BMRB Entry 30970

Name: NMR structure of a designed cold unfolding four helix bundle
Published: 2022-02-25

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PDB ID: 7t03
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30970
MolProbity Validation Chart

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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 structure of a designed cold unfolding four helix bundle

Deposition date:

2021-11-29

Original release date:

2022-02-25

Authors:

Pulavarti, S.; Szyperski, T.; Yuen, S.; Maguire, J.; Griffin, J.; Kuhlman, B.

Citation:

Citation: Pulavarti, Surya; Maguire, Jack; Yuen, Shirley; Harrison, Joseph; Griffin, Jermel; Premkumar, Lakshmanane; Esposito, Edward; Makhatadze, George; Garcia, Angel; Weiss, Thomas; Snell, Edward; Kuhlman, Brian; Szyperski, Thomas. "From Protein Design to the Energy Landscape of a Cold Unfolding Protein" J. Phys. Chem. B 126, 1212-1231 (2022).
PubMed: 35128921

Assembly members:

Assembly members:
entity_1, polymer, 104 residues, 12099.824 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)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHQEYIKKVADELKENSQN INDLLKEVEKNPEDMEYWNK IYRLLHTNKEIAETAGFSSV AKVEHTAMNLVDKMLNSEIK ITSDLIDKIKKKVDMSTREI DKKV

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	461
15N chemical shifts	109
1H chemical shifts	764

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_1 104 residues - 12099.824 Da.

1

GLY

SER

HIS

GLN

GLU

TYR

ILE

LYS

VAL

2

ALA

ASP

GLU

LEU

LYS

GLU

ASN

SER

GLN

ASN

3

ILE

ASN

ASP

LEU

LYS

GLU

VAL

GLU

LYS

4

ASN

PRO

GLU

ASP

MET

GLU

TYR

TRP

ASN

LYS

5

ILE

TYR

ARG

LEU

HIS

THR

ASN

LYS

GLU

6

ILE

ALA

GLU

THR

ALA

GLY

PHE

SER

VAL

7

ALA

LYS

VAL

GLU

HIS

THR

ALA

MET

ASN

LEU

8

VAL

ASP

LYS

MET

LEU

ASN

SER

GLU

ILE

LYS

9

ILE

THR

SER

ASP

LEU

ILE

ASP

LYS

ILE

LYS

10

LYS

VAL

ASP

MET

SER

THR

ARG

GLU

ILE

11

ASP

LYS

VAL

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
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 30970

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: