BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 25098

Title: NMR solution structure of copper binding protein in the apo form

Deposition date: 2014-07-17 Original release date: 2015-07-27

Authors: Fu, Yue; Wu, Hongwei; Bruce, Kevin; Giedroc, David

Citation: Fu, Yue; Wu, Hongwei; Bruce, Kevin; Giedroc, David. "Characterization of the structure and dynamics of the copper chaperone CupA"  Not known ., .-..

Assembly members:
entity, polymer, 98 residues, 10887.662 Da.

Natural source:   Common Name: firmicutes   Taxonomy ID: 1313   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptococcus pneumoniae

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

Entity Sequences (FASTA):
entity: GAMGQKAQQKNGYQEIRVEV MGGYTPELIVLKKSVPARIV FDRKDPSPCLDQIVFPDFGV HANLPMGEEYVVEITPEQAG EFSFACGMNMMHGKMIVE

Data sets:
Data typeCount
13C chemical shifts269
15N chemical shifts84
1H chemical shifts599

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 98 residues - 10887.662 Da.

1   GLYALAMETGLYGLNLYSALAGLNGLNLYS
2   ASNGLYTYRGLNGLUILEARGVALGLUVAL
3   METGLYGLYTYRTHRPROGLULEUILEVAL
4   LEULYSLYSSERVALPROALAARGILEVAL
5   PHEASPARGLYSASPPROSERPROCYSLEU
6   ASPGLNILEVALPHEPROASPPHEGLYVAL
7   HISALAASNLEUPROMETGLYGLUGLUTYR
8   VALVALGLUILETHRPROGLUGLNALAGLY
9   GLUPHESERPHEALACYSGLYMETASNMET
10   METHISGLYLYSMETILEVALGLU

Samples:

sample_1: entity, [U-98% 13C; U-98% 15N], 0.4 – 0.6 mM; sodium phosphate 50 mM; sodium chloride 50 mM; EDTA 5 mM; TCEP 5 mM; DSS 10 uM; sodium azide 0.02%; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 300 mM; pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CcpNmr_Analysis v2.3.0, CCPN - data analysis, peak picking

SPARKY v2.6, Goddard - chemical shift assignment, peak picking

NMRPipe v8.1, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

PSVS v1.5, Bhattacharya and Montelione - structure validation

PINE v2.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

X-PLOR_NIH v2.36, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Agilent VNMRS 800 MHz
  • Agilent VNMRS 600 MHz

Related Database Links:

PDB
EMBL CAR68500 CBW32317 CBW34276 CBW36290 CCM08344
GB AAK74869 AAK99444 ABJ54623 ACA36045 ACB89929
REF NP_358234 WP_000935053 WP_000935062 WP_000935063 WP_000935064

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