Header list of 1jm7.pdb file
Complete list - b 23 2 Bytes
HEADER ANTITUMOR 17-JUL-01 1JM7
TITLE SOLUTION STRUCTURE OF THE BRCA1/BARD1 RING-DOMAIN HETERODIMER
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RING-DOMAIN;
COMPND 5 SYNONYM: BRCA1;
COMPND 6 ENGINEERED: YES;
COMPND 7 OTHER_DETAILS: RESIDUES 104-112 OF CHAIN A AND 123-142 OF CHAIN B ARE
COMPND 8 MISSING IN EACH MODEL DUE TO DISORDER.;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: BRCA1-ASSOCIATED RING DOMAIN PROTEIN 1;
COMPND 11 CHAIN: B;
COMPND 12 FRAGMENT: RING-DOMAIN;
COMPND 13 SYNONYM: BARD1;
COMPND 14 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: BRCA1;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLAMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET11A;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: BARD1;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21 DE3;
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PET11A
KEYWDS BRCA1, BARD1, RING FINGER, ZINC-BINDING PROTEIN, HETERODIMER,
KEYWDS 2 UBIQUITIN LIGASE, ANTITUMOR
EXPDTA SOLUTION NMR
NUMMDL 14
AUTHOR P.S.BRZOVIC,P.RAJAGOPAL,D.W.HOYT,M.-C.KING,R.E.KLEVIT
REVDAT 4 23-FEB-22 1JM7 1 REMARK SEQADV LINK
REVDAT 3 24-FEB-09 1JM7 1 VERSN
REVDAT 2 01-APR-03 1JM7 1 JRNL
REVDAT 1 03-OCT-01 1JM7 0
JRNL AUTH P.S.BRZOVIC,P.RAJAGOPAL,D.W.HOYT,M.C.KING,R.E.KLEVIT
JRNL TITL STRUCTURE OF A BRCA1-BARD1 HETERODIMERIC RING-RING COMPLEX.
JRNL REF NAT.STRUCT.BIOL. V. 8 833 2001
JRNL REFN ISSN 1072-8368
JRNL PMID 11573085
JRNL DOI 10.1038/NSB1001-833
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 2.6, CNS
REMARK 3 AUTHORS : BRUNGER (CNS)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: STRUCTURES ARE BASED ON A TOTAL OF 1664
REMARK 3 RESTRAINTS, 480 INTRARESIDUE RESTRAINTS, 475 SEQUENTIAL
REMARK 3 RESTRAINTS, 215 MEDIUM-RANGE RESTRAINTS, 256 LONG-RANGE
REMARK 3 RESTRAINTS, 82 INTERMOLECULAR RESTRAINTS, 70 HYDROGEN BOND
REMARK 3 RESTRAINTS, 16 ZINC RESTRAINTS
REMARK 4
REMARK 4 1JM7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 23-JUL-01.
REMARK 100 THE DEPOSITION ID IS D_1000013931.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 315; 315; 315; 315
REMARK 210 PH : 6.8; 6.8; 6.8; 6.8
REMARK 210 IONIC STRENGTH : 0.2M NACL; 0.2M NACL; 0.2M NACL;
REMARK 210 0.2M NACL
REMARK 210 PRESSURE : AMBIENT; AMBIENT; AMBIENT;
REMARK 210 AMBIENT
REMARK 210 SAMPLE CONTENTS : SAMPLE 1: 0.8-1.1MM U-15N,13C
REMARK 210 BRCA1; UNLABELED BARD1, 25MM
REMARK 210 SODIUM PHOSPHATE, 0.2M NACL, 2MM
REMARK 210 DTT. SAMPLE 2: 0.8-1.1MM U-15N,
REMARK 210 13C BARD1; UNLABELED BRCA1, 25MM
REMARK 210 SODIUM PHOSPHATE, 0.2M NACL, 2MM
REMARK 210 DTT. SAMPLE 3: 0.8-1.1MM U-15N,
REMARK 210 13C,85%-2H BRCA1; UNLABELED
REMARK 210 BARD1, 25MM SODIUM PHOSPHATE,
REMARK 210 0.2M NACL, 2MM DTT. SAMPLE 4:
REMARK 210 0.8-1.1MM U-15N,13C,85%-2H BARD1;
REMARK 210 UNLABELED BRCA,1 25MM SODIUM
REMARK 210 PHOSPHATE, 0.2M NACL, 2MM DTT.;
REMARK 210 0.8-1.1MM U-15N,13C BARD1;
REMARK 210 UNLABELED BRCA1 25MM SODIUM
REMARK 210 PHOSPHATE 0.2M NACL 2MM DTT; 0.8-
REMARK 210 1.1MM U-15N,13C,85%-2H BRCA1;
REMARK 210 UNLABELED BARD1 25MM SODIUM
REMARK 210 PHOSPHATE 0.2M NACL 2MM DTT; 0.8-
REMARK 210 1.1MM U-15N,13C,85%-2H BARD1;
REMARK 210 UNLABELED BRCA1 25MM SODIUM
REMARK 210 PHOSPHATE 0.2M NACL 2MM DTT
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 3D_15N-SEPARATED_NOESY; 4D_13C
REMARK 210 -SEPARATED_NOESY; 3D_15N/13C-
REMARK 210 SEPARATED_NOESY
REMARK 210 SPECTROMETER FIELD STRENGTH : 500 MHZ; 600 MHZ; 800 MHZ
REMARK 210 SPECTROMETER MODEL : DMX; INOVA
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; VARIAN
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : VNMR, NMRPIPE, NMRVIEW 5.0, CNS
REMARK 210 1.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY SIMULATED
REMARK 210 ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 25
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 14
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LEAST
REMARK 210 RESTRAINT VIOLATIONS, STRUCTURES
REMARK 210 WITH THE LOWEST ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 2
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR
REMARK 210 SPECTROSCOPY
REMARK 215
REMARK 215 NMR STUDY
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION
REMARK 215 NMR DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE THAT
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON
REMARK 215 THESE RECORDS ARE MEANINGLESS.
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: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 123 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 24 SG
REMARK 620 2 CYS A 27 SG 86.9
REMARK 620 3 CYS A 44 SG 88.2 138.2
REMARK 620 4 CYS A 47 SG 123.2 128.2 88.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 124 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 39 SG
REMARK 620 2 HIS A 41 NE2 106.7
REMARK 620 3 CYS A 61 SG 109.0 109.7
REMARK 620 4 CYS A 64 SG 89.1 149.0 89.0
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 143 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 50 SG
REMARK 620 2 CYS B 53 SG 107.4
REMARK 620 3 CYS B 71 SG 88.1 88.6
REMARK 620 4 CYS B 74 SG 161.6 88.2 102.5
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 144 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 66 SG
REMARK 620 2 HIS B 68 ND1 132.7
REMARK 620 3 CYS B 83 SG 128.2 90.1
REMARK 620 4 CYS B 86 SG 93.2 73.9 131.2
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 123
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 124
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 143
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 144
DBREF 1JM7 A 1 110 UNP P38398 BRCA1_HUMAN 1 110
DBREF 1JM7 B 26 140 UNP Q99728 BARD1_HUMAN 26 140
SEQADV 1JM7 GLY A 111 UNP P38398 CLONING ARTIFACT
SEQADV 1JM7 LYS A 112 UNP P38398 CLONING ARTIFACT
SEQADV 1JM7 GLY B 141 UNP Q99728 CLONING ARTIFACT
SEQADV 1JM7 LYS B 142 UNP Q99728 CLONING ARTIFACT
SEQRES 1 A 112 MET ASP LEU SER ALA LEU ARG VAL GLU GLU VAL GLN ASN
SEQRES 2 A 112 VAL ILE ASN ALA MET GLN LYS ILE LEU GLU CYS PRO ILE
SEQRES 3 A 112 CYS LEU GLU LEU ILE LYS GLU PRO VAL SER THR LYS CYS
SEQRES 4 A 112 ASP HIS ILE PHE CYS LYS PHE CYS MET LEU LYS LEU LEU
SEQRES 5 A 112 ASN GLN LYS LYS GLY PRO SER GLN CYS PRO LEU CYS LYS
SEQRES 6 A 112 ASN ASP ILE THR LYS ARG SER LEU GLN GLU SER THR ARG
SEQRES 7 A 112 PHE SER GLN LEU VAL GLU GLU LEU LEU LYS ILE ILE CYS
SEQRES 8 A 112 ALA PHE GLN LEU ASP THR GLY LEU GLU TYR ALA ASN SER
SEQRES 9 A 112 TYR ASN PHE ALA LYS LYS GLY LYS
SEQRES 1 B 117 MET GLU PRO ASP GLY ARG GLY ALA TRP ALA HIS SER ARG
SEQRES 2 B 117 ALA ALA LEU ASP ARG LEU GLU LYS LEU LEU ARG CYS SER
SEQRES 3 B 117 ARG CYS THR ASN ILE LEU ARG GLU PRO VAL CYS LEU GLY
SEQRES 4 B 117 GLY CYS GLU HIS ILE PHE CYS SER ASN CYS VAL SER ASP
SEQRES 5 B 117 CYS ILE GLY THR GLY CYS PRO VAL CYS TYR THR PRO ALA
SEQRES 6 B 117 TRP ILE GLN ASP LEU LYS ILE ASN ARG GLN LEU ASP SER
SEQRES 7 B 117 MET ILE GLN LEU CYS SER LYS LEU ARG ASN LEU LEU HIS
SEQRES 8 B 117 ASP ASN GLU LEU SER ASP LEU LYS GLU ASP LYS PRO ARG
SEQRES 9 B 117 LYS SER LEU PHE ASN ASP ALA GLY ASN LYS LYS GLY LYS
HET ZN A 123 1
HET ZN A 124 1
HET ZN B 143 1
HET ZN B 144 1
HETNAM ZN ZINC ION
FORMUL 3 ZN 4(ZN 2+)
HELIX 1 1 ARG A 7 LEU A 22 1 16
HELIX 2 2 LYS A 45 GLN A 54 1 10
HELIX 3 3 SER A 80 THR A 97 1 18
HELIX 4 4 TRP B 34 LEU B 47 1 14
HELIX 5 5 CYS B 74 ILE B 79 5 6
HELIX 6 6 ASN B 98 ASP B 117 1 20
SHEET 1 A 1 VAL A 35 SER A 36 0
SHEET 1 B 1 ILE A 42 PHE A 43 0
SHEET 1 C 1 GLN A 74 GLU A 75 0
SHEET 1 D 1 VAL B 61 CYS B 62 0
SHEET 1 E 1 ILE B 69 PHE B 70 0
LINK SG CYS A 24 ZN ZN A 123 1555 1555 2.41
LINK SG CYS A 27 ZN ZN A 123 1555 1555 2.42
LINK SG CYS A 39 ZN ZN A 124 1555 1555 2.39
LINK NE2 HIS A 41 ZN ZN A 124 1555 1555 2.45
LINK SG CYS A 44 ZN ZN A 123 1555 1555 2.41
LINK SG CYS A 47 ZN ZN A 123 1555 1555 2.41
LINK SG CYS A 61 ZN ZN A 124 1555 1555 2.40
LINK SG CYS A 64 ZN ZN A 124 1555 1555 2.40
LINK SG CYS B 50 ZN ZN B 143 1555 1555 2.42
LINK SG CYS B 53 ZN ZN B 143 1555 1555 2.41
LINK SG CYS B 66 ZN ZN B 144 1555 1555 2.42
LINK ND1 HIS B 68 ZN ZN B 144 1555 1555 2.61
LINK SG CYS B 71 ZN ZN B 143 1555 1555 2.40
LINK SG CYS B 74 ZN ZN B 143 1555 1555 2.42
LINK SG CYS B 83 ZN ZN B 144 1555 1555 2.42
LINK SG CYS B 86 ZN ZN B 144 1555 1555 2.42
SITE 1 AC1 5 CYS A 24 ILE A 26 CYS A 27 CYS A 44
SITE 2 AC1 5 CYS A 47
SITE 1 AC2 4 CYS A 39 HIS A 41 CYS A 61 CYS A 64
SITE 1 AC3 4 CYS B 50 CYS B 53 CYS B 71 CYS B 74
SITE 1 AC4 4 CYS B 66 HIS B 68 CYS B 83 CYS B 86
CRYST1 1
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 1.000000 0.000000 0.000000 0.00000
SCALE2 0.000000 1.000000 0.000000 0.00000
SCALE3 0.000000 0.000000 1.000000 0.00000
MODEL 1
Complete list - b 23 2 Bytes