Header list of 1bor.pdb file
Complete list - 16 202 Bytes
HEADER TRANSCRIPTION REGULATION 27-SEP-95 1BOR
TITLE TRANSCRIPTION FACTOR PML, A PROTO-ONCOPROTEIN, NMR, 1 REPRESENTATIVE
TITLE 2 STRUCTURE AT PH 7.5, 30 C, IN THE PRESENCE OF ZINC
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRANSCRIPTION FACTOR PML;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RING FINGER DOMAIN, RESIDUES 49 - 104;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606
KEYWDS PROTO-ONCOGENE, NUCLEAR BODIES (PODS), LEUKEMIA, TRANSCRIPTION
KEYWDS 2 REGULATION
EXPDTA SOLUTION NMR
AUTHOR K.L.B.BORDEN,P.S.FREEMONT
REVDAT 4 16-FEB-22 1BOR 1 REMARK LINK
REVDAT 3 24-FEB-09 1BOR 1 VERSN
REVDAT 2 01-APR-03 1BOR 1 JRNL
REVDAT 1 01-APR-97 1BOR 0
JRNL AUTH K.L.BORDEN,M.N.BODDY,J.LALLY,N.J.O'REILLY,S.MARTIN,K.HOWE,
JRNL AUTH 2 E.SOLOMON,P.S.FREEMONT
JRNL TITL THE SOLUTION STRUCTURE OF THE RING FINGER DOMAIN FROM THE
JRNL TITL 2 ACUTE PROMYELOCYTIC LEUKAEMIA PROTO-ONCOPROTEIN PML.
JRNL REF EMBO J. V. 14 1532 1995
JRNL REFN ISSN 0261-4189
JRNL PMID 7729428
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH P.S.FREEMONT
REMARK 1 TITL THE RING FINGER. A NOVEL PROTEIN SEQUENCE MOTIF RELATED TO
REMARK 1 TITL 2 THE ZINC FINGER
REMARK 1 REF ANN.N.Y.ACAD.SCI. V. 684 174 1993
REMARK 1 REFN ISSN 0077-8923
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : NULL
REMARK 3 AUTHORS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 1BOR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.
REMARK 100 THE DEPOSITION ID IS D_1000171968.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 303
REMARK 210 PH : 7.5
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : NULL
REMARK 210 SAMPLE CONTENTS : NULL
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : NULL
REMARK 210 SPECTROMETER MODEL : NULL
REMARK 210 SPECTROMETER MANUFACTURER : NULL
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NULL
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : NULL
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : REPRESENTATIVE STRUCTURE
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL
REMARK 210
REMARK 210 REMARK: NULL
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: 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 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 3 -94.90 59.69
REMARK 500 GLN A 5 15.96 -157.18
REMARK 500 LEU A 7 23.29 -160.86
REMARK 500 ARG A 8 -75.51 -127.31
REMARK 500 ALA A 14 -63.93 -126.32
REMARK 500 GLU A 15 86.24 -150.02
REMARK 500 ALA A 16 99.55 21.27
REMARK 500 LYS A 20 154.15 -47.49
REMARK 500 LEU A 21 160.40 -38.65
REMARK 500 CYS A 24 63.16 -113.94
REMARK 500 LEU A 25 57.24 27.22
REMARK 500 LEU A 28 -109.66 -81.31
REMARK 500 SER A 30 89.52 -51.79
REMARK 500 GLU A 34 65.00 -169.18
REMARK 500 ALA A 35 25.50 47.55
REMARK 500 GLN A 39 65.66 132.22
REMARK 500 ILE A 42 38.28 30.91
REMARK 500 CYS A 43 -78.52 -38.28
REMARK 500 GLN A 44 71.89 24.10
REMARK 500 ALA A 45 -64.39 -171.14
REMARK 500 ALA A 51 -99.99 -100.22
REMARK 500 ALA A 55 -178.38 74.15
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 ARG A 8 0.18 SIDE CHAIN
REMARK 500
REMARK 500 REMARK: NULL
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 57 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 9 SG
REMARK 620 2 CYS A 12 SG 106.6
REMARK 620 3 CYS A 29 SG 110.5 112.1
REMARK 620 4 CYS A 32 SG 108.5 109.8 109.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 58 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 24 SG
REMARK 620 2 CYS A 24 O 64.8
REMARK 620 3 HIS A 26 ND1 106.9 88.8
REMARK 620 4 CYS A 40 SG 112.5 64.8 113.9
REMARK 620 5 CYS A 43 SG 111.3 170.4 100.8 110.9
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: ZN1
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: FIRST ZINC BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: ZN2
REMARK 800 EVIDENCE_CODE: UNKNOWN
REMARK 800 SITE_DESCRIPTION: SECOND ZINC BINDING SITE.
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 57
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 58
DBREF 1BOR A 1 56 UNP P29590 PML_HUMAN 49 104
SEQRES 1 A 56 GLU GLU GLU PHE GLN PHE LEU ARG CYS GLN GLN CYS GLN
SEQRES 2 A 56 ALA GLU ALA LYS CYS PRO LYS LEU LEU PRO CYS LEU HIS
SEQRES 3 A 56 THR LEU CYS SER GLY CYS LEU GLU ALA SER GLY MET GLN
SEQRES 4 A 56 CYS PRO ILE CYS GLN ALA PRO TRP PRO LEU GLY ALA ASP
SEQRES 5 A 56 THR PRO ALA LEU
HET ZN A 57 1
HET ZN A 58 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
HELIX 1 1 GLU A 34 MET A 38 1RIGHT-HANDED 5
HELIX 2 1 ALA A 45 PRO A 48 5RIGHT-HANDED 3/10 4
SHEET 1 B1 4 GLN A 5 ARG A 8 0
SHEET 2 B1 4 PRO A 19 LEU A 21 -1
SHEET 3 B1 4 HIS A 26 LEU A 28 -1
SHEET 4 B1 4 THR A 53 LEU A 56 1
LINK SG CYS A 9 ZN ZN A 57 1555 1555 2.30
LINK SG CYS A 12 ZN ZN A 57 1555 1555 2.29
LINK SG CYS A 24 ZN ZN A 58 1555 1555 2.26
LINK O CYS A 24 ZN ZN A 58 1555 1555 2.67
LINK ND1 HIS A 26 ZN ZN A 58 1555 1555 1.93
LINK SG CYS A 29 ZN ZN A 57 1555 1555 2.28
LINK SG CYS A 32 ZN ZN A 57 1555 1555 2.30
LINK SG CYS A 40 ZN ZN A 58 1555 1555 2.27
LINK SG CYS A 43 ZN ZN A 58 1555 1555 2.29
SITE 1 ZN1 5 CYS A 9 CYS A 12 CYS A 29 CYS A 32
SITE 2 ZN1 5 ZN A 57
SITE 1 ZN2 5 HIS A 26 CYS A 24 CYS A 40 CYS A 43
SITE 2 ZN2 5 ZN A 58
SITE 1 AC1 4 CYS A 9 CYS A 12 CYS A 29 CYS A 32
SITE 1 AC2 5 LYS A 20 CYS A 24 HIS A 26 CYS A 40
SITE 2 AC2 5 CYS A 43
CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 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
Complete list - 16 202 Bytes