BMRB Entry 19027

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19027
MolProbity Validation Chart

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for rubredoxin type protein from Mycobacterium ulcerans
Deposition date:
2013-02-11
Original release date:
2013-03-12
Authors:
Barnwal, Ravi P; Varani, Gabriele
Citation:

Citation: Barnwal, Ravi P; Varani, Gabriele. "Backbone 1H, 13C, and 15N Chemical Shift Assignments for rubredoxin type protein from Mycobacterium ulcerans"  To be Published ., .-..

Assembly members:

Assembly members:
rubredoxin_type_protein, polymer, 56 residues, 6462.213 Da.

Natural source:

Natural source:   Common Name: High GC Gram+   Taxonomy ID: 1809   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium ulcerans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a-AVA

Entity Sequences (FASTA):

Entity Sequences (FASTA):
rubredoxin_type_protein: MTAYRCPVCDYTYDEGKGDP REGFPAGTRWDQIPDDWCCP DCSVREKVDFERMGGK

Data sets:
Data typeCount
13C chemical shifts206
15N chemical shifts51
1H chemical shifts286

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1rubredoxin_type_protein1

Entities:

Entity 1, rubredoxin_type_protein 56 residues - 6462.213 Da.

1   METTHRALATYRARGCYSPROVALCYSASP
2   TYRTHRTYRASPGLUGLYLYSGLYASPPRO
3   ARGGLUGLYPHEPROALAGLYTHRARGTRP
4   ASPGLNILEPROASPASPTRPCYSCYSPRO
5   ASPCYSSERVALARGGLULYSVALASPPHE
6   GLUARGMETGLYGLYLYS

Samples:

sample_1: rubredoxin type protein, [U-98% 15N], 1.2 mM; rubredoxin type protein, [U-95% 13C; U-95% 15N], 1.4 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TOPSPIN, Bruker Biospin - collection, processing

CcpNMR, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker AMX 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CDM75406
GB ABL04927 ACC39750 AGC61411 EPQ48959 EPQ70501
REF WP_011740542 WP_020788371

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks