BMRB Entry 34115

Name: Solution structure of detergent-solubilized Rcf1, a yeast mitochondrial inner membrane protein involved in respiratory Complex III/IV supercomplex formation
Published: 2018-02-23

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PDB ID: 5nf8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34115
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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 detergent-solubilized Rcf1, a yeast mitochondrial inner membrane protein involved in respiratory Complex III/IV supercomplex formation

Deposition date:

2017-03-13

Original release date:

2018-02-23

Authors:

Zhou, S.; Pettersson, P.; Sjoholm, J.; Sjostrand, D.; Hogbom, M.; Brzezinski, P.; Maler, L.; Adelroth, P.

Citation:

Citation: Zhou, Shu; Pettersson, Pontus; Huang, Jingjing; Sjoholm, Johannes; Sjostrand, Dan; Pomes, Regis; Hogbom, Martin; Brzezinski, Peter; Maler, Lena; Adelroth, Pia. "Solution NMR structure of yeast Rcf1, a protein involved in respiratory supercomplex formation." Proc. Natl. Acad. Sci. U.S.A. 115, 3048-3053 (2018).
PubMed: 29507228

Assembly members:

Assembly members:
entity_1, polymer, 174 residues, 20388.496 Da.

Natural source:

Natural source: Common Name: Baker's yeast Taxonomy ID: 4932 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSRMPSSFDVTERDLDDMTF GERIIYHCKKQPLVPIGCLL TTGAVILAAQNVRLGNKWKA QYYFRWRVGLQAATLVALVA GSFIYGTSGKELKAKEEQLK EKAKMREKLWIQELERREEE TEARRKRAELARMKTLENEE EIKNLEKELSDLENKLGKKE FRVPGSHHHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	623
15N chemical shifts	149
1H chemical shifts	1007

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, 1	1
2	entity_1, 2	1

Entities:

Entity 1, entity_1, 1 174 residues - 20388.496 Da.

1

MET

SER

ARG

MET

PRO

SER

PHE

ASP

VAL

2

THR

GLU

ARG

ASP

LEU

ASP

MET

THR

PHE

3

GLY

GLU

ARG

ILE

TYR

HIS

CYS

LYS

4

GLN

PRO

LEU

VAL

PRO

ILE

GLY

CYS

LEU

5

THR

GLY

ALA

VAL

ILE

LEU

ALA

GLN

6

ASN

VAL

ARG

LEU

GLY

ASN

LYS

TRP

LYS

ALA

7

GLN

TYR

PHE

ARG

TRP

ARG

VAL

GLY

LEU

8

GLN

ALA

THR

LEU

VAL

ALA

LEU

VAL

ALA

9

GLY

SER

PHE

ILE

TYR

GLY

THR

SER

GLY

LYS

10

GLU

LEU

LYS

ALA

LYS

GLU

GLN

LEU

LYS

11

GLU

LYS

ALA

LYS

MET

ARG

GLU

LYS

LEU

TRP

12

ILE

GLN

GLU

LEU

GLU

ARG

GLU

13

THR

GLU

ALA

ARG

LYS

ARG

ALA

GLU

LEU

14

ALA

ARG

MET

LYS

THR

LEU

GLU

ASN

GLU

15

GLU

ILE

LYS

ASN

LEU

GLU

LYS

GLU

LEU

SER

16

ASP

LEU

GLU

ASN

LYS

LEU

GLY

LYS

GLU

17

PHE

ARG

VAL

PRO

GLY

SER

HIS

18

HIS

Samples:

sample_2: rcf1, [U-13C; U-15N; U-2H], 0.4 mM

sample_3: rcf1, [U-13C; U-15N], 0.4 mM

sample_4: rcf1, [U-13C; U-15N; 50% U-2H], 0.4 mM

sample_5: rcf1, [U-15N; U-2H; 99%-1HD, 13CD-IL; 99%-1HG, 13CG-V], 0.4 mM

sample_6: rcf1, [U-50% 13C; U-50% 15N; U-50% 12C; U-50% 14N], 0.4 mM

sample_1: rcf1, [U-15N], 0.4 mM

sample_conditions_1: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_2: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_3: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_4: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_5: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_6: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HN(COCA)CB	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D HN(CO)CA	sample_2	isotropic	sample_conditions_2
3D N-NOESY-HSQC	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_3
3D CC(CO)NH	sample_3	isotropic	sample_conditions_3
3D H(CCO)NH	sample_3	isotropic	sample_conditions_3
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_3
3D N-NOESY-HSQC	sample_3	isotropic	sample_conditions_3
3D C-NOESY-HSQC	sample_3	isotropic	sample_conditions_3
2D 1H-13C HSQC	sample_4	isotropic	sample_conditions_4
3D N-NOESY-HSQC	sample_4	isotropic	sample_conditions_4
3D C-NOESY-HSQC	sample_4	isotropic	sample_conditions_4
2D 1H-13C HSQC	sample_5	isotropic	sample_conditions_5
3D C-NOESY-HSQC	sample_5	isotropic	sample_conditions_5
3D F1-13C/15N-filtered, F3-15N-edited-NOESY-HSQC	sample_6	isotropic	sample_conditions_6
3D F1-13C/15N-filtered, F3-13C-edited-NOESY-HSQC	sample_6	isotropic	sample_conditions_6

Software:

TOPSPIN, Bruker Biospin - collection

CcpNMR, CCPN - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMR spectrometers:

Bruker AvanceIII 900 MHz
Bruker AvanceIII 700 MHz

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