BMRB Entry 25068

Name: NMR Structure and 1H, 13C and 15N Chemical Shift Assignments for High mobility group protein from Plasmodium falciparum 3D7.
Published: 2014-07-21

Click here to enlarge.

PDB ID: 2mrc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25068
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:

NMR Structure and 1H, 13C and 15N Chemical Shift Assignments for High mobility group protein from Plasmodium falciparum 3D7.

Deposition date:

2014-07-02

Original release date:

2014-07-21

Authors:

Tang, Changyan; Barnwal, Ravi P; Varani, Gabriele

Citation:

Citation: Tang, Changyan; Barnwal, Ravi P; Varani, Gabriele. "NMR Structure and 1H, 13C and 15N Chemical Shift Assignments for High mobility group protein from Plasmodium falciparum 3D7." To be Published ., .-..

Assembly members:

Assembly members:
entity, polymer, 92 residues, 10861.796 Da.

Natural source:

Natural source: Common Name: apicomplexans Taxonomy ID: 36329 Superkingdom: Eukaryota Kingdom: not available Genus/species: Plasmodium falciparum

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MAHHHHHHMKKKDPLAPKRA LSAYMFYVKDKRLEIIKEKP ELAKDVAQVGKLIGEAWGQL SPAQKAPYEKKAQLDKVRYS KEIEEYRKKNQE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
1H chemical shifts	497
13C chemical shifts	351
15N chemical shifts	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 92 residues - 10861.796 Da.

1

MET

ALA

HIS

MET

LYS

2

LYS

ASP

PRO

LEU

ALA

PRO

LYS

ARG

ALA

3

LEU

SER

ALA

TYR

MET

PHE

TYR

VAL

LYS

ASP

4

LYS

ARG

LEU

GLU

ILE

LYS

GLU

LYS

PRO

5

GLU

LEU

ALA

LYS

ASP

VAL

ALA

GLN

VAL

GLY

6

LYS

LEU

ILE

GLY

GLU

ALA

TRP

GLY

GLN

LEU

7

SER

PRO

ALA

GLN

LYS

ALA

PRO

TYR

GLU

LYS

8

LYS

ALA

GLN

LEU

ASP

LYS

VAL

ARG

TYR

SER

9

LYS

GLU

ILE

GLU

TYR

ARG

LYS

ASN

10

GLN

GLU

Samples:

sample_1: High mobility group protein, [U-95% 13C; U-95% 15N], 0.9 mM; H2O 93%; D20 7%

sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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 HNCO	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution, refinement

CCPNMR, CCPN - data analysis, chemical shift assignment, peak picking

NMR spectrometers:

Bruker AMX 500 MHz
Bruker Avance 800 MHz