BMRB Entry 6559

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6559
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Structure of the FBP11WW1 domain complexed to the peptide APPTPPPLPP
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
Formin, polymer, 10 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
Formin: APPTPPPLPP

Data typeCount
1H chemical shifts483
13C chemical shifts122
15N chemical shifts42

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Formin-binding protein 31
2Formin2

Entities:

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

1   GLYSERARGARGALASERVALGLYSERALA
2   LYSSERMETTRPTHRGLUHISLYSSERPRO
3   ASPGLYARGTHRTYRTYRTYRASNTHRGLU
4   THRLYSGLNSERTHRTRPGLULYSPROASP
5   ASP

Entity 2, Formin 10 residues - Formula weight is not available

1   ALAPROPROTHRPROPROPROLEUPROPRO

Samples:

sample_1: Formin-binding protein 3, [U-15N; U-13C], 1.8 mM; Formin 3.6 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; Formin 3.6 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; Formin 3.6 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; Formin 3.6 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:

SWISS-PROT O75400
REF XP_001926823 XP_001916024 XP_001508338 XP_001365548 NP_060362
GenBank AAH11788 AAC27506 AAC27502 AAC27501 AAB93495
DBJ BAB15016
PDB
BMRB 6721 6719 6558

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