BMRB Entry 52447

Name: Backbone [1H, 13C, 15N] Chemical Shift Assignment for LpAFP
Published: 2024-06-25

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52447

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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:

Backbone [1H, 13C, 15N] Chemical Shift Assignment for LpAFP

Deposition date:

2024-05-08

Original release date:

2024-06-25

Authors:

Bruss, Elias; Kumeta, Hiroyuki; Arai, Tatsuya; Tsuda, Sakae; Kondo, Hidemasa

Citation:

Citation: Bruss, Elias; Kumeta, Hiroyuki; Arai, Tatsuya; Tsuda, Sakae; Kondo, Hidemasa. "Nanodisc titration reveals temperature-dependent membrane affinity of fish type II AFP ice binding site" Sci. Rep. ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 127 residues, Formula weight is not available

Natural source:

Natural source: Common Name: budding yeasts Taxonomy ID: 4922 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Pichia pastoris

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Pichia pastoris Vector: pICZa

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ALVCPAGWTLHGQRCFYSEA TAMTWDLAEANCVNKGGHLA SIHSLEEQLYIKDIVAGIVW IGGSACKVAGAWSWTDGTPV DYRTWCPTKPNDILSDCCMQ MTAAVDKCWDDLPCPASHAS ICAKAAI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	444
15N chemical shifts	114
1H chemical shifts	245

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LpAFP	1

Entities:

Entity 1, LpAFP 127 residues - Formula weight is not available

1

ALA

LEU

VAL

CYS

PRO

ALA

GLY

TRP

THR

LEU

2

HIS

GLY

GLN

ARG

CYS

PHE

TYR

SER

GLU

ALA

3

THR

ALA

MET

THR

TRP

ASP

LEU

ALA

GLU

ALA

4

ASN

CYS

VAL

ASN

LYS

GLY

HIS

LEU

ALA

5

SER

ILE

HIS

SER

LEU

GLU

GLN

LEU

TYR

6

ILE

LYS

ASP

ILE

VAL

ALA

GLY

ILE

VAL

TRP

7

ILE

GLY

SER

ALA

CYS

LYS

VAL

ALA

GLY

8

ALA

TRP

SER

TRP

THR

ASP

GLY

THR

PRO

VAL

9

ASP

TYR

ARG

THR

TRP

CYS

PRO

THR

LYS

PRO

10

ASN

ASP

ILE

LEU

SER

ASP

CYS

MET

GLN

11

MET

THR

ALA

VAL

ASP

LYS

CYS

TRP

ASP

12

ASP

LEU

PRO

CYS

PRO

ALA

SER

HIS

ALA

SER

13

ILE

CYS

ALA

LYS

ALA

ILE

Samples:

sample_1: LpAFP, [U-99% 13C; U-99% 15N], 0.6 mM; D2O 10%; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 61.225 M; pH: 6.0; pressure: 1 atm; temperature: 25 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
HN(CA)HA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment, data analysis

NMR spectrometers:

Agilent Unity INOVA 600AA 600 MHz

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