HEADER TRANSCRIPTION 28-OCT-14 4ROC
TITLE HUMAN TFIIB-RELATED FACTOR 2 (BRF2) AND TBP BOUND TO U6#2 PROMOTER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR IIIB 50 KDA SUBUNIT;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: TFIIIB50, HTFIIIB50, B-RELATED FACTOR 2, BRF-2, HBRFU;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: TATA-BOX-BINDING PROTEIN;
COMPND 8 CHAIN: B;
COMPND 9 SYNONYM: TATA SEQUENCE-BINDING PROTEIN, TATA-BINDING FACTOR, TATA-BOX
COMPND 10 FACTOR, TRANSCRIPTION INITIATION FACTOR TFIID TBP SUBUNIT;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: TEMPLATE STRAND;
COMPND 14 CHAIN: N;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 4;
COMPND 17 MOLECULE: NON-TEMPLATE STRAND;
COMPND 18 CHAIN: T;
COMPND 19 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: BRF2, BRFU, PRO1470;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 GENE: TBP, GTF2D1, TF2D, TFIID;
SOURCE 13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 14 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 15 MOL_ID: 3;
SOURCE 16 SYNTHETIC: YES;
SOURCE 17 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 18 ORGANISM_TAXID: 32630;
SOURCE 19 OTHER_DETAILS: OLIGONUCLEOTIDE;
SOURCE 20 MOL_ID: 4;
SOURCE 21 SYNTHETIC: YES;
SOURCE 22 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 23 ORGANISM_TAXID: 32630;
SOURCE 24 OTHER_DETAILS: OLIGONUCLEOTIDE
KEYWDS TRANSCRIPTION FACTOR, TRANSCRIPTION
EXPDTA X-RAY DIFFRACTION
AUTHOR A.VANNINI,J.GOUGE,K.SATIA,N.GUTHERTZ
REVDAT 2 20-SEP-23 4ROC 1 REMARK SEQADV
REVDAT 1 30-DEC-15 4ROC 0
JRNL AUTH J.GOUGE,K.SATIA,N.GUTHERTZ,M.WIDYA,A.J.THOMPSON,P.COUSIN,
JRNL AUTH 2 O.DERGAI,N.HERNANDEZ,A.VANNINI
JRNL TITL REDOX SIGNALING BY THE RNA POLYMERASE III TFIIB-RELATED
JRNL TITL 2 FACTOR BRF2.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 163 1375 2015
JRNL REFN ISSN 0092-8674
JRNL PMID 26638071
JRNL DOI 10.1016/J.CELL.2015.11.005
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.1
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.51
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.1
REMARK 3 NUMBER OF REFLECTIONS : 56427
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) : 0.187
REMARK 3 R VALUE (WORKING SET) : 0.186
REMARK 3 FREE R VALUE : 0.215
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.960
REMARK 3 FREE R VALUE TEST SET COUNT : 2797
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 1.95
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.14
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 4072
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2746
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 3869
REMARK 3 BIN R VALUE (WORKING SET) : 0.2741
REMARK 3 BIN FREE R VALUE : 0.2837
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.99
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 203
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 : 3805
REMARK 3 NUCLEIC ACID ATOMS : 1101
REMARK 3 HETEROGEN ATOMS : 1
REMARK 3 SOLVENT ATOMS : 379
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 45.20
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 62.19
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.16570
REMARK 3 B22 (A**2) : 0.19630
REMARK 3 B33 (A**2) : -0.03060
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) : 0.312
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.137
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
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 : 0.964
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.952
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 5133 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 7184 ; 2.000 ; HARMONIC
REMARK 3 TORSION ANGLES : 2128 ; 2.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 77 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 619 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 5133 ; 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 : 673 ; 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 : 5738 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.95
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.13
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 3.20
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 12
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|65 - A|167 }
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5867 0.5927 4.4123
REMARK 3 T TENSOR
REMARK 3 T11: -0.0884 T22: -0.1001
REMARK 3 T33: -0.0494 T12: -0.0126
REMARK 3 T13: -0.0814 T23: -0.0316
REMARK 3 L TENSOR
REMARK 3 L11: 6.1834 L22: 3.5112
REMARK 3 L33: 2.0151 L12: -1.7641
REMARK 3 L13: -0.9448 L23: 0.2059
REMARK 3 S TENSOR
REMARK 3 S11: 0.1637 S12: 0.4633 S13: -0.5442
REMARK 3 S21: -0.5442 S22: -0.1859 S23: 0.5305
REMARK 3 S31: 0.0720 S32: -0.3542 S33: 0.0222
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { A|168 - A|364 }
REMARK 3 ORIGIN FOR THE GROUP (A): 29.0607 16.8436 6.3204
REMARK 3 T TENSOR
REMARK 3 T11: -0.1370 T22: -0.0467
REMARK 3 T33: -0.0034 T12: 0.0063
REMARK 3 T13: 0.0586 T23: 0.0293
REMARK 3 L TENSOR
REMARK 3 L11: 1.8455 L22: 1.0887
REMARK 3 L33: 2.5255 L12: 0.3594
REMARK 3 L13: -1.1726 L23: -0.2500
REMARK 3 S TENSOR
REMARK 3 S11: 0.0367 S12: -0.1436 S13: -0.0508
REMARK 3 S21: -0.0470 S22: 0.0365 S23: -0.1690
REMARK 3 S31: -0.0242 S32: 0.3168 S33: -0.0731
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: { A|375 - A|378 }
REMARK 3 ORIGIN FOR THE GROUP (A): 9.6110 24.7124 42.5352
REMARK 3 T TENSOR
REMARK 3 T11: 0.0709 T22: 0.1275
REMARK 3 T33: 0.0726 T12: -0.0005
REMARK 3 T13: -0.0076 T23: 0.0062
REMARK 3 L TENSOR
REMARK 3 L11: 1.7810 L22: 1.0190
REMARK 3 L33: 0.1603 L12: 0.3477
REMARK 3 L13: 1.4401 L23: 0.6641
REMARK 3 S TENSOR
REMARK 3 S11: -0.0004 S12: -0.0745 S13: -0.0040
REMARK 3 S21: 0.0505 S22: -0.0027 S23: 0.0026
REMARK 3 S31: 0.0036 S32: -0.0289 S33: 0.0032
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: { A|379 - A|395 }
REMARK 3 ORIGIN FOR THE GROUP (A): -13.7580 29.2005 49.0093
REMARK 3 T TENSOR
REMARK 3 T11: 0.1715 T22: -0.1366
REMARK 3 T33: -0.2231 T12: 0.0639
REMARK 3 T13: 0.1520 T23: -0.0047
REMARK 3 L TENSOR
REMARK 3 L11: 0.0000 L22: 0.0000
REMARK 3 L33: 2.8543 L12: 2.9104
REMARK 3 L13: -0.8449 L23: -2.5852
REMARK 3 S TENSOR
REMARK 3 S11: -0.0882 S12: -0.3144 S13: 0.1296
REMARK 3 S21: 0.4594 S22: -0.0825 S23: 0.1928
REMARK 3 S31: 0.3221 S32: -0.0138 S33: 0.1708
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: { A|396 - A|407 }
REMARK 3 ORIGIN FOR THE GROUP (A): -24.6716 41.7757 33.7390
REMARK 3 T TENSOR
REMARK 3 T11: -0.0528 T22: -0.0317
REMARK 3 T33: 0.1215 T12: -0.0373
REMARK 3 T13: 0.0738 T23: -0.1101
REMARK 3 L TENSOR
REMARK 3 L11: 1.9661 L22: 1.3592
REMARK 3 L33: 0.8209 L12: -2.9104
REMARK 3 L13: -0.4667 L23: -2.9104
REMARK 3 S TENSOR
REMARK 3 S11: -0.0847 S12: 0.0141 S13: -0.1479
REMARK 3 S21: -0.1855 S22: 0.1302 S23: 0.1802
REMARK 3 S31: -0.0053 S32: -0.0852 S33: -0.0455
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: { B|158 - B|334 }
REMARK 3 ORIGIN FOR THE GROUP (A): -1.9123 13.3114 35.0497
REMARK 3 T TENSOR
REMARK 3 T11: -0.0175 T22: -0.1061
REMARK 3 T33: -0.1162 T12: -0.0398
REMARK 3 T13: 0.0651 T23: 0.0715
REMARK 3 L TENSOR
REMARK 3 L11: 1.8306 L22: 1.8746
REMARK 3 L33: 1.2866 L12: -1.0453
REMARK 3 L13: -0.8493 L23: 0.7886
REMARK 3 S TENSOR
REMARK 3 S11: -0.1783 S12: -0.2466 S13: -0.2084
REMARK 3 S21: 0.4246 S22: 0.0483 S23: 0.1982
REMARK 3 S31: 0.1373 S32: 0.1443 S33: 0.1299
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: { N|2 - N|5 }
REMARK 3 ORIGIN FOR THE GROUP (A): 19.2885 34.0544 10.1485
REMARK 3 T TENSOR
REMARK 3 T11: 0.0955 T22: 0.0825
REMARK 3 T33: 0.0084 T12: -0.1005
REMARK 3 T13: 0.1520 T23: 0.1510
REMARK 3 L TENSOR
REMARK 3 L11: 1.2289 L22: 1.3320
REMARK 3 L33: 0.2657 L12: -0.0772
REMARK 3 L13: -0.8760 L23: 0.3433
REMARK 3 S TENSOR
REMARK 3 S11: 0.0029 S12: -0.0195 S13: -0.0353
REMARK 3 S21: 0.0311 S22: 0.0348 S23: -0.0225
REMARK 3 S31: 0.0663 S32: 0.0605 S33: -0.0377
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: { N|6 - N|14 }
REMARK 3 ORIGIN FOR THE GROUP (A): 4.2160 21.3064 21.3501
REMARK 3 T TENSOR
REMARK 3 T11: -0.2507 T22: -0.2351
REMARK 3 T33: -0.0694 T12: -0.0193
REMARK 3 T13: 0.0112 T23: 0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 0.6854 L22: 3.8940
REMARK 3 L33: 8.2829 L12: -2.1593
REMARK 3 L13: -2.8118 L23: -2.9104
REMARK 3 S TENSOR
REMARK 3 S11: 0.1251 S12: 0.1917 S13: 0.5442
REMARK 3 S21: -0.1377 S22: 0.0841 S23: 0.0537
REMARK 3 S31: -0.5442 S32: -0.2856 S33: -0.2092
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: { N|15 - N|28 }
REMARK 3 ORIGIN FOR THE GROUP (A): -20.7570 5.0878 17.9394
REMARK 3 T TENSOR
REMARK 3 T11: -0.0844 T22: -0.0132
REMARK 3 T33: 0.2785 T12: -0.0831
REMARK 3 T13: -0.0492 T23: -0.1520
REMARK 3 L TENSOR
REMARK 3 L11: 1.2208 L22: 0.0000
REMARK 3 L33: 2.6934 L12: -0.1291
REMARK 3 L13: 0.0765 L23: -0.7894
REMARK 3 S TENSOR
REMARK 3 S11: 0.0483 S12: 0.4150 S13: -0.5442
REMARK 3 S21: -0.1009 S22: -0.0308 S23: 0.5442
REMARK 3 S31: 0.5394 S32: -0.5442 S33: -0.0176
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: { T|1 - T|4 }
REMARK 3 ORIGIN FOR THE GROUP (A): -33.0799 0.5824 10.3785
REMARK 3 T TENSOR
REMARK 3 T11: 0.0880 T22: 0.0715
REMARK 3 T33: 0.0294 T12: -0.0151
REMARK 3 T13: -0.1520 T23: -0.0551
REMARK 3 L TENSOR
REMARK 3 L11: 0.9197 L22: 1.8957
REMARK 3 L33: 0.2306 L12: -0.2366
REMARK 3 L13: 0.2345 L23: 0.3803
REMARK 3 S TENSOR
REMARK 3 S11: 0.0046 S12: -0.0481 S13: -0.0153
REMARK 3 S21: -0.0061 S22: 0.0069 S23: 0.0043
REMARK 3 S31: -0.0132 S32: -0.0013 S33: -0.0115
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: { T|5 - T|14 }
REMARK 3 ORIGIN FOR THE GROUP (A): -14.0183 10.4240 21.4358
REMARK 3 T TENSOR
REMARK 3 T11: -0.2062 T22: -0.1243
REMARK 3 T33: 0.0140 T12: -0.0265
REMARK 3 T13: -0.0297 T23: 0.0052
REMARK 3 L TENSOR
REMARK 3 L11: 0.2880 L22: 0.0000
REMARK 3 L33: 4.1600 L12: -1.8803
REMARK 3 L13: 0.5318 L23: -0.1872
REMARK 3 S TENSOR
REMARK 3 S11: 0.1123 S12: 0.0455 S13: -0.5442
REMARK 3 S21: 0.1693 S22: 0.1052 S23: 0.3724
REMARK 3 S31: 0.1307 S32: -0.1561 S33: -0.2175
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: { T|15 - T|27 }
REMARK 3 ORIGIN FOR THE GROUP (A): 9.9769 27.3888 18.1238
REMARK 3 T TENSOR
REMARK 3 T11: 0.0599 T22: -0.1273
REMARK 3 T33: 0.0572 T12: -0.0394
REMARK 3 T13: 0.1327 T23: 0.1055
REMARK 3 L TENSOR
REMARK 3 L11: 2.0452 L22: 0.6287
REMARK 3 L33: 1.4830 L12: -0.1470
REMARK 3 L13: 0.3450 L23: 2.4727
REMARK 3 S TENSOR
REMARK 3 S11: 0.0494 S12: 0.0595 S13: 0.5442
REMARK 3 S21: -0.4438 S22: 0.0694 S23: -0.2445
REMARK 3 S31: -0.5442 S32: 0.3769 S33: -0.1188
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE DENSITY BETWEEN THE RESIDUES 365
REMARK 3 AND 374 IS VERY POOR, THE LINKER HAS BEEN BUILT WITH 0 OCCUPANCY
REMARK 4
REMARK 4 4ROC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-OCT-14.
REMARK 100 THE DEPOSITION ID IS D_1000087593.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 04-DEC-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.968620
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 56530
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 29.510
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.500
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 4.200
REMARK 200 R MERGE (I) : 0.05800
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 11.2000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.00
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 4.20
REMARK 200 R MERGE FOR SHELL (I) : 3.19300
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.500
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: 1C9B
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.09
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20% PEG 3350, 50-100 MM MGCL2, 2 MM
REMARK 280 DTT, PH 7.9, 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 38.63800
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 51.23100
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.95550
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 51.23100
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.63800
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 44.95550
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 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 11830 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 30290 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -55.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, N, T
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 60
REMARK 465 PRO A 61
REMARK 465 ASN A 62
REMARK 465 GLU A 63
REMARK 465 GLN A 64
REMARK 465 GLY A 315
REMARK 465 THR A 316
REMARK 465 ALA A 317
REMARK 465 GLU A 318
REMARK 465 VAL A 319
REMARK 465 GLU A 320
REMARK 465 THR A 321
REMARK 465 ARG A 322
REMARK 465 GLU A 323
REMARK 465 LYS A 324
REMARK 465 GLU A 325
REMARK 465 PRO A 326
REMARK 465 PRO A 327
REMARK 465 GLY A 328
REMARK 465 TRP A 329
REMARK 465 GLY A 330
REMARK 465 GLN A 331
REMARK 465 GLY A 332
REMARK 465 GLN A 333
REMARK 465 GLY A 334
REMARK 465 GLU A 335
REMARK 465 GLY A 336
REMARK 465 GLU A 337
REMARK 465 VAL A 338
REMARK 465 GLY A 339
REMARK 465 ASN A 340
REMARK 465 ASN A 341
REMARK 465 SER A 342
REMARK 465 LEU A 343
REMARK 465 GLY A 344
REMARK 465 LEU A 345
REMARK 465 PRO A 346
REMARK 465 GLN A 347
REMARK 465 GLY A 348
REMARK 465 LYS A 349
REMARK 465 ARG A 350
REMARK 465 PRO A 351
REMARK 465 ALA A 352
REMARK 465 SER A 353
REMARK 465 PRO A 354
REMARK 465 ALA A 355
REMARK 465 ALA A 408
REMARK 465 ARG A 409
REMARK 465 GLN A 410
REMARK 465 ALA A 411
REMARK 465 ALA A 412
REMARK 465 THR A 413
REMARK 465 SER A 414
REMARK 465 VAL A 415
REMARK 465 PRO A 416
REMARK 465 ASN A 417
REMARK 465 PRO A 418
REMARK 465 PRO A 419
REMARK 465 PHE B 335
REMARK 465 ARG B 336
REMARK 465 LYS B 337
REMARK 465 THR B 338
REMARK 465 THR B 339
REMARK 465 DA N 1
REMARK 465 DT T 28
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 DT N 2 P OP1 OP2
REMARK 475
REMARK 475 ZERO OCCUPANCY RESIDUES
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)
REMARK 475 M RES C SSEQI
REMARK 475 SER A 365
REMARK 475 PRO A 366
REMARK 475 LYS A 367
REMARK 475 ARG A 368
REMARK 475 ILE A 369
REMARK 475 CYS A 370
REMARK 475 PRO A 371
REMARK 475 VAL A 372
REMARK 475 PRO A 373
REMARK 475 PRO A 374
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 DT N 12 O3' DT N 12 C3' -0.048
REMARK 500 DT T 2 O3' DT T 2 C3' -0.045
REMARK 500 DT T 14 O3' DT T 14 C3' -0.040
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 DC N 10 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
REMARK 500 DT N 12 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DT N 21 O4' - C1' - N1 ANGL. DEV. = 2.8 DEGREES
REMARK 500 DG N 24 O4' - C1' - N9 ANGL. DEV. = 1.8 DEGREES
REMARK 500 DC T 7 O4' - C1' - N1 ANGL. DEV. = 2.4 DEGREES
REMARK 500 DC T 9 O4' - C1' - N1 ANGL. DEV. = 4.0 DEGREES
REMARK 500 DC T 21 O4' - C1' - N1 ANGL. DEV. = 1.9 DEGREES
REMARK 500 DC T 22 O4' - C1' - N1 ANGL. DEV. = 2.0 DEGREES
REMARK 500 DC T 25 O4' - C1' - N1 ANGL. DEV. = 2.3 DEGREES
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 GLN A 238 69.83 -150.09
REMARK 500 PHE B 250 77.54 -119.08
REMARK 500
REMARK 500 REMARK: NULL
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG N 101 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH N 207 O
REMARK 620 2 HOH N 210 O 77.8
REMARK 620 3 HOH N 229 O 62.8 66.9
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG N 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4ROC RELATED DB: PDB
REMARK 900 RELATED ID: 4ROD RELATED DB: PDB
REMARK 900 RELATED ID: 4ROE RELATED DB: PDB
DBREF 4ROC A 62 419 UNP Q9HAW0 BRF2_HUMAN 62 419
DBREF 4ROC B 159 339 UNP P20226 TBP_HUMAN 159 339
DBREF 4ROC N 1 28 PDB 4ROC 4ROC 1 28
DBREF 4ROC T 1 28 PDB 4ROC 4ROC 1 28
SEQADV 4ROC GLY A 60 UNP Q9HAW0 EXPRESSION TAG
SEQADV 4ROC PRO A 61 UNP Q9HAW0 EXPRESSION TAG
SEQADV 4ROC GLY B 157 UNP P20226 EXPRESSION TAG
SEQADV 4ROC PRO B 158 UNP P20226 EXPRESSION TAG
SEQRES 1 A 360 GLY PRO ASN GLU GLN VAL SER ARG SER GLN GLN ARG GLY
SEQRES 2 A 360 LEU ARG ARG VAL ARG ASP LEU CYS ARG VAL LEU GLN LEU
SEQRES 3 A 360 PRO PRO THR PHE GLU ASP THR ALA VAL ALA TYR TYR GLN
SEQRES 4 A 360 GLN ALA TYR ARG HIS SER GLY ILE ARG ALA ALA ARG LEU
SEQRES 5 A 360 GLN LYS LYS GLU VAL LEU VAL GLY CYS CYS VAL LEU ILE
SEQRES 6 A 360 THR CYS ARG GLN HIS ASN TRP PRO LEU THR MET GLY ALA
SEQRES 7 A 360 ILE CYS THR LEU LEU TYR ALA ASP LEU ASP VAL PHE SER
SEQRES 8 A 360 SER THR TYR MET GLN ILE VAL LYS LEU LEU GLY LEU ASP
SEQRES 9 A 360 VAL PRO SER LEU CYS LEU ALA GLU LEU VAL LYS THR TYR
SEQRES 10 A 360 CYS SER SER PHE LYS LEU PHE GLN ALA SER PRO SER VAL
SEQRES 11 A 360 PRO ALA LYS TYR VAL GLU ASP LYS GLU LYS MET LEU SER
SEQRES 12 A 360 ARG THR MET GLN LEU VAL GLU LEU ALA ASN GLU THR TRP
SEQRES 13 A 360 LEU VAL THR GLY ARG HIS PRO LEU PRO VAL ILE THR ALA
SEQRES 14 A 360 ALA THR PHE LEU ALA TRP GLN SER LEU GLN PRO ALA ASP
SEQRES 15 A 360 ARG LEU SER CYS SER LEU ALA ARG PHE CYS LYS LEU ALA
SEQRES 16 A 360 ASN VAL ASP LEU PRO TYR PRO ALA SER SER ARG LEU GLN
SEQRES 17 A 360 GLU LEU LEU ALA VAL LEU LEU ARG MET ALA GLU GLN LEU
SEQRES 18 A 360 ALA TRP LEU ARG VAL LEU ARG LEU ASP LYS ARG SER VAL
SEQRES 19 A 360 VAL LYS HIS ILE GLY ASP LEU LEU GLN HIS ARG GLN SER
SEQRES 20 A 360 LEU VAL ARG SER ALA PHE ARG ASP GLY THR ALA GLU VAL
SEQRES 21 A 360 GLU THR ARG GLU LYS GLU PRO PRO GLY TRP GLY GLN GLY
SEQRES 22 A 360 GLN GLY GLU GLY GLU VAL GLY ASN ASN SER LEU GLY LEU
SEQRES 23 A 360 PRO GLN GLY LYS ARG PRO ALA SER PRO ALA LEU LEU LEU
SEQRES 24 A 360 PRO PRO CYS MET LEU LYS SER PRO LYS ARG ILE CYS PRO
SEQRES 25 A 360 VAL PRO PRO VAL SER THR VAL THR GLY ASP GLU ASN ILE
SEQRES 26 A 360 SER ASP SER GLU ILE GLU GLN TYR LEU ARG THR PRO GLN
SEQRES 27 A 360 GLU VAL ARG ASP PHE GLN ARG ALA GLN ALA ALA ARG GLN
SEQRES 28 A 360 ALA ALA THR SER VAL PRO ASN PRO PRO
SEQRES 1 B 183 GLY PRO SER GLY ILE VAL PRO GLN LEU GLN ASN ILE VAL
SEQRES 2 B 183 SER THR VAL ASN LEU GLY CYS LYS LEU ASP LEU LYS THR
SEQRES 3 B 183 ILE ALA LEU ARG ALA ARG ASN ALA GLU TYR ASN PRO LYS
SEQRES 4 B 183 ARG PHE ALA ALA VAL ILE MET ARG ILE ARG GLU PRO ARG
SEQRES 5 B 183 THR THR ALA LEU ILE PHE SER SER GLY LYS MET VAL CYS
SEQRES 6 B 183 THR GLY ALA LYS SER GLU GLU GLN SER ARG LEU ALA ALA
SEQRES 7 B 183 ARG LYS TYR ALA ARG VAL VAL GLN LYS LEU GLY PHE PRO
SEQRES 8 B 183 ALA LYS PHE LEU ASP PHE LYS ILE GLN ASN MET VAL GLY
SEQRES 9 B 183 SER CYS ASP VAL LYS PHE PRO ILE ARG LEU GLU GLY LEU
SEQRES 10 B 183 VAL LEU THR HIS GLN GLN PHE SER SER TYR GLU PRO GLU
SEQRES 11 B 183 LEU PHE PRO GLY LEU ILE TYR ARG MET ILE LYS PRO ARG
SEQRES 12 B 183 ILE VAL LEU LEU ILE PHE VAL SER GLY LYS VAL VAL LEU
SEQRES 13 B 183 THR GLY ALA LYS VAL ARG ALA GLU ILE TYR GLU ALA PHE
SEQRES 14 B 183 GLU ASN ILE TYR PRO ILE LEU LYS GLY PHE ARG LYS THR
SEQRES 15 B 183 THR
SEQRES 1 N 28 DA DT DT DG DA DA DG DG DG DC DT DT DA
SEQRES 2 N 28 DA DA DA DT DA DG DG DT DG DT DG DA DC
SEQRES 3 N 28 DA DG
SEQRES 1 T 28 DC DT DG DT DC DA DC DA DC DC DT DA DT
SEQRES 2 T 28 DT DT DT DA DA DG DC DC DC DT DT DC DA
SEQRES 3 T 28 DA DT
HET MG N 101 1
HETNAM MG MAGNESIUM ION
FORMUL 5 MG MG 2+
FORMUL 6 HOH *379(H2 O)
HELIX 1 1 SER A 66 LEU A 83 1 18
HELIX 2 2 PRO A 86 ARG A 102 1 17
HELIX 3 3 HIS A 103 ALA A 108 1 6
HELIX 4 4 ARG A 110 HIS A 129 1 20
HELIX 5 5 THR A 134 TYR A 143 1 10
HELIX 6 6 ASP A 145 LEU A 160 1 16
HELIX 7 7 CYS A 168 SER A 179 1 12
HELIX 8 8 PRO A 190 VAL A 194 5 5
HELIX 9 9 ASP A 196 THR A 214 1 19
HELIX 10 10 PRO A 222 GLN A 238 1 17
HELIX 11 11 GLN A 238 LEU A 243 1 6
HELIX 12 12 SER A 246 ALA A 254 1 9
HELIX 13 13 PRO A 261 GLU A 278 1 18
HELIX 14 14 LEU A 280 VAL A 285 1 6
HELIX 15 15 VAL A 293 LYS A 295 5 3
HELIX 16 16 HIS A 296 HIS A 303 1 8
HELIX 17 17 HIS A 303 ASP A 314 1 12
HELIX 18 18 SER A 385 GLN A 391 1 7
HELIX 19 19 THR A 395 ALA A 407 1 13
HELIX 20 20 ASP B 179 ALA B 187 1 9
HELIX 21 21 SER B 226 LEU B 244 1 19
HELIX 22 22 ARG B 269 HIS B 277 1 9
HELIX 23 23 VAL B 317 GLY B 334 1 18
SHEET 1 A10 ALA B 190 ASN B 193 0
SHEET 2 A10 PHE B 197 ILE B 204 -1 O ILE B 201 N GLU B 191
SHEET 3 A10 THR B 209 ILE B 213 -1 O ALA B 211 N MET B 202
SHEET 4 A10 LYS B 218 ALA B 224 -1 O THR B 222 N THR B 210
SHEET 5 A10 GLN B 164 ASN B 173 -1 N SER B 170 O CYS B 221
SHEET 6 A10 LEU B 251 ASP B 263 -1 O GLN B 256 N VAL B 169
SHEET 7 A10 LYS B 309 ALA B 315 -1 O LEU B 312 N GLY B 260
SHEET 8 A10 ILE B 300 ILE B 304 -1 N LEU B 303 O VAL B 311
SHEET 9 A10 LEU B 291 MET B 295 -1 N TYR B 293 O LEU B 302
SHEET 10 A10 SER B 281 SER B 282 -1 N SER B 282 O ILE B 292
LINK MG MG N 101 O HOH N 207 1555 1555 2.49
LINK MG MG N 101 O HOH N 210 1555 1555 2.53
LINK MG MG N 101 O HOH N 229 1555 1555 2.61
CISPEP 1 LEU A 363 LYS A 364 0 1.63
CISPEP 2 GLU B 206 PRO B 207 0 -9.17
CISPEP 3 LYS B 297 PRO B 298 0 -7.85
SITE 1 AC1 3 HOH N 207 HOH N 210 HOH N 229
CRYST1 77.276 89.911 102.462 90.00 90.00 90.00 P 21 21 21 4
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 0.012941 0.000000 0.000000 0.00000
SCALE2 0.000000 0.011122 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009760 0.00000
(ATOM LINES ARE NOT SHOWN.)
END