BMRB Entry 17509

Name: NMR structure of the protein YP_557733.1 from Burkholderia xenovorans
Published: 2011-03-25

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PDB ID: 2la7
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17509
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of the protein YP_557733.1 from Burkholderia xenovorans

Deposition date:

2011-03-04

Original release date:

2011-03-25

Authors:

Jaudzems, Kristaps; Serrano, Pedro; Michael, Geralt; Reto, Horst; Wuthrich, Kurt

Citation:

Citation: Jaudzems, Kristaps; Serrano, Pedro; Michael, Geralt; Reto, Horst; Wuthrich, Kurt. "Null" To be Published ., .-..

Assembly members:

Assembly members:
YP_557733.1, polymer, 145 residues, 15414.306 Da.

Natural source:

Natural source: Common Name: Burkholderia xenovorans Taxonomy ID: 36873 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia xenovorans

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YP_557733.1: IPKHPDSEAVAPDPFNPAAT QLLDDTSWVLSAWKQADGTA RAVPSADQGAPITLTLSTST GQRHASGFSGCNRYMGSYAL KDGKLSFGTLGGTRMACMTP GGQIEGAYLNALTHIDRTGV QMRAPQQMQLVLDNGDTLTF DRSTR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	462
15N chemical shifts	159
1H chemical shifts	969

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	YP_557733.1	1

Entities:

Entity 1, YP_557733.1 145 residues - 15414.306 Da.

1

ILE

PRO

LYS

HIS

PRO

ASP

SER

GLU

ALA

VAL

2

ALA

PRO

ASP

PRO

PHE

ASN

PRO

ALA

THR

3

GLN

LEU

ASP

THR

SER

TRP

VAL

LEU

4

SER

ALA

TRP

LYS

GLN

ALA

ASP

GLY

THR

ALA

5

ARG

ALA

VAL

PRO

SER

ALA

ASP

GLN

GLY

ALA

6

PRO

ILE

THR

LEU

THR

LEU

SER

THR

SER

THR

7

GLY

GLN

ARG

HIS

ALA

SER

GLY

PHE

SER

GLY

8

CYS

ASN

ARG

TYR

MET

GLY

SER

TYR

ALA

LEU

9

LYS

ASP

GLY

LYS

LEU

SER

PHE

GLY

THR

LEU

10

GLY

THR

ARG

MET

ALA

CYS

MET

THR

PRO

11

GLY

GLN

ILE

GLU

GLY

ALA

TYR

LEU

ASN

12

ALA

LEU

THR

HIS

ILE

ASP

ARG

THR

GLY

VAL

13

GLN

MET

ARG

ALA

PRO

GLN

MET

GLN

LEU

14

VAL

LEU

ASP

ASN

GLY

ASP

THR

LEU

THR

PHE

15

ASP

ARG

SER

THR

ARG

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 1 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.225 M; pH: 6.0; 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 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
5D APSY-HACACONH	sample_1	isotropic	sample_conditions_1
4D APSY-HACANH	sample_1	isotropic	sample_conditions_1
5D APSY-CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

UNIO, Unio Herrmann Wuthrich - chemical shift assignment, processing, structure solution

TOPSPIN, Bruker Biospin - collection, data analysis, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2LA7
GB	ABE29681 EIF32471
REF	WP_007175698 WP_011487414