Header list of 1dsq.pdb file
Complete list - 16 20 Bytes
HEADER VIRAL PROTEIN 08-JAN-00 1DSQ
TITLE STRUCTURE OF THE MMTV NUCLEOCAPSID PROTEIN (ZINC FINGER 1)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEIC ACID BINDING PROTEIN P14;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER 1 OF NUCLEOCAPSID PROTEIN;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: MOUSE MAMMARY TUMOR VIRUS;
SOURCE 3 ORGANISM_TAXID: 11757;
SOURCE 4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 5 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)PLYSE;
SOURCE 7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 8 EXPRESSION_SYSTEM_PLASMID: PET-3D
KEYWDS CCHC TYPE ZINC FINGER, VIRUS/VIRAL PROTEIN, VIRAL PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR D.J.KLEIN,P.E.JOHNSON,E.S.ZOLLARS,R.N.DE GUZMAN,M.F.SUMMERS
REVDAT 4 16-FEB-22 1DSQ 1 REMARK LINK
REVDAT 3 24-FEB-09 1DSQ 1 VERSN
REVDAT 2 18-FEB-00 1DSQ 1 JRNL
REVDAT 1 28-JAN-00 1DSQ 0
JRNL AUTH D.J.KLEIN,P.E.JOHNSON,E.S.ZOLLARS,R.N.DE GUZMAN,M.F.SUMMERS
JRNL TITL THE NMR STRUCTURE OF THE NUCLEOCAPSID PROTEIN FROM THE MOUSE
JRNL TITL 2 MAMMARY TUMOR VIRUS REVEALS UNUSUAL FOLDING OF THE
JRNL TITL 3 C-TERMINAL ZINC KNUCKLE.
JRNL REF BIOCHEMISTRY V. 39 1604 2000
JRNL REFN ISSN 0006-2960
JRNL PMID 10677209
JRNL DOI 10.1021/BI9922493
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : DYANA 1.5
REMARK 3 AUTHORS : GUNTERT
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: DATA WAS COLLECTED ON THE INTACT
REMARK 3 NUCLEOCAPSID PROTEIN BUT THE STRUCTURES OF THE N- AND C-TERMINAL
REMARK 3 ZINC FINGERS WERE CALCULATED INDEPENDENTLY. THESE TWO DOMAINS DO
REMARK 3 NOT INTERACT WITH EACH OTHER
REMARK 4
REMARK 4 1DSQ COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JAN-00.
REMARK 100 THE DEPOSITION ID IS D_1000010334.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 25
REMARK 210 PH : 7.0
REMARK 210 IONIC STRENGTH : ~50 MM
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1 MM UNLABELLED MMTV NC, 25 MM
REMARK 210 ACETATE (D3), PH 7.0, 20 MM NACL,
REMARK 210 0.1 MM ZNCL2, 0.1 MM BME
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : NULL
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AVANCE; PSG
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER; GE
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : NMRPIPE 1.7, NMRVIEW 3
REMARK 210 METHOD USED : NULL
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : TARGET FUNCTION
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
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 2 LYS A 45 64.06 -153.56
REMARK 500 2 GLU A 46 -46.74 -172.59
REMARK 500 3 GLU A 46 -59.46 -157.04
REMARK 500 4 LYS A 45 63.40 -176.04
REMARK 500 6 GLU A 46 -60.05 -165.63
REMARK 500 7 LYS A 45 70.24 68.19
REMARK 500 7 GLU A 46 -46.37 -136.48
REMARK 500 8 LYS A 45 65.28 -159.18
REMARK 500 8 GLU A 46 -37.63 -178.70
REMARK 500 9 GLU A 46 -38.18 177.68
REMARK 500 10 GLU A 46 -60.22 -153.11
REMARK 500 11 LYS A 45 64.92 -174.91
REMARK 500 14 LYS A 45 89.28 44.32
REMARK 500 15 LYS A 45 71.60 -163.09
REMARK 500 18 LYS A 45 80.34 -171.74
REMARK 500 19 LYS A 45 60.66 74.31
REMARK 500 20 LYS A 45 55.09 -169.95
REMARK 500 20 GLU A 46 -44.05 -160.59
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 144 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 31 SG
REMARK 620 2 CYS A 34 SG 85.0
REMARK 620 3 HIS A 39 NE2 90.9 106.3
REMARK 620 4 CYS A 44 SG 98.4 158.2 95.2
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 144
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1DSV RELATED DB: PDB
REMARK 900 STRUCTURE OF THE MMTV NUCLEOCAPSID PROTEIN (C-TERMINAL ZINC FINGER)
DBREF 1DSQ A 27 47 UNP P11284 GAG_MMTVC 523 543
SEQRES 1 A 21 LYS GLY PRO VAL CYS PHE SER CYS GLY LYS THR GLY HIS
SEQRES 2 A 21 ILE LYS ARG ASP CYS LYS GLU GLU
HET ZN A 144 1
HETNAM ZN ZINC ION
FORMUL 2 ZN ZN 2+
LINK SG CYS A 31 ZN ZN A 144 1555 1555 2.36
LINK SG CYS A 34 ZN ZN A 144 1555 1555 2.36
LINK NE2 HIS A 39 ZN ZN A 144 1555 1555 2.08
LINK SG CYS A 44 ZN ZN A 144 1555 1555 2.30
SITE 1 AC1 4 CYS A 31 CYS A 34 HIS A 39 CYS A 44
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
MODEL 1
Complete list - 16 20 Bytes