BMRB Entry 15453

Title:
FBP28WW2 domain in complex with the PPLIPPPP peptide
Deposition date:
2007-09-01
Original release date:
2008-06-25
Authors:
Ramirez-Espain, Ximena; Ruiz, Lidia; Martin-Malpartida, Pau; Oschkinat, Hartmut; Macias, Maria
Citation:

Citation: Ramirez-Espain, Ximena; Ruiz, Lidia; Martin-Malpartida, Pau; Oschkinat, Hartmut; Macias, Maria. "Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains"  J. Mol. Biol. 373, 1255-1268 (2007).
PubMed: 17915251

Assembly members:

Assembly members:
FBP28WW2, polymer, 37 residues, 5237.882 Da.
ligand, polymer, 9 residues, 5237.882 Da.

Natural source:

Natural source:   Common Name: Mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: petm30

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FBP28WW2: GATAVSEWTEYKTADGKTYY YNNRTLESTWEKPQELK
ligand: GPPLIPPPP

Data sets:
Data typeCount
1H chemical shifts281

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FBP28WW21
2ligand2

Entities:

Entity 1, FBP28WW2 37 residues - 5237.882 Da.

1   GLYALATHRALAVALSERGLUTRPTHRGLU
2   TYRLYSTHRALAASPGLYLYSTHRTYRTYR
3   TYRASNASNARGTHRLEUGLUSERTHRTRP
4   GLULYSPROGLNGLULEULYS

Entity 2, ligand 9 residues - 5237.882 Da.

1   GLYPROPROLEUILEPROPROPROPRO

Samples:

sample_1: FBP28WW2 1 mM; ligand 1 mM; sodium phosphate 100 mM; sodium chloride 50 mM

sample_2: FBP28WW2 1 mM; ligand 1 mM; sodium phosphate 100 mM; sodium chloride 50 mM

sample_3: FBP28WW2, [U-100% 15N], 1 mM; ligand, [U-100% 15N], 1 mM; sodium phosphate 100 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.100 M; pH: 5.8; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1

Software:

UXNMR, Bruker Biospin - collection

ARIA, Linge, O'Donoghue and Nilges - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ProcheckNMR, Laskowski and MacArthur - data validation

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 11007 11008 25309 25310 25311 25678 25679 25680 25681 25682 25683 4714
PDB
GB AAC52477 EGW05321 EHB12574 ELW66441 EMP40899
REF XP_004697122 XP_006977759 XP_007653449 XP_008253407 XP_008926141
AlphaFold Q05859