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Biological Magnetic Resonance Data Bank


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BMRB Entry 11041

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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/BMR11041
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Title: Solution structure of domains 3 and 4 of human ATP7B   PubMed: 18558714

Deposition date: 2008-04-04 Original release date: 2008-06-30

Authors: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Rosenzweig, Amy; Yatsunyk, Liliya

Citation: Banci, Lucia; Bertini, Ivano; Cantini, Francesca; Rosenzweig, Amy; Yatsunyk, Liliya. "Metal Binding Domains 3 and 4 of the Wilson Disease Protein: Solution Structure and Interaction with the Copper(I) Chaperone HAH1."  Biochemistry 47, 7423-7429 (2008).

Assembly members:
The third and fourth copper(I) binding soluble domains, polymer, 204 residues, Formula weight is not available

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):
The third and fourth copper(I) binding soluble domains: LSSANQNFNNSETLGHQGSH VVTLQLRIDGMHCKSCVLNI EENIGQLLGVQSIQVSLENK TAQVKYDPSCTSPVALQRAI EALPPGNFKVSLPDGAEGSG TDHRSSSSHSPGSPPRNQVQ GTCSTTLIAIAGMTCASCVH SIEGMISQLEGVQQISVSLA EGTATVLYNPAVISPEELRA AIEDMGFEASVVSESCSTNP LGNH

Data sets:
Data typeCount
13C chemical shifts681
15N chemical shifts184
1H chemical shifts1167

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1The third and fourth copper(I) binding soluble domains1

Entities:

Entity 1, The third and fourth copper(I) binding soluble domains 204 residues - Formula weight is not available

It consists of following 5 regions of the Copper-transporting ATPase, ATP7B. ( -1 - 19) the linker region connecting domains 2-3, no tags ( 20 - 90) the third soluble domain VTLQLRIDGMHCKSCVLNIE ENIGQLLGVQSIQVSLENKT AQVKYDPSCTSPVALQRAIE ALPPGNFKVSL ( 91 - 119) the inter-domain linker region between the third and fourth soluble domain, no tags (120 - 190) the fourth soluble domain TCSTTLIAIAGMTCASCVHS IEGMISQLEGVQQISVSLAE GTATVLYNPAVISPEELRAA IEDMGFEASVV (191 - 202) the linker region connecting domains 4-5, no tags We have solved the solution structure of all construct including also the linker region but due to its random-coiled like conformation the two domains reorient freely in solution, without any stabilizing inter-domain interaction. For this reason I decided to omit the submission of the coordinates for the linker region. I have instead included the assignment for the latter region.

1   LEUSERSERALAASNGLNASNPHEASNASN
2   SERGLUTHRLEUGLYHISGLNGLYSERHIS
3   VALVALTHRLEUGLNLEUARGILEASPGLY
4   METHISCYSLYSSERCYSVALLEUASNILE
5   GLUGLUASNILEGLYGLNLEULEUGLYVAL
6   GLNSERILEGLNVALSERLEUGLUASNLYS
7   THRALAGLNVALLYSTYRASPPROSERCYS
8   THRSERPROVALALALEUGLNARGALAILE
9   GLUALALEUPROPROGLYASNPHELYSVAL
10   SERLEUPROASPGLYALAGLUGLYSERGLY
11   THRASPHISARGSERSERSERSERHISSER
12   PROGLYSERPROPROARGASNGLNVALGLN
13   GLYTHRCYSSERTHRTHRLEUILEALAILE
14   ALAGLYMETTHRCYSALASERCYSVALHIS
15   SERILEGLUGLYMETILESERGLNLEUGLU
16   GLYVALGLNGLNILESERVALSERLEUALA
17   GLUGLYTHRALATHRVALLEUTYRASNPRO
18   ALAVALILESERPROGLUGLULEUARGALA
19   ALAILEGLUASPMETGLYPHEGLUALASER
20   VALVALSERGLUSERCYSSERTHRASNPRO
21   LEUGLYASNHIS

Samples:

sample_1: The third and fourth copper(I) binding soluble domains, [U-99% 13C; U-99% 15N], 0.1 – 0.4 mM; Na Pi 20 mM; NaCl 150 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.3 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
R1sample_1isotropicsample_conditions_1
R2sample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm, Guntert, Mumenthaler and Wuthrich, Keller and Wuthrich - chemical shift assignment, data analysis, data analysis

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

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Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone or all simulated shifts