BMRB Entry 25440

Name: 1H and 113Cd chemical shift assignments for the cysteins and metals of Bud31p Cd3
Published: 2015-03-09

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25440

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

1H and 113Cd chemical shift assignments for the cysteins and metals of Bud31p Cd3

Deposition date:

2015-01-19

Original release date:

2015-03-09

Authors:

van Roon, Anne-Marie; Yang, Ji-Chun; Mathieu, Daniel; Bermel, Wolfgang; Nagai, Kiyoshi; Neuhaus, David

Citation:

Citation: van Roon, Anne-Marie; Yang, Ji-Chun; Mathieu, Daniel; Bermel, Wolfgang; Nagai, Kiyoshi; Neuhaus, David. "113 Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p" Angew. Chem. Int. Ed. Engl. 54, 4861-4864 (2015).
PubMed: 25703931

Assembly members:

Assembly members:
Bud31p_polypeptide, polymer, 159 residues, 18554.609 Da.
CADMIUM ION, non-polymer, 112.411 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: pRK172

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bud31p_polypeptide: GGSPRIKTRRSKPAPDGFEK IKPTLTDFEIQLRDAQKDKS SKLAAKSNEQLWEIMQLHHQ RSRYIYTLYYKRKAISKDLY DWLIKEKYADKLLIAKWRKT GYEKLCCLRCIQKNETNNGS TCICRVPRAQLEEEARKKGT QVSFHQCVHCGCRGCASTD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
113Cd chemical shifts	6
1H chemical shifts	49

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Bud31p polypeptide	1
2	Cadmium 1	2
3	Cadmium 2	2
4	Cadmium 3	2

Entities:

Entity 1, Bud31p polypeptide 159 residues - 18554.609 Da.

1

GLY

SER

PRO

ARG

ILE

LYS

THR

ARG

2

SER

LYS

PRO

ALA

PRO

ASP

GLY

PHE

GLU

LYS

3

ILE

LYS

PRO

THR

LEU

THR

ASP

PHE

GLU

ILE

4

GLN

LEU

ARG

ASP

ALA

GLN

LYS

ASP

LYS

SER

5

SER

LYS

LEU

ALA

LYS

SER

ASN

GLU

GLN

6

LEU

TRP

GLU

ILE

MET

GLN

LEU

HIS

GLN

7

ARG

SER

ARG

TYR

ILE

TYR

THR

LEU

TYR

8

LYS

ARG

LYS

ALA

ILE

SER

LYS

ASP

LEU

TYR

9

ASP

TRP

LEU

ILE

LYS

GLU

LYS

TYR

ALA

ASP

10

LYS

LEU

ILE

ALA

LYS

TRP

ARG

LYS

THR

11

GLY

TYR

GLU

LYS

LEU

CYS

LEU

ARG

CYS

12

ILE

GLN

LYS

ASN

GLU

THR

ASN

GLY

SER

13

THR

CYS

ILE

CYS

ARG

VAL

PRO

ARG

ALA

GLN

14

LEU

GLU

ALA

ARG

LYS

GLY

THR

15

GLN

VAL

SER

PHE

HIS

GLN

CYS

VAL

HIS

CYS

16

GLY

CYS

ARG

GLY

CYS

ALA

SER

THR

ASP

Entity 2, Cadmium 1 - Cd - 112.411 Da.

1

CD

Samples:

sample_1: Bud31p (113Cd)3 2.6 mM; sodium phosphate 20 mM; sodium chloride 150 mM; DTT, [U-2H], 5 mM; D2O 100%

sample_conditions_1: ionic strength: 0.27 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.27 M; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 113Cd-113Cd COSY	sample_1	isotropic	sample_conditions_1
2D 113Cd-1H HSQC NOESY	sample_1	isotropic	sample_conditions_1
2D 113Cd-1H HMQC-RELAY	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC aliphatic (natural abundance)	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic (natural abundance)	sample_1	isotropic	sample_conditions_2

Software:

TOPSPIN v3.1, Bruker Biospin - processing

SPARKY v3.115, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance AVIII 850 MHz
Bruker Avance AVIII 500 MHz