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 5654

Title: A Protein Contorsionist-Core Mutations Switch Monomeric Protein GB1 into an Intertwined Tetramer   PubMed: 12379842

Deposition date: 2002-11-06 Original release date: 2003-08-08

Authors: Frank, M.; Dyda, F.; Dobrodumov, A.; Gronenborn, A.

Citation: Frank, M.; Dyda, F.; Dobrodumov, A.; Gronenborn, A.. "Core Mutations Switch Monomeric Protein GB1 into an Intertwined Tetramer"  Nat. Struct. Biol. 9, 877-885 (2002).

Assembly members:
mmunoglobulin G binding protein G, polymer, 56 residues, Formula weight is not available

Natural source:   Common Name: Streptococcus   Taxonomy ID: 1306   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Streptococcus sp.

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

Entity Sequences (FASTA):
mmunoglobulin G binding protein G: MQYKVILNGKTLKGETTTEA VDAATFEKVVKQFFNDNGVD GEWTYDDATKTFTVTE

Data sets:
Data typeCount
13C chemical shifts250
15N chemical shifts61
1H chemical shifts356
coupling constants44

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Immunoglobulin G binding protein G chain A1
2Immunoglobulin G binding protein G chain B1
3Immunoglobulin G binding protein G chain C1
4Immunoglobulin G binding protein G chain D1

Entities:

Entity 1, Immunoglobulin G binding protein G chain A 56 residues - Formula weight is not available

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

Samples:

sample_1: mmunoglobulin G binding protein G, [U-15N; U-13C], 3.5 mM; sodium phosphate 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: mmunoglobulin G binding protein G, [U-15N], 2.89 mM; sodium phosphate 50 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_3: mmunoglobulin G binding protein G, [U-15N; U-13C], 3.5 mM; sodium phosphate 50 mM; sodium azide 0.02%; D2O 100%

sample_4: mmunoglobulin G binding protein G 0.7 mM; mmunoglobulin G binding protein G, [U-15N; U-13C], 0.7 mM; sodium phosphate 50 mM; sodium azide 0.02%; D2O 100%

sample_cond_1: ionic strength: 50 mM; pH: 5.45; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D 15N-separated NOESYnot availablenot availablenot available
HNHAnot availablenot availablenot available
3D 13C-separated NOESYnot availablenot availablenot available
4D 13C-separated NOESYnot availablenot availablenot available
4D 13C/15N-separated NOESYnot availablenot availablenot available
3D 12C-filtered 13C-separated NOESYnot availablenot availablenot available

Software:

NMRPipe v2.2 - processing

PIPP v4.3.2 - data analysis

xwinnmr v2.6 - collection

X-PLOR v4.0 - refinement

CNS v1.0 - structure solution

NMR spectrometers:

  • Bruker DMX 500 MHz

Related Database Links:

BMRB 5875
PDB

Download simulated HSQC data in one of the following formats:
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