BMRB Entry 15614
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15614
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Title: Solution structure of the complex between E.coli NusA-AR2 and RNAP-aCTD
Deposition date: 2008-01-02 Original release date: 2009-11-03
Authors: Prasch, Stefan; Schweimer, Kristian; Roesch, Paul
Citation: Prasch, Stefan; Schweimer, Kristian; Roesch, Paul. "structural basis of transcription elongation control: the NusA-aCTD complex" . ., .-..
Assembly members:
actd, polymer, 99 residues, 9014.511 Da.
ar2, polymer, 74 residues, 7470.336 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
actd: GPDLRDVRQPEVKEEKPEFD
PILLRPVDDLELTVRSANCL
KAEAIHYIGDLVQRTEVELL
KTPNLGKKSLTEIKDVLASR
GLSLGMRLENWPPASIADE
ar2: GPSLGDNKPADDLLNLEGVD
RDLAFKLAARGVCTLEDLAE
QGIDDLADIEGLTDEKAGAL
IMAARNICWFGDEA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 540 |
| 15N chemical shifts | 170 |
| 1H chemical shifts | 1176 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 99 residues - 9014.511 Da.
| 1 | GLY | PRO | ASP | LEU | ARG | ASP | VAL | ARG | GLN | PRO | ||||
| 2 | GLU | VAL | LYS | GLU | GLU | LYS | PRO | GLU | PHE | ASP | ||||
| 3 | PRO | ILE | LEU | LEU | ARG | PRO | VAL | ASP | ASP | LEU | ||||
| 4 | GLU | LEU | THR | VAL | ARG | SER | ALA | ASN | CYS | LEU | ||||
| 5 | LYS | ALA | GLU | ALA | ILE | HIS | TYR | ILE | GLY | ASP | ||||
| 6 | LEU | VAL | GLN | ARG | THR | GLU | VAL | GLU | LEU | LEU | ||||
| 7 | LYS | THR | PRO | ASN | LEU | GLY | LYS | LYS | SER | LEU | ||||
| 8 | THR | GLU | ILE | LYS | ASP | VAL | LEU | ALA | SER | ARG | ||||
| 9 | GLY | LEU | SER | LEU | GLY | MET | ARG | LEU | GLU | ASN | ||||
| 10 | TRP | PRO | PRO | ALA | SER | ILE | ALA | ASP | GLU |
Entity 2, entity_2 74 residues - 7470.336 Da.
| 1 | GLY | PRO | SER | LEU | GLY | ASP | ASN | LYS | PRO | ALA | ||||
| 2 | ASP | ASP | LEU | LEU | ASN | LEU | GLU | GLY | VAL | ASP | ||||
| 3 | ARG | ASP | LEU | ALA | PHE | LYS | LEU | ALA | ALA | ARG | ||||
| 4 | GLY | VAL | CYS | THR | LEU | GLU | ASP | LEU | ALA | GLU | ||||
| 5 | GLN | GLY | ILE | ASP | ASP | LEU | ALA | ASP | ILE | GLU | ||||
| 6 | GLY | LEU | THR | ASP | GLU | LYS | ALA | GLY | ALA | LEU | ||||
| 7 | ILE | MET | ALA | ALA | ARG | ASN | ILE | CYS | TRP | PHE | ||||
| 8 | GLY | ASP | GLU | ALA |
Samples:
sample_1: actd, [U-98% 13C; U-98% 15N], 0.7 mM; ar2 2.1 mM; potassium phosphate 10 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM
sample_2: ar2, [U-98% 13C; U-98% 15N], 0.7 mM; actd 2.1 mM; potassium phosphate 10 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM
sample_conditions_1: pH: 6.4; 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 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAA11840 BAB37583 BAE75528 BAE77996 BAG79094 BAB37473 BAE77215 BAG78979 BAI27449 BAI32628 |
| EMBL | CAA25337 CAA26395 CAA37838 CAA37839 CAD09171 CAA25200 CAP77631 CAQ33504 CAQ90641 CAR00133 |
| GB | AAA24577 AAA27214 AAA58092 AAC76320 AAG58416 AAA57972 AAC76203 AAG58305 AAN44677 AAN82367 |
| PIR | AB1009 |
| REF | NP_312187 NP_417754 NP_458485 NP_462319 NP_709083 NP_289745 NP_312077 NP_417638 NP_708970 NP_755793 |
| SP | A0KF45 A1AGI6 A1JS01 A4SSY1 A4TH15 P0AFF6 P0AFF7 P0AFF8 P0AFF9 |
| BMRB | 5800 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts