BMRB Entry 11001

Name: Solution structure of Cu(I) loaded human Sco2
Published: 2008-03-13

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11001

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HSco2: SFTGQGDFHLLDHRGRARCK ADFRGQWVLMYFGFTHCPDI CPDELEKLVQVVRQLEAEPG LPPVQPVFITVDPERDDVEA MARYVQDFHPRLLGLTGSTK QVAQASHSYRVYYNAGPKDE DQDYIVDHSIAIYLLNPDGL FTDYYGRSRSAEQISDSVRR HMAAFRSVLS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	650
15N chemical shifts	182
1H chemical shifts	1121

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	HSco2	1
2	COPPER (I) ION	2

Entities:

Entity 1, HSco2 170 residues - 19446.004 Da.

1	SER	PHE	THR	GLY	GLN	GLY	ASP	PHE	HIS	LEU
2	LEU	ASP	HIS	ARG	GLY	ARG	ALA	ARG	CYS	LYS
3	ALA	ASP	PHE	ARG	GLY	GLN	TRP	VAL	LEU	MET
4	TYR	PHE	GLY	PHE	THR	HIS	CYS	PRO	ASP	ILE
5	CYS	PRO	ASP	GLU	LEU	GLU	LYS	LEU	VAL	GLN
6	VAL	VAL	ARG	GLN	LEU	GLU	ALA	GLU	PRO	GLY
7	LEU	PRO	PRO	VAL	GLN	PRO	VAL	PHE	ILE	THR
8	VAL	ASP	PRO	GLU	ARG	ASP	ASP	VAL	GLU	ALA
9	MET	ALA	ARG	TYR	VAL	GLN	ASP	PHE	HIS	PRO
10	ARG	LEU	LEU	GLY	LEU	THR	GLY	SER	THR	LYS
11	GLN	VAL	ALA	GLN	ALA	SER	HIS	SER	TYR	ARG
12	VAL	TYR	TYR	ASN	ALA	GLY	PRO	LYS	ASP	GLU
13	ASP	GLN	ASP	TYR	ILE	VAL	ASP	HIS	SER	ILE
14	ALA	ILE	TYR	LEU	LEU	ASN	PRO	ASP	GLY	LEU
15	PHE	THR	ASP	TYR	TYR	GLY	ARG	SER	ARG	SER
16	ALA	GLU	GLN	ILE	SER	ASP	SER	VAL	ARG	ARG
17	HIS	MET	ALA	ALA	PHE	ARG	SER	VAL	LEU	SER

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_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

PDB	2RLI
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

1	SER	PHE	THR	GLY	GLN	GLY	ASP	PHE	HIS	LEU
2	LEU	ASP	HIS	ARG	GLY	ARG	ALA	ARG	CYS	LYS
3	ALA	ASP	PHE	ARG	GLY	GLN	TRP	VAL	LEU	MET
4	TYR	PHE	GLY	PHE	THR	HIS	CYS	PRO	ASP	ILE
5	CYS	PRO	ASP	GLU	LEU	GLU	LYS	LEU	VAL	GLN
6	VAL	VAL	ARG	GLN	LEU	GLU	ALA	GLU	PRO	GLY
7	LEU	PRO	PRO	VAL	GLN	PRO	VAL	PHE	ILE	THR
8	VAL	ASP	PRO	GLU	ARG	ASP	ASP	VAL	GLU	ALA
9	MET	ALA	ARG	TYR	VAL	GLN	ASP	PHE	HIS	PRO
10	ARG	LEU	LEU	GLY	LEU	THR	GLY	SER	THR	LYS
11	GLN	VAL	ALA	GLN	ALA	SER	HIS	SER	TYR	ARG
12	VAL	TYR	TYR	ASN	ALA	GLY	PRO	LYS	ASP	GLU
13	ASP	GLN	ASP	TYR	ILE	VAL	ASP	HIS	SER	ILE
14	ALA	ILE	TYR	LEU	LEU	ASN	PRO	ASP	GLY	LEU
15	PHE	THR	ASP	TYR	TYR	GLY	ARG	SER	ARG	SER
16	ALA	GLU	GLN	ILE	SER	ASP	SER	VAL	ARG	ARG
17	HIS	MET	ALA	ALA	PHE	ARG	SER	VAL	LEU	SER

1	SER	PHE	THR	GLY	GLN	GLY	ASP	PHE	HIS	LEU
2	LEU	ASP	HIS	ARG	GLY	ARG	ALA	ARG	CYS	LYS
3	ALA	ASP	PHE	ARG	GLY	GLN	TRP	VAL	LEU	MET
4	TYR	PHE	GLY	PHE	THR	HIS	CYS	PRO	ASP	ILE
5	CYS	PRO	ASP	GLU	LEU	GLU	LYS	LEU	VAL	GLN
6	VAL	VAL	ARG	GLN	LEU	GLU	ALA	GLU	PRO	GLY
7	LEU	PRO	PRO	VAL	GLN	PRO	VAL	PHE	ILE	THR
8	VAL	ASP	PRO	GLU	ARG	ASP	ASP	VAL	GLU	ALA
9	MET	ALA	ARG	TYR	VAL	GLN	ASP	PHE	HIS	PRO
10	ARG	LEU	LEU	GLY	LEU	THR	GLY	SER	THR	LYS
11	GLN	VAL	ALA	GLN	ALA	SER	HIS	SER	TYR	ARG
12	VAL	TYR	TYR	ASN	ALA	GLY	PRO	LYS	ASP	GLU
13	ASP	GLN	ASP	TYR	ILE	VAL	ASP	HIS	SER	ILE
14	ALA	ILE	TYR	LEU	LEU	ASN	PRO	ASP	GLY	LEU
15	PHE	THR	ASP	TYR	TYR	GLY	ARG	SER	ARG	SER
16	ALA	GLU	GLN	ILE	SER	ASP	SER	VAL	ARG	ARG
17	HIS	MET	ALA	ALA	PHE	ARG	SER	VAL	LEU	SER