BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15003

Title: SOLUTION STRUCTURE OF GROUP IV WW DOMAIN: A.NIDULANS PINA   PubMed: 17693144

Authors: Ng, C.; Kato, Y.; Tanokura, M.; Brownlee, R.

Citation: Kato, Yusuke; Ng, Chai; Brownlee, Robert; Tanokura, Masaru. "PinA from Aspergillus nidulans binds to pS/pT-P motifs using the same Loop I and XP groove as mammalian Pin1."  Biochim. Biophys. Acta. 1774, 1208-1212 (2007).

Assembly members:
WW_Domain_polypeptide, polymer, 53 residues, 6205.003 Da.

Natural source:   Common Name: Aspergillus Nidulans   Taxonomy ID: 162425   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Emericella nidulans

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

Entity Sequences (FASTA):
WW_Domain_polypeptide: SMVNTGLPAGWEVRHSNSKN LPYYFNPATRESRWEPPADT DMETLKMYMATYH

Data sets:
Data typeCount
13C chemical shifts145
15N chemical shifts49
1H chemical shifts330

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1WW Domain1

Entities:

Entity 1, WW Domain 53 residues - 6205.003 Da.

1   SERMETVALASNTHRGLYLEUPROALAGLY
2   TRPGLUVALARGHISSERASNSERLYSASN
3   LEUPROTYRTYRPHEASNPROALATHRARG
4   GLUSERARGTRPGLUPROPROALAASPTHR
5   ASPMETGLUTHRLEULYSMETTYRMETALA
6   THRTYRHIS

Samples:

sample: WW Domain polypeptide, [U-100% 13C; U-100% 15N], 1.8 mM; sodium phosphate 50 mM; sodium chloride 50 mM; sodium azide 0.02%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 5.0; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
3D HNHAsampleisotropicsample_conditions_1
3D_13C- SEPARATED_NOESYsampleisotropicsample_conditions_1
3D_15N- SEPARATED_NOESYsampleisotropicsample_conditions_1
2D 1H-15N HSQCsampleisotropicsample_conditions_1
3D HNCACBsampleisotropicsample_conditions_1
3D HNCAsampleisotropicsample_conditions_1
3D HN(COCA)CBsampleisotropicsample_conditions_1
3D HCCH-COSYsampleisotropicsample_conditions_1
3D HCCH-TOCSYsampleisotropicsample_conditions_1

Software:

CYANA v2.1, T Herrmann, P Guntert and K Wuthrich - automated peak assignments, refinement, structure solution

NMRPipe, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing

SPARKY v3, T Goddard - chemical shift assignment, data analysis

VNMR, Varian - collection

TALOS, G Cornilescu, F Delaglio and A Bax - coupling constant

NMR spectrometers:

  • Varian INOVA 500 MHz

Related Database Links:

BMRB 15466
PDB 2JV4
GB AAC49984 EAA57931
REF XP_663749
TPE CBF70093