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Chemical Shift Assignment of the PP1 and Microtubule binding domain of human KNL-1
Authors
Bajaj, R., Page, R., Peti, W.
Assembly
N terminal 80 residues of of KNL-1
Entity
1. N terminal 80 residues of of KNL-1 (polymer, Thiol state: all free), 84 monomers, 9490.531 Da Detail

GAMGMDGVSS EANEENDNIE RPVRRRHSSI LKPPRSPLQD LRGGNETVQE SNALRNKKNS RRVSFADTIK VFQTESHMKI VRKS


Formula weight
9490.531 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.4 %, Completeness: 41.9 %, Completeness (bb): 64.7 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All41.9 % (406 of 970)18.0 % (93 of 518)64.9 % (235 of 362)86.7 % (78 of 90)
Backbone64.7 % (321 of 496)48.5 % (82 of 169)65.2 % (161 of 247)97.5 % (78 of 80)
Sidechain29.3 % (162 of 553) 3.2 % (11 of 349)77.8 % (151 of 194) 0.0 % (0 of 10)
Aromatic 0.0 % (0 of 28) 0.0 % (0 of 14) 0.0 % (0 of 14)
Methyl50.0 % (35 of 70) 5.7 % (2 of 35)94.3 % (33 of 35)

1. KNL-1

GAMGMDGVSS EANEENDNIE RPVRRRHSSI LKPPRSPLQD LRGGNETVQE SNALRNKKNS RRVSFADTIK VFQTESHMKI VRKS

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 283 K, pH 6.5


#NameIsotope labelingTypeConcentration
1KNL-1[U-98% 13C; U-98% 15N]0.6 mM
2HEPESnatural abundance10 mM
3Sodium cloridenatural abundance50 mM

LACS Plot; CA
Referencing offset: 0.13 ppm, Outliers: 2 Detail
LACS Plot; CB
Referencing offset: 0.13 ppm, Outliers: 2 Detail
Release date
2017-03-26
Citation
KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive
Bajaj, R., Bollen, M., Peti, W., Page, R.
Structure (2018), 26, 1327-11336, PubMed 30100357 , DOI 10.1016/j.str.2018.06.013 ,
Related entities 1. N terminal 80 residues of of KNL-1, : 2 : 6 entities Detail
Interaction partners 1. N terminal 80 residues of of KNL-1, : 41 interactors Detail
Experiments performed 6 experiments Detail
Chemical shift validation 3 contents Detail
Keywords KNL-1, Kinetochore, Microtubule binding, Protein phosphatase1, cell cycle