HEADER SIGNALING PROTEIN 22-SEP-11 3TWQ
TITLE CRYSTAL STRUCTURE OF ARC4 FROM HUMAN TANKYRASE 2 (APO FORM)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 484-655;
COMPND 5 SYNONYM: TANK2, POLY [ADP-RIBOSE] POLYMERASE 5B, TNKS-2, TRF1-
COMPND 6 INTERACTING ANKYRIN-RELATED ADP-RIBOSE POLYMERASE 2, TANKYRASE II,
COMPND 7 TANKYRASE-LIKE PROTEIN, TANKYRASE-RELATED PROTEIN;
COMPND 8 EC: 2.4.2.30;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: PARP5B, TANK2, TNKL, TNKS2;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS(DE3)-RIL;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PETM-30
KEYWDS ANKYRIN REPEAT, PROTEIN-PROTEIN INTERACTION, POLY(ADP-RIBOSYL)ATION,
KEYWDS 2 SUBSTRATE RECRUITMENT, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GUETTLER,F.SICHERI
REVDAT 3 28-FEB-24 3TWQ 1 REMARK SEQADV
REVDAT 2 28-DEC-11 3TWQ 1 JRNL
REVDAT 1 07-DEC-11 3TWQ 0
JRNL AUTH S.GUETTLER,J.LAROSE,E.PETSALAKI,G.GISH,A.SCOTTER,T.PAWSON,
JRNL AUTH 2 R.ROTTAPEL,F.SICHERI
JRNL TITL STRUCTURAL BASIS AND SEQUENCE RULES FOR SUBSTRATE
JRNL TITL 2 RECOGNITION BY TANKYRASE EXPLAIN THE BASIS FOR CHERUBISM
JRNL TITL 3 DISEASE.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 147 1340 2011
JRNL REFN ISSN 0092-8674
JRNL PMID 22153077
JRNL DOI 10.1016/J.CELL.2011.10.046
REMARK 2
REMARK 2 RESOLUTION. 2.15 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.15
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 36.93
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.500
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.0
REMARK 3 NUMBER OF REFLECTIONS : 17647
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.177
REMARK 3 R VALUE (WORKING SET) : 0.174
REMARK 3 FREE R VALUE : 0.235
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 905
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 36.9341 - 3.9079 0.96 2874 149 0.1679 0.2130
REMARK 3 2 3.9079 - 3.1023 0.98 2846 149 0.1521 0.2118
REMARK 3 3 3.1023 - 2.7103 0.97 2793 146 0.1784 0.2309
REMARK 3 4 2.7103 - 2.4625 0.97 2746 155 0.1725 0.2525
REMARK 3 5 2.4625 - 2.2861 0.97 2733 160 0.1900 0.2717
REMARK 3 6 2.2861 - 2.1510 0.97 2750 146 0.2229 0.2834
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.38
REMARK 3 B_SOL : 32.76
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.560
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.750
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.38510
REMARK 3 B22 (A**2) : -0.38510
REMARK 3 B33 (A**2) : 0.77010
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 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 2568
REMARK 3 ANGLE : 1.046 3474
REMARK 3 CHIRALITY : 0.070 390
REMARK 3 PLANARITY : 0.005 450
REMARK 3 DIHEDRAL : 13.187 934
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 481:502)
REMARK 3 ORIGIN FOR THE GROUP (A): 4.3883 -11.0488 14.0414
REMARK 3 T TENSOR
REMARK 3 T11: 0.1108 T22: 0.2041
REMARK 3 T33: 0.1179 T12: -0.0352
REMARK 3 T13: 0.0053 T23: 0.0122
REMARK 3 L TENSOR
REMARK 3 L11: 0.3658 L22: 6.8191
REMARK 3 L33: 1.6172 L12: -1.5029
REMARK 3 L13: 0.7089 L23: -2.9744
REMARK 3 S TENSOR
REMARK 3 S11: -0.1829 S12: 0.1701 S13: 0.0579
REMARK 3 S21: 0.0139 S22: 0.3109 S23: 0.1754
REMARK 3 S31: 0.0270 S32: -0.3086 S33: -0.1318
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 503:521)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.4338 -19.3751 16.4010
REMARK 3 T TENSOR
REMARK 3 T11: 0.1960 T22: 0.1167
REMARK 3 T33: 0.1196 T12: -0.0474
REMARK 3 T13: 0.0619 T23: -0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 1.3763 L22: 2.3726
REMARK 3 L33: 1.2297 L12: 0.7507
REMARK 3 L13: -0.8823 L23: -0.4043
REMARK 3 S TENSOR
REMARK 3 S11: -0.1744 S12: 0.1484 S13: -0.0784
REMARK 3 S21: -0.7830 S22: 0.2550 S23: -0.4982
REMARK 3 S31: -0.0282 S32: 0.1580 S33: -0.0459
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 522:538)
REMARK 3 ORIGIN FOR THE GROUP (A): 5.8807 -14.5728 25.4311
REMARK 3 T TENSOR
REMARK 3 T11: 0.1057 T22: 0.0841
REMARK 3 T33: 0.0860 T12: 0.0114
REMARK 3 T13: 0.0169 T23: 0.0150
REMARK 3 L TENSOR
REMARK 3 L11: 2.2952 L22: 4.3648
REMARK 3 L33: 1.8271 L12: 1.1591
REMARK 3 L13: -0.9835 L23: 0.4321
REMARK 3 S TENSOR
REMARK 3 S11: 0.0163 S12: 0.0917 S13: 0.1647
REMARK 3 S21: -0.0979 S22: 0.0719 S23: 0.2395
REMARK 3 S31: 0.0409 S32: -0.2070 S33: -0.0046
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 539:571)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.2437 -16.0183 29.3958
REMARK 3 T TENSOR
REMARK 3 T11: 0.1004 T22: 0.0875
REMARK 3 T33: 0.0727 T12: -0.0133
REMARK 3 T13: 0.0037 T23: 0.0137
REMARK 3 L TENSOR
REMARK 3 L11: 1.6778 L22: 2.4779
REMARK 3 L33: 1.9076 L12: 1.0929
REMARK 3 L13: -0.1891 L23: 0.2296
REMARK 3 S TENSOR
REMARK 3 S11: -0.0382 S12: -0.0026 S13: -0.1667
REMARK 3 S21: 0.0343 S22: 0.0044 S23: -0.0585
REMARK 3 S31: 0.0485 S32: 0.0300 S33: -0.0172
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 572:580)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.1680 -22.2077 36.0329
REMARK 3 T TENSOR
REMARK 3 T11: 0.2585 T22: 0.1211
REMARK 3 T33: 0.1120 T12: 0.0666
REMARK 3 T13: -0.0351 T23: 0.0409
REMARK 3 L TENSOR
REMARK 3 L11: 6.0783 L22: 4.5295
REMARK 3 L33: 8.7296 L12: 1.8873
REMARK 3 L13: -1.9546 L23: -3.7026
REMARK 3 S TENSOR
REMARK 3 S11: 0.1696 S12: -0.3040 S13: -0.6724
REMARK 3 S21: 0.0893 S22: -0.0869 S23: -0.2527
REMARK 3 S31: 0.3056 S32: 0.5212 S33: 0.1339
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 581:594)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.9743 -6.9033 37.5316
REMARK 3 T TENSOR
REMARK 3 T11: 0.0485 T22: 0.1336
REMARK 3 T33: 0.1322 T12: -0.1221
REMARK 3 T13: -0.0397 T23: -0.0306
REMARK 3 L TENSOR
REMARK 3 L11: 4.7038 L22: 1.4552
REMARK 3 L33: 1.0544 L12: -1.3753
REMARK 3 L13: 0.4241 L23: -1.0032
REMARK 3 S TENSOR
REMARK 3 S11: -0.0304 S12: 0.3396 S13: -0.1078
REMARK 3 S21: -0.0214 S22: -0.1102 S23: -0.0035
REMARK 3 S31: 0.0409 S32: 0.1088 S33: 0.0495
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 595:614)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.9780 -16.7454 45.1291
REMARK 3 T TENSOR
REMARK 3 T11: 0.0986 T22: 0.1030
REMARK 3 T33: 0.0587 T12: 0.0062
REMARK 3 T13: -0.0087 T23: -0.0014
REMARK 3 L TENSOR
REMARK 3 L11: 4.4432 L22: 6.1726
REMARK 3 L33: 4.7226 L12: 1.2060
REMARK 3 L13: -1.8309 L23: 0.1998
REMARK 3 S TENSOR
REMARK 3 S11: -0.1547 S12: -0.1688 S13: -0.2598
REMARK 3 S21: -0.1039 S22: 0.1483 S23: 0.0665
REMARK 3 S31: 0.3105 S32: -0.1050 S33: -0.0063
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESSEQ 615:644)
REMARK 3 ORIGIN FOR THE GROUP (A): 9.0743 -9.6407 51.4670
REMARK 3 T TENSOR
REMARK 3 T11: 0.1023 T22: 0.1289
REMARK 3 T33: 0.0763 T12: 0.0140
REMARK 3 T13: -0.0088 T23: 0.0054
REMARK 3 L TENSOR
REMARK 3 L11: 3.2868 L22: 3.8197
REMARK 3 L33: 0.8200 L12: -1.3639
REMARK 3 L13: -0.3414 L23: -0.2341
REMARK 3 S TENSOR
REMARK 3 S11: -0.0563 S12: -0.3992 S13: -0.0721
REMARK 3 S21: 0.2197 S22: 0.0416 S23: 0.0891
REMARK 3 S31: 0.1337 S32: 0.0639 S33: 0.0201
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 481:502)
REMARK 3 ORIGIN FOR THE GROUP (A): 12.5748 4.0985 28.2241
REMARK 3 T TENSOR
REMARK 3 T11: 0.1587 T22: 0.0795
REMARK 3 T33: 0.0878 T12: -0.0073
REMARK 3 T13: 0.0039 T23: -0.0260
REMARK 3 L TENSOR
REMARK 3 L11: 6.8411 L22: 0.4260
REMARK 3 L33: 1.1203 L12: 1.6047
REMARK 3 L13: -2.4455 L23: -0.4617
REMARK 3 S TENSOR
REMARK 3 S11: 0.0915 S12: -0.0609 S13: 0.4626
REMARK 3 S21: 0.0945 S22: 0.0156 S23: 0.1431
REMARK 3 S31: -0.0709 S32: 0.0129 S33: -0.1008
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 503:561)
REMARK 3 ORIGIN FOR THE GROUP (A): 20.9575 1.1584 19.7906
REMARK 3 T TENSOR
REMARK 3 T11: 0.0856 T22: 0.0742
REMARK 3 T33: 0.0854 T12: -0.0072
REMARK 3 T13: 0.0048 T23: 0.0089
REMARK 3 L TENSOR
REMARK 3 L11: 2.3697 L22: 2.1131
REMARK 3 L33: 2.8896 L12: 1.2161
REMARK 3 L13: 0.7994 L23: 0.0275
REMARK 3 S TENSOR
REMARK 3 S11: 0.1865 S12: -0.0921 S13: -0.0547
REMARK 3 S21: 0.0518 S22: -0.1238 S23: -0.0061
REMARK 3 S31: 0.0822 S32: -0.0359 S33: -0.0666
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 562:581)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.4902 0.5563 7.3457
REMARK 3 T TENSOR
REMARK 3 T11: 0.0650 T22: 0.1411
REMARK 3 T33: 0.0509 T12: -0.0089
REMARK 3 T13: -0.0001 T23: -0.0028
REMARK 3 L TENSOR
REMARK 3 L11: 2.4430 L22: 7.0910
REMARK 3 L33: 5.0312 L12: 0.2703
REMARK 3 L13: 1.2701 L23: -1.9968
REMARK 3 S TENSOR
REMARK 3 S11: 0.0173 S12: 0.1164 S13: -0.1898
REMARK 3 S21: -0.2180 S22: 0.1102 S23: -0.3621
REMARK 3 S31: 0.0153 S32: 0.3725 S33: -0.0525
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESSEQ 582:644)
REMARK 3 ORIGIN FOR THE GROUP (A): 17.1888 -2.6229 -4.1574
REMARK 3 T TENSOR
REMARK 3 T11: 0.1664 T22: 0.1174
REMARK 3 T33: 0.1022 T12: 0.0282
REMARK 3 T13: -0.0037 T23: -0.0287
REMARK 3 L TENSOR
REMARK 3 L11: 1.5066 L22: 1.7278
REMARK 3 L33: 3.0478 L12: -0.3718
REMARK 3 L13: 0.1097 L23: -0.8336
REMARK 3 S TENSOR
REMARK 3 S11: 0.0288 S12: 0.2245 S13: -0.0119
REMARK 3 S21: -0.2128 S22: -0.0727 S23: -0.1907
REMARK 3 S31: 0.2877 S32: 0.3371 S33: -0.0015
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 3TWQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-SEP-11.
REMARK 100 THE DEPOSITION ID IS D_1000068015.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-JUL-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 24-ID-E
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9792
REMARK 200 MONOCHROMATOR : SI (220), SI (311)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 17759
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.150
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.2
REMARK 200 DATA REDUNDANCY : 3.100
REMARK 200 R MERGE (I) : 0.15400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.15
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.23
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : 3.10
REMARK 200 R MERGE FOR SHELL (I) : 0.59200
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 43.31
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M HEPES-NAOH PH 8.0, 0.2 M LI2SO4,
REMARK 280 35% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 1 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+1/3
REMARK 290 3555 -X+Y,-X,Z+2/3
REMARK 290 4555 -Y,-X,-Z+2/3
REMARK 290 5555 -X+Y,Y,-Z+1/3
REMARK 290 6555 X,X-Y,-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 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 83.64500
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 167.29000
REMARK 290 SMTRY1 4 0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 167.29000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 83.64500
REMARK 290 SMTRY1 6 0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4130 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14440 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -70.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 156 LIES ON A SPECIAL POSITION.
REMARK 375 HOH B 133 LIES ON A SPECIAL POSITION.
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 GLY A 645
REMARK 465 ASP A 646
REMARK 465 ALA A 647
REMARK 465 ALA A 648
REMARK 465 LEU A 649
REMARK 465 LEU A 650
REMARK 465 ASP A 651
REMARK 465 ALA A 652
REMARK 465 ALA A 653
REMARK 465 LYS A 654
REMARK 465 LYS A 655
REMARK 465 GLY B 645
REMARK 465 ASP B 646
REMARK 465 ALA B 647
REMARK 465 ALA B 648
REMARK 465 LEU B 649
REMARK 465 LEU B 650
REMARK 465 ASP B 651
REMARK 465 ALA B 652
REMARK 465 ALA B 653
REMARK 465 LYS B 654
REMARK 465 LYS B 655
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O VAL B 585 O HOH B 34 2.17
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH B 155 O HOH B 155 5555 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 ASP A 589 -167.61 -75.99
REMARK 500
REMARK 500 REMARK: NULL
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 2
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 5
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 656
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 3
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 4
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TWR RELATED DB: PDB
REMARK 900 RELATED ID: 3TWS RELATED DB: PDB
REMARK 900 RELATED ID: 3TWT RELATED DB: PDB
REMARK 900 RELATED ID: 3TWU RELATED DB: PDB
REMARK 900 RELATED ID: 3TWV RELATED DB: PDB
REMARK 900 RELATED ID: 3TWW RELATED DB: PDB
REMARK 900 RELATED ID: 3TWX RELATED DB: PDB
DBREF 3TWQ A 484 655 UNP Q9H2K2 TNKS2_HUMAN 484 655
DBREF 3TWQ B 484 655 UNP Q9H2K2 TNKS2_HUMAN 484 655
SEQADV 3TWQ GLY A 481 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWQ ALA A 482 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWQ MET A 483 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWQ GLY B 481 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWQ ALA B 482 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWQ MET B 483 UNP Q9H2K2 EXPRESSION TAG
SEQRES 1 A 175 GLY ALA MET GLY ILE SER LEU GLY ASN SER GLU ALA ASP
SEQRES 2 A 175 ARG GLN LEU LEU GLU ALA ALA LYS ALA GLY ASP VAL GLU
SEQRES 3 A 175 THR VAL LYS LYS LEU CYS THR VAL GLN SER VAL ASN CYS
SEQRES 4 A 175 ARG ASP ILE GLU GLY ARG GLN SER THR PRO LEU HIS PHE
SEQRES 5 A 175 ALA ALA GLY TYR ASN ARG VAL SER VAL VAL GLU TYR LEU
SEQRES 6 A 175 LEU GLN HIS GLY ALA ASP VAL HIS ALA LYS ASP LYS GLY
SEQRES 7 A 175 GLY LEU VAL PRO LEU HIS ASN ALA CYS SER TYR GLY HIS
SEQRES 8 A 175 TYR GLU VAL ALA GLU LEU LEU VAL LYS HIS GLY ALA VAL
SEQRES 9 A 175 VAL ASN VAL ALA ASP LEU TRP LYS PHE THR PRO LEU HIS
SEQRES 10 A 175 GLU ALA ALA ALA LYS GLY LYS TYR GLU ILE CYS LYS LEU
SEQRES 11 A 175 LEU LEU GLN HIS GLY ALA ASP PRO THR LYS LYS ASN ARG
SEQRES 12 A 175 ASP GLY ASN THR PRO LEU ASP LEU VAL LYS ASP GLY ASP
SEQRES 13 A 175 THR ASP ILE GLN ASP LEU LEU ARG GLY ASP ALA ALA LEU
SEQRES 14 A 175 LEU ASP ALA ALA LYS LYS
SEQRES 1 B 175 GLY ALA MET GLY ILE SER LEU GLY ASN SER GLU ALA ASP
SEQRES 2 B 175 ARG GLN LEU LEU GLU ALA ALA LYS ALA GLY ASP VAL GLU
SEQRES 3 B 175 THR VAL LYS LYS LEU CYS THR VAL GLN SER VAL ASN CYS
SEQRES 4 B 175 ARG ASP ILE GLU GLY ARG GLN SER THR PRO LEU HIS PHE
SEQRES 5 B 175 ALA ALA GLY TYR ASN ARG VAL SER VAL VAL GLU TYR LEU
SEQRES 6 B 175 LEU GLN HIS GLY ALA ASP VAL HIS ALA LYS ASP LYS GLY
SEQRES 7 B 175 GLY LEU VAL PRO LEU HIS ASN ALA CYS SER TYR GLY HIS
SEQRES 8 B 175 TYR GLU VAL ALA GLU LEU LEU VAL LYS HIS GLY ALA VAL
SEQRES 9 B 175 VAL ASN VAL ALA ASP LEU TRP LYS PHE THR PRO LEU HIS
SEQRES 10 B 175 GLU ALA ALA ALA LYS GLY LYS TYR GLU ILE CYS LYS LEU
SEQRES 11 B 175 LEU LEU GLN HIS GLY ALA ASP PRO THR LYS LYS ASN ARG
SEQRES 12 B 175 ASP GLY ASN THR PRO LEU ASP LEU VAL LYS ASP GLY ASP
SEQRES 13 B 175 THR ASP ILE GLN ASP LEU LEU ARG GLY ASP ALA ALA LEU
SEQRES 14 B 175 LEU ASP ALA ALA LYS LYS
HET SO4 A 1 5
HET SO4 A 2 5
HET SO4 A 5 5
HET GOL A 656 6
HET SO4 B 3 5
HET SO4 B 4 5
HET GOL B 2 6
HETNAM SO4 SULFATE ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 3 SO4 5(O4 S 2-)
FORMUL 6 GOL 2(C3 H8 O3)
FORMUL 10 HOH *157(H2 O)
HELIX 1 1 SER A 490 GLY A 503 1 14
HELIX 2 2 ASP A 504 CYS A 512 1 9
HELIX 3 3 THR A 528 TYR A 536 1 9
HELIX 4 4 ARG A 538 HIS A 548 1 11
HELIX 5 5 VAL A 561 GLY A 570 1 10
HELIX 6 6 HIS A 571 HIS A 581 1 11
HELIX 7 7 THR A 594 GLY A 603 1 10
HELIX 8 8 LYS A 604 HIS A 614 1 11
HELIX 9 9 THR A 627 VAL A 632 5 6
HELIX 10 10 ASP A 636 ARG A 644 1 9
HELIX 11 11 SER B 490 GLY B 503 1 14
HELIX 12 12 ASP B 504 CYS B 512 1 9
HELIX 13 13 THR B 528 TYR B 536 1 9
HELIX 14 14 ARG B 538 GLN B 547 1 10
HELIX 15 15 VAL B 561 TYR B 569 1 9
HELIX 16 16 HIS B 571 HIS B 581 1 11
HELIX 17 17 THR B 594 GLY B 603 1 10
HELIX 18 18 LYS B 604 HIS B 614 1 11
HELIX 19 19 THR B 627 VAL B 632 1 6
HELIX 20 20 ASP B 636 ARG B 644 1 9
SITE 1 AC1 5 HOH A 69 HOH A 145 GLY A 603 TYR A 605
SITE 2 AC1 5 GLU A 606
SITE 1 AC2 6 HOH A 82 HOH A 88 ASN A 537 GLY A 570
SITE 2 AC2 6 TYR A 572 GLU A 573
SITE 1 AC3 3 LYS A 592 SER B 490 GLU B 491
SITE 1 AC4 6 ARG A 494 GLU A 498 LYS A 501 GLU A 523
SITE 2 AC4 6 PHE A 532 GLY A 635
SITE 1 AC5 7 HOH B 104 HOH B 125 ASN B 537 GLY B 570
SITE 2 AC5 7 HIS B 571 TYR B 572 GLU B 573
SITE 1 AC6 5 HOH B 128 GLY B 603 LYS B 604 TYR B 605
SITE 2 AC6 5 GLU B 606
SITE 1 AC7 6 HOH B 32 LEU B 497 GLU B 498 LYS B 501
SITE 2 AC7 6 ASP B 521 PHE B 532
CRYST1 47.524 47.524 250.935 90.00 90.00 120.00 P 31 1 2 12
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 0.021042 0.012149 0.000000 0.00000
SCALE2 0.000000 0.024297 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003985 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
