BMRB Entry 16802
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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/BMR16802
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Title: Solution structure of N-terminal domain of CcmH from Escherichia.coli PubMed: 22789558
Deposition date: 2010-03-30 Original release date: 2014-03-04
Authors: Hong, Jing; Zheng, Xueming; Hu, Hongyu; Lin, Donghai
Citation: Zheng, Xue-Ming; Hong, Jing; Li, Hai-Yin; Lin, Dong-Hai; Hu, Hong-Yu. "Biochemical properties and catalytic domain structure of the CcmH protein from Escherichia coli." Biochim. Biophys. Acta 1824, 1394-1400 (2012).
Assembly members:
CcmH, polymer, 81 residues, 9459.733 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CcmH: TIDVLQFKDEAQEQQFRQLT
EELRCPKCQNNSIADSNSMI
ATDLRQKVYELMQEGKSKKE
IVDYMVARYGNFVTYDPPLT
P
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 323 |
| 15N chemical shifts | 73 |
| 1H chemical shifts | 566 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CcmH | 1 |
Entities:
Entity 1, CcmH 81 residues - 9459.733 Da.
| 1 | THR | ILE | ASP | VAL | LEU | GLN | PHE | LYS | ASP | GLU | ||||
| 2 | ALA | GLN | GLU | GLN | GLN | PHE | ARG | GLN | LEU | THR | ||||
| 3 | GLU | GLU | LEU | ARG | CYS | PRO | LYS | CYS | GLN | ASN | ||||
| 4 | ASN | SER | ILE | ALA | ASP | SER | ASN | SER | MET | ILE | ||||
| 5 | ALA | THR | ASP | LEU | ARG | GLN | LYS | VAL | TYR | GLU | ||||
| 6 | LEU | MET | GLN | GLU | GLY | LYS | SER | LYS | LYS | GLU | ||||
| 7 | ILE | VAL | ASP | TYR | MET | VAL | ALA | ARG | TYR | GLY | ||||
| 8 | ASN | PHE | VAL | THR | TYR | ASP | PRO | PRO | LEU | THR | ||||
| 9 | PRO |
Samples:
sample_1: entity 1 mM; D2O 10%; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 5 mM; H2O 90%
sample_2: entity 1 mM; D2O 100%; sodium phosphate 50 mM; sodium chloride 100 mM; DTT 5 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger A. T. et.al. - refinement
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB36506 BAE76657 BAG77986 BAI26332 BAI31440 |
| EMBL | CAP76696 CAQ32597 CAQ89785 CAQ99121 CAR03622 |
| GB | AAA16386 AAC75254 AAG57329 AAN43797 AAN81185 |
| REF | NP_311110 NP_416698 NP_708090 WP_001211546 WP_001211547 |
| SP | P0ABM9 P0ABN0 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts