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Backbone 1H, 13C, and 15N Chemical Shift Assignments for PriC N-terminal domain
Authors
Aramaki, T., Abe, Y., Katayama, T., Ueda, T.
Assembly
PriC N-temrinal domain
Entity
1. PriC N-temrinal domain (polymer, Thiol state: all free), 98 monomers, 10994.43 Da Detail

MKTALLLEKL EGQLATLRQR CAPVSQFATL SARFDRHLFQ TRATTLQACL DEAGDNLAAL RHAVEQQQLP QVAWLAEHLA AQLEAIAREA SAWSLREW


Formula weight
10994.43 Da
Source organism
Escherichia coli
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.0 %, Completeness: 95.5 %, Completeness (bb): 96.6 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All95.5 % (1085 of 1136)95.4 % (559 of 586)95.5 % (420 of 440)96.4 % (106 of 110)
Backbone96.6 % (564 of 584)96.4 % (189 of 196)96.9 % (283 of 292)95.8 % (92 of 96)
Sidechain94.8 % (614 of 648)94.9 % (370 of 390)94.3 % (230 of 244)100.0 % (14 of 14)
Aromatic84.6 % (66 of 78)84.6 % (33 of 39)83.3 % (30 of 36)100.0 % (3 of 3)
Methyl97.8 % (131 of 134)98.5 % (66 of 67)97.0 % (65 of 67)

1. PriC N-terminal domain

MKTALLLEKL EGQLATLRQR CAPVSQFATL SARFDRHLFQ TRATTLQACL DEAGDNLAAL RHAVEQQQLP QVAWLAEHLA AQLEAIAREA SAWSLREW

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6.0


#NameIsotope labelingTypeConcentration
1PriC N-terminal domain[U-99% 13C; U-99% 15N]protein0.5 mM
2sodium chloridenatural abundance150 mM
3H2Osolvent90 %
4D2Osolvent10 %

LACS Plot; CA
Referencing offset: -0.1 ppm, Outliers: 3 Detail
LACS Plot; CB
Referencing offset: -0.1 ppm, Outliers: 3 Detail
LACS Plot; HA
Referencing offset: 0.03 ppm, Outliers: 1 Detail
LACS Plot; CO
Referencing offset: -0.32 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2RT6, Strand ID: A Detail


Release date
2013-08-04
Citation
Solution structure of the N-terminal domain of a replication restart primosome factor, PriC, in Escherichia coli
Aramaki, T., Abe, Y., Katayama, T., Ueda, T.
Protein Sci. (2013), 22, 1279-1286, PubMed 23868391 , DOI 10.1002/pro.2314 ,
Related entities 1. PriC N-temrinal domain, : 1 : 2 : 3 entities Detail
Interaction partners 1. PriC N-temrinal domain, : 20 interactors Detail
Experiments performed 18 experiments Detail
NMR combined restraints 5 contents Detail
Keywords PriC, Primosome, Protein structure, Replication restart