BMRB Entry 15989

Name: Solution NMR structure of the R2R3 DNA binding domain of Myb1 protein from protozoan parasite Trichomonas vaginalis
Published: 2009-04-04

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PDB ID: 2k9n
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15989
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of the R2R3 DNA binding domain of Myb1 protein from protozoan parasite Trichomonas vaginalis

Deposition date:

2008-10-16

Original release date:

2009-04-04

Authors:

Lou, Yuan-Chao; Wei, Shu-Yi; Rajasekaran, M.; Chou, Chun-Chi; Hsu, Hong-Ming; Tai, Jung-Hsiang; Chen, Chinpan

Citation:

Citation: Lou, Yuan-Chao; Wei, Shu-Yi; Rajasekaran, M.; Chou, Chun-Chi; Hsu, Hong-Ming; Tai, Jung-Hsiang; Chen, Chinpan. "NMR structural analysis of DNA recognition by a novel Myb1 DNA-binding domain in the protozoan parasite Trichomonas vaginalis" Nucleic Acids Res. 37, 2381-2394 (2009).
PubMed: 19246540

Assembly members:

Assembly members:
R2R3 DNA binding domain, polymer, 107 residues, 13218.344 Da.

Natural source:

Natural source: Common Name: Trichomonas vaginalis Taxonomy ID: 5722 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trichomonas vaginalis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
R2R3 DNA binding domain: KVKFTEEEDLKLQQLVMRYG AKDWIRISQLMITRNPRQCR ERWNNYINPALRTDPWSPEE DMLLDQKYAEYGPKWNKISK FLKNRSDNNIRNRWMMIARH RAKHQKS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
heteronucl_NOEs
- heteronuclear_noe_list_1

Data type	Count
13C chemical shifts	493
15N chemical shifts	121
1H chemical shifts	789
heteronuclear NOE values	92

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	R2R3 DNA binding domain	1

Entities:

Entity 1, R2R3 DNA binding domain 107 residues - 13218.344 Da.

1

LYS

VAL

LYS

PHE

THR

GLU

ASP

LEU

2

LYS

LEU

GLN

LEU

VAL

MET

ARG

TYR

GLY

3

ALA

LYS

ASP

TRP

ILE

ARG

ILE

SER

GLN

LEU

4

MET

ILE

THR

ARG

ASN

PRO

ARG

GLN

CYS

ARG

5

GLU

ARG

TRP

ASN

TYR

ILE

ASN

PRO

ALA

6

LEU

ARG

THR

ASP

PRO

TRP

SER

PRO

GLU

7

ASP

MET

LEU

ASP

GLN

LYS

TYR

ALA

GLU

8

TYR

GLY

PRO

LYS

TRP

ASN

LYS

ILE

SER

LYS

9

PHE

LEU

LYS

ASN

ARG

SER

ASP

ASN

ILE

10

ARG

ASN

ARG

TRP

MET

ILE

ALA

ARG

HIS

11

ARG

ALA

LYS

HIS

GLN

LYS

SER

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

PDB	2K9N 2KDZ
GB	AAX51243 EAY03723
REF	XP_001315946

BMRB Entry 15989

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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