BMRB Entry 36418

Name: Solution structure of Terfa derived from Danio rerio
Published: 2025-11-01

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PDB ID: 7elk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36418
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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 Terfa derived from Danio rerio

Deposition date:

2021-04-11

Original release date:

2025-11-01

Authors:

Yun, J.; Kim, M.; Lee, W.

Citation:

Citation: Kim, M.; Yun, J.; Lee, W.. "Solution structure of Terfa derived from Danio rerio" .

Assembly members:

Assembly members:
Terfa protein, polymer, 63 residues, 7469.786 Da.

Natural source:

Natural source: Common Name: leopard danio Taxonomy ID: 7955 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Danio rerio

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Terfa protein: STAPAKKYTRKMWSVQESEW LKQGVVRYGVGHWERIRSAF PFAGRTAVNLKDRWRTMVKL KMV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	231
15N chemical shifts	54
1H chemical shifts	365

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 63 residues - 7469.786 Da.

1

SER

THR

ALA

PRO

ALA

LYS

TYR

THR

ARG

2

LYS

MET

TRP

SER

VAL

GLN

GLU

SER

GLU

TRP

3

LEU

LYS

GLN

GLY

VAL

ARG

TYR

GLY

VAL

4

GLY

HIS

TRP

GLU

ARG

ILE

ARG

SER

ALA

PHE

5

PRO

PHE

ALA

GLY

ARG

THR

ALA

VAL

ASN

LEU

6

LYS

ASP

ARG

TRP

ARG

THR

MET

VAL

LYS

LEU

7

LYS

MET

VAL

Samples:

sample_1: Terfa, [U-13C; U-15N], 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_2: Terfa, [U-15N], 1 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0 pH*; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D-NOESY	sample_1	anisotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	anisotropic	sample_conditions_1
3D HNCACB	sample_1	anisotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	anisotropic	sample_conditions_1
3D HNCO	sample_1	anisotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	anisotropic	sample_conditions_1
2D 1H-15N HSQC NH2 only	sample_1	anisotropic	sample_conditions_1

Software:

NMRPipe v2.2.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky v2.2.5, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - peak picking

XwinNMR, Bruker Biospin - collection

NMR spectrometers:

Bruker AVANCE DRX 600 MHz
Bruker AVANCE DRX 850 MHz

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