BMRB Entry 11007

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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/BMR11007
MolProbity Validation Chart

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Title:
FBP28WW2 domain in complex with PTPPPLPP peptide
Deposition date:
2007-09-03
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.
PTPPPLPP, polymer, 8 residues, 821.025 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
PTPPPLPP: PTPPPLPP

Data sets:
Data typeCount
1H chemical shifts279

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FBP28WW21
2PTPPPLPP2

Entities:

Entity 1, FBP28WW2 37 residues - 4365.766 Da.

1   GLYALATHRALAVALSERGLUTRPTHRGLU
2   TYRLYSTHRALAASPGLYLYSTHRTYRTYR
3   TYRASNASNARGTHRLEUGLUSERTHRTRP
4   GLULYSPROGLNGLULEULYS

Entity 2, PTPPPLPP 8 residues - 821.025 Da.

1   PROTHRPROPROPROLEUPROPRO

Samples:

sample_1: entity_1 1 mM; entity_2 3 mM; sodium phosphate 100 mM; sodium chloride 50 mM

sample_2: entity_1 1 mM; entity_2 3 mM; sodium phosphate 100 mM; sodium chloride 50 mM

sample_3: entity_1, [U-100% 15N], 1 mM; entity_2 3 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-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - collection

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

XEASY, Keller and Wuthrich - data analysis

Molmol, Koradi, Billeter and Wuthrich - structure display

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

ProcheckNMR, Laskowski and MacArthur - structure analysis

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 600 MHz

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