BMRB Entry 19027
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19027
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for rubredoxin type protein from Mycobacterium ulcerans
Deposition date: 2013-02-11 Original release date: 2013-03-12
Authors: Barnwal, Ravi P; Varani, Gabriele
Citation: Barnwal, Ravi P; Varani, Gabriele. "Backbone 1H, 13C, and 15N Chemical Shift Assignments for rubredoxin type protein from Mycobacterium ulcerans" To be Published ., .-..
Assembly members:
rubredoxin_type_protein, polymer, 56 residues, 6462.213 Da.
Natural source: Common Name: High GC Gram+ Taxonomy ID: 1809 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium ulcerans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
rubredoxin_type_protein: MTAYRCPVCDYTYDEGKGDP
REGFPAGTRWDQIPDDWCCP
DCSVREKVDFERMGGK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 206 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 286 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rubredoxin_type_protein | 1 |
Entities:
Entity 1, rubredoxin_type_protein 56 residues - 6462.213 Da.
| 1 | MET | THR | ALA | TYR | ARG | CYS | PRO | VAL | CYS | ASP | ||||
| 2 | TYR | THR | TYR | ASP | GLU | GLY | LYS | GLY | ASP | PRO | ||||
| 3 | ARG | GLU | GLY | PHE | PRO | ALA | GLY | THR | ARG | TRP | ||||
| 4 | ASP | GLN | ILE | PRO | ASP | ASP | TRP | CYS | CYS | PRO | ||||
| 5 | ASP | CYS | SER | VAL | ARG | GLU | LYS | VAL | ASP | PHE | ||||
| 6 | GLU | ARG | MET | GLY | GLY | LYS |
Samples:
sample_1: rubredoxin type protein, [U-98% 15N], 1.2 mM; rubredoxin type protein, [U-95% 13C; U-95% 15N], 1.4 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 7; 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 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
TOPSPIN, Bruker Biospin - collection, processing
CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker AMX 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| EMBL | CDM75406 |
| GB | ABL04927 ACC39750 AGC61411 EPQ48959 EPQ70501 |
| REF | WP_011740542 WP_020788371 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts