BMRB Entry 17403

Name: 1H, 15N and 13C resonance assignment of the N-terminal C39-peptidase like domain of the ABC transporter Haemolysin B (HlyB)
Published: 2011-03-07

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PDB ID: 3zua
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17403
MolProbity Validation Chart

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 15N and 13C resonance assignment of the N-terminal C39-peptidase like domain of the ABC transporter Haemolysin B (HlyB)

Deposition date:

2011-01-10

Original release date:

2011-03-07

Authors:

Lecher, Justin; Willbold, Dieter; Stoldt, Matthias; Schmitt, Lutz; Smits, Sander; Schwarz, Christian

Citation:

Citation: Lecher, Justin; Stoldt, Matthias; Schwarz, Christian; Smits, Sander; Schmitt, Lutz; Willbold, Dieter. "1H, 15N and 13C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB)." Biomol. NMR Assignments 5, 199-201 (2011).
PubMed: 21347827

Assembly members:

Assembly members:
HlyB_C39_domain, polymer, 142 residues, 16089.4973 Da.

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HlyB_C39_domain: GAMANSDSCHKIDYGLYALE ILAQYHNVSVNPEEIKHRFD TDGTGLGLTSWLLAAKSLEL KVKQVKKTIDRLNFISLPAL VWREDGRHFILTKVSKEANR YLIFDLEQRNPRVLEQSEFE ALYQGHIILIASRSSVAGKL AK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	657
15N chemical shifts	169
1H chemical shifts	1069

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	C39-137	1

Entities:

Entity 1, C39-137 142 residues - 16089.4973 Da.

1

GLY

ALA

MET

ALA

ASN

SER

ASP

SER

CYS

HIS

2

LYS

ILE

ASP

TYR

GLY

LEU

TYR

ALA

LEU

GLU

3

ILE

LEU

ALA

GLN

TYR

HIS

ASN

VAL

SER

VAL

4

ASN

PRO

GLU

ILE

LYS

HIS

ARG

PHE

ASP

5

THR

ASP

GLY

THR

GLY

LEU

GLY

LEU

THR

SER

6

TRP

LEU

ALA

LYS

SER

LEU

GLU

LEU

7

LYS

VAL

LYS

GLN

VAL

LYS

THR

ILE

ASP

8

ARG

LEU

ASN

PHE

ILE

SER

LEU

PRO

ALA

LEU

9

VAL

TRP

ARG

GLU

ASP

GLY

ARG

HIS

PHE

ILE

10

LEU

THR

LYS

VAL

SER

LYS

GLU

ALA

ASN

ARG

11

TYR

LEU

ILE

PHE

ASP

LEU

GLU

GLN

ARG

ASN

12

PRO

ARG

VAL

LEU

GLU

GLN

SER

GLU

PHE

GLU

13

ALA

LEU

TYR

GLN

GLY

HIS

ILE

LEU

ILE

14

ALA

SER

ARG

SER

VAL

ALA

GLY

LYS

LEU

15

ALA

LYS

Samples:

Uniform_15N13C: C39-137, [U-13C; U-15N], 2.0 mM; H2O, [U-13C; U-15N], 93%; D2O, [U-13C; U-15N], 7%

Uniform_15N: C39-137, [U-15N], 2.5 mM; H2O, [U-15N], 93%; D2O, [U-15N], 7%

Uniform_15N13C_deuterated_buffer: C39-137, [U-13C; U-15N], 2.5 mM; H2O, [U-13C; U-15N], 93%; D2O, [U-13C; U-15N], 7%

Uniform_15N13C_deuterated_buffer-D2O: C39-137, [U-13C; U-15N], 2.5 mM; D2O, [U-13C; U-15N], 100%

standard: ionic strength: 0.200 M; pH: 6.000; pressure: 1.000 atm; temperature: 303.000 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	Uniform_15N	isotropic	standard
3D CBCA(CO)NH	Uniform_15N13C	isotropic	standard
3D HBHA(CO)NH	Uniform_15N13C	isotropic	standard
3D HNHA	Uniform_15N	isotropic	standard
3D HNCO	Uniform_15N13C	isotropic	standard
3D HNCACB	Uniform_15N13C	isotropic	standard
3D H(CCO)NH	Uniform_15N13C	isotropic	standard
3D C(CO)NH	Uniform_15N13C	isotropic	standard
3D HCCH-COSY	Uniform_15N13C_deuterated_buffer	isotropic	standard
2D 1H-15N HMQC	Uniform_15N	isotropic	standard
2D 1H-13C HSQC aromatic	Uniform_15N13C_deuterated_buffer	isotropic	standard
2D 1H-13C HSQC aliphatic	Uniform_15N13C_deuterated_buffer-D2O	isotropic	standard
3D 1H-15N NOESY	Uniform_15N	isotropic	standard
3D 1H-13C NOESY aliphatic	Uniform_15N13C_deuterated_buffer	isotropic	standard
3D 1H-13C NOESY aromatic	Uniform_15N13C_deuterated_buffer	isotropic	standard

Software:

AZARA v2.8, Wayne Boucher - processing

ANALYSIS v2.1, CCPN - assignment, data evaluation

NMRPipe v5.4.2010.250.17.50, NIH - conversion, processing

VnmrJ v2.3A, Agilent Technologies (formerly Varian) - data recording, spectrometer operation

NMR spectrometers:

Varian VNMRS 900 MHz
Varian VNMRS 800 MHz

UNP	Q47258
PDB	3ZUA
EMBL	CAD33760 CAD42038 CAK02716 CAM84370 CAM84374
GB	AAA23976 AAA23978 AAN82021 ABE10328 ABG71799
REF	WP_000376537 WP_000376540 WP_000376541 WP_000376543 WP_000376544
SP	P10089 Q47258 Q8FDZ8
AlphaFold	Q47258 P10089 Q47258 Q8FDZ8