BMRB Entry 52755

Name: NMR chemical shifts of [15N,13C] DynorphinA (1-17) bound to DYNA_1b7 designed binding protein
Published: 2024-12-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52755

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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:

NMR chemical shifts of [15N,13C] DynorphinA (1-17) bound to DYNA_1b7 designed binding protein

Deposition date:

2024-12-15

Original release date:

2024-12-19

Authors:

Ramelot, Theresa; Gaur, Amit; Wu, Kejia; Baker, David; Montelione, Gaetano

Citation:

Citation: Wu, Kejia. "Sequence-specific targeting of intrinsically disordered protein regions" BioRxiv ., .-. (2024).

Assembly members:

Assembly members:
entity_1, polymer, 17 residues, 2147.5 Da.
entity_2, polymer, 217 residues, 25149.5 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET15_SUMO_NESG

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: YGGFLRRIRPKLKWDNQ
entity_2: MSGKEEEIEKEFEEKKKIIE ENLKEAEEEGEEEAAEKLKE ALKKLEEAIKLHREGANPVE VELEEVTAIILNNLAVLLRE GEEELAKELEKAIKLLEEKK DAPEEERLKAIAIAIIRSVL VLIKWEGGKDEETIEEIEEI LENRENLSLEELREAYVRAE IAYLIESGIDPEAAKKVREK YERGAPLEELLKDIEKIEKE AKKREEEKKGSHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	71
15N chemical shifts	18
1H chemical shifts	118

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	peptide	1
2	protein	2

Entities:

Entity 1, peptide 17 residues - 2147.5 Da.

1

TYR

GLY

PHE

LEU

ARG

ILE

ARG

PRO

2

LYS

LEU

LYS

TRP

ASP

ASN

GLN

Entity 2, protein 217 residues - 25149.5 Da.

1

MET

SER

GLY

LYS

GLU

ILE

GLU

LYS

2

GLU

PHE

GLU

LYS

ILE

GLU

3

GLU

ASN

LEU

LYS

GLU

ALA

GLU

GLY

4

GLU

ALA

GLU

LYS

LEU

LYS

GLU

5

ALA

LEU

LYS

LEU

GLU

ALA

ILE

LYS

6

LEU

HIS

ARG

GLU

GLY

ALA

ASN

PRO

VAL

GLU

7

VAL

GLU

LEU

GLU

VAL

THR

ALA

ILE

8

LEU

ASN

LEU

ALA

VAL

LEU

ARG

GLU

9

GLY

GLU

LEU

ALA

LYS

GLU

LEU

GLU

10

LYS

ALA

ILE

LYS

LEU

GLU

LYS

11

ASP

ALA

PRO

GLU

ARG

LEU

LYS

ALA

12

ILE

ALA

ILE

ALA

ILE

ARG

SER

VAL

LEU

13

VAL

LEU

ILE

LYS

TRP

GLU

GLY

LYS

ASP

14

GLU

THR

ILE

GLU

ILE

GLU

ILE

15

LEU

GLU

ASN

ARG

GLU

ASN

LEU

SER

LEU

GLU

16

GLU

LEU

ARG

GLU

ALA

TYR

VAL

ARG

ALA

GLU

17

ILE

ALA

TYR

LEU

ILE

GLU

SER

GLY

ILE

ASP

18

PRO

GLU

ALA

LYS

VAL

ARG

GLU

LYS

19

TYR

GLU

ARG

GLY

ALA

PRO

LEU

GLU

LEU

20

LEU

LYS

ASP

ILE

GLU

LYS

ILE

GLU

LYS

GLU

21

ALA

LYS

ARG

GLU

LYS

GLY

22

SER

HIS

Samples:

sample_1: peptide, [U-13C; U-15N], 0.14 ± 0.05 mM; sodium chloride 150 ± 5 mM; sodium azide 0.02 ± .005 %; sodium phosphate 20 ± 1 mM; DA7 DYNA_1b7 0.14 ± 0.05 mM

sample_conditions_1: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 308 K

sample_conditions_3: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 283 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HMQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D TOCSY-NHSQC	sample_1	isotropic	sample_conditions_2
3D CCH-TOCSY aliph	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_2
2D 1H-15N HMQC	sample_1	isotropic	sample_conditions_2
1D 1H	sample_1	isotropic	sample_conditions_3
2D 1H-15N HMQC	sample_1	isotropic	sample_conditions_3

Software:

NMRFAM-SPARKY v1.37 - peak picking, spectra visualization, and exporting bmrb file

NMRPipe vv10.9 - processing

TOPSPIN v4.0 - collection

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE III 600 MHz