BMRB Entry 18733

Name: NMR structure of the protein NB7890A from Shewanella sp
Published: 2012-10-22

Click here to enlarge.

PDB ID: 2lyy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18733
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

NMR structure of the protein NB7890A from Shewanella sp

Deposition date:

2012-09-21

Original release date:

2012-10-22

Authors:

Serrano, Pedro; Geralt, Michael; Pedrini, Bill; Wuthrich, Kurt; Horst, Reto; Augustyniak, Wojtek

Citation:

Citation: Serrano, Pedro; Wuthrich, Kurt. "NMR structure of the protein NB7890A from Shewanella sp" .

Assembly members:

Assembly members:
NB7890A, polymer, 208 residues, 22935.424 Da.

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 50422 Superkingdom: Bacteria Kingdom: not available Genus/species: Shewanella sp

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NB7890A: SNNENAFYARATELIKLANQ QNQNTEIQTGEVSASFMWAL ARYNAWFGSTSFETKEQMQA KKQEMMDYYMDRYKEMLDAN MEDYIENFDHYRATQKMEDY IENFDHYRATQKSNNENAFY ARATELIKLANQQNQNTEIQ TGEVSASFMWALARYNAWFG STSFETKEQMQAKKQEMMDY YMDRYKEMLDANMEDYIENF DHYRATQK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	336
15N chemical shifts	115
1H chemical shifts	673

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NB7890A	1

Entities:

Entity 1, NB7890A 208 residues - 22935.424 Da.

1

SER

ASN

GLU

ASN

ALA

PHE

TYR

ALA

ARG

2

ALA

THR

GLU

LEU

ILE

LYS

LEU

ALA

ASN

GLN

3

GLN

ASN

GLN

ASN

THR

GLU

ILE

GLN

THR

GLY

4

GLU

VAL

SER

ALA

SER

PHE

MET

TRP

ALA

LEU

5

ALA

ARG

TYR

ASN

ALA

TRP

PHE

GLY

SER

THR

6

SER

PHE

GLU

THR

LYS

GLU

GLN

MET

GLN

ALA

7

LYS

GLN

GLU

MET

ASP

TYR

MET

8

ASP

ARG

TYR

LYS

GLU

MET

LEU

ASP

ALA

ASN

9

MET

GLU

ASP

TYR

ILE

GLU

ASN

PHE

ASP

HIS

10

TYR

ARG

ALA

THR

GLN

LYS

MET

GLU

ASP

TYR

11

ILE

GLU

ASN

PHE

ASP

HIS

TYR

ARG

ALA

THR

12

GLN

LYS

SER

ASN

GLU

ASN

ALA

PHE

TYR

13

ALA

ARG

ALA

THR

GLU

LEU

ILE

LYS

LEU

ALA

14

ASN

GLN

ASN

GLN

ASN

THR

GLU

ILE

GLN

15

THR

GLY

GLU

VAL

SER

ALA

SER

PHE

MET

TRP

16

ALA

LEU

ALA

ARG

TYR

ASN

ALA

TRP

PHE

GLY

17

SER

THR

SER

PHE

GLU

THR

LYS

GLU

GLN

MET

18

GLN

ALA

LYS

GLN

GLU

MET

ASP

TYR

19

TYR

MET

ASP

ARG

TYR

LYS

GLU

MET

LEU

ASP

20

ALA

ASN

MET

GLU

ASP

TYR

ILE

GLU

ASN

PHE

21

ASP

HIS

TYR

ARG

ALA

THR

GLN

LYS

Samples:

sample_1: NB7890A, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.220 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
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

NMR spectrometers:

Bruker Avance 600 MHz
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