HEADER GENE REGULATION 23-JUN-14 4TU6
TITLE CRYSTAL STRUCTURE OF APO ATAD2A BROMODOMAIN WITH N1064 ALTERNATE
TITLE 2 CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ATPASE FAMILY AAA DOMAIN-CONTAINING PROTEIN 2;
COMPND 3 CHAIN: A, B, C, D;
COMPND 4 FRAGMENT: BROMODOMAIN (UNP RESIDUES 981-1108);
COMPND 5 SYNONYM: AAA NUCLEAR COREGULATOR CANCER-ASSOCIATED PROTEIN,ANCCA;
COMPND 6 EC: 3.6.1.3;
COMPND 7 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: ATAD2, L16, PRO2000;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4
KEYWDS BROMODOMAIN- CONSERVED ASPARAGINE CONFORMATIONS, GENE REGULATION
EXPDTA X-RAY DIFFRACTION
AUTHOR G.PONCET-MONTANGE,Y.ZHAN,J.BARDENHAGEN,A.PETROCCHI,E.LEO,X.SHI,G.LEE,
AUTHOR 2 P.LEONARD,M.GECK DO,M.CARDOZO,W.PALMER,J.ANDERSEN,P.JONES,J.LADBURY
REVDAT 4 27-SEP-23 4TU6 1 REMARK
REVDAT 3 22-NOV-17 4TU6 1 SOURCE JRNL REMARK
REVDAT 2 04-MAR-15 4TU6 1 JRNL
REVDAT 1 24-DEC-14 4TU6 0
JRNL AUTH G.PONCET-MONTANGE,Y.ZHAN,J.P.BARDENHAGEN,A.PETROCCHI,E.LEO,
JRNL AUTH 2 X.SHI,G.R.LEE,P.G.LEONARD,M.K.GECK DO,M.G.CARDOZO,
JRNL AUTH 3 J.N.ANDERSEN,W.S.PALMER,P.JONES,J.E.LADBURY
JRNL TITL OBSERVED BROMODOMAIN FLEXIBILITY REVEALS HISTONE PEPTIDE-
JRNL TITL 2 AND SMALL MOLECULE LIGAND-COMPATIBLE FORMS OF ATAD2.
JRNL REF BIOCHEM.J. V. 466 337 2015
JRNL REFN ESSN 1470-8728
JRNL PMID 25486442
JRNL DOI 10.1042/BJ20140933
REMARK 2
REMARK 2 RESOLUTION. 2.27 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.7.0029
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) : 2.27
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.06
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8
REMARK 3 NUMBER OF REFLECTIONS : 31181
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) : 0.192
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.248
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1571
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) : 2.27
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.33
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2134
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 97.58
REMARK 3 BIN R VALUE (WORKING SET) : 0.2770
REMARK 3 BIN FREE R VALUE SET COUNT : 121
REMARK 3 BIN FREE R VALUE : 0.3340
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 4179
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 226
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 17.86
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 0.00000
REMARK 3 B22 (A**2) : -0.01000
REMARK 3 B33 (A**2) : 0.00000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.01000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.268
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.222
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.160
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.917
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.948
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.917
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 4295 ; 0.016 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 4027 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5831 ; 1.769 ; 1.980
