BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17922

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17922

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Title: Backbone 1H, 13C, 15N assignment of HIV-1 accessory protein Nef   PubMed: 21365684

Deposition date: 2011-09-06 Original release date: 2012-09-20

Authors: Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Gronenborn, Angela

Citation: Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Gronenborn, Angela. "Structure, dynamics, and Hck interaction of full-length HIV-1 Nef."  Proteins 79, 1609-1622 (2011).

Assembly members:
Nef, polymer, 217 residues, Formula weight is not available

Natural source:   Common Name: HIV-1   Taxonomy ID: 11676   Superkingdom: Viruses   Kingdom: not available   Genus/species: Lentivirus HIV-1

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Nef: MEGKWSKRSVSGWPAVRERM RRAEPAAEGVGAVSRDLEKH GAITSSNTAATNAACAWLEA QEEEEVGFPVRPQVPLRPMT YKAAVDLSHFLKEKGGLEGL IYSQKRQDILDLWVYHTQGY FPDWQNYTPGPGIRYPLTFG WCFKLVPVEPEKVEEANEGE NNCLLHPMSQHGMDDPEKEV LVWKFDSKLAFHHMARELHP EYYKDCAAALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts509
15N chemical shifts150
1H chemical shifts159

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nef1

Entities:

Entity 1, Nef 217 residues - Formula weight is not available

1   METGLUGLYLYSTRPSERLYSARGSERVAL
2   SERGLYTRPPROALAVALARGGLUARGMET
3   ARGARGALAGLUPROALAALAGLUGLYVAL
4   GLYALAVALSERARGASPLEUGLULYSHIS
5   GLYALAILETHRSERSERASNTHRALAALA
6   THRASNALAALACYSALATRPLEUGLUALA
7   GLNGLUGLUGLUGLUVALGLYPHEPROVAL
8   ARGPROGLNVALPROLEUARGPROMETTHR
9   TYRLYSALAALAVALASPLEUSERHISPHE
10   LEULYSGLULYSGLYGLYLEUGLUGLYLEU
11   ILETYRSERGLNLYSARGGLNASPILELEU
12   ASPLEUTRPVALTYRHISTHRGLNGLYTYR
13   PHEPROASPTRPGLNASNTYRTHRPROGLY
14   PROGLYILEARGTYRPROLEUTHRPHEGLY
15   TRPCYSPHELYSLEUVALPROVALGLUPRO
16   GLULYSVALGLUGLUALAASNGLUGLYGLU
17   ASNASNCYSLEULEUHISPROMETSERGLN
18   HISGLYMETASPASPPROGLULYSGLUVAL
19   LEUVALTRPLYSPHEASPSERLYSLEUALA
20   PHEHISHISMETALAARGGLULEUHISPRO
21   GLUTYRTYRLYSASPCYSALAALAALALEU
22   GLUHISHISHISHISHISHIS

Samples:

sample_1: Nef, [U-13C; U-15N; U-2H], 0.1 mM; H2O 95%; D2O 5%; DTT 10 mM; HEPES 10 mM; sodium chloride 100 mM; sodium azide 0.02 w/v

sample_conditions_1: ionic strength: 0.1 M; pH: 8.0; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection

CARA v1.8.4, Rochus Keller - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

GB AAA03700

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts