+Open data
-Basic information
Entry | Database: PDB / ID: 1dz1 | ||||||
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Title | Mouse HP1 (M31) C terminal (shadow chromo) domain | ||||||
Components | MODIFIER 1 PROTEIN | ||||||
Keywords | CHROMATIN STRUCTURE / CHROMO DOMAIN / HETEROCHROMATIN PROTEIN PROTEIN INTERACTION / DIMERIC | ||||||
Function / homology | Function and homology information chromocenter / histone methyltransferase binding / male pronucleus / female pronucleus / site of DNA damage / chromosome, centromeric region / pericentric heterochromatin / methylated histone binding / spindle / chromatin organization ...chromocenter / histone methyltransferase binding / male pronucleus / female pronucleus / site of DNA damage / chromosome, centromeric region / pericentric heterochromatin / methylated histone binding / spindle / chromatin organization / chromosome, telomeric region / molecular adaptor activity / nuclear body / intracellular membrane-bounded organelle / negative regulation of DNA-templated transcription / DNA damage response / chromatin binding / chromatin / negative regulation of transcription by RNA polymerase II / enzyme binding / DNA binding / nucleoplasm / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | MUS MUSCULUS (house mouse) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Brasher, S.V. / Smith, B.O. / Fogh, R.H. / Nietlispach, D. / Thiru, A. / Nielsen, P.R. / Broadhurst, R.W. / Ball, L.J. / Murzina, N. / Laue, E.D. | ||||||
Citation | Journal: Embo J. / Year: 2000 Title: The Structure of Mouse Hp1 Suggests a Unique Mode of Single Peptide Recognition by the Shadow Chromo Domain Dimer Authors: Brasher, S.V. / Smith, B.O. / Fogh, R.H. / Nietlispach, D. / Thiru, A. / Nielsen, P.R. / Broadhurst, R.W. / Ball, L.J. / Murzina, N. / Laue, E.D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dz1.cif.gz | 695.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dz1.ent.gz | 602.5 KB | Display | PDB format |
PDBx/mmJSON format | 1dz1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dz/1dz1 ftp://data.pdbj.org/pub/pdb/validation_reports/dz/1dz1 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8076.179 Da / Num. of mol.: 2 / Fragment: SHADOW CHROMO DOMAIN, RESIDUES 104-171 Source method: isolated from a genetically manipulated source Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PET16B / Production host: Escherichia coli BL21(DE3) / References: UniProt: P83917 Sequence details | HIS A 102 CLONING ARTIFACT MUTATION ARISING FROM VECTOR MET A 103 CLONING ARTIFACT MUTATION ARISING ...HIS A 102 CLONING ARTIFACT MUTATION ARISING FROM VECTOR MET A 103 CLONING ARTIFACT MUTATION ARISING FROM VECTOR HIS B 102 CLONING ARTIFACT MUTATION ARISING FROM VECTOR MET B 103 CLONING ARTIFACT MUTATION ARISING FROM VECTOR | |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. DOUBLE-HALF FILTERED 2D NOESY AND HALF-FILTERED HSQC-NOESY ON A MIXED LABELED/UNLABELED SAMPLE ...Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED PROTEIN. DOUBLE-HALF FILTERED 2D NOESY AND HALF-FILTERED HSQC-NOESY ON A MIXED LABELED/UNLABELED SAMPLE WERE USED TO DISTINGUISH INTRA- AND INTER-MONOMER NOES. RESIDUES 102-109 AND 171 ARE INSUFFICIENTLY CONSTRAINED BY THE INPUT DATA AND SHOULD BE CONSIDERED OF UNKNOWN STRUCTURE. THUS THE STRUCTURE IS ONLY DEFINED FOR RESIDUES 110 - 170. |
-Sample preparation
Details | Contents: 0.6-1.4 MM MOUSE HP1 C-TERMINAL DOMAIN (AS MONOMER), 10 MM SODIUM PHOSPHATE BUFFER, 10 MM PERDEUTERATED DTT, 0.05% SODIUM AZIDE |
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Sample conditions | pH: 8.0 / Pressure: 1 atm / Temperature: 303 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. STRUCTURE WAS GENERATED FROM EXPERIMENTS CARRIED OUT AT 303-308K WITH PH 7.5-8.0 | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LEAST NOE VIOLATION ENERGY / Conformers calculated total number: 35 / Conformers submitted total number: 16 |