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- PDB-1sut: NMR STUDY OF THE PROLINE REPEAT FROM TUS -

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Basic information

Entry
Database: PDB / ID: 1sut
TitleNMR STUDY OF THE PROLINE REPEAT FROM TUS
ComponentsTUS PROLINE REPEAT
KeywordsDNA BINDING PROTEIN / DNA-BINDING PROTEIN
Function / homologyDNA replication terminus site-binding protein / Replication terminator Tus, domain 1 / Replication terminator Tus superfamily / DNA replication terminus site-binding protein (Ter protein) / replication fork arrest involved in DNA replication termination / DNA replication termination / sequence-specific DNA binding / cytoplasm / DNA replication terminus site-binding protein
Function and homology information
MethodSOLUTION NMR
AuthorsButcher, D.J. / Nedved, M.L. / Neiss, T.G. / Moe, G.R.
Citation
Journal: Biochemistry / Year: 1996
Title: Proline pipe helix: structure of the tus proline repeat determined by 1H NMR.
Authors: Butcher, D.J. / Nedved, M.L. / Neiss, T.G. / Moe, G.R.
#1: Journal: Nucleic Acids Res. / Year: 1994
Title: Cd and DNA Binding Studies of a Proline Repeat-Containing Segment of the Replication Arrest Protein Tus
Authors: Nedved, M.L. / Gottlieb, P.A. / Moe, G.R.
History
DepositionNov 29, 1995Processing site: BNL
Revision 1.0Apr 3, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 3, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Structure summary
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_keywords / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name / _struct_keywords.text / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TUS PROLINE REPEAT


Theoretical massNumber of molelcules
Total (without water)2,6101
Polymers2,6101
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Atom site foot note1: GLN 15 - PRO 16 MODEL 1 OMEGA = 146.83 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
2: PRO 16 - ILE 17 MODEL 1 OMEGA = 216.85 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
3: PRO 16 - ILE 17 MODEL 2 OMEGA = 214.53 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
4: ARG 20 - VAL 21 MODEL 3 OMEGA = 227.62 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
5: VAL 21 - TYR 22 MODEL 4 OMEGA = 133.63 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
6: PRO 16 - ILE 17 MODEL 5 OMEGA = 216.27 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
7: PRO 1 - GLN 2 MODEL 6 OMEGA = 144.81 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
8: ARG 10 - PRO 11 MODEL 6 OMEGA = 140.95 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
9: GLN 15 - PRO 16 MODEL 6 OMEGA = 136.64 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
10: PRO 16 - ILE 17 MODEL 6 OMEGA = 216.19 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
11: ARG 20 - VAL 21 MODEL 7 OMEGA = 231.36 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
12: PRO 16 - ILE 17 MODEL 8 OMEGA = 212.26 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
13: VAL 21 - TYR 22 MODEL 8 OMEGA = 133.52 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
14: PRO 16 - ILE 17 MODEL 9 OMEGA = 218.25 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
15: PRO 1 - GLN 2 MODEL 10 OMEGA = 129.29 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
16: ARG 10 - PRO 11 MODEL 10 OMEGA = 146.57 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
17: PRO 16 - ILE 17 MODEL 10 OMEGA = 226.08 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
18: ARG 20 - VAL 21 MODEL 10 OMEGA = 227.18 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / -
Representative

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Components

#1: Protein/peptide TUS PROLINE REPEAT


Mass: 2610.216 Da / Num. of mol.: 1 / Fragment: TUS PROLINE REPEAT DOMAIN, RESIDUES 223 - 244
Source method: isolated from a genetically manipulated source
References: UniProt: P16525

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other

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Processing

NMR software
NameDeveloperClassification
NMRCHITECTBIOSYMrefinement
DiscoverBIOSYMrefinement
NMR ensembleConformers submitted total number: 10

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