BMRB Entry 19885

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

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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:
Data typeCount
13C chemical shifts609
15N chemical shifts215
1H chemical shifts389

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1SENP11

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   METHISHISHISHISHISHISGLUASNLEU
2   TYRPHEGLNGLYGLUPHEPROGLUILETHR
3   GLUGLUMETGLULYSGLUILELYSASNVAL
4   PHEARGASNGLYASNGLNASPGLUVALLEU
5   SERGLUALAPHEARGLEUTHRILETHRARG
6   LYSASPILEGLNTHRLEUASNHISLEUASN
7   TRPLEUASNASPGLUILEILEASNPHETYR
8   METASNMETLEUMETGLUARGSERLYSGLU
9   LYSGLYLEUPROSERVALHISALAPHEASN
10   THRPHEPHEPHETHRLYSLEULYSTHRALA
11   GLYTYRGLNALAVALLYSARGTRPTHRLYS
12   LYSVALASPVALPHESERVALASPILELEU
13   LEUVALPROILEHISLEUGLYVALHISTRP
14   CYSLEUALAVALVALASPPHEARGLYSLYS
15   ASNILETHRTYRTYRASPSERMETGLYGLY
16   ILEASNASNGLUALACYSARGILELEULEU
17   GLNTYRLEULYSGLNGLUSERILEASPLYS
18   LYSARGLYSGLUPHEASPTHRASNGLYTRP
19   GLNLEUPHESERLYSLYSSERGLNGLUILE
20   PROGLNGLNMETASNGLYSERASPCYSGLY
21   METPHEALACYSLYSTYRALAASPCYSILE
22   THRLYSASPARGPROILEASNPHETHRGLN
23   GLNHISMETPROTYRPHEARGLYSARGMET
24   VALTRPGLUILELEUHISARGLYSLEULEU

Samples:

sample_1: SENP1, [U-10% 13C; U-100% 15N], 0.4 mM

sample_2: SENP1, [U-10% 13C; U-100% 15N], 0.4 mM

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 295 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(COCA)CBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D HMCM-VALsample_2isotropicsample_conditions_1
2D HMCM-LEUsample_2isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY v3, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19083
PDB
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

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks