HEADER TRANSFERASE 25-MAY-14 4TK0
TITLE CRYSTAL STRUCTURE OF HUMAN TANKYRASE 2 IN COMPLEX WITH DPQ.
CAVEAT 4TK0 RESIDUE 1202 A 32Z HAS POOR RSR Z-SCORE
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 4TK0 1 REMARK
REVDAT 3 22-NOV-17 4TK0 1 SOURCE REMARK
REVDAT 2 07-JAN-15 4TK0 1 JRNL
REVDAT 1 05-NOV-14 4TK0 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. 1.65 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) : 1.65
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 76.82
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 92.0
REMARK 3 NUMBER OF REFLECTIONS : 100882
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) : 0.188
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 0.990
REMARK 3 FREE R VALUE TEST SET COUNT : 997
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) : 1.65
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.69
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.97
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 6702
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2115
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 6631
REMARK 3 BIN R VALUE (WORKING SET) : 0.2112
REMARK 3 BIN FREE R VALUE : 0.2416
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 1.06
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 71
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 : 6483
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 69
REMARK 3 SOLVENT ATOMS : 932
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 23.04
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.07
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.99280
REMARK 3 B22 (A**2) : -0.95600
REMARK 3 B33 (A**2) : 2.94880
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) : 0.217
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.110
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.108
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.103
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.104
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 : 0.957
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.937
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6831 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9264 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2567 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 151 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1012 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6831 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : 1 ; 5.000 ; SEMIHARMONIC
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 796 ; 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 : 7981 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 1.06
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 4.11
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.73
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): 18.5651 49.3494 -1.3332
REMARK 3 T TENSOR
REMARK 3 T11: -0.0081 T22: -0.0394
REMARK 3 T33: -0.0740 T12: -0.0218
REMARK 3 T13: 0.0075 T23: 0.0086
REMARK 3 L TENSOR
REMARK 3 L11: 1.0830 L22: 0.4044
REMARK 3 L33: 2.6329 L12: -0.2239
REMARK 3 L13: 0.3030 L23: -0.6062
REMARK 3 S TENSOR
REMARK 3 S11: 0.0528 S12: 0.1966 S13: 0.0463
REMARK 3 S21: 0.0521 S22: -0.1133 S23: -0.0273
REMARK 3 S31: -0.1333 S32: 0.1993 S33: 0.0604
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0149 -9.3533 36.7777
REMARK 3 T TENSOR
REMARK 3 T11: -0.0441 T22: -0.0378
REMARK 3 T33: -0.0670 T12: 0.0113
REMARK 3 T13: -0.0047 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 1.2612 L22: 0.9886
REMARK 3 L33: 1.6519 L12: -0.2627
REMARK 3 L13: 0.1297 L23: -0.3343
REMARK 3 S TENSOR
REMARK 3 S11: -0.0424 S12: -0.2120 S13: -0.0313
REMARK 3 S21: -0.0403 S22: 0.0616 S23: -0.0383
REMARK 3 S31: 0.0214 S32: -0.0126 S33: -0.0192
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { C|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.7321 32.0993 31.5791
REMARK 3 T TENSOR
REMARK 3 T11: -0.0394 T22: -0.0531
REMARK 3 T33: -0.0637 T12: -0.0245
REMARK 3 T13: 0.0065 T23: -0.0033
REMARK 3 L TENSOR
REMARK 3 L11: 1.0639 L22: 1.0092
REMARK 3 L33: 1.7063 L12: -0.3761
REMARK 3 L13: -0.1614 L23: -0.3224
REMARK 3 S TENSOR
REMARK 3 S11: -0.0104 S12: -0.1464 S13: -0.0121
REMARK 3 S21: -0.0298 S22: 0.0515 S23: 0.0022
REMARK 3 S31: -0.0395 S32: 0.0688 S33: -0.0411
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { D|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 18.1500 8.5315 4.4242
REMARK 3 T TENSOR
REMARK 3 T11: 0.0371 T22: -0.0178
REMARK 3 T33: -0.0688 T12: -0.0739
REMARK 3 T13: 0.0081 T23: 0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 0.9182 L22: 0.0000
REMARK 3 L33: 1.6353 L12: -0.6387
REMARK 3 L13: 0.2340 L23: -0.1872
REMARK 3 S TENSOR
REMARK 3 S11: 0.0143 S12: 0.2261 S13: 0.1025
REMARK 3 S21: -0.0095 S22: -0.1115 S23: -0.0530
REMARK 3 S31: -0.0394 S32: 0.1341 S33: 0.0972
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4TK0 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_1000201768.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-AUG-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 : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS 2005/3, XPREP
REMARK 200 DATA SCALING SOFTWARE : XPREP
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 101327
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.650
