BMRB Entry 5654
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5654
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
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
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 250 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 356 |
| coupling constants | 44 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Immunoglobulin G binding protein G chain A | 1 |
| 2 | Immunoglobulin G binding protein G chain B | 1 |
| 3 | Immunoglobulin G binding protein G chain C | 1 |
| 4 | Immunoglobulin G binding protein G chain D | 1 |
Entities:
Entity 1, Immunoglobulin G binding protein G chain A 56 residues - Formula weight is not available
| 1 | MET | GLN | TYR | LYS | VAL | ILE | LEU | ASN | GLY | LYS | ||||
| 2 | THR | LEU | LYS | GLY | GLU | THR | THR | THR | GLU | ALA | ||||
| 3 | VAL | ASP | ALA | ALA | THR | PHE | GLU | LYS | VAL | VAL | ||||
| 4 | LYS | GLN | PHE | PHE | ASN | ASP | ASN | GLY | VAL | ASP | ||||
| 5 | GLY | GLU | TRP | THR | TYR | ASP | ASP | ALA | THR | LYS | ||||
| 6 | THR | PHE | THR | VAL | THR | GLU |
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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 15N-separated NOESY | not available | not available | not available |
| HNHA | not available | not available | not available |
| 3D 13C-separated NOESY | not available | not available | not available |
| 4D 13C-separated NOESY | not available | not available | not available |
| 4D 13C/15N-separated NOESY | not available | not available | not available |
| 3D 12C-filtered 13C-separated NOESY | not available | not available | not 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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts