BMRB Entry 26909

Title:
N-terminal domain of the E. coli DNA polymerase III delta subunit
Deposition date:
2016-09-26
Original release date:
2017-05-24
Authors:
Alyami, Esmael; Rizzo, Alessandro; Korzhnev, Dmitry
Citation:

Citation: Alyami, Esmael; Rizzo, Alessandro; Beuning, Penny; Korzhnev, Dmitry. "NMR resonance assignments for the N-terminal domain of the delta subunit of the E. coli gamma clamp loader complex"  Biomol. NMR Assignments 11, 169-173 (2017).
PubMed: 28265855

Assembly members:

Assembly members:
E_coli_DNA_polymerase_III_delta_subunit_(residues_1-140), polymer, 143 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28b+

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts587
15N chemical shifts148
1H chemical shifts953

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1E coli DNA polymerase III delta subunit (residues 1-140)1

Entities:

Entity 1, E coli DNA polymerase III delta subunit (residues 1-140) 143 residues - Formula weight is not available

GSH are cloning artifacts. The native residues are M1-Q140

1   GLYSERHISMETILEARGLEUTYRPROGLU
2   GLNLEUARGALAGLNLEUASNGLUGLYLEU
3   ARGALAALATYRLEULEULEUGLYASNASP
4   PROLEULEULEUGLNGLUSERGLNASPALA
5   VALARGGLNVALALAALAALAGLNGLYPHE
6   GLUGLUHISHISTHRPHESERILEASPPRO
7   ASNTHRASPTRPASNALAILEPHESERLEU
8   CYSGLNALAMETSERLEUPHEALASERARG
9   GLNTHRLEULEULEULEULEUPROGLUASN
10   GLYPROASNALAALAILEASNGLUGLNLEU
11   LEUTHRLEUTHRGLYLEULEUHISASPASP
12   LEULEULEUILEVALARGGLYASNLYSLEU
13   SERLYSALAGLNGLUASNALAALATRPPHE
14   THRALALEUALAASNARGSERVALGLNVAL
15   THRCYSGLN

Samples:

sample_1: E coli DNA polymerase III delta subunit (residues 1-140), [U-13C; U-15N], 1.5 mM; D2O 7.5%; sodium phosphate 20 mM; NaCl 100 mM; DTT 10 mM; EDTA 1 mM; sodium azide 0.05 % v/v; Halt protease inhibitor cocktail 0.33 % v/v

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(Ca)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1

Software:

Analysis, CCPN - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMRJ, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Agilent VNMRS 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks