BMRB Entry 17090
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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/BMR17090
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Title: Solution NMR structure of the protein YP_399305.1
Deposition date: 2010-07-30 Original release date: 2010-08-18
Authors: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt
Citation: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt. "Solution NMR structure of the protein YP_399305.1" Not known ., .-..
Assembly members:
entity, polymer, 120 residues, 13856.833 Da.
Natural source: Common Name: cyanobacteria Taxonomy ID: 32046 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechococcus elongatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MGITITDELLWAILKDELSD
AEANALVWQALGYVWDEAQS
CWKTDLVAPEWRQDYPEPPD
FIASRPATVKLTRSIPAPYK
QLLKEELGFAGYSINELVPR
KTRRATMTNWLLAYRRSQQD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 513 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 886 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YP_399305.1 | 1 |
Entities:
Entity 1, YP_399305.1 120 residues - 13856.833 Da.
| 1 | MET | GLY | ILE | THR | ILE | THR | ASP | GLU | LEU | LEU | |
| 2 | TRP | ALA | ILE | LEU | LYS | ASP | GLU | LEU | SER | ASP | |
| 3 | ALA | GLU | ALA | ASN | ALA | LEU | VAL | TRP | GLN | ALA | |
| 4 | LEU | GLY | TYR | VAL | TRP | ASP | GLU | ALA | GLN | SER | |
| 5 | CYS | TRP | LYS | THR | ASP | LEU | VAL | ALA | PRO | GLU | |
| 6 | TRP | ARG | GLN | ASP | TYR | PRO | GLU | PRO | PRO | ASP | |
| 7 | PHE | ILE | ALA | SER | ARG | PRO | ALA | THR | VAL | LYS | |
| 8 | LEU | THR | ARG | SER | ILE | PRO | ALA | PRO | TYR | LYS | |
| 9 | GLN | LEU | LEU | LYS | GLU | GLU | LEU | GLY | PHE | ALA | |
| 10 | GLY | TYR | SER | ILE | ASN | GLU | LEU | VAL | PRO | ARG | |
| 11 | LYS | THR | ARG | ARG | ALA | THR | MET | THR | ASN | TRP | |
| 12 | LEU | LEU | ALA | TYR | ARG | ARG | SER | GLN | GLN | ASP |
Samples:
sample_1: YP_399305.1, [U-98% 13C; U-98% 15N], 1.1 mM; H2O 95%; D2O 5%; 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 |
|---|---|---|---|
| 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 |
| 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 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA vCYANA3.0, Guntert, Mumenthaler and Wuthrich - structure solution
Molmol v2K.1, Koradi, Billeter and Wuthrich - Analysis and display of molecules
CARA, Keller and Wuthrich - chemical shift assignment
TOPSPIN v1.3, Bruker Biospin - collection, processing
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
UNIO v2.0.0, (UNIO)-Torsten Herrmann - peak picking, structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts