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- PDB-2nef: HIV-1 NEF (REGULATORY FACTOR), NMR, 40 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 2nef
TitleHIV-1 NEF (REGULATORY FACTOR), NMR, 40 STRUCTURES
ComponentsNEGATIVE FACTOR (F-PROTEIN)
KeywordsREGULATORY FACTOR / AIDS / MYRISTYLATION / GTP-BINDING
Function / homology
Function and homology information


negative regulation of glycoprotein biosynthetic process / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II / symbiont-mediated suppression of host autophagy / symbiont-mediated suppression of host apoptosis / thioesterase binding / CD4 receptor binding / MHC class I protein binding / host cell Golgi membrane / viral life cycle ...negative regulation of glycoprotein biosynthetic process / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class I / symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC class II / symbiont-mediated suppression of host autophagy / symbiont-mediated suppression of host apoptosis / thioesterase binding / CD4 receptor binding / MHC class I protein binding / host cell Golgi membrane / viral life cycle / regulation of calcium-mediated signaling / SH3 domain binding / virion component / ATPase binding / symbiont-mediated suppression of host innate immune response / signaling receptor binding / protein kinase binding / GTP binding / host cell plasma membrane / extracellular region / membrane
Similarity search - Function
Nef Regulatory Factor / Nef Regulatory Factor / HIV-1 Nef protein, anchor domain superfamily / HIV negative factor Nef / HIV-1 Nef protein, core domain superfamily / Negative factor, (F-Protein) or Nef / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesHuman immunodeficiency virus type 1
MethodSOLUTION NMR
AuthorsGrzesiek, S. / Bax, A. / Clore, G.M. / Gronenborn, A.M. / Hu, J.S. / Kaufman, J. / Palmer, I. / Stahl, S.J. / Tjandra, N. / Wingfield, P.T.
Citation
Journal: Protein Sci. / Year: 1997
Title: Refined solution structure and backbone dynamics of HIV-1 Nef.
Authors: Grzesiek, S. / Bax, A. / Hu, J.S. / Kaufman, J. / Palmer, I. / Stahl, S.J. / Tjandra, N. / Wingfield, P.T.
#1: Journal: Nat.Struct.Biol. / Year: 1996
Title: The Solution Structure of HIV-1 Nef Reveals an Unexpected Fold and Permits Delineation of the Binding Surface for the SH3 Domain of HCK Tyrosine Protein Kinase
Authors: Grzesiek, S. / Bax, A. / Clore, G.M. / Gronenborn, A.M. / Hu, J.S. / Kaufman, J. / Palmer, I. / Stahl, S.J. / Wingfield, P.T.
History
DepositionFeb 12, 1997Processing site: BNL
SupersessionJul 7, 1997ID: 1NEF
Revision 1.0Jul 7, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4May 1, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: NEGATIVE FACTOR (F-PROTEIN)


Theoretical massNumber of molelcules
Total (without water)16,1481
Polymers16,1481
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)40 / -
Representative

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Components

#1: Protein NEGATIVE FACTOR (F-PROTEIN) / HIV-1 NEF


Mass: 16148.163 Da / Num. of mol.: 1 / Mutation: DEL(2-39), DEL(159-173), C206A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus type 1 / Genus: Lentivirus / Species: Human immunodeficiency virus 1 / Strain: BH10 / Gene: HIV-1 NEF / Plasmid: PET11A / Gene (production host): HIV-1 NEF / Production host: Escherichia coli (E. coli) / Strain (production host): DE3 / References: UniProt: Q70627
Sequence detailsTHE MATERIAL USED WAS A DELETION MUTANT: DELTA 2 - 39 AND DELTA 159 - 173, WHICH REMOVES THE ...THE MATERIAL USED WAS A DELETION MUTANT: DELTA 2 - 39 AND DELTA 159 - 173, WHICH REMOVES THE DISORDERED N-TERMINUS AND REDUCES THE SIZE OF A LONG DISORDERED SOLVENT EXPOSED LOOP. IT ALSO CONTAINS A CYS 206 TO ALA MUTATION TO PREVENT THE FORMATION OF INTERMOLECULAR DISULFIDES. THE HIV-1 STRAIN FROM WHICH THE PROTEIN WAS DERIVED IS STRAIN BH10.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR detailsText: THE 3D STRUCTURE OF THE HIV-1 NEF (DELTA2 - 39, DELTA 159 - 173) SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR IS BASED ON 1250 EXPERIMENTAL RESTRAINTS: 338 SEQUENTIAL (|I- ...Text: THE 3D STRUCTURE OF THE HIV-1 NEF (DELTA2 - 39, DELTA 159 - 173) SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR IS BASED ON 1250 EXPERIMENTAL RESTRAINTS: 338 SEQUENTIAL (|I-J|=1), 101 MEDIUM RANGE (1 < |I-J| <=5) AND 245 LONG RANGE (|I-J| >5) INTERRESIDUES AND 70 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 64 DISTANCE RESTRAINTS FOR 32 HYDROGEN BONDS; 157 TORSION ANGLE (78 PHI, 10 PSI, 55 CHI1 AND 14 CHI2) RESTRAINTS; 91 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 184 (93 CALPHA AND 91 CBETA) 13C SHIFT RESTRAINTS.

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Sample preparation

Crystal grow
*PLUS
Method: other / Details: NMR

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
RefinementSoftware ordinal: 1
Details: THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129 - 136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE ...Details: THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129 - 136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99 - 103) AND CARBON CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92 - 96) RESTRAINTS. THE COORDINATES OF THE 40 FINAL SIMULATED ANNEALING STRUCTURES ARE PRESENTED IN THIS ENTRY. THE B FACTOR FIELD PRESENTS THE AVERAGE RMS OF THE 40 INDIVIDUAL STRUCTURES ABOUT THE MEAN COORDINATE POSITIONS OBTAINED BY BEST FITTING RESIDUES 76 - 94, 97 - 102, 106 -147, 181 - 191, AND 194 -199. THESE RESIDUES CORRESPOND TO THE NON-MOBILE CORE OF THE PROTEIN AS EVIDENCED BY 15N RELAXATION DATA.
NMR ensembleConformers submitted total number: 40

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