BMRB Entry 17501
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17501
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Title: The NMR structure of the protein NP_344798.1 reveals a CCA-adding enzyme head domain
Deposition date: 2011-03-01 Original release date: 2011-03-25
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 NP_344798.1" Not known ., .-..
Assembly members:
NP_344798.1, polymer, 191 residues, 22835.953 Da.
Natural source: Common Name: Streptococcus pneumoniae TIGR4 Taxonomy ID: 170187 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pneumoniae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NP_344798.1: GMNTVKNKQEILEAFRESPD
MMAILTIIRDLGLKDSWLAA
GSVRNFIWNLLSDKSPFDHE
TDIDVIFFDPDFSYEETLLL
EKKLREDFPQYQWELKNQVY
MHQHSPHTASYTSSRDAMSK
YPERCTAVGLRLNEELDFEL
YVPYGLEDILNFQVRPTPHF
LENEDRMELYQTRLSKKNWQ
EKWKNLIFKNT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 834 |
| 15N chemical shifts | 208 |
| 1H chemical shifts | 1393 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NP_344798.1 | 1 |
Entities:
Entity 1, NP_344798.1 191 residues - 22835.953 Da.
| 1 | GLY | MET | ASN | THR | VAL | LYS | ASN | LYS | GLN | GLU | ||||
| 2 | ILE | LEU | GLU | ALA | PHE | ARG | GLU | SER | PRO | ASP | ||||
| 3 | MET | MET | ALA | ILE | LEU | THR | ILE | ILE | ARG | ASP | ||||
| 4 | LEU | GLY | LEU | LYS | ASP | SER | TRP | LEU | ALA | ALA | ||||
| 5 | GLY | SER | VAL | ARG | ASN | PHE | ILE | TRP | ASN | LEU | ||||
| 6 | LEU | SER | ASP | LYS | SER | PRO | PHE | ASP | HIS | GLU | ||||
| 7 | THR | ASP | ILE | ASP | VAL | ILE | PHE | PHE | ASP | PRO | ||||
| 8 | ASP | PHE | SER | TYR | GLU | GLU | THR | LEU | LEU | LEU | ||||
| 9 | GLU | LYS | LYS | LEU | ARG | GLU | ASP | PHE | PRO | GLN | ||||
| 10 | TYR | GLN | TRP | GLU | LEU | LYS | ASN | GLN | VAL | TYR | ||||
| 11 | MET | HIS | GLN | HIS | SER | PRO | HIS | THR | ALA | SER | ||||
| 12 | TYR | THR | SER | SER | ARG | ASP | ALA | MET | SER | LYS | ||||
| 13 | TYR | PRO | GLU | ARG | CYS | THR | ALA | VAL | GLY | LEU | ||||
| 14 | ARG | LEU | ASN | GLU | GLU | LEU | ASP | PHE | GLU | LEU | ||||
| 15 | TYR | VAL | PRO | TYR | GLY | LEU | GLU | ASP | ILE | LEU | ||||
| 16 | ASN | PHE | GLN | VAL | ARG | PRO | THR | PRO | HIS | PHE | ||||
| 17 | LEU | GLU | ASN | GLU | ASP | ARG | MET | GLU | LEU | TYR | ||||
| 18 | GLN | THR | ARG | LEU | SER | LYS | LYS | ASN | TRP | GLN | ||||
| 19 | GLU | LYS | TRP | LYS | ASN | LEU | ILE | PHE | LYS | ASN | ||||
| 20 | THR |
Samples:
sample_1: NP_344798.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 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 |
| 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, Mumenthaler and Wuthrich - 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
Related Database Links:
| PDB | |
| EMBL | CAR68108 CBW33875 CBW35903 CEO61672 CEO63344 |
| GB | AAK74438 AAK99043 ABJ54676 ACO17445 ACO19518 |
| REF | NP_357833 WP_001098892 WP_001098893 WP_001098894 WP_001098895 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts