BMRB Entry 5813

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PDB ID: 1p6t
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5813
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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:

The solution structure of the whole N-terminal domain of the ATPase CopA from Bacillus Subtilis. Implications for the function

Deposition date:

2003-05-31

Original release date:

2004-01-21

Authors:

Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Gonnelli, L.; Su, X.

Citation:

Citation: Banci, L.; Bertini, I.; Ciofi-Baffoni, S.; Gonnelli, L.; Su, X.. "Structural basis for the function of the N terminal domain of the ATPase CopA from Bacillus subtilis" J. Biol. Chem. 278, 50506-50513 (2003).
PubMed: 14514665

Assembly members:

Assembly members:
copper-transporting ATPase CopA, polymer, 151 residues, 16380.7 Da.

Natural source:

Natural source: Common Name: Bacillus subtilis Taxonomy ID: 224308 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
copper-transporting ATPase CopA: MLSEQKEIAMQVSGMTCAAC AARIEKGLKRMPGVTDANVN LATETVNVIYDPAETGTAAI QEKIEKLGYHVVTEKAEFDI EGMTCAACANRIEKRLNKIE GVANAPVNFALETVTVEYNP KEASVSDLKEAVDKLGYKLK LKGEQDSIEGR

Data sets:

assigned_chemical_shifts
- chemical_shift_set_1

Data type	Count
13C chemical shifts	552
15N chemical shifts	156
1H chemical shifts	947

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CopA	1

Entities:

Entity 1, CopA 151 residues - 16380.7 Da.

1

MET

LEU

SER

GLU

GLN

LYS

GLU

ILE

ALA

MET

2

GLN

VAL

SER

GLY

MET

THR

CYS

ALA

CYS

3

ALA

ARG

ILE

GLU

LYS

GLY

LEU

LYS

ARG

4

MET

PRO

GLY

VAL

THR

ASP

ALA

ASN

VAL

ASN

5

LEU

ALA

THR

GLU

THR

VAL

ASN

VAL

ILE

TYR

6

ASP

PRO

ALA

GLU

THR

GLY

THR

ALA

ILE

7

GLN

GLU

LYS

ILE

GLU

LYS

LEU

GLY

TYR

HIS

8

VAL

THR

GLU

LYS

ALA

GLU

PHE

ASP

ILE

9

GLU

GLY

MET

THR

CYS

ALA

CYS

ALA

ASN

10

ARG

ILE

GLU

LYS

ARG

LEU

ASN

LYS

ILE

GLU

11

GLY

VAL

ALA

ASN

ALA

PRO

VAL

ASN

PHE

ALA

12

LEU

GLU

THR

VAL

THR

VAL

GLU

TYR

ASN

PRO

13

LYS

GLU

ALA

SER

VAL

SER

ASP

LEU

LYS

GLU

14

ALA

VAL

ASP

LYS

LEU

GLY

TYR

LYS

LEU

LYS

15

LEU

LYS

GLY

GLU

GLN

ASP

SER

ILE

GLU

GLY

16

ARG

Samples:

sample_1: copper-transporting ATPase CopA, [U-95% 13C; U-90% 15N], 1.5 mM; phosphate 20 mM; H2O 90%; D2O 10%; DTT 2.0 mM

sample_cond_1: ionic strength: 22 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D NOESY	not available	not available	not available
2D TOCSY	not available	not available	not available
3D 13C-separated NOESY	not available	not available	not available
3D 15N-separated NOESY	not available	not available	not available
HNHA	not available	not available	not available
HNHB	not available	not available	not available
CC(CO)NH	not available	not available	not available
(H)CCH-TOCSY	not available	not available	not available
CBCANH	not available	not available	not available
CBCA(CO)NH	not available	not available	not available

Software:

xwinnmr v2.6 - processing

DYANA v1.5 - structure solution

XEASY v1.3 - structure solution

AMBER v5.0 - refinement

NMR spectrometers:

Bruker AVANCE 800 MHz
Bruker AVANCE 700 MHz
Bruker AVANCE 500 MHz