BMRB Entry 6558

Title:
Structure of the FBP11WW1 domain
Deposition date:
2005-03-18
Original release date:
2005-08-22
Authors:
Pires, J.; Parthier, C.; Aido-Machado, R.; Wiedemann, U.; Otte, L.; Boehm, G.; Rudolph, R.; Oschkinat, H.
Citation:

Citation: Pires, J.; Parthier, C.; Aido-Machado, R.; Wiedemann, U.; Otte, L.; Boehm, G.; Rudolph, R.; Oschkinat, H.. "Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain"  J. Mol. Biol. 348, 399-408 (2005).
PubMed: 15811376

Assembly members:

Assembly members:
Formin-binding protein 3, polymer, 41 residues, Formula weight is not available

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Formin-binding protein 3: GSRRASVGSAKSMWTEHKSP DGRTYYYNTETKQSTWEKPD D

Data sets:
Data typeCount
1H chemical shifts395
13C chemical shifts129
15N chemical shifts44

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Formin-binding protein 31

Entities:

Entity 1, Formin-binding protein 3 41 residues - Formula weight is not available

1   GLYSERARGARGALASERVALGLYSERALA
2   LYSSERMETTRPTHRGLUHISLYSSERPRO
3   ASPGLYARGTHRTYRTYRTYRASNTHRGLU
4   THRLYSGLNSERTHRTRPGLULYSPROASP
5   ASP

Samples:

sample_1: Formin-binding protein 3, [U-15N; U-13C], 1.8 mM; phosphate buffer 10 mM; Nacl 100 mM; DTT 0.1 mM; EDTA 0.1 mM; H2O 90%; D2O 10%

sample_2: Formin-binding protein 3, [U-15N; U-13C], 1.8 mM; phosphate buffer 10 mM; Nacl 100 mM; DTT 0.1 mM; EDTA 0.1 mM; D2O 100%

sample_3: Formin-binding protein 3, [U-15N], 1.8 mM; phosphate buffer 10 mM; Nacl 100 mM; DTT 0.1 mM; EDTA 0.1 mM; H2O 90%; D2O 10%

sample_4: Formin-binding protein 3 1.8 mM; phosphate buffer 10 mM; Nacl 100 mM; DTT 0.1 mM; EDTA 0.1 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.0; temperature: 298 K; ionic strength: 100 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
triple-resonancenot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available
3D 15N-separated NOESYnot availablenot availablenot available
2D NOESYnot availablenot availablenot available
2D TOCSYnot availablenot availablenot available

Software:

CNS v1.1 - refinement

XWINNMR v3.2 - collection, processing

Sparky v3.1 - data analysis

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 6721
PDB
DBJ BAB15016
GB AAB93495 AAC27501 AAC27502 AAC27506 AAH11788
REF NP_001231502 NP_060362 XP_001916024 XP_002685399 XP_002749482
SP O75400
TPG DAA32724
AlphaFold O75400

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