BMRB Entry 34965

Name: NMR solution structure of the GEFH1 C1 domain
Published: 2025-10-31

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PDB ID: 9h75
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34965
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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:

NMR solution structure of the GEFH1 C1 domain

Deposition date:

2024-10-26

Original release date:

2025-10-31

Authors:

Choi, S.; Gossert, A.; Steinmetz, M.

Citation:

Citation: Choi, S.; Gossert, A.; Steinmetz, M.. "NMR solution structure of the GEFH1 C1 domain" .

Assembly members:

Assembly members:
entity_1, polymer, 75 residues, 8250.749 Da.
entity_ZN, non-polymer, 65.409 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GPMKEAKDARYTNGHLFTTI SVSGMTMCYACNKSITAKEA LICPTCNVTIHNRCKDTLAN CTKVKQKQQKAALLK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	254
15N chemical shifts	82
1H chemical shifts	532

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2
3	unit_3	2

Entities:

Entity 1, unit_1 75 residues - 8250.749 Da.

1

GLY

PRO

MET

LYS

GLU

ALA

LYS

ASP

ALA

ARG

2

TYR

THR

ASN

GLY

HIS

LEU

PHE

THR

ILE

3

SER

VAL

SER

GLY

MET

THR

MET

CYS

TYR

ALA

4

CYS

ASN

LYS

SER

ILE

THR

ALA

LYS

GLU

ALA

5

LEU

ILE

CYS

PRO

THR

CYS

ASN

VAL

THR

ILE

6

HIS

ASN

ARG

CYS

LYS

ASP

THR

LEU

ALA

ASN

7

CYS

THR

LYS

VAL

LYS

GLN

LYS

GLN

LYS

8

ALA

LEU

LYS

Entity 2, unit_2 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: GEFH1 28-100, [U-13C; U-15N], 1.0 ± 0.2 mM; NaCl 150 mM; NaPi 25 mM; D2O, [U-2H], 10 % v/v; H2O 90 % v/v

sample_conditions_1: ionic strength: 175 mM; pH: 7.2; pressure: 1 bar; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNmr Analysis, CCPN - peak picking

NMR spectrometers:

Bruker AVANCE NEO 700 MHz
Bruker AVANCE III HD 600 MHz

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