BMRB Entry 11001

Title:
Solution structure of Cu(I) loaded human Sco2
Deposition date:
2007-07-11
Original release date:
2008-03-13
Authors:
Banci, Lucia; Bertini, Ivano; Ciofi-baffoni, Simone; Gerothanassis, Ioannis; Leontari, Iliana; Martinelli, Manuele; Wang, Shenlin
Citation:

Citation: Banci, Lucia; Bertini, Ivano; Ciofi-baffoni, Simone; Gerothanassis, Ioannis; Leontari, Iliana; Martinelli, Manuele; Wang, Shenlin. "A structural characterization of human SCO2."  Structure 15, 1132-1140 (2007).
PubMed: 17850752

Assembly members:

Assembly members:
HSco2, polymer, 170 residues, 19446.004 Da.
CU1, non-polymer, 63.546 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PETG-30A

Data sets:
Data typeCount
13C chemical shifts650
15N chemical shifts182
1H chemical shifts1121

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HSco21
2COPPER (I) ION2

Entities:

Entity 1, HSco2 170 residues - 19446.004 Da.

1   SERPHETHRGLYGLNGLYASPPHEHISLEU
2   LEUASPHISARGGLYARGALAARGCYSLYS
3   ALAASPPHEARGGLYGLNTRPVALLEUMET
4   TYRPHEGLYPHETHRHISCYSPROASPILE
5   CYSPROASPGLULEUGLULYSLEUVALGLN
6   VALVALARGGLNLEUGLUALAGLUPROGLY
7   LEUPROPROVALGLNPROVALPHEILETHR
8   VALASPPROGLUARGASPASPVALGLUALA
9   METALAARGTYRVALGLNASPPHEHISPRO
10   ARGLEULEUGLYLEUTHRGLYSERTHRLYS
11   GLNVALALAGLNALASERHISSERTYRARG
12   VALTYRTYRASNALAGLYPROLYSASPGLU
13   ASPGLNASPTYRILEVALASPHISSERILE
14   ALAILETYRLEULEUASNPROASPGLYLEU
15   PHETHRASPTYRTYRGLYARGSERARGSER
16   ALAGLUGLNILESERASPSERVALARGARG
17   HISMETALAALAPHEARGSERVALLEUSER

Entity 2, COPPER (I) ION - Cu - 63.546 Da.

1   CU1

Samples:

sample_1: Cu(I)HSco2, [U-100% 13C; U-100% 15N], 0.8 ± 0.1 mM

sample_2: Cu(I)HSco2, [U-100% 15N], 0.8 ± 0.1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.2; pressure: 1 atm; temperature: 308 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

xwinnmr v3.6, Bruker Biospin - collection, processing

CARA v2.0, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

DYANA v1.5, Guntert, Braun and Wuthrich - structure solution

AMBER v8.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Koll - refinement

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAI46393
EMBL CAA16671 CAG30455 CAK54599 CAK54898
GB AAF05313 AAI02025 AAI02026 AIC50475 AKI71892
REF NP_001162580 NP_001162581 NP_001162582 NP_005129 XP_003317370
SP O43819
AlphaFold O43819

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