BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26822

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments of Human integrin alpha1 I domain mutant E317A   PubMed: 27342747

Deposition date: 2016-06-20 Original release date: 2016-08-31

Authors: Nunes, Ana Monica; Zhu, Jie; Jezioro, Jacqueline; Minetti, Conceicao; Remeta, David; Farndale, Richard; Hamaia, Samir; Baum, Jean

Citation: Nunes, Ana Monica; Zhu, Jie; Jezioro, Jacqueline; Minetti, Conceicao; Remeta, David; Farndale, Richard; Hamaia, Samir; Baum, Jean. "Intrinsic local destabilization of the C-terminus predisposes integrin alpha1 I domain to a conformational switch induced by collagen binding"  Protein Sci. 25, 1672-1681 (2016).

Assembly members:
integrin_alpha1_I_domain_mutant_E317A, polymer, 216 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):
integrin_alpha1_I_domain_mutant_E317A: MNHHHHHHHHHHTSLYKKAG FTQLDIVIVLDGSNSIYPWD SVTAFLNDLLERMDIGPKQT QVGIVQYGENVTHEFNLNKY SSTEEVLVAAKKIVQRGGRQ TMTALGIDTARKEAFTEARG ARRGVKKVMVIVTDGESHDN HRLKKVIQDCEDENIQRFSI AILGSYNRGNLSTEKFVEEI KSIASEPTEKHFFNVSDALA LVTIVKTLGERIFALE

Data sets:
Data typeCount
13C chemical shifts475
15N chemical shifts166
1H chemical shifts166

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1a1I_E317A1

Entities:

Entity 1, a1I_E317A 216 residues - Formula weight is not available

1   METASNHISHISHISHISHISHISHISHIS
2   HISHISTHRSERLEUTYRLYSLYSALAGLY
3   PHETHRGLNLEUASPILEVALILEVALLEU
4   ASPGLYSERASNSERILETYRPROTRPASP
5   SERVALTHRALAPHELEUASNASPLEULEU
6   GLUARGMETASPILEGLYPROLYSGLNTHR
7   GLNVALGLYILEVALGLNTYRGLYGLUASN
8   VALTHRHISGLUPHEASNLEUASNLYSTYR
9   SERSERTHRGLUGLUVALLEUVALALAALA
10   LYSLYSILEVALGLNARGGLYGLYARGGLN
11   THRMETTHRALALEUGLYILEASPTHRALA
12   ARGLYSGLUALAPHETHRGLUALAARGGLY
13   ALAARGARGGLYVALLYSLYSVALMETVAL
14   ILEVALTHRASPGLYGLUSERHISASPASN
15   HISARGLEULYSLYSVALILEGLNASPCYS
16   GLUASPGLUASNILEGLNARGPHESERILE
17   ALAILELEUGLYSERTYRASNARGGLYASN
18   LEUSERTHRGLULYSPHEVALGLUGLUILE
19   LYSSERILEALASERGLUPROTHRGLULYS
20   HISPHEPHEASNVALSERASPALALEUALA
21   LEUVALTHRILEVALLYSTHRLEUGLYGLU
22   ARGILEPHEALALEUGLU

Samples:

sample_1: integrin alpha1 I domain mutant E317A, [U-99% 13C; U-99% 15N], 0.45 mM; potassium phosphate 50 mM; sodium chloride 140 mM; Magnesium chloride 5 mM; 2-Mercaptoethanol 20 mM; H2O 95%; D2O, [U-99% 2H], 5%

sample_conditions_1: ionic strength: 0.46 M; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D HCACOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance III 700 MHz

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