BMRB Entry 31185

Name: Solution NMR structure of a single-state de novo alternative conformation (design 6306) of the N-terminal domain of chicken troponin C (E41A mutant)
Published: 2025-05-29

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PDB ID: 9cif
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31185
MolProbity Validation Chart

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NMR-STAR v3 text file.
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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 NMR structure of a single-state de novo alternative conformation (design 6306) of the N-terminal domain of chicken troponin C (E41A mutant)

Deposition date:

2024-07-03

Original release date:

2025-05-29

Authors:

Guo, A.; Kelly, M.; Kortemme, T.

Citation:

Citation: Guo, Amy; Akpinaroglu, Deniz; Stephens, Christina; Grabe, Michael; Smith, Colin; Kelly, Mark; Kortemme, Tanja. "Deep learning-guided design of dynamic proteins" Science 388, eadr7094-eadr7094 (2025).
PubMed: 40403060

Assembly members:

Assembly members:
entity_1, polymer, 94 residues, 10298.522 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32630 Superkingdom: not available Kingdom: not available Genus/species: synthetic construct

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET-28a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMASMSDEQAEARAFLSE EMIAEFKAAFDMFDADGGGE ISAKAFGTVARMNNVPVDPR VQEYVKRLTDQDGSGTISFE EFLVLMVKSMKQDA

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	286
15N chemical shifts	94
1H chemical shifts	619

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 94 residues - 10298.522 Da.

1

GLY

SER

HIS

MET

ALA

SER

MET

SER

ASP

GLU

2

GLN

ALA

GLU

ALA

ARG

ALA

PHE

LEU

SER

GLU

3

GLU

MET

ILE

ALA

GLU

PHE

LYS

ALA

PHE

4

ASP

MET

PHE

ASP

ALA

ASP

GLY

GLU

5

ILE

SER

ALA

LYS

ALA

PHE

GLY

THR

VAL

ALA

6

ARG

MET

ASN

VAL

PRO

VAL

ASP

PRO

ARG

7

VAL

GLN

GLU

TYR

VAL

LYS

ARG

LEU

THR

ASP

8

GLN

ASP

GLY

SER

GLY

THR

ILE

SER

PHE

GLU

9

GLU

PHE

LEU

VAL

LEU

MET

VAL

LYS

SER

MET

10

LYS

GLN

ASP

ALA

Samples:

sample_1: Single-state design 6306, [U-99% 13C; U-99% 15N], 400 uM; potassium chloride 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.7; pressure: 1 atm; temperature: 298.1 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	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
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDCEHE	sample_1	isotropic	sample_conditions_1
2D HBCBCGCDHD	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH v3.7, Schwieters, Kuszewski, Tjandra and Clore - refinement

ARTINA, Klukowski, P., Riek, R. and Guntert, P. - chemical shift assignment, peak picking, structure calculation

NMR spectrometers:

Bruker AVANCE 800 MHz
Bruker AVANCE 600 MHz

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