Header list of 2a51.pdb file
Complete list - 9 20 Bytes
HEADER VIRAL PROTEIN,METAL BINDING PROTEIN 30-JUN-05 2A51
TITLE STRUCTURE OF THE (13-51) DOMAIN OF THE NUCLEOCAPSID PROTEIN NCP8 FROM
TITLE 2 SIVLHOEST
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: NUCLEOCAPSID PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: ZINC FINGER DOMAIN;
COMPND 5 SYNONYM: NUCLEOCAPSID PROTEIN NCP8;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN SIV(SIMIAN
SOURCE 4 IMMUNODEFICIENCY VIRUS)
KEYWDS SIVLHOEST, NCP8, NUCLEOCAPSID, VIRAL PROTEIN, METAL BINDING PROTEIN
EXPDTA SOLUTION NMR
NUMMDL 20
AUTHOR N.MORELLET,H.MEUDAL,S.BOUAZIZ,B.P.ROQUES
REVDAT 3 09-MAR-22 2A51 1 REMARK LINK
REVDAT 2 24-FEB-09 2A51 1 VERSN
REVDAT 1 20-JUN-06 2A51 0
JRNL AUTH N.MORELLET,H.MEUDAL,S.BOUAZIZ,B.P.ROQUES
JRNL TITL STRUCTURE OF THE ZINC FINGER DOMAIN ENCOMPASSING RESIDUES
JRNL TITL 2 13-51 OF THE NUCLEOCAPSID PROTEIN FROM SIMIAN
JRNL TITL 3 IMMUNODEFICIENCY VIRUS
JRNL REF BIOCHEM.J. V. 393 725 2006
JRNL REFN ISSN 0264-6021
JRNL PMID 16229684
JRNL DOI 10.1042/BJ20051203
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR 3.0, DISCOVER 98
REMARK 3 AUTHORS : BRUKER (XWINNMR), ACCELRYS (DISCOVER)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURES ARE BASED ON A TOTAL OF
REMARK 3 474 NOE-DERIVED DISTANCE CONSTRAINTS
REMARK 4
REMARK 4 2A51 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-JUL-05.
REMARK 100 THE DEPOSITION ID IS D_1000033496.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 293
REMARK 210 PH : 6.0
REMARK 210 IONIC STRENGTH : NULL
REMARK 210 PRESSURE : AMBIENT
REMARK 210 SAMPLE CONTENTS : 1MM (13-51)NCP7
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D NOESY; 2D TOCSY
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : DRX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR 3.0
REMARK 210 METHOD USED : SIMULATED ANNEALING
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 20
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH THE LOWEST
REMARK 210 ENERGY
REMARK 210
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : 1
REMARK 210
REMARK 210 REMARK: THIS STRUCTURE WAS DETERMINED USING STANDARD 2D
REMARK 210 HOMONUCLEAR TECHNIQUES
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 PHE A 4 31.21 -88.68
REMARK 500 1 ASN A 5 -71.47 -139.52
REMARK 500 2 ASN A 5 -62.66 -100.94
REMARK 500 4 ASN A 5 -73.75 -137.20
REMARK 500 5 PHE A 4 31.78 -92.27
REMARK 500 5 ASN A 5 -71.35 -140.11
REMARK 500 6 ASN A 5 -67.62 -135.35
REMARK 500 7 PHE A 4 36.82 -93.45
REMARK 500 7 ASN A 5 -73.85 -142.92
REMARK 500 8 PHE A 4 33.94 -94.64
REMARK 500 8 ASN A 5 -72.72 -144.74
REMARK 500 9 ASN A 5 -73.69 -97.01
REMARK 500 10 PHE A 4 37.24 -97.48
REMARK 500 10 ASN A 5 -70.91 -144.19
REMARK 500 11 PHE A 4 31.80 -89.90
REMARK 500 11 ASN A 5 -71.73 -139.06
REMARK 500 12 PHE A 4 38.82 -93.65
REMARK 500 12 ASN A 5 -70.38 -146.53
REMARK 500 13 PHE A 4 32.66 -90.61
REMARK 500 13 ASN A 5 -73.90 -140.31
REMARK 500 14 ASN A 5 -72.08 -135.04
REMARK 500 15 ASN A 5 -73.47 -128.28
REMARK 500 15 GLU A 22 -64.70 -90.51
REMARK 500 16 PHE A 4 35.45 -89.64
REMARK 500 16 ASN A 5 -66.23 -145.00
REMARK 500 17 PHE A 4 41.16 -104.44
REMARK 500 17 ASN A 5 -71.01 -146.00
REMARK 500 19 PHE A 4 35.95 -90.47
REMARK 500 19 ASN A 5 -73.09 -145.73
REMARK 500 19 PRO A 19 171.81 -58.00
REMARK 500 20 PHE A 4 30.09 -87.08
REMARK 500 20 ASN A 5 -74.53 -138.44
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 54H ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 3 SG
REMARK 620 2 CYS A 6 SG 109.5
REMARK 620 3 HIS A 11 NE2 104.8 113.2
REMARK 620 4 CYS A 16 SG 107.9 111.3 109.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 55H ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 24 SG
REMARK 620 2 CYS A 27 SG 112.6
REMARK 620 3 HIS A 32 NE2 107.3 109.7
REMARK 620 4 CYS A 37 SG 105.6 113.4 107.9
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 54H
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 55H
DBREF 2A51 A 1 39 PDB 2A51 2A51 1 39
SEQRES 1 A 39 LEU THR CYS PHE ASN CYS GLY LYS PRO GLY HIS THR ALA
SEQRES 2 A 39 ARG MET CYS ARG GLN PRO ARG GLN GLU GLY CYS TRP ASN
SEQRES 3 A 39 CYS GLY SER LYS GLU HIS ARG PHE ALA GLN CYS PRO LYS
HET ZN A 54H 1
HET ZN A 55H 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
LINK SG CYS A 3 ZN ZN A 54H 1555 1555 2.22
LINK SG CYS A 6 ZN ZN A 54H 1555 1555 2.25
LINK NE2 HIS A 11 ZN ZN A 54H 1555 1555 2.06
LINK SG CYS A 16 ZN ZN A 54H 1555 1555 2.23
LINK SG CYS A 24 ZN ZN A 55H 1555 1555 2.28
LINK SG CYS A 27 ZN ZN A 55H 1555 1555 2.21
LINK NE2 HIS A 32 ZN ZN A 55H 1555 1555 2.00
LINK SG CYS A 37 ZN ZN A 55H 1555 1555 2.19
SITE 1 AC1 5 CYS A 3 CYS A 6 HIS A 11 CYS A 16
SITE 2 AC1 5 GLN A 18
SITE 1 AC2 4 CYS A 24 CYS A 27 HIS A 32 CYS A 37
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 - 9 20 Bytes