BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 11008

Title: FBP28WW2 domain in complex with a PPPLIPPPP peptide   PubMed: 17915251

Deposition date: 2007-09-06 Original release date: 2008-06-25

Authors: Ramirez-Espain, Ximena; Ruiz, Lidia; Martin-Malpartida, Pau; Oschkinat, Hartmut; Macias, Maria

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).

Assembly members:
FBP28WW2, polymer, 37 residues, 4365.766 Da.
PPPLIPPPP, polymer, 9 residues, 931.203 Da.

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

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

Entity Sequences (FASTA):
FBP28WW2: GATAVSEWTEYKTADGKTYY YNNRTLESTWEKPQELK
PPPLIPPPP: PPPLIPPPP

Data sets:
Data typeCount
1H chemical shifts284

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FBP28WW21
2PPPLIPPPP2

Entities:

Entity 1, FBP28WW2 37 residues - 4365.766 Da.

1   GLYALATHRALAVALSERGLUTRPTHRGLU
2   TYRLYSTHRALAASPGLYLYSTHRTYRTYR
3   TYRASNASNARGTHRLEUGLUSERTHRTRP
4   GLULYSPROGLNGLULEULYS

Entity 2, PPPLIPPPP 9 residues - 931.203 Da.

1   PROPROPROLEUILEPROPROPROPRO

Samples:

sample_1: FPB28WW2 1 mM; PPPLIPPPP 3 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_2: FPB28WW2 1 mM; PPPLIPPPP 3 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_3: FPB28WW2, [U-100% 15N], 1 mM; PPPLIPPPP 3 mM; sodium phosphate 50 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 150 mM; 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 NOESYsample_2isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

XEASY, Keller and Wuthrich - chemical shift assignment

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

ProcheckNMR, Laskowski and MacArthur - structure validation

ARIA, Linge, O, . - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure display

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 11007 15453 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