BMRB Entry 15510

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15510

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Title:
N-terminal SH3 domain of human Nckalpha
Deposition date:
2007-10-05
Original release date:
2008-11-14
Authors:
Santiveri, Clara; Borroto, Aldo; Simon, Luis; Rico, Manuel; Ortiz, Angel; Alarcon, Balbino; Jimenez, M. Angeles
Citation:

Citation: Santiveri, Clara; Borroto, Aldo; Simon, Luis; Rico, Manuel; Alarcon, Balbino; Jimenez, M. Angeles. "Interaction between the N-terminal SH3 domain of Nckalpha and CD3varepsilon-derived peptides: Non-canonical and canonical recognition motifs."  Biochim. Biophys. Acta 1794, 110-117 (2009).
PubMed: 18955169

Assembly members:

Assembly members:
Nckalpha-SH3.1, polymer, 72 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   Vector: pGEX4T

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Nckalpha-SH3.1: GSTMAEEVVVVAKFDYVAQQ EQELDIKKNERLWLLDDSKS WWRVRNSMNKTGFVPSNYVE RKNSARAAANSS

Data typeCount
13C chemical shifts421
15N chemical shifts84
1H chemical shifts1175

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1chain A1

Entities:

Entity 1, chain A 72 residues - Formula weight is not available

1   GLYSERTHRMETALAGLUGLUVALVALVAL
2   VALALALYSPHEASPTYRVALALAGLNGLN
3   GLUGLNGLULEUASPILELYSLYSASNGLU
4   ARGLEUTRPLEULEUASPASPSERLYSSER
5   TRPTRPARGVALARGASNSERMETASNLYS
6   THRGLYPHEVALPROSERASNTYRVALGLU
7   ARGLYSASNSERALAARGALAALAALAASN
8   SERSER

Samples:

sample_1: Nckalpha-SH3.1 1 mM; sodium phosphate 50 mM; H2O 90%; D2O, [U-100% 2H], 10%; DSS 0.1 mM

sample_2: Nckalpha-SH3.1, 1 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 100%; DSS 0.1 mM

sample_3: Nckalpha-SH3.1, [U-100% 15N], 1 mM; sodium phosphate 50 mM; H2O 90%; D2O, [U-100% 2H], 10%; DSS 0.1 mM

sample_4: Nckalpha-SH3.1, [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 50 mM; H2O 90%; D2O, [U-100% 2H], 10%; DSS 0.1 mM

sample_5: Nckalpha-SH3.1, [U-100% 13C; U-100% 15N], 1.2 mM; sodium phosphate 50 mM; D2O, [U-100% 2H], 100%; DSS 0.1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 5.7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_4isotropicsample_conditions_1
3D HNCOsample_4isotropicsample_conditions_1
3D HNCAsample_4isotropicsample_conditions_1
3D CBCA(CO)NHsample_4isotropicsample_conditions_1
3D CBCANHsample_4isotropicsample_conditions_1
3D HBHA(CO)NHsample_4isotropicsample_conditions_1
3D HACANHsample_4isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_conditions_1
3D 1H-13C NOESYsample_5isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_5isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_5isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, processing

xwinnmr, Bruker Biospin - collection, processing

Molmol, Koradi, Billeter and Wuthrich - structure analysis

ProcheckNMR, Laskowski and MacArthur - structure analysis

SPARKY, Goddard - chemical shift assignment, data analysis

PROMOTIF, (PROMOTIF)-Hutchinson and Thornton - structure analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB EAW79106 EAW79107
REF XP_003931007 XP_004278992 XP_004314905 XP_004314906 XP_004588395