BMRB Entry 5875
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5875
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Title: 1H, 13C, and 15N Chemical Shift Assignments of the dimeric mutant of GB1 PubMed: 14516749
Deposition date: 2003-07-18 Original release date: 2003-12-05
Authors: Byeon, In-Ja; Louis, John; Gronenborn, Angela
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).
Assembly members:
Immunoglobulin Binding domain 1 of Protein G, polymer, 56 residues, 6220.8 Da.
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: Production method: recombinant technology
Entity Sequences (FASTA):
Immunoglobulin Binding domain 1 of Protein G: MQYKVILNGKTLKGETTTEA
VDAATAEKVVKQFFNDNGVD
GEWTYDDATKTFTVTE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 175 |
| 15N chemical shifts | 61 |
| 1H chemical shifts | 362 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GB1 subunit A | 1 |
| 2 | GB1 subunit B | 1 |
Entities:
Entity 1, GB1 subunit A 56 residues - 6220.8 Da.
| 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 | ALA | 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: 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:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-1H NOESY | not available | not available | not available |
| 2D 1H-1H TOCSY | not available | not available | not available |
| 2D 1H-15N HSQC | not available | not available | not available |
| 2D 1H-13C HSQC/HMQC | not available | not available | not available |
| 3D HNCO | not available | not available | not available |
| 3D HNCACB | not available | not available | not available |
| 3D CBCA(CO)NH | not available | not available | not available |
| 3D H(CCO)NH-TOCSY | not available | not available | not available |
| 3D C(CCO)NH-TOCSY | not available | not available | not available |
| 3D HNHB | not available | not available | not available |
| 3D HACAHB-COSY | not available | not available | not available |
| 2D 13C | not available | not available | not available |
| 5875 | not available | not available | not available |
| not available | not available | not available | not available |
| not available | ifference | arom' | not available |
| not available | 6 | 2D [13C-13C] long-range correlation experiment | not available |
| not available | 7 | 3D 15N-edited TOCSY | not available |
| not available | 8 | 3D 15N-edited NOESY | not available |
| not available | not available | not available | not 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
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts