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- PDB-2hqi: NMR SOLUTION STRUCTURE OF THE OXIDIZED FORM OF MERP, 14 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 2hqi
TitleNMR SOLUTION STRUCTURE OF THE OXIDIZED FORM OF MERP, 14 STRUCTURES
ComponentsMERCURIC TRANSPORT PROTEIN
KeywordsTRANSPORT / MERP / MERCURIC ION BINDING PROTEIN
Function / homology
Function and homology information


mercury ion transmembrane transporter activity / mercury ion binding / periplasmic space
Similarity search - Function
Mercuric transport protein periplasmic component / Mercuric transport protein periplasmic component/copper chaperone CopZ / Heavy-metal-associated, conserved site / Heavy-metal-associated domain. / Heavy-metal-associated domain / Heavy metal-associated domain superfamily / Heavy-metal-associated domain profile. / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / Alpha-Beta Plaits ...Mercuric transport protein periplasmic component / Mercuric transport protein periplasmic component/copper chaperone CopZ / Heavy-metal-associated, conserved site / Heavy-metal-associated domain. / Heavy-metal-associated domain / Heavy metal-associated domain superfamily / Heavy-metal-associated domain profile. / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Mercuric transport protein periplasmic component
Similarity search - Component
Biological speciesShigella flexneri (bacteria)
MethodSOLUTION NMR / SA
AuthorsQian, H. / Sahlman, L. / Eriksson, P.O. / Hambreus, C. / Edlund, U. / Sethson, I.
CitationJournal: Biochemistry / Year: 1998
Title: NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Authors: Qian, H. / Sahlman, L. / Eriksson, P.O. / Hambraeus, C. / Edlund, U. / Sethson, I.
History
DepositionMar 31, 1998Processing site: BNL
Revision 1.0Nov 11, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MERCURIC TRANSPORT PROTEIN


Theoretical massNumber of molelcules
Total (without water)7,4841
Polymers7,4841
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)14 / 20LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein MERCURIC TRANSPORT PROTEIN / MERP


Mass: 7483.630 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Shigella flexneri (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P04129

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: NOESY
NMR detailsText: TRIPLE RESONANCE EXPERIMENTS ON 13C, 15N-LABELED MERP

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Sample preparation

DetailsContents: WATER
Sample conditionsIonic strength: 0.3 / pH: 4.9 / Pressure: 1 atm / Temperature: 309 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.8model building
X-PLOR3.8refinement
X-PLOR3.8phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.8BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: SA / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 20 / Conformers submitted total number: 14

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