+Open data
-Basic information
Entry | Database: PDB / ID: 2n1w | ||||||
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Title | Solution structure of human SUMO2 | ||||||
Components | Small ubiquitin-related modifier 2 | ||||||
Keywords | STRUCTURAL GENOMICS / Ubiquitin-like protein | ||||||
Function / homology | Function and homology information SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / SUMOylation of RNA binding proteins / SUMO transferase activity / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / protein sumoylation ...SUMO is proteolytically processed / SUMO is conjugated to E1 (UBA2:SAE1) / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / Vitamin D (calciferol) metabolism / SUMOylation of SUMOylation proteins / SUMOylation of RNA binding proteins / SUMO transferase activity / ubiquitin-like protein ligase binding / SUMOylation of DNA replication proteins / protein sumoylation / SUMOylation of transcription factors / SUMOylation of DNA damage response and repair proteins / SUMOylation of chromatin organization proteins / SUMOylation of transcription cofactors / SUMOylation of intracellular receptors / PML body / protein tag activity / Formation of Incision Complex in GG-NER / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Processing of DNA double-strand break ends / ubiquitin protein ligase binding / positive regulation of transcription by RNA polymerase II / RNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics, DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Naik, M.T. / Naik, N. / Shih, H. / Huang, T. | ||||||
Citation | Journal: To Be Published Title: Structures of human SUMO Authors: Naik, M.T. / Naik, N. / Shih, H. / Huang, T. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n1w.cif.gz | 572.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n1w.ent.gz | 479.7 KB | Display | PDB format |
PDBx/mmJSON format | 2n1w.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n1/2n1w ftp://data.pdbj.org/pub/pdb/validation_reports/n1/2n1w | HTTPS FTP |
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-Related structure data
Related structure data | 2n1vC 2n1x 2n1y 2n1z 2n20 C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 12242.603 Da / Num. of mol.: 1 / Fragment: UNP residues 1-93 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) Description: Plasmid pCDF PylT-1 with SUMO2 insert and pAcKRS-3 as described in Neumann et al., Mol Cell, 36, 153, 2009 Gene: SMT3B, SMT3H2, SUMO2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P61956 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Solution structure of Small Ubiquitin-related MOdifier 2. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: NMR data was acquired at 295K using Shigemi NMR tubes. |
-Sample preparation
Details |
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Sample |
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Sample conditions | pH: 6.5 / Pressure: ambient atm / Temperature: 290 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: torsion angle dynamics, DGSA-distance geometry simulated annealing Software ordinal: 1 Details: Initial structure ensemble was calculated by semi-automated NOESY assignment by CYANA. The assignments were manually verified in Sparky and final structure annealing was performed in CYANA. ...Details: Initial structure ensemble was calculated by semi-automated NOESY assignment by CYANA. The assignments were manually verified in Sparky and final structure annealing was performed in CYANA.Structure and restraints from CYANA were imported in Xplor-NIH for explicit water refinement., Initial structure ensemble was calculated by semi-automated NOESY assignment by CYANA. The assignments were manually verified in Sparky and final structure annealing was performed in CYANA.Structure and restraints from CYANA were imported in Xplor-NIH for explicit water refinement. | ||||||||||||||||||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2519 / NOE intraresidue total count: 526 / NOE long range total count: 902 / NOE medium range total count: 453 / NOE sequential total count: 638 / Disulfide bond constraints total count: 0 / Hydrogen bond constraints total count: 56 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 68 / Protein psi angle constraints total count: 68 | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 400 / Conformers submitted total number: 20 / Maximum distance constraint violation: 0.77 Å / Maximum torsion angle constraint violation: 5 ° / Representative conformer: 1 / Torsion angle constraint violation method: PSVS 1.5 | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble rms | Distance rms dev: 0.03 Å |