Search

1H, 15N and 13C resonance assignments of the N-terminal region of calponin
Authors
Bramham, J., Smith, B.O., Uhrin, D., Barlow, P.N., Winder, S.J.
Assembly
calponin CH domain
Entity
1. calponin CH domain (polymer, Thiol state: all free), 108 monomers, 12249.81 Da Detail

MPQTERQLRV WIEGATGRRI GDNFMDGLKD GVILCELINK LQPGSVQKVN DPVQNWHKLE NIGNFLRAIK HYGVKPHDIF EANDLFENTN HTQVQSTLIA LASQAKTK


Formula weight
12249.81 Da
Source organism
Gallus gallus
Exptl. method
NMR
Refine. method
SIMULATED ANNEALING
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 100.0 %, Completeness: 97.1 %, Completeness (bb): 96.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All97.1 % (1254 of 1291)96.6 % (653 of 676)98.2 % (483 of 492)95.9 % (118 of 123)
Backbone96.9 % (620 of 640)95.9 % (211 of 220)98.1 % (310 of 316)95.2 % (99 of 104)
Sidechain97.7 % (734 of 751)96.9 % (442 of 456)98.9 % (273 of 276)100.0 % (19 of 19)
Aromatic93.2 % (82 of 88)93.2 % (41 of 44)92.9 % (39 of 42)100.0 % (2 of 2)
Methyl100.0 % (124 of 124)100.0 % (62 of 62)100.0 % (62 of 62)

1. calponin CH domain

MPQTERQLRV WIEGATGRRI GDNFMDGLKD GVILCELINK LQPGSVQKVN DPVQNWHKLE NIGNFLRAIK HYGVKPHDIF EANDLFENTN HTQVQSTLIA LASQAKTK

Sample

Temperature 291 K


#NameIsotope labelingTypeConcentration
1calponin CH domain[U-99% 15N; U-98% 15N]1.0 mM

LACS Plot; CA
Referencing offset: -0.26 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.26 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.03 ppm, Outliers: 2 Detail
LACS Plot; CO
Referencing offset: -0.61 ppm, Outliers: 5 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 1H67, Strand ID: A Detail


Release date
2001-02-26
Citation 1
Letter to the Editor: 1H, 15N and 13C resonance assignments of the N-terminal region of calponin
Bramham, J., Smith, B.O., Uhrin, D., Barlow, P.N., Winder, S.J.
J. Biomol. NMR (2001), 19, 189-190, PubMed , DOI:
Citation 2
1H, 13C and 15N chemical shift referencing in biomolecular NMR
Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L., Sykes, B.D.
J. Biomol. NMR (1995), 6, 135-140, PubMed 8589602 , DOI: ,
Related entities 1. calponin CH domain, : 1 : 2 : 133 entities Detail
Interaction partners 1. calponin CH domain, : 1 interactors Detail
Experiments performed 10 experiments Detail
nullKeywords calponin, CH domain, NMR, chemical shift