REMARK 3 BOND ANGLES OTHERS (DEGREES): 9253 ; 0.888 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 518 ; 5.498 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 222 ;34.966 ;23.829
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 757 ;15.200 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 42 ;17.389 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 672 ; 0.103 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4801 ; 0.009 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 947 ; 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 NCS TYPE: LOCAL
REMARK 3 NUMBER OF DIFFERENT NCS PAIRS : 6
REMARK 3 GROUP CHAIN1 RANGE CHAIN2 RANGE COUNT RMS WEIGHT
REMARK 3 1 A 979 1108 B 979 1108 7716 0.140 0.050
REMARK 3 2 A 982 1107 C 982 1107 7496 0.140 0.050
REMARK 3 3 A 979 1108 D 979 1108 7796 0.130 0.050
REMARK 3 4 B 982 1107 C 982 1107 7509 0.120 0.050
REMARK 3 5 B 979 1108 D 979 1108 7677 0.130 0.050
REMARK 3 6 C 982 1107 D 982 1107 7665 0.110 0.050
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 979 A 1108
REMARK 3 ORIGIN FOR THE GROUP (A): -1.568 -0.217 5.696
REMARK 3 T TENSOR
REMARK 3 T11: 0.0403 T22: 0.0437
REMARK 3 T33: 0.1044 T12: -0.0249
REMARK 3 T13: -0.0085 T23: 0.0158
REMARK 3 L TENSOR
REMARK 3 L11: 2.2008 L22: 2.4706
REMARK 3 L33: 6.9334 L12: -0.4228
REMARK 3 L13: -0.3351 L23: 0.7995
REMARK 3 S TENSOR
REMARK 3 S11: -0.0820 S12: 0.2599 S13: 0.0272
REMARK 3 S21: 0.0022 S22: 0.0059 S23: 0.0890
REMARK 3 S31: 0.4614 S32: -0.2216 S33: 0.0760
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 979 B 1108
REMARK 3 ORIGIN FOR THE GROUP (A): 17.534 -25.671 9.880
REMARK 3 T TENSOR
REMARK 3 T11: 0.1840 T22: 0.0268
REMARK 3 T33: 0.0993 T12: 0.0407
REMARK 3 T13: 0.0348 T23: 0.0417
REMARK 3 L TENSOR
REMARK 3 L11: 3.6802 L22: 2.5155
REMARK 3 L33: 3.8151 L12: -1.5735
REMARK 3 L13: -1.6083 L23: 1.7234
REMARK 3 S TENSOR
REMARK 3 S11: -0.0669 S12: 0.0107 S13: -0.0800
REMARK 3 S21: 0.2091 S22: 0.0867 S23: 0.0659
REMARK 3 S31: 0.0034 S32: 0.0883 S33: -0.0197
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 980 C 1107
REMARK 3 RESIDUE RANGE : C 1201 C 1201
REMARK 3 ORIGIN FOR THE GROUP (A): 0.933 -45.291 35.471
REMARK 3 T TENSOR
REMARK 3 T11: 0.0325 T22: 0.0987
REMARK 3 T33: 0.1121 T12: -0.0010
REMARK 3 T13: 0.0431 T23: -0.0116
REMARK 3 L TENSOR
REMARK 3 L11: 5.0368 L22: 1.9123
REMARK 3 L33: 3.1809 L12: 0.3523
REMARK 3 L13: 2.2722 L23: -0.0211
REMARK 3 S TENSOR
REMARK 3 S11: -0.1615 S12: -0.0238 S13: 0.1383
REMARK 3 S21: 0.0955 S22: 0.0415 S23: 0.0026
REMARK 3 S31: -0.0610 S32: -0.1804 S33: 0.1199
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 979 D 1108
REMARK 3 ORIGIN FOR THE GROUP (A): -18.493 -25.730 51.032
REMARK 3 T TENSOR
REMARK 3 T11: 0.1303 T22: 0.0906
REMARK 3 T33: 0.1199 T12: -0.0142
REMARK 3 T13: 0.0569 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 1.4246 L22: 3.2546
REMARK 3 L33: 5.6314 L12: -0.1741
REMARK 3 L13: 0.4848 L23: -1.5037
REMARK 3 S TENSOR
REMARK 3 S11: 0.0114 S12: 0.2571 S13: 0.1091
REMARK 3 S21: -0.0733 S22: -0.2054 S23: -0.1438
REMARK 3 S31: -0.5710 S32: 0.0116 S33: 0.1941
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: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 4
REMARK 4 4TU6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-JUN-14.
