HEADER ANTITUMOR PROTEIN 07-NOV-06 2NTE
TITLE CRYSTAL STRUCTURE OF THE BARD1 BRCT DOMAINS
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BRCA1-ASSOCIATED RING DOMAIN PROTEIN 1;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: BRCT DOMAIN;
COMPND 5 SYNONYM: BARD-1;
COMPND 6 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: BARD1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 511693;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET-6H
KEYWDS BRCT, RING FINGER, BRCA1, ZINC-BINDING PROTEIN, UBIQUITIN LIGASE,
KEYWDS 2 ANTITUMOR PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.BIRRANE,A.K.VARMA,A.SONI,J.A.A.LADIAS
REVDAT 5 27-DEC-23 2NTE 1 REMARK LINK
REVDAT 4 13-JUL-11 2NTE 1 VERSN
REVDAT 3 24-FEB-09 2NTE 1 VERSN
REVDAT 2 18-SEP-07 2NTE 1 JRNL
REVDAT 1 12-JUN-07 2NTE 0
JRNL AUTH G.BIRRANE,A.K.VARMA,A.SONI,J.A.LADIAS
JRNL TITL CRYSTAL STRUCTURE OF THE BARD1 BRCT DOMAINS.
JRNL REF BIOCHEMISTRY V. 46 7706 2007
JRNL REFN ISSN 0006-2960
JRNL PMID 17550235
JRNL DOI 10.1021/BI700323T
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0019
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.87
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.8
REMARK 3 NUMBER OF REFLECTIONS : 36401
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) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.247
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1910
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) : 1.90
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 1.97
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2018
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 72.02
REMARK 3 BIN R VALUE (WORKING SET) : 0.2500
REMARK 3 BIN FREE R VALUE SET COUNT : 108
REMARK 3 BIN FREE R VALUE : 0.3760
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3382
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 33
REMARK 3 SOLVENT ATOMS : 238
REMARK 3
REMARK 3 B VALUES.
REMARK 3 B VALUE TYPE : LIKELY RESIDUAL
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 40.93
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.19000
REMARK 3 B22 (A**2) : 0.50000
REMARK 3 B33 (A**2) : -0.31000
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): 0.159
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.155
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.111
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.346
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.952
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.922
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3489 ; 0.022 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 2465 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4714 ; 1.865 ; 1.972
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6001 ; 0.987 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 417 ; 6.984 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 152 ;36.720 ;23.684
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 626 ;15.017 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 22 ;19.555 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 512 ; 0.114 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3772 ; 0.009 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 696 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 734 ; 0.224 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2488 ; 0.205 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1684 ; 0.191 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 1847 ; 0.090 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 197 ; 0.198 ; 0.200
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): 8 ; 0.553 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 55 ; 0.254 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 15 ; 0.130 ; 0.200
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): 2644 ; 1.527 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 840 ; 0.363 ; 1.500
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 3402 ; 1.860 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1637 ; 2.808 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1312 ; 3.910 ; 4.500
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 : 8
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 568 A 658
REMARK 3 ORIGIN FOR THE GROUP (A): 18.0600 11.8770 38.0030
REMARK 3 T TENSOR
REMARK 3 T11: -0.2062 T22: -0.2139
REMARK 3 T33: -0.1741 T12: -0.0570
REMARK 3 T13: 0.0168 T23: -0.0729
REMARK 3 L TENSOR
REMARK 3 L11: 3.9002 L22: 2.9312
REMARK 3 L33: 4.9465 L12: 1.0462
REMARK 3 L13: -2.1764 L23: 0.4489
REMARK 3 S TENSOR
REMARK 3 S11: 0.0879 S12: -0.2475 S13: 0.1542
REMARK 3 S21: -0.0361 S22: -0.1242 S23: 0.0949
REMARK 3 S31: -0.4903 S32: 0.2049 S33: 0.0363
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 : A 659 A 709
REMARK 3 ORIGIN FOR THE GROUP (A): 22.2420 -2.4210 19.0840
REMARK 3 T TENSOR
REMARK 3 T11: -0.2087 T22: -0.1812
REMARK 3 T33: -0.1351 T12: -0.0334
REMARK 3 T13: 0.0134 T23: -0.0275
REMARK 3 L TENSOR
REMARK 3 L11: 2.0368 L22: 2.3500
REMARK 3 L33: 5.4657 L12: 0.5311
REMARK 3 L13: -1.8189 L23: 0.6890
REMARK 3 S TENSOR
REMARK 3 S11: 0.2583 S12: -0.1828 S13: 0.2677
REMARK 3 S21: 0.0755 S22: -0.1609 S23: -0.0351
REMARK 3 S31: -0.3078 S32: 0.1957 S33: -0.0974
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 : A 710 A 739
REMARK 3 ORIGIN FOR THE GROUP (A): 17.0170 -13.0940 15.6230
REMARK 3 T TENSOR
REMARK 3 T11: -0.2142 T22: -0.1926
REMARK 3 T33: -0.1834 T12: -0.0108
REMARK 3 T13: -0.0118 T23: -0.0403
REMARK 3 L TENSOR
REMARK 3 L11: 2.5671 L22: 5.5102
REMARK 3 L33: 3.5146 L12: -0.4387
REMARK 3 L13: 0.2191 L23: -0.8391
REMARK 3 S TENSOR
REMARK 3 S11: 0.1082 S12: -0.1207 S13: -0.0665
REMARK 3 S21: -0.1494 S22: -0.2132 S23: 0.1743
REMARK 3 S31: 0.0695 S32: -0.0921 S33: 0.1051
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 : A 740 A 777
REMARK 3 ORIGIN FOR THE GROUP (A): 13.5280 -1.9730 12.0820
REMARK 3 T TENSOR
REMARK 3 T11: -0.1214 T22: -0.2165
REMARK 3 T33: -0.1072 T12: 0.0480
REMARK 3 T13: -0.0540 T23: -0.0333
REMARK 3 L TENSOR
REMARK 3 L11: 2.9379 L22: 7.0654
REMARK 3 L33: 5.6577 L12: -0.0020
REMARK 3 L13: -0.8101 L23: 3.3439
REMARK 3 S TENSOR
REMARK 3 S11: 0.1782 S12: 0.0869 S13: 0.3322
REMARK 3 S21: -0.7416 S22: -0.3252 S23: 0.4495
REMARK 3 S31: -0.6332 S32: -0.3948 S33: 0.1469
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 569 B 641
REMARK 3 ORIGIN FOR THE GROUP (A): 41.0900 15.9440 10.6140
REMARK 3 T TENSOR
REMARK 3 T11: -0.0317 T22: -0.2493
REMARK 3 T33: -0.1768 T12: -0.0635
REMARK 3 T13: 0.0360 T23: -0.0427
REMARK 3 L TENSOR
REMARK 3 L11: 1.6981 L22: 5.6688
REMARK 3 L33: 7.7337 L12: 0.7209
REMARK 3 L13: 2.2826 L23: 4.4468
REMARK 3 S TENSOR
REMARK 3 S11: -0.1332 S12: 0.0731 S13: 0.1006
REMARK 3 S21: -0.4507 S22: 0.0026 S23: 0.0378
REMARK 3 S31: -1.0507 S32: 0.0868 S33: 0.1305
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 642 B 668
REMARK 3 ORIGIN FOR THE GROUP (A): 48.4720 5.9940 13.6170
REMARK 3 T TENSOR
REMARK 3 T11: -0.1145 T22: -0.0436
REMARK 3 T33: 0.0286 T12: -0.0191
REMARK 3 T13: -0.0974 T23: -0.1401
REMARK 3 L TENSOR
REMARK 3 L11: 1.5419 L22: 8.6236
REMARK 3 L33: 10.1379 L12: -2.1093
REMARK 3 L13: -1.2177 L23: 7.5566
REMARK 3 S TENSOR
REMARK 3 S11: 0.0109 S12: -0.0572 S13: -0.0268
REMARK 3 S21: 0.6605 S22: 0.7147 S23: -0.8285
REMARK 3 S31: 0.2233 S32: 0.7315 S33: -0.7256
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 669 B 715
REMARK 3 ORIGIN FOR THE GROUP (A): 35.3510 -0.7120 -10.4740
REMARK 3 T TENSOR
REMARK 3 T11: -0.0766 T22: -0.1963
REMARK 3 T33: -0.0685 T12: -0.0181
REMARK 3 T13: 0.0027 T23: 0.0790
REMARK 3 L TENSOR
REMARK 3 L11: 9.3922 L22: 4.0780
REMARK 3 L33: 4.0986 L12: -0.1160
REMARK 3 L13: 2.0054 L23: -0.1527
REMARK 3 S TENSOR
REMARK 3 S11: -0.0482 S12: 0.3113 S13: 0.3659
REMARK 3 S21: -0.3456 S22: 0.0645 S23: -0.0581
REMARK 3 S31: -0.2627 S32: 0.0107 S33: -0.0163
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 716 B 777
REMARK 3 ORIGIN FOR THE GROUP (A): 35.6190 -10.3220 -5.0520
REMARK 3 T TENSOR
REMARK 3 T11: -0.1209 T22: -0.1891
REMARK 3 T33: -0.1223 T12: 0.0055
REMARK 3 T13: -0.0006 T23: 0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 5.0852 L22: 1.8926
REMARK 3 L33: 2.1506 L12: -0.0847
REMARK 3 L13: 0.1348 L23: 0.1942
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: -0.1525 S13: -0.1007
REMARK 3 S21: 0.1037 S22: 0.0786 S23: -0.1259
REMARK 3 S31: 0.0726 S32: -0.0599 S33: -0.0693
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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 3 POSITIONS
REMARK 4
REMARK 4 2NTE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-NOV-06.
REMARK 100 THE DEPOSITION ID IS D_1000040278.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 10-SEP-05
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : NSLS
REMARK 200 BEAMLINE : X12B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9784
REMARK 200 MONOCHROMATOR : SI 111 CHANNEL
REMARK 200 OPTICS : DUAL SLITS
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40185
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.900
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.3
REMARK 200 DATA REDUNDANCY : 7.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.06400
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.7000
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) : 1.97
REMARK 200 COMPLETENESS FOR SHELL (%) : 91.7
REMARK 200 DATA REDUNDANCY IN SHELL : 6.10
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.40200
REMARK 200 <I/SIGMA(I)> FOR SHELL : 4.300
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: SHELXS
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.25
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM MES, 20% PEG 8K, 150MM AMMONIUM
REMARK 280 SULFATE, PH 6.5, VAPOR DIFFUSION, SITTING 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 28.72050
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 58.28500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 37.89850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.28500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 28.72050
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 37.89850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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: MONOMERIC
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 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 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 B 568
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 CYS B 620 CB CYS B 620 SG -0.106
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 PRO A 569 C - N - CA ANGL. DEV. = 10.0 DEGREES
REMARK 500 ASP A 612 CB - CG - OD1 ANGL. DEV. = 5.5 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 GLU A 655 -119.79 75.66
REMARK 500 LYS A 684 -44.08 -137.72
REMARK 500 GLU B 655 -121.45 73.27
REMARK 500 PRO B 709 23.87 -75.36
REMARK 500 ASP B 710 57.44 173.53
REMARK 500 ASP B 712 -67.01 -13.42
REMARK 500 ASN B 718 42.32 -144.89
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 ASP B 776 SER B 777 -149.13
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 306
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 305
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 307
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 308
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 309
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 310
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 311
DBREF 2NTE A 568 777 UNP Q99728 BARD1_HUMAN 568 777
DBREF 2NTE B 568 777 UNP Q99728 BARD1_HUMAN 568 777
SEQRES 1 A 210 GLY PRO LEU VAL LEU ILE GLY SER GLY LEU SER SER GLU
SEQRES 2 A 210 GLN GLN LYS MET LEU SER GLU LEU ALA VAL ILE LEU LYS
SEQRES 3 A 210 ALA LYS LYS TYR THR GLU PHE ASP SER THR VAL THR HIS
SEQRES 4 A 210 VAL VAL VAL PRO GLY ASP ALA VAL GLN SER THR LEU LYS
SEQRES 5 A 210 CYS MET LEU GLY ILE LEU ASN GLY CYS TRP ILE LEU LYS
SEQRES 6 A 210 PHE GLU TRP VAL LYS ALA CYS LEU ARG ARG LYS VAL CYS
SEQRES 7 A 210 GLU GLN GLU GLU LYS TYR GLU ILE PRO GLU GLY PRO ARG
SEQRES 8 A 210 ARG SER ARG LEU ASN ARG GLU GLN LEU LEU PRO LYS LEU
SEQRES 9 A 210 PHE ASP GLY CYS TYR PHE TYR LEU TRP GLY THR PHE LYS
SEQRES 10 A 210 HIS HIS PRO LYS ASP ASN LEU ILE LYS LEU VAL THR ALA
SEQRES 11 A 210 GLY GLY GLY GLN ILE LEU SER ARG LYS PRO LYS PRO ASP
SEQRES 12 A 210 SER ASP VAL THR GLN THR ILE ASN THR VAL ALA TYR HIS
SEQRES 13 A 210 ALA ARG PRO ASP SER ASP GLN ARG PHE CYS THR GLN TYR
SEQRES 14 A 210 ILE ILE TYR GLU ASP LEU CYS ASN TYR HIS PRO GLU ARG
SEQRES 15 A 210 VAL ARG GLN GLY LYS VAL TRP LYS ALA PRO SER SER TRP
SEQRES 16 A 210 PHE ILE ASP CYS VAL MET SER PHE GLU LEU LEU PRO LEU
SEQRES 17 A 210 ASP SER
SEQRES 1 B 210 GLY PRO LEU VAL LEU ILE GLY SER GLY LEU SER SER GLU
SEQRES 2 B 210 GLN GLN LYS MET LEU SER GLU LEU ALA VAL ILE LEU LYS
SEQRES 3 B 210 ALA LYS LYS TYR THR GLU PHE ASP SER THR VAL THR HIS
SEQRES 4 B 210 VAL VAL VAL PRO GLY ASP ALA VAL GLN SER THR LEU LYS
SEQRES 5 B 210 CYS MET LEU GLY ILE LEU ASN GLY CYS TRP ILE LEU LYS
SEQRES 6 B 210 PHE GLU TRP VAL LYS ALA CYS LEU ARG ARG LYS VAL CYS
SEQRES 7 B 210 GLU GLN GLU GLU LYS TYR GLU ILE PRO GLU GLY PRO ARG
SEQRES 8 B 210 ARG SER ARG LEU ASN ARG GLU GLN LEU LEU PRO LYS LEU
SEQRES 9 B 210 PHE ASP GLY CYS TYR PHE TYR LEU TRP GLY THR PHE LYS
SEQRES 10 B 210 HIS HIS PRO LYS ASP ASN LEU ILE LYS LEU VAL THR ALA
SEQRES 11 B 210 GLY GLY GLY GLN ILE LEU SER ARG LYS PRO LYS PRO ASP
SEQRES 12 B 210 SER ASP VAL THR GLN THR ILE ASN THR VAL ALA TYR HIS
SEQRES 13 B 210 ALA ARG PRO ASP SER ASP GLN ARG PHE CYS THR GLN TYR
SEQRES 14 B 210 ILE ILE TYR GLU ASP LEU CYS ASN TYR HIS PRO GLU ARG
SEQRES 15 B 210 VAL ARG GLN GLY LYS VAL TRP LYS ALA PRO SER SER TRP
SEQRES 16 B 210 PHE ILE ASP CYS VAL MET SER PHE GLU LEU LEU PRO LEU
SEQRES 17 B 210 ASP SER
HET SO4 A 302 5
HET CL A 304 1
HET EDO A 307 4
HET EDO A 309 4
HET EDO A 310 4
HET SO4 B 301 5
HET CL B 306 1
HET CL B 305 1
HET EDO B 308 4
HET EDO B 311 4
HETNAM SO4 SULFATE ION
HETNAM CL CHLORIDE ION
HETNAM EDO 1,2-ETHANEDIOL
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 SO4 2(O4 S 2-)
FORMUL 4 CL 3(CL 1-)
FORMUL 5 EDO 5(C2 H6 O2)
FORMUL 13 HOH *238(H2 O)
HELIX 1 1 SER A 578 LEU A 592 1 15
HELIX 2 2 THR A 617 ASN A 626 1 10
HELIX 3 3 PHE A 633 LYS A 643 1 11
HELIX 4 4 GLN A 647 TYR A 651 5 5
HELIX 5 5 GLU A 655 GLN A 666 1 12
HELIX 6 6 PRO A 687 GLY A 698 1 12
HELIX 7 7 LYS A 708 THR A 716 5 9
HELIX 8 8 SER A 728 PHE A 732 5 5
HELIX 9 9 SER A 760 PHE A 770 1 11
HELIX 10 10 SER B 578 LEU B 592 1 15
HELIX 11 11 THR B 617 GLY B 627 1 11
HELIX 12 12 PHE B 633 LYS B 643 1 11
HELIX 13 13 GLN B 647 GLU B 652 5 6
HELIX 14 14 GLU B 655 GLN B 666 1 12
HELIX 15 15 PRO B 687 GLY B 698 1 12
HELIX 16 16 SER B 711 ILE B 717 1 7
HELIX 17 17 SER B 728 PHE B 732 5 5
HELIX 18 18 SER B 760 PHE B 770 1 11
SHEET 1 A 4 LYS A 595 TYR A 597 0
SHEET 2 A 4 VAL A 571 GLY A 574 1 N LEU A 572 O LYS A 595
SHEET 3 A 4 HIS A 606 VAL A 609 1 O VAL A 608 N ILE A 573
SHEET 4 A 4 TRP A 629 LYS A 632 1 O TRP A 629 N VAL A 607
SHEET 1 B 5 GLN A 701 LEU A 703 0
SHEET 2 B 5 TYR A 676 LEU A 679 1 N PHE A 677 O LEU A 703
SHEET 3 B 5 GLN A 735 TYR A 739 1 O TYR A 736 N TYR A 678
SHEET 4 B 5 VAL A 755 PRO A 759 1 O TRP A 756 N ILE A 737
SHEET 5 B 5 ARG A 751 GLN A 752 -1 N GLN A 752 O VAL A 755
SHEET 1 C 4 LYS B 595 LYS B 596 0
SHEET 2 C 4 VAL B 571 GLY B 574 1 N LEU B 572 O LYS B 595
SHEET 3 C 4 HIS B 606 VAL B 609 1 O VAL B 608 N ILE B 573
SHEET 4 C 4 TRP B 629 LYS B 632 1 O LEU B 631 N VAL B 609
SHEET 1 D 5 GLN B 701 ILE B 702 0
SHEET 2 D 5 TYR B 676 LEU B 679 1 N PHE B 677 O GLN B 701
SHEET 3 D 5 GLN B 735 TYR B 739 1 O ILE B 738 N TYR B 678
SHEET 4 D 5 VAL B 755 PRO B 759 1 O ALA B 758 N ILE B 737
SHEET 5 D 5 ARG B 751 GLN B 752 -1 N GLN B 752 O VAL B 755
LINK O3 SO4 B 301 OG SER B 575 1555 1555 2.05
SITE 1 AC1 6 HOH B 63 HOH B 277 SER B 575 GLY B 576
SITE 2 AC1 6 THR B 617 LYS B 619
SITE 1 AC2 5 HOH A 10 SER A 575 GLY A 576 THR A 617
SITE 2 AC2 5 LYS A 619
SITE 1 AC3 1 ASN A 718
SITE 1 AC4 1 LYS B 757
SITE 1 AC5 3 ASP B 710 SER B 711 GLN B 715
SITE 1 AC6 6 HOH A 280 PRO A 707 SER A 711 ASP A 712
SITE 2 AC6 6 VAL A 713 GLN A 735
SITE 1 AC7 7 PHE B 672 ASP B 673 GLY B 674 CYS B 675
SITE 2 AC7 7 GLY B 699 GLY B 700 GLN B 701
SITE 1 AC8 4 HOH A 280 LEU A 703 SER A 704 ARG A 705
SITE 1 AC9 5 THR A 617 LEU A 618 MET A 621 HIS A 686
SITE 2 AC9 5 ASN A 690
SITE 1 BC1 2 ARG A 658 TYR B 678
CRYST1 57.441 75.797 116.570 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 0.017409 0.000000 0.000000 0.00000
SCALE2 0.000000 0.013193 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008579 0.00000
(ATOM LINES ARE NOT SHOWN.)
END