BMRB Entry 15895

Title:
Solution structures of apo form PCuA (cis conformation of the peptide bond involving the nitrogen of P14)
Deposition date:
2008-07-28
Original release date:
2008-11-14
Authors:
Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Wang, Shenlin
Citation:

Citation: Abriata, Luciano; Banci, Lucia; Bertini, Ivano; Ciofi-Baffoni, Simone; Gkazonis, Petros; Spyroulias, Georgios; Vila, Alejandro; Wang, Shenlin. "Mechanism of Cu(A) assembly."  Nat. Chemical Biol. 4, 599-601 (2008).
PubMed: 18758441

Assembly members:

Assembly members:
apo form PCuA, polymer, 120 residues, 13222.670 Da.

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 274   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: BL21-Glod

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts104
1H chemical shifts841

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1apo form PCuA1

Entities:

Entity 1, apo form PCuA 120 residues - 13222.670 Da.

1   GLYSERPHETHRGLUGLYTRPVALARGPHE
2   SERPROGLYPROASNALAALAALATYRLEU
3   THRLEUGLUASNPROGLYASPLEUPROLEU
4   ARGLEUVALGLYALAARGTHRPROVALALA
5   GLUARGVALGLULEUHISGLUTHRPHEMET
6   ARGGLUVALGLUGLYLYSLYSVALMETGLY
7   METARGPROVALPROPHELEUGLUVALPRO
8   PROLYSGLYARGVALGLULEULYSPROGLY
9   GLYTYRHISPHEMETLEULEUGLYLEULYS
10   ARGPROLEULYSALAGLYGLUGLUVALGLU
11   LEUASPLEULEUPHEALAGLYGLYLYSVAL
12   LEULYSVALVALLEUPROVALGLUALAARG

Samples:

sample_1: entity, [U-100% 15N], 0.8 ± 0.1 mM; D2O 10%; H2O 90%; Pi 50 mM

sample_2: entity, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM; D2O 10%; H2O 90%; Pi 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
15N R2sample_1isotropicsample_conditions_1
15N R1sample_1isotropicsample_conditions_1
1H-15N NOEsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 500 MHz
  • Bruker Avance 400 MHz

Related Database Links:

BMRB 15894 15896 15897
PDB
DBJ BAD71766
GB AAS81922 AEG34334 AFH39883
REF WP_011173952 WP_011229034 WP_014510965 WP_014630387 YP_145209

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