REMARK 100 THE DEPOSITION ID IS D_1000202288.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 26-NOV-13
REMARK 200 TEMPERATURE (KELVIN) : 193
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 8.3.1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.11587
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 : NULL
REMARK 200 DATA SCALING SOFTWARE : SCALA 0.1.27
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 32012
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.270
REMARK 200 RESOLUTION RANGE LOW (A) : 61.923
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : 6.000
REMARK 200 R MERGE (I) : 0.14400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.27
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.34
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.97500
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: NULL
REMARK 200 STARTING MODEL: 3DAI
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 55.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM SULFATE, 0.1M BIS-TRIS
REMARK 280 PH 5.5, 25% W/V PEG3350, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 273K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,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 0.00000
REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 54.30000
REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 3
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 4
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 SER C 979
REMARK 465 ARG C 1108
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 980 CG SD CE
REMARK 470 LYS A1004 CG CD CE NZ
REMARK 470 ASP A1016 CG OD1 OD2
REMARK 470 GLU A1017 CG CD OE1 OE2
REMARK 470 ARG A1051 CG CD NE CZ NH1 NH2
REMARK 470 ARG A1067 CG CD NE CZ NH1 NH2
REMARK 470 MET B 980 CG SD CE
REMARK 470 LYS B1004 CG CD CE NZ
REMARK 470 LYS B1011 CG CD CE NZ
REMARK 470 ASP B1016 CG OD1 OD2
REMARK 470 GLU B1017 CG CD OE1 OE2
REMARK 470 ARG B1067 CG CD NE CZ NH1 NH2
REMARK 470 ARG B1072 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1090 CG CD CE NZ
REMARK 470 GLU B1091 CG CD OE1 OE2
REMARK 470 LYS C1004 CG CD CE NZ
REMARK 470 ARG C1007 CG CD NE CZ NH1 NH2
REMARK 470 LYS C1011 CG CD CE NZ
REMARK 470 ASP C1016 CG OD1 OD2
REMARK 470 GLU C1017 CG CD OE1 OE2
REMARK 470 LYS C1026 CG CD CE NZ
REMARK 470 ARG C1067 CG CD NE CZ NH1 NH2
REMARK 470 GLU C1106 CG CD OE1 OE2
REMARK 470 MET D 980 CG SD CE
REMARK 470 GLN D 981 CG CD OE1 NE2
REMARK 470 GLU D 983 CG CD OE1 OE2
REMARK 470 LYS D1004 CG CD CE NZ
REMARK 470 ARG D1007 CG CD NE CZ NH1 NH2
REMARK 470 GLU D1091 CG CD OE1 OE2
REMARK 470 GLU D1095 CG CD OE1 OE2
REMARK 470 GLU D1106 CG CD OE1 OE2
REMARK 470 ARG D1108 CG CD NE CZ NH1 NH2
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 OD2 ASP B 1071 O HOH B 1353 2.15
REMARK 500 OD2 ASP D 1068 CG ASP D 1071 2.18
