BMRB Entry 30021

Name: Solution structure of the pore-forming region of C. elegans Mitochondrial Calcium Uniporter (MCU)
Published: 2016-05-23

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PDB ID: 5id3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30021
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution structure of the pore-forming region of C. elegans Mitochondrial Calcium Uniporter (MCU) PubMed: 27135929

Deposition date: 2016-02-23 Original release date: 2016-05-23

Authors: Oxenoid, K.; Dong, Y.; Cao, C.; Cui, T.; Sancak, Y.; Markhard, A.; Grabarek, Z.; Kong, L.; Liu, Z.; Ouyang, B.; Cong, Y.; Mootha, V.; Chou, J.

Citation: Oxenoid, K.; Dong, Y.; Cao, C.; Cui, T.; Sancak, Y.; Markhard, A.; Grabarek, Z.; Kong, L.; Liu, Z.; Ouyang, B.; Cong, Y.; Mootha, V.; Chou, J.. "Architecture of the Mitochondrial Calcium Uniporter" Nature 533, 269-273 (2016).

Assembly members:
Mitochondrial Calcium Uniporter, polymer, 159 residues, 18927.207 Da.

Natural source: Common Name: nematodes Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans

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

Entity Sequences (FASTA):
Mitochondrial Calcium Uniporter: MAALSVDEYKLSREKKLLLQ LENAETLLAPLHDAKRKIEQ EAEAHTDRVAWAGFAASGVQ TGLFARLTWWEYSWDIVEPV TYFATYSTVAATFGYYLYTQ QSFEYPSARERVYTKQFYRR AQKQNFDIEKYNRLVTEVDE LRNQLKRLRDPLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	385
15N chemical shifts	136
1H chemical shifts	136

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity 1	1
2	entity 2	1
3	entity 3	1
4	entity 4	1
5	entity 5	1

Entities:

Entity 1, entity 1 159 residues - 18927.207 Da.

1

MET

ALA

LEU

SER

VAL

ASP

GLU

TYR

LYS

2

LEU

SER

ARG

GLU

LYS

LEU

GLN

3

LEU

GLU

ASN

ALA

GLU

THR

LEU

ALA

PRO

4

LEU

HIS

ASP

ALA

LYS

ARG

LYS

ILE

GLU

GLN

5

GLU

ALA

GLU

ALA

HIS

THR

ASP

ARG

VAL

ALA

6

TRP

ALA

GLY

PHE

ALA

SER

GLY

VAL

GLN

7

THR

GLY

LEU

PHE

ALA

ARG

LEU

THR

TRP

8

GLU

TYR

SER

TRP

ASP

ILE

VAL

GLU

PRO

VAL

9

THR

TYR

PHE

ALA

THR

TYR

SER

THR

VAL

ALA

10

ALA

THR

PHE

GLY

TYR

LEU

TYR

THR

GLN

11

GLN

SER

PHE

GLU

TYR

PRO

SER

ALA

ARG

GLU

12

ARG

VAL

TYR

THR

LYS

GLN

PHE

TYR

ARG

13

ALA

GLN

LYS

GLN

ASN

PHE

ASP

ILE

GLU

LYS

14

TYR

ASN

ARG

LEU

VAL

THR

GLU

VAL

ASP

GLU

15

LEU

ARG

ASN

GLN

LEU

LYS

ARG

LEU

ARG

ASP

16

PRO

LEU

GLU

HIS

Samples:

sample_1: EDTA 2 ± 1 mM; Foscholine-14 27 ± 5 mM; MCU-dNTD, [100% 13C; 100% 15N; 85% 2H], 0.8 ± 0.05 mM; MES 20 ± 1 mM; NaCl 75 ± 1 mM; NaN3 0.3 ± 0.5 mM; H2O 95%; D2O 5%

sample_2: EDTA 2 ± 1 mM; Foscholine-14, [100% 2H at acyl chain], 27 ± 5 mM; MCU-dNTD, [100% 13C; 100% 15N], 0.8 ± 0.05 mM; MES 20 ± 1 mM; NaCl 75 ± 1 mM; NaN3 0.3 ± 0.5 mM; H2O 95%; D2O 5%

sample_3: EDTA 2 ± 1 mM; Foscholine-14, [100% 2H at acyl chain], 27 ± 5 mM; MCU-dNTD-1, [100% 15N; 100% 2H], 0.4 ± 0.05 mM; MCU-dNTD-2, [15% 13C], 0.4 ± 0.05 mM; MES 20 ± 1 mM; NaCl 75 ± 1 mM; NaN3 0.3 ± 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 306 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 306 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D tr-HNCA	sample_1	isotropic	sample_conditions_2
3D tr-HN(CO)CA	sample_1	isotropic	sample_conditions_2
3D tr-HN(CA)CO	sample_1	isotropic	sample_conditions_2
3D tr-HNCO	sample_1	isotropic	sample_conditions_2
3D tr-HN(CA)CB	sample_1	isotropic	sample_conditions_2
3D 15N-15N HSQC-NOESY-TROSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY-TROSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY-TROSY	sample_2	isotropic	sample_conditions_2
3D 1H-13C Methyl NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C Methyl NOESY	sample_2	isotropic	sample_conditions_2
3D 1H-15N NOESY-TROSY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY-TROSY	sample_3	isotropic	sample_conditions_2
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_3	isotropic	sample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

XEASY, Bartels et al. - chemical shift assignment

XPLOR-NIH, Schwieters et al - structure calculation

NMR spectrometers:

Bruker AvanceII 600 MHz
Bruker AvanceIII 900 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts