BMRB Entry 50115
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50115
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone 13C, and 15N Chemical Shift Assignments for ChiZ N-terminal Domain
Deposition date: 2019-12-06 Original release date: 2020-06-23
Authors: Escobar, Cristian; Cross, Timothy
Citation: Hicks, Alan; Escobar, Cristian; Cross, Timothy; Zhou, Huan-Xiang. "Sequence-Dependent Correlated Segments in the Intrinsically Disordered Region of ChiZ" Biomolecules 10, 946-946 (2020).
Assembly members:
entity_1, polymer, 67 residues, Formula weight is not available
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pTBSG1
Entity Sequences (FASTA):
entity_1: SNAMTPVRPPHTPDPLNLRG
PLDGPRWRRAEPAQSRRPGR
SRPGGAPLRYHRTGVGMSRT
GHGSRPV
- H_exch_rates
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
Data type | Count |
13C chemical shifts | 183 |
15N chemical shifts | 52 |
1H chemical shifts | 52 |
H exchange rates | 50 |
T1 relaxation values | 50 |
T2 relaxation values | 50 |
heteronuclear NOE values | 52 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | N-terminal domain | 1 |
Entities:
Entity 1, N-terminal domain 67 residues - Formula weight is not available
ChiZ residues 1 to 64 plus first 3 residues (SNA) left from TEV protease cleavage site. Residues 1-64 correspond to the cytoplasmatic soluble domain of ChiZ membrane protein.
1 | SER | ASN | ALA | MET | THR | PRO | VAL | ARG | PRO | PRO | ||||
2 | HIS | THR | PRO | ASP | PRO | LEU | ASN | LEU | ARG | GLY | ||||
3 | PRO | LEU | ASP | GLY | PRO | ARG | TRP | ARG | ARG | ALA | ||||
4 | GLU | PRO | ALA | GLN | SER | ARG | ARG | PRO | GLY | ARG | ||||
5 | SER | ARG | PRO | GLY | GLY | ALA | PRO | LEU | ARG | TYR | ||||
6 | HIS | ARG | THR | GLY | VAL | GLY | MET | SER | ARG | THR | ||||
7 | GLY | HIS | GLY | SER | ARG | PRO | VAL |
Samples:
sample_1: entity_1, [U-13C; U-15N], 1 mM; sodium phosphate 20 mM; DSS 50 uM; D2O 10 % v/v; sodium chloride 25 mM
sample_conditions_1: ionic strength: 45 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
15N-(1H) NOE | sample_1 | isotropic | sample_conditions_1 |
Het. Nuc. T1 relaxation | sample_1 | isotropic | sample_conditions_1 |
Het. Nuc. T2 relaxation | sample_1 | isotropic | sample_conditions_1 |
CLEANEX-PM (15N-HSQC) | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - processing
CcpNMR v2.4.2, CCPN - chemical shift assignment
NMR spectrometers:
- Bruker Avance 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts