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 16159

Title: Beta1A Integrin Cytoplasmic Tail 1H and 15N Chemical Shift Assignments   PubMed: 19798053

Deposition date: 2009-02-03 Original release date: 2009-10-07

Authors: Anthis, Nicholas; Wegener, Kate; Campbell, Iain

Citation: Anthis, Nicholas; Wegener, Kate; Ye, Feng; Kim, Chungho; Goult, Benjamin; Lowe, Edward; Vakonakis, Ioannis; Bate, Neil; Critchley, David; Ginsberg, Mark; Campbell, Iain. "The structure of an integrin/talin complex reveals the basis of inside-out signal transduction."  EMBO J. 28, 3623-3632 (2009).

Assembly members:
beta1A_integrin, polymer, 49 residues, 5710 Da.

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):
beta1A_integrin: GPKLLMIIHDRREFAKFEKE KMNAKWDTGENPIYKSAVTT VVNPKYEGK

Data sets:
Data typeCount
15N chemical shifts100
1H chemical shifts347

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1beta1A integrin tail1

Entities:

Entity 1, beta1A integrin tail 49 residues - 5710 Da.

This is the cytoplasmic tail of the beta1A integrin tail. The first two residues (GP) are a cloning artifact.

1   GLYPROLYSLEULEUMETILEILEHISASP
2   ARGARGGLUPHEALALYSPHEGLULYSGLU
3   LYSMETASNALALYSTRPASPTHRGLYGLU
4   ASNPROILETYRLYSSERALAVALTHRTHR
5   VALVALASNPROLYSTYRGLUGLYLYS

Samples:

pH_6.1: D2O, [U-2H], 5%; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 1 mM; DSS 0.1 mM; beta1A integrin, [U-15N], 0.05 mM

pH_5.0: D2O, [U-2H], 5%; sodium acetate 20 mM; sodium azide 0.02%; DSS 0.1 mM; beta1A integrin, [U-15N], 1 mM

sample_conditions_1: pH: 6.1; pressure: 1.0 atm; temperature: 298 K

sample_conditions_2: pH: 5.0; pressure: 1.0 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCpH_6.1isotropicsample_conditions_1
3D 1H-15N NOESYpH_5.0isotropicsample_conditions_2
3D 1H-15N TOCSYpH_5.0isotropicsample_conditions_2
2D 1H-15N HSQCpH_5.0isotropicsample_conditions_2

Software:

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

SPARKY, Goddard - data analysis

Omega Spectrometer Operating Software vBeta 6.0.3b2, GE - collection

ANALYSIS, Boucher and Stevens - chemical shift assignment

NMR spectrometers:

  • GE OMEGA 600 MHz

Related Database Links:

UNP P05556
DBJ BAC39546 BAC40532 BAE39731 BAF84386 BAG72587
EMBL CAA30790 CAA33272 CAA68738 CAD97649 CAF97757
GB AAA48926 AAA49889 AAA49890 AAA59182 AAA74402
PIR PH0104
REF NP_001030143 NP_001030159 NP_001034343 NP_001041625 NP_001081286
SP A5Z1X6 B0FYY4 P05556 P07228 P09055
TPG DAA23553

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