BMRB Entry 15086
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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/BMR15086
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Title: Solution NMR structure of Hypothetical Protein Cgl2762 from Corynebacterium Glutamicum: Northeast Structural Genomics Consortium Target CgR3 PubMed: 18175328
Deposition date: 2006-12-28 Original release date: 2007-02-23
Authors: Singarapu, Kiran Kumar; sukumaran, Dinesh; Parish, David; Chen, Chen; Kellie, Cunningham; Rong, Xiao; G V T, Swapna; Montelione, Gaetano; Szyperski, Thomas
Citation: Singarapu, Kiran Kumar; Xiao, Rong; Sukumaran, Dinesh; Acton, Thomas; Montelione, Gaetano; Szyperski, Thomas. "NMR structure of protein Cgl2762 from Corynebacterium glutamicum implicated in DNA transposition reveals a helix-turn-helix motif attached to a flexibly disordered leucine zipper." Proteins 70, 1650-1654 (2008).
Assembly members:
hypothetical_protein_Cgl2762, polymer, 97 residues, 11048.383 Da.
Natural source: Common Name: Corynebacterium glutamicum Taxonomy ID: 1718 Superkingdom: Bacteria Kingdom: not available Genus/species: Corynebacterium glutamicum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
hypothetical_protein_Cgl2762: MPTKTYSEEFKRDAVALYEN
SDGASLQQIANDLGINRVTL
KNWIIKYGSNHNVQGTTPSA
AVSEAEQIRQLKKENALQRA
RTRHPAESCLEHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 411 |
15N chemical shifts | 108 |
1H chemical shifts | 671 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | hypothetical protein Cgl2762 | 1 |
Entities:
Entity 1, hypothetical protein Cgl2762 97 residues - 11048.383 Da.
1 | MET | PRO | THR | LYS | THR | TYR | SER | GLU | GLU | PHE | ||||
2 | LYS | ARG | ASP | ALA | VAL | ALA | LEU | TYR | GLU | ASN | ||||
3 | SER | ASP | GLY | ALA | SER | LEU | GLN | GLN | ILE | ALA | ||||
4 | ASN | ASP | LEU | GLY | ILE | ASN | ARG | VAL | THR | LEU | ||||
5 | LYS | ASN | TRP | ILE | ILE | LYS | TYR | GLY | SER | ASN | ||||
6 | HIS | ASN | VAL | GLN | GLY | THR | THR | PRO | SER | ALA | ||||
7 | ALA | VAL | SER | GLU | ALA | GLU | GLN | ILE | ARG | GLN | ||||
8 | LEU | LYS | LYS | GLU | ASN | ALA | LEU | GLN | ARG | ALA | ||||
9 | ARG | THR | ARG | HIS | PRO | ALA | GLU | SER | CYS | LEU | ||||
10 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: hypothetical protein Cgl2762, [U-100% 13C; U-100% 15N], 1.2 ± 0.2 mM
sample_conditions_1: ionic strength: 100 mM; pH: 4.4; 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 |
4,3D GFT HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
4,3D GFT CABCACONNH | sample_1 | isotropic | sample_conditions_1 |
4,3D GFT HABCABCONNH | sample_1 | isotropic | sample_conditions_1 |
4,3D GFT HCCH TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 13C,15N simulatanious NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
DYANA v1.5, Guntert, Braun and Wuthrich - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement
AutoStruct v2.0, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - data analysis
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR, Varian - collection
NMR spectrometers:
- Varian INOVA 750 MHz
Related Database Links:
PDB | |
DBJ | BAC00156 |
EMBL | CAF20784 CCH25886 |
GB | AGT06475 |
REF | NP_601957 WP_011015358 |
Download simulated HSQC data in one of the following formats:
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