BMRB Entry 17320

Name: NMR structure of the protein YP_926445.1 from Shewanella Amazonensis
Published: 2012-07-25

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PDB ID: 2l6o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17320
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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_926445.1 from Shewanella Amazonensis

Deposition date:

2010-11-23

Original release date:

2012-07-25

Authors:

Serrano, Pedro; Geralt, Michael; Mohanty, Biswaranjan; Horst, Reto; Wuthrich, Kurt

Citation:

Citation: Serrano, Pedro; Geralt, Michael; Mohanty, Biswaranjan; Horst, Reto; Wuthrich, Kurt. "NMR structure of the protein YP_926445.1 from Shewanella Amazonensis" .

Assembly members:

Assembly members:
YP_926445.1, polymer, 114 residues, 12793.651 Da.

Natural source:

Natural source: Common Name: Shewanella amazonensis Taxonomy ID: 60478 Superkingdom: Bacteria Kingdom: not available Genus/species: Shewanella amazonensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YP_926445.1: MGAGQTPHPQLIWPALLKQQ GCNELLPLRTNDDWQRFCAD SKHLLQYGDKLVDSNFHCFV LEEDAHWHPAAPLPPEGLND LIRAHCATLGHCCTSKMHLH SVMDAIDFLNALEG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	385
15N chemical shifts	119
1H chemical shifts	785

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	YP_926445.1	1

Entities:

Entity 1, YP_926445.1 114 residues - 12793.651 Da.

1

MET

GLY

ALA

GLY

GLN

THR

PRO

HIS

PRO

GLN

2

LEU

ILE

TRP

PRO

ALA

LEU

LYS

GLN

3

GLY

CYS

ASN

GLU

LEU

PRO

LEU

ARG

THR

4

ASN

ASP

TRP

GLN

ARG

PHE

CYS

ALA

ASP

5

SER

LYS

HIS

LEU

GLN

TYR

GLY

ASP

LYS

6

LEU

VAL

ASP

SER

ASN

PHE

HIS

CYS

PHE

VAL

7

LEU

GLU

ASP

ALA

HIS

TRP

HIS

PRO

ALA

8

ALA

PRO

LEU

PRO

GLU

GLY

LEU

ASN

ASP

9

LEU

ILE

ARG

ALA

HIS

CYS

ALA

THR

LEU

GLY

10

HIS

CYS

THR

SER

LYS

MET

HIS

LEU

HIS

11

SER

VAL

MET

ASP

ALA

ILE

ASP

PHE

LEU

ASN

12

ALA

LEU

GLU

GLY

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 50 mM; DTT 8 mM; sodium azide 4.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.113 M; pH: 6.5; 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 (ali)	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY (Aro)	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, Guntert, Mumenthaler and Wuthrich - structure solution

OPALp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

TOPSPIN v2.1, Bruker Biospin - collection, processing

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

UNIO, Herrmann and Wuthrich - chemical shift assignment, peak picking, structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2L6O
GB	ABL98775
REF	WP_011758685