BMRB Entry 17022
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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/BMR17022
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Title: Solution NMR Structure of A3DHT5 from Clostridium thermocellum, Northeast Structural Genomics Consortium Target CmR116
Deposition date: 2010-06-25 Original release date: 2010-08-19
Authors: Mills, Jeffrey; Eletsky, Alexander; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Rost, B.; Acton, T.; Xiao, R.; Everett, J.; Prestegard, James; Montelione, G.; Szyperski, Thomas
Citation: Mills, Jeffrey; Eletsky, Alexander; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Rost, B.; Acton, T.; Xiao, R.; Everett, J.; Prestegard, James; Montelione, G.; Szyperski, Thomas. "Northeast Structural Genomics Consortium Target CmR116" To be published ., .-..
Assembly members:
CmR116, polymer, 131 residues, 14849.378 Da.
Natural source: Common Name: C. thermocellum Taxonomy ID: 1515 Superkingdom: Bacteria Kingdom: not available Genus/species: Clostridium thermocellum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CmR116: MKDGTYYAEADDFDESGWKD
TVTIEVKNGKIVSVDWNAIN
KDGGDDKDTLSRNGGYKMVE
YGGAQAEWHEQAEKVEAYLV
EKQDPTDIKYKDNDGHTDAI
SGATIKVKKFFDLAQKALKD
AEKLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 512 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 823 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CmR116 | 1 |
Entities:
Entity 1, CmR116 131 residues - 14849.378 Da.
| 1 | MET | LYS | ASP | GLY | THR | TYR | TYR | ALA | GLU | ALA | ||||
| 2 | ASP | ASP | PHE | ASP | GLU | SER | GLY | TRP | LYS | ASP | ||||
| 3 | THR | VAL | THR | ILE | GLU | VAL | LYS | ASN | GLY | LYS | ||||
| 4 | ILE | VAL | SER | VAL | ASP | TRP | ASN | ALA | ILE | ASN | ||||
| 5 | LYS | ASP | GLY | GLY | ASP | ASP | LYS | ASP | THR | LEU | ||||
| 6 | SER | ARG | ASN | GLY | GLY | TYR | LYS | MET | VAL | GLU | ||||
| 7 | TYR | GLY | GLY | ALA | GLN | ALA | GLU | TRP | HIS | GLU | ||||
| 8 | GLN | ALA | GLU | LYS | VAL | GLU | ALA | TYR | LEU | VAL | ||||
| 9 | GLU | LYS | GLN | ASP | PRO | THR | ASP | ILE | LYS | TYR | ||||
| 10 | LYS | ASP | ASN | ASP | GLY | HIS | THR | ASP | ALA | ILE | ||||
| 11 | SER | GLY | ALA | THR | ILE | LYS | VAL | LYS | LYS | PHE | ||||
| 12 | PHE | ASP | LEU | ALA | GLN | LYS | ALA | LEU | LYS | ASP | ||||
| 13 | ALA | GLU | LYS | LEU | GLU | HIS | HIS | HIS | HIS | HIS | ||||
| 14 | HIS |
Samples:
NC: CmR116, [U-100% 13C; U-100% 15N], 0.97 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; H2O 90%; D2O 10%
NC5: CmR116, [U-5% 13C; U-100% 15N], 1.0 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; H2O 90%; D2O 10%
NC5-RDC: CmR116, [U-5% 13C; U-100% 15N], 1.0 mM; sodium azide 0.02%; DTT 10 mM; calcium chloride 5 mM; sodium chloride 100 mM; MES 20 mM; PEG 4%; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.5; pressure: 1 .; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC5-RDC | anisotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement, structure solution
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
PROSA, Guntert - processing
CARA v1.8, Keller et al. - chemical shift assignment, data analysis, peak picking
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| EMBL | CDG36832 |
| GB | ABN53514 ADU75963 EEU01223 EFB38080 EIC03805 |
| REF | WP_003513428 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts