BMRB Entry 11008

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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/BMR11008
MolProbity Validation Chart

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Title:
FBP28WW2 domain in complex with a PPPLIPPPP peptide
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:

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, 4365.766 Da.
PPPLIPPPP, polymer, 9 residues, 931.203 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
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'Donoghue and Nilges - structure solution

Molmol, Koradi, Billeter and Wuthrich - structure display

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

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