REMARK 200 RESOLUTION RANGE LOW (A) : 79.570
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 92.4
REMARK 200 DATA REDUNDANCY : 6.470
REMARK 200 R MERGE (I) : 0.06200
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 18.4500
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.65
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.67
REMARK 200 COMPLETENESS FOR SHELL (%) : 77.6
REMARK 200 DATA REDUNDANCY IN SHELL : 3.57
REMARK 200 R MERGE FOR SHELL (I) : 0.60200
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 (%): 43.50
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 37.02000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 76.82000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.78500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 76.82000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 37.02000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.78500
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 PRO A 960
REMARK 465 ASP A 961
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 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 ASP D 962
REMARK 465 LYS D 963
REMARK 465 PRO D 1129
REMARK 465 SER D 1130
REMARK 465 VAL D 1131
REMARK 465 ASN D 1132
REMARK 465 GLY D 1133
REMARK 465 LEU D 1134
REMARK 465 ALA D 1135
REMARK 465 GLU D 1161
REMARK 465 GLY D 1162
REMARK 465 MET D 1163
REMARK 465 VAL D 1164
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 MET A1113 88.32 -150.73
REMARK 500 ASN B1022 30.09 70.66
REMARK 500 ASN B1132 -0.55 83.03
REMARK 500 ILE D1051 -0.05 -55.19
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 A1391 DISTANCE = 7.55 ANGSTROMS
REMARK 525 HOH B1467 DISTANCE = 7.96 ANGSTROMS
REMARK 525 HOH B1494 DISTANCE = 7.01 ANGSTROMS
REMARK 525 HOH C1488 DISTANCE = 9.74 ANGSTROMS
REMARK 525 HOH C1541 DISTANCE = 6.73 ANGSTROMS
REMARK 525 HOH D1260 DISTANCE = 7.79 ANGSTROMS
REMARK 525 HOH D1275 DISTANCE = 6.08 ANGSTROMS
REMARK 525 HOH D1393 DISTANCE = 9.10 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 111.5
REMARK 620 3 CYS A1089 SG 108.0 107.7
REMARK 620 4 CYS A1092 SG 116.7 98.5 114.0
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 112.5
REMARK 620 3 CYS B1089 SG 110.4 104.4
REMARK 620 4 CYS B1092 SG 117.0 100.0 111.5
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 111.6
REMARK 620 3 CYS C1089 SG 110.2 106.9
REMARK 620 4 CYS C1092 SG 115.1 100.0 112.4
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 32Z 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 32Z 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 32Z C 1202
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: 4TK5 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 4TK0 A 959 1164 UNP Q9H2K2 TNKS2_HUMAN 959 1164
DBREF 4TK0 B 959 1164 UNP Q9H2K2 TNKS2_HUMAN 959 1164
DBREF 4TK0 C 959 1164 UNP Q9H2K2 TNKS2_HUMAN 959 1164
DBREF 4TK0 D 959 1164 UNP Q9H2K2 TNKS2_HUMAN 959 1164
SEQADV 4TK0 MET A 938 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 4TK0 GLY A 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER A 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER A 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS A 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS A 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS A 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS A 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS A 946 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS A 947 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER A 948 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER A 949 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLY A 950 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 ARG A 951 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLU A 952 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 ASN A 953 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 LEU A 954 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 TYR A 955 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 PHE A 956 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLN A 957 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLY A 958 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 MET B 938 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 4TK0 GLY B 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER B 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER B 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS B 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS B 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS B 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS B 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS B 946 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS B 947 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER B 948 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER B 949 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLY B 950 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 ARG B 951 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLU B 952 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 ASN B 953 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 LEU B 954 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 TYR B 955 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 PHE B 956 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLN B 957 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLY B 958 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 MET C 938 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 4TK0 GLY C 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER C 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER C 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS C 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS C 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS C 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS C 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS C 946 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS C 947 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER C 948 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER C 949 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLY C 950 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 ARG C 951 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLU C 952 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 ASN C 953 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 LEU C 954 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 TYR C 955 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 PHE C 956 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLN C 957 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLY C 958 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 MET D 938 UNP Q9H2K2 INITIATING METHIONINE
SEQADV 4TK0 GLY D 939 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER D 940 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER D 941 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS D 942 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS D 943 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS D 944 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS D 945 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS D 946 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 HIS D 947 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER D 948 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 SER D 949 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLY D 950 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 ARG D 951 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLU D 952 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 ASN D 953 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 LEU D 954 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 TYR D 955 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 PHE D 956 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 GLN D 957 UNP Q9H2K2 EXPRESSION TAG
SEQADV 4TK0 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 32Z A1202 48
HET ZN B1201 1
HET 32Z B1202 48
HET ZN C1201 1
HET 32Z C1202 48
HETNAM ZN ZINC ION
HETNAM 32Z 5-[4-(PIPERIDIN-1-YL)BUTOXY]-3,4-DIHYDROISOQUINOLIN-
HETNAM 2 32Z 1(2H)-ONE
FORMUL 5 ZN 3(ZN 2+)
FORMUL 6 32Z 3(C18 H26 N2 O2)
FORMUL 11 HOH *932(H2 O)
HELIX 1 AA1 ASP A 962 THR A 975 1 14
HELIX 2 AA2 ASN A 1002 GLU A 1019 1 18
HELIX 3 AA3 PHE A 1035 GLY A 1043 1 9
HELIX 4 AA4 ASP A 1045 ALA A 1049 5 5
HELIX 5 AA5 ASN A 1064 GLN A 1070 1 7
HELIX 6 AA6 GLY A 1074 GLY A 1078 5 5
HELIX 7 AA7 ARG A 1143 GLU A 1145 5 3
HELIX 8 AA8 ASP B 962 THR B 975 1 14
HELIX 9 AA9 ASN B 1002 GLU B 1019 1 18
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 GLU C 1019 1 18
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 PHE D 965 THR D 975 1 11
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 THR A1154 N LYS A 996
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 VAL A1125 O VAL A1140
SHEET 4 AA2 4 SER A1106 GLN A1109 1 N PHE A1107 O THR A1126
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 GLU B1150 N VAL B1000
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 THR C1126
SHEET 1 AA7 4 TYR D 992 LYS D 999 0
SHEET 2 AA7 4 ALA D1147 ILE D1157 -1 O THR D1154 N LYS D 996
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 ALA D1062 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 2.08
LINK SG CYS A1089 ZN ZN A1201 1555 1555 2.17
LINK SG CYS A1092 ZN ZN A1201 1555 1555 2.36
LINK SG CYS B1081 ZN ZN B1201 1555 1555 2.27
LINK ND1 HIS B1084 ZN ZN B1201 1555 1555 2.07
LINK SG CYS B1089 ZN ZN B1201 1555 1555 2.24
LINK SG CYS B1092 ZN ZN B1201 1555 1555 2.35
LINK SG CYS C1081 ZN ZN C1201 1555 1555 2.27
LINK ND1 HIS C1084 ZN ZN C1201 1555 1555 2.05
LINK SG CYS C1089 ZN ZN C1201 1555 1555 2.27
LINK SG CYS C1092 ZN ZN C1201 1555 1555 2.33
CISPEP 1 ASN A 1132 GLY A 1133 0 -7.01
SITE 1 AC1 4 CYS A1081 HIS A1084 CYS A1089 CYS A1092
SITE 1 AC2 8 HIS A1031 GLY A1032 GLY A1053 TYR A1060
SITE 2 AC2 8 PHE A1061 SER A1068 TYR A1071 GLU A1138
SITE 1 AC3 4 CYS B1081 HIS B1084 CYS B1089 CYS B1092
SITE 1 AC4 8 HIS B1031 GLY B1032 TYR B1060 PHE B1061
SITE 2 AC4 8 LYS B1067 SER B1068 TYR B1071 HOH B1505
SITE 1 AC5 4 CYS C1081 HIS C1084 CYS C1089 CYS C1092
SITE 1 AC6 10 HIS C1031 GLY C1032 TYR C1060 PHE C1061
SITE 2 AC6 10 LYS C1067 SER C1068 TYR C1071 ILE C1075
SITE 3 AC6 10 GLU C1138 HOH C1437
CRYST1 74.040 79.570 153.640 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 0.013506 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012568 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006509 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
