BMRB Entry 27442

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for residues 1-136 of yeast Rpn5.
Published: 2018-09-19

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27442

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for residues 1-136 of yeast Rpn5.

Deposition date:

2018-04-04

Original release date:

2018-09-19

Authors:

Zhang, Wenbo; Zhao, Cong; Hu, Yunfei; Jin, Changwen

Citation:

Citation: Zhang, Wenbo; Zhao, Cong; Hu, Yunfei; Jin, Changwen. "Solution structure of the N-terminal domain of proteasome lid subunit Rpn5" Biochem. Biophys. Res. Commun. 504, 225-230 (2018).
PubMed: 30177392

Assembly members:

Assembly members:
Rpn5, polymer, 136 residues, 15.6 Da.

Natural source:

Natural source: Common Name: baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a (+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rpn5: MSRDAPIKADKDYSQILKEE FPKIDSLAQNDCNSALDQLL VLEKKTRQASDLASSKEVLA KIVDLLASRNKWDDLNEQLT LLSKKHGQLKLSIQYMIQKV MEYLKSSKSLDLNTRISVIE TIRVVTENKIFVEVER

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	557
15N chemical shifts	144
1H chemical shifts	866

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rpn5	1

Entities:

Entity 1, Rpn5 136 residues - 15.6 Da.

1

MET

SER

ARG

ASP

ALA

PRO

ILE

LYS

ALA

ASP

2

LYS

ASP

TYR

SER

GLN

ILE

LEU

LYS

GLU

3

PHE

PRO

LYS

ILE

ASP

SER

LEU

ALA

GLN

ASN

4

ASP

CYS

ASN

SER

ALA

LEU

ASP

GLN

LEU

5

VAL

LEU

GLU

LYS

THR

ARG

GLN

ALA

SER

6

ASP

LEU

ALA

SER

LYS

GLU

VAL

LEU

ALA

7

LYS

ILE

VAL

ASP

LEU

ALA

SER

ARG

ASN

8

LYS

TRP

ASP

LEU

ASN

GLU

GLN

LEU

THR

9

LEU

SER

LYS

HIS

GLY

GLN

LEU

LYS

10

LEU

SER

ILE

GLN

TYR

MET

ILE

GLN

LYS

VAL

11

MET

GLU

TYR

LEU

LYS

SER

LYS

SER

LEU

12

ASP

LEU

ASN

THR

ARG

ILE

SER

VAL

ILE

GLU

13

THR

ILE

ARG

VAL

THR

GLU

ASN

LYS

ILE

14

PHE

VAL

GLU

VAL

GLU

ARG

Samples:

sample_1: Rpn5, [U-95% 13C; U-95% 15N], 0.3 mM; D2O, [U-99% 2H], 10 % v/v; DSS 0.1 mg/mL; DTT 1 mM; sodium phosphate 50 mM; sodium sulfate 50 mM; trifluoroethanol 2 % v/v; sucrose 5 % w/v

sample_conditions_1: ionic strength: 194 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 950 MHz

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