BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 17448

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: 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"  Not known ., .-..

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

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

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

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

Data sets:
Data typeCount
13C chemical shifts471
15N chemical shifts117
1H chemical shifts761

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1protein YP_546394.11

Entities:

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

1   GLYMETGLYTHRTHRGLULYSSERGLYILE
2   LYSGLUILEILEILEGLNGLYLEUTHRARG
3   ALAGLYLYSPROPHEARGPROSERASPTRP
4   VALASPARGMETCYSSERTHRTYRALASER
5   PHEGLYALAASPARGLYSLEUARGTYRSER
6   PROTYRLEULYSPROARGVALILEGLUGLY
7   VALARGCYSLEUALAVALASPLEULYSLEU
8   LYSASPTHRASNPROGLUGLYPHEASNGLN
9   LEUMETHISPHEALATHRGLUASNGLNLEU
10   ASNILELEUASPALAGLUGLYASNSERILE
11   ASPALAALAGLNVALTHRGLUILE

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
4D APSY - HACANHsample_1isotropicsample_conditions_1
5D APSY - HACACONHsample_1isotropicsample_conditions_1
5D APSY - CBCACONHsample_1isotropicsample_conditions_1
15N resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Cali resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Caro resolved [1H,1H]-NOESYsample_1isotropicsample_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

Related Database Links:

PDB
GB ABE50553
REF WP_011480507

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts