BMRB Entry 30330

Name: Solution structure of yeast Med15 ABD2 residues 277-368
Published: 2018-03-16

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PDB ID: 6aly
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30330
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 Med15 ABD2 residues 277-368 PubMed: 29562181

Deposition date: 2017-08-08 Original release date: 2018-03-16

Authors: Tuttle, L.; Pacheco, D.; Warfield, L.; Hahn, S.; Klevit, R.

Citation: Tuttle, L.; Pachecko, D.; Warfield, L.; Luo, J.; Ranish, J.; Hahn, S.; Klevit, R.. "Gcn4-Mediator Specificity Is Mediated by a Large and Dynamic Fuzzy Protein-Protein Complex." Cell Rep. 22, 3251-3264 (2018).

Assembly members:
entity_1, polymer, 92 residues, 10525.714 Da.

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

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

Entity Sequences (FASTA):
entity_1: NNPLQQQSSQNTVPNVLNQI NQIFSPEEQRSLLQEAIETC KNFEKTQLGSTMTEPVKQSF IRKYINQKALRKIQALRDVK NNNNANNNGSNL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	379
15N chemical shifts	87
1H chemical shifts	464

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 92 residues - 10525.714 Da.

1

ASN

PRO

LEU

GLN

SER

GLN

2

ASN

THR

VAL

PRO

ASN

VAL

LEU

ASN

GLN

ILE

3

ASN

GLN

ILE

PHE

SER

PRO

GLU

GLN

ARG

4

SER

LEU

GLN

GLU

ALA

ILE

GLU

THR

CYS

5

LYS

ASN

PHE

GLU

LYS

THR

GLN

LEU

GLY

SER

6

THR

MET

THR

GLU

PRO

VAL

LYS

GLN

SER

PHE

7

ILE

ARG

LYS

TYR

ILE

ASN

GLN

LYS

ALA

LEU

8

ARG

LYS

ILE

GLN

ALA

LEU

ARG

ASP

VAL

LYS

9

ASN

ALA

ASN

GLY

SER

10

ASN

LEU

Samples:

sample_1: DTT 5 mM; EDTA 0.1 mM; Med15 ABD2, [U-15N], 500 uM; PMSF 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_2: DTT 5 mM; EDTA 0.1 mM; Med15 ABD2, [U-13C; U-15N], 500 uM; PMSF 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_3: DTT 5 mM; EDTA 0.1 mM; Med15 ABD2, [U-13C; U-15N], 500 uM; PMSF 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_4: C12E6/Hexanol 10%; DTT 5 mM; EDTA 0.1 mM; Med15 ABD2, [U-15N], 2.6 mM; PMSF 0.1 mM; sodium chloride 150 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	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 CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_conditions_1
2D 1H-15N HSQC IPAP	sample_4	anisotropic	sample_conditions_1
2D 1H-15N HSQC IPAP	sample_1	isotropic	sample_conditions_1

Software:

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

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

TALOS, Cornilescu, Delaglio and Bax - structure calculation

TOPSPIN, Bruker Biospin - collection

X-PLOR NIH v2.45, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker AvanceIII 500 MHz
Bruker AvanceIII 600 MHz
Bruker AvanceIII 800 MHz

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