BMRB Entry 18887

Name: Solution structure of hypothetical protein lmo0427
Published: 2012-12-21

Click here to enlarge.

PDB ID: 2m1z
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18887
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:

Solution structure of hypothetical protein lmo0427

Deposition date:

2012-12-10

Original release date:

2012-12-21

Authors:

Zhang, Yongbo; Winsor, James; Radhakrishnan, Ishwar; Anderson, Wayne

Citation:

Citation: Zhang, Yongbo; Winsor, James; Radhakrishnan, Ishwar; Anderson, Wayne. "Solution structure of hypothetical protein lmo0427" .

Assembly members:

Assembly members:
entity, polymer, 106 residues, 11395.479 Da.

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pBR322

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MKRKIIAVTACATGVAHTYM AAQALKKGAKKMGNLIKVET QGATGIENELTEKDVNIGEV VIFAVDTKVRNKERFDGKVV LEVPVSAPIKDAEKVINAAL ALIDEK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	462
15N chemical shifts	112
1H chemical shifts	766

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hypothetical protein lmo0427	1

Entities:

Entity 1, hypothetical protein lmo0427 106 residues - 11395.479 Da.

1

MET

LYS

ARG

LYS

ILE

ALA

VAL

THR

ALA

2

CYS

ALA

THR

GLY

VAL

ALA

HIS

THR

TYR

MET

3

ALA

GLN

ALA

LEU

LYS

GLY

ALA

LYS

4

LYS

MET

GLY

ASN

LEU

ILE

LYS

VAL

GLU

THR

5

GLN

GLY

ALA

THR

GLY

ILE

GLU

ASN

GLU

LEU

6

THR

GLU

LYS

ASP

VAL

ASN

ILE

GLY

GLU

VAL

7

VAL

ILE

PHE

ALA

VAL

ASP

THR

LYS

VAL

ARG

8

ASN

LYS

GLU

ARG

PHE

ASP

GLY

LYS

VAL

9

LEU

GLU

VAL

PRO

VAL

SER

ALA

PRO

ILE

LYS

10

ASP

ALA

GLU

LYS

VAL

ILE

ASN

ALA

LEU

11

ALA

LEU

ILE

ASP

GLU

LYS

Samples:

sample_1: Listeria monocytogenes EGD-e, [U-95% 13C; U-95% 15N], 1.2 mM; potassium phosphate 20 mM; sodium chloride 100 mM

sample_2: Listeria monocytogenes EGD-e, [U-95% 13C; U-95% 15N], 1.2 mM; potassium phosphate 20 mM; sodium chloride 100 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.7; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

ARIA v1.2, Linge, O'Donoghue and Nilges - refinement, structure solution

NMRPipe, Delaglio, Zhengrong and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Varian INOVA 600 MHz

PDB	2M1Z
EMBL	CAC98506 CAK19805 CAR83139 CAS04216 CBY02952
GB	AAT03227 ACK40550 ADB67216 ADB70305 AEH91456
REF	NP_463956 WP_003722977 WP_003760426 WP_036088242 WP_047584151