BMRB Entry 17352

Name: The structure of a domain from yeast
Published: 2011-03-30

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PDB ID: 2l7e
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17352
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: The structure of a domain from yeast PubMed: 21355849

Deposition date: 2010-12-08 Original release date: 2011-03-30

Authors: Zhang, Wen; Zhang, Jiahai; Tu, Xiaoming

Citation: Zhang, Wen; Zhang, Jiahai; Zhang, Xuecheng; Xu, Chao; Tu, Xiaoming. "Solution structure of the Taf14 YEATS domain and its roles in cell growth of Saccharomyces cerevisiae." Biochem. J. 436, 83-90 (2011).

Assembly members:
a_domain, polymer, 131 residues, Formula weight is not available

Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi

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

Entity Sequences (FASTA):
a_domain: MVATVKRTIRIKTQQHILPE VPPVENFPVRQWSIEIVLLD DEGKEIPATIFDKVIYHLHP TFANPNRTFTDPPFRIEEQG WGGFPLDISVFLLEKAGERK IPHDLNFLQESYEVEHVIQI PLNLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	392
15N chemical shifts	107
1H chemical shifts	689

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Taf14 YEATS domain	1

Entities:

Entity 1, Taf14 YEATS domain 131 residues - Formula weight is not available

1

MET

VAL

ALA

THR

VAL

LYS

ARG

THR

ILE

ARG

2

ILE

LYS

THR

GLN

HIS

ILE

LEU

PRO

GLU

3

VAL

PRO

VAL

GLU

ASN

PHE

PRO

VAL

ARG

4

GLN

TRP

SER

ILE

GLU

ILE

VAL

LEU

ASP

5

ASP

GLU

GLY

LYS

GLU

ILE

PRO

ALA

THR

ILE

6

PHE

ASP

LYS

VAL

ILE

TYR

HIS

LEU

HIS

PRO

7

THR

PHE

ALA

ASN

PRO

ASN

ARG

THR

PHE

THR

8

ASP

PRO

PHE

ARG

ILE

GLU

GLN

GLY

9

TRP

GLY

PHE

PRO

LEU

ASP

ILE

SER

VAL

10

PHE

LEU

GLU

LYS

ALA

GLY

GLU

ARG

LYS

11

ILE

PRO

HIS

ASP

LEU

ASN

PHE

LEU

GLN

GLU

12

SER

TYR

GLU

VAL

GLU

HIS

VAL

ILE

GLN

ILE

13

PRO

LEU

ASN

LEU

GLU

HIS

14

HIS

Samples:

sample_1: a_domain 0.7 mM; sodium phosphate 20 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: a_domain 0.7 mM; sodium phosphate 20 mM; sodium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 0.12 M; pH: 6.7; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment, chemical shift calculation, data analysis

NMR spectrometers:

Bruker DMX 500 MHz

PDB	2L7E 3QRL 5D7E
DBJ	GAA26845
EMBL	CAA49192 CAA81125 CAY86832
GB	AAA61644 AAB68235 AHY78050 AJP42018 AJU23462
REF	NP_015196
SP	P35189
TPG	DAA11304

Biological Magnetic Resonance Data Bank