BMRB Entry 26624

Title:
integrin beta1 transmembrane and cytoplasmic domain
Deposition date:
2015-08-02
Original release date:
2017-03-03
Authors:
Lu, Zhenwei
Citation:

Citation: Lu, Zhenwei; Mathew, Sijo; Chen, Jiang; Hadziselimovic, Arina; Palamuttam, Riya; Hudson, Billy; Fassler, Reinhard; Pozzi, Ambra; Sanders, Charles; Zent, Roy. "Implications of the differing roles of the beta1 and beta3 transmembrane and cytoplasmic domains for integrin function"  Elife 5, e18633-e18633 (2016).
PubMed: 27929375

Assembly members:

Assembly members:
integrin_beta1_C723S_TM-CT, polymer, 90 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet16b

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts188
15N chemical shifts68
1H chemical shifts68

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1integrin beta1 TM/CT1

Entities:

Entity 1, integrin beta1 TM/CT 90 residues - Formula weight is not available

Residues 1-10 represent a non-native affinity tag This is the membrane and cytoplasmic domain of integrin beta1

1   METGLYHISHISHISHISHISHISGLYMET
2   GLUASNPROGLUSERPROTHRGLYPROASP
3   ILEILEPROILEVALALAGLYVALVALALA
4   GLYILEVALLEUILEGLYLEUALALEULEU
5   LEUILETRPLYSLEULEUMETILEILEHIS
6   ASPARGARGGLUPHEALALYSPHEGLULYS
7   GLULYSMETASNALALYSTRPASPTHRGLY
8   GLUASNPROILETYRLYSSERALAVALTHR
9   THRVALVALASNPROLYSTYRGLUGLYLYS

Samples:

sample_1: integrin beta1 TM/CT, [U-100% 13C; U-100% 15N], 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 250 mM; pH: 6.5; pressure: 1 atm; temperature: 318 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz

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