BMRB Entry 36111

Name: Solution structure of yeast Fra2
Published: 2018-03-26

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PDB ID: 5y4b
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36111
MolProbity Validation Chart

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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: Solution structure of yeast Fra2 PubMed: 29524511

Deposition date: 2017-08-03 Original release date: 2018-03-26

Authors: Tang, Y.; Chi, C.; Zhang, J.; Dai, Y.; Abdalla, M.; Chen, Y.; Zhou, C.

Citation: Chi, C.; Tang, Y.; Zhang, J.; Dai, Y.; Abdalla, M.; Chen, Y.; Zhou, C.. "Structural and Biochemical Insights into the Multiple Functions of Yeast Grx3" J. Mol. Biol. 2836, 30110-30114 (2018).

Assembly members:
BolA-like protein 2, polymer, 93 residues, 10810.320 Da.

Natural source: Common Name: Baker's yeast Taxonomy ID: 559292 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
BolA-like protein 2: MPVTEQGLRERIESAIPQVY HIIVTDLSYGCGQSFDIVVV SDFFQGKSKLMRSRAVNKAV KEELQEIHAFSCKCYTEEEW SKIVVLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	254
15N chemical shifts	76
1H chemical shifts	539

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 93 residues - 10810.320 Da.

1

MET

PRO

VAL

THR

GLU

GLN

GLY

LEU

ARG

GLU

2

ARG

ILE

GLU

SER

ALA

ILE

PRO

GLN

VAL

TYR

3

HIS

ILE

VAL

THR

ASP

LEU

SER

TYR

GLY

4

CYS

GLY

GLN

SER

PHE

ASP

ILE

VAL

5

SER

ASP

PHE

GLN

GLY

LYS

SER

LYS

LEU

6

MET

ARG

SER

ARG

ALA

VAL

ASN

LYS

ALA

VAL

7

LYS

GLU

LEU

GLN

GLU

ILE

HIS

ALA

PHE

8

SER

CYS

LYS

CYS

TYR

THR

GLU

TRP

9

SER

LYS

ILE

VAL

LEU

GLU

HIS

10

HIS

Samples:

sample_1: Fra2, [U-13C; U-15N], 0.8 mM; NaCl 150 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: Fra2, [U-13C; U-15N], 0.8 mM; NaCl 150 mM; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 150 mM; pH: 8.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 15N-1H HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D (H)C(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CBCA)-(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(C)(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

ProcheckNMR, Laskowski and MacArthur - refinement

SPARKY, Goddard - chemical shift assignment, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker DMX 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts