BMRB Entry 17448
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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/BMR17448
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Title: Solution structure of the protein YP_546394.1, the first structural representative of the pfam family PF12112
Deposition date: 2011-02-08 Original release date: 2011-03-08
Authors: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WUTHRICH, KURT
Citation: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WUTHRICH, KURT. "Solution structure of the protein YP_546394.1, the first structural representative of the pfam family PF12112" Not known ., .-..
Assembly members:
YP_546394.1, polymer, 108 residues, 12034.806 Da.
Natural source: Common Name: b-proteobacteria Taxonomy ID: 405 Superkingdom: Bacteria Kingdom: not available Genus/species: Methylobacillus flagellatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
YP_546394.1: GMGTTEKSGIKEIIIQGLTR
AGKPFRPSDWVDRMCSTYAS
FGADRKLRYSPYLKPRVIEG
VRCLAVDLKLKDTNPEGFNQ
LMHFATENQLNILDAEGNSI
DAAQVTEI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 471 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 761 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | protein YP_546394.1 | 1 |
Entities:
Entity 1, protein YP_546394.1 108 residues - 12034.806 Da.
| 1 | GLY | MET | GLY | THR | THR | GLU | LYS | SER | GLY | ILE | ||||
| 2 | LYS | GLU | ILE | ILE | ILE | GLN | GLY | LEU | THR | ARG | ||||
| 3 | ALA | GLY | LYS | PRO | PHE | ARG | PRO | SER | ASP | TRP | ||||
| 4 | VAL | ASP | ARG | MET | CYS | SER | THR | TYR | ALA | SER | ||||
| 5 | PHE | GLY | ALA | ASP | ARG | LYS | LEU | ARG | TYR | SER | ||||
| 6 | PRO | TYR | LEU | LYS | PRO | ARG | VAL | ILE | GLU | GLY | ||||
| 7 | VAL | ARG | CYS | LEU | ALA | VAL | ASP | LEU | LYS | LEU | ||||
| 8 | LYS | ASP | THR | ASN | PRO | GLU | GLY | PHE | ASN | GLN | ||||
| 9 | LEU | MET | HIS | PHE | ALA | THR | GLU | ASN | GLN | LEU | ||||
| 10 | ASN | ILE | LEU | ASP | ALA | GLU | GLY | ASN | SER | ILE | ||||
| 11 | ASP | ALA | ALA | GLN | VAL | THR | GLU | ILE |
Samples:
sample_1: YP_546394.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 4.5 mM; H20 95%; D20 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 |
| 2D 1H-13C 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 |
Software:
CYANA v3.0, Guntert P. - structure calculation
UNIO v2.0.0, Herrmann and Wuthrich - chemical shift assignment, NOE assignment, peak picking, structure solution
CARA v1.5.3, Keller and Wuthrich - chemical shift assignment
TOPSPIN v1.3, Bruker Biospin - data collection, processing
OPALp v1.2, Koradi,Billeter and Guntert - energy refinement
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