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1H, 13C, and 15N Chemical Shift Assignments for DnaG-C
Authors
Oakley, A.J., Loscha, K.V., Schaeffer, P.M., Liepinsh, E., Pintacuda, G., Wilce, M.C.J., Otting, G., Dixon, N.E.
Assembly
DnaG-C
Entity
1. DnaG-C (polymer, Thiol state: all free), 148 monomers, 16700.82 Da Detail

AAESGVSRPV PQLKRTTMRI LIGLLVQNPE LATLVPPLEN LDENKLPGLG LFRELVNTCL SQPGLTTGQL LEHYRGTNNA ATLEKLSMWD DIADKNIAEQ TFTDSLNHMF DSLLELRQEE LIARERTHGL SNEERLELWT LNQELAKK


Formula weight
16700.82 Da
Source organism
Escherichia coli
Exptl. method
NMR
Refine. method
torsion angle dynamics
Data set
assigned_chemical_shifts
Chem. Shift Complete1
Sequence coverage: 99.3 %, Completeness: 57.1 %, Completeness (bb): 98.7 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All57.1 % (993 of 1738)42.7 % (387 of 907)66.5 % (446 of 671)100.0 % (160 of 160)
Backbone98.7 % (863 of 874)99.7 % (296 of 297)97.7 % (426 of 436)100.0 % (141 of 141)
Sidechain26.4 % (265 of 1004)15.2 % (93 of 610)40.8 % (153 of 375)100.0 % (19 of 19)
Aromatic12.2 % (9 of 74)18.9 % (7 of 37) 0.0 % (0 of 35)100.0 % (2 of 2)
Methyl18.0 % (35 of 194)15.5 % (15 of 97)20.6 % (20 of 97)

1. DnaG-C

AAESGVSRPV PQLKRTTMRI LIGLLVQNPE LATLVPPLEN LDENKLPGLG LFRELVNTCL SQPGLTTGQL LEHYRGTNNA ATLEKLSMWD DIADKNIAEQ TFTDSLNHMF DSLLELRQEE LIARERTHGL SNEERLELWT LNQELAKK

Sample

Temperature 298 (±1) K, pH 6 (±0.1)


#NameIsotope labelingTypeConcentration
1DnaG-C[U-90% 13C; U-15N]0.6 mM
2phosphate buffer10 mM
3DTT1 mM
4NaCl100 mM
5NaN30.1 %

Chem. Shift Complete2
Sequence coverage: 98.0 %, Completeness: 66.8 %, Completeness (bb): 88.7 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All66.8 % (2321 of 3476)64.8 % (1175 of 1814)62.7 % (842 of 1342)95.0 % (304 of 320)
Backbone88.7 % (1550 of 1748)96.5 % (573 of 594)79.9 % (697 of 872)99.3 % (280 of 282)
Sidechain50.9 % (1022 of 2008)49.5 % (604 of 1220)52.5 % (394 of 750)63.2 % (24 of 38)
Aromatic29.7 % (44 of 148)55.4 % (41 of 74) 0.0 % (0 of 70)75.0 % (3 of 4)
Methyl53.1 % (206 of 388)53.6 % (104 of 194)52.6 % (102 of 194)

1. DnaG-C

AAESGVSRPV PQLKRTTMRI LIGLLVQNPE LATLVPPLEN LDENKLPGLG LFRELVNTCL SQPGLTTGQL LEHYRGTNNA ATLEKLSMWD DIADKNIAEQ TFTDSLNHMF DSLLELRQEE LIARERTHGL SNEERLELWT LNQELAKK

Sample

Temperature 298 (±1) K, pH 6 (±0.1)


#NameIsotope labelingTypeConcentration
6DnaG-C[U-90% 13C; U-15N]0.4 mM
7phosphate buffer10 mM
8DTT1 mM
9NaCl100 mM
10NaN30.1 %

LACS Plot; CA
Referencing offset: -0.18 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.18 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.06 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2HAJ, Strand ID: A Detail


Release date
2005-03-15
Citation
Crystal and solution structures of the helicase-binding domain of Escherichia coli primase
Oakley, A.J., Loscha, K.V., Schaeffer, P.M., Liepinsh, E., Pintacuda, G., Wilce, M.C.J., Otting, G., Dixon, N.E.
J. Biol. Chem. (2005), 280, 11495-11504, PubMed 15649896 , DOI 10.1074/jbc.M412645200 ,
Entries sharing articles Swiss-Prot: 1 entries Detail
  Swiss-Prot: P0ABS5 released on 1986-07-21
    Title DNAG_ECOLI Entity DNA primase
Related entities 1. DnaG-C, : 1 : 6 : 1 : 10 entities Detail
Experiments performed 1 experiments Detail
nullKeywords DnaB helicase, DnaG primase, NMR