BMRB Entry 36037

Name: Solution structure of a histone binding domain
Published: 2017-05-15

Click here to enlarge.

PDB ID: 5wqz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR36037
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of a histone binding domain

Deposition date:

2016-11-29

Original release date:

2017-05-15

Authors:

Mi, J.

Citation:

Citation: Mi, J.. "Solution Structure Of A Histone Binding Domain" .

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 13878.720 Da.

Natural source:

Natural source: Common Name: Trypanosoma brucei Taxonomy ID: 185431 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET-22B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSQNRQLLYPREEMVSLVRS LDRPQENGLFSQDVLLQYPE LAESYTKVCPNRCDLATAAD RAAKGAYGYDVQLTTLKEDI RLMVNNCILFNGAEGAYADA ARTFEKFAMGKIDAYISQKV GGLE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	315
15N chemical shifts	133
1H chemical shifts	616

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 124 residues - 13878.720 Da.

1

MET

SER

GLN

ASN

ARG

GLN

LEU

TYR

PRO

2

ARG

GLU

MET

VAL

SER

LEU

VAL

ARG

SER

3

LEU

ASP

ARG

PRO

GLN

GLU

ASN

GLY

LEU

PHE

4

SER

GLN

ASP

VAL

LEU

GLN

TYR

PRO

GLU

5

LEU

ALA

GLU

SER

TYR

THR

LYS

VAL

CYS

PRO

6

ASN

ARG

CYS

ASP

LEU

ALA

THR

ALA

ASP

7

ARG

ALA

LYS

GLY

ALA

TYR

GLY

TYR

ASP

8

VAL

GLN

LEU

THR

LEU

LYS

GLU

ASP

ILE

9

ARG

LEU

MET

VAL

ASN

CYS

ILE

LEU

PHE

10

ASN

GLY

ALA

GLU

GLY

ALA

TYR

ALA

ASP

ALA

11

ALA

ARG

THR

PHE

GLU

LYS

PHE

ALA

MET

GLY

12

LYS

ILE

ASP

ALA

TYR

ILE

SER

GLN

LYS

VAL

13

GLY

LEU

GLU

Samples:

sample_1: entity_1, [U-13C, U-15N], mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.8 mM; pH: 6.8; pressure: 1 atm; temperature: 293 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 CBCA(CO)NH	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 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, GUNTERT, MUMENTHALER AND WUTHRICH - refinement

NMR spectrometers:

BRUKER DMX 600 MHz

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