BMRB Entry 11525

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain
Deposition date:
2013-04-24
Original release date:
2013-08-05
Authors:
Aramaki, Takahiko; Abe, Yoshito; Katayama, Tsutomu; Ueda, Tadashi
Citation:

Citation: Aramaki, Takahiko; Abe, Yoshito; Katayama, Tsutomu; Ueda, Tadashi. "Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli"  Protein Sci. ., .-..
PubMed: 23868391

Assembly members:

Assembly members:
PriC_N-terminal_domain, polymer, 98 residues, 11007.640 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET22b(+)

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts423
15N chemical shifts112
1H chemical shifts696

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PriC_N-terminal_domain1

Entities:

Entity 1, PriC_N-terminal_domain 98 residues - 11007.640 Da.

1   METLYSTHRALALEULEULEUGLULYSLEU
2   GLUGLYGLNLEUALATHRLEUARGGLNARG
3   CYSALAPROVALSERGLNPHEALATHRLEU
4   SERALAARGPHEASPARGHISLEUPHEGLN
5   THRARGALATHRTHRLEUGLNALACYSLEU
6   ASPGLUALAGLYASPASNLEUALAALALEU
7   ARGHISALAVALGLUGLNGLNGLNLEUPRO
8   GLNVALALATRPLEUALAGLUHISLEUALA
9   ALAGLNLEUGLUALAILEALAARGGLUALA
10   SERALATRPSERLEUARGGLUTRP

Samples:

sample_1: PriC N-terminal domain, [U-99% 13C; U-99% 15N], 0.5 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_2: PriC N-terminal domain, [U-98% 15N], 0.2 mM; sodium chloride 150 mM; D2O 100%

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

Olivia v1.16.6, Olivia Developer Team - chemical shift assignment, data analysis

CNS v1.21, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA03055 BAB33943 BAE76246 BAG76016 BAI23841
EMBL CAP75000 CAQ30940 CAQ97342 CAR01811 CAR06700
GB AAB40221 AAC73569 AAN42067 AAN79064 AAP15944
REF NP_308547 NP_415000 NP_706360 WP_000626986 WP_000844845
SP P23862
AlphaFold P23862

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