BMRB Entry 26607

Name: Neisseria meningititis Fic
Published: 2016-01-06

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26607

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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:

Neisseria meningititis Fic

Deposition date:

2015-07-13

Original release date:

2016-01-06

Authors:

Burmann, Bjoern; Hiller, Sebastian

Citation:

Citation: Stanger, Frederic; Burmann, Bjoern; Harms, Alexander; Correia, Hugo; Mazur, Adam; Sharpe, Timothy; Dehio, Christoph; Hiller, Sebastian; Schirmer, Tilman. "Intrinsic regulation of FIC-domain AMP-transferases by oligomerization and automodification" Proc. Natl. Acad. Sci. U. S. A. ., .-..

Assembly members:

Assembly members:
NmFic, polymer, 188 residues, Formula weight is not available

Natural source:

Natural source: Common Name: b-proteobacteria Taxonomy ID: 487 Superkingdom: Bacteria Kingdom: not available Genus/species: Neisseria meningitidis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pRSF-DUET1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NmFic: MHHHHHHMKSIDEQSLHNAR RLFESGDIDRIEVGTTAGLQ QIHRYLFGGLYDFAGQIRED NISKGGFRFANAMYLKEALV KIEQMPERTFEEIIAKYVRM NIAAPFLEGNGRSTRIWLDL VLKKNLKKVVNWQNVSKTLY LQAMERSPVNDLRLRFLLKD NLTDDVDNREIIFKGIEQSY YYEGYEKG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	524
15N chemical shifts	172
1H chemical shifts	172

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NmFic	1

Entities:

Entity 1, NmFic 188 residues - Formula weight is not available

1

MET

HIS

MET

LYS

SER

2

ILE

ASP

GLU

GLN

SER

LEU

HIS

ASN

ALA

ARG

3

ARG

LEU

PHE

GLU

SER

GLY

ASP

ILE

ASP

ARG

4

ILE

GLU

VAL

GLY

THR

ALA

GLY

LEU

GLN

5

GLN

ILE

HIS

ARG

TYR

LEU

PHE

GLY

LEU

6

TYR

ASP

PHE

ALA

GLY

GLN

ILE

ARG

GLU

ASP

7

ASN

ILE

SER

LYS

GLY

PHE

ARG

PHE

ALA

8

ASN

ALA

MET

TYR

LEU

LYS

GLU

ALA

LEU

VAL

9

LYS

ILE

GLU

GLN

MET

PRO

GLU

ARG

THR

PHE

10

GLU

ILE

ALA

LYS

TYR

VAL

ARG

MET

11

ASN

ILE

ALA

PRO

PHE

LEU

GLU

GLY

ASN

12

GLY

ARG

SER

THR

ARG

ILE

TRP

LEU

ASP

LEU

13

VAL

LEU

LYS

ASN

LEU

LYS

VAL

14

ASN

TRP

GLN

ASN

VAL

SER

LYS

THR

LEU

TYR

15

LEU

GLN

ALA

MET

GLU

ARG

SER

PRO

VAL

ASN

16

ASP

LEU

ARG

LEU

ARG

PHE

LEU

LYS

ASP

17

ASN

LEU

THR

ASP

VAL

ASP

ASN

ARG

GLU

18

ILE

PHE

LYS

GLY

ILE

GLU

GLN

SER

TYR

19

TYR

GLU

GLY

TYR

GLU

LYS

GLY

Samples:

sample_1: NmFic, [U-100% 13C; U-100% 15N], 500 uM; D2O 10%; MES 25 mM; sodium chloride 150 mM; H2O 90%

sample_conditions_1: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

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

Software:

TOPSPIN v3.0, Bruker Biospin, Guntert, Keller and Wuthrich - chemical shift assignment, collection, processing

NMR spectrometers:

Bruker Avance 700 MHz

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