BMRB Entry 17632

Click here to enlarge.

PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17632
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Title:
Solution structure of the Vav1 SH2 domain complexed with a Syk-derived doubly phosphorylated peptide
Deposition date:
2011-05-09
Original release date:
2011-06-03
Authors:
Chen, Chih-Hong; Gorenstein, Nina; Post, Carol
Citation:

Citation: Chen, Chih-Hong; Martin, Victoria; Gorenstein, Nina; Geahlen, Robert; Post, Carol Beth. "Two closely-spaced tyrosines regulate NFAT signaling in B cells via Syk association with Vav."  Mol. Cell. Biol. 31, 2984-2996 (2011).
PubMed: 21606197

Assembly members:

Assembly members:
entity_1, polymer, 107 residues, 12335.253 Da.
entity_2, polymer, 13 residues, 1674.475 Da.

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   Vector: pETTEV411

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMQDLSVHLWYAGPMERAG AESILANRSDGTFLVRQRVK DAAEFAISIKYNVEVKHIKI MTAEGLYRITEKKAFRGLTE LVEFYQQNSLKDCFKSLDTT LQFPFKE
entity_2: DTEVXESPXADPE

Data sets:
Data typeCount
13C chemical shifts355
15N chemical shifts95
1H chemical shifts771

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 107 residues - 12335.253 Da.

1   GLYHISMETGLNASPLEUSERVALHISLEU
2   TRPTYRALAGLYPROMETGLUARGALAGLY
3   ALAGLUSERILELEUALAASNARGSERASP
4   GLYTHRPHELEUVALARGGLNARGVALLYS
5   ASPALAALAGLUPHEALAILESERILELYS
6   TYRASNVALGLUVALLYSHISILELYSILE
7   METTHRALAGLUGLYLEUTYRARGILETHR
8   GLULYSLYSALAPHEARGGLYLEUTHRGLU
9   LEUVALGLUPHETYRGLNGLNASNSERLEU
10   LYSASPCYSPHELYSSERLEUASPTHRTHR
11   LEUGLNPHEPROPHELYSGLU

Entity 2, entity_2 13 residues - 1674.475 Da.

1   ASPTHRGLUVALPTRGLUSERPROPTRALA
2   ASPPROGLU

Samples:

sample_1: entity_1, [U-13C; U-15N], 1.1 mM; TRIS 20 mM; sodium chloride 100 mM; DTT 1 mM; sodium azide 0.02%; entity_2 1.1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 120 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 500 MHz

Related Database Links:

BMRB 19423
PDB
DBJ BAG36112 BAG62721 BAJ21026
EMBL CAA58783
GB AAC25011 AAH13361 AAI23647 AIC59346 EAW69057
REF NP_001071542 NP_001245135 NP_001245136 NP_005419 XP_002801087
SP P15498 Q08DN7
TPG DAA27902
AlphaFold P15498 Q08DN7 P48025

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