BMRB Entry 5875

Title:
1H, 13C, and 15N Chemical Shift Assignments of the dimeric mutant of GB1
Deposition date:
2003-07-18
Original release date:
2003-12-05
Authors:
Byeon, In-Ja; Louis, John; Gronenborn, Angela
Citation:

Citation: Byeon, In-Ja; Louis, John; Gronenborn, Angela. "A Protein Contortionist: Core Mutations of GB1 that Induce Dimerization and Domain Swapping"  J. Mol. Biol. 333, 141-152 (2003).
PubMed: 14516749

Assembly members:

Assembly members:
Immunoglobulin Binding domain 1 of Protein G, polymer, 56 residues, 6220.8 Da.

Natural source:

Natural source:   Common Name: Streptococcus sp. (Lancefield Group G)   Taxonomy ID: 1306   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Streptococcus Streptococcus sp. (Lancefield Group G)

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Immunoglobulin Binding domain 1 of Protein G: MQYKVILNGKTLKGETTTEA VDAATAEKVVKQFFNDNGVD GEWTYDDATKTFTVTE

Data sets:
Data typeCount
13C chemical shifts175
15N chemical shifts61
1H chemical shifts362

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1GB1 subunit A1
2GB1 subunit B1

Entities:

Entity 1, GB1 subunit A 56 residues - 6220.8 Da.

1   METGLNTYRLYSVALILELEUASNGLYLYS
2   THRLEULYSGLYGLUTHRTHRTHRGLUALA
3   VALASPALAALATHRALAGLULYSVALVAL
4   LYSGLNPHEPHEASNASPASNGLYVALASP
5   GLYGLUTRPTHRTYRASPASPALATHRLYS
6   THRPHETHRVALTHRGLU

Samples:

sample_1: Immunoglobulin Binding domain 1 of Protein G, [U-95% 13C; U-95% 15N], 1.7 mM

Ex-cond_1: pH: 6.0; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-1H TOCSYnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
2D 1H-13C HSQC/HMQCnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D H(CCO)NH-TOCSYnot availablenot availablenot available
3D C(CCO)NH-TOCSYnot availablenot availablenot available
3D HNHBnot availablenot availablenot available
3D HACAHB-COSYnot availablenot availablenot available
2D 13C'-{13CG} spin-echo differencenot availablenot availablenot available
2D 15N-{13C'} spin-echo differencenot availablenot availablenot available
2D 13C'-{13CG} spin-echo difference aromnot availablenot availablenot available
2D 15N-{13C'} spin-echo difference aromnot availablenot availablenot available
2D [13C-13C] long-range correlation experimentnot availablenot availablenot available
3D 15N-edited TOCSYnot availablenot availablenot available
3D 15N-edited NOESYnot availablenot availablenot available

Software:

NMRPipe v2.2 - processing

PIPP v4.3.2 - data analysis

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DMX 750 MHz
  • Bruker DRX 600 MHz
  • Bruker DMX 600 MHz
  • Bruker DMX 500 MHz

Related Database Links:

BMRB 5654
PDB

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