Header list of 1dsv.pdb file
Complete list - 16 20 Bytes
HEADER VIRAL PROTEIN 08-JAN-00 1DSV TITLE STRUCTURE OF THE MMTV NUCLEOCAPSID PROTEIN (C-TERMINAL ZINC FINGER) COMPND MOL_ID: 1; COMPND 2 MOLECULE: NUCLEIC ACID BINDING PROTEIN P14; COMPND 3 CHAIN: A; COMPND 4 FRAGMENT: C-TERMINAL ZINC FINGER 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 1DSV 1 REMARK LINK REVDAT 3 24-FEB-09 1DSV 1 VERSN REVDAT 2 18-FEB-00 1DSV 1 JRNL REVDAT 1 28-JAN-00 1DSV 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 1DSV 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_1000010335. 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 1 CYS A 58 102.53 -43.60 REMARK 500 1 HIS A 66 167.60 178.90 REMARK 500 1 LYS A 77 151.63 -37.25 REMARK 500 1 LEU A 82 99.66 -39.16 REMARK 500 2 CYS A 58 103.99 -45.97 REMARK 500 2 HIS A 66 164.12 179.66 REMARK 500 2 LYS A 77 151.53 -37.32 REMARK 500 2 LEU A 82 99.55 -39.04 REMARK 500 3 CYS A 58 101.96 -42.94 REMARK 500 3 HIS A 66 173.06 179.30 REMARK 500 3 LYS A 77 150.07 -37.28 REMARK 500 3 LEU A 82 99.48 -38.92 REMARK 500 4 LEU A 57 108.20 -53.74 REMARK 500 4 CYS A 58 101.41 -41.94 REMARK 500 4 HIS A 66 169.99 175.79 REMARK 500 4 LYS A 77 150.54 -37.13 REMARK 500 4 LEU A 82 99.47 -38.92 REMARK 500 5 PRO A 55 -72.77 -75.02 REMARK 500 5 CYS A 58 102.46 -43.41 REMARK 500 5 HIS A 66 174.36 177.89 REMARK 500 5 LYS A 77 153.80 -36.89 REMARK 500 6 CYS A 58 105.98 -49.74 REMARK 500 6 ARG A 60 -66.90 -90.97 REMARK 500 6 LYS A 77 149.90 -36.78 REMARK 500 6 LEU A 82 99.23 -38.57 REMARK 500 7 CYS A 58 101.92 -42.67 REMARK 500 7 HIS A 66 171.08 177.17 REMARK 500 7 LYS A 77 150.68 -37.08 REMARK 500 7 LEU A 82 99.52 -38.99 REMARK 500 8 CYS A 58 104.94 -47.45 REMARK 500 8 ARG A 60 -67.54 -90.28 REMARK 500 8 LYS A 77 151.25 -37.10 REMARK 500 8 LEU A 82 99.41 -38.77 REMARK 500 9 CYS A 58 104.60 -47.21 REMARK 500 9 ARG A 60 -67.27 -90.64 REMARK 500 9 SER A 73 -178.77 -60.25 REMARK 500 9 LYS A 77 150.32 -36.27 REMARK 500 9 LEU A 82 159.18 -40.15 REMARK 500 10 CYS A 58 100.96 -41.60 REMARK 500 10 HIS A 66 168.99 176.50 REMARK 500 10 LYS A 77 150.08 -36.73 REMARK 500 10 LEU A 82 158.86 -40.11 REMARK 500 11 PRO A 55 -168.97 -75.01 REMARK 500 11 CYS A 58 106.44 -50.07 REMARK 500 11 ARG A 60 -67.96 -90.88 REMARK 500 11 LYS A 77 151.98 -36.33 REMARK 500 12 LEU A 57 109.66 -49.23 REMARK 500 12 CYS A 58 103.96 -45.99 REMARK 500 12 LYS A 63 15.33 -140.54 REMARK 500 12 HIS A 66 171.72 176.42 REMARK 500 REMARK 500 THIS ENTRY HAS 83 RAMACHANDRAN OUTLIERS. 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 171 ZN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 CYS A 58 SG REMARK 620 2 CYS A 61 SG 96.1 REMARK 620 3 HIS A 66 NE2 94.9 109.5 REMARK 620 4 CYS A 71 SG 130.0 122.8 99.4 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 171 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 1DSQ RELATED DB: PDB REMARK 900 N-TERMINAL ZINC FINGER OF THE MMTV NUCLEOCAPSID PROTEIN DBREF 1DSV A 54 84 UNP P11284 GAG_MMTVC 550 580 SEQRES 1 A 31 PRO PRO GLY LEU CYS PRO ARG CYS LYS LYS GLY TYR HIS SEQRES 2 A 31 TRP LYS SER GLU CYS LYS SER LYS PHE ASP LYS ASP GLY SEQRES 3 A 31 ASN PRO LEU PRO PRO HET ZN A 171 1 HETNAM ZN ZINC ION FORMUL 2 ZN ZN 2+ HELIX 1 1 LYS A 77 GLY A 79 5 3 SHEET 1 A 2 PHE A 75 ASP A 76 0 SHEET 2 A 2 ASN A 80 PRO A 81 -1 O ASN A 80 N ASP A 76 LINK SG CYS A 58 ZN ZN A 171 1555 1555 2.39 LINK SG CYS A 61 ZN ZN A 171 1555 1555 2.36 LINK NE2 HIS A 66 ZN ZN A 171 1555 1555 2.07 LINK SG CYS A 71 ZN ZN A 171 1555 1555 2.30 SITE 1 AC1 4 CYS A 58 CYS A 61 HIS A 66 CYS A 71 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