Header list of 1q3z.pdb file
Complete list - 27 202 Bytes
HEADER VIRAL PROTEIN 01-AUG-03 1Q3Z
TITLE NMR STRUCTURE OF THE CYS28HIS MUTANT (E FORM) OF THE NUCLEOCAPSID
TITLE 2 PROTEIN NCP7 OF HIV-1.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GAG PROTEIN;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: RESIDUES 390-431;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 SYNTHETIC: YES;
SOURCE 3 OTHER_DETAILS: TWO PEPTIDES HAVE BEEN CHEMICALLY SYNTHESIZED WITH
SOURCE 4 AND WITHOUT A 15N/13C LABELLED HISTIDINE RESIDUE AT POSITION 28
KEYWDS CCHC ZINC KNUCKLE, CCHH ZINC KNUCKLE, VIRAL PROTEIN
EXPDTA SOLUTION NMR
AUTHOR S.RAMBOARINA,S.DRUILLENNEC,N.MORELLET,S.BOUAZIZ,B.P.ROQUES
REVDAT 3 27-OCT-21 1Q3Z 1 REMARK SEQADV LINK
REVDAT 2 24-FEB-09 1Q3Z 1 VERSN
REVDAT 1 07-SEP-04 1Q3Z 0
JRNL AUTH S.RAMBOARINA,S.DRUILLENNEC,N.MORELLET,S.BOUAZIZ,B.P.ROQUES
JRNL TITL TARGET SPECIFICITY OF HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
JRNL TITL 2 NCP7 REQUIRES AN INTACT CONFORMATION OF ITS CCHC N-TERMINAL
JRNL TITL 3 ZINC FINGER.
JRNL REF J.VIROL. V. 78 6682 2004
JRNL REFN ISSN 0022-538X
JRNL PMID 15163759
JRNL DOI 10.1128/JVI.78.12.6682-6687.2004
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH S.RAMBOARINA,N.MORELLET,M.C.FOURNIE-ZALUSKI,B.P.ROQUES
REMARK 1 TITL STRUCTURAL INVESTIGATION ON THE REQUIREMENT OF CCHH ZINC
REMARK 1 TITL 2 FINGER TYPE IN NUCLEOCAPSID PROTEIN OF HUMAN
REMARK 1 TITL 3 IMMUNODEFICIENCY VIRUS 1.
REMARK 1 REF BIOCHEMISTRY V. 38 9600 1999
REMARK 1 REFN ISSN 0006-2960
REMARK 1 DOI 10.1021/BI9905258
REMARK 2
REMARK 2 RESOLUTION. NOT APPLICABLE.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : XWINNMR VERSION 3.0, X-PLOR VERSION 3.851
REMARK 3 AUTHORS : BRUKER (XWINNMR), BRUNGER (X-PLOR)
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: THE STRUCTURE HAS BEEN CALCULATED USING
REMARK 3 339 NOE DERIVED DISTANCE RESTRAINTS.
REMARK 4
REMARK 4 1Q3Z COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-AUG-03.
REMARK 100 THE DEPOSITION ID IS D_1000019886.
REMARK 210
REMARK 210 EXPERIMENTAL DETAILS
REMARK 210 EXPERIMENT TYPE : NMR
REMARK 210 TEMPERATURE (KELVIN) : 278; 293
REMARK 210 PH : 6.6; 6.6
REMARK 210 IONIC STRENGTH : 6 MM ZNSO4; 6 MM ZNSO4
REMARK 210 PRESSURE : AMBIENT; AMBIENT
REMARK 210 SAMPLE CONTENTS : 2 MM HIS28(12-53)NCP7 90% H2O,
REMARK 210 10% D2O WITH 3 EQUIVALENTS OF
REMARK 210 ZINC; 2 MM HIS28(12-53)NCP7 100%
REMARK 210 D2O WITH 3 EQUIVALENTS OF ZINC
REMARK 210
REMARK 210 NMR EXPERIMENTS CONDUCTED : 2D TOCSY; 2D NOESY; 1H-15N HSQC
REMARK 210 SPECTROMETER FIELD STRENGTH : 600 MHZ
REMARK 210 SPECTROMETER MODEL : AMX
REMARK 210 SPECTROMETER MANUFACTURER : BRUKER
REMARK 210
REMARK 210 STRUCTURE DETERMINATION.
REMARK 210 SOFTWARE USED : XWINNMR VERSION 3.0, FELIX
REMARK 210 VERSION 98.0
REMARK 210 METHOD USED : DISTANCE GEOMETRY, SIMULATED
REMARK 210 ANNEALING AND MOLECULAR DYNAMICS
REMARK 210
REMARK 210 CONFORMERS, NUMBER CALCULATED : 100
REMARK 210 CONFORMERS, NUMBER SUBMITTED : 1
REMARK 210 CONFORMERS, SELECTION CRITERIA : STRUCTURES WITH ACCEPTABLE
REMARK 210 COVALENT GEOMETRY,STRUCTURES
REMARK 210 WITH FAVORABLE NON-BOND ENERGY,
REMARK 210 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 : 1
REMARK 210
REMARK 210 REMARK: THE STRUCTURE WAS DETERMINED
REMARK 210 USING STANDARD 2D HOMONUCLEAR
REMARK 210 EXPERIMENTS AND 1H-15N HSQC
REMARK 210 EXPERIMENTS.
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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 465 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465 RES C SSSEQI
REMARK 465 ASN A 12
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 PHE A 16 -55.91 74.34
REMARK 500 ASN A 17 -40.01 -158.45
REMARK 500 THR A 24 99.83 51.54
REMARK 500 ARG A 26 -52.98 -151.11
REMARK 500 LYS A 33 158.80 68.27
REMARK 500 TRP A 37 19.60 54.51
REMARK 500 LYS A 38 -38.74 -172.57
REMARK 500 GLN A 45 -150.59 -108.48
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 26 0.27 SIDE CHAIN
REMARK 500 ARG A 29 0.25 SIDE CHAIN
REMARK 500 ARG A 32 0.27 SIDE CHAIN
REMARK 500 ARG A 52 0.29 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 1 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 15 SG
REMARK 620 2 CYS A 18 SG 118.8
REMARK 620 3 HIS A 23 ND1 106.3 127.0
REMARK 620 4 HIS A 28 NE2 79.4 91.3 70.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 2 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 36 SG
REMARK 620 2 CYS A 39 SG 119.6
REMARK 620 3 HIS A 44 NE2 88.6 113.1
REMARK 620 4 CYS A 49 SG 107.6 111.7 114.5
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 1
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 2
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 1ESK RELATED DB: PDB
REMARK 900 WILD TYPE SEQUENCE OF THE SAME PROTEIN
REMARK 900 RELATED ID: 1Q3Y RELATED DB: PDB
REMARK 900 NMR STRUCTURE OF THE CYS28HIS MUTANT (D FORM) OF THE NUCLEOCAPSID
REMARK 900 PROTEIN NCP7 OF HIV-1.
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 THE SEQUENCE HERE CORRESPONDS TO A STRAIN DIFFERENT
REMARK 999 THAN THAT FOUND IN THE SEQUENCE DATABASE (GENBANK ACCESSION
REMARK 999 CAB98186).
DBREF 1Q3Z A 12 53 UNP Q9PY17 Q9PY17_9HIV1 390 431
SEQADV 1Q3Z VAL A 13 UNP Q9PY17 ILE 391 SEE REMARK 999
SEQADV 1Q3Z HIS A 28 UNP Q9PY17 CYS 406 ENGINEERED MUTATION
SEQRES 1 A 42 ASN VAL LYS CYS PHE ASN CYS GLY LYS GLU GLY HIS THR
SEQRES 2 A 42 ALA ARG ASN HIS ARG ALA PRO ARG LYS LYS GLY CYS TRP
SEQRES 3 A 42 LYS CYS GLY LYS GLU GLY HIS GLN MET LYS ASP CYS THR
SEQRES 4 A 42 GLU ARG GLN
HET ZN A 1 1
HET ZN A 2 1
HETNAM ZN ZINC ION
FORMUL 2 ZN 2(ZN 2+)
LINK ZN ZN A 1 SG CYS A 15 1555 1555 2.56
LINK ZN ZN A 1 SG CYS A 18 1555 1555 2.54
LINK ZN ZN A 1 ND1 HIS A 23 1555 1555 2.24
LINK ZN ZN A 1 NE2 HIS A 28 1555 1555 2.35
LINK ZN ZN A 2 SG CYS A 36 1555 1555 2.62
LINK ZN ZN A 2 SG CYS A 39 1555 1555 2.63
LINK ZN ZN A 2 NE2 HIS A 44 1555 1555 2.40
LINK ZN ZN A 2 SG CYS A 49 1555 1555 2.61
SITE 1 AC1 5 CYS A 15 CYS A 18 LYS A 20 HIS A 23
SITE 2 AC1 5 HIS A 28
SITE 1 AC2 5 CYS A 36 CYS A 39 LYS A 41 HIS A 44
SITE 2 AC2 5 CYS A 49
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 - 27 202 Bytes