Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53279

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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:

Lag20 artificial IDP, backbone chemical shifts

Deposition date:

2025-07-11

Original release date:

2026-06-11

Authors:

Kobayashi, Ryoga; Miyanoiri, Yohei; Yoshida, Norio; Ekari, Miu; Nakamura, Hideki; Tochio, Hidehito; Kodama, Takashi; Sekiyama, Naotaka

Citation:

Citation: Kobayashi, Ryoga. "Sequence-encoded conformational biases correlate with self-assembly modes of intrinsically disordered proteins " PNAS Nexus ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 91 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHHHHHHHSENL YFQGPMVPGGSASQRNQAQV YYFPYSGPPGSGNQENQTQV WYWPYGAPPGSGNQQSQTQV LYWPVGAPMGQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	192
15N chemical shifts	64
1H chemical shifts	64

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	His-TEV-Lag20	1

Entities:

Entity 1, His-TEV-Lag20 91 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

HIS

SER

GLU

ASN

LEU

3

TYR

PHE

GLN

GLY

PRO

MET

VAL

PRO

GLY

4

SER

ALA

SER

GLN

ARG

ASN

GLN

ALA

GLN

VAL

5

TYR

PHE

PRO

TYR

SER

GLY

PRO

GLY

6

SER

GLY

ASN

GLN

GLU

ASN

GLN

THR

GLN

VAL

7

TRP

TYR

TRP

PRO

TYR

GLY

ALA

PRO

GLY

8

SER

GLY

ASN

GLN

SER

GLN

THR

GLN

VAL

9

LEU

TYR

TRP

PRO

VAL

GLY

ALA

PRO

MET

GLY

10

GLN

Samples:

sample_1: His-TEV-Lag20, [U-13C; U-15N], 500 uM; D2O, [U-100% 2H], 5%; DTT 1 mM; MES 50 mM; sodium chloride 150 mM; 1,6-hexanediol 12%

sample_conditions_1: pH: 6.5; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.2 - collection

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker AVANCE III 600 MHz

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

BMRB Entry 53279