BMRB Entry 17819

Title:
Backbone 1H, 13C, 15N assignment of Hck kinase regulatory segment complex with full length Nef
Deposition date:
2011-07-29
Original release date:
2014-04-23
Authors:
Jung, Jinwon; Byeon, In-Ja; Ahn, Jinwoo; Gronenborn, Angela
Citation:

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).
PubMed: 21365684

Assembly members:

Assembly members:
Hck32L, polymer, 193 residues, Formula weight is not available
Nef, polymer, 217 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Data sets:
Data typeCount
13C chemical shifts259
15N chemical shifts146
1H chemical shifts146

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hck32L1
2Nef2

Entities:

Entity 1, Hck32L 193 residues - Formula weight is not available

This construct is 72-256 of Hck kinase. Last 8 residues (LEHHHHHH) are a histag.

1   GLYILEARGGLUALAGLYSERGLUASPILE
2   ILEVALVALALALEUTYRASPTYRGLUALA
3   ILEHISHISGLUASPLEUSERPHEGLNLYS
4   GLYASPGLNMETVALVALLEUGLUGLUSER
5   GLYGLUTRPTRPLYSALAARGSERLEUALA
6   THRARGLYSGLUGLYTYRILEPROSERASN
7   TYRVALALAARGVALASPSERLEUGLUTHR
8   GLUGLUTRPPHEPHELYSGLYILESERARG
9   LYSASPALAGLUARGGLNLEULEUALAPRO
10   GLYASNMETLEUGLYSERPHEMETILEARG
11   ASPSERGLUTHRTHRLYSGLYSERTYRSER
12   LEUSERVALARGASPTYRASPPROARGGLN
13   GLYASPTHRVALLYSHISTYRLYSILEARG
14   THRLEUASPASNGLYGLYPHETYRILESER
15   PROARGSERTHRPHESERTHRLEUGLNGLU
16   LEUVALASPHISTYRLYSLYSGLYASNASP
17   GLYLEUCYSGLNLYSLEUSERVALPROCYS
18   METSERSERLYSPROGLNLYSPROTRPGLU
19   LYSASPALATRPGLULEUGLUHISHISHIS
20   HISHISHIS

Entity 2, 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: Hck32L, [U-13C; U-15N; U-2H], 0.5 mM; H2O 95%; D2O 5%; DTT 10 mM; HEPES 10 mM; sodium chloride 100 mM; sodium azide 0.02 w/v; Nef 0.6 mM

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

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

Related Database Links:

UNP P08631
BMRB 17740 17922
PDB
DBJ BAB15482 BAF82585 BAF83617 BAG60878
EMBL CAC44031
GB AAA52643 AAA52644 AAH14435 AAH94847 AAI08931 AAA03700
REF NP_001165600 NP_001165601 NP_001165602 NP_001165603 NP_001165604
SP P08631 Q95M30
AlphaFold Q9UMJ5 Q95M30 P08631

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks