BMRB Entry 19885

Name: Backbone 1H, 13C, and 15N; and VL 13CH3 Side-chain Chemical Shift Assignments for SENP1 Catalytic Domain
Published: 2014-09-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19885

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

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

Deposition date:

2014-04-01

Original release date:

2014-09-26

Authors:

Namanja, Andrew; Chen, Chih-Hong; Chen, Yuan

Citation:

Citation: Chen, Chih-Hong; Namanja, Andrew; Chen, Yuan. "Conformational flexibility and changes underlying activation of the SUMO-specific protease SENP1 by remote substrate binding" Nat. Commun. ., .-..

Assembly members:

Assembly members:
SENP1, polymer, 240 residues, 28608 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SENP1: MHHHHHHENLYFQGEFPEIT EEMEKEIKNVFRNGNQDEVL SEAFRLTITRKDIQTLNHLN WLNDEIINFYMNMLMERSKE KGLPSVHAFNTFFFTKLKTA GYQAVKRWTKKVDVFSVDIL LVPIHLGVHWCLAVVDFRKK NITYYDSMGGINNEACRILL QYLKQESIDKKRKEFDTNGW QLFSKKSQEIPQQMNGSDCG MFACKYADCITKDRPINFTQ QHMPYFRKRMVWEILHRKLL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	609
15N chemical shifts	215
1H chemical shifts	389

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SENP1	1

Entities:

Entity 1, SENP1 240 residues - 28608 Da.

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.

1	MET	HIS	HIS	HIS	HIS	HIS	HIS	GLU	ASN	LEU
2	TYR	PHE	GLN	GLY	GLU	PHE	PRO	GLU	ILE	THR
3	GLU	GLU	MET	GLU	LYS	GLU	ILE	LYS	ASN	VAL
4	PHE	ARG	ASN	GLY	ASN	GLN	ASP	GLU	VAL	LEU
5	SER	GLU	ALA	PHE	ARG	LEU	THR	ILE	THR	ARG
6	LYS	ASP	ILE	GLN	THR	LEU	ASN	HIS	LEU	ASN
7	TRP	LEU	ASN	ASP	GLU	ILE	ILE	ASN	PHE	TYR
8	MET	ASN	MET	LEU	MET	GLU	ARG	SER	LYS	GLU
9	LYS	GLY	LEU	PRO	SER	VAL	HIS	ALA	PHE	ASN
10	THR	PHE	PHE	PHE	THR	LYS	LEU	LYS	THR	ALA
11	GLY	TYR	GLN	ALA	VAL	LYS	ARG	TRP	THR	LYS
12	LYS	VAL	ASP	VAL	PHE	SER	VAL	ASP	ILE	LEU
13	LEU	VAL	PRO	ILE	HIS	LEU	GLY	VAL	HIS	TRP
14	CYS	LEU	ALA	VAL	VAL	ASP	PHE	ARG	LYS	LYS
15	ASN	ILE	THR	TYR	TYR	ASP	SER	MET	GLY	GLY
16	ILE	ASN	ASN	GLU	ALA	CYS	ARG	ILE	LEU	LEU
17	GLN	TYR	LEU	LYS	GLN	GLU	SER	ILE	ASP	LYS
18	LYS	ARG	LYS	GLU	PHE	ASP	THR	ASN	GLY	TRP
19	GLN	LEU	PHE	SER	LYS	LYS	SER	GLN	GLU	ILE
20	PRO	GLN	GLN	MET	ASN	GLY	SER	ASP	CYS	GLY
21	MET	PHE	ALA	CYS	LYS	TYR	ALA	ASP	CYS	ILE
22	THR	LYS	ASP	ARG	PRO	ILE	ASN	PHE	THR	GLN
23	GLN	HIS	MET	PRO	TYR	PHE	ARG	LYS	ARG	MET
24	VAL	TRP	GLU	ILE	LEU	HIS	ARG	LYS	LEU	LEU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D HMCM-VAL	sample_2	isotropic	sample_conditions_1
2D HMCM-LEU	sample_2	isotropic	sample_conditions_1

