BMRB Entry 25176

Title:
The structure of Filamin repeat 21 bound to integrin
Deposition date:
2014-08-28
Original release date:
2015-03-20
Authors:
Liu, Jianmin; Qin, Jun
Citation:

Citation: Liu, Jianmin; Das, Mitali; Yang, Jun; Ithychanda, Sujay; Yakubenko, Valentin; Plow, Edward; Qin, Jun. "Structural mechanism of integrin inactivation by filamin"  Nat. Struct. Mol. Biol. ., .-. (2015).

Assembly members:

Assembly members:
entity_1, polymer, 95 residues, 9762.817 Da.
entity_2, polymer, 21 residues, 2581.817 Da.
entity_3, polymer, 47 residues, 5618.380 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: pGST parallel

Data sets:
Data typeCount
1H chemical shifts897
13C chemical shifts400
15N chemical shifts133

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22
3entity_33

Entities:

Entity 1, entity_1 95 residues - 9762.817 Da.

1   GLYGLYALAHISLYSVALARGALAGLYGLY
2   PROGLYLEUGLUARGALAGLUALAGLYVAL
3   PROALAGLUPHESERILETRPTHRARGGLU
4   ALAGLYALAGLYGLYLEUALAILEALAVAL
5   GLUGLYPROSERLYSALAGLUILESERPHE
6   GLUASPARGLYSASPGLYSERCYSGLYVAL
7   ALATYRVALVALGLNGLUPROGLYASPTYR
8   GLUVALSERVALLYSPHEASNGLUGLUHIS
9   ILEPROASPSERPROPHEVALVALPROVAL
10   ALASERPROSERGLY

Entity 2, entity_2 21 residues - 2581.817 Da.

1   TRPLYSVALGLYPHEPHELYSARGASNARG
2   PROPROLEUGLUGLUASPASPGLUGLUGLY
3   GLU

Entity 3, entity_3 47 residues - 5618.380 Da.

1   LYSLYSLYSILETHRILEHISASPARGLYS
2   GLUPHEALALYSPHEGLUGLUGLUARGALA
3   ARGALALYSTRPASPTHRALAASNASNPRO
4   LEUTYRLYSGLUALATHRSERTHRPHETHR
5   ASNILETHRTYRARGGLYTHR

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N; U-80% 2H], 1 mM; entity_2, [U-100% 13C; U-100% 15N; U-80% 2H], mM; entity_3, [U-100% 13C; U-100% 15N; U-80% 2H], mM; H2O 90%; D2O 10%

sample_conditions_1: temperature: 298 K; pH: 6.4; pressure: 1 atm; ionic strength: 25 mM

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
REF XP_010831141
AlphaFold Q17R67 Q16499

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