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 ARG B1067 -94.11 168.44
REMARK 500 HIS C1041 32.20 71.90
REMARK 500 ARG C1067 -92.30 -118.28
REMARK 500 ASP D1066 76.33 -69.20
REMARK 500 ARG D1067 -113.97 -130.53
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 C1342 DISTANCE = 5.82 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 A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4TT2 RELATED DB: PDB
REMARK 900 RELATED ID: 4TT4 RELATED DB: PDB
REMARK 900 RELATED ID: 4TT6 RELATED DB: PDB
REMARK 900 RELATED ID: 4TTE RELATED DB: PDB
REMARK 900 RELATED ID: 4TU4 RELATED DB: PDB
DBREF 4TU6 A 981 1108 UNP Q6PL18 ATAD2_HUMAN 981 1108
DBREF 4TU6 B 981 1108 UNP Q6PL18 ATAD2_HUMAN 981 1108
DBREF 4TU6 C 981 1108 UNP Q6PL18 ATAD2_HUMAN 981 1108
DBREF 4TU6 D 981 1108 UNP Q6PL18 ATAD2_HUMAN 981 1108
SEQADV 4TU6 SER A 979 UNP Q6PL18 EXPRESSION TAG
SEQADV 4TU6 MET A 980 UNP Q6PL18 EXPRESSION TAG
SEQADV 4TU6 SER B 979 UNP Q6PL18 EXPRESSION TAG
SEQADV 4TU6 MET B 980 UNP Q6PL18 EXPRESSION TAG
SEQADV 4TU6 SER C 979 UNP Q6PL18 EXPRESSION TAG
SEQADV 4TU6 MET C 980 UNP Q6PL18 EXPRESSION TAG
SEQADV 4TU6 SER D 979 UNP Q6PL18 EXPRESSION TAG
SEQADV 4TU6 MET D 980 UNP Q6PL18 EXPRESSION TAG
SEQRES 1 A 130 SER MET GLN GLU GLU ASP THR PHE ARG GLU LEU ARG ILE
SEQRES 2 A 130 PHE LEU ARG ASN VAL THR HIS ARG LEU ALA ILE ASP LYS
SEQRES 3 A 130 ARG PHE ARG VAL PHE THR LYS PRO VAL ASP PRO ASP GLU
SEQRES 4 A 130 VAL PRO ASP TYR VAL THR VAL ILE LYS GLN PRO MET ASP
SEQRES 5 A 130 LEU SER SER VAL ILE SER LYS ILE ASP LEU HIS LYS TYR
SEQRES 6 A 130 LEU THR VAL LYS ASP TYR LEU ARG ASP ILE ASP LEU ILE
SEQRES 7 A 130 CYS SER ASN ALA LEU GLU TYR ASN PRO ASP ARG ASP PRO
SEQRES 8 A 130 GLY ASP ARG LEU ILE ARG HIS ARG ALA CYS ALA LEU ARG
SEQRES 9 A 130 ASP THR ALA TYR ALA ILE ILE LYS GLU GLU LEU ASP GLU
SEQRES 10 A 130 ASP PHE GLU GLN LEU CYS GLU GLU ILE GLN GLU SER ARG
SEQRES 1 B 130 SER MET GLN GLU GLU ASP THR PHE ARG GLU LEU ARG ILE
SEQRES 2 B 130 PHE LEU ARG ASN VAL THR HIS ARG LEU ALA ILE ASP LYS
SEQRES 3 B 130 ARG PHE ARG VAL PHE THR LYS PRO VAL ASP PRO ASP GLU
SEQRES 4 B 130 VAL PRO ASP TYR VAL THR VAL ILE LYS GLN PRO MET ASP
SEQRES 5 B 130 LEU SER SER VAL ILE SER LYS ILE ASP LEU HIS LYS TYR
SEQRES 6 B 130 LEU THR VAL LYS ASP TYR LEU ARG ASP ILE ASP LEU ILE
SEQRES 7 B 130 CYS SER ASN ALA LEU GLU TYR ASN PRO ASP ARG ASP PRO
SEQRES 8 B 130 GLY ASP ARG LEU ILE ARG HIS ARG ALA CYS ALA LEU ARG
SEQRES 9 B 130 ASP THR ALA TYR ALA ILE ILE LYS GLU GLU LEU ASP GLU
SEQRES 10 B 130 ASP PHE GLU GLN LEU CYS GLU GLU ILE GLN GLU SER ARG
SEQRES 1 C 130 SER MET GLN GLU GLU ASP THR PHE ARG GLU LEU ARG ILE
SEQRES 2 C 130 PHE LEU ARG ASN VAL THR HIS ARG LEU ALA ILE ASP LYS
SEQRES 3 C 130 ARG PHE ARG VAL PHE THR LYS PRO VAL ASP PRO ASP GLU
SEQRES 4 C 130 VAL PRO ASP TYR VAL THR VAL ILE LYS GLN PRO MET ASP
SEQRES 5 C 130 LEU SER SER VAL ILE SER LYS ILE ASP LEU HIS LYS TYR
SEQRES 6 C 130 LEU THR VAL LYS ASP TYR LEU ARG ASP ILE ASP LEU ILE
SEQRES 7 C 130 CYS SER ASN ALA LEU GLU TYR ASN PRO ASP ARG ASP PRO
SEQRES 8 C 130 GLY ASP ARG LEU ILE ARG HIS ARG ALA CYS ALA LEU ARG
SEQRES 9 C 130 ASP THR ALA TYR ALA ILE ILE LYS GLU GLU LEU ASP GLU
SEQRES 10 C 130 ASP PHE GLU GLN LEU CYS GLU GLU ILE GLN GLU SER ARG
SEQRES 1 D 130 SER MET GLN GLU GLU ASP THR PHE ARG GLU LEU ARG ILE
SEQRES 2 D 130 PHE LEU ARG ASN VAL THR HIS ARG LEU ALA ILE ASP LYS
SEQRES 3 D 130 ARG PHE ARG VAL PHE THR LYS PRO VAL ASP PRO ASP GLU
SEQRES 4 D 130 VAL PRO ASP TYR VAL THR VAL ILE LYS GLN PRO MET ASP
SEQRES 5 D 130 LEU SER SER VAL ILE SER LYS ILE ASP LEU HIS LYS TYR
SEQRES 6 D 130 LEU THR VAL LYS ASP TYR LEU ARG ASP ILE ASP LEU ILE
SEQRES 7 D 130 CYS SER ASN ALA LEU GLU TYR ASN PRO ASP ARG ASP PRO
SEQRES 8 D 130 GLY ASP ARG LEU ILE ARG HIS ARG ALA CYS ALA LEU ARG
SEQRES 9 D 130 ASP THR ALA TYR ALA ILE ILE LYS GLU GLU LEU ASP GLU
SEQRES 10 D 130 ASP PHE GLU GLN LEU CYS GLU GLU ILE GLN GLU SER ARG
HET SO4 A1201 5
HET SO4 B1201 5
HET SO4 C1201 5
HET SO4 D1201 5
HETNAM SO4 SULFATE ION
FORMUL 5 SO4 4(O4 S 2-)
FORMUL 9 HOH *226(H2 O)
HELIX 1 AA1 SER A 979 ILE A 1002 1 24
HELIX 2 AA2 ASP A 1003 THR A 1010 5 8
HELIX 3 AA3 ASP A 1020 ILE A 1025 1 6
HELIX 4 AA4 ASP A 1030 LEU A 1040 1 11
HELIX 5 AA5 THR A 1045 ASN A 1064 1 20
HELIX 6 AA6 ASP A 1068 LEU A 1093 1 26
HELIX 7 AA7 ASP A 1094 SER A 1107 1 14
HELIX 8 AA8 MET B 980 ASP B 1003 1 24
HELIX 9 AA9 LYS B 1004 THR B 1010 5 7
HELIX 10 AB1 ASP B 1020 ILE B 1025 1 6
HELIX 11 AB2 ASP B 1030 LEU B 1040 1 11
HELIX 12 AB3 THR B 1045 ASN B 1064 1 20
HELIX 13 AB4 ASP B 1068 LEU B 1093 1 26
HELIX 14 AB5 ASP B 1094 ARG B 1108 1 15
HELIX 15 AB6 GLU C 982 ILE C 1002 1 21
HELIX 16 AB7 ASP C 1003 THR C 1010 5 8
HELIX 17 AB8 ASP C 1020 ILE C 1025 1 6
HELIX 18 AB9 ASP C 1030 LEU C 1040 1 11
HELIX 19 AC1 THR C 1045 ASN C 1064 1 20
HELIX 20 AC2 ASP C 1068 LEU C 1093 1 26
HELIX 21 AC3 ASP C 1094 SER C 1107 1 14
HELIX 22 AC4 MET D 980 ASP D 1003 1 24
HELIX 23 AC5 LYS D 1004 THR D 1010 5 7
HELIX 24 AC6 ASP D 1020 ILE D 1025 1 6
HELIX 25 AC7 ASP D 1030 LEU D 1040 1 11
HELIX 26 AC8 THR D 1045 ASN D 1064 1 20
HELIX 27 AC9 ASP D 1068 LEU D 1093 1 26
HELIX 28 AD1 ASP D 1094 SER D 1107 1 14
SITE 1 AC1 4 ARG A 987 ARG A 990 ARG A 994 HOH A1355
SITE 1 AC2 4 ARG B 987 ARG B 990 ARG B 994 HOH B1358
SITE 1 AC3 3 ARG C 987 ARG C 990 ARG C 994
SITE 1 AC4 4 ARG D 987 ARG D 990 ARG D 994 HIS D1041
CRYST1 41.980 108.600 77.650 90.00 103.90 90.00 P 1 21 1 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 0.023821 0.000000 0.005895 0.00000
SCALE2 0.000000 0.009208 0.000000 0.00000
SCALE3 0.000000 0.000000 0.013267 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
