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Biological Magnetic Resonance Data Bank


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BMRB Entry 17740

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17740

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Title: Backbone 1H, 13C, 15N assignment of Hck kinase regulatory segment   PubMed: 21365684

Deposition date: 2011-06-28 Original release date: 2011-09-01

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:
Hck32L, polymer, 193 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
Hck32L: GIREAGSEDIIVVALYDYEA IHHEDLSFQKGDQMVVLEES GEWWKARSLATRKEGYIPSN YVARVDSLETEEWFFKGISR KDAERQLLAPGNMLGSFMIR DSETTKGSYSLSVRDYDPRQ GDTVKHYKIRTLDNGGFYIS PRSTFSTLQELVDHYKKGND GLCQKLSVPCMSSKPQKPWE KDAWELEHHHHHH

Data sets:
Data typeCount
13C chemical shifts482
15N chemical shifts170
1H chemical shifts170

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Hck32L1

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

Samples:

sample_1: Hck32L, [U-13C; U-15N; U-2H], 0.3 mM; H2O 95%; D2O 5%; DTT 10 mM; HEPES 10 mM; sodium chloride 100 mM; sodium azide 0.02 w/v

sample_2: Hck32L, [U-13C; U-15N; U-2H], 0.6 mM; H2O 95%; D2O 5%; DTT 10 mM; HEPES 10 mM; sodium chloride 50 mM; sodium azide 0.02 w/v; glutamate 50 mM; arginine 50 mM

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

sample_conditions_2: ionic strength: 0.1 M; pH: 7.2; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_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 600 MHz

Related Database Links:

BMRB 17819
PDB
DBJ BAB15482 BAF82585 BAF83617 BAG60878
EMBL CAC44031
GB AAA52643 AAA52644 AAH14435 AAH94847 AAI08931
REF NP_001165600 NP_001165601 NP_001165602 NP_001165603 NP_001165604
SP P08631 Q95M30

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