BMRB Entry 18654

Name: NMR Structures of Single-chain Insulin
Published: 2012-09-07

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PDB ID: 2lwz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18654
MolProbity Validation Chart

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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 Structures of Single-chain Insulin

Deposition date:

2012-08-09

Original release date:

2012-09-07

Authors:

Weiss, Michael; Yang, Yanwu

Citation:

Citation: Yang, Yanwu; Wan, Zhu-li; Hua, Qing-xin; Phillips, Nelson; Huang, Kun; Yeh, I-Ju; Liu, Yule; Hu, Shi-Quan; Hattier, Thomas; Whittaker, Jonathan; Weiss, Michael. "Dynamic repair of an amyloidogenic protein: insulin fibrillation is blocked by tethering a nascent alpha-helix" .

Assembly members:

Assembly members:
Single-chain Insulin, polymer, 57 residues, 6382.218 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Single-chain Insulin: FVNQHLCGSDLVEALYLVCG ERGFFYTDPTGGGPRRGIVE QCCHSICSLYQLENYCN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	191
15N chemical shifts	54
1H chemical shifts	368

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Single-chain Insulin	1

Entities:

Entity 1, Single-chain Insulin 57 residues - 6382.218 Da.

1

PHE

VAL

ASN

GLN

HIS

LEU

CYS

GLY

SER

ASP

2

LEU

VAL

GLU

ALA

LEU

TYR

LEU

VAL

CYS

GLY

3

GLU

ARG

GLY

PHE

TYR

THR

ASP

PRO

THR

4

GLY

PRO

ARG

GLY

ILE

VAL

GLU

5

GLN

CYS

HIS

SER

ILE

CYS

SER

LEU

TYR

6

GLN

LEU

GLU

ASN

TYR

CYS

ASN

Samples:

sample_1: Single Chain Insulin, [U-100% 13C; U-100% 15N], 0.9 mM; H2O 93%; H2O 7%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C 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 C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
4D Time-shared NOESY (4D-N15,C13-edited and 4D-C13,C13-edited NOESY)	sample_1	isotropic	sample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

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

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PIPP, Garrett - peak picking

xwinnmr, Bruker Biospin - collection

InsightII, Accelrys Software Inc. - data analysis

Molmol, Koradi, Billeter and Wuthrich - structure display

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 700 MHz