BMRB Entry 25024
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR25024
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Gao, Daiwen; Yang, Daiwen. "3D structure of RP domain of MiSp" .
Assembly members:
entity, polymer, 125 residues, 12115.084 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET-M
Entity Sequences (FASTA):
entity: GNAFAQSLSSNLLSSGDFVQ
MISSTTSTDQAVSVATSVAQ
NVGNQLGLDANAMNSLLGAV
SGYVSTLGNAISDASAYANA
ISSAIGNVLANSGSISESTA
SSAASSAASSVTTTLTSYGP
AVFYA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 136 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 263 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RP domain of MiSp | 1 |
Entities:
Entity 1, RP domain of MiSp 125 residues - 12115.084 Da.
| 1 | GLY | ASN | ALA | PHE | ALA | GLN | SER | LEU | SER | SER | ||||
| 2 | ASN | LEU | LEU | SER | SER | GLY | ASP | PHE | VAL | GLN | ||||
| 3 | MET | ILE | SER | SER | THR | THR | SER | THR | ASP | GLN | ||||
| 4 | ALA | VAL | SER | VAL | ALA | THR | SER | VAL | ALA | GLN | ||||
| 5 | ASN | VAL | GLY | ASN | GLN | LEU | GLY | LEU | ASP | ALA | ||||
| 6 | ASN | ALA | MET | ASN | SER | LEU | LEU | GLY | ALA | VAL | ||||
| 7 | SER | GLY | TYR | VAL | SER | THR | LEU | GLY | ASN | ALA | ||||
| 8 | ILE | SER | ASP | ALA | SER | ALA | TYR | ALA | ASN | ALA | ||||
| 9 | ILE | SER | SER | ALA | ILE | GLY | ASN | VAL | LEU | ALA | ||||
| 10 | ASN | SER | GLY | SER | ILE | SER | GLU | SER | THR | ALA | ||||
| 11 | SER | SER | ALA | ALA | SER | SER | ALA | ALA | SER | SER | ||||
| 12 | VAL | THR | THR | THR | LEU | THR | SER | TYR | GLY | PRO | ||||
| 13 | ALA | VAL | PHE | TYR | ALA |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 0.6 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.3 M; pH: 7; pressure: 1 atm; temperature: 302 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks