BMRB Entry 26730

Name: Structural and dynamics studies of Pax5 reveal asymmetry in stability and DNA binding by the Paired domain
Published: 2016-07-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26730

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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:

Structural and dynamics studies of Pax5 reveal asymmetry in stability and DNA binding by the Paired domain

Deposition date:

2016-01-14

Original release date:

2016-07-14

Authors:

Perez-Borrajero, Cecilia; McIntosh, Lawrence

Citation:

Citation: Perez-Borrajero, Cecilia; Okon, Mark; McIntosh, Lawrence. "Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain" J. Mol. Biol. 428, 2372-2391 (2016).
PubMed: 27067111

Assembly members:

Assembly members:
Paired_domain_of_Pax5, polymer, 151 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28-MHL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Paired_domain_of_Pax5: GHMDLEKNYPTPRTSRTGHG GVNQLGGVFVNGRPLPDVVR QRIVELAHQGVRPCDISRQL RVSHGCVSKILGRYYETGSI KPGVIGGSKPKVATPKVVEK IAEYKRQNPTMFAWEIRDRL LAERVCDNDTVPSVSSINRI IRTKVQQPPNQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	431
15N chemical shifts	137
1H chemical shifts	137

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Paired domain of Pax5	1

Entities:

Entity 1, Paired domain of Pax5 151 residues - Formula weight is not available

1

GLY

HIS

MET

ASP

LEU

GLU

LYS

ASN

TYR

PRO

2

THR

PRO

ARG

THR

SER

ARG

THR

GLY

HIS

GLY

3

GLY

VAL

ASN

GLN

LEU

GLY

VAL

PHE

VAL

4

ASN

GLY

ARG

PRO

LEU

PRO

ASP

VAL

ARG

5

GLN

ARG

ILE

VAL

GLU

LEU

ALA

HIS

GLN

GLY

6

VAL

ARG

PRO

CYS

ASP

ILE

SER

ARG

GLN

LEU

7

ARG

VAL

SER

HIS

GLY

CYS

VAL

SER

LYS

ILE

8

LEU

GLY

ARG

TYR

GLU

THR

GLY

SER

ILE

9

LYS

PRO

GLY

VAL

ILE

GLY

SER

LYS

PRO

10

LYS

VAL

ALA

THR

PRO

LYS

VAL

GLU

LYS

11

ILE

ALA

GLU

TYR

LYS

ARG

GLN

ASN

PRO

THR

12

MET

PHE

ALA

TRP

GLU

ILE

ARG

ASP

ARG

LEU

13

LEU

ALA

GLU

ARG

VAL

CYS

ASP

ASN

ASP

THR

14

VAL

PRO

SER

VAL

SER

ILE

ASN

ARG

ILE

15

ILE

ARG

THR

LYS

VAL

GLN

PRO

ASN

16

GLN

Samples:

sample_1: Paired domain of Pax5, [U-100% 13C; U-100% 15N], 0.35 mM; MES 20 mM; NaCl 200 mM; DTT 2 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298.15 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 850 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks