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1H, 13C, 15N assignments of human Cofilin
Authors
Zierler-Gould, K.M., Pope, B.J., Weeds, A.G., Ball, L.J.
Assembly
Cofilin, non-muscle isoform
Entity
1. Cofilin, non-muscle isoform (polymer, Thiol state: all free), 166 monomers, 18502.27 Da Detail

MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL


Formula weight
18502.27 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.8 %, Completeness: 86.9 %, Completeness (bb): 84.5 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All86.9 % (1705 of 1961)94.6 % (971 of 1026)74.5 % (573 of 769)97.0 % (161 of 166)
Backbone84.5 % (831 of 984)97.0 % (325 of 335)71.6 % (350 of 489)97.5 % (156 of 160)
Sidechain90.9 % (1031 of 1134)93.8 % (648 of 691)86.3 % (377 of 437)100.0 % (6 of 6)
Aromatic88.6 % (101 of 114)96.5 % (55 of 57)80.4 % (45 of 56)100.0 % (1 of 1)
Methyl98.9 % (186 of 188)98.9 % (93 of 94)98.9 % (93 of 94)

1. cofilin

MASGVAVSDG VIKVFNDMKV RKSSTPEEVK KRKKAVLFCL SEDKKNIILE EGKEILVGDV GQTVDDPYAT FVKMLPDKDC RYALYDATYE TKESKKEDLV FIFWAPESAP LKSKMIYASS KDAIKKKLTG IKHELQANCY EEVKDRCTLA EKLGGSAVIS LEGKPL

Sample #1

Pressure 1 atm, Temperature 300 (±2) K, pH 6.0 (±0.2)


#NameIsotope labelingTypeConcentration
1cofilin[U-15N; U-13C]0.8 mM
2phosphate buffer10 mM
3H2O90 %
4D2O10 %
Sample #2

Pressure 1 atm, Temperature 300 (±2) K, pH 6.0 (±0.2)


#NameIsotope labelingTypeConcentration
5cofilin[U-15N]1 mM
6phosphate buffer10 mM
7H2O90 %
8D2O10 %

LACS Plot; CA
Referencing offset: -0.07 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.07 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: -0.05 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 1Q8G, Strand ID: A Detail


Release date
2004-11-14
Citation
Backbone and sidechain 1H, 13C and 15N resonance assignments of human cofilin
Zierler-Gould, K.M., Pope, B.J., Weeds, A.G., Ball, L.J.
J. Biomol. NMR (2004), 29, 429-430, PubMed 15213453 , DOI 10.1023/B:JNMR.0000032508.54841.0f ,
Related entities 1. Cofilin, non-muscle isoform, : 1 : 8 : 8 : 148 entities Detail
Interaction partners 1. Cofilin, non-muscle isoform, : 102 interactors Detail
Experiments performed 8 experiments Detail
nullKeywords cofilin/ADF, NMR, chemical shift, actin binding, cytoskeleton