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Amide chemical shifts of mature human SUMO-1
Authors
McIntosh, L.P.
Assembly
SUMO-1
Entity
1. SUMO-1 (polymer, Thiol state: all free), 100 monomers, 11413.67 Da Detail

GSHMSDQEAK PSTEDLGDKK EGEYIKLKVI GQDSSEIHFK VKMTTHLKKL KESYCQRQGV PMNSLRFLFE GQRIADNHTP KELGMEEEDV IEVYQEQTGG


Formula weight
11413.67 Da
Source organism
Homo sapiens
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 93.0 %, Completeness: 26.3 %, Completeness (bb): 61.7 % Detail

Polymer type: polypeptide(L)

Total1H15N
All26.3 % (192 of 731)15.8 % (99 of 625)87.7 % (93 of 106)
Backbone61.7 % (187 of 303)45.6 % (94 of 206)95.9 % (93 of 97)
Sidechain 1.2 % (5 of 428) 1.2 % (5 of 419) 0.0 % (0 of 9)
Aromatic 0.0 % (0 of 35) 0.0 % (0 of 35)
Methyl 4.9 % (2 of 41) 4.9 % (2 of 41)

1. SUMO-1

GSHMSDQEAK PSTEDLGDKK EGEYIKLKVI GQDSSEIHFK VKMTTHLKKL KESYCQRQGV PMNSLRFLFE GQRIADNHTP KELGMEEEDV IEVYQEQTGG

Sample

Temperature 290 (±0) K, pH 6.5 (±0.1)


#NameIsotope labelingTypeConcentration
1SUMO-1
2KCl100 mM
3KPhos10 mM
4DTT2 mM
5D2O10 %

Release date
2004-11-28
Citation
Structural and dynamic independence of isopeptide-linked RanGAP1 and SUMO-1
Macauley, M.S., Errington, W.J., Okon, M., Scharpf, M., Mackereth, C.D., Schulman, B.A., McIntosh, L.P.
J. Biol. Chem. (2004), 279, 49131-49137, PubMed 15355965 , DOI 10.1074/jbc.M408705200 ,
Related entities 1. SUMO-1, : 1 : 31 : 99 entities Detail
Interaction partners 1. SUMO-1, : 123 interactors Detail
Experiments performed 3 experiments Detail
Chemical shift validation 3 contents Detail
Keywords sumo, ubiquitin-like protein