BMRB Entry 25627

Name: Solution structure of the meiosis-expressed gene 1 (Meig1)
Published: 2016-01-19

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PDB ID: 2n2y
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/BMR25627
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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 meiosis-expressed gene 1 (Meig1)

Deposition date:

2015-05-16

Original release date:

2016-01-19

Authors:

Williams, David; Walavalkar, Ninad; Buchwald, William

Citation:

Citation: Li, Wei; Walavalkar, Ninad; Buchwald, William; Teves, Maria; Zhang, Ling; Liu, Junping; Bilinovich, S.; Peterson, Darrell; Strauss, Jerome; Williams, David; Zhang, Zhibing. "Dissecting the structural basis of MEIG1 interaction with PACRG" Sci. Rep. 6, 18278-18278 (2016).
PubMed: 26726850

Assembly members:

Assembly members:
entity, polymer, 92 residues, 11256.876 Da.

Natural source:

Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSHMMATSDVKPKSISRAKK WSEEIENLYRFQQAGYRDEI EYKQVKQVAMVDRWPETGYV KKLQRRDNTFFYYNKERECE DKEVHKVKVYVY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	410
15N chemical shifts	99
1H chemical shifts	623

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 92 residues - 11256.876 Da.

1

GLY

SER

HIS

MET

ALA

THR

SER

ASP

VAL

2

LYS

PRO

LYS

SER

ILE

SER

ARG

ALA

LYS

3

TRP

SER

GLU

ILE

GLU

ASN

LEU

TYR

ARG

4

PHE

GLN

ALA

GLY

TYR

ARG

ASP

GLU

ILE

5

GLU

TYR

LYS

GLN

VAL

LYS

GLN

VAL

ALA

MET

6

VAL

ASP

ARG

TRP

PRO

GLU

THR

GLY

TYR

VAL

7

LYS

LEU

GLN

ARG

ASP

ASN

THR

PHE

8

PHE

TYR

ASN

LYS

GLU

ARG

GLU

CYS

GLU

9

ASP

LYS

GLU

VAL

HIS

LYS

VAL

LYS

VAL

TYR

10

VAL

TYR

Samples:

sample_1: sodium phosphate 10 mM; Meig1, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 40 mM; pH: 6.5; pressure: 1 atm; temperature: 298 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 C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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 H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D IPAP-HSQC	sample_1	anisotropic	sample_conditions_1
2D IPAP-HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNMR, CCPN - data analysis

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 700 MHz
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