Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for SENP1 Catalytic Domain

Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding.

The first 14 residues (MHHHHHHENLYFQG) at the N-terminus represent a non-native
His-tag and TEV recognition sequence. The residues that follow represent the
catalytic domain of human sentrin-specific protease 1 (SENP1) E419 to L644.

The Structure Of Senp1 Sumo-2 Co-Complex Suggests A Structural Basis For Discrimination Between Sumo Paralogues During Processi

Crystal Structure Of Human Senp1 Mutant (C603s) In Complex With Sumo-1

Crystal Structure Of Human Senp1 With The Bound Cobalt

Detection Of Cobalt In Previously Unassigned Human Senp1 Structure

sentrin/SUMO-specific protease [Homo sapiens]

SUMO1/sentrin specific peptidase 1 [Mus musculus]

SUMO1/sentrin specific peptidase 1 [Homo sapiens]

SUMO1/sentrin specific peptidase 1, isoform CRA_a [Homo sapiens]

sentrin-specific protease 1 [Pongo abelii]

sentrin-specific protease 1 [Bos taurus]

sentrin-specific protease 1 [Homo sapiens]

sentrin-specific protease 1 [Mus musculus]

RecName: Full=Sentrin-specific protease 1; AltName: Full=SUMO-1 protease 2; Short=SuPr-2; AltName: Full=Sentrin/SUMO-specific p

RecName: Full=Sentrin-specific protease 1; AltName: Full=Sentrin/SUMO-specific protease SENP1

TPA: SUMO1/sentrin specific peptidase 1 [Bos taurus]

Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for Mutant SENP1 C603S Catalytic Domain

For stereospecific assignments of Val/Leu methyls

U-13C, U-15N, U-2H sample contained selective 1H at Val and Leu methyl groups. 6M GuHCl unfolded and refolded in NMR buffer