BMRB Entry 36330

Name: Solution NMR structure of NF5; de novo designed protein with a novel fold
Published: 2021-03-29

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PDB ID: 7bpp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36330
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 NF5; 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, 109 residues, 12920.676 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: GEDDEILQRAKDILKEDPNR KILIILNPDGKIELYEVTSE EDIKRIAKKAGISEELLRRI LQSFRDGQYDLFFIAKTEDD ERRARELKERMGKPVEILRG SLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	467
15N chemical shifts	110
1H chemical shifts	761

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_1 109 residues - 12920.676 Da.

1

GLY

GLU

ASP

GLU

ILE

LEU

GLN

ARG

ALA

2

LYS

ASP

ILE

LEU

LYS

GLU

ASP

PRO

ASN

ARG

3

LYS

ILE

LEU

ILE

LEU

ASN

PRO

ASP

GLY

4

LYS

ILE

GLU

LEU

TYR

GLU

VAL

THR

SER

GLU

5

GLU

ASP

ILE

LYS

ARG

ILE

ALA

LYS

ALA

6

GLY

ILE

SER

GLU

LEU

ARG

ILE

7

LEU

GLN

SER

PHE

ARG

ASP

GLY

GLN

TYR

ASP

8

LEU

PHE

ILE

ALA

LYS

THR

GLU

ASP

9

GLU

ARG

ALA

ARG

GLU

LEU

LYS

GLU

ARG

10

MET

GLY

LYS

PRO

VAL

GLU

ILE

LEU

ARG

GLY

11

SER

LEU

GLU

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 HNCO	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 HCCH-TOCSY aliphatic	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 36330

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: