BMRB Entry 16277

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16277
MolProbity Validation Chart

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Title:
Solution structure of the Actuator domain of the copper-transporting ATPase ATP7A
Deposition date:
2009-05-06
Original release date:
2009-09-04
Authors:
Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Migliardi, Manuele; Nushi, Fiorentin; Natile, Giovanni; Rosato, Antonio
Citation:

Citation: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Migliardi, Manuele; Nushi, Fiorentin; Natile, Giovanni; Rosato, Antonio. "SOLUTION STRUCTURES OF THE ACTUATOR DOMAIN OF ATP7A AND ATP7B, THE MENKES AND WILSON DISEASE PROTEINS"  J. Biol. Chem. 48, 7849-7855 (2009).
PubMed: 19645496

Assembly members:

Assembly members:
Actd, polymer, 119 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: not available   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETG-20A (EMBL)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Actd: SEALAKLISLQATEATIVTL DSDNILLSEEQVDVELVQRG DIIKVVPGGKFPVDGRVIEG HSMVDESLITGEAMPVAKKP GSTVIAGSINQNGSLLICAT HVGADTTLSQIVKLVEEAQ

Data sets:
Data typeCount
13C chemical shifts494
15N chemical shifts122
1H chemical shifts834

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Actd1

Entities:

Entity 1, Actd 119 residues - Formula weight is not available

Residues GSFTM at the N-terminus represent a non-native tag and they have been removed from the coordinates file

1   SERGLUALALEUALALYSLEUILESERLEU
2   GLNALATHRGLUALATHRILEVALTHRLEU
3   ASPSERASPASNILELEULEUSERGLUGLU
4   GLNVALASPVALGLULEUVALGLNARGGLY
5   ASPILEILELYSVALVALPROGLYGLYLYS
6   PHEPROVALASPGLYARGVALILEGLUGLY
7   HISSERMETVALASPGLUSERLEUILETHR
8   GLYGLUALAMETPROVALALALYSLYSPRO
9   GLYSERTHRVALILEALAGLYSERILEASN
10   GLNASNGLYSERLEULEUILECYSALATHR
11   HISVALGLYALAASPTHRTHRLEUSERGLN
12   ILEVALLYSLEUVALGLUGLUALAGLN

Samples:

sample_1: Actd 0.2-0.3 ± 0.05 mM; H2O 90%; D2O 10%; phosphate 50 mM; arginine 50 mM; glutamate 50 mM; DTT 1 mM

sample_3: Actd, [U-13C; U-15N], 0.2-0.3 ± 0.05 mM; H2O 90%; D2O 10%; phosphate 50 mM; arginine 50 mM; glutamate 50 mM; DTT 1 mM

sample_2: Actd, [U-15N], 0.2-0.3 ± 0.05 mM; H2O 90%; D2O 10%; phosphate 50 mM; arginine 50 mM; glutamate 50 mM; DTT 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment

XEASY, Bartels et al. - data analysis

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 800 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAF62333
EMBL CAB08162 CAB94714
GB AAA35580 AAA96010 AAB39918 AAI56438 EAW98605
REF NP_000043 NP_001179781 NP_001269153 XP_002720177 XP_002806338
SP P49015 Q04656
TPG DAA12973
AlphaFold P49015 Q04656

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