BMRB	19083
PDB	2CKG 2CKH 2G4D 2IY0 2IY1 2IYC 2IYD 2XPH 2XRE
DBJ	BAC26011 BAC26106 BAC40442 BAF84749
EMBL	CAH90949
GB	AAF31171 AAH23129 AAH45639 AIC60034 EAW57971
REF	NP_001129011 NP_001193805 NP_001254523 NP_001254524 NP_659100
SP	P59110 Q5RBB1 Q9P0U3
TPG	DAA29877
AlphaFold	P59110 Q5RBB1 Q9P0U3

BMRB Entry 19885

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

Related Database Links:

1	MET	HIS	HIS	HIS	HIS	HIS	HIS	GLU	ASN	LEU
2	TYR	PHE	GLN	GLY	GLU	PHE	PRO	GLU	ILE	THR
3	GLU	GLU	MET	GLU	LYS	GLU	ILE	LYS	ASN	VAL
4	PHE	ARG	ASN	GLY	ASN	GLN	ASP	GLU	VAL	LEU
5	SER	GLU	ALA	PHE	ARG	LEU	THR	ILE	THR	ARG
6	LYS	ASP	ILE	GLN	THR	LEU	ASN	HIS	LEU	ASN
7	TRP	LEU	ASN	ASP	GLU	ILE	ILE	ASN	PHE	TYR
8	MET	ASN	MET	LEU	MET	GLU	ARG	SER	LYS	GLU
9	LYS	GLY	LEU	PRO	SER	VAL	HIS	ALA	PHE	ASN
10	THR	PHE	PHE	PHE	THR	LYS	LEU	LYS	THR	ALA
11	GLY	TYR	GLN	ALA	VAL	LYS	ARG	TRP	THR	LYS
12	LYS	VAL	ASP	VAL	PHE	SER	VAL	ASP	ILE	LEU
13	LEU	VAL	PRO	ILE	HIS	LEU	GLY	VAL	HIS	TRP
14	CYS	LEU	ALA	VAL	VAL	ASP	PHE	ARG	LYS	LYS
15	ASN	ILE	THR	TYR	TYR	ASP	SER	MET	GLY	GLY
16	ILE	ASN	ASN	GLU	ALA	CYS	ARG	ILE	LEU	LEU
17	GLN	TYR	LEU	LYS	GLN	GLU	SER	ILE	ASP	LYS
18	LYS	ARG	LYS	GLU	PHE	ASP	THR	ASN	GLY	TRP
19	GLN	LEU	PHE	SER	LYS	LYS	SER	GLN	GLU	ILE
20	PRO	GLN	GLN	MET	ASN	GLY	SER	ASP	CYS	GLY
21	MET	PHE	ALA	CYS	LYS	TYR	ALA	ASP	CYS	ILE
22	THR	LYS	ASP	ARG	PRO	ILE	ASN	PHE	THR	GLN
23	GLN	HIS	MET	PRO	TYR	PHE	ARG	LYS	ARG	MET
24	VAL	TRP	GLU	ILE	LEU	HIS	ARG	LYS	LEU	LEU

1	MET	HIS	HIS	HIS	HIS	HIS	HIS	GLU	ASN	LEU
2	TYR	PHE	GLN	GLY	GLU	PHE	PRO	GLU	ILE	THR
3	GLU	GLU	MET	GLU	LYS	GLU	ILE	LYS	ASN	VAL
4	PHE	ARG	ASN	GLY	ASN	GLN	ASP	GLU	VAL	LEU
5	SER	GLU	ALA	PHE	ARG	LEU	THR	ILE	THR	ARG
6	LYS	ASP	ILE	GLN	THR	LEU	ASN	HIS	LEU	ASN
7	TRP	LEU	ASN	ASP	GLU	ILE	ILE	ASN	PHE	TYR
8	MET	ASN	MET	LEU	MET	GLU	ARG	SER	LYS	GLU
9	LYS	GLY	LEU	PRO	SER	VAL	HIS	ALA	PHE	ASN
10	THR	PHE	PHE	PHE	THR	LYS	LEU	LYS	THR	ALA
11	GLY	TYR	GLN	ALA	VAL	LYS	ARG	TRP	THR	LYS
12	LYS	VAL	ASP	VAL	PHE	SER	VAL	ASP	ILE	LEU
13	LEU	VAL	PRO	ILE	HIS	LEU	GLY	VAL	HIS	TRP
14	CYS	LEU	ALA	VAL	VAL	ASP	PHE	ARG	LYS	LYS
15	ASN	ILE	THR	TYR	TYR	ASP	SER	MET	GLY	GLY
16	ILE	ASN	ASN	GLU	ALA	CYS	ARG	ILE	LEU	LEU
17	GLN	TYR	LEU	LYS	GLN	GLU	SER	ILE	ASP	LYS
18	LYS	ARG	LYS	GLU	PHE	ASP	THR	ASN	GLY	TRP
19	GLN	LEU	PHE	SER	LYS	LYS	SER	GLN	GLU	ILE
20	PRO	GLN	GLN	MET	ASN	GLY	SER	ASP	CYS	GLY
21	MET	PHE	ALA	CYS	LYS	TYR	ALA	ASP	CYS	ILE
22	THR	LYS	ASP	ARG	PRO	ILE	ASN	PHE	THR	GLN
23	GLN	HIS	MET	PRO	TYR	PHE	ARG	LYS	ARG	MET
24	VAL	TRP	GLU	ILE	LEU	HIS	ARG	LYS	LEU	LEU

1	MET	HIS	HIS	HIS	HIS	HIS	HIS	GLU	ASN	LEU
2	TYR	PHE	GLN	GLY	GLU	PHE	PRO	GLU	ILE	THR
3	GLU	GLU	MET	GLU	LYS	GLU	ILE	LYS	ASN	VAL
4	PHE	ARG	ASN	GLY	ASN	GLN	ASP	GLU	VAL	LEU
5	SER	GLU	ALA	PHE	ARG	LEU	THR	ILE	THR	ARG
6	LYS	ASP	ILE	GLN	THR	LEU	ASN	HIS	LEU	ASN
7	TRP	LEU	ASN	ASP	GLU	ILE	ILE	ASN	PHE	TYR
8	MET	ASN	MET	LEU	MET	GLU	ARG	SER	LYS	GLU
9	LYS	GLY	LEU	PRO	SER	VAL	HIS	ALA	PHE	ASN
10	THR	PHE	PHE	PHE	THR	LYS	LEU	LYS	THR	ALA
11	GLY	TYR	GLN	ALA	VAL	LYS	ARG	TRP	THR	LYS
12	LYS	VAL	ASP	VAL	PHE	SER	VAL	ASP	ILE	LEU
13	LEU	VAL	PRO	ILE	HIS	LEU	GLY	VAL	HIS	TRP
14	CYS	LEU	ALA	VAL	VAL	ASP	PHE	ARG	LYS	LYS
15	ASN	ILE	THR	TYR	TYR	ASP	SER	MET	GLY	GLY
16	ILE	ASN	ASN	GLU	ALA	CYS	ARG	ILE	LEU	LEU
17	GLN	TYR	LEU	LYS	GLN	GLU	SER	ILE	ASP	LYS
18	LYS	ARG	LYS	GLU	PHE	ASP	THR	ASN	GLY	TRP
19	GLN	LEU	PHE	SER	LYS	LYS	SER	GLN	GLU	ILE
20	PRO	GLN	GLN	MET	ASN	GLY	SER	ASP	CYS	GLY
21	MET	PHE	ALA	CYS	LYS	TYR	ALA	ASP	CYS	ILE
22	THR	LYS	ASP	ARG	PRO	ILE	ASN	PHE	THR	GLN
23	GLN	HIS	MET	PRO	TYR	PHE	ARG	LYS	ARG	MET
24	VAL	TRP	GLU	ILE	LEU	HIS	ARG	LYS	LEU	LEU