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 10123

Title: Solution structure of the PWWP domain of mouse Hepatoma-derived growth factor, related protein 3   PubMed: 15689505

Deposition date: 2007-04-02 Original release date: 2008-07-16

Authors: Nameki, N.; Kigawa, T.; Koshiba, S.; Kobayashi, N.; Tochio, N.; Inoue, M.; Yokoyama, S.

Citation: Nameki, N.; Tochio, N.; Koshiba, S.; Inoue, M.; Yabuki, T.; Aoki, M.; Seki, E.; Matsuda, T.; Fujikura, Y.; Saito, M.; Ikari, M.; Watanabe, M.; Terada, T.; Shirouzu, M.; Yoshida, M.; Hirota, H.; Tanaka, A.; Hayashizaki, Y.; Guntert, P.; Kigawa, T.; Yokoyama, S.. "Solution structure of the PWWP domain of the hepatoma-derived growth factor family."  Protein Sci. 14, 756-764 (2005).

Assembly members:
PWWP domain, polymer, 96 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis

Entity Sequences (FASTA):
PWWP domain: GSSGSSGEYKAGDLVFAKMK GYPHWPARIDELPEGAVKPP ANKYPIFFFGTHETAFLGPK DLFPYKEYKDKFGKSNKRKG FNEGLWEIENSGPSSG

Data sets:
Data typeCount
13C chemical shifts438
15N chemical shifts91
1H chemical shifts644

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PWWP domain1

Entities:

Entity 1, PWWP domain 96 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYGLUTYRLYS
2   ALAGLYASPLEUVALPHEALALYSMETLYS
3   GLYTYRPROHISTRPPROALAARGILEASP
4   GLULEUPROGLUGLYALAVALLYSPROPRO
5   ALAASNLYSTYRPROILEPHEPHEPHEGLY
6   THRHISGLUTHRALAPHELEUGLYPROLYS
7   ASPLEUPHEPROTYRLYSGLUTYRLYSASP
8   LYSPHEGLYLYSSERASNLYSARGLYSGLY
9   PHEASNGLUGLYLEUTRPGLUILEGLUASN
10   SERGLYPROSERSERGLY

Samples:

sample_1: PWWP domain, [U-13C; U-15N], 0.7 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 120 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B.A. - data analysis

Kujira v0.613, Kobayashi, N. - data analysis

CYANA v1.0.6, Guntert, P. - structure solution

OPALp, Billeter, M., Guntert, P., Koradi, R. - refinement

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAA90477 BAA90478 BAA91597 BAB31754 BAC32123
GB AAD34137 AAH15483 AAH55734 AAI51803 AAK72965
REF NP_001178297 NP_001297902 NP_038914 NP_057157 NP_665728
SP Q923W4 Q9JMG7 Q9Y3E1
TPG DAA17616

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts