BMRB Entry 17448

Name: Solution structure of the protein YP_546394.1, the first structural representative of the pfam family PF12112
Published: 2011-03-08

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PDB ID: 2l9d
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17448
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of the protein YP_546394.1, the first structural representative of the pfam family PF12112

Deposition date:

2011-02-08

Original release date:

2011-03-08

Authors:

MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WUTHRICH, KURT

Citation:

Citation: MOHANTY, BISWARANJAN; SERRANO, PEDRO; GERALT, MICHAEL; HORST, RETO; WUTHRICH, KURT. "Solution structure of the protein YP_546394.1, the first structural representative of the pfam family PF12112" .

Assembly members:

Assembly members:
YP_546394.1, polymer, 108 residues, 12034.806 Da.

Natural source:

Natural source: Common Name: b-proteobacteria Taxonomy ID: 405 Superkingdom: Bacteria Kingdom: not available Genus/species: Methylobacillus flagellatus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
YP_546394.1: GMGTTEKSGIKEIIIQGLTR AGKPFRPSDWVDRMCSTYAS FGADRKLRYSPYLKPRVIEG VRCLAVDLKLKDTNPEGFNQ LMHFATENQLNILDAEGNSI DAAQVTEI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	471
15N chemical shifts	117
1H chemical shifts	761

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	protein YP_546394.1	1

Entities:

Entity 1, protein YP_546394.1 108 residues - 12034.806 Da.

1

GLY

MET

GLY

THR

GLU

LYS

SER

GLY

ILE

2

LYS

GLU

ILE

GLN

GLY

LEU

THR

ARG

3

ALA

GLY

LYS

PRO

PHE

ARG

PRO

SER

ASP

TRP

4

VAL

ASP

ARG

MET

CYS

SER

THR

TYR

ALA

SER

5

PHE

GLY

ALA

ASP

ARG

LYS

LEU

ARG

TYR

SER

6

PRO

TYR

LEU

LYS

PRO

ARG

VAL

ILE

GLU

GLY

7

VAL

ARG

CYS

LEU

ALA

VAL

ASP

LEU

LYS

LEU

8

LYS

ASP

THR

ASN

PRO

GLU

GLY

PHE

ASN

GLN

9

LEU

MET

HIS

PHE

ALA

THR

GLU

ASN

GLN

LEU

10

ASN

ILE

LEU

ASP

ALA

GLU

GLY

ASN

SER

ILE

11

ASP

ALA

GLN

VAL

THR

GLU

ILE

Samples:

sample_1: YP_546394.1, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 4.5 mM; H20 95%; D20 5%

sample_conditions_1: ionic strength: 0.113 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
4D APSY - HACANH	sample_1	isotropic	sample_conditions_1
5D APSY - HACACONH	sample_1	isotropic	sample_conditions_1
5D APSY - CBCACONH	sample_1	isotropic	sample_conditions_1
15N resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
13Cali resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1
13Caro resolved [1H,1H]-NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.0, Guntert P. - structure calculation

UNIO v2.0.0, Herrmann and Wuthrich - chemical shift assignment, NOE assignment, peak picking, structure solution

CARA v1.5.3, Keller and Wuthrich - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - data collection, processing

OPALp v1.2, Koradi,Billeter and Guntert - energy refinement

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2L9D
GB	ABE50553
REF	WP_011480507