BMRB Entry 30777

Name: Solution structure of a reconstructed XCL1 ancestor
Published: 2020-12-26

Click here to enlarge.

PDB ID: 7jh1
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30777
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of a reconstructed XCL1 ancestor

Deposition date:

2020-07-20

Original release date:

2020-12-26

Authors:

Tyler, R.; Peterson, F.; Volkman, B.

Citation:

Citation: Dishman, A.; Tyler, R.; Fox, J.; Kleist, A.; Prehoda, K.; Babu, M.; Peterson, F.; Volkman, B.. "Evolution of fold switching in a metamorphic protein" Science 371, 86-90 (2021).
PubMed: 33384377

Assembly members:

Assembly members:
entity_1, polymer, 64 residues, 7483.078 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: 32644 Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ARKSCCLKYTKRPLPLKRIK SYTIQSNEACNIKAIIFTTK KGRKICANPNEKWVQKAMKH LDKK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	289
15N chemical shifts	64
1H chemical shifts	418

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 64 residues - 7483.078 Da.

1

ALA

ARG

LYS

SER

CYS

LEU

LYS

TYR

THR

2

LYS

ARG

PRO

LEU

PRO

LEU

LYS

ARG

ILE

LYS

3

SER

TYR

THR

ILE

GLN

SER

ASN

GLU

ALA

CYS

4

ASN

ILE

LYS

ALA

ILE

PHE

THR

LYS

5

LYS

GLY

ARG

LYS

ILE

CYS

ALA

ASN

PRO

ASN

6

GLU

LYS

TRP

VAL

GLN

LYS

ALA

MET

LYS

HIS

7

LEU

ASP

LYS

Samples:

sample_1: Anc.0, [U-99% 13C; U-99% 15N], 1.0 mM; sodium phosphate 20 mM; sodium azide 0.02%

sample_conditions_1: ionic strength: 29 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

TopSpin v3, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY, Bartels et al. - data analysis, peak picking

GARANT, Bartels, Guntert, Billeter and Wuthrich - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

TALOS, Cornilescu, Delaglio and Bax - data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - geometry optimization

NMR spectrometers:

Bruker AVANCE DRX 600.13 MHz

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