HEADER SIGNALING PROTEIN/PEPTIDE 22-SEP-11 3TWW
TITLE CRYSTAL STRUCTURE OF ARC4 FROM HUMAN TANKYRASE 2 IN COMPLEX WITH
TITLE 2 PEPTIDE FROM HUMAN LNPEP (CHIMERIC PEPTIDE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TANKYRASE-2;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: UNP RESIDUES 488-649;
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;
COMPND 10 MOL_ID: 2;
COMPND 11 MOLECULE: HUMAN LNPEP;
COMPND 12 CHAIN: C, D;
COMPND 13 ENGINEERED: YES;
COMPND 14 OTHER_DETAILS: CHIMERIC PEPTIDE FROM HUMAN LNPEP
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;
SOURCE 11 MOL_ID: 2;
SOURCE 12 SYNTHETIC: YES;
SOURCE 13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 14 ORGANISM_COMMON: HUMAN;
SOURCE 15 ORGANISM_TAXID: 9606;
SOURCE 16 OTHER_DETAILS: SOLID-STATE SYNTHESIZED PEPTIDE
KEYWDS ANKYRIN REPEAT, PROTEIN-PROTEIN INTERACTION, SUBSTRATE RECRUITMENT,
KEYWDS 2 POLY(ADP-RIBOSYL)ATION, SIGNALING PROTEIN-PEPTIDE COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR S.GUETTLER,F.SICHERI
REVDAT 2 28-DEC-11 3TWW 1 JRNL
REVDAT 1 07-DEC-11 3TWW 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. 2.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-
REMARK 3 : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,
REMARK 3 : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL
REMARK 3 : MORIARTY,REETAL PAI,RANDY READ,JANE
REMARK 3 : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM
REMARK 3 : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,
REMARK 3 : LAURENT STORONI,TOM TERWILLIGER,PETER
REMARK 3 : ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 35.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.490
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 3 NUMBER OF REFLECTIONS : 23224
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.221
REMARK 3 R VALUE (WORKING SET) : 0.218
REMARK 3 FREE R VALUE : 0.268
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 1192
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 35.7380 - 4.1583 0.92 2465 127 0.2365 0.2536
REMARK 3 2 4.1583 - 3.3013 0.92 2315 158 0.1904 0.2459
REMARK 3 3 3.3013 - 2.8842 0.98 2459 135 0.2006 0.2526
REMARK 3 4 2.8842 - 2.6206 0.99 2478 118 0.2149 0.2649
REMARK 3 5 2.6206 - 2.4328 0.99 2495 136 0.1949 0.2749
REMARK 3 6 2.4328 - 2.2894 1.00 2455 130 0.2178 0.2774
REMARK 3 7 2.2894 - 2.1748 0.99 2455 127 0.2331 0.3316
REMARK 3 8 2.1748 - 2.0801 0.99 2438 144 0.2578 0.3478
REMARK 3 9 2.0801 - 2.0000 1.00 2472 117 0.2851 0.3505
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.30
REMARK 3 SHRINKAGE RADIUS : 1.06
REMARK 3 K_SOL : 0.35
REMARK 3 B_SOL : 50.83
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.630
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.010
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) : 3.87110
REMARK 3 B22 (A**2) : 0.12070
REMARK 3 B33 (A**2) : -3.99180
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 : 0.008 2668
REMARK 3 ANGLE : 1.051 3610
REMARK 3 CHIRALITY : 0.073 399
REMARK 3 PLANARITY : 0.005 479
REMARK 3 DIHEDRAL : 15.512 988
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 20
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: chain 'A' and (resseq 488:502)
REMARK 3 ORIGIN FOR THE GROUP (A): -15.1111 -12.5344 -0.9688
REMARK 3 T TENSOR
REMARK 3 T11: 0.2403 T22: 0.2208
REMARK 3 T33: 0.3720 T12: -0.0889
REMARK 3 T13: 0.0160 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 5.6994 L22: 3.5299
REMARK 3 L33: 4.0670 L12: -1.9733
REMARK 3 L13: 0.0931 L23: -3.1197
REMARK 3 S TENSOR
REMARK 3 S11: -0.2558 S12: 0.1688 S13: -0.7702
REMARK 3 S21: -0.1794 S22: 0.1215 S23: 0.5092
REMARK 3 S31: 1.0758 S32: -0.6187 S33: -0.0302
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: chain 'A' and (resseq 503:511)
REMARK 3 ORIGIN FOR THE GROUP (A): -21.5076 -4.9933 -5.3373
REMARK 3 T TENSOR
REMARK 3 T11: 0.1761 T22: 0.4002
REMARK 3 T33: 0.5304 T12: -0.0583
REMARK 3 T13: -0.1034 T23: -0.0487
REMARK 3 L TENSOR
REMARK 3 L11: 6.9620 L22: 2.3773
REMARK 3 L33: 3.5695 L12: 0.1812
REMARK 3 L13: -2.3973 L23: -0.0018
REMARK 3 S TENSOR
REMARK 3 S11: -0.0842 S12: 0.4412 S13: 0.2016
REMARK 3 S21: -0.2800 S22: 0.1404 S23: 0.7413
REMARK 3 S31: 0.0828 S32: -1.1598 S33: -0.0467
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: chain 'A' and (resseq 512:538)
REMARK 3 ORIGIN FOR THE GROUP (A): -9.9076 -6.5022 1.8225
REMARK 3 T TENSOR
REMARK 3 T11: 0.0892 T22: 0.1976
REMARK 3 T33: 0.2512 T12: -0.0351
REMARK 3 T13: -0.0143 T23: -0.0144
REMARK 3 L TENSOR
REMARK 3 L11: 4.2510 L22: 1.7970
REMARK 3 L33: 5.0246 L12: -0.2758
REMARK 3 L13: -1.6877 L23: -0.7226
REMARK 3 S TENSOR
REMARK 3 S11: -0.0310 S12: -0.5146 S13: 0.0347
REMARK 3 S21: 0.1511 S22: -0.0566 S23: 0.5177
REMARK 3 S31: 0.3011 S32: -0.1094 S33: 0.0460
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: chain 'A' and (resseq 539:548)
REMARK 3 ORIGIN FOR THE GROUP (A): -16.1442 3.5235 -2.7152
REMARK 3 T TENSOR
REMARK 3 T11: 0.0796 T22: 0.3327
REMARK 3 T33: 0.4502 T12: 0.0433
REMARK 3 T13: -0.0768 T23: -0.0256
REMARK 3 L TENSOR
REMARK 3 L11: 7.2848 L22: 1.6035
REMARK 3 L33: 4.6494 L12: -0.9779
REMARK 3 L13: -5.5559 L23: 1.5250
REMARK 3 S TENSOR
REMARK 3 S11: 0.0790 S12: 0.0779 S13: 0.7674
REMARK 3 S21: -0.0916 S22: -0.0657 S23: 0.3459
REMARK 3 S31: -0.3944 S32: -0.7208 S33: -0.1870
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: chain 'A' and (resseq 549:561)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.7944 -1.3026 6.0211
REMARK 3 T TENSOR
REMARK 3 T11: 0.1247 T22: 0.2841
REMARK 3 T33: 0.2225 T12: 0.0084
REMARK 3 T13: -0.0201 T23: -0.0017
REMARK 3 L TENSOR
REMARK 3 L11: 7.3140 L22: 3.8059
REMARK 3 L33: 6.2932 L12: -0.6990
REMARK 3 L13: 0.2183 L23: -0.7245
REMARK 3 S TENSOR
REMARK 3 S11: 0.1423 S12: -0.6066 S13: -0.2723
REMARK 3 S21: 0.1363 S22: -0.0513 S23: 0.2197
REMARK 3 S31: 0.2216 S32: 0.2350 S33: -0.0067
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: chain 'A' and (resseq 562:580)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.1836 4.9752 -5.0547
REMARK 3 T TENSOR
REMARK 3 T11: 0.1141 T22: 0.1995
REMARK 3 T33: 0.2305 T12: -0.0150
REMARK 3 T13: -0.0228 T23: 0.0332
REMARK 3 L TENSOR
REMARK 3 L11: 6.7015 L22: 2.9891
REMARK 3 L33: 7.7225 L12: 0.5376
REMARK 3 L13: 0.1501 L23: 2.1165
REMARK 3 S TENSOR
REMARK 3 S11: -0.1707 S12: 0.2564 S13: 0.4361
REMARK 3 S21: -0.0323 S22: -0.0227 S23: 0.0158
REMARK 3 S31: -0.3227 S32: 0.1003 S33: 0.1171
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: chain 'A' and (resseq 581:594)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.8694 3.1643 4.9573
REMARK 3 T TENSOR
REMARK 3 T11: 0.0768 T22: 0.3122
REMARK 3 T33: 0.2339 T12: -0.0204
REMARK 3 T13: -0.0323 T23: -0.0512
REMARK 3 L TENSOR
REMARK 3 L11: 6.6060 L22: 3.0262
REMARK 3 L33: 2.1545 L12: -0.6943
REMARK 3 L13: 0.3725 L23: -0.1850
REMARK 3 S TENSOR
REMARK 3 S11: 0.0607 S12: -0.5276 S13: 0.5373
REMARK 3 S21: 0.1292 S22: -0.1348 S23: -0.0623
REMARK 3 S31: -0.1648 S32: 0.0782 S33: 0.0862
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: chain 'A' and (resseq 595:604)
REMARK 3 ORIGIN FOR THE GROUP (A): 7.8881 3.1543 -5.4358
REMARK 3 T TENSOR
REMARK 3 T11: 0.1431 T22: 0.4104
REMARK 3 T33: 0.2906 T12: -0.0193
REMARK 3 T13: -0.0509 T23: 0.0124
REMARK 3 L TENSOR
REMARK 3 L11: 7.1002 L22: 1.8746
REMARK 3 L33: 4.4776 L12: -0.5143
REMARK 3 L13: 1.8446 L23: 1.9494
REMARK 3 S TENSOR
REMARK 3 S11: -0.2970 S12: 0.6002 S13: -0.0459
REMARK 3 S21: -0.1174 S22: 0.2079 S23: 0.0674
REMARK 3 S31: 0.0355 S32: 0.2070 S33: -0.0583
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: chain 'A' and (resseq 605:614)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.9256 12.7992 -6.6914
REMARK 3 T TENSOR
REMARK 3 T11: 0.1948 T22: 0.3405
REMARK 3 T33: 0.6743 T12: -0.1433
REMARK 3 T13: -0.1700 T23: 0.2284
REMARK 3 L TENSOR
REMARK 3 L11: 3.0050 L22: 1.6773
REMARK 3 L33: 1.7826 L12: 1.4805
REMARK 3 L13: 1.2539 L23: 0.5013
REMARK 3 S TENSOR
REMARK 3 S11: -0.4280 S12: 0.5758 S13: 1.3796
REMARK 3 S21: -0.2860 S22: 0.0491 S23: 0.2433
REMARK 3 S31: -0.5146 S32: 0.1576 S33: 0.2353
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: chain 'A' and (resseq 615:627)
REMARK 3 ORIGIN FOR THE GROUP (A): 13.8870 5.6451 4.1276
REMARK 3 T TENSOR
REMARK 3 T11: 0.1712 T22: 0.4856
REMARK 3 T33: 0.4190 T12: -0.0371
REMARK 3 T13: -0.0927 T23: -0.0027
REMARK 3 L TENSOR
REMARK 3 L11: 7.4299 L22: 7.3778
REMARK 3 L33: 2.7867 L12: -5.3897
REMARK 3 L13: 1.1467 L23: -0.0628
REMARK 3 S TENSOR
REMARK 3 S11: -0.5236 S12: -0.9232 S13: 0.6405
REMARK 3 S21: 0.3950 S22: 0.1632 S23: 0.1728
REMARK 3 S31: -0.2295 S32: 0.2835 S33: 0.2185
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: chain 'A' and (resseq 628:644)
REMARK 3 ORIGIN FOR THE GROUP (A): 15.7264 8.0595 -9.0113
REMARK 3 T TENSOR
REMARK 3 T11: 0.1797 T22: 0.7540
REMARK 3 T33: 0.3238 T12: -0.1888
REMARK 3 T13: -0.0428 T23: 0.1455
REMARK 3 L TENSOR
REMARK 3 L11: 3.4147 L22: 1.9580
REMARK 3 L33: 2.4421 L12: 0.8567
REMARK 3 L13: 1.0502 L23: 0.0071
REMARK 3 S TENSOR
REMARK 3 S11: -0.3264 S12: 1.1278 S13: 0.5007
REMARK 3 S21: -0.4291 S22: 0.4107 S23: -0.0312
REMARK 3 S31: -0.2144 S32: 0.4524 S33: 0.0453
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: chain 'B' and (resseq 487:502)
REMARK 3 ORIGIN FOR THE GROUP (A): -25.3795 2.8835 -30.4976
REMARK 3 T TENSOR
REMARK 3 T11: 0.3585 T22: 0.5759
REMARK 3 T33: 0.4006 T12: 0.0243
REMARK 3 T13: -0.0498 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 7.0370 L22: 2.7221
REMARK 3 L33: 3.6666 L12: -2.3622
REMARK 3 L13: 4.9507 L23: -2.2535
REMARK 3 S TENSOR
REMARK 3 S11: -0.2851 S12: -0.2770 S13: 0.4137
REMARK 3 S21: -0.0157 S22: 0.0706 S23: 0.6306
REMARK 3 S31: -0.7509 S32: -1.7320 S33: 0.1519
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: chain 'B' and (resseq 503:538)
REMARK 3 ORIGIN FOR THE GROUP (A): -18.0137 1.5513 -29.8633
REMARK 3 T TENSOR
REMARK 3 T11: 0.2253 T22: 0.3121
REMARK 3 T33: 0.2059 T12: -0.0481
REMARK 3 T13: -0.0587 T23: -0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 4.7789 L22: 3.5765
REMARK 3 L33: 5.0884 L12: 0.9489
REMARK 3 L13: 2.3861 L23: 1.7150
REMARK 3 S TENSOR
REMARK 3 S11: -0.0473 S12: -0.1404 S13: 0.2525
REMARK 3 S21: 0.1104 S22: -0.2048 S23: 0.3036
REMARK 3 S31: -0.0112 S32: -0.8032 S33: 0.1192
REMARK 3 TLS GROUP : 14
REMARK 3 SELECTION: chain 'B' and (resseq 539:561)
REMARK 3 ORIGIN FOR THE GROUP (A): -10.3879 0.9458 -31.7026
REMARK 3 T TENSOR
REMARK 3 T11: 0.1852 T22: 0.1912
REMARK 3 T33: 0.1865 T12: -0.0164
REMARK 3 T13: -0.1038 T23: -0.0095
REMARK 3 L TENSOR
REMARK 3 L11: 3.7841 L22: 5.6943
REMARK 3 L33: 5.4067 L12: 2.5706
REMARK 3 L13: -1.2960 L23: -0.1896
REMARK 3 S TENSOR
REMARK 3 S11: -0.1711 S12: -0.0739 S13: -0.1320
REMARK 3 S21: -0.2086 S22: -0.0839 S23: -0.0665
REMARK 3 S31: 0.0054 S32: -0.0023 S33: 0.1934
REMARK 3 TLS GROUP : 15
REMARK 3 SELECTION: chain 'B' and (resseq 562:580)
REMARK 3 ORIGIN FOR THE GROUP (A): -3.8383 5.3474 -24.9248
REMARK 3 T TENSOR
REMARK 3 T11: 0.2754 T22: 0.1199
REMARK 3 T33: 0.2220 T12: -0.0465
REMARK 3 T13: -0.0805 T23: 0.0084
REMARK 3 L TENSOR
REMARK 3 L11: 2.1372 L22: 2.7668
REMARK 3 L33: 5.7829 L12: 2.2530
REMARK 3 L13: -0.6527 L23: 0.7728
REMARK 3 S TENSOR
REMARK 3 S11: -0.1913 S12: 0.0078 S13: 0.0735
REMARK 3 S21: 0.1628 S22: 0.0965 S23: -0.1869
REMARK 3 S31: -0.4227 S32: 0.1400 S33: 0.0630
REMARK 3 TLS GROUP : 16
REMARK 3 SELECTION: chain 'B' and (resseq 581:594)
REMARK 3 ORIGIN FOR THE GROUP (A): -2.2172 12.0663 -35.0343
REMARK 3 T TENSOR
REMARK 3 T11: 0.4397 T22: 0.3157
REMARK 3 T33: 0.2489 T12: -0.0971
REMARK 3 T13: -0.1064 T23: 0.0486
REMARK 3 L TENSOR
REMARK 3 L11: 2.6827 L22: 2.5882
REMARK 3 L33: 2.5903 L12: 0.8569
REMARK 3 L13: -0.6343 L23: 1.9769
REMARK 3 S TENSOR
REMARK 3 S11: 0.1068 S12: 0.1635 S13: 0.2191
REMARK 3 S21: -0.1245 S22: -0.1256 S23: -0.7659
REMARK 3 S31: -0.5971 S32: 0.3970 S33: -0.0164
REMARK 3 TLS GROUP : 17
REMARK 3 SELECTION: chain 'B' and (resseq 595:627)
REMARK 3 ORIGIN FOR THE GROUP (A): 3.4810 15.1546 -27.5045
REMARK 3 T TENSOR
REMARK 3 T11: 0.4467 T22: 0.3235
REMARK 3 T33: 0.4938 T12: -0.2085
REMARK 3 T13: -0.2270 T23: 0.1725
REMARK 3 L TENSOR
REMARK 3 L11: 2.4560 L22: 2.4919
REMARK 3 L33: 2.7837 L12: 0.4393
REMARK 3 L13: -0.1622 L23: -0.8912
REMARK 3 S TENSOR
REMARK 3 S11: 0.1965 S12: 0.0769 S13: -0.2729
REMARK 3 S21: 0.3811 S22: -0.1676 S23: -0.6228
REMARK 3 S31: -0.5480 S32: 0.4260 S33: 0.1748
REMARK 3 TLS GROUP : 18
REMARK 3 SELECTION: chain 'B' and (resseq 628:643)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2741 21.5025 -20.9089
REMARK 3 T TENSOR
REMARK 3 T11: 0.8058 T22: 0.3481
REMARK 3 T33: 0.5258 T12: -0.3814
REMARK 3 T13: -0.2941 T23: 0.2998
REMARK 3 L TENSOR
REMARK 3 L11: 0.8255 L22: 1.6395
REMARK 3 L33: 0.9732 L12: 0.5257
REMARK 3 L13: -0.2465 L23: -0.6358
REMARK 3 S TENSOR
REMARK 3 S11: 0.1210 S12: -0.1360 S13: -0.0380
REMARK 3 S21: 0.3508 S22: -0.1203 S23: -0.0999
REMARK 3 S31: -0.1427 S32: 0.0811 S33: -0.0331
REMARK 3 TLS GROUP : 19
REMARK 3 SELECTION: chain 'C'
REMARK 3 ORIGIN FOR THE GROUP (A): 1.0244 -6.5595 -7.5084
REMARK 3 T TENSOR
REMARK 3 T11: 0.2184 T22: 0.3160
REMARK 3 T33: 0.2626 T12: 0.0585
REMARK 3 T13: 0.0511 T23: 0.0077
REMARK 3 L TENSOR
REMARK 3 L11: 2.7869 L22: 0.8525
REMARK 3 L33: 1.7080 L12: 0.2112
REMARK 3 L13: 0.9998 L23: 0.6765
REMARK 3 S TENSOR
REMARK 3 S11: 0.0731 S12: -0.2406 S13: -0.2497
REMARK 3 S21: -0.1464 S22: 0.0802 S23: -0.1892
REMARK 3 S31: 0.2558 S32: 0.4307 S33: -0.0460
REMARK 3 TLS GROUP : 20
REMARK 3 SELECTION: chain 'D'
REMARK 3 ORIGIN FOR THE GROUP (A): -12.3661 13.2025 -21.7287
REMARK 3 T TENSOR
REMARK 3 T11: 0.3916 T22: 0.3100
REMARK 3 T33: 0.3243 T12: 0.0646
REMARK 3 T13: -0.1313 T23: -0.0419
REMARK 3 L TENSOR
REMARK 3 L11: 1.1957 L22: 0.8550
REMARK 3 L33: 0.8865 L12: 0.2392
REMARK 3 L13: -0.1684 L23: 0.0508
REMARK 3 S TENSOR
REMARK 3 S11: -0.0509 S12: -0.0715 S13: 0.2096
REMARK 3 S21: 0.0064 S22: 0.2561 S23: 0.0872
REMARK 3 S31: -0.2471 S32: -0.0945 S33: -0.1471
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 3TWW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-SEP-11.
REMARK 100 THE RCSB ID CODE IS RCSB068021.
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 : 5.5
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 : 23309
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.700
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6
REMARK 200 DATA REDUNDANCY : 5.800
REMARK 200 R MERGE (I) : 0.10700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 14.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.07
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.8
REMARK 200 DATA REDUNDANCY IN SHELL : 6.00
REMARK 200 R MERGE FOR SHELL (I) : 0.59900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.700
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 (%): 41.26
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.09
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAOAC PH 5.5, 2% (V/V) PEG 400,
REMARK 280 2.5 M (NH4)2SO4, VAPOR DIFFUSION, HANGING DROP, 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 22.18000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.74950
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.09550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.74950
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 22.18000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.09550
REMARK 290 SMTRY3 4 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: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14810 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, 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 GLY A 485
REMARK 465 ALA A 486
REMARK 465 MET A 487
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 GLY B 485
REMARK 465 ALA B 486
REMARK 465 ARG B 644
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 C 1
REMARK 465 PRO C 2
REMARK 465 HIS C 3
REMARK 465 LEU C 4
REMARK 465 LEU D 1
REMARK 465 PRO D 2
REMARK 465 HIS D 3
REMARK 465 LEU D 4
REMARK 465 GLN D 5
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 GLU B 523 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 NH2 ARG A 520 OE1 GLN A 526 1.93
REMARK 500 NH1 ARG A 494 OE2 GLU A 498 2.06
REMARK 500 OD2 ASP B 617 NZ LYS B 620 2.13
REMARK 500 OD2 ASP A 493 O HOH A 79 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 NH1 ARG A 520 O HOH B 39 2455 1.88
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 -168.88 -78.15
REMARK 500 GLN A 613 -19.84 -49.18
REMARK 500 ASP B 589 -161.49 -78.73
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 A 130 DISTANCE = 5.48 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 17
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3TWQ RELATED DB: PDB
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: 3TWX RELATED DB: PDB
DBREF 3TWW A 488 649 UNP Q9H2K2 TNKS2_HUMAN 488 649
DBREF 3TWW B 488 649 UNP Q9H2K2 TNKS2_HUMAN 488 649
DBREF 3TWW C 1 16 PDB 3TWW 3TWW 1 16
DBREF 3TWW D 1 16 PDB 3TWW 3TWW 1 16
SEQADV 3TWW GLY A 485 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWW ALA A 486 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWW MET A 487 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWW GLY B 485 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWW ALA B 486 UNP Q9H2K2 EXPRESSION TAG
SEQADV 3TWW MET B 487 UNP Q9H2K2 EXPRESSION TAG
SEQRES 1 A 165 GLY ALA MET GLY ASN SER GLU ALA ASP ARG GLN LEU LEU
SEQRES 2 A 165 GLU ALA ALA LYS ALA GLY ASP VAL GLU THR VAL LYS LYS
SEQRES 3 A 165 LEU CYS THR VAL GLN SER VAL ASN CYS ARG ASP ILE GLU
SEQRES 4 A 165 GLY ARG GLN SER THR PRO LEU HIS PHE ALA ALA GLY TYR
SEQRES 5 A 165 ASN ARG VAL SER VAL VAL GLU TYR LEU LEU GLN HIS GLY
SEQRES 6 A 165 ALA ASP VAL HIS ALA LYS ASP LYS GLY GLY LEU VAL PRO
SEQRES 7 A 165 LEU HIS ASN ALA CYS SER TYR GLY HIS TYR GLU VAL ALA
SEQRES 8 A 165 GLU LEU LEU VAL LYS HIS GLY ALA VAL VAL ASN VAL ALA
SEQRES 9 A 165 ASP LEU TRP LYS PHE THR PRO LEU HIS GLU ALA ALA ALA
SEQRES 10 A 165 LYS GLY LYS TYR GLU ILE CYS LYS LEU LEU LEU GLN HIS
SEQRES 11 A 165 GLY ALA ASP PRO THR LYS LYS ASN ARG ASP GLY ASN THR
SEQRES 12 A 165 PRO LEU ASP LEU VAL LYS ASP GLY ASP THR ASP ILE GLN
SEQRES 13 A 165 ASP LEU LEU ARG GLY ASP ALA ALA LEU
SEQRES 1 B 165 GLY ALA MET GLY ASN SER GLU ALA ASP ARG GLN LEU LEU
SEQRES 2 B 165 GLU ALA ALA LYS ALA GLY ASP VAL GLU THR VAL LYS LYS
SEQRES 3 B 165 LEU CYS THR VAL GLN SER VAL ASN CYS ARG ASP ILE GLU
SEQRES 4 B 165 GLY ARG GLN SER THR PRO LEU HIS PHE ALA ALA GLY TYR
SEQRES 5 B 165 ASN ARG VAL SER VAL VAL GLU TYR LEU LEU GLN HIS GLY
SEQRES 6 B 165 ALA ASP VAL HIS ALA LYS ASP LYS GLY GLY LEU VAL PRO
SEQRES 7 B 165 LEU HIS ASN ALA CYS SER TYR GLY HIS TYR GLU VAL ALA
SEQRES 8 B 165 GLU LEU LEU VAL LYS HIS GLY ALA VAL VAL ASN VAL ALA
SEQRES 9 B 165 ASP LEU TRP LYS PHE THR PRO LEU HIS GLU ALA ALA ALA
SEQRES 10 B 165 LYS GLY LYS TYR GLU ILE CYS LYS LEU LEU LEU GLN HIS
SEQRES 11 B 165 GLY ALA ASP PRO THR LYS LYS ASN ARG ASP GLY ASN THR
SEQRES 12 B 165 PRO LEU ASP LEU VAL LYS ASP GLY ASP THR ASP ILE GLN
SEQRES 13 B 165 ASP LEU LEU ARG GLY ASP ALA ALA LEU
SEQRES 1 C 16 LEU PRO HIS LEU GLN ARG GLN SER PRO ASP GLY GLN SER
SEQRES 2 C 16 PHE ARG SET
SEQRES 1 D 16 LEU PRO HIS LEU GLN ARG GLN SER PRO ASP GLY GLN SER
SEQRES 2 D 16 PHE ARG SET
MODRES 3TWW SET C 16 SER AMINOSERINE
MODRES 3TWW SET D 16 SER AMINOSERINE
HET SET C 16 7
HET SET D 16 7
HET SO4 B 1 5
HET SO4 D 17 5
HETNAM SET AMINOSERINE
HETNAM SO4 SULFATE ION
FORMUL 3 SET 2(C3 H8 N2 O2)
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *143(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 TYR A 569 1 9
HELIX 6 6 HIS A 571 HIS A 581 1 11
HELIX 7 7 THR A 594 LYS A 602 1 9
HELIX 8 8 LYS A 604 HIS A 614 1 11
HELIX 9 9 THR A 627 VAL A 632 1 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 LEU B 643 1 8
LINK C ARG C 15 N SET C 16 1555 1555 1.33
LINK C ARG D 15 N SET D 16 1555 1555 1.33
CISPEP 1 ASP A 634 GLY A 635 0 5.21
SITE 1 AC1 8 HOH A 35 HOH B 71 HOH B 78 HOH B 119
SITE 2 AC1 8 ARG B 538 VAL B 539 SER B 540 ARG C 15
SITE 1 AC2 2 TYR B 569 SER D 13
CRYST1 44.360 74.191 103.499 90.00 90.00 90.00 P 21 21 21 8
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 0.022543 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013479 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009662 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
