BMRB Entry 34921

Name: Solution structure of Tx33.1 from Conus textile
Published: 2025-06-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34921

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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 Tx33.1 from Conus textile

Deposition date:

2024-06-19

Original release date:

2025-06-24

Authors:

Ellgaard, L.; Khilji, M.; Hackney, C.; Teilum, K.

Citation:

Citation: Khilji, M.; Hackney, C.; Koch, T.; Hone, A.; Rogalski, A.; Watkins, M.; Olivera, B.; McIntosh, M.; Safavi-Hemami, H.; Teilum, K.; Ellgaard, L.. "Solution structure of Tx33.1 from Conus textile" .

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 13735.990 Da.

Natural source:

Natural source: Common Name: Conus textile Taxonomy ID: 6494 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Conus textile

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: KSHTTCPTSTEIDSCSNDNN ACGKDVSGSCSSLCNCGNGQ TCFTDSNHTITLVPYYTEDG PFEKKYYTCGDPSELDECYD IDKALEVNESDDPNSVEVLC HCPSDKIYLWIHRGYYICIT PPQP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	456
15N chemical shifts	108
1H chemical shifts	689

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 124 residues - 13735.990 Da.

1

LYS

SER

HIS

THR

CYS

PRO

THR

SER

THR

2

GLU

ILE

ASP

SER

CYS

SER

ASN

ASP

ASN

3

ALA

CYS

GLY

LYS

ASP

VAL

SER

GLY

SER

CYS

4

SER

LEU

CYS

ASN

CYS

GLY

ASN

GLY

GLN

5

THR

CYS

PHE

THR

ASP

SER

ASN

HIS

THR

ILE

6

THR

LEU

VAL

PRO

TYR

THR

GLU

ASP

GLY

7

PRO

PHE

GLU

LYS

TYR

THR

CYS

GLY

8

ASP

PRO

SER

GLU

LEU

ASP

GLU

CYS

TYR

ASP

9

ILE

ASP

LYS

ALA

LEU

GLU

VAL

ASN

GLU

SER

10

ASP

PRO

ASN

SER

VAL

GLU

VAL

LEU

CYS

11

HIS

CYS

PRO

SER

ASP

LYS

ILE

TYR

LEU

TRP

12

ILE

HIS

ARG

GLY

TYR

ILE

CYS

ILE

THR

13

PRO

GLN

PRO

Samples:

sample_1: entity_1 mM; MES 10 mM; sodium chloride 50 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 50 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 HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
13C-NOESY-HSQC	sample_1	isotropic	sample_conditions_1
13C-NOESY-HSQC aromatic	sample_1	isotropic	sample_conditions_1
15N-NOESY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

CcpNmr Analysis, CCPN - peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker AVANCE III HD 600 MHz
Bruker AVANCE III HD 750 MHz

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