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Open data
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Basic information
Entry | Database: PDB / ID: 1sut | ||||||
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Title | NMR STUDY OF THE PROLINE REPEAT FROM TUS | ||||||
![]() | TUS PROLINE REPEAT | ||||||
![]() | DNA BINDING PROTEIN / DNA-BINDING PROTEIN | ||||||
Function / homology | DNA 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![]() | ||||||
Method | SOLUTION NMR | ||||||
![]() | Butcher, D.J. / Nedved, M.L. / Neiss, T.G. / Moe, G.R. | ||||||
![]() | ![]() 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: ![]() 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 |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 86 KB | Display | ![]() |
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PDB format | ![]() | 51.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 349.1 KB | Display | ![]() |
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Full document | ![]() | 418.8 KB | Display | |
Data in XML | ![]() | 8.8 KB | Display | |
Data in CIF | ![]() | 12.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Atom site foot note | 1: 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 |
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Components
#1: Protein/peptide | 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
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Crystal grow | *PLUS Method: other |
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Processing
NMR software |
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NMR ensemble | Conformers submitted total number: 10 |