BMRB Entry 15067
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15067
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Kempf, James; Jung, Ju-yeon; Ragain, Christina; Sampson, Nicole; Loria, J.. "Dynamic Requirements for a Functional Protein Hinge" J. Mol. Biol. 368, 131-149 (2007).
PubMed: 17336327
Assembly members:
PGG/GGG, polymer, 248 residues, 26620 Da.
PGA, non-polymer, 156.031 Da.
Natural source: Common Name: chicken Taxonomy ID: 9031 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Gallus gallus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b/PGG/GGG
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
| Data type | Count |
| 13C chemical shifts | 394 |
| 15N chemical shifts | 177 |
| 1H chemical shifts | 177 |
| heteronuclear NOE values | 172 |
| T1 relaxation values | 172 |
| T2 relaxation values | 172 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PGG/GGG monomer, 1 | 1 |
| 2 | PGG/GGG monomer, 2 | 1 |
| 3 | 2-PGA | 2 |
Entities:
Entity 1, PGG/GGG monomer, 1 248 residues - 26620 Da.
26.6kDa monomer of 53.1 kDa homodimer reported
| 1 | MET | ALA | PRO | ARG | LYS | PHE | PHE | VAL | GLY | GLY | ||||
| 2 | ASN | TRP | LYS | MET | ASN | GLY | ASP | LYS | LYS | SER | ||||
| 3 | LEU | GLY | GLU | LEU | ILE | HIS | THR | LEU | ASN | GLY | ||||
| 4 | ALA | LYS | LEU | SER | ALA | ASP | THR | GLU | VAL | VAL | ||||
| 5 | CYS | GLY | ALA | PRO | SER | ILE | TYR | LEU | ASP | PHE | ||||
| 6 | ALA | ARG | GLN | LYS | LEU | ASP | ALA | LYS | ILE | GLY | ||||
| 7 | VAL | ALA | ALA | GLN | ASN | CYS | TYR | LYS | VAL | PRO | ||||
| 8 | LYS | GLY | ALA | PHE | THR | GLY | GLU | ILE | SER | PRO | ||||
| 9 | ALA | MET | ILE | LYS | ASP | ILE | GLY | ALA | ALA | TRP | ||||
| 10 | VAL | ILE | LEU | GLY | HIS | SER | GLU | ARG | ARG | HIS | ||||
| 11 | VAL | PHE | GLY | GLU | SER | ASP | GLU | LEU | ILE | GLY | ||||
| 12 | GLN | LYS | VAL | ALA | HIS | ALA | LEU | ALA | GLU | GLY | ||||
| 13 | LEU | GLY | VAL | ILE | ALA | CYS | ILE | GLY | GLU | LYS | ||||
| 14 | LEU | ASP | GLU | ARG | GLU | ALA | GLY | ILE | THR | GLU | ||||
| 15 | LYS | VAL | VAL | PHE | GLU | GLN | THR | LYS | ALA | ILE | ||||
| 16 | ALA | ASP | ASN | VAL | LYS | ASP | TRP | SER | LYS | VAL | ||||
| 17 | VAL | LEU | ALA | TYR | GLU | PRO | GLY | GLY | ALA | ILE | ||||
| 18 | GLY | THR | GLY | GLY | GLY | GLY | THR | PRO | GLN | GLN | ||||
| 19 | ALA | GLN | GLU | VAL | HIS | GLU | LYS | LEU | ARG | GLY | ||||
| 20 | TRP | LEU | LYS | SER | HIS | VAL | SER | ASP | ALA | VAL | ||||
| 21 | ALA | GLN | SER | THR | ARG | ILE | ILE | TYR | GLY | GLY | ||||
| 22 | SER | VAL | THR | GLY | GLY | ASN | CYS | LYS | GLU | LEU | ||||
| 23 | ALA | SER | GLN | HIS | ASP | VAL | ASP | GLY | PHE | LEU | ||||
| 24 | VAL | GLY | GLY | ALA | SER | LEU | LYS | PRO | GLU | PHE | ||||
| 25 | VAL | ASP | ILE | ILE | ASN | ALA | LYS | HIS |
Entity 2, 2-PGA - C2 H5 O6 P - 156.031 Da.
| 1 | PGA |
Samples:
2H_15N_sample: triosephosphate isomerase, [U-99% 15N; U-99%2H], 0.9 mM; D2O 7.5%; sodium azide 0.02%; sodium chloride 10 mM; MES, [U-2H], 10 mM; 2-phosphoglycolate 25 mM
2H_13C_15N_sample: triosephosphate isomerase, [U-99% 13C; U-99% 15N; U-99% 2H], 0.9 mM; D2O 7.5%; sodium azide 0.02%; sodium chloride 10 mM; MES, [U-2H], 10 mM; 2-phosphoglycolate 25 mM
standard_conditions: ionic strength: . mM; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCA | 2H_13C_15N_sample | isotropic | standard_conditions |
| 3D HN(CO)CA | 2H_13C_15N_sample | isotropic | standard_conditions |
| 3D HN(CA)CO | 2H_13C_15N_sample | isotropic | standard_conditions |
| 3D HNCO | 2H_13C_15N_sample | isotropic | standard_conditions |
| 1H-15N ssNOE | 2H_15N_sample | isotropic | standard_conditions |
| 1H-15N T1 | 2H_15N_sample | isotropic | standard_conditions |
| 1H-15N T2 | 2H_15N_sample | isotropic | standard_conditions |
Software:
SPARKY, Goddard - data analysis
PISTACHIO, Eghbalnia - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 15064 15065 15066 |
| PDB | |
| EMBL | CAE45562 CAE45563 CAE45564 |
| GB | AAA49094 AAA49095 KFP89361 KFP99577 KFQ92375 |
| REF | NP_990782 XP_009506417 XP_010147293 XP_010168177 XP_010716134 |
| SP | P00940 |
| AlphaFold | P00940 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks