BMRB Entry 5212

Title:
SAP/SH2D1A bound to peptide n-pY
Deposition date:
2001-11-15
Original release date:
2002-05-08
Authors:
Hwang, P.; Li, C.; Morra, M.; Lillywhite, J.; Gertler, F.; Terhorst, C.; Kay, L.; Pawson, T.; Forman-Kay, J.; Li, S.-C.
Citation:

Citation: Hwang, P.; Li, C.; Morra, M.; Lillywhite, J.; Muhandiram, D.; Gertler, F.; Terhorst, C.; Kay, L.; Pawson, T.; Forman-Kay, J.; Li, S.-C.. "A "three-pronged" Binding Mechanism for the SAP/SH2D1A SH2 Domain: Structural Basis and Relevance to the XLP Syndrome"  EMBO J. 21, 314-323 (2002).
PubMed: 11823424

Assembly members:

Assembly members:
SAP/SH2D1A, polymer, 128 residues, Formula weight is not available
peptide n-pY, polymer, 9 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

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

Data sets:
Data typeCount
1H chemical shifts773
15N chemical shifts133
13C chemical shifts557

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SH2 DOMAIN PROTEIN 1A1
2peptide n-pY2

Entities:

Entity 1, SH2 DOMAIN PROTEIN 1A 128 residues - Formula weight is not available

1   METASPALAVALALAVALTYRHISGLYLYS
2   ILESERARGGLUTHRGLYGLULYSLEULEU
3   LEUALATHRGLYLEUASPGLYSERTYRLEU
4   LEUARGASPSERGLUSERVALPROGLYVAL
5   TYRCYSLEUCYSVALLEUTYRHISGLYTYR
6   ILETYRTHRTYRARGVALSERGLNTHRGLU
7   THRGLYSERTRPSERALAGLUTHRALAPRO
8   GLYVALHISLYSARGTYRPHEARGLYSILE
9   LYSASNLEUILESERALAPHEGLNLYSPRO
10   ASPGLNGLYILEVALILEPROLEUGLNTYR
11   PROVALGLULYSLYSSERSERALAARGSER
12   THRGLNGLYTHRTHRGLYILEARGGLUASP
13   PROASPVALCYSLEULYSALAPRO

Entity 2, peptide n-pY 9 residues - Formula weight is not available

1   ARGLYSSERLEUTHRILEPTRALANH2

Samples:

sample_1: SAP/SH2D1A, [U-15N; U-13C], 1 mM; peptide n-pY 1 mM; phosphate buffer 20 mM; NaCl 100 mM; H2O 90%; D2O 10%

sample_cond_1: pH: 6.0; temperature: 303 K; ionic strength: 120 mM; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
3D HN(CO)HBsample_1not availablesample_cond_1
3D HNHBsample_1not availablesample_cond_1
3D 15N,13C-separated NOESYsample_1not availablesample_cond_1

Software:

ARIA v1.0 - structure solution

NMRPipe v1.8 - processing

NMRView v3.0 - data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

REF NP_002342.1 XP_865096.1 NP_001028009.1
SWISS-PROT O60880
GenBank AAK11578.1 AAX37129.1 AAC62631.1 AAH20732.1 AAC62630.1
EMBL CAG46840.1 CAA19222.1 CAG46828.1 CAA18777.1
PDB
BMRB 5211

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