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- PDB-1hi7: NMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMA... -

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Basic information

Entry
Database: PDB / ID: 1hi7
TitleNMR SOLUTION STRUCTURE OF THE DISULPHIDE-LINKED HOMODIMER OF HUMAN TFF1, 10 STRUCTURES
ComponentsPS2 PROTEIN
KeywordsGROWTH FACTOR / CELL MOTILITY / TUMOR SUPPRESSOR / TREFOIL DOMAIN
Function / homology
Function and homology information


maintenance of gastrointestinal epithelium / response to iron ion / response to immobilization stress / growth factor activity / response to peptide hormone / Estrogen-dependent gene expression / cell population proliferation / carbohydrate metabolic process / cell differentiation / negative regulation of cell population proliferation ...maintenance of gastrointestinal epithelium / response to iron ion / response to immobilization stress / growth factor activity / response to peptide hormone / Estrogen-dependent gene expression / cell population proliferation / carbohydrate metabolic process / cell differentiation / negative regulation of cell population proliferation / extracellular space / extracellular region
Similarity search - Function
P-type trefoil, chordata / Spasmolytic Protein, domain 1 / Spasmolytic Protein; domain 1 / P-type trefoil, conserved site / P-type 'Trefoil' domain signature. / Trefoil (P-type) domain / P-type trefoil domain / P-type trefoil domain superfamily / P-type 'Trefoil' domain profile. / P or trefoil or TFF domain ...P-type trefoil, chordata / Spasmolytic Protein, domain 1 / Spasmolytic Protein; domain 1 / P-type trefoil, conserved site / P-type 'Trefoil' domain signature. / Trefoil (P-type) domain / P-type trefoil domain / P-type trefoil domain superfamily / P-type 'Trefoil' domain profile. / P or trefoil or TFF domain / Few Secondary Structures / Irregular
Similarity search - Domain/homology
Biological speciesHOMO SAPIENS (human)
MethodSOLUTION NMR / simulated annealing
AuthorsWilliams, M.A. / Feeney, J.
Citation
Journal: FEBS Lett. / Year: 2001
Title: The Solution Structure of the Disulphide-Linked Dimeric of the Human Trefoil Protein Tff1
Authors: Williams, M.A. / Westley, B.R. / May, F.E. / Feeney, J.
#1: Journal: J.Mol.Biol. / Year: 1997
Title: High-Resolution Solution Structure of Human Pnr-2/ Ps2: A Single Trefoil Motif Protein
Authors: Polshakov, V.I. / Williams, M.A. / Gargaro, A.R. / Frenkiel, T.A. / Westley, B.R. / Chadwick, M.P. / May, F.E.B. / Feeney, J.
#2: Journal: Biochem.J. / Year: 1997
Title: Homodimerization and Hetero_Oligomerization of the Single Domain Trefoil Protein Pnr-2/Ps2 Through Cysteine 58
Authors: Chadwick, M.P. / May, F.E.B. / Westley, B.R.
#3: Journal: Biochem.J. / Year: 1995
Title: Production and Comparison of Mature Single-Domain 'Trefoil' Peptides Pnr-2/Ps2 Cys58 and Pnr-2/Ps2 Ser58
Authors: Chadwick, M.P. / May, F.E.B. / Westley, B.R.
#4: Journal: Eur.J.Biochem. / Year: 1995
Title: NMR-Based Structural Studies of the Pnr-2/Ps2 Single Domain Trefoil Peptide. Similarities to Porcine Spasmolytic Peptide and Evidence for a Monomeric Structure
Authors: Polshakov, V.I. / Frenkiel, T.A. / Westley, B. / Chadwick, M. / May, F. / Carr, M.D. / Feeney, J.
History
DepositionJan 3, 2001Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 3, 2001Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 14, 2017Group: Structure summary / Category: pdbx_nmr_representative / Item: _pdbx_nmr_representative.conformer_id
Revision 1.4Apr 10, 2019Group: Data collection / Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id / _entity_src_gen.pdbx_host_org_scientific_name
Revision 1.5Oct 9, 2024Group: Data collection / Database references ...Data collection / Database references / Other / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_mr / _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: PS2 PROTEIN
B: PS2 PROTEIN


Theoretical massNumber of molelcules
Total (without water)13,3572
Polymers13,3572
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 11TOTAL NOE CONSTRAINT VIOLATIONS < 1.0 A
RepresentativeModel #6

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Components

#1: Protein PS2 PROTEIN / PNR-2 / PS2 / TFF1 / BREAST CANCER ESTROGEN INDUCIBLE PROTEIN / TREFOIL FACTOR FAMILY 1 PROTEIN


Mass: 6678.365 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: DISULPHIDE LINK BETWEEN C58 OF BOTH SUBUNITS / Source: (gene. exp.) HOMO SAPIENS (human) / Tissue: EPITHELIAL / Cell: MCF-7, UACL / Cellular location: EXTRACELLULAR / Gene: TFF1 / Organ: BREAST, STOMACH / Cellular location (production host): CYTOPLASM / Gene (production host): TFF1 / Production host: ESCHERICHIA COLI HB101 (bacteria) / References: UniProt: P04155
Has protein modificationY
Sequence details1PS2 SWS P04155 1 - 24 NOT IN ATOMS LIST

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112-D 1H-1H HOMONUCLEAR TOCSY
121ROESY
131NOESY
1411H/15N HSQC
151HSQC-NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TWO AND THREE DIMENSIONAL NMR EXPERIMENTS ON, RESPECTIVELY, UNLABELLED AND N-15 LABELLED TFF1 DIMER PROTEIN. MANY ASSIGN WERE MADE BY MAKING USE IF THE BETTER ...Text: THE STRUCTURE WAS DETERMINED USING TWO AND THREE DIMENSIONAL NMR EXPERIMENTS ON, RESPECTIVELY, UNLABELLED AND N-15 LABELLED TFF1 DIMER PROTEIN. MANY ASSIGN WERE MADE BY MAKING USE IF THE BETTER RESOLVED MONOMER SPECTRA (POLSHAKOV ET AL. 1995,1997)

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Sample preparation

Sample conditionsIonic strength: 0.01 / pH: 5.9 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITYVarianUNITY5001
Varian UNITYPLUSVarianUNITYPLUS6002

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Processing

NMR software
NameVersionDeveloperClassification
CNS1BRUNGERrefinement
CNS1structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: TOTAL NOE CONSTRAINT VIOLATIONS < 1.0 A
Conformers calculated total number: 11 / Conformers submitted total number: 10

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