BMRB Entry 6604

Title:
1H, 13C, and 15N complete chemical shift assignments for v-Src SH2 domain complexed with PQpYEEIPI ligand.
Deposition date:
2005-04-22
Original release date:
2005-10-26
Authors:
Fawaz, Radwan; Taylor, Jonathan; Williams, Mark; Ababou, Abdessamad; Ladbury, John
Citation:

Citation: Taylor, Jonathan; Fawaz, Radwan; Ababou, Abdessamad; Williams, Mark; Ladbury, John. "NMR Assignment of the Apo and Peptide-bound SH2 Domain from the Rous Sarcoma Viral Protein Src"  J. Biomol. NMR 32, 339-339 (2005).
PubMed: 16211495

Assembly members:

Assembly members:
v-Src SH2, polymer, 106 residues, Formula weight is not available
PQpYEEIPI, polymer, 8 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Rous Sarcoma virus   Taxonomy ID: 11886   Superkingdom: Viruses   Kingdom: Not applicable   Genus/species: alpharetrovirus Rous sarcoma virus (Schmidt-Ruppin A)

Experimental source:

Experimental source:   Production method: recombinant technology   Vector: pET3a

Data sets:
Data typeCount
13C chemical shifts481
15N chemical shifts120
1H chemical shifts747

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1v-Src SH21
2PQpYEEIPI2

Entities:

Entity 1, v-Src SH2 106 residues - Formula weight is not available

1   GLNALAGLUGLUTRPTYRPHEGLYLYSILE
2   THRARGARGGLUSERGLUARGLEULEULEU
3   ASNPROGLUASNPROARGGLYTHRPHELEU
4   VALARGGLUSERGLUTHRTHRLYSGLYALA
5   TYRCYSLEUSERVALSERASPPHEASPASN
6   ALALYSGLYLEUASNVALLYSHISTYRLYS
7   ILEARGLYSLEUASPSERGLYGLYPHETYR
8   ILETHRSERARGTHRGLNPHESERSERLEU
9   GLNGLNLEUVALALATYRTYRSERLYSHIS
10   ALAASPGLYLEUCYSHISARGLEUTHRASN
11   VALCYSPROTHRSERLYS

Entity 2, PQpYEEIPI 8 residues - Formula weight is not available

1   PROGLNPTRGLUGLUILEPROILE

Samples:

sample_1: v-Src SH2, [U-95% 13C], 0.5 mM; v-Src SH2, [U-90% 15N], 0.5 mM; PQpYEEIPI 1.5 mM; MES 20 mM; NaCl 50 mM; DTT 1 mM

conditions_1: ionic strength: 0.05 M; pH: 6; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
HNCAsample_1not availableconditions_1
HNCACBsample_1not availableconditions_1
HNCOsample_1not availableconditions_1
CBCACONHsample_1not availableconditions_1
C(CO)NHsample_1not availableconditions_1
1H-15N HSQCsample_1not availableconditions_1
1H-13C HSQCsample_1not availableconditions_1
1H-15N NOESY-HSQCsample_1not availableconditions_1
1H-15N TOWNY-HSQCsample_1not availableconditions_1
1H-13C NOESY-HSQCsample_1not availableconditions_1
1H-13C HCCH-TOCSYsample_1not availableconditions_1
HNHAsample_1not availableconditions_1
CBHDsample_1not availableconditions_1

Software:

ANSIG v3.3 -

NMR spectrometers:

  • Varian UNITY-INOVA 800 MHz
  • Varian UNITY-INOVA 600 MHz
  • Varian UNITY-INOVA 500 MHz

Related Database Links:

PDB
DBJ BAA01500 BAE26865 BAI47379
EMBL CAA23696 CAA24495 CAA26485 CAA32012 CAA36156
GB AAA40135 AAA42563 AAA42565 AAA42573 AAA42581
PRF 0903255A
REF NP_001020566 NP_001104274 NP_005408 NP_033297 NP_114183
SP P00523 P00524 P00525 P05480 P12931
AlphaFold P00525 P12931 P05480 P00523 P00524

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks