Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53512

NMR-STAR file interactive viewer.
NMR-STAR v3 text 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

Please specify the pdb ID.

Title:

Backbone 1H and 15N Chemical Shift Assignments for Human Arf1 (ADP-ribosylation factors) I42S Mutant

Deposition date:

2026-01-22

Original release date:

2026-07-20

Authors:

Peters, Edgar; Koduru, Tejaswi; McCallum, Scott; Yee, Estella; Cherfils, Jacqueline; Royer, Catherine

Citation:

Citation: Peters, Edgar; Koduru, Tejaswi; McCallum, Scott; Yee, Estella; Cherfils, Jacqueline; Royer, Catherine. "Mapping bidirectional allosteric communication in Arf GTPases " Biophys. J. 125, 1506-1515 (2026).
PubMed: 41689259

Assembly members:

Assembly members:
entity_1, polymer, 181 residues, Formula weight is not available
entity_GDP, non-polymer, 443.201 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-15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGNIFANLFKGLFGKKEMRI LMVGLDAAGKTTILYKLKLG ESVTTIPTIGFNVETVEYKN ISFTVWDVGGQDKIRPLWRH YFQNTQGLIFVVDSNDRERV NEAREELMRMLAEDELRDAV LLVFANKQDLPNAMNAAEIT DKLGLHSLRHRNWYIQATCA TSGDGLYEGLDWLSNQLRNQ K

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	133
1H chemical shifts	133

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	1	1
2	2	2

Entities:

Entity 1, 1 181 residues - Formula weight is not available

1

MET

GLY

ASN

ILE

PHE

ALA

ASN

LEU

PHE

LYS

2

GLY

LEU

PHE

GLY

LYS

GLU

MET

ARG

ILE

3

LEU

MET

VAL

GLY

LEU

ASP

ALA

GLY

LYS

4

THR

ILE

LEU

TYR

LYS

LEU

LYS

LEU

GLY

5

GLU

SER

VAL

THR

ILE

PRO

THR

ILE

GLY

6

PHE

ASN

VAL

GLU

THR

VAL

GLU

TYR

LYS

ASN

7

ILE

SER

PHE

THR

VAL

TRP

ASP

VAL

GLY

8

GLN

ASP

LYS

ILE

ARG

PRO

LEU

TRP

ARG

HIS

9

TYR

PHE

GLN

ASN

THR

GLN

GLY

LEU

ILE

PHE

10

VAL

ASP

SER

ASN

ASP

ARG

GLU

ARG

VAL

11

ASN

GLU

ALA

ARG

GLU

LEU

MET

ARG

MET

12

LEU

ALA

GLU

ASP

GLU

LEU

ARG

ASP

ALA

VAL

13

LEU

VAL

PHE

ALA

ASN

LYS

GLN

ASP

LEU

14

PRO

ASN

ALA

MET

ASN

ALA

GLU

ILE

THR

15

ASP

LYS

LEU

GLY

LEU

HIS

SER

LEU

ARG

HIS

16

ARG

ASN

TRP

TYR

ILE

GLN

ALA

THR

CYS

ALA

17

THR

SER

GLY

ASP

GLY

LEU

TYR

GLU

GLY

LEU

18

ASP

TRP

LEU

SER

ASN

GLN

LEU

ARG

ASN

GLN

19

LYS

Entity 2, 2 - C10 H15 N5 O11 P2 - 443.201 Da.

1

GDP

Samples:

sample_1: Arf6 I42S, [U-100% 15N], 0.5 mM; Guanosine 5'-Diphosphate 0.5 mM; Bis-Tris 50 mM; MgCl2 1 mM; NaCl 150 mM

sample_conditions_1: ionic strength: 180 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 15N-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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

BMRB Entry 53512