BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15351

Title: Solution structure of first SH3 domain of adaptor Nck   PubMed: 18269246

Authors: Hake, Michael; Choowongkomon, Kiattawee; Carlin, Cathleen; Sonnichsen, Frank

Citation: Hake, Michael; Choowongkomon, Kiattawee; Kostenko, Olga; Carlin, Cathleen; Sonnichsen, Frank. "Specificity Determinants of a Novel Nck Interaction with the Juxtamembrane Domain of the Epidermal Growth Factor Receptor"  Biochemistry 47, 3096-3108 (2008).

Assembly members:
Nck1-1, polymer, 63 residues, 7461.453 Da.

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

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

Entity Sequences (FASTA):
Nck1-1: GSMAEEVVVVAKFDYVAQQE QELDIKKNERLWLLDDSKSW WRVRNSMNKTGFVPSNYVER KNS

Data sets:
Data typeCount
13C chemical shifts281
15N chemical shifts67
1H chemical shifts441

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nck1-1 SH31

Entities:

Entity 1, Nck1-1 SH3 63 residues - 7461.453 Da.

1   GLYSERMETALAGLUGLUVALVALVALVAL
2   ALALYSPHEASPTYRVALALAGLNGLNGLU
3   GLNGLULEUASPILELYSLYSASNGLUARG
4   LEUTRPLEULEUASPASPSERLYSSERTRP
5   TRPARGVALARGASNSERMETASNLYSTHR
6   GLYPHEVALPROSERASNTYRVALGLUARG
7   LYSASNSER

Samples:

sample_1: Nck1-1, [U-99% 13C; U-99% 15N], 0.5 – 1.0 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 6.1; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRView v5.2.1, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

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

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - water refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Varian INOVA 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAG35571 BAG73433 BAK63238
EMBL CAA35599
GB AAD13752 AAH02015 AAH06403 AAI16110 AAI67009
REF NP_001069540 NP_001100321 NP_001131102 NP_001159671 NP_001233509
SP P16333 Q99M51
TPG DAA33097