BMRB Entry 30527

Name: De novo Designed Protein Foldit3
Published: 2019-06-07

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PDB ID: 6msp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30527
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:

De novo Designed Protein Foldit3

Deposition date:

2018-10-17

Original release date:

2019-06-07

Authors:

Liu, G.; Ishida, Y.; Swapna, G.; Kleinfelter, S.; Koepnick, B.; Baker, D.; Montelione, G.

Citation:

Citation: Koepnick, Brian; Flatten, Jeff; Husain, Tamir; Ford, Alex; Silva, Daniel-Adriano; Bick, Matthew; Bauer, Aaron; Liu, Gaohua; Ishida, Yojiro; Boykov, Alexander; Estep, Roger; Kleinfelter, Susan; Norgard-Solano, Toke; Wei, Linda; Players, Foldit; Montelione, Gaetano; DiMaio, Frank; Popovic, Zoran; Khatib, Firas; Cooper, Seth; Baker, David. "De novo protein design by citizen scientists." Nature 570, 390-394 (2019).
PubMed: 31168091

Assembly members:

Assembly members:
entity_1, polymer, 97 residues, 11725.060 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli K-12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGHHHHHHENLYFQSHMTDE LLERLRQLFEELHERGTEIV VEVHINGERDEIRVRNISKE ELKKLLERIREKIEREGSSE VEVNVHSGGQTWTFNEK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	285
15N chemical shifts	92
1H chemical shifts	605

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 97 residues - 11725.060 Da.

1

MET

GLY

HIS

GLU

ASN

2

LEU

TYR

PHE

GLN

SER

HIS

MET

THR

ASP

GLU

3

LEU

GLU

ARG

LEU

ARG

GLN

LEU

PHE

GLU

4

GLU

LEU

HIS

GLU

ARG

GLY

THR

GLU

ILE

VAL

5

VAL

GLU

VAL

HIS

ILE

ASN

GLY

GLU

ARG

ASP

6

GLU

ILE

ARG

VAL

ARG

ASN

ILE

SER

LYS

GLU

7

GLU

LEU

LYS

LEU

GLU

ARG

ILE

ARG

8

GLU

LYS

ILE

GLU

ARG

GLU

GLY

SER

GLU

9

VAL

GLU

VAL

ASN

VAL

HIS

SER

GLY

GLN

10

THR

TRP

THR

PHE

ASN

GLU

LYS

Samples:

sample_1: foldit3, [U-13C; U-15N], 0.3 ± 0.05 mM

sample_conditions_1: ionic strength: 0.2 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStructure, Huang, Tejero, Powers and Montelione - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

SPARKY, Goddard - peak picking

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceIII 600 MHz

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