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- PDB-5frf: Solution structure of reduced and zinc-bound RsrA -

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Basic information

Entry
Database: PDB / ID: 5frf
TitleSolution structure of reduced and zinc-bound RsrA
ComponentsANTI-SIGMA FACTOR RSRA
KeywordsTRANSCRIPTION / ANTI-SIGMA FACTOR / REDOX SENSING
Function / homology
Function and homology information


detection of redox state / sporulation / sigma factor antagonist activity / response to redox state / sporulation resulting in formation of a cellular spore / zinc ion binding
Similarity search - Function
Anti-sigma factor / Anti sigma-R factor, mycothiol system,RsrA / Putative zinc-finger / Putative zinc-finger
Similarity search - Domain/homology
Anti-sigma factor RsrA
Similarity search - Component
Biological speciesSTREPTOMYCES COELICOLOR (bacteria)
MethodSOLUTION NMR
AuthorsZdanowski, K. / Pecqueur, L. / Werner, J. / Potts, J.R. / Kleanthous, C.
CitationJournal: Nat.Commun. / Year: 2016
Title: The Anti-Sigma Factor Rsra Responds to Oxidative Stress by Reburying its Hydrophobic Core.
Authors: Rajasekar, K.V. / Zdanowski, K. / Yan, J. / Hopper, J.T. / Francis, M.L. / Seepersad, C. / Sharp, C. / Pecqueur, L. / Werner, J.M. / Robinson, C.V. / Mohammed, S. / Potts, J.R. / Kleanthous, C.
History
DepositionDec 17, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 3, 2016Provider: repository / Type: Initial release
Revision 2.0Oct 23, 2019Group: Atomic model / Data collection / Other
Category: atom_site / pdbx_database_status / pdbx_nmr_spectrometer
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_nmr_spectrometer.model
Revision 2.1May 15, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: ANTI-SIGMA FACTOR RSRA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)11,9002
Polymers11,8351
Non-polymers651
Water00
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 100LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein ANTI-SIGMA FACTOR RSRA / REGULATOR OF SIGR / SIGMA-R ANTI-SIGMA FACTOR RSRA


Mass: 11835.058 Da / Num. of mol.: 1 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) STREPTOMYCES COELICOLOR (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: Q7AKG8
#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
Sequence detailsCOMPARED TO THE SEQUENCE CORRESPONDING TO THIS SEQUENCE ACCESSION NUMBER THERE ARE THREE N-TERMINAL ...COMPARED TO THE SEQUENCE CORRESPONDING TO THIS SEQUENCE ACCESSION NUMBER THERE ARE THREE N-TERMINAL NON-NATIVE RESIDUES AND FIVE MUTATIONS (AS STATED ABOVE) IN THE SUBMITTED PDB FILES.

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121TOCSY (2D
1313D)
141HNCA
151CBCANH
161CBCA(CO)NH
171HNCO
181HN(CA)CO
NMR detailsText: NONE

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Sample preparation

DetailsContents: 5% D2O/(5% WATER
Sample conditionspH: 7.1 / Temperature: 298.0 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz

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Processing

NMR software
NameDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-KUNSTLEVE, JIANG,KUSZEWSKI,NILGES,PANNU,READ,RICE,SIMONSON, WARRENrefinement
CNSstructure solution
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 100 / Conformers submitted total number: 10

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