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 46.98500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 47.78500
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 46.98500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 47.78500
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 59.12500
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 46.98500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 47.78500
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 59.12500
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 46.98500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 47.78500
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5870 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10650 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 10640 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -30.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 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 C 1114
REMARK 465 GLY C 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 D 1114
REMARK 465 GLY D 1162
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 HIS A 984 CG HIS A 984 CD2 0.057
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 55.87 -147.21
REMARK 500 HIS A1021 50.36 38.63
REMARK 500 VAL C1131 -61.00 -140.90
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 A1204 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1081 SG
REMARK 620 2 HIS A1084 ND1 109.5
REMARK 620 3 CYS A1089 SG 116.4 105.2
REMARK 620 4 CYS A1092 SG 113.8 97.6 112.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1204 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1081 SG
REMARK 620 2 HIS B1084 ND1 102.6
REMARK 620 3 CYS B1089 SG 110.1 103.0
REMARK 620 4 CYS B1092 SG 117.8 104.1 116.7
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 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 431 A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PEG A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 431 B 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 1204
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3U9H RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH NICOTINAMIDE
REMARK 900 RELATED ID: 3U9Y RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH OLAPARIB
REMARK 900 RELATED ID: 3UA9 RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH A SELECTIVE INHIBITOR
REMARK 900 RELATED ID: 4HKI RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH FLAVONE
REMARK 900 RELATED ID: 4HKK RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH APIGENIN
REMARK 900 RELATED ID: 4HKN RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH LUTEOLIN
REMARK 900 RELATED ID: 4HL5 RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH 7-HYDROXY -4'-METHOXYFLAVONE
REMARK 900 RELATED ID: 4HLF RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH 7,3',4'-TRIHYDROXYFLAVONE
REMARK 900 RELATED ID: 4HLG RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH 3'-HYDROXYFLAVONE
REMARK 900 RELATED ID: 4HLH RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLE WITH 4'-FLUOROFLAVONE
REMARK 900 RELATED ID: 4HLM RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLEX WITH 3',4'-DIHYDROXYFLAVONE
REMARK 900 RELATED ID: 4HMH RELATED DB: PDB
REMARK 900 TANKYRASE 2 IN COMPLEX WITH 7,3-DIHYDROXYFLAVONE
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 AUTHOR STATES THAT THE BACTERIAL EXPRESSED TANKYRASE 2 CATALYTIC
REMARK 999 DOMAIN (UNP RESIDUES 946-1162) WAS CLEAVED WITH CHYMOTRYPSIN
REMARK 999 PRODUCING TWO POLYPEPTIDES OF RESIDUES 946-1113 (CHAIN A AND B) AND
REMARK 999 RESIDUES 1114-1162(CHAIN C AND D).
DBREF 4HLK A 946 1113 UNP Q9H2K2 TNKS2_HUMAN 946 1113
DBREF 4HLK C 1114 1162 UNP Q9H2K2 TNKS2_HUMAN 1114 1162
DBREF 4HLK B 946 1113 UNP Q9H2K2 TNKS2_HUMAN 946 1113
DBREF 4HLK D 1114 1162 UNP Q9H2K2 TNKS2_HUMAN 1114 1162
SEQADV 4HLK MET A 923 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS A 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS A 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS A 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS A 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS A 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS A 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK SER A 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK SER A 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK GLY A 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK VAL A 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK ASP A 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK LEU A 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK GLY A 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK THR A 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK GLU A 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK ASN A 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK LEU A 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK TYR A 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK PHE A 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK GLN A 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK SER A 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK MET A 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK MET B 923 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS B 924 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS B 925 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS B 926 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS B 927 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS B 928 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK HIS B 929 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK SER B 930 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK SER B 931 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK GLY B 932 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK VAL B 933 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK ASP B 934 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK LEU B 935 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK GLY B 936 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK THR B 937 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK GLU B 938 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK ASN B 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK LEU B 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK TYR B 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK PHE B 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK GLN B 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK SER B 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4HLK MET B 945 UNP Q9H2K2 EXPRESSION TAG
SEQRES 1 A 191 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 A 191 GLY THR GLU ASN LEU TYR PHE GLN SER MET LEU ASN THR
SEQRES 3 A 191 SER GLY SER GLY THR ILE LEU ILE ASP LEU SER PRO ASP
SEQRES 4 A 191 ASP LYS GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER
SEQRES 5 A 191 THR VAL ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY
SEQRES 6 A 191 ILE PHE ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL
SEQRES 7 A 191 CYS ASN LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG
SEQRES 8 A 191 LYS GLU VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU
SEQRES 9 A 191 ARG MET LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE
SEQRES 10 A 191 ILE HIS LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY
SEQRES 11 A 191 GLY MET PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER
SEQRES 12 A 191 SER LYS SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY
SEQRES 13 A 191 THR GLY CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE
SEQRES 14 A 191 CYS HIS ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY
SEQRES 15 A 191 LYS SER PHE LEU GLN PHE SER ALA MET
SEQRES 1 C 49 LYS MET ALA HIS SER PRO PRO GLY HIS HIS SER VAL THR
SEQRES 2 C 49 GLY ARG PRO SER VAL ASN GLY LEU ALA LEU ALA GLU TYR
SEQRES 3 C 49 VAL ILE TYR ARG GLY GLU GLN ALA TYR PRO GLU TYR LEU
SEQRES 4 C 49 ILE THR TYR GLN ILE MET ARG PRO GLU GLY
SEQRES 1 B 191 MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU
SEQRES 2 B 191 GLY THR GLU ASN LEU TYR PHE GLN SER MET LEU ASN THR
SEQRES 3 B 191 SER GLY SER GLY THR ILE LEU ILE ASP LEU SER PRO ASP
SEQRES 4 B 191 ASP LYS GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER
SEQRES 5 B 191 THR VAL ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY
SEQRES 6 B 191 ILE PHE ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL
SEQRES 7 B 191 CYS ASN LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG
SEQRES 8 B 191 LYS GLU VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU
SEQRES 9 B 191 ARG MET LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE
SEQRES 10 B 191 ILE HIS LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY
SEQRES 11 B 191 GLY MET PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER
SEQRES 12 B 191 SER LYS SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY
SEQRES 13 B 191 THR GLY CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE
SEQRES 14 B 191 CYS HIS ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY
SEQRES 15 B 191 LYS SER PHE LEU GLN PHE SER ALA MET
SEQRES 1 D 49 LYS MET ALA HIS SER PRO PRO GLY HIS HIS SER VAL THR
SEQRES 2 D 49 GLY ARG PRO SER VAL ASN GLY LEU ALA LEU ALA GLU TYR
SEQRES 3 D 49 VAL ILE TYR ARG GLY GLU GLN ALA TYR PRO GLU TYR LEU
SEQRES 4 D 49 ILE THR TYR GLN ILE MET ARG PRO GLU GLY
HET SO4 A1201 5
HET SO4 A1202 5
HET 431 A1203 18
HET ZN A1204 1
HET PEG A1205 7
HET GOL C1201 6
HET SO4 B1201 5
HET SO4 B1202 5
HET 431 B1203 18
HET ZN B1204 1
HETNAM SO4 SULFATE ION
HETNAM 431 2-(4-METHYLPHENYL)-4H-CHROMEN-4-ONE
HETNAM ZN ZINC ION
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM GOL GLYCEROL
HETSYN 431 4'-METHYLFLAVONE
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 7 431 2(C16 H12 O2)
FORMUL 8 ZN 2(ZN 2+)
FORMUL 9 PEG C4 H10 O3
FORMUL 10 GOL C3 H8 O3
FORMUL 15 HOH *239(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 C 1143 GLU C 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 D 1143 GLU D 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 C1147 ILE C1157 -1 O LEU C1152 N GLN A 998
SHEET 4 A 5 ARG A1094 THR A1102 -1 N ARG A1094 O TYR C1155
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 C1138 ILE C1141 -1 O ILE C1141 N ILE A1059
SHEET 3 B 4 SER C1124 PRO C1129 -1 N GLY C1127 O GLU C1138
SHEET 4 B 4 SER A1106 SER A1111 1 N PHE A1107 O SER C1124
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 D1147 ILE D1157 -1 O GLN D1156 N ASN B 993
SHEET 4 C 5 ARG B1094 THR B1102 -1 N ARG B1094 O TYR D1155
SHEET 5 C 5 GLU B1026 HIS B1031 -1 N HIS B1031 O LEU B1097
SHEET 1 D 4 ILE B1059 ALA B1062 0
SHEET 2 D 4 GLU D1138 ILE D1141 -1 O TYR D1139 N PHE B1061
SHEET 3 D 4 SER D1124 PRO D1129 -1 N GLY D1127 O GLU D1138
SHEET 4 D 4 SER B1106 SER B1111 1 N GLN B1109 O THR D1126
LINK SG CYS A1081 ZN ZN A1204 1555 1555 2.29
LINK ND1 HIS A1084 ZN ZN A1204 1555 1555 2.25
LINK SG CYS A1089 ZN ZN A1204 1555 1555 2.29
LINK SG CYS A1092 ZN ZN A1204 1555 1555 2.32
LINK SG CYS B1081 ZN ZN B1204 1555 1555 2.23
LINK ND1 HIS B1084 ZN ZN B1204 1555 1555 2.08
LINK SG CYS B1089 ZN ZN B1204 1555 1555 2.23
LINK SG CYS B1092 ZN ZN B1204 1555 1555 2.35
SITE 1 AC1 8 ARG A 977 HIS A 979 ARG A 980 LYS A1067
SITE 2 AC1 8 GLN A1070 HOH A1400 HOH C1309 HOH C1312
SITE 1 AC2 5 ASN A 990 ARG A 991 PRO C1160 GLU C1161
SITE 2 AC2 5 HOH C1306
SITE 1 AC3 9 HIS A1031 GLY A1032 TYR A1050 TYR A1060
SITE 2 AC3 9 ALA A1062 LYS A1067 SER A1068 TYR A1071
SITE 3 AC3 9 GLU C1138
SITE 1 AC4 4 CYS A1081 HIS A1084 CYS A1089 CYS A1092
SITE 1 AC5 1 GLU C1150
SITE 1 AC6 4 PRO C1129 SER C1130 VAL C1131 GLY C1133
SITE 1 AC7 7 ARG B 977 HIS B 979 ARG B 980 LYS B1067
SITE 2 AC7 7 GLN B1070 HOH B1363 HOH B1373
SITE 1 AC8 5 ASN B 990 ARG B 991 PRO D1160 GLU D1161
SITE 2 AC8 5 HOH D1203
SITE 1 AC9 9 HIS B1031 GLY B1032 ALA B1049 TYR B1050
SITE 2 AC9 9 TYR B1060 LYS B1067 SER B1068 TYR B1071
SITE 3 AC9 9 GLU D1138
SITE 1 BC1 4 CYS B1081 HIS B1084 CYS B1089 CYS B1092
CRYST1 93.970 95.570 118.250 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 0.010642 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010464 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008457 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
