BMRB Entry 36329

Name: Solution NMR structure of NF7; de novo designed protein with a novel fold
Published: 2021-03-29

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PDB ID: 7bpn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36329
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:

Solution NMR structure of NF7; de novo designed protein with a novel fold

Deposition date:

2020-03-23

Original release date:

2021-03-29

Authors:

Kobayashi, N.; Sugiki, T.; Fujiwara, T.; Minami, S.; Koga, R.; Chikenji, G.; Koga, N.

Citation:

Citation: MInami, S.; Kobayashi, N.; Sugiki, T.; Nagashima, T.; Fujiwara, T.; Koga, R.; Chikenji, G.; Koga, N.. "Exploration of novel alpha-beta protein folds through de novo design" Nat. Struct. Mol. Biol. 30, 1132-1140 (2023).
PubMed: 37400653

Assembly members:

Assembly members:
entity_1, polymer, 124 residues, 14352.258 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GQIQYFNVDENPEQVRKLIE QAGLDPDELREAEVIIIIIS RTPEQLEKLSRQVKELGADR LLEFNVDENPEQASKLAKTA GISEKQLREADYIILILVRD EKKAKKFADSLRKKGSLEHH HHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	518
15N chemical shifts	124
1H chemical shifts	844

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_1 124 residues - 14352.258 Da.

1

GLY

GLN

ILE

GLN

TYR

PHE

ASN

VAL

ASP

GLU

2

ASN

PRO

GLU

GLN

VAL

ARG

LYS

LEU

ILE

GLU

3

GLN

ALA

GLY

LEU

ASP

PRO

ASP

GLU

LEU

ARG

4

GLU

ALA

GLU

VAL

ILE

SER

5

ARG

THR

PRO

GLU

GLN

LEU

GLU

LYS

LEU

SER

6

ARG

GLN

VAL

LYS

GLU

LEU

GLY

ALA

ASP

ARG

7

LEU

GLU

PHE

ASN

VAL

ASP

GLU

ASN

PRO

8

GLU

GLN

ALA

SER

LYS

LEU

ALA

LYS

THR

ALA

9

GLY

ILE

SER

GLU

LYS

GLN

LEU

ARG

GLU

ALA

10

ASP

TYR

ILE

LEU

ILE

LEU

VAL

ARG

ASP

11

GLU

LYS

ALA

LYS

PHE

ALA

ASP

SER

12

LEU

ARG

LYS

GLY

SER

LEU

GLU

HIS

13

HIS

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
3D BEST HNCO	sample_1	isotropic	sample_conditions_1
3D BEST HNCACB	sample_1	isotropic	sample_conditions_1
3D BEST HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY aromatic	sample_1	isotropic	sample_conditions_1
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
2D 1H-15N HSQC IPAP	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC IPAP	sample_2	anisotropic	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 36329

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: