HEADER GENE REGULATION/ANTITUMOR PROTEIN/DNA 27-AUG-02 1MJE
TITLE STRUCTURE OF A BRCA2-DSS1-SSDNA COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: 5'-D(P*TP*TP*TP*TP*TP*T)-3';
COMPND 3 CHAIN: C;
COMPND 4 ENGINEERED: YES;
COMPND 5 MOL_ID: 2;
COMPND 6 MOLECULE: DELETED IN SPLIT HAND/SPLIT FOOT PROTEIN 1;
COMPND 7 CHAIN: B;
COMPND 8 SYNONYM: DSS1, SPLIT HAND/FOOT DELETED PROTEIN 1;
COMPND 9 ENGINEERED: YES;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: BREAST CANCER 2;
COMPND 12 CHAIN: A;
COMPND 13 FRAGMENT: SEQUENCE DATABASE RESIDUES 2378-2792, 2880-3113 (RESIDUES
COMPND 14 2793-2879 REMOVED);
COMPND 15 SYNONYM: BRCA2;
COMPND 16 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 MOL_ID: 2;
SOURCE 4 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 5 ORGANISM_COMMON: HUMAN;
SOURCE 6 ORGANISM_TAXID: 9606;
SOURCE 7 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 8 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;
SOURCE 11 MOL_ID: 3;
SOURCE 12 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 13 ORGANISM_COMMON: HOUSE MOUSE;
SOURCE 14 ORGANISM_TAXID: 10090;
SOURCE 15 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 16 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 18 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS
KEYWDS TUMOR SUPPRESSOR, BREAST CANCER SUSCEPTIBILITY, DNA-BINDING, GENE
KEYWDS 2 REGULATION-ANTITUMOR PROTEIN-DNA COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR H.YANG,P.D.JEFFREY,J.MILLER,E.KINNUCAN,Y.SUN,N.H.THOMA,N.ZHENG,
AUTHOR 2 P.L.CHEN,W.H.LEE,N.P.PAVLETICH
REVDAT 4 14-FEB-24 1MJE 1 REMARK
REVDAT 3 09-AUG-17 1MJE 1 SOURCE REMARK
REVDAT 2 24-FEB-09 1MJE 1 VERSN
REVDAT 1 27-SEP-02 1MJE 0
JRNL AUTH H.YANG,P.D.JEFFREY,J.MILLER,E.KINNUCAN,Y.SUN,N.H.THOMA,
JRNL AUTH 2 N.ZHENG,P.L.CHEN,W.H.LEE,N.P.PAVLETICH
JRNL TITL BRCA2 FUNCTION IN DNA BINDING AND RECOMBINATION FROM A
JRNL TITL 2 BRCA2-DSS1-SSDNA STRUCTURE.
JRNL REF SCIENCE V. 297 1837 2002
JRNL REFN ISSN 0036-8075
JRNL PMID 12228710
JRNL DOI 10.1126/SCIENCE.297.5588.1837
REMARK 2
REMARK 2 RESOLUTION. 3.50 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNS
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 REFINEMENT TARGET : ENGH & HUBER
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 15.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 22508
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM 2.5%
REMARK 3 R VALUE (WORKING SET) : 0.245
REMARK 3 FREE R VALUE : 0.278
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 565
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 : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
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 : 5077
REMARK 3 NUCLEIC ACID ATOMS : 121
REMARK 3 HETEROGEN ATOMS : 0
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.014
REMARK 3 BOND ANGLES (DEGREES) : NULL
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3 NCS RESTRAINTS. RMS SIGMA/WEIGHT
REMARK 3 GROUP 1 POSITIONAL (A) : NULL ; NULL
REMARK 3 GROUP 1 B-FACTOR (A**2) : NULL ; NULL
REMARK 3
REMARK 3 PARAMETER FILE 1 : NULL
REMARK 3 TOPOLOGY FILE 1 : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1MJE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-SEP-02.
REMARK 100 THE DEPOSITION ID IS D_1000016957.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 01-OCT-01
REMARK 200 TEMPERATURE (KELVIN) : 113
REMARK 200 PH : 5.8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : A1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.95
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 4
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24950
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.500
REMARK 200 RESOLUTION RANGE LOW (A) : 25.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.62
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.2
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
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: AMORE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 79.34
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM ACETATE, SODIUM CITRATE, NACL,
REMARK 280 DTT, PH 5.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -Y,X,Z
REMARK 290 4555 Y,-X,Z
REMARK 290 5555 -X,Y,-Z
REMARK 290 6555 X,-Y,-Z
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z
REMARK 290 9555 X+1/2,Y+1/2,Z+1/2
REMARK 290 10555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 11555 -Y+1/2,X+1/2,Z+1/2
REMARK 290 12555 Y+1/2,-X+1/2,Z+1/2
REMARK 290 13555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 14555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 15555 Y+1/2,X+1/2,-Z+1/2
REMARK 290 16555 -Y+1/2,-X+1/2,-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 0.00000
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 0.00000
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 0.00000
REMARK 290 SMTRY1 9 1.000000 0.000000 0.000000 99.43300
REMARK 290 SMTRY2 9 0.000000 1.000000 0.000000 99.43300
REMARK 290 SMTRY3 9 0.000000 0.000000 1.000000 100.02350
REMARK 290 SMTRY1 10 -1.000000 0.000000 0.000000 99.43300
REMARK 290 SMTRY2 10 0.000000 -1.000000 0.000000 99.43300
REMARK 290 SMTRY3 10 0.000000 0.000000 1.000000 100.02350
REMARK 290 SMTRY1 11 0.000000 -1.000000 0.000000 99.43300
REMARK 290 SMTRY2 11 1.000000 0.000000 0.000000 99.43300
REMARK 290 SMTRY3 11 0.000000 0.000000 1.000000 100.02350
REMARK 290 SMTRY1 12 0.000000 1.000000 0.000000 99.43300
REMARK 290 SMTRY2 12 -1.000000 0.000000 0.000000 99.43300
REMARK 290 SMTRY3 12 0.000000 0.000000 1.000000 100.02350
REMARK 290 SMTRY1 13 -1.000000 0.000000 0.000000 99.43300
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 99.43300
REMARK 290 SMTRY3 13 0.000000 0.000000 -1.000000 100.02350
REMARK 290 SMTRY1 14 1.000000 0.000000 0.000000 99.43300
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 99.43300
REMARK 290 SMTRY3 14 0.000000 0.000000 -1.000000 100.02350
REMARK 290 SMTRY1 15 0.000000 1.000000 0.000000 99.43300
REMARK 290 SMTRY2 15 1.000000 0.000000 0.000000 99.43300
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 100.02350
REMARK 290 SMTRY1 16 0.000000 -1.000000 0.000000 99.43300
REMARK 290 SMTRY2 16 -1.000000 0.000000 0.000000 99.43300
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 100.02350
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: TRIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, B, 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 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 MET B 1
REMARK 465 SER B 2
REMARK 465 GLU B 3
REMARK 465 LYS B 4
REMARK 465 LYS B 5
REMARK 465 GLN B 6
REMARK 465 ASP B 26
REMARK 465 TRP B 27
REMARK 465 ALA B 28
REMARK 465 GLY B 29
REMARK 465 LEU B 30
REMARK 465 ASP B 31
REMARK 465 GLU B 32
REMARK 465 ASP B 33
REMARK 465 GLU B 34
REMARK 465 ASP B 35
REMARK 465 ALA B 36
REMARK 465 ASP B 46
REMARK 465 ASN B 47
REMARK 465 VAL B 48
REMARK 465 GLU B 49
REMARK 465 GLY B 64
REMARK 465 TYR B 65
REMARK 465 LYS B 66
REMARK 465 MET B 67
REMARK 465 GLU B 68
REMARK 465 THR B 69
REMARK 465 SER B 70
REMARK 465 ASN A 2378
REMARK 465 GLN A 2379
REMARK 465 LYS A 2380
REMARK 465 SER A 2381
REMARK 465 THR A 2382
REMARK 465 ASP A 2383
REMARK 465 GLY A 2384
REMARK 465 ASP A 2385
REMARK 465 ARG A 2386
REMARK 465 GLU A 2387
REMARK 465 ASP A 2388
REMARK 465 GLY A 2389
REMARK 465 ASN A 2390
REMARK 465 ASP A 2391
REMARK 465 SER A 2392
REMARK 465 HIS A 2393
REMARK 465 VAL A 2394
REMARK 465 ARG A 2395
REMARK 465 GLN A 2396
REMARK 465 PHE A 2397
REMARK 465 ASN A 2398
REMARK 465 ILE A 2615
REMARK 465 SER A 2616
REMARK 465 PRO A 2617
REMARK 465 SER A 2618
REMARK 465 THR A 2619
REMARK 465 LYS A 2620
REMARK 465 VAL A 2621
REMARK 465 SER A 2622
REMARK 465 GLU A 2623
REMARK 465 THR A 2624
REMARK 465 SER A 2625
REMARK 465 GLY A 2626
REMARK 465 GLY A 2627
REMARK 465 LYS A 2628
REMARK 465 THR A 2629
REMARK 465 SER A 2630
REMARK 465 GLY A 2631
REMARK 465 GLU A 2632
REMARK 465 ASP A 2633
REMARK 465 ALA A 2634
REMARK 465 ASN A 2635
REMARK 465 LYS A 2636
REMARK 465 GLU A 2880
REMARK 465 GLY A 2881
REMARK 465 SER A 3111
REMARK 465 THR A 3112
REMARK 465 PRO A 3113
REMARK 465 ASN A 3114
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 PRO B 7 CG CD
REMARK 470 GLU B 25 CG CD OE1 OE2
REMARK 470 HIS B 37 CG ND1 CD2 CE1 NE2
REMARK 470 ASP B 50 CG OD1 OD2
REMARK 470 LYS B 62 CG CD CE NZ
REMARK 470 HIS B 63 CB CG ND1 CD2 CE1 NE2
REMARK 470 SER A2457 OG
REMARK 470 PRO A2458 CG CD
REMARK 470 LYS A2459 CG CD CE NZ
REMARK 470 GLN A2460 CG CD OE1 NE2
REMARK 470 LEU A2461 CG CD1 CD2
REMARK 470 LYS A2468 CG CD CE NZ
REMARK 470 GLU A2469 CG CD OE1 OE2
REMARK 470 VAL A2637 CG1 CG2
REMARK 470 TRP A3110 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A3110 CZ3 CH2
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 DT C 506 C5' C4' O4' C3' O3' C2' C1'
REMARK 480 DT C 506 N1 C2 O2 N3 C4 O4 C5
REMARK 480 DT C 506 C7 C6
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 O LEU A 3028 N GLU A 3030 1.97
REMARK 500 O ILE A 2509 N SER A 2511 2.15
REMARK 500
REMARK 500 REMARK: NULL
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 C 501 P DT C 501 OP3 -0.073
REMARK 500 VAL A2790 CA VAL A2790 CB 0.154
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 A2453 C - N - CA ANGL. DEV. = 14.9 DEGREES
REMARK 500 PRO A2453 C - N - CD ANGL. DEV. = -15.0 DEGREES
REMARK 500 VAL A2889 CB - CA - C ANGL. DEV. = -13.1 DEGREES
REMARK 500 GLY A3005 N - CA - C ANGL. DEV. = -20.3 DEGREES
REMARK 500 PRO A3054 C - N - CA ANGL. DEV. = 9.9 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 ASP B 17 -23.83 177.16
REMARK 500 GLU B 21 -76.54 -31.47
REMARK 500 PRO B 23 -27.36 -17.81
REMARK 500 ALA B 24 79.56 -109.79
REMARK 500 VAL B 38 -29.65 -27.72
REMARK 500 ASP B 41 -94.20 -45.99
REMARK 500 TRP B 43 -129.79 -62.00
REMARK 500 ASP B 44 134.44 -33.91
REMARK 500 LEU B 56 -73.43 -57.71
REMARK 500 ASP A2400 -160.38 94.96
REMARK 500 SER A2403 -77.34 -58.64
REMARK 500 SER A2404 42.98 -72.37
REMARK 500 GLN A2406 1.30 -68.25
REMARK 500 SER A2407 47.32 -90.06
REMARK 500 ALA A2408 -20.43 167.56
REMARK 500 LYS A2417 -84.45 -52.13
REMARK 500 ASN A2418 -34.81 -31.18
REMARK 500 SER A2430 -77.79 -62.24
REMARK 500 LEU A2431 -76.10 -34.88
REMARK 500 TYR A2432 -47.37 -28.97
REMARK 500 SER A2437 179.61 -57.66
REMARK 500 ALA A2447 3.92 -55.13
REMARK 500 ASP A2450 40.89 32.27
REMARK 500 PRO A2453 119.47 -6.22
REMARK 500 ALA A2455 67.19 -112.36
REMARK 500 CYS A2456 86.72 -66.94
REMARK 500 PRO A2458 98.16 95.59
REMARK 500 LEU A2461 65.60 172.51
REMARK 500 ILE A2463 -81.59 -29.68
REMARK 500 TYR A2464 -38.91 -14.38
REMARK 500 VAL A2466 -109.86 1.40
REMARK 500 SER A2467 67.93 93.61
REMARK 500 LYS A2468 4.00 -58.46
REMARK 500 CYS A2470 -65.85 -124.86
REMARK 500 ILE A2471 -48.96 -21.67
REMARK 500 ASN A2472 40.06 -77.31
REMARK 500 SER A2475 -38.51 -20.35
REMARK 500 ASN A2477 59.85 -94.12
REMARK 500 TYR A2480 -106.15 -77.73
REMARK 500 PHE A2481 -93.23 70.37
REMARK 500 GLN A2482 115.67 63.47
REMARK 500 ILE A2485 -0.94 -46.88
REMARK 500 PHE A2489 -61.59 -147.39
REMARK 500 LYS A2491 4.83 -174.07
REMARK 500 GLU A2492 -109.66 -39.71
REMARK 500 ALA A2496 -115.04 -81.20
REMARK 500 ALA A2503 175.98 30.18
REMARK 500 ASP A2504 -16.00 53.43
REMARK 500 ILE A2509 66.26 -102.91
REMARK 500 PRO A2510 62.54 -20.12
REMARK 500
REMARK 500 THIS ENTRY HAS 164 RAMACHANDRAN OUTLIERS.
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: PLANAR GROUPS
REMARK 500
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS
REMARK 500 AN RMSD GREATER THAN THIS VALUE
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 M RES CSSEQI RMS TYPE
REMARK 500 TYR A3072 0.07 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1IYJ RELATED DB: PDB
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 RESIDUES 2793-2879 OF THE BRCA2 CHAIN
REMARK 999 WERE REMOVED PROTEOLYTICALLY.
REMARK 999 RESIDUES 3087 AND 3089 ARE COVALENTLY
REMARK 999 BOUND. 3088 WAS SKIPPED IN THE NUMBERING.
DBREF 1MJE B 1 70 UNP P60896 DSS1_HUMAN 1 70
DBREF 1MJE A 2378 2792 GB 17973451 AAK57537 2378 2792
DBREF 1MJE A 2880 3114 GB 17973451 AAK57537 2880 3113
DBREF 1MJE C 501 506 PDB 1MJE 1MJE 501 506
SEQRES 1 C 6 DT DT DT DT DT DT
SEQRES 1 B 70 MET SER GLU LYS LYS GLN PRO VAL ASP LEU GLY LEU LEU
SEQRES 2 B 70 GLU GLU ASP ASP GLU PHE GLU GLU PHE PRO ALA GLU ASP
SEQRES 3 B 70 TRP ALA GLY LEU ASP GLU ASP GLU ASP ALA HIS VAL TRP
SEQRES 4 B 70 GLU ASP ASN TRP ASP ASP ASP ASN VAL GLU ASP ASP PHE
SEQRES 5 B 70 SER ASN GLN LEU ARG ALA GLU LEU GLU LYS HIS GLY TYR
SEQRES 6 B 70 LYS MET GLU THR SER
SEQRES 1 A 649 ASN GLN LYS SER THR ASP GLY ASP ARG GLU ASP GLY ASN
SEQRES 2 A 649 ASP SER HIS VAL ARG GLN PHE ASN LYS ASP LEU MET SER
SEQRES 3 A 649 SER LEU GLN SER ALA ARG ASP LEU GLN ASP MET ARG ILE
SEQRES 4 A 649 LYS ASN LYS GLU ARG ARG HIS LEU ARG LEU GLN PRO GLY
SEQRES 5 A 649 SER LEU TYR LEU THR LYS SER SER THR LEU PRO ARG ILE
SEQRES 6 A 649 SER LEU GLN ALA ALA VAL GLY ASP ARG ALA PRO SER ALA
SEQRES 7 A 649 CYS SER PRO LYS GLN LEU TYR ILE TYR GLY VAL SER LYS
SEQRES 8 A 649 GLU CYS ILE ASN VAL ASN SER LYS ASN ALA GLU TYR PHE
SEQRES 9 A 649 GLN PHE ASP ILE GLN ASP HIS PHE GLY LYS GLU ASP LEU
SEQRES 10 A 649 CYS ALA GLY LYS GLY PHE GLN LEU ALA ASP GLY GLY TRP
SEQRES 11 A 649 LEU ILE PRO SER ASN ASP GLY LYS ALA GLY LYS GLU GLU
SEQRES 12 A 649 PHE TYR ARG ALA LEU CYS ASP THR PRO GLY VAL ASP PRO
SEQRES 13 A 649 LYS LEU ILE SER SER ILE TRP VAL ALA ASN HIS TYR ARG
SEQRES 14 A 649 TRP ILE VAL TRP LYS LEU ALA ALA MET GLU PHE ALA PHE
SEQRES 15 A 649 PRO LYS GLU PHE ALA ASN ARG CYS LEU ASN PRO GLU ARG
SEQRES 16 A 649 VAL LEU LEU GLN LEU LYS TYR ARG TYR ASP VAL GLU ILE
SEQRES 17 A 649 ASP ASN SER ARG ARG SER ALA LEU LYS LYS ILE LEU GLU
SEQRES 18 A 649 ARG ASP ASP THR ALA ALA LYS THR LEU VAL LEU CYS ILE
SEQRES 19 A 649 SER ASP ILE ILE SER PRO SER THR LYS VAL SER GLU THR
SEQRES 20 A 649 SER GLY GLY LYS THR SER GLY GLU ASP ALA ASN LYS VAL
SEQRES 21 A 649 ASP THR ILE GLU LEU THR ASP GLY TRP TYR ALA VAL ARG
SEQRES 22 A 649 ALA GLN LEU ASP PRO PRO LEU MET ALA LEU VAL LYS SER
SEQRES 23 A 649 GLY LYS LEU THR VAL GLY GLN LYS ILE ILE THR GLN GLY
SEQRES 24 A 649 ALA GLU LEU VAL GLY SER PRO ASP ALA CYS ALA PRO LEU
SEQRES 25 A 649 GLU ALA PRO ASP SER LEU ARG LEU LYS ILE SER ALA ASN
SEQRES 26 A 649 SER THR ARG PRO ALA ARG TRP HIS SER ARG LEU GLY PHE
SEQRES 27 A 649 PHE ARG ASP PRO ARG PRO PHE PRO LEU PRO LEU SER SER
SEQRES 28 A 649 LEU PHE SER ASP GLY GLY ASN VAL GLY CYS VAL ASP ILE
SEQRES 29 A 649 ILE VAL GLN ARG VAL TYR PRO LEU GLN TRP VAL GLU LYS
SEQRES 30 A 649 THR VAL SER GLY LEU TYR ILE PHE ARG SER GLU ARG GLU
SEQRES 31 A 649 GLU GLU LYS GLU ALA LEU ARG PHE ALA GLU ALA GLN GLN
SEQRES 32 A 649 LYS LYS LEU GLU ALA LEU PHE THR LYS VAL HIS THR GLU
SEQRES 33 A 649 GLY LEU SER ARG ASP VAL THR THR VAL TRP LYS LEU ARG
SEQRES 34 A 649 VAL THR SER TYR LYS LYS LYS GLU LYS SER ALA LEU LEU
SEQRES 35 A 649 SER ILE TRP ARG PRO SER SER ASP LEU SER SER LEU LEU
SEQRES 36 A 649 THR GLU GLY LYS ARG TYR ARG ILE TYR HIS LEU ALA VAL
SEQRES 37 A 649 SER LYS SER LYS SER LYS PHE GLU ARG PRO SER ILE GLN
SEQRES 38 A 649 LEU THR ALA THR LYS ARG THR GLN TYR GLN GLN LEU PRO
SEQRES 39 A 649 VAL SER SER GLU THR LEU LEU GLN VAL TYR GLN PRO ARG
SEQRES 40 A 649 GLU SER LEU HIS PHE SER ARG LEU SER ASP PRO ALA PHE
SEQRES 41 A 649 GLN PRO PRO CYS SER GLU VAL ASP VAL VAL GLY VAL VAL
SEQRES 42 A 649 VAL SER VAL VAL LYS PRO ILE GLY LEU ALA PRO LEU VAL
SEQRES 43 A 649 TYR LEU SER ASP GLU CYS LEU ASN LEU LEU VAL VAL LYS
SEQRES 44 A 649 PHE GLY ILE ASP LEU ASN GLU ASP ILE LYS PRO ARG VAL
SEQRES 45 A 649 LEU ILE ALA ALA SER ASN LEU GLN CYS GLN PRO GLU SER
SEQRES 46 A 649 THR SER GLY VAL PRO THR LEU PHE ALA CYS HIS PHE SER
SEQRES 47 A 649 ILE PHE SER ALA SER PRO LYS GLU ALA TYR PHE GLN GLU
SEQRES 48 A 649 LYS VAL ASN ASN LEU LYS HIS ALA ILE GLU ASN ILE ASP
SEQRES 49 A 649 THR PHE TYR LYS GLU ALA GLU LYS LYS LEU ILE HIS VAL
SEQRES 50 A 649 LEU GLU GLY ASP SER PRO LYS TRP SER THR PRO ASN
HELIX 1 1 GLN B 55 LEU B 60 1 6
HELIX 2 2 MET A 2402 SER A 2404 5 3
HELIX 3 3 LEU A 2405 ARG A 2421 1 17
HELIX 4 4 GLY A 2429 SER A 2437 1 9
HELIX 5 5 GLN A 2445 GLY A 2449 5 5
HELIX 6 6 GLY A 2517 ASP A 2527 1 11
HELIX 7 7 ILE A 2539 PHE A 2557 1 19
HELIX 8 8 ASN A 2569 ILE A 2585 1 17
HELIX 9 9 SER A 2591 LEU A 2597 1 7
HELIX 10 10 ASP A 2654 GLY A 2664 1 11
HELIX 11 11 SER A 2700 ASN A 2702 5 3
HELIX 12 12 SER A 2764 GLU A 2768 5 5
HELIX 13 13 GLU A 2769 HIS A 2791 1 23
HELIX 14 14 ASP A 2914 LEU A 2918 5 5
HELIX 15 15 SER A 2960 TYR A 2968 1 9
HELIX 16 16 PHE A 2976 ASP A 2981 5 6
HELIX 17 17 GLU A 3070 ILE A 3087 1 18
HELIX 18 18 LYS A 3093 GLY A 3105 1 13
SHEET 1 A 2 LEU B 13 GLU B 14 0
SHEET 2 A 2 ILE A2442 SER A2443 1 O ILE A2442 N GLU B 14
SHEET 1 B 7 GLU A2678 VAL A2680 0
SHEET 2 B 7 ARG A2696 ILE A2699 -1 N ARG A2696 O VAL A2680
SHEET 3 B 7 ALA A2648 LEU A2653 1 O ARG A2650 N LEU A2697
SHEET 4 B 7 ILE A2640 THR A2643 -1 O ILE A2640 N ALA A2651
SHEET 5 B 7 LEU A2607 ASP A2613 -1 O CYS A2610 N THR A2643
SHEET 6 B 7 LYS A2671 THR A2674 -1 O ILE A2672 N LEU A2609
SHEET 7 B 7 THR A2704 PRO A2706 -1 N ARG A2705 O ILE A2673
SHEET 1 C 8 TYR A2760 ARG A2763 0
SHEET 2 C 8 TRP A2751 LYS A2754 -1 N TRP A2751 O ARG A2763
SHEET 3 C 8 VAL A2886 SER A2896 -1 O THR A2887 N VAL A2752
SHEET 4 C 8 VAL A2736 VAL A2746 -1 N ILE A2742 O THR A2895
SHEET 5 C 8 ARG A2924 LYS A2934 -1 O TYR A2925 N ILE A2741
SHEET 6 C 8 ILE A2944 LEU A2957 -1 N GLN A2945 O SER A2933
SHEET 7 C 8 ALA A2904 TRP A2909 1 O LEU A2905 N LEU A2946
SHEET 8 C 8 VAL A2886 SER A2896 -1 O TRP A2890 N ILE A2908
SHEET 1 D 6 VAL A2991 SER A2999 0
SHEET 2 D 6 TYR A3011 SER A3013 -1 O TYR A3011 N VAL A2998
SHEET 3 D 6 LEU A3019 PHE A3024 -1 O LEU A3020 N LEU A3012
SHEET 4 D 6 THR A3055 ALA A3058 1 O LEU A3056 N LYS A3023
SHEET 5 D 6 LEU A3037 GLN A3046 -1 N GLN A3044 O PHE A3057
SHEET 6 D 6 VAL A2991 SER A2999 -1 O VAL A2991 N LEU A3043
CRYST1 198.866 198.866 200.047 90.00 90.00 90.00 I 4 2 2 16
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 0.005029 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005029 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004999 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
