BMRB Entry 18836

Name: Backbone assignments of 8M urea denatured S-YibK-C variant from Haemophilus influenzae (HI0766)
Published: 2019-08-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18836

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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 assignments of 8M urea denatured S-YibK-C variant from Haemophilus influenzae (HI0766)

Deposition date:

2012-11-12

Original release date:

2019-08-30

Authors:

Hsieh, Shu-Ju Micky; Chien, Chih-Ta Henry; Hsu, Shang-Te Danny

Citation:

Citation: Hsieh, Shu-Ju Micky; Mallam, Anna; Jackson, Sophie; Hsu, Shang-Te Danny. "Backbone 1H, 13C and 15N assignments of YibK and avariant containing a unique cysteine residue at C-terminus in 8 M urea-denatured states" Biomol. NMR Assignments 8, 439-442 (2014).
PubMed: 23853076

Assembly members:

Assembly members:
S-YibK-C, polymer, 167 residues, Formula weight is not available

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 727 Superkingdom: Bacteria Kingdom: not available Genus/species: Haemophilus influenzae

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: Pet 17b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
S-YibK-C: MSGSMLDIVLYEPEIPQNTG NIIRLAANTGFRLHLIEPLG FTWDDKRLRRSGLDYHEFAE IKRHKTFEAFLESEKPKRLF ALTTKGAPAHSQVKFKLGDY LMFGPETRGIPMSILNEMPM EQKIRIPMTANSRSMNLSNS VAVTVYEAWRQLGYKGAVNL PEVKGSC

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	387
15N chemical shifts	145
1H chemical shifts	283

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	S-YibK-C	1

Entities:

Entity 1, S-YibK-C 167 residues - Formula weight is not available

1

MET

SER

GLY

SER

MET

LEU

ASP

ILE

VAL

LEU

2

TYR

GLU

PRO

GLU

ILE

PRO

GLN

ASN

THR

GLY

3

ASN

ILE

ARG

LEU

ALA

ASN

THR

GLY

4

PHE

ARG

LEU

HIS

LEU

ILE

GLU

PRO

LEU

GLY

5

PHE

THR

TRP

ASP

LYS

ARG

LEU

ARG

6

SER

GLY

LEU

ASP

TYR

HIS

GLU

PHE

ALA

GLU

7

ILE

LYS

ARG

HIS

LYS

THR

PHE

GLU

ALA

PHE

8

LEU

GLU

SER

GLU

LYS

PRO

LYS

ARG

LEU

PHE

9

ALA

LEU

THR

LYS

GLY

ALA

PRO

ALA

HIS

10

SER

GLN

VAL

LYS

PHE

LYS

LEU

GLY

ASP

TYR

11

LEU

MET

PHE

GLY

PRO

GLU

THR

ARG

GLY

ILE

12

PRO

MET

SER

ILE

LEU

ASN

GLU

MET

PRO

MET

13

GLU

GLN

LYS

ILE

ARG

ILE

PRO

MET

THR

ALA

14

ASN

SER

ARG

SER

MET

ASN

LEU

SER

ASN

SER

15

VAL

ALA

VAL

THR

VAL

TYR

GLU

ALA

TRP

ARG

16

GLN

LEU

GLY

TYR

LYS

GLY

ALA

VAL

ASN

LEU

17

PRO

GLU

VAL

LYS

GLY

SER

CYS

Samples:

sample_1: S-YibK-C, [U-13C; U-15N], 350 uM; D2O 10%; TRIS 50 mM; potassium chloride 200 mM; glycerol 10%; urea 8 M; H2O 90%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection, data analysis

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

NMR spectrometers:

Bruker Avance 800 MHz

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