BMRB Entry 50007

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for proIAPP in DPC Micelles
Published: 2020-02-21

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PDB ID: 6ucj
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50007
MolProbity Validation Chart

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for proIAPP in DPC Micelles PubMed: 32077246

Deposition date: 2019-08-31 Original release date: 2020-02-21

Authors: DeLisle, Charles; Malooley, Alexander; Banerjee, Indrani; Lorieau, Justin

Citation: DeLisle, Charles; Malooley, Alexander; Banerjee, Indrani; Lorieau, Justin. "Pro-Islet Amyloid Polypeptide in Micelles Contains a Helical Prohormone Segment" FEBS J. 287, 4440-4457 (2020).

Assembly members:
entity_1, polymer, 72 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET15b

Entity Sequences (FASTA):
entity_1: TPIESHQVEKRKCNTATCAT QRLANFLVHSSNNFGAILSS TNVGSNTYGKRNAVEVLKRE PLNYLPLKKKKD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	459
15N chemical shifts	123
1H chemical shifts	550

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	proIAPP-K4D	1

Entities:

Entity 1, proIAPP-K4D 72 residues - Formula weight is not available

1

THR

PRO

ILE

GLU

SER

HIS

GLN

VAL

GLU

LYS

2

ARG

LYS

CYS

ASN

THR

ALA

THR

CYS

ALA

THR

3

GLN

ARG

LEU

ALA

ASN

PHE

LEU

VAL

HIS

SER

4

SER

ASN

PHE

GLY

ALA

ILE

LEU

SER

5

THR

ASN

VAL

GLY

SER

ASN

THR

TYR

GLY

LYS

6

ARG

ASN

ALA

VAL

GLU

VAL

LEU

LYS

ARG

GLU

7

PRO

LEU

ASN

TYR

LEU

PRO

LEU

LYS

8

LYS

ASP

Samples:

sample_1: DPC 200 mM; TRIS 30 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 10 v/v; sodium azide 0.03%; proIAPP-K4D, [U-100% 13C; U-100% 15N], 1.0 ± 0.2 mM

sample_2: DPC 200 mM; sodium acetate 30 mM; sodium chloride 50 mM; D2O, [U-100% 2H], 10 v/v; sodium azide 0.03%; proIAPP-K4D, [U-100% 13C; U-100% 15N], 1.0 ± 0.2 mM

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 305 K

sample_conditions_2: pH: 4.5; pressure: 1 atm; temperature: 305 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCA	sample_2	isotropic	sample_conditions_2
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_2
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2

Software:

software_1, Keller and Wuthrich - chemical shift assignment, peak picking

software_2, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

software_3, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 500 MHz

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