BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11502

Title: Copper(I) loaded form of the first domain of the human copper chaperone for SOD1, CCS

Authors: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Kozyreva, Tatiana; Rubino, Jeffrey

Citation: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Kozyreva, Tatiana; Rubino, Jeffrey. "Copper(I) loaded form of the first domain of the human copper chaperone for SOD1, CCS"  Not known ., .-..

Assembly members:
D1CCS, polymer, 89 residues, 7561.739 Da.
entity_CU1, non-polymer, 63.546 Da.

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

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

Entity Sequences (FASTA):
D1CCS: GSFTMASDSGNQGTLCTLEF AVQMTCQSCVDAVRKSLQGV AGVQDVEVHLEDQMVLVHTT LPSQEVQALLEGTGRQAVLK GMGSGQLQN

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts94
1H chemical shifts475

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1D1CCS1
2COPPER (I) ION2

Entities:

Entity 1, D1CCS 89 residues - 7561.739 Da.

GSFT gateway system. We have removed residues MASDSGNQ at the Nterminus and residues SGQLQN at the Cterminus because they are unstructured

1   GLYSERPHETHRMETALASERASPSERGLY
2   ASNGLNGLYTHRLEUCYSTHRLEUGLUPHE
3   ALAVALGLNMETTHRCYSGLNSERCYSVAL
4   ASPALAVALARGLYSSERLEUGLNGLYVAL
5   ALAGLYVALGLNASPVALGLUVALHISLEU
6   GLUASPGLNMETVALLEUVALHISTHRTHR
7   LEUPROSERGLNGLUVALGLNALALEULEU
8   GLUGLYTHRGLYARGGLNALAVALLEULYS
9   GLYMETGLYSERGLYGLNLEUGLNASN

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

1   CU1

Samples:

sample_1: D1CCS, [U-99% 15N], 0.5 ± 0.1 mM; H2O 90%; D2O 10%; Na phosphate 0.1 mM; NaCl 0.1 mM

sample_2: D1CCS, [U-99% 13C; U-99% 15N], 0.5 ± 0.1 mM; H2O 90%; D2O 10%; Na phosphate 0.1 mM; NaCl 0.1 mM

sample_3: D1CCS 0.5 ± 0.1 mM; H2O 90%; D2O 10%; Na phosphate 0.1 mM; NaCl 0.1 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 0.2 M; pH: 6.0; temperature: 298 K

sample_conditions_3: ionic strength: 0.2 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_2
2D 1H-1H NOESYsample_3isotropicsample_conditions_3
3D CBCA(CO)NHsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_2isotropicsample_conditions_2

Software:

TOPSPIN v2.0, Bruker Biospin - collection, processing

XEASY, Bartels et al. - data analysis

CARA, Keller, R. and W thrich, K. - chemical shift assignment

AMBER v10, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA v2.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAI63082 BAI63083 BAI63084 BAI63087
EMBL CAG46726
GB AAC51764 AAI05017 AAI12056 AAM50090 AAX36906
REF NP_001167001 NP_001171971 NP_005116 XP_002821513 XP_003828733
SP O14618