BMRB Entry 16969

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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/BMR16969
MolProbity Validation Chart

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Title:
Structural basis for homodimerization of the Src-associated during mitosis, 68 kD protein (Sam68) Qua1 domain
Deposition date:
2010-06-02
Original release date:
2010-07-26
Authors:
Meyer, N. Helge; Tripsianes, Konstantinos; Vincendeaux, Michelle; Madl, Tobias; Kateb, Fatiha; Brack-werner, Ruth; Sattler, Michael
Citation:

Citation: Meyer, N. Helge; Tripsianes, Konstantinos; Vincendeau, Michelle; Madl, Tobias; Kateb, Fatiha; Brack-Werner, Ruth; Sattler, Michael. "Structural basis for homodimerization of the Src-associated during mitosis, 68-kDa protein (Sam68) Qua1 domain."  J. Biol. Chem. 285, 28893-28901 (2010).
PubMed: 20610388

Assembly members:

Assembly members:
KH_DOMAIN-CONTAINING,RNA-BINDING,SIGNAL_TRANSDUCTION-ASSOCIATED_PROTEIN_1, polymer, 41 residues, 4602.2333 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: pETM11 ZZ sam68 Qua1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
KH_DOMAIN-CONTAINING,RNA-BINDING,SIGNAL_TRANSDUCTION-ASSOCIATED_PROTEIN_1: GAMEPENKYLPELMAEKDSL DPSFTHAMQLLTAEIEKIQK G

Data sets:
Data typeCount
1H chemical shifts293
13C chemical shifts176
15N chemical shifts39

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KH DOMAIN-CONTAINING\,RNA-BINDING\,SIGNAL TRANSDUCTION-ASSOCIATED PROTEIN 1, chain 11
2KH DOMAIN-CONTAINING\,RNA-BINDING\,SIGNAL TRANSDUCTION-ASSOCIATED PROTEIN 1, chain 21

Entities:

Entity 1, KH DOMAIN-CONTAINING\,RNA-BINDING\,SIGNAL TRANSDUCTION-ASSOCIATED PROTEIN 1, chain 1 41 residues - 4602.2333 Da.

1   GLYALAMETGLUPROGLUASNLYSTYRLEU
2   PROGLULEUMETALAGLULYSASPSERLEU
3   ASPPROSERPHETHRHISALAMETGLNLEU
4   LEUTHRALAGLUILEGLULYSILEGLNLYS
5   GLY

Samples:

sample_1: sam68 Qua1, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; NaCl 100 mM; potassium phosphate 20 mM

sample_2: sam68 Qua1, [U-100% 13C; U-100% 15N], 1 mM; H2O 90%; D2O 10%; NaCl 100 mM; potassium phosphate 20 mM

sample_conditions_1: ionic strength: 100.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1solutionsample_conditions_1
3D 1H-15N NOESYsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HNCACBsample_1solutionsample_conditions_1
HNCOCACBsample_1solutionsample_conditions_1
HCC(H)-TOCSYsample_1solutionsample_conditions_1
14N/12C-filtered 3D 1H-13C NOESYsample_1solutionsample_conditions_1
14N/12C-filtered 3D 1H-15N NOESYsample_1solutionsample_conditions_1
HNCOsample_1solutionsample_conditions_1
HSQC (RDC)sample_2isotropicsample_conditions_1
HNCO (RDC)sample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1solutionsample_conditions_1
2D 1H-15N HSQCsample_1solutionsample_conditions_1

Software:

ARIA v2.2, JP.LINGE,MA.WILLIAMS,CA.SPRONK,AM.BONVIN,M. - structure solution, refinement

AutoDep v4.3, AutoDep - data submission

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky vany, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 750 MHz
  • Bruker Avance 600 MHz

Related Database Links:

UNP KHDR1_HUMAN
PDB
DBJ BAC03643 BAE02326 BAG35762 BAG56883 BAG64305
GB AAA59990 AAB47504 AAH00717 AAH10132 AAH19109
REF NP_001039907 NP_001230525 NP_001258807 NP_001270324 NP_006550
SP Q07666
TPG DAA32307
AlphaFold Q99760 Q07666

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