BMRB Entry 17105
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17105
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Title: Solution Structure of the N-terminal Domain of NP_954075.1
Deposition date: 2010-08-05 Original release date: 2010-08-18
Authors: Susac, Lukas; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Susac, Lukas; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein NP_954075.1 from Geobacter sulfurreducens" Not known ., .-..
Assembly members:
NP_954075.1, polymer, 109 residues, 12045.543 Da.
Natural source: Common Name: d-proteobacteria Taxonomy ID: 35554 Superkingdom: bacteria Kingdom: not available Genus/species: Geobacter sulfurreducens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NP_954075.1: GMSADGSEYGRYFEQLQKVN
LTVRLGDTGSFDGTAAITSL
KGSLAWLELFGAEQPPPNTL
SEGAEVSVSVWTGGALCRCD
GRVETLRDDRQFAIRLVGRV
RELQRREYF
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 353 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 732 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NP_954075.1 | 1 |
Entities:
Entity 1, NP_954075.1 109 residues - 12045.543 Da.
| 1 | GLY | MET | SER | ALA | ASP | GLY | SER | GLU | TYR | GLY | ||||
| 2 | ARG | TYR | PHE | GLU | GLN | LEU | GLN | LYS | VAL | ASN | ||||
| 3 | LEU | THR | VAL | ARG | LEU | GLY | ASP | THR | GLY | SER | ||||
| 4 | PHE | ASP | GLY | THR | ALA | ALA | ILE | THR | SER | LEU | ||||
| 5 | LYS | GLY | SER | LEU | ALA | TRP | LEU | GLU | LEU | PHE | ||||
| 6 | GLY | ALA | GLU | GLN | PRO | PRO | PRO | ASN | THR | LEU | ||||
| 7 | SER | GLU | GLY | ALA | GLU | VAL | SER | VAL | SER | VAL | ||||
| 8 | TRP | THR | GLY | GLY | ALA | LEU | CYS | ARG | CYS | ASP | ||||
| 9 | GLY | ARG | VAL | GLU | THR | LEU | ARG | ASP | ASP | ARG | ||||
| 10 | GLN | PHE | ALA | ILE | ARG | LEU | VAL | GLY | ARG | VAL | ||||
| 11 | ARG | GLU | LEU | GLN | ARG | ARG | GLU | TYR | PHE |
Samples:
sample_1: NP_954075.1, [U-95% 13C; U-95% 15N], 0.9 mM; sodium phosphate 25 mM; sodium azide 4.5 mM; H2O 95%; H2O 5%
sample_conditions_1: ionic strength: 0.075 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (ali) | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (aro) | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment, peak picking
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
TOPSPIN, Bruker Biospin - collection, processing
UNIO, Hermann and Wuthrich - chemical shift assignment, peak picking, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts