BMRB Entry 31103
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31103
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Title: Solution structure for a putative Type I site-specific deoxyribonuclease from Neisseria gonorrhoeae (NCCP11945). Seattle Structural Genomics Center for Infectious Disease target NegoA.19201.a
Deposition date: 2023-08-27 Original release date: 2023-10-07
Authors: Buchko, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), .
Citation: Buchko, G.; van Voorhis, W.; Myler, P.. "Structural characterization of a putative Type I site-specific deoxyribonuclease from Neisseria gonorrhoeae (NCCP11945)." .
Assembly members:
entity_1, polymer, 115 residues, 14149.816 Da.
Natural source: Common Name: Neisseria gonorrhoeae Taxonomy ID: 521006 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria gonorrhoeae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21
Entity Sequences (FASTA):
entity_1: MAHHHHHHMFLDDVNVFLDD
LNTNPITDEWYMSNFADKHI
KILESYEAFDILKQFVDYMI
EEHDEKSEYEIMEILRQLKY
QADTNEKFYTNTQKQKIVEL
YKQEISQDILNEIFR
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 418 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 646 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
Entities:
Entity 1, unit_1 115 residues - 14149.816 Da.
| 1 | MET | ALA | HIS | HIS | HIS | HIS | HIS | HIS | MET | PHE | ||||
| 2 | LEU | ASP | ASP | VAL | ASN | VAL | PHE | LEU | ASP | ASP | ||||
| 3 | LEU | ASN | THR | ASN | PRO | ILE | THR | ASP | GLU | TRP | ||||
| 4 | TYR | MET | SER | ASN | PHE | ALA | ASP | LYS | HIS | ILE | ||||
| 5 | LYS | ILE | LEU | GLU | SER | TYR | GLU | ALA | PHE | ASP | ||||
| 6 | ILE | LEU | LYS | GLN | PHE | VAL | ASP | TYR | MET | ILE | ||||
| 7 | GLU | GLU | HIS | ASP | GLU | LYS | SER | GLU | TYR | GLU | ||||
| 8 | ILE | MET | GLU | ILE | LEU | ARG | GLN | LEU | LYS | TYR | ||||
| 9 | GLN | ALA | ASP | THR | ASN | GLU | LYS | PHE | TYR | THR | ||||
| 10 | ASN | THR | GLN | LYS | GLN | LYS | ILE | VAL | GLU | LEU | ||||
| 11 | TYR | LYS | GLN | GLU | ILE | SER | GLN | ASP | ILE | LEU | ||||
| 12 | ASN | GLU | ILE | PHE | ARG |
Samples:
sample_1: N1, [U-99% 13C; U-99% 15N], 0.8 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.2 mM; DTT 1 ± 0.1 mM
sample_2: N1, [U-99% 15N], 0.8 ± 0.2 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.2 mM; DTT 1 ± 0.1 mM
sample_3: N1, [U-10% 13C; U-99% 15N], 0.5 ± 0.1 mM; sodium chloride 100 ± 2 mM; TRIS 20 ± 0.2 mM; DTT 1 ± 0.1 mM
sample_conditions_1: ionic strength: 120 mM; pH: 7; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-13C HSQC | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | anisotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | anisotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | anisotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | anisotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | anisotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | anisotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | anisotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_3 | anisotropic | sample_conditions_1 |
Software:
Felix v2017, Accelrys Software Inc. - processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.5, Bhattacharya and Montelione - data analysis
TALOS+, Cornilescu, Delaglio and Bax - data analysis
Poky, Manthey, Tonelli, Clos II, Rahimi, Markley, Lee - data analysis
NMR spectrometers:
- Agilent VNMRS 600 MHz
- Bruker AVANCE III 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts