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 26643

Title: Backbone 1H, 13C, and 15N chemical shift assignments for the N-WASP-GBD Nck complex

Deposition date: 2015-08-30 Original release date: 2015-09-23

Authors: Wu, Qiong; Okrut, Julia; Taunton, Jack

Citation: Okrut, Julia; Prakash, Sumit; Wu, Qiong; Kelly, Mark; Taunton, Jack. "Allosteric N-WASP activation by an inter-SH3 domain linker in Nck"  Not known ., .-..

Assembly members:
GBD-Nck, polymer, 108 residues, Formula weight is not available

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):
GBD-Nck: GHMTKADIGTPSNFQHIGHV GWDPNTGFDLNNLDPELKNL FDMCGISEAQLKDRETSKVI YDFIEKTGGVEAVKNELRRQ GGSGGSARKASIVKNLKDTL GIGKVKRK

Data sets:
Data typeCount
13C chemical shifts264
15N chemical shifts88
1H chemical shifts136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GBD-Nck1

Entities:

Entity 1, GBD-Nck 108 residues - Formula weight is not available

Residue 1-3 are cloning artifacts. Residues 4-80 correspond to N-WASP aa 196-272. Residues 81-86 constitute a GGSGGS linker. Residues 87-108 correspond to Nck1 aa 62-83.

1   GLYHISMETTHRLYSALAASPILEGLYTHR
2   PROSERASNPHEGLNHISILEGLYHISVAL
3   GLYTRPASPPROASNTHRGLYPHEASPLEU
4   ASNASNLEUASPPROGLULEULYSASNLEU
5   PHEASPMETCYSGLYILESERGLUALAGLN
6   LEULYSASPARGGLUTHRSERLYSVALILE
7   TYRASPPHEILEGLULYSTHRGLYGLYVAL
8   GLUALAVALLYSASNGLULEUARGARGGLN
9   GLYGLYSERGLYGLYSERALAARGLYSALA
10   SERILEVALLYSASNLEULYSASPTHRLEU
11   GLYILEGLYLYSVALLYSARGLYS

Samples:

sample_1: GBD-Nck, [U-98% 13C; U-98% 15N], 550 uM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMRPipe, Delaglio, Zhengrong and Bax - processing

VNMRJ v4.2, Varian - collection

NMR spectrometers:

  • Agilent DD2 600 MHz

Related Database Links:

BMRB 18165
PDB
DBJ BAA11082 BAA21534 BAE25143 BAE25639 BAE28201
EMBL CAC69994 CAH89371 CAH91010 CAL26602
GB AAH52955 AAH55045 AAI51608 AAQ96857 AAV38348
REF NP_001103835 NP_001128797 NP_001253726 NP_003932 NP_082735
SP O00401 O08816 Q91YD9 Q95107
TPG DAA30422

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts