BMRB Entry 52756

Name: NMR chemical shifts of [15N,13C] DynorphinA (1-17) bound to DYNA_2b2 designed binding protein
Published: 2024-12-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52756

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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_2b2 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_3, polymer, 208 residues, 23748.7 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_3: MSGSDKFSITVDREELLKVI EENLERVEDEELKEKLQEVI DELKSTKELTESDLIKLIAK YNKVVAEEDGNEEAIKLYDK AIELAEKGTEEDLLIAVAYI NAANALLDGDEEEAEKLQKA AEELKENPTEENKLRLAALI NYVVAKREYEEGKGVTKEEV EALKKAYEKYKELSKEEVIK AINDLVDKHPGLEVIEKKQE GSHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	52
15N chemical shifts	20
1H chemical shifts	82

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 208 residues - 23748.7 Da.

1

MET

SER

GLY

SER

ASP

LYS

PHE

SER

ILE

THR

2

VAL

ASP

ARG

GLU

LEU

LYS

VAL

ILE

3

GLU

ASN

LEU

GLU

ARG

VAL

GLU

ASP

GLU

4

GLU

LEU

LYS

GLU

LYS

LEU

GLN

GLU

VAL

ILE

5

ASP

GLU

LEU

LYS

SER

THR

LYS

GLU

LEU

THR

6

GLU

SER

ASP

LEU

ILE

LYS

LEU

ILE

ALA

LYS

7

TYR

ASN

LYS

VAL

ALA

GLU

ASP

GLY

8

ASN

GLU

ALA

ILE

LYS

LEU

TYR

ASP

LYS

9

ALA

ILE

GLU

LEU

ALA

GLU

LYS

GLY

THR

GLU

10

GLU

ASP

LEU

ILE

ALA

VAL

ALA

TYR

ILE

11

ASN

ALA

ASN

ALA

LEU

ASP

GLY

ASP

12

GLU

ALA

GLU

LYS

LEU

GLN

LYS

ALA

13

ALA

GLU

LEU

LYS

GLU

ASN

PRO

THR

GLU

14

GLU

ASN

LYS

LEU

ARG

LEU

ALA

LEU

ILE

15

ASN

TYR

VAL

ALA

LYS

ARG

GLU

TYR

GLU

16

GLU

GLY

LYS

GLY

VAL

THR

LYS

GLU

VAL

17

GLU

ALA

LEU

LYS

ALA

TYR

GLU

LYS

TYR

18

LYS

GLU

LEU

SER

LYS

GLU

VAL

ILE

LYS

19

ALA

ILE

ASN

ASP

LEU

VAL

ASP

LYS

HIS

PRO

20

GLY

LEU

GLU

VAL

ILE

GLU

LYS

GLN

GLU

21

GLY

SER

HIS

Samples:

sample_1: peptide, [U-13C; U-15N], 0.2 ± 0.05 mM; sodium chloride 150 ± 5 mM; sodium azide 0.02 ± .005 %; sodium phosphate 20 ± 1 mM; 1C10 DYNA_2b2 0.2 ± 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: 283 K

sample_conditions_3: ionic strength: 150 mM; pH: 6.0; pressure: 1 atm; temperature: 308 K

Experiments:

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

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