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- PDB-3epz: Structure of the replication foci-targeting sequence of human DNA... -

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Basic information

Entry
Database: PDB / ID: 3epz
TitleStructure of the replication foci-targeting sequence of human DNA cytosine methyltransferase DNMT1
ComponentsDNA (cytosine-5)-methyltransferase 1
KeywordsTRANSFERASE / WINGED HELIX DOMAIN / SH3-LIKE BARREL / CELL CYCLE / METAL BINDING / DNA BINDING / DNA REPLICATION / TRANSCRIPTIONAL SILENCING / CHROMATIN / PHOSPHORYLATION / TRANSCRIPTION / TRANSCRIPTION REGULATION / EPIGENETICS ZINC / ZINC-FINGER / Methyltransferase / Nucleus / Phosphoprotein / Repressor / S-adenosyl-L-methionine / STRUCTURAL GENOMICS / STRUCTURAL GENOMICS CONSORTIUM / SGC
Function / homology
Function and homology information


negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching / : / epigenetic programming of gene expression / cellular response to bisphenol A / negative regulation of vascular associated smooth muscle cell apoptotic process / DNA-methyltransferase activity / DNA (cytosine-5-)-methyltransferase / DNA (cytosine-5-)-methyltransferase activity / DNA methylation-dependent heterochromatin formation / SUMOylation of DNA methylation proteins ...negative regulation of vascular associated smooth muscle cell differentiation involved in phenotypic switching / : / epigenetic programming of gene expression / cellular response to bisphenol A / negative regulation of vascular associated smooth muscle cell apoptotic process / DNA-methyltransferase activity / DNA (cytosine-5-)-methyltransferase / DNA (cytosine-5-)-methyltransferase activity / DNA methylation-dependent heterochromatin formation / SUMOylation of DNA methylation proteins / negative regulation of gene expression via chromosomal CpG island methylation / female germ cell nucleus / methyl-CpG binding / pericentric heterochromatin / positive regulation of vascular associated smooth muscle cell proliferation / DNA methylation / replication fork / PRC2 methylates histones and DNA / Defective pyroptosis / promoter-specific chromatin binding / cellular response to amino acid stimulus / NoRC negatively regulates rRNA expression / negative regulation of gene expression / DNA-templated transcription / positive regulation of gene expression / negative regulation of transcription by RNA polymerase II / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus
Similarity search - Function
Arc Repressor Mutant, subunit A - #2230 / DNA (cytosine-5)-methyltransferase 1-like / DNA (cytosine-5)-methyltransferase 1, replication foci domain / Cytosine specific DNA methyltransferase replication foci domain / DMAP1-binding Domain / DMAP1-binding Domain / DMAP1-binding domain / DMAP1-binding domain profile. / DNA methylase, C-5 cytosine-specific, conserved site / C-5 cytosine-specific DNA methylases C-terminal signature. ...Arc Repressor Mutant, subunit A - #2230 / DNA (cytosine-5)-methyltransferase 1-like / DNA (cytosine-5)-methyltransferase 1, replication foci domain / Cytosine specific DNA methyltransferase replication foci domain / DMAP1-binding Domain / DMAP1-binding Domain / DMAP1-binding domain / DMAP1-binding domain profile. / DNA methylase, C-5 cytosine-specific, conserved site / C-5 cytosine-specific DNA methylases C-terminal signature. / DNA methylase, C-5 cytosine-specific, active site / C-5 cytosine-specific DNA methylases active site. / CXXC zinc finger domain / Zinc finger, CXXC-type / Zinc finger CXXC-type profile. / C-5 cytosine-specific DNA methylase (Dnmt) domain profile. / C-5 cytosine methyltransferase / C-5 cytosine-specific DNA methylase / Bromo adjacent homology (BAH) domain superfamily / Bromo adjacent homology domain / Bromo adjacent homology (BAH) domain / BAH domain / BAH domain profile. / Arc Repressor Mutant, subunit A / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
beta-D-glucopyranose / DNA (cytosine-5)-methyltransferase 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.31 Å
AuthorsWalker, J.R. / Avvakumov, G.V. / Xue, S. / Li, Y. / Bountra, C. / Weigelt, J. / Arrowsmith, C.H. / Edwards, A.M. / Bochkarev, A. / Dhe-Paganon, S. / Structural Genomics Consortium (SGC)
CitationJournal: J.Biol.Chem. / Year: 2011
Title: The replication focus targeting sequence (RFTS) domain is a DNA-competitive inhibitor of Dnmt1.
Authors: Syeda, F. / Fagan, R.L. / Wean, M. / Avvakumov, G.V. / Walker, J.R. / Xue, S. / Dhe-Paganon, S. / Brenner, C.
History
DepositionSep 30, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 25, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.2Sep 14, 2011Group: Database references
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA (cytosine-5)-methyltransferase 1
B: DNA (cytosine-5)-methyltransferase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,2567
Polymers60,8302
Non-polymers4265
Water1,63991
1
A: DNA (cytosine-5)-methyltransferase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,7765
Polymers30,4151
Non-polymers3614
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: DNA (cytosine-5)-methyltransferase 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)30,4812
Polymers30,4151
Non-polymers651
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)57.544, 59.768, 96.286
Angle α, β, γ (deg.)90.00, 92.31, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein / Sugars , 2 types, 3 molecules AB

#1: Protein DNA (cytosine-5)-methyltransferase 1 / Dnmt1 / MCMT / DNA methyltransferase HsaI / DNA MTase HsaI / M.HsaI / CXXC-type zinc finger protein 9


Mass: 30415.188 Da / Num. of mol.: 2 / Fragment: REPLICATION FOCI-TARGETING SEQUENCE
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AIM, CXX9, CXXC9, DNMT, DNMT1 / Plasmid: PET28-MHL / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3)
References: UniProt: P26358, DNA (cytosine-5-)-methyltransferase
#3: Sugar ChemComp-BGC / beta-D-glucopyranose / Glucose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DGlcpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-glucopyranoseCOMMON NAMEGMML 1.0
b-D-GlcpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 4 types, 95 molecules

#2: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 91 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.72 Å3/Da / Density % sol: 54.77 %
Description: DATA SET USED FOR PHASING WAS COLLECTED AT 0.97937
Crystal growTemperature: 298 K / pH: 6
Details: 23 % PEG 3350, 0.1 M BIS-TRIS PH 6.0,0.2 M SODIUM ACETATE, 0.005 M TCEP, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K, pH 6.00

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.0332
DetectorType: MARMOSAIC 300 MM CCD QUANTUM 315 / Detector: CCD / Date: Jul 27, 2008 / Details: MIRRORS
RadiationMonochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.3→50 Å / Num. obs: 28832 / % possible obs: 99.1 % / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Rsym value: 0.085 / Net I/σ(I): 16.6849
Reflection shellResolution: 2.3→2.38 Å / Redundancy: 3 % / Mean I/σ(I) obs: 1.3 / Rsym value: 0.979 / % possible all: 91.6

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Processing

Software
NameVersionClassification
HKL-2000data collection
SOLVEphasing
REFMAC5.5.0044refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 2.31→48.11 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.915 / SU B: 14.965 / SU ML: 0.17 / Cross valid method: THROUGHOUT / ESU R: 0.261 / ESU R Free: 0.224 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS, ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS.
RfactorNum. reflection% reflectionSelection details
Rfree0.26413 1473 5.1 %RANDOM
Rwork0.21299 ---
obs0.21559 27330 99.53 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 32.675 Å2
Baniso -1Baniso -2Baniso -3
1--0.64 Å20 Å2-0.51 Å2
2---1.19 Å20 Å2
3---1.79 Å2
Refinement stepCycle: LAST / Resolution: 2.31→48.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3438 0 21 91 3550
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.0223541
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.1541.9784808
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.6465440
X-RAY DIFFRACTIONr_dihedral_angle_2_deg38.69725.232151
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.68415553
X-RAY DIFFRACTIONr_dihedral_angle_4_deg24.8411510
X-RAY DIFFRACTIONr_chiral_restr0.0820.2541
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0212677
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.4111.52242
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.79223602
X-RAY DIFFRACTIONr_scbond_it1.36431299
X-RAY DIFFRACTIONr_scangle_it2.1164.51206
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.309→2.369 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.336 103 -
Rwork0.292 1908 -
obs--95.13 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
17.0691-0.73580.18358.79272.41467.924-0.1545-1.04540.14811.024-0.03610.1820.6037-0.82560.19060.1949-0.01190.01320.2729-0.02090.169832.950914.1056108.3979
24.185-0.06640.50273.2725-1.09639.54830.1067-0.8393-0.01470.5277-0.0543-0.215-0.17560.5637-0.05240.2419-0.0352-0.03890.2661-0.02790.284443.352116.0731108.0479
33.45542.66862.15093.70431.5641.3481-0.3119-0.18360.3956-0.24850.0373-0.1477-0.2185-0.12730.27460.1804-0.0284-0.00310.20420.04230.309945.993921.134587.6727
46.1225-3.3832-3.33775.94161.455111.528-0.22460.7828-0.1332-1.0847-0.0502-0.38260.12341.16310.27480.3738-0.15250.12250.4440.00820.323545.530718.168974.1829
51.9816-0.6104-0.43931.8561-0.05981.8439-0.04610.14470.0373-0.21740.0074-0.1333-0.0008-0.02480.03870.1591-0.02210.0080.20760.01130.231841.2339.562792.9594
64.59361.06970.77564.4925-0.18890.8156-0.14610.352-0.0665-0.31980.0267-0.27980.04250.07720.11940.2211-0.00130.00320.21830.00140.196740.10139.87389.8847
72.51740.6120.93523.8334-1.21962.31760.0110.1149-0.2239-0.37210.0091-0.32780.23810.2188-0.02010.163-0.00870.04280.22090.00440.208442.11195.896986.7175
82.00621.9835-0.1083.25490.81131.17040.03040.061-0.04810.0222-0.0546-0.18840.01920.06740.02420.13450.0454-0.01010.21120.0210.292543.7914-1.632996.097
92.41221.84180.65554.63990.71462.8041-0.06130.159-0.1698-0.2226-0.0256-0.27110.189-0.00460.08690.11010.04870.06480.1935-0.02720.292643.7172-14.710292.0284
104.69231.5781.32365.7001-2.76537.4989-0.1599-0.26960.2360.22970.19920.0218-0.0511-0.4565-0.03940.1978-0.01250.03460.1887-0.00910.245332.0416-12.217297.7869
114.1348-1.33751.68399.2944-3.43561.8577-0.12010.43110.3611-0.33610.04420.1211-0.0514-0.15650.07590.26140.03260.03120.42460.00620.256427.2504-12.174985.9291
122.2423-0.71322.38442.6396-2.92498.727-0.10890.1296-0.15930.01650.0919-0.08520.32920.09020.0170.1688-0.01970.01710.2113-0.01140.235130.2092-21.526199.1104
133.9467-3.5355-3.861811.98521.14238.1535-0.08080.0037-0.6055-0.4231-0.2473-0.56850.63440.66420.32810.25860.01850.00190.3006-0.04110.367336.1876-25.3605103.5648
145.7753-4.5068-4.01974.13861.44767.5056-0.2050.7164-0.72930.0758-0.43830.45520.543-0.90950.64330.5758-0.0571-0.20280.1546-0.04050.342421.26817.149441.5556
1512.3046-7.8753-1.14016.40160.13080.39610.40750.4149-0.61930.832-0.25441.0986-0.6007-0.0578-0.15321.1971-0.00650.23680.2508-0.00430.674312.00219.798441.567
164.71031.0307-2.06454.65040.4522.83930.32010.32490.25690.05050.02310.6668-0.7421-0.1033-0.34320.58980.14510.01050.15160.00610.241117.875838.41451.4452
171.0150.6832-2.12836.6919-0.13594.9864-0.16460.0715-0.0081-0.55590.2093-0.2238-0.0225-0.3132-0.04480.49340.0725-0.06880.21090.0350.044921.237820.318250.6407
184.2486-0.54920.32654.70832.20095.21810.0410.12760.0565-0.0481-0.110.8468-0.6953-0.64420.06910.49320.1072-0.08020.12050.04390.235514.752233.866153.8113
191.24471.58780.65588.8241-2.42542.0510.0846-0.2537-0.06790.41870.24510.5968-0.3493-0.4224-0.32970.51780.1117-0.07120.16990.0270.10319.333829.027760.9658
201.40460.03780.56798.345-5.67996.02560.0447-0.08860.0878-0.38640.37180.82250.1033-1.0594-0.41660.3328-0.01-0.18130.34440.01630.154510.806718.709356.5103
214.74591.72720.66452.208-1.04429.8671-0.0266-0.11360.0764-0.2268-0.13780.3695-0.1046-0.3150.16440.23850.0283-0.01040.24650.00440.226519.770418.960169.4394
224.3050.7685-0.30590.9502-0.85424.66720.02360.13550.3010.0747-0.01950.3833-0.6168-0.4167-0.0040.1920.0796-0.00470.2777-0.00140.195618.242620.315679.1862
230.9101-1.2447-2.75581.7353.87078.6640.37370.5852-0.2213-0.3396-0.86720.2178-0.7104-2.26770.49340.1669-0.0438-0.19621.1560.26940.27569.491414.578169.885
245.33221.36161.60196.0618-0.19576.79230.13580.3328-0.0058-0.3541-0.0813-0.36990.33840.1902-0.05450.25570.04930.00260.25560.07350.102526.256413.283570.2494
258.3536-1.19311.33995.7538-1.77643.6248-0.46360.26760.2396-0.45550.4912-0.2021-0.492-0.2994-0.02760.2169-0.0384-0.00260.2650.0070.14530.213916.7879.4043
266.6141.1383-2.57656.0076-2.5631.7779-0.0441.02460.1108-0.79630.0671-0.03170.3161-0.3454-0.0230.24310.06770.04130.32150.01570.336732.96724.961974.7169
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A350 - 359
2X-RAY DIFFRACTION2A360 - 369
3X-RAY DIFFRACTION3A370 - 378
4X-RAY DIFFRACTION4A379 - 390
5X-RAY DIFFRACTION5A401 - 427
6X-RAY DIFFRACTION6A428 - 447
7X-RAY DIFFRACTION7A451 - 488
8X-RAY DIFFRACTION8A489 - 515
9X-RAY DIFFRACTION9A516 - 549
10X-RAY DIFFRACTION10A550 - 563
11X-RAY DIFFRACTION11A564 - 581
12X-RAY DIFFRACTION12A582 - 592
13X-RAY DIFFRACTION13A593 - 599
14X-RAY DIFFRACTION14B342 - 360
15X-RAY DIFFRACTION15B361 - 372
16X-RAY DIFFRACTION16B373 - 408
17X-RAY DIFFRACTION17B409 - 435
18X-RAY DIFFRACTION18B436 - 463
19X-RAY DIFFRACTION19B464 - 488
20X-RAY DIFFRACTION20B489 - 505
21X-RAY DIFFRACTION21B506 - 514
22X-RAY DIFFRACTION22B515 - 536
23X-RAY DIFFRACTION23B537 - 548
24X-RAY DIFFRACTION24B549 - 568
25X-RAY DIFFRACTION25B569 - 587
26X-RAY DIFFRACTION26B588 - 597

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External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

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Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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