BMRB Entry 17414
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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/BMR17414
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Title: Structure of an engineered splicing intein mutant based on Mycobacterium tuberculosis RecA PubMed: 21604815
Deposition date: 2011-01-19 Original release date: 2012-01-04
Authors: Du, Zhenming; Wang, Chunyu
Citation: Du, Zhenming; Zheng, Yuchuan; Liu, Yangzhong; Belfort, Marlene; Wang, Chunyu. "pK(a) coupling at the intein active site: implications for the coordination mechanism of protein splicing with a conserved aspartate" J. Am. Chem. Soc. 133, 10275-10282 (2011).
Assembly members:
RecA, polymer, 139 residues, 15365.621 Da.
Natural source: Common Name: high GC Gram+ Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RecA: CLAEGTRIFDPVTGTTHRIE
DVVGGRKPIHVVAAAKDGTL
HARPVVSWFDQGTRDVIGLR
IAGGAILWATPDHKVLTEYG
WRAAGELRKGDRVAVRDVET
GELRYSVIREVLPTRRARTF
DLEVEELHTLVAEGVVVHN
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 288 |
| 15N chemical shifts | 137 |
| 1H chemical shifts | 904 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | RecA | 1 |
Entities:
Entity 1, RecA 139 residues - 15365.621 Da.
| 1 | CYS | LEU | ALA | GLU | GLY | THR | ARG | ILE | PHE | ASP | ||||
| 2 | PRO | VAL | THR | GLY | THR | THR | HIS | ARG | ILE | GLU | ||||
| 3 | ASP | VAL | VAL | GLY | GLY | ARG | LYS | PRO | ILE | HIS | ||||
| 4 | VAL | VAL | ALA | ALA | ALA | LYS | ASP | GLY | THR | LEU | ||||
| 5 | HIS | ALA | ARG | PRO | VAL | VAL | SER | TRP | PHE | ASP | ||||
| 6 | GLN | GLY | THR | ARG | ASP | VAL | ILE | GLY | LEU | ARG | ||||
| 7 | ILE | ALA | GLY | GLY | ALA | ILE | LEU | TRP | ALA | THR | ||||
| 8 | PRO | ASP | HIS | LYS | VAL | LEU | THR | GLU | TYR | GLY | ||||
| 9 | TRP | ARG | ALA | ALA | GLY | GLU | LEU | ARG | LYS | GLY | ||||
| 10 | ASP | ARG | VAL | ALA | VAL | ARG | ASP | VAL | GLU | THR | ||||
| 11 | GLY | GLU | LEU | ARG | TYR | SER | VAL | ILE | ARG | GLU | ||||
| 12 | VAL | LEU | PRO | THR | ARG | ARG | ALA | ARG | THR | PHE | ||||
| 13 | ASP | LEU | GLU | VAL | GLU | GLU | LEU | HIS | THR | LEU | ||||
| 14 | VAL | ALA | GLU | GLY | VAL | VAL | VAL | HIS | ASN |
Samples:
sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 1 mM; entity, [U-98% 13C; U-98% 15N], 0.15 – 0.2 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker ARX 800 MHz
- Bruker ARX 600 MHz
Related Database Links:
| BMRB | 15560 16634 |
| PDB | |
| EMBL | CFR77613 CMM98736 |
| GB | EPZ65824 KAM73204 |
| REF | WP_049963343 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts