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 10089

Title: Solution structure of phosphotyrosine interaction domain of mouse Numb protein

Deposition date: 2007-01-24 Original release date: 2008-08-14

Authors: Sato, M.; Tomizawa, T.; Koshiba, S.; Tochio, N.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Sato, M.; Tomizawa, T.; Koshiba, S.; Tochio, N.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution structure of phosphotyrosine interaction domain of mouse Numb protein"  . ., .-..

Assembly members:
PID domain, polymer, 156 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):
PID domain: GSSGSSGASRPHQWQTDEEG VRTGKCSFPVKYLGHVEVDE SRGMHICEDAVKRLKATGKK AVKAVLWVSADGLRVVDEKT KDLIVDQTIEKVSFCAPDRN FDRAFSYICRDGTTRRWICH CFMAVKDTGERLSHAVGCAF AACLERKQKRSGPSSG

Data sets:
Data typeCount
13C chemical shifts666
15N chemical shifts162
1H chemical shifts1038

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Numb protein1

Entities:

Entity 1, Numb protein 156 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYALASERARG
2   PROHISGLNTRPGLNTHRASPGLUGLUGLY
3   VALARGTHRGLYLYSCYSSERPHEPROVAL
4   LYSTYRLEUGLYHISVALGLUVALASPGLU
5   SERARGGLYMETHISILECYSGLUASPALA
6   VALLYSARGLEULYSALATHRGLYLYSLYS
7   ALAVALLYSALAVALLEUTRPVALSERALA
8   ASPGLYLEUARGVALVALASPGLULYSTHR
9   LYSASPLEUILEVALASPGLNTHRILEGLU
10   LYSVALSERPHECYSALAPROASPARGASN
11   PHEASPARGALAPHESERTYRILECYSARG
12   ASPGLYTHRTHRARGARGTRPILECYSHIS
13   CYSPHEMETALAVALLYSASPTHRGLYGLU
14   ARGLEUSERHISALAVALGLYCYSALAPHE
15   ALAALACYSLEUGLUARGLYSGLNLYSARG
16   SERGLYPROSERSERGLY

Samples:

sample_1: PID domain, [U-13C; U-15N], 1.3 mM; phosphate 20 mM; NaCl 100 mM; d-DTT 5 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_1not availablecondition_1
3D 15N-separated NOESYsample_1not availablecondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

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

Kujira v0.8996, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAB23367 BAE45130 BAG37583
EMBL CAD66588 CAH91534
GB AAB09586 AAC97962 AAD47834 AAD49434 AAD54281
REF NP_001005745 NP_001095421 NP_001125900 NP_001258984 NP_001258985
TPG DAA25078

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