BMRB Entry 18235

Name: Solution Structure Of The N-Terminal Domain Of The Yeast Protein Dre2
Published: 2015-07-24

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR18235

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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:

Solution Structure Of The N-Terminal Domain Of The Yeast Protein Dre2

Deposition date:

2012-02-01

Original release date:

2015-07-24

Authors:

Craescu, Constantin; Vernis, Laurence; Pastore, Annalisa

Citation:

Citation: Soler, Nicolas; Craescu, Costantin; Gallay, Jacques; Frapart, Yves-Michel; Mansuy, Daniel; Raynal, Bertrand; Baldacci, Giuseppe; Pastore, Annalisa; Huang, Meng-Er; Vernis, Laurence. "A S-adenosylmethionine methyltransferase-like domain within the essential, Fe-S-containing yeast protein Dre2" FEBS J. 279, 2108-2119 (2012).
PubMed: 22487307

Assembly members:

Assembly members:
N-dre2, polymer, 136 residues, Formula weight is not available

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: pSKB3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
N-dre2: GHMMSQYKTGLLLIHPAVTT TPELVENTKAQAASKKVKFV DQFLINKLNDGSITLENAKY ETVHYLTPEAQTDIKFPKKL ISVLADSLKPNGSLIGLSDI YKVDALINGFEIINEPDYCW IKMDSSKLNQTVSIPL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	466
15N chemical shifts	127
1H chemical shifts	873

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-dre2	1

Entities:

Entity 1, N-dre2 136 residues - Formula weight is not available

The first three residues are a tag. Numbering of the entry starts at the second Met, that is the natural sequence.

1

GLY

HIS

MET

SER

GLN

TYR

LYS

THR

GLY

2

LEU

ILE

HIS

PRO

ALA

VAL

THR

3

THR

PRO

GLU

LEU

VAL

GLU

ASN

THR

LYS

ALA

4

GLN

ALA

SER

LYS

VAL

LYS

PHE

VAL

5

ASP

GLN

PHE

LEU

ILE

ASN

LYS

LEU

ASN

ASP

6

GLY

SER

ILE

THR

LEU

GLU

ASN

ALA

LYS

TYR

7

GLU

THR

VAL

HIS

TYR

LEU

THR

PRO

GLU

ALA

8

GLN

THR

ASP

ILE

LYS

PHE

PRO

LYS

LEU

9

ILE

SER

VAL

LEU

ALA

ASP

SER

LEU

LYS

PRO

10

ASN

GLY

SER

LEU

ILE

GLY

LEU

SER

ASP

ILE

11

TYR

LYS

VAL

ASP

ALA

LEU

ILE

ASN

GLY

PHE

12

GLU

ILE

ASN

GLU

PRO

ASP

TYR

CYS

TRP

13

ILE

LYS

MET

ASP

SER

LYS

LEU

ASN

GLN

14

THR

VAL

SER

ILE

PRO

LEU

Samples:

sample_1: potassium phosphate 50 mM; DTT 1 mM; sodium chloride 50 mM; N-dre2 0.5 mM; H2O 93%; D2O 7%

sample_conditions_1: ionic strength: 0.100 M; pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR, Accelrys Software Inc. - structure solution

NMR spectrometers:

Varian Unity 500 MHz
Bruker Avance 800 MHz

PDB	2KM1 2KM1
DBJ	GAA24792
EMBL	CAA82150 CAY81149
GB	AHY76305 AJP40099 AJS30297 AJS30598 AJS30896
REF	NP_012997
SP	A7A031 B3LRE5 C7GX69 C8ZCN3 P36152
TPG	DAA09222
AlphaFold	A7A031 B3LRE5 C7GX69 C8ZCN3 P36152