BMRB Entry 25259

Title:
NMR structure of hypothetical protein NP_344732.1 from Streptococcus pneumoniae TIGR4
Deposition date:
2014-10-01
Original release date:
2014-11-03
Authors:
Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of hypothetical protein NP_344732.1 from Streptococcus pneumoniae TIGR4"  .

Assembly members:

Assembly members:
entity, polymer, 165 residues, 18399.924 Da.

Natural source:

Natural source:   Common Name: firmicutes   Taxonomy ID: 170187   Superkingdom: not available   Kingdom: Streptococcus   Genus/species: pneumoniae TIGR4

Experimental source:

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

Data sets:
Data typeCount
1H chemical shifts1158
13C chemical shifts565
15N chemical shifts175

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 165 residues - 18399.924 Da.

1   GLYPROALATHRLYSTHRGLULYSASPTHR
2   LEUGLNSERALALEUPROVALILEGLUASN
3   ALAGLULYSASNTHRVALVALTHRLYSTHR
4   LEUVALLEUPROLYSSERASPASPGLYSER
5   GLNGLNTHRGLNTHRILETHRTYRLYSASP
6   LYSTHRPHELEUSERLEUALAILEGLNGLN
7   LYSARGPROVALSERASPGLULEULYSTHR
8   TYRILEASPGLNHISGLYVALGLUGLUTHR
9   GLNLYSALALEULEUGLUALAGLUGLULYS
10   ASPLYSSERILEILEGLUALAARGLYSLEU
11   ALAGLYPHELYSLEUGLUTHRLYSLEULEU
12   SERALATHRGLULEUGLNTHRTHRTHRSER
13   PHEASPPHEGLNVALLEUASPVALLYSLYS
14   ALASERGLNLEUGLUHISLEULYSASNILE
15   GLYLEUGLUASNLEULEULYSASNGLUPRO
16   SERLYSTYRILESERASPARGLEUALAASN
17   GLYALATHRGLUGLN

Samples:

sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 95%; D2O 5%

sample_conditions_1: temperature: 298 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.0798 M

Experiments:

NameSampleSample stateSample conditions
APSY 4D-HACANHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert P., Herrmann, Guntert and Wuthrich - structure solution, chemical shift assignment, peak picking, structure solution

TOPSPIN v3.1, Bruker Biospin - collection, processing

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

UNIO'10, Herrmann, Guntert and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAR68045 CBJ23157 CBW31879 CBW33812 CBW35841
GB AAK74372 AAK98978 ABJ53699 ACA36140 ACB89456
REF NP_357768 WP_000725123 WP_000725125 WP_000725127 WP_000725131

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