HEADER TRANSFERASE 25-MAY-14 4TK5
TITLE CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH EB47.
CAVEAT 4TK5 UHB A 1202 HAS WRONG CHIRALITY AT ATOM C24 UHB B 1202 HAS
CAVEAT 2 4TK5 WRONG CHIRALITY AT ATOM C24 UHB D 1201 HAS WRONG CHIRALITY
CAVEAT 3 4TK5 AT ATOM C22 UHB D 1201 HAS WRONG CHIRALITY AT ATOM C24
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: PARP, CATALYTIC DOMAIN;
COMPND 5 SYNONYM: TANK2,ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 6,ARTD6,
COMPND 6 POLY [ADP-RIBOSE] POLYMERASE 5B,TNKS-2,TRF1-INTERACTING ANKYRIN-
COMPND 7 RELATED ADP-RIBOSE POLYMERASE 2,TANKYRASE II,TANKYRASE-LIKE PROTEIN,
COMPND 8 TANKYRASE-RELATED PROTEIN;
COMPND 9 EC: 2.4.2.30;
COMPND 10 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: TNKS2, PARP5B, TANK2, TNKL;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS POLY(ADP-RIBOSYLATION) POLYMERASE (PARP), TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.QIU,R.LAM,V.ROMANOV,R.GORDON,S.GEBREMESKEL,J.VODSEDALEK,C.THOMPSON,
AUTHOR 2 I.BELETSKAYA,K.P.BATTAILE,E.F.PAI,N.Y.CHIRGADZE
REVDAT 4 27-DEC-23 4TK5 1 REMARK
REVDAT 3 22-NOV-17 4TK5 1 HEADER SOURCE REMARK
REVDAT 2 07-JAN-15 4TK5 1 JRNL
REVDAT 1 15-OCT-14 4TK5 0
JRNL AUTH W.QIU,R.LAM,O.VOYTYUK,V.ROMANOV,R.GORDON,S.GEBREMESKEL,
JRNL AUTH 2 J.VODSEDALEK,C.THOMPSON,I.BELETSKAYA,K.P.BATTAILE,E.F.PAI,
JRNL AUTH 3 R.ROTTAPEL,N.Y.CHIRGADZE
JRNL TITL INSIGHTS INTO THE BINDING OF PARP INHIBITORS TO THE
JRNL TITL 2 CATALYTIC DOMAIN OF HUMAN TANKYRASE-2.
JRNL REF ACTA CRYSTALLOGR.,SECT.D V. 70 2740 2014
JRNL REFN ESSN 1399-0047
JRNL PMID 25286857
JRNL DOI 10.1107/S1399004714017660
REMARK 2
REMARK 2 RESOLUTION. 2.02 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER-TNT BUSTER 2.10.0
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.57
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.6
REMARK 3 NUMBER OF REFLECTIONS : 60027
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) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.177
REMARK 3 FREE R VALUE : 0.212
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.630
REMARK 3 FREE R VALUE TEST SET COUNT : 980
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.07
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.61
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4183
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.1984
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 4130
REMARK 3 BIN R VALUE (WORKING SET) : 0.1981
REMARK 3 BIN FREE R VALUE : 0.2262
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.27
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 53
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6532
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 159
REMARK 3 SOLVENT ATOMS : 803
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 30.24
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 34.46
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -2.08120
REMARK 3 B22 (A**2) : -2.91390
REMARK 3 B33 (A**2) : 4.99510
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 COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.233
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.195
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.156
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.179
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.151
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.950
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.934
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 7000 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9531 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2753 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 150 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1031 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 7000 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 0 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 802 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 8044 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.05
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.64
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 17.13
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.6798 49.2401 -1.2457
REMARK 3 T TENSOR
REMARK 3 T11: -0.0010 T22: -0.0465
REMARK 3 T33: -0.0659 T12: -0.0137
REMARK 3 T13: 0.0155 T23: 0.0096
REMARK 3 L TENSOR
REMARK 3 L11: 0.8928 L22: 0.5614
REMARK 3 L33: 2.4198 L12: -0.1841
REMARK 3 L13: -0.0559 L23: -0.5194
REMARK 3 S TENSOR
REMARK 3 S11: 0.0689 S12: 0.1533 S13: 0.0471
REMARK 3 S21: 0.0732 S22: -0.0640 S23: -0.0110
REMARK 3 S31: -0.1717 S32: 0.0902 S33: -0.0050
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.2605 -9.3874 36.5433
REMARK 3 T TENSOR
REMARK 3 T11: -0.0634 T22: -0.0427
REMARK 3 T33: -0.0673 T12: 0.0049
REMARK 3 T13: -0.0023 T23: 0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 1.3458 L22: 0.9148
REMARK 3 L33: 1.8985 L12: -0.1038
REMARK 3 L13: 0.1208 L23: -0.4511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0254 S12: -0.2166 S13: -0.0460
REMARK 3 S21: -0.0414 S22: 0.0308 S23: -0.0406
REMARK 3 S31: -0.0057 S32: 0.0091 S33: -0.0055
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.8416 31.9833 31.4310
REMARK 3 T TENSOR
REMARK 3 T11: -0.0560 T22: -0.0617
REMARK 3 T33: -0.0549 T12: -0.0260
REMARK 3 T13: 0.0084 T23: 0.0021
REMARK 3 L TENSOR
REMARK 3 L11: 0.9922 L22: 1.1636
REMARK 3 L33: 1.6082 L12: -0.4275
REMARK 3 L13: -0.0736 L23: -0.1921
REMARK 3 S TENSOR
REMARK 3 S11: -0.0029 S12: -0.1327 S13: 0.0058
REMARK 3 S21: -0.0682 S22: 0.0661 S23: -0.0301
REMARK 3 S31: -0.0130 S32: 0.0401 S33: -0.0632
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.4411 8.0939 4.3741
REMARK 3 T TENSOR
REMARK 3 T11: 0.0331 T22: 0.0093
REMARK 3 T33: -0.0586 T12: -0.0922
REMARK 3 T13: -0.0014 T23: 0.0313
REMARK 3 L TENSOR
REMARK 3 L11: 0.9677 L22: 0.0000
REMARK 3 L33: 2.4624 L12: -0.4842
REMARK 3 L13: 0.5147 L23: 0.1327
REMARK 3 S TENSOR
REMARK 3 S11: -0.0700 S12: 0.2587 S13: 0.1071
REMARK 3 S21: 0.0334 S22: -0.0453 S23: -0.0139
REMARK 3 S31: -0.1401 S32: 0.2736 S33: 0.1153
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TK5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000201769.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-OCT-09
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.000
REMARK 200 MONOCHROMATOR : GRAPHITE
REMARK 200 OPTICS : MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MAR CCD 165 MM
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 2005/3, XPREP
REMARK 200 DATA SCALING SOFTWARE : XPREP
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 60172
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.020
REMARK 200 RESOLUTION RANGE LOW (A) : 79.620
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 13.95
REMARK 200 R MERGE (I) : 0.07500
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 26.3900
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.12
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.5
REMARK 200 DATA REDUNDANCY IN SHELL : 8.68
REMARK 200 R MERGE FOR SHELL (I) : 0.40300
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: NULL
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.48
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NACL, 0.1M SODIUM, HEPES BUFFER
REMARK 280 AT PH7.5, 12-15% ISO-PROPANOL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 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 37.01000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.76000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.81000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.76000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.01000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.81000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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 300 REMARK: 1
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 350
REMARK 350 BIOMOLECULE: 3
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: 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: 4
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: 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 938
REMARK 465 GLY A 939
REMARK 465 SER A 940
REMARK 465 SER A 941
REMARK 465 HIS A 942
REMARK 465 HIS A 943
REMARK 465 HIS A 944
REMARK 465 HIS A 945
REMARK 465 HIS A 946
REMARK 465 HIS A 947
REMARK 465 SER A 948
REMARK 465 SER A 949
REMARK 465 GLY A 950
REMARK 465 ARG A 951
REMARK 465 GLU A 952
REMARK 465 ASN A 953
REMARK 465 LEU A 954
REMARK 465 TYR A 955
REMARK 465 PHE A 956
REMARK 465 GLN A 957
REMARK 465 GLY A 958
REMARK 465 SER A 959
REMARK 465 GLU A 1161
REMARK 465 GLY A 1162
REMARK 465 MET A 1163
REMARK 465 VAL A 1164
REMARK 465 MET B 938
REMARK 465 GLY B 939
REMARK 465 SER B 940
REMARK 465 SER B 941
REMARK 465 HIS B 942
REMARK 465 HIS B 943
REMARK 465 HIS B 944
REMARK 465 HIS B 945
REMARK 465 HIS B 946
REMARK 465 HIS B 947
REMARK 465 SER B 948
REMARK 465 SER B 949
REMARK 465 GLY B 950
REMARK 465 ARG B 951
REMARK 465 GLU B 952
REMARK 465 ASN B 953
REMARK 465 SER B 959
REMARK 465 PRO B 960
REMARK 465 ASP B 961
REMARK 465 ILE B 1051
REMARK 465 GLU B 1161
REMARK 465 GLY B 1162
REMARK 465 MET B 1163
REMARK 465 VAL B 1164
REMARK 465 MET C 938
REMARK 465 GLY C 939
REMARK 465 SER C 940
REMARK 465 SER C 941
REMARK 465 HIS C 942
REMARK 465 HIS C 943
REMARK 465 HIS C 944
REMARK 465 HIS C 945
REMARK 465 HIS C 946
REMARK 465 HIS C 947
REMARK 465 SER C 948
REMARK 465 SER C 949
REMARK 465 GLY C 950
REMARK 465 ARG C 951
REMARK 465 GLU C 952
REMARK 465 GLU C 1161
REMARK 465 GLY C 1162
REMARK 465 MET C 1163
REMARK 465 VAL C 1164
REMARK 465 MET D 938
REMARK 465 GLY D 939
REMARK 465 SER D 940
REMARK 465 SER D 941
REMARK 465 HIS D 942
REMARK 465 HIS D 943
REMARK 465 HIS D 944
REMARK 465 HIS D 945
REMARK 465 HIS D 946
REMARK 465 HIS D 947
REMARK 465 SER D 948
REMARK 465 SER D 949
REMARK 465 GLY D 950
REMARK 465 ARG D 951
REMARK 465 GLU D 952
REMARK 465 ASN D 953
REMARK 465 LEU D 954
REMARK 465 TYR D 955
REMARK 465 PHE D 956
REMARK 465 GLN D 957
REMARK 465 GLY D 958
REMARK 465 SER D 959
REMARK 465 PRO D 960
REMARK 465 ASP D 961
REMARK 465 GLU D 1161
REMARK 465 GLY D 1162
REMARK 465 MET D 1163
REMARK 465 VAL D 1164
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 PRO C 960 CG CD
REMARK 470 ASP C 961 CG OD1 OD2
REMARK 470 ASP D 962 CG OD1 OD2
REMARK 470 GLU D 978 CG CD OE1 OE2
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 ND1 HIS D 1084 O HOH D 1338 2.14
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 ILE A1051 108.89 -51.55
REMARK 500 ILE D1051 98.80 -61.41
REMARK 500 ALA D1137 158.30 -46.66
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A1506 DISTANCE = 6.48 ANGSTROMS
REMARK 525 HOH B1452 DISTANCE = 5.82 ANGSTROMS
REMARK 525 HOH B1459 DISTANCE = 5.85 ANGSTROMS
REMARK 525 HOH B1476 DISTANCE = 6.56 ANGSTROMS
REMARK 525 HOH C1490 DISTANCE = 6.60 ANGSTROMS
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 A1201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1081 SG
REMARK 620 2 HIS A1084 ND1 111.1
REMARK 620 3 CYS A1089 SG 109.8 104.6
REMARK 620 4 CYS A1092 SG 115.8 101.0 113.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B1201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1081 SG
REMARK 620 2 HIS B1084 ND1 109.9
REMARK 620 3 CYS B1089 SG 110.1 103.7
REMARK 620 4 CYS B1092 SG 117.0 101.6 113.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C1201 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS C1081 SG
REMARK 620 2 HIS C1084 ND1 111.9
REMARK 620 3 CYS C1089 SG 111.9 103.2
REMARK 620 4 CYS C1092 SG 114.8 101.5 112.4
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 A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UHB A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UHB B 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UHB C 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue UHB D 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4PML RELATED DB: PDB
REMARK 900 RELATED ID: 4PNL RELATED DB: PDB
REMARK 900 RELATED ID: 4PNM RELATED DB: PDB
REMARK 900 RELATED ID: 4PNN RELATED DB: PDB
REMARK 900 RELATED ID: 4PNQ RELATED DB: PDB
REMARK 900 RELATED ID: 4PNT RELATED DB: PDB
REMARK 900 RELATED ID: 4PNR RELATED DB: PDB
REMARK 900 RELATED ID: 4PNS RELATED DB: PDB
REMARK 900 RELATED ID: 4TJU RELATED DB: PDB
REMARK 900 RELATED ID: 4TJW RELATED DB: PDB
REMARK 900 RELATED ID: 4TJY RELATED DB: PDB
REMARK 900 RELATED ID: 4TK0 RELATED DB: PDB
REMARK 900 RELATED ID: 4TKF RELATED DB: PDB
REMARK 900 RELATED ID: 4TKG RELATED DB: PDB
REMARK 900 RELATED ID: 4TKI RELATED DB: PDB
DBREF 4TK5 A 959 1164 UNP Q9H2K2 TNKS2_HUMAN 959 1164
DBREF 4TK5 B 959 1164 UNP Q9H2K2 TNKS2_HUMAN 959 1164
DBREF 4TK5 C 959 1164 UNP Q9H2K2 TNKS2_HUMAN 959 1164
DBREF 4TK5 D 959 1164 UNP Q9H2K2 TNKS2_HUMAN 959 1164
SEQADV 4TK5 MET A 938 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 4TK5 GLY A 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER A 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER A 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS A 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS A 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS A 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS A 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS A 946 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS A 947 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER A 948 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER A 949 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLY A 950 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 ARG A 951 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLU A 952 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 ASN A 953 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 LEU A 954 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 TYR A 955 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 PHE A 956 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLN A 957 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLY A 958 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 MET B 938 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 4TK5 GLY B 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER B 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER B 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS B 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS B 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS B 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS B 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS B 946 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS B 947 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER B 948 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER B 949 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLY B 950 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 ARG B 951 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLU B 952 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 ASN B 953 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 LEU B 954 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 TYR B 955 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 PHE B 956 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLN B 957 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLY B 958 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 MET C 938 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 4TK5 GLY C 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER C 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER C 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS C 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS C 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS C 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS C 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS C 946 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS C 947 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER C 948 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER C 949 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLY C 950 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 ARG C 951 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLU C 952 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 ASN C 953 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 LEU C 954 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 TYR C 955 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 PHE C 956 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLN C 957 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLY C 958 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 MET D 938 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 4TK5 GLY D 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER D 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER D 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS D 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS D 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS D 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS D 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS D 946 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 HIS D 947 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER D 948 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 SER D 949 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLY D 950 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 ARG D 951 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLU D 952 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 ASN D 953 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 LEU D 954 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 TYR D 955 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 PHE D 956 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLN D 957 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK5 GLY D 958 UNP Q9H2K2 EXPRESSION TAG
SEQRES 1 A 227 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 227 ARG GLU ASN LEU TYR PHE GLN GLY SER PRO ASP ASP LYS
SEQRES 3 A 227 GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER THR VAL
SEQRES 4 A 227 ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY ILE PHE
SEQRES 5 A 227 ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL CYS ASN
SEQRES 6 A 227 LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG LYS GLU
SEQRES 7 A 227 VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU ARG MET
SEQRES 8 A 227 LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE ILE HIS
SEQRES 9 A 227 LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY GLY MET
SEQRES 10 A 227 PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER SER LYS
SEQRES 11 A 227 SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY THR GLY
SEQRES 12 A 227 CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE CYS HIS
SEQRES 13 A 227 ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY LYS SER
SEQRES 14 A 227 PHE LEU GLN PHE SER ALA MET LYS MET ALA HIS SER PRO
SEQRES 15 A 227 PRO GLY HIS HIS SER VAL THR GLY ARG PRO SER VAL ASN
SEQRES 16 A 227 GLY LEU ALA LEU ALA GLU TYR VAL ILE TYR ARG GLY GLU
SEQRES 17 A 227 GLN ALA TYR PRO GLU TYR LEU ILE THR TYR GLN ILE MET
SEQRES 18 A 227 ARG PRO GLU GLY MET VAL
SEQRES 1 B 227 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 227 ARG GLU ASN LEU TYR PHE GLN GLY SER PRO ASP ASP LYS
SEQRES 3 B 227 GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER THR VAL
SEQRES 4 B 227 ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY ILE PHE
SEQRES 5 B 227 ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL CYS ASN
SEQRES 6 B 227 LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG LYS GLU
SEQRES 7 B 227 VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU ARG MET
SEQRES 8 B 227 LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE ILE HIS
SEQRES 9 B 227 LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY GLY MET
SEQRES 10 B 227 PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER SER LYS
SEQRES 11 B 227 SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY THR GLY
SEQRES 12 B 227 CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE CYS HIS
SEQRES 13 B 227 ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY LYS SER
SEQRES 14 B 227 PHE LEU GLN PHE SER ALA MET LYS MET ALA HIS SER PRO
SEQRES 15 B 227 PRO GLY HIS HIS SER VAL THR GLY ARG PRO SER VAL ASN
SEQRES 16 B 227 GLY LEU ALA LEU ALA GLU TYR VAL ILE TYR ARG GLY GLU
SEQRES 17 B 227 GLN ALA TYR PRO GLU TYR LEU ILE THR TYR GLN ILE MET
SEQRES 18 B 227 ARG PRO GLU GLY MET VAL
SEQRES 1 C 227 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 C 227 ARG GLU ASN LEU TYR PHE GLN GLY SER PRO ASP ASP LYS
SEQRES 3 C 227 GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER THR VAL
SEQRES 4 C 227 ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY ILE PHE
SEQRES 5 C 227 ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL CYS ASN
SEQRES 6 C 227 LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG LYS GLU
SEQRES 7 C 227 VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU ARG MET
SEQRES 8 C 227 LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE ILE HIS
SEQRES 9 C 227 LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY GLY MET
SEQRES 10 C 227 PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER SER LYS
SEQRES 11 C 227 SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY THR GLY
SEQRES 12 C 227 CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE CYS HIS
SEQRES 13 C 227 ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY LYS SER
SEQRES 14 C 227 PHE LEU GLN PHE SER ALA MET LYS MET ALA HIS SER PRO
SEQRES 15 C 227 PRO GLY HIS HIS SER VAL THR GLY ARG PRO SER VAL ASN
SEQRES 16 C 227 GLY LEU ALA LEU ALA GLU TYR VAL ILE TYR ARG GLY GLU
SEQRES 17 C 227 GLN ALA TYR PRO GLU TYR LEU ILE THR TYR GLN ILE MET
SEQRES 18 C 227 ARG PRO GLU GLY MET VAL
SEQRES 1 D 227 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 D 227 ARG GLU ASN LEU TYR PHE GLN GLY SER PRO ASP ASP LYS
SEQRES 3 D 227 GLU PHE GLN SER VAL GLU GLU GLU MET GLN SER THR VAL
SEQRES 4 D 227 ARG GLU HIS ARG ASP GLY GLY HIS ALA GLY GLY ILE PHE
SEQRES 5 D 227 ASN ARG TYR ASN ILE LEU LYS ILE GLN LYS VAL CYS ASN
SEQRES 6 D 227 LYS LYS LEU TRP GLU ARG TYR THR HIS ARG ARG LYS GLU
SEQRES 7 D 227 VAL SER GLU GLU ASN HIS ASN HIS ALA ASN GLU ARG MET
SEQRES 8 D 227 LEU PHE HIS GLY SER PRO PHE VAL ASN ALA ILE ILE HIS
SEQRES 9 D 227 LYS GLY PHE ASP GLU ARG HIS ALA TYR ILE GLY GLY MET
SEQRES 10 D 227 PHE GLY ALA GLY ILE TYR PHE ALA GLU ASN SER SER LYS
SEQRES 11 D 227 SER ASN GLN TYR VAL TYR GLY ILE GLY GLY GLY THR GLY
SEQRES 12 D 227 CYS PRO VAL HIS LYS ASP ARG SER CYS TYR ILE CYS HIS
SEQRES 13 D 227 ARG GLN LEU LEU PHE CYS ARG VAL THR LEU GLY LYS SER
SEQRES 14 D 227 PHE LEU GLN PHE SER ALA MET LYS MET ALA HIS SER PRO
SEQRES 15 D 227 PRO GLY HIS HIS SER VAL THR GLY ARG PRO SER VAL ASN
SEQRES 16 D 227 GLY LEU ALA LEU ALA GLU TYR VAL ILE TYR ARG GLY GLU
SEQRES 17 D 227 GLN ALA TYR PRO GLU TYR LEU ILE THR TYR GLN ILE MET
SEQRES 18 D 227 ARG PRO GLU GLY MET VAL
HET ZN A1201 1
HET UHB A1202 39
HET ZN B1201 1
HET UHB B1202 39
HET ZN C1201 1
HET UHB C1202 39
HET UHB D1201 39
HETNAM ZN ZINC ION
HETNAM UHB 2-[4-[(2S,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-
HETNAM 2 UHB BIS(OXIDANYL)OXOLAN-2-YL]CARBONYLPIPERAZIN-1-YL]-N-(1-
HETNAM 3 UHB OXIDANYLIDENE-2,3-DIHYDROISOINDOL-4-YL)ETHANAMIDE
FORMUL 5 ZN 3(ZN 2+)
FORMUL 6 UHB 4(C24 H27 N9 O6)
FORMUL 12 HOH *803(H2 O)
HELIX 1 AA1 ASP A 961 THR A 975 1 15
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 LYS B 963 THR B 975 1 13
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
HELIX 15 AB6 ASP C 962 THR C 975 1 14
HELIX 16 AB7 ASN C 1002 ASN C 1020 1 19
HELIX 17 AB8 PHE C 1035 GLY C 1043 1 9
HELIX 18 AB9 ASP C 1045 ALA C 1049 5 5
HELIX 19 AC1 ASN C 1064 GLN C 1070 1 7
HELIX 20 AC2 GLY C 1074 GLY C 1078 5 5
HELIX 21 AC3 ARG C 1143 GLU C 1145 5 3
HELIX 22 AC4 LYS D 963 THR D 975 1 13
HELIX 23 AC5 ASN D 1002 ASN D 1020 1 19
HELIX 24 AC6 PHE D 1035 GLY D 1043 1 9
HELIX 25 AC7 ASP D 1045 ALA D 1049 5 5
HELIX 26 AC8 ASN D 1064 GLN D 1070 1 7
HELIX 27 AC9 GLY D 1074 GLY D 1078 5 5
HELIX 28 AD1 ARG D 1143 GLU D 1145 5 3
SHEET 1 AA1 4 TYR A 992 LYS A 999 0
SHEET 2 AA1 4 ALA A1147 ILE A1157 -1 O LEU A1152 N GLN A 998
SHEET 3 AA1 4 ARG A1094 THR A1102 -1 N ARG A1094 O TYR A1155
SHEET 4 AA1 4 GLU A1026 HIS A1031 -1 N LEU A1029 O CYS A1099
SHEET 1 AA2 4 ILE A1059 PHE A1061 0
SHEET 2 AA2 4 GLU A1138 ILE A1141 -1 O ILE A1141 N ILE A1059
SHEET 3 AA2 4 SER A1124 GLY A1127 -1 N GLY A1127 O GLU A1138
SHEET 4 AA2 4 SER A1106 GLN A1109 1 N PHE A1107 O SER A1124
SHEET 1 AA3 5 TYR B 955 PHE B 956 0
SHEET 2 AA3 5 TYR B 992 VAL B1000 -1 O LYS B 999 N PHE B 956
SHEET 3 AA3 5 ALA B1147 ILE B1157 -1 O LEU B1152 N GLN B 998
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 PHE B1061 0
SHEET 2 AA4 4 GLU B1138 ILE B1141 -1 O ILE B1141 N ILE B1059
SHEET 3 AA4 4 SER B1124 GLY B1127 -1 N VAL B1125 O VAL B1140
SHEET 4 AA4 4 SER B1106 GLN B1109 1 N PHE B1107 O SER B1124
SHEET 1 AA5 5 TYR C 955 GLN C 957 0
SHEET 2 AA5 5 TYR C 992 VAL C1000 -1 O LYS C 999 N PHE C 956
SHEET 3 AA5 5 ALA C1147 ILE C1157 -1 O GLU C1150 N VAL C1000
SHEET 4 AA5 5 ARG C1094 THR C1102 -1 N ARG C1094 O TYR C1155
SHEET 5 AA5 5 GLU C1026 HIS C1031 -1 N LEU C1029 O CYS C1099
SHEET 1 AA6 4 ILE C1059 PHE C1061 0
SHEET 2 AA6 4 GLU C1138 ILE C1141 -1 O ILE C1141 N ILE C1059
SHEET 3 AA6 4 SER C1124 GLY C1127 -1 N VAL C1125 O VAL C1140
SHEET 4 AA6 4 SER C1106 GLN C1109 1 N PHE C1107 O SER C1124
SHEET 1 AA7 4 TYR D 992 LYS D 999 0
SHEET 2 AA7 4 ALA D1147 ILE D1157 -1 O LEU D1152 N GLN D 998
SHEET 3 AA7 4 ARG D1094 THR D1102 -1 N ARG D1094 O TYR D1155
SHEET 4 AA7 4 GLU D1026 HIS D1031 -1 N LEU D1029 O CYS D1099
SHEET 1 AA8 4 ILE D1059 PHE D1061 0
SHEET 2 AA8 4 GLU D1138 ILE D1141 -1 O ILE D1141 N ILE D1059
SHEET 3 AA8 4 SER D1124 GLY D1127 -1 N GLY D1127 O GLU D1138
SHEET 4 AA8 4 SER D1106 GLN D1109 1 N PHE D1107 O THR D1126
LINK SG CYS A1081 ZN ZN A1201 1555 1555 2.26
LINK ND1 HIS A1084 ZN ZN A1201 1555 1555 2.11
LINK SG CYS A1089 ZN ZN A1201 1555 1555 2.23
LINK SG CYS A1092 ZN ZN A1201 1555 1555 2.36
LINK SG CYS B1081 ZN ZN B1201 1555 1555 2.29
LINK ND1 HIS B1084 ZN ZN B1201 1555 1555 2.11
LINK SG CYS B1089 ZN ZN B1201 1555 1555 2.23
LINK SG CYS B1092 ZN ZN B1201 1555 1555 2.36
LINK SG CYS C1081 ZN ZN C1201 1555 1555 2.23
LINK ND1 HIS C1084 ZN ZN C1201 1555 1555 2.10
LINK SG CYS C1089 ZN ZN C1201 1555 1555 2.27
LINK SG CYS C1092 ZN ZN C1201 1555 1555 2.36
SITE 1 AC1 4 CYS A1081 HIS A1084 CYS A1089 CYS A1092
SITE 1 AC2 20 HIS A1031 GLY A1032 SER A1033 PHE A1035
SITE 2 AC2 20 ALA A1038 ILE A1039 GLY A1043 PHE A1044
SITE 3 AC2 20 ASP A1045 HIS A1048 ALA A1049 GLY A1058
SITE 4 AC2 20 TYR A1060 SER A1068 TYR A1071 HOH A1350
SITE 5 AC2 20 HOH A1377 HOH A1409 HOH A1423 HOH A1441
SITE 1 AC3 4 CYS B1081 HIS B1084 CYS B1089 CYS B1092
SITE 1 AC4 23 HIS B1031 GLY B1032 SER B1033 PHE B1035
SITE 2 AC4 23 ALA B1038 ILE B1039 GLY B1043 PHE B1044
SITE 3 AC4 23 ASP B1045 HIS B1048 ALA B1049 GLY B1058
SITE 4 AC4 23 TYR B1060 SER B1068 TYR B1071 ILE B1075
SITE 5 AC4 23 HOH B1363 HOH B1381 HOH B1390 HOH B1399
SITE 6 AC4 23 HOH B1413 HOH B1432 HOH B1447
SITE 1 AC5 4 CYS C1081 HIS C1084 CYS C1089 CYS C1092
SITE 1 AC6 19 HIS C1031 GLY C1032 SER C1033 ILE C1039
SITE 2 AC6 19 GLY C1043 PHE C1044 ASP C1045 HIS C1048
SITE 3 AC6 19 ALA C1049 TYR C1060 SER C1068 TYR C1071
SITE 4 AC6 19 ILE C1075 HOH C1344 HOH C1388 HOH C1391
SITE 5 AC6 19 HOH C1426 HOH C1470 HOH C1516
SITE 1 AC7 18 HIS D1031 GLY D1032 SER D1033 PHE D1035
SITE 2 AC7 18 ILE D1039 GLY D1043 PHE D1044 ASP D1045
SITE 3 AC7 18 HIS D1048 ALA D1049 GLY D1058 TYR D1060
SITE 4 AC7 18 SER D1068 TYR D1071 GLU D1138 HOH D1327
SITE 5 AC7 18 HOH D1382 HOH D1388
CRYST1 74.020 79.620 153.520 90.00 90.00 90.00 P 21 21 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 0.013510 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012560 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006514 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
