BMRB Entry 16771

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16771
MolProbity Validation Chart

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Title:
Integrin beta3 subunit in a disulfide linked alphaIIb-beta3 cytosolic domain
Deposition date:
2010-03-10
Original release date:
2011-05-19
Authors:
Metcalf, Douglas; Kielec, Joseph; Valentine, Kathleen; Wand, A Joshua; Bennett, Joel; William, DeGrado; Moore, David; Molnar, Kathleen
Citation:

Citation: Metcalf, Douglas; Moore, David; Wu, Yibing; Kielec, Joseph; Molnar, Kathleen; Valentine, Kathleen; Wand, A. Joshua; Bennett, Joel; DeGrado, William. "NMR analysis of the alphaIIb beta3 cytoplasmic interaction suggests a mechanism for integrin regulation."  Proc. Natl. Acad. Sci. U.S.A. 107, 22481-22486 (2010).
PubMed: 21156831

Assembly members:

Assembly members:
alphaIIb, polymer, 25 residues, 2994.3 Da.
beta3, polymer, 75 residues, 8699.9 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-16b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
alphaIIb: SPECWKVGFFKRNRPPLEED DEEGE
beta3: MGSSHHHHHHSSGLVPRGSH MSPECLIWKLLITIHDRKEF AKFEEERARAKWDTANNPLY KEATSTFTNITYRGT

Data sets:
Data typeCount
13C chemical shifts231
15N chemical shifts62
1H chemical shifts379

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alphaIIb1
2beta32

Entities:

Entity 1, alphaIIb 25 residues - 2994.3 Da.

1   SERPROGLUCYSTRPLYSVALGLYPHEPHE
2   LYSARGASNARGPROPROLEUGLUGLUASP
3   ASPGLUGLUGLYGLU

Entity 2, beta3 75 residues - 8699.9 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METSERPROGLUCYSLEUILETRPLYSLEU
4   LEUILETHRILEHISASPARGLYSGLUPHE
5   ALALYSPHEGLUGLUGLUARGALAARGALA
6   LYSTRPASPTHRALAASNASNPROLEUTYR
7   LYSGLUALATHRSERTHRPHETHRASNILE
8   THRTYRARGGLYTHR

Samples:

sample_1: sodium phosphate 5 mM; DPC, [U-99% 2H], 100 mM; sodium azide 0.02%; TFA 25 mM; entity_beta3, [U-99% 13C; U-99% 15N], 1 mM; entity_alphaIIb 1 mM; H2O 90%; D2O 10%

sample_2: sodium phosphate 5 mM; DPC, [U-99% 2H], 100 mM; sodium azide 0.02%; TFA 25 mM; entity_beta3, [U-10% 13C; U-99% 15N], 1 mM; entity_alphaIIb 1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
4D (13C)HSQC-NOESY-(13C)HSQCsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

FELIX, Accelrys Software Inc. - processing

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAG37735 BAI46167 BAE34283 BAJ17755
EMBL CAA29987 CAD29521
GB AAA52597 AAA53150 AAA60114 AAA65936 AAI17444 AAA35927 AAA52589 AAA52600 AAA60122 AAB27096
REF NP_000410 NP_001014929 NP_001075262 XP_001114526 XP_001150497 NP_000203 NP_001003162 NP_001075271 NP_001075535 NP_001193419
SP P08514 P53711 O54890 P05106
TPG DAA18359 DAA18403
BMRB 15552 16496
AlphaFold P08514 P53711 O54890 P05106

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