BMRB Entry 15034

Name: 1H,13C and 15N NMR Assignments of the Yellow Fever Envelope Protein Domain III
Published: 2007-06-27

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15034

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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:

1H,13C and 15N NMR Assignments of the Yellow Fever Envelope Protein Domain III

Deposition date:

2006-11-16

Original release date:

2007-06-27

Authors:

Volk, David; Gandham, Sai; May, Fiona; Barrett, Alan; Gorenstein, David

Citation:

Citation: Volk, David; Gandham, Sai; May, Fiona; Anderson, Anjenique; Barrett, Alan; Gorenstein, David. "NMR assignments of the yellow fever virus envelope protein domain III" Biomol. NMR Assignments 1, 49-50 (2007).
PubMed: 19636823

Assembly members:

Assembly members:
YFED3, polymer, 112 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Yellow fever virus Taxonomy ID: 11089 Superkingdom: Viruses Kingdom: not available Genus/species: Flavivirus Yellow fever virus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YFED3: MSALTLKGTSYKMCTDKMSF VKNPTDTGHGTVVMQVKVPK GAPCKIPVIVADDLTAAINK GILVTVNPIASTNDDEVLIE VNPPFGDSYIIVGTGDSRLT YQWHKEGSSIGK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	462
15N chemical shifts	111
1H chemical shifts	768

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	YFED3 monomer	1

Entities:

Entity 1, YFED3 monomer 112 residues - Formula weight is not available

All residues (1-112) represent natural amino acids in the YF-ED3

1

MET

SER

ALA

LEU

THR

LEU

LYS

GLY

THR

SER

2

TYR

LYS

MET

CYS

THR

ASP

LYS

MET

SER

PHE

3

VAL

LYS

ASN

PRO

THR

ASP

THR

GLY

HIS

GLY

4

THR

VAL

MET

GLN

VAL

LYS

VAL

PRO

LYS

5

GLY

ALA

PRO

CYS

LYS

ILE

PRO

VAL

ILE

VAL

6

ALA

ASP

LEU

THR

ALA

ILE

ASN

LYS

7

GLY

ILE

LEU

VAL

THR

VAL

ASN

PRO

ILE

ALA

8

SER

THR

ASN

ASP

GLU

VAL

LEU

ILE

GLU

9

VAL

ASN

PRO

PHE

GLY

ASP

SER

TYR

ILE

10

ILE

VAL

GLY

THR

GLY

ASP

SER

ARG

LEU

THR

11

TYR

GLN

TRP

HIS

LYS

GLU

GLY

SER

ILE

12

GLY

LYS

Samples:

sample_1: YFED3, [U-98% 13C; U-98% 15N], 0.1 – 0.3 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 5.8; pressure: 1 atm; temperature: 298 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 HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)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
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ, Varian - collection, data analysis

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 750 MHz

PDB	2JQM 2JV6
GB	AAA92693 AAA92694 AAA92695 AAA92698 AAA92699
SP	Q074N0 Q1X880 Q1X881 Q6DV88 Q6J3P1
AlphaFold	Q074N0 Q1X880 Q1X881 Q6DV88 Q6J3P1