BMRB Entry 17002
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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/BMR17002
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Title: Solution NMR structure of the protein YP_510488.1 PubMed: NA
Deposition date: 2010-06-15 Original release date: 2010-09-02
Authors: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WILSON, IAN; WUTHRICH, KURT
Citation: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WILSON, IAN; WUTHRICH, KURT. "Solution NMR structure of the protein YP_510488.1" Not known ., .-..
Assembly members:
entity, polymer, 85 residues, 9367.771 Da.
Natural source: Common Name: Jannaschia sp. CCS1 Taxonomy ID: 290400 Superkingdom: Bacteria Kingdom: not available Genus/species: Jannaschia not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GMQFKAEARRNKLMGLWVAE
VLGKSGDEANAYAAEVVKAD
FEEAGHEDVMRKVLGDLDGK
RPEAEVRAKYEGLMAVAKAQ
LMDEL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 352 |
| 15N chemical shifts | 90 |
| 1H chemical shifts | 595 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YP_510488.1 | 1 |
Entities:
Entity 1, YP_510488.1 85 residues - 9367.771 Da.
| 1 | GLY | MET | GLN | PHE | LYS | ALA | GLU | ALA | ARG | ARG | ||||
| 2 | ASN | LYS | LEU | MET | GLY | LEU | TRP | VAL | ALA | GLU | ||||
| 3 | VAL | LEU | GLY | LYS | SER | GLY | ASP | GLU | ALA | ASN | ||||
| 4 | ALA | TYR | ALA | ALA | GLU | VAL | VAL | LYS | ALA | ASP | ||||
| 5 | PHE | GLU | GLU | ALA | GLY | HIS | GLU | ASP | VAL | MET | ||||
| 6 | ARG | LYS | VAL | LEU | GLY | ASP | LEU | ASP | GLY | LYS | ||||
| 7 | ARG | PRO | GLU | ALA | GLU | VAL | ARG | ALA | LYS | TYR | ||||
| 8 | GLU | GLY | LEU | MET | ALA | VAL | ALA | LYS | ALA | GLN | ||||
| 9 | LEU | MET | ASP | GLU | LEU |
Samples:
sample_1: PC07345C, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.113 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY - HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY - HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY - CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 15N Resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 13Cali Resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 13Caro Resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA vCYANA3.0, Guntert, Mumenthaler and Wuthrich - TORSION ANGLE DYNAMICS
UNIO vUNIO2.0.0, Torsten Herrmann - structure solution
TOPSPIN v1.3, Bruker Biospin - processing
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
CARA, Keller and Wuthrich - chemical shift assignment
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