BMRB Entry 15760

Title:
Solution structure of a cytoskeletal protein complex
Deposition date:
2008-05-06
Original release date:
2008-11-12
Authors:
Wang, Xiaoxia; Fukuda, Koichi; Byeon, In-Ja; Velyvis, Algirdas; Wu, Chuanyue; Gronenborn, Angela; Qin, Jun
Citation:

Citation: Wang, Xiaoxia; Fukuda, Koichi; Byeon, In-Ja; Velyvis, Algirdas; Wu, Chuanyue; Gronenborn, Angela; Qin, Jun. "The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly"  J. Biol. Chem. 283, 21113-21119 (2008).
PubMed: 18508764

Assembly members:

Assembly members:
alpha-parvin, polymer, 129 residues, 15011.396 Da.
LD1, polymer, 10 residues, 1087.189 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: pET3a

Data sets:
Data typeCount
13C chemical shifts500
15N chemical shifts139
1H chemical shifts1046

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1alpha-parvin1
2LD12

Entities:

Entity 1, alpha-parvin 129 residues - 15011.396 Da.

1   ARGHISGLUARGASPALAPHEASPTHRLEU
2   PHEASPHISALAPROASPLYSLEUASNVAL
3   VALLYSLYSTHRLEUILETHRPHEVALASN
4   LYSHISLEUASNLYSLEUASNLEUGLUVAL
5   THRGLULEUGLUTHRGLNPHEALAASPGLY
6   VALTYRLEUVALLEULEUMETGLYLEULEU
7   GLUGLYTYRPHEVALPROLEUHISSERPHE
8   PHELEUTHRPROASPSERPHEGLUGLNLYS
9   VALLEUASNVALSERPHEALAPHEGLULEU
10   METGLNASPGLYGLYLEUGLULYSPROLYS
11   PROARGPROGLUASPILEVALASNCYSASP
12   LEULYSSERTHRLEUARGVALLEUTYRASN
13   LEUPHETHRLYSTYRARGASNVALGLU

Entity 2, LD1 10 residues - 1087.189 Da.

1   ASPLEUASPALALEULEUALAASPLEUGLU

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.25 mM; entity_2, [U-13C; U-15N], 0.25 mM

sample_conditions_1: ionic strength: 130 mM; pH: 7.2; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Brunger - refinement, structure solution

NMR spectrometers:

  • Bruker N/A 600 MHz

Related Database Links:

BMRB 15899
PDB
DBJ BAA91815 BAA97981 BAC36771 BAE28686 BAG73514
GB AAG09802 AAG09803 AAG27173 AAG27175 AAH14535
REF NP_001092614 NP_060692 NP_065631 NP_065707 XP_001091788
SP Q9EPC1 Q9HB97 Q9NVD7
TPG DAA22326
AlphaFold Q9NVD7 Q9EPC1 Q9HB97

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