BMRB Entry 15479

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15479

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Title:
1H, 13C and 15N Resonance Assignment for the transmembrane and cytoplasmic domains of human CD4
Deposition date:
2007-09-19
Original release date:
2008-06-25
Authors:
Wittlich, Marc; Koenig, Bernd; Hoffmann, Silke; Willbold, Dieter
Citation:

Citation: Wittlich, Marc; Koenig, Bernd; Hoffmann, Silke; Willbold, Dieter. "Structural characterization of the transmembrane and cytoplasmic domains of human CD4."  Biochim. Biophys. Acta 1768, 2949-2960 (2007).
PubMed: 18035040

Assembly members:

Assembly members:
CD4_coreceptor_polypeptide, polymer, 70 residues, 7850.4 Da.

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: pTKK19xb/ub

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CD4_coreceptor_polypeptide: GPLVPRGSMALIVLGGVAGL LLFIGLGIFFSVRSRHRRRQ AERMSQIKRLLSEKKTSQSP HRFQKTHSPI

Data sets:
Data typeCount
13C chemical shifts329
15N chemical shifts68
1H chemical shifts529

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1CD4mut1

Entities:

Entity 1, CD4mut 70 residues - 7850.4 Da.

Residues 1-8 proteolytic left-over, human CD4(372-433) C394S/C397S/C420S/C422S/C430H

1   GLYPROLEUVALPROARGGLYSERMETALA
2   LEUILEVALLEUGLYGLYVALALAGLYLEU
3   LEULEUPHEILEGLYLEUGLYILEPHEPHE
4   SERVALARGSERARGHISARGARGARGGLN
5   ALAGLUARGMETSERGLNILELYSARGLEU
6   LEUSERGLULYSLYSTHRSERGLNSERPRO
7   HISARGPHEGLNLYSTHRHISSERPROILE

Samples:

sample_1: CD4 coreceptor polypeptide, [U-100% 13C; U-100% 15N], 0.5-1 mM; DPC, [U-100% 2H], 200 mM; sodium chloride 150 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 150 mM; pH: 6.2; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

CARA v1.8.4a.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Keller and Wuthrich - chemical shift assignment, data analysis, processing

NMR spectrometers:

  • Varian INOVA 800 MHz
  • Varian INOVA 600 MHz

Related Database Links:

BMRB 16853
PDB

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