HEADER PROTEIN BINDING 01-DEC-11 3UW9
TITLE CRYSTAL STRUCTURE OF THE FIRST BROMODOMAIN OF HUMAN BRD4 IN COMPLEX
TITLE 2 WITH A DIACETYLATED HISTONE 4 PEPTIDE (H4K8ACK12AC)
CAVEAT 3UW9 ALY E 1 HAS WRONG CHIRALITY AT ATOM CA ALY E 11 HAS WRONG
CAVEAT 2 3UW9 CHIRALITY AT ATOM CA ALY F 1 HAS WRONG CHIRALITY AT ATOM CA
CAVEAT 3 3UW9 ALY F 5 HAS WRONG CHIRALITY AT ATOM CA THE CHIRALITY OF ALY
CAVEAT 4 3UW9 AND CHAINS E AND F IS NOT IN AGREEMENT WITH THE LIGAND
CAVEAT 5 3UW9 DEFINITION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BROMODOMAIN-CONTAINING PROTEIN 4;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: UNP RESIDEUS 44-168;
COMPND 5 SYNONYM: PROTEIN HUNK1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: HISTONE H4;
COMPND 9 CHAIN: E;
COMPND 10 FRAGMENT: UNP RESIDUES 8-18;
COMPND 11 SYNONYM: PEPTIDE (H4K8ACK12AC);
COMPND 12 ENGINEERED: YES;
COMPND 13 MOL_ID: 3;
COMPND 14 MOLECULE: HISTONE H4;
COMPND 15 CHAIN: F;
COMPND 16 FRAGMENT: UNP RESIDUES 8-18;
COMPND 17 SYNONYM: PEPTIDE (H4K8ACK12AC);
COMPND 18 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: BRD4, HUNK1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4;
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 MOL_ID: 3;
SOURCE 17 SYNTHETIC: YES;
SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 19 ORGANISM_COMMON: HUMAN;
SOURCE 20 ORGANISM_TAXID: 9606
KEYWDS BROMODOMAIN, BROMODOMAIN CONTAINING PROTEIN 4, CAP, HUNK1, MCAP,
KEYWDS 2 MITOTIC CHROMOSOME ASSOCIATED PROTEIN, PEPTIDE COMPLEX, STRUCTURAL
KEYWDS 3 GENOMICS CONSORTIUM, SGC, PROTEIN BINDING
EXPDTA X-RAY DIFFRACTION
AUTHOR P.FILIPPAKOPOULOS,I.FELLETAR,S.PICAUD,T.KEATES,J.MUNIZ,O.GILEADI,
AUTHOR 2 F.VON DELFT,C.H.ARROWSMITH,A.M.EDWARDS,J.WEIGELT,C.BOUNTRA,S.KNAPP,
AUTHOR 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)
REVDAT 4 06-DEC-23 3UW9 1 REMARK
REVDAT 3 13-SEP-23 3UW9 1 CAVEAT COMPND SOURCE REMARK
REVDAT 3 2 1 DBREF SEQADV SEQRES LINK
REVDAT 3 3 1 SITE ATOM
REVDAT 2 11-APR-12 3UW9 1 JRNL
REVDAT 1 14-MAR-12 3UW9 0
JRNL AUTH P.FILIPPAKOPOULOS,S.PICAUD,M.MANGOS,T.KEATES,J.P.LAMBERT,
JRNL AUTH 2 D.BARSYTE-LOVEJOY,I.FELLETAR,R.VOLKMER,S.MULLER,T.PAWSON,
JRNL AUTH 3 A.C.GINGRAS,C.H.ARROWSMITH,S.KNAPP
JRNL TITL HISTONE RECOGNITION AND LARGE-SCALE STRUCTURAL ANALYSIS OF
JRNL TITL 2 THE HUMAN BROMODOMAIN FAMILY.
JRNL REF CELL(CAMBRIDGE,MASS.) V. 149 214 2012
JRNL REFN ISSN 0092-8674
JRNL PMID 22464331
JRNL DOI 10.1016/J.CELL.2012.02.013
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 42.33
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 31231
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) : 0.203
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.257
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1575
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.30
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.36
REMARK 3 REFLECTION IN BIN (WORKING SET) : 1947
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.90
REMARK 3 BIN R VALUE (WORKING SET) : 0.2760
REMARK 3 BIN FREE R VALUE SET COUNT : 106
REMARK 3 BIN FREE R VALUE : 0.4010
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3804
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 124
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 48.40
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 53.13
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.16000
REMARK 3 B22 (A**2) : 0.16000
REMARK 3 B33 (A**2) : -0.32000
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 OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.249
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.219
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.170
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 13.840
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.954
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.918
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3918 ; 0.014 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 2614 ; 0.003 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5337 ; 1.682 ; 1.960
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6365 ; 1.688 ; 3.005
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 463 ; 5.605 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 188 ;38.372 ;25.851
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 647 ;16.701 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 7 ;13.154 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 581 ; 0.081 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4288 ; 0.008 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 755 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 4
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 43 A 166
REMARK 3 ORIGIN FOR THE GROUP (A): 34.4942 17.6497 52.9451
REMARK 3 T TENSOR
REMARK 3 T11: 0.0415 T22: 0.0505
REMARK 3 T33: 0.0715 T12: -0.0255
REMARK 3 T13: -0.0164 T23: 0.0473
REMARK 3 L TENSOR
REMARK 3 L11: 2.0901 L22: 5.3557
REMARK 3 L33: 5.3152 L12: -0.4561
REMARK 3 L13: -1.3199 L23: 2.9151
REMARK 3 S TENSOR
REMARK 3 S11: -0.0244 S12: 0.0351 S13: 0.1916
REMARK 3 S21: 0.1031 S22: -0.0795 S23: 0.1571
REMARK 3 S31: 0.1926 S32: 0.0018 S33: 0.1038
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 58 B 166
REMARK 3 ORIGIN FOR THE GROUP (A): 39.9963 26.8964 28.2650
REMARK 3 T TENSOR
REMARK 3 T11: 0.0639 T22: 0.1095
REMARK 3 T33: 0.0751 T12: 0.0621
REMARK 3 T13: 0.0537 T23: 0.0752
REMARK 3 L TENSOR
REMARK 3 L11: 5.8511 L22: 7.3505
REMARK 3 L33: 3.3557 L12: -2.1354
REMARK 3 L13: -0.7403 L23: -1.3931
REMARK 3 S TENSOR
REMARK 3 S11: 0.1272 S12: 0.2329 S13: 0.4449
REMARK 3 S21: 0.0406 S22: 0.0414 S23: -0.1450
REMARK 3 S31: -0.3246 S32: -0.2198 S33: -0.1686
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 56 C 167
REMARK 3 ORIGIN FOR THE GROUP (A): 22.3642 -1.1643 27.5994
REMARK 3 T TENSOR
REMARK 3 T11: 0.3268 T22: 0.1335
REMARK 3 T33: 0.1657 T12: 0.0352
REMARK 3 T13: 0.0072 T23: -0.1233
REMARK 3 L TENSOR
REMARK 3 L11: 4.0881 L22: 5.5164
REMARK 3 L33: 5.6920 L12: 1.0728
REMARK 3 L13: 1.5715 L23: 0.3021
REMARK 3 S TENSOR
REMARK 3 S11: 0.4523 S12: 0.0491 S13: -0.1826
REMARK 3 S21: -0.0359 S22: -0.3350 S23: 0.3807
REMARK 3 S31: 0.6826 S32: -0.1943 S33: -0.1173
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 59 D 167
REMARK 3 ORIGIN FOR THE GROUP (A): 8.5739 22.3437 29.7943
REMARK 3 T TENSOR
REMARK 3 T11: 0.0655 T22: 0.1148
REMARK 3 T33: 0.0998 T12: 0.0225
REMARK 3 T13: -0.0165 T23: -0.0589
REMARK 3 L TENSOR
REMARK 3 L11: 6.8787 L22: 3.3838
REMARK 3 L33: 2.0901 L12: -0.4320
REMARK 3 L13: -0.3811 L23: -0.0609
REMARK 3 S TENSOR
REMARK 3 S11: 0.1061 S12: -0.2104 S13: 0.1214
REMARK 3 S21: 0.0359 S22: -0.1233 S23: 0.0349
REMARK 3 S31: 0.0869 S32: -0.0862 S33: 0.0173
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS:
REMARK 3 HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
REMARK 3 U VALUES: WITH TLS ADDED
REMARK 4
REMARK 4 3UW9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-DEC-11.
REMARK 100 THE DEPOSITION ID IS D_1000069287.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 14-OCT-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 : DIAMOND
REMARK 200 BEAMLINE : I04
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9763
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315R
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA 3.3.16
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31295
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 42.330
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 9.000
REMARK 200 R MERGE (I) : 0.14600
REMARK 200 R SYM (I) : 0.14600
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 8.80
REMARK 200 R MERGE FOR SHELL (I) : 0.98000
REMARK 200 R SYM FOR SHELL (I) : 0.98000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.800
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.1.4
REMARK 200 STARTING MODEL: ENSEMBLE OF PDB ENTRIES 2OSS, 2OUO, 2GRC, 2OO1,
REMARK 200 3DAI, 3D7C
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 54.56
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 0.3M LICL 15% PEG6000, 10%
REMARK 280 ETGLY, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K, PH 8.0
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+1/2
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 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 68.35000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 49.80000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 49.80000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 34.17500
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 49.80000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 49.80000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 102.52500
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 49.80000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 49.80000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 34.17500
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 49.80000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 49.80000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 102.52500
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 68.35000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14350 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, E
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 1980 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 12340 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D, F
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 SER A 42
REMARK 465 GLU A 167
REMARK 465 GLU A 168
REMARK 465 SER B 42
REMARK 465 MET B 43
REMARK 465 ASN B 44
REMARK 465 PRO B 45
REMARK 465 PRO B 46
REMARK 465 PRO B 47
REMARK 465 PRO B 48
REMARK 465 GLU B 49
REMARK 465 THR B 50
REMARK 465 SER B 51
REMARK 465 ASN B 52
REMARK 465 PRO B 53
REMARK 465 ASN B 54
REMARK 465 LYS B 55
REMARK 465 PRO B 56
REMARK 465 LYS B 57
REMARK 465 GLU B 167
REMARK 465 GLU B 168
REMARK 465 SER C 42
REMARK 465 MET C 43
REMARK 465 ASN C 44
REMARK 465 PRO C 45
REMARK 465 PRO C 46
REMARK 465 PRO C 47
REMARK 465 PRO C 48
REMARK 465 GLU C 49
REMARK 465 THR C 50
REMARK 465 SER C 51
REMARK 465 ASN C 52
REMARK 465 PRO C 53
REMARK 465 ASN C 54
REMARK 465 LYS C 55
REMARK 465 GLU C 168
REMARK 465 SER D 42
REMARK 465 MET D 43
REMARK 465 ASN D 44
REMARK 465 PRO D 45
REMARK 465 PRO D 46
REMARK 465 PRO D 47
REMARK 465 PRO D 48
REMARK 465 GLU D 49
REMARK 465 THR D 50
REMARK 465 SER D 51
REMARK 465 ASN D 52
REMARK 465 PRO D 53
REMARK 465 ASN D 54
REMARK 465 LYS D 55
REMARK 465 PRO D 56
REMARK 465 LYS D 57
REMARK 465 ARG D 58
REMARK 465 GLU D 168
REMARK 465 GLY E 0
REMARK 465 ALY E 5
REMARK 465 GLY E 6
REMARK 465 GLY E 7
REMARK 465 ALA E 8
REMARK 465 LYS E 9
REMARK 465 ARG E 10
REMARK 465 GLY F 0
REMARK 465 GLY F 7
REMARK 465 ALA F 8
REMARK 465 LYS F 9
REMARK 465 ARG F 10
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 MET A 43 CG SD CE
REMARK 470 ARG A 58 CD NE CZ NH1 NH2
REMARK 470 ARG A 68 CZ NH1 NH2
REMARK 470 LYS A 99 CD CE NZ
REMARK 470 LYS A 112 CE NZ
REMARK 470 THR A 166 OG1 CG2
REMARK 470 ARG B 58 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 91 CD CE NZ
REMARK 470 LEU B 92 CG CD1 CD2
REMARK 470 LYS B 99 CG CD CE NZ
REMARK 470 LYS B 102 CG CD CE NZ
REMARK 470 LYS B 112 CE NZ
REMARK 470 LYS B 155 CD CE NZ
REMARK 470 GLN B 159 CG CD OE1 NE2
REMARK 470 GLU B 163 CG CD OE1 OE2
REMARK 470 THR B 166 OG1 CG2
REMARK 470 LYS C 57 CG CD CE NZ
REMARK 470 LYS C 91 CG CD CE NZ
REMARK 470 LEU C 94 CG CD1 CD2
REMARK 470 LYS C 102 CE NZ
REMARK 470 LYS C 112 CD CE NZ
REMARK 470 LYS C 141 CG CD CE NZ
REMARK 470 GLU C 167 CG CD OE1 OE2
REMARK 470 GLN D 59 CG CD OE1 NE2
REMARK 470 THR D 60 OG1 CG2
REMARK 470 ARG D 68 CG CD NE CZ NH1 NH2
REMARK 470 LYS D 72 CD CE NZ
REMARK 470 LYS D 76 CE NZ
REMARK 470 GLN D 78 CD OE1 NE2
REMARK 470 LYS D 91 CE NZ
REMARK 470 LYS D 102 CD CE NZ
REMARK 470 LYS D 112 CD CE NZ
REMARK 470 GLU D 167 CG CD OE1 OE2
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 MET A 43 N MET A 43 CA 0.125
REMARK 500 MET A 43 CA MET A 43 CB 0.154
REMARK 500 TRP A 75 CE2 TRP A 75 CD2 0.074
REMARK 500 TRP C 120 CE2 TRP C 120 CD2 0.074
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 ARG B 68 NE - CZ - NH2 ANGL. DEV. = -3.4 DEGREES
REMARK 500 ARG C 113 NE - CZ - NH1 ANGL. DEV. = 3.1 DEGREES
REMARK 500 ALY E 11 C - N - CA ANGL. DEV. = 17.9 DEGREES
REMARK 500 ALY F 5 C - N - CA ANGL. DEV. = 17.9 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 LYS C 57 121.71 -33.55
REMARK 500 VAL C 87 106.54 -56.23
REMARK 500 VAL C 90 -70.89 -62.66
REMARK 500 LEU C 94 75.20 -118.73
REMARK 500 ALY F 5 62.68 -108.84
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 PRO C 56 LYS C 57 -149.98
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 ALY E 11
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN E OF HISTONE H4
DBREF 3UW9 A 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 3UW9 B 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 3UW9 C 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 3UW9 D 44 168 UNP O60885 BRD4_HUMAN 44 168
DBREF 3UW9 E 0 10 UNP P62805 H4_HUMAN 8 18
DBREF 3UW9 F 0 10 UNP P62805 H4_HUMAN 8 18
SEQADV 3UW9 SER A 42 UNP O60885 EXPRESSION TAG
SEQADV 3UW9 MET A 43 UNP O60885 EXPRESSION TAG
SEQADV 3UW9 SER B 42 UNP O60885 EXPRESSION TAG
SEQADV 3UW9 MET B 43 UNP O60885 EXPRESSION TAG
SEQADV 3UW9 SER C 42 UNP O60885 EXPRESSION TAG
SEQADV 3UW9 MET C 43 UNP O60885 EXPRESSION TAG
SEQADV 3UW9 SER D 42 UNP O60885 EXPRESSION TAG
SEQADV 3UW9 MET D 43 UNP O60885 EXPRESSION TAG
SEQRES 1 A 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 A 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 A 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 A 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 A 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 A 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 A 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 A 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 A 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 A 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
SEQRES 1 B 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 B 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 B 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 B 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 B 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 B 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 B 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 B 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 B 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 B 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
SEQRES 1 C 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 C 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 C 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 C 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 C 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 C 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 C 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 C 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 C 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 C 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
SEQRES 1 D 127 SER MET ASN PRO PRO PRO PRO GLU THR SER ASN PRO ASN
SEQRES 2 D 127 LYS PRO LYS ARG GLN THR ASN GLN LEU GLN TYR LEU LEU
SEQRES 3 D 127 ARG VAL VAL LEU LYS THR LEU TRP LYS HIS GLN PHE ALA
SEQRES 4 D 127 TRP PRO PHE GLN GLN PRO VAL ASP ALA VAL LYS LEU ASN
SEQRES 5 D 127 LEU PRO ASP TYR TYR LYS ILE ILE LYS THR PRO MET ASP
SEQRES 6 D 127 MET GLY THR ILE LYS LYS ARG LEU GLU ASN ASN TYR TYR
SEQRES 7 D 127 TRP ASN ALA GLN GLU CYS ILE GLN ASP PHE ASN THR MET
SEQRES 8 D 127 PHE THR ASN CYS TYR ILE TYR ASN LYS PRO GLY ASP ASP
SEQRES 9 D 127 ILE VAL LEU MET ALA GLU ALA LEU GLU LYS LEU PHE LEU
SEQRES 10 D 127 GLN LYS ILE ASN GLU LEU PRO THR GLU GLU
SEQRES 1 E 12 GLY ALY GLY LEU GLY ALY GLY GLY ALA LYS ARG ALY
SEQRES 1 F 11 GLY ALY GLY LEU GLY ALY GLY GLY ALA LYS ARG
MODRES 3UW9 ALY E 1 LYS N(6)-ACETYLLYSINE
MODRES 3UW9 ALY F 1 LYS N(6)-ACETYLLYSINE
MODRES 3UW9 ALY F 5 LYS N(6)-ACETYLLYSINE
HET ALY E 1 12
HET ALY E 11 12
HET ALY F 1 12
HET ALY F 5 12
HETNAM ALY N(6)-ACETYLLYSINE
FORMUL 5 ALY 4(C8 H16 N2 O3)
FORMUL 7 HOH *124(H2 O)
HELIX 1 1 LYS A 55 VAL A 69 1 15
HELIX 2 2 VAL A 69 HIS A 77 1 9
HELIX 3 3 ALA A 80 GLN A 84 5 5
HELIX 4 4 ASP A 96 ILE A 101 1 6
HELIX 5 5 ASP A 106 ASN A 116 1 11
HELIX 6 6 ASN A 121 ASN A 140 1 20
HELIX 7 7 ASP A 144 ASN A 162 1 19
HELIX 8 8 GLN B 59 VAL B 69 1 11
HELIX 9 9 VAL B 69 LYS B 76 1 8
HELIX 10 10 ALA B 80 GLN B 84 5 5
HELIX 11 11 ASP B 88 ASN B 93 1 6
HELIX 12 12 ASP B 96 ILE B 101 1 6
HELIX 13 13 ASP B 106 ASN B 116 1 11
HELIX 14 14 ASN B 121 ASN B 140 1 20
HELIX 15 15 ASP B 144 ASN B 162 1 19
HELIX 16 16 GLN C 59 VAL C 69 1 11
HELIX 17 17 VAL C 69 LYS C 76 1 8
HELIX 18 18 ALA C 80 GLN C 84 5 5
HELIX 19 19 ASP C 88 ASN C 93 1 6
HELIX 20 20 ASP C 96 ILE C 101 1 6
HELIX 21 21 ASP C 106 ASN C 116 1 11
HELIX 22 22 ASN C 121 ASN C 140 1 20
HELIX 23 23 ASP C 144 ASN C 162 1 19
HELIX 24 24 THR D 60 VAL D 69 1 10
HELIX 25 25 VAL D 69 HIS D 77 1 9
HELIX 26 26 ALA D 80 GLN D 84 5 5
HELIX 27 27 ASP D 88 ASN D 93 1 6
HELIX 28 28 ASP D 96 ILE D 101 1 6
HELIX 29 29 ASP D 106 ASN D 116 1 11
HELIX 30 30 ASN D 121 ASN D 140 1 20
HELIX 31 31 ASP D 144 ASN D 162 1 19
LINK C ALY E 1 N GLY E 2 1555 1555 1.33
LINK C GLY E 4 N ALY E 11 1555 1555 1.34
LINK C ALY F 1 N GLY F 2 1555 1555 1.33
LINK C GLY F 4 N ALY F 5 1555 1555 1.35
LINK C ALY F 5 N GLY F 6 1555 1555 1.33
SITE 1 AC1 5 VAL C 87 LEU C 92 CYS C 136 ASN C 140
SITE 2 AC1 5 GLY E 4
SITE 1 AC2 9 TRP A 81 VAL A 87 LEU A 92 ASN A 140
SITE 2 AC2 9 ASP A 145 HOH A 170 ASP C 145 ALY E 11
SITE 3 AC2 9 HOH E 12
CRYST1 99.600 99.600 136.700 90.00 90.00 90.00 P 41 21 2 32
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 0.010040 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010040 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007315 0.00000
(ATOM LINES ARE NOT SHOWN.)
END