BMRB Entry 53396

Name: Chemical shifts of the full-length ATPase inhibitory factor 1 (IF1) homodimer
Published: 2025-10-21

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53396

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Chemical shifts of the full-length ATPase inhibitory factor 1 (IF1) homodimer

Deposition date:

2025-10-17

Original release date:

2025-10-21

Authors:

Jerolamon Martinez, Julia; Alder, Nathan; Alexandrescu, Andrei

Citation:

Citation: Jerolamon Martinez, Julia; Alder, Nathan; Alexandrescu, Andrei. "Chemical shifts of the full-length ATPase inhibitory factor 1 (IF1) homodimer" Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 81 residues, 9516.56 Da.

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSDQSENVDRGAGSIREAGG AFGKREQAEEERYFRAQSRE QLAALKKHHEEEIVHHKKEI ERLQKEIERHKQKIKMLKHD D

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	313
15N chemical shifts	86
1H chemical shifts	494

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	IF1, chain 1	1
2	IF1, chain 2	1

Entities:

Entity 1, IF1, chain 1 81 residues - 9516.56 Da.

1

GLY

SER

ASP

GLN

SER

GLU

ASN

VAL

ASP

ARG

2

GLY

ALA

GLY

SER

ILE

ARG

GLU

ALA

GLY

3

ALA

PHE

GLY

LYS

ARG

GLU

GLN

ALA

GLU

4

GLU

ARG

TYR

PHE

ARG

ALA

GLN

SER

ARG

GLU

5

GLN

LEU

ALA

LEU

LYS

HIS

GLU

6

GLU

ILE

VAL

HIS

LYS

GLU

ILE

7

GLU

ARG

LEU

GLN

LYS

GLU

ILE

GLU

ARG

HIS

8

LYS

GLN

LYS

ILE

LYS

MET

LEU

LYS

HIS

ASP

9

ASP

Samples:

sample_1: ATPase inhibitor, mitochondrial, [U-100% 13C; U-100% 15N], 110 uM; potassium phosphate 25 mM; sodium chloride 0.2 M; D2O, [U-2H], 10 % v/v; H2O 90 % v/v

sample_2: ATPase inhibitor, mitochondrial, [U-100% 13C; U-100% 15N], 110 uM; potassium phosphate 25 mM; sodium chloride 0.2 M; D2O, [U-2H], 100 % v/v

sample_3: ATPase inhibitor, mitochondrial, [U-100% 13C; U-100% 15N; U-80% 2H], 446 uM; potassium phosphate 25 mM; sodium chloride 0.2 M; D2O, [U-2H], 5 % v/v; H2O 95 % v/v

sample_conditions_1: ionic strength: 0.209 M; pH: 5.3; pressure: 1 atm; temperature: 310.15 K

sample_conditions_2: ionic strength: 0.209 M; pH: 5.6; pressure: 1 atm; temperature: 310.15 K

sample_conditions_3: ionic strength: 0.209 M; pH: 5.3; pressure: 1 atm; temperature: 310.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_2
3D CCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_2
3D 1H-15N TOCSY	sample_3	isotropic	sample_conditions_3
3D 1H-15N NOESY	sample_3	isotropic	sample_conditions_3
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_3

Software:

ANALYSIS v2.5.2 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 600 MHz