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- PDB-5bq2: Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransf... -

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Basic information

Entry
Database: PDB / ID: 5bq2
TitleCrystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (UDP-N-acetylglucosamine enolpyruvyl transferase, EPT) from Pseudomonas aeruginosa
ComponentsUDP-N-acetylglucosamine 1-carboxyvinyltransferase
KeywordsTRANSFERASE / SSGCID / UDP-N-acetylglucosamine 1-carboxyvinyltransferase / UDP-N-acetylglucosamine enolpyruvyl transferase / Enoylpyruvate transferase / EPT / murA / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease
Function / homology
Function and homology information


UDP-N-acetylglucosamine 1-carboxyvinyltransferase / UDP-N-acetylglucosamine 1-carboxyvinyltransferase activity / UDP-N-acetylgalactosamine biosynthetic process / peptidoglycan biosynthetic process / cell wall organization / regulation of cell shape / cell cycle / cell division / cytoplasm
Similarity search - Function
UDP-N-acetylglucosamine 1-carboxyvinyltransferase / Enolpyruvate transferase domain / Alpha-beta prism / UDP-n-acetylglucosamine1-carboxyvinyl-transferase; Chain / Enolpyruvate transferase domain / Enolpyruvate transferase domain superfamily / EPSP synthase (3-phosphoshikimate 1-carboxyvinyltransferase) / RNA 3'-terminal phosphate cyclase/enolpyruvate transferase, alpha/beta / Alpha Beta
Similarity search - Domain/homology
Chem-EPU / UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Similarity search - Component
Biological speciesPseudomonas aeruginosa PAO1 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.7 Å
AuthorsSSGCID / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: to be published
Title: Crystal structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase (UDP-N-acetylglucosamine enolpyruvyl transferase, EPT) from Pseudomonas aeruginosa
Authors: Abendroth, J. / Dranow, D.M. / Lorimer, D.D. / Edwards, T.E.
History
DepositionMay 28, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 15, 2015Provider: repository / Type: Initial release
Revision 1.1Sep 27, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Refinement description / Source and taxonomy
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / entity_src_gen / pdbx_initial_refinement_model / pdbx_prerelease_seq / pdbx_struct_conn_angle / pdbx_struct_oper_list / pdbx_validate_close_contact / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_src_gen.pdbx_alt_source_flag / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_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_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_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 / _pdbx_struct_oper_list.symmetry_operation / _struct_conn.conn_type_id / _struct_conn.id / _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
Revision 1.2Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
B: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
C: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
D: UDP-N-acetylglucosamine 1-carboxyvinyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)186,42214
Polymers183,5674
Non-polymers2,85510
Water36,8952048
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15090 Å2
ΔGint-82 kcal/mol
Surface area52500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)130.170, 166.810, 81.450
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein
UDP-N-acetylglucosamine 1-carboxyvinyltransferase / / Enoylpyruvate transferase / UDP-N-acetylglucosamine enolpyruvyl transferase / EPT


Mass: 45891.738 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria) / Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228 / Gene: murA, PA4450 / Plasmid: PsaeA.00952.a.B1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q9HVW7, UDP-N-acetylglucosamine 1-carboxyvinyltransferase
#2: Chemical
ChemComp-EPU / URIDINE-DIPHOSPHATE-2(N-ACETYLGLUCOSAMINYL) BUTYRIC ACID / ENOLPYRUVYL-URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE


Mass: 677.400 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C20H29N3O19P2
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 2048 / 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: 2.42 Å3/Da / Density % sol: 49 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop
Details: Microlytics MCSG1 A11: 10% PEG 4000, 200mM MgCl2, 100mM MES/NaOH pH 6.5, PsaeA.00952.a.B1.PS02212 at 17mg/ml + 3mM UDP-N-acetylglucosamine + 3mM phosphoenolpyruvate, cryo: 20% EG in 2 steps; ...Details: Microlytics MCSG1 A11: 10% PEG 4000, 200mM MgCl2, 100mM MES/NaOH pH 6.5, PsaeA.00952.a.B1.PS02212 at 17mg/ml + 3mM UDP-N-acetylglucosamine + 3mM phosphoenolpyruvate, cryo: 20% EG in 2 steps; tray 260011a11, puck fvw9-7

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: Apr 2, 2015
RadiationMonochromator: Diamond [111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 1.7→50 Å / Num. all: 194666 / Num. obs: 193295 / % possible obs: 99.3 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Biso Wilson estimate: 13 Å2 / Rmerge F obs: 0.997 / Rmerge(I) obs: 0.083 / Rrim(I) all: 0.095 / Χ2: 0.983 / Net I/σ(I): 12.07 / Num. measured all: 780951
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Highest resolution (Å)Redundancy (%)Rmerge F obsRmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible all
1.7-1.744.10.8210.4592.885869814261142250.52699.7
1.74-1.790.8760.3733.525717013888138610.42899.8
1.79-1.840.9030.3264.065589613543135000.37399.7
1.84-1.90.9340.2635.085393813131130810.30299.6
1.9-1.960.9510.226.115219512772127000.25399.4
1.96-2.030.9650.1837.425030112360122840.2199.4
2.03-2.110.9750.1538.784815211900118230.17699.4
2.11-2.190.9810.12810.334616111508114520.14799.5
2.19-2.290.9850.11511.424411211052109630.13399.2
2.29-2.40.9890.09713.244177610545104800.11199.4
2.4-2.530.9910.08914.26398631003099690.10299.4
2.53-2.690.9920.07915.6337795952294880.09199.6
2.69-2.870.9940.06717.7935215894989130.07799.6
2.87-3.10.9960.05919.8832994839083470.06899.5
3.1-3.40.9970.04922.8530035772676630.05799.2
3.4-3.80.9970.04325.6727127699469300.0599.1
3.8-4.390.9980.03827.5423910621861370.04398.7
4.39-5.380.9980.03528.5920476530052370.0498.8
5.38-7.60.9990.03227.7916440417240570.03797.2
7.60.9990.02430.588697240521850.02890.9

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation6.67 Å43.41 Å
Translation6.67 Å43.41 Å

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Processing

Software
NameClassification
XDSdata reduction
XSCALEdata scaling
PHASERphasing
ARPmodel building
Cootmodel building
PHENIXrefinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3vcy modified with CCP4 program CHAINSAW
Resolution: 1.7→43.414 Å / SU ML: 0.15 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 17.25 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1809 9570 4.95 %Random selection
Rwork0.1484 183696 --
obs0.1501 193266 99.29 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 60.33 Å2 / Biso mean: 17.1776 Å2 / Biso min: 4.87 Å2
Refinement stepCycle: final / Resolution: 1.7→43.414 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12630 0 182 2060 14872
Biso mean--11.66 28.41 -
Num. residues----1700
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00813353
X-RAY DIFFRACTIONf_angle_d1.16918234
X-RAY DIFFRACTIONf_chiral_restr0.0512158
X-RAY DIFFRACTIONf_plane_restr0.0062379
X-RAY DIFFRACTIONf_dihedral_angle_d12.68101
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.7-1.71930.23043020.19746089X-RAY DIFFRACTION100
1.7193-1.73960.23123250.1966081X-RAY DIFFRACTION100
1.7396-1.76080.23742910.18266095X-RAY DIFFRACTION100
1.7608-1.78310.20383270.1826150X-RAY DIFFRACTION100
1.7831-1.80650.22343250.18026081X-RAY DIFFRACTION100
1.8065-1.83130.21762960.17926072X-RAY DIFFRACTION100
1.8313-1.85750.24563220.17786124X-RAY DIFFRACTION99
1.8575-1.88520.21262960.17246056X-RAY DIFFRACTION100
1.8852-1.91460.20763180.17176112X-RAY DIFFRACTION100
1.9146-1.9460.21513190.16576092X-RAY DIFFRACTION99
1.946-1.97960.18643040.16116088X-RAY DIFFRACTION99
1.9796-2.01560.18943250.15236069X-RAY DIFFRACTION99
2.0156-2.05430.18563440.14956057X-RAY DIFFRACTION99
2.0543-2.09630.19282940.15116145X-RAY DIFFRACTION99
2.0963-2.14190.18553160.15426122X-RAY DIFFRACTION100
2.1419-2.19170.21142980.1486099X-RAY DIFFRACTION99
2.1917-2.24650.18752990.14716117X-RAY DIFFRACTION99
2.2465-2.30720.19853070.1466085X-RAY DIFFRACTION99
2.3072-2.37510.18673300.14036118X-RAY DIFFRACTION99
2.3751-2.45180.17173340.14376099X-RAY DIFFRACTION99
2.4518-2.53940.19373300.14596131X-RAY DIFFRACTION99
2.5394-2.6410.17913470.14986137X-RAY DIFFRACTION100
2.641-2.76120.19183240.14736107X-RAY DIFFRACTION100
2.7612-2.90680.16923170.14526222X-RAY DIFFRACTION100
2.9068-3.08880.17453280.15046112X-RAY DIFFRACTION99
3.0888-3.32730.17983030.14236209X-RAY DIFFRACTION99
3.3273-3.66190.15673420.13256161X-RAY DIFFRACTION99
3.6619-4.19150.14323380.1236182X-RAY DIFFRACTION99
4.1915-5.27930.13573320.12276240X-RAY DIFFRACTION99
5.2793-500.16823370.15116244X-RAY DIFFRACTION95
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)
11.52840.10550.68080.6957-0.03572.10250.0263-0.0456-0.15480.017-0.027-0.04830.23810.07750.02490.10830.02390.00420.04710.00120.1128-72.493615.7328110.1793
21.82660.67660.48141.27780.25051.7652-0.02570.0217-0.2474-0.0521-0.0193-0.00020.2266-0.03350.0460.1181-0.00580.00580.0531-0.01110.095-92.511213.819597.3597
32.0204-0.13670.10940.8244-0.09380.7853-0.05750.0932-0.1742-0.06070.00250.06250.213-0.21060.0480.1227-0.04580.00160.1107-0.010.0837-102.354815.9561100.7558
41.7601-0.11960.35311.3088-0.75312.0793-0.0426-0.03520.1098-0.01680.0580.11-0.039-0.3193-0.01110.06590.00420.01230.1202-0.00380.081-106.670426.4107.0282
52.22570.6160.47231.5422-0.19471.5257-0.04840.07220.2889-0.08510.02140.2156-0.1044-0.27370.06670.07880.0061-0.01420.1110.00940.1106-102.229233.943895.7859
61.98460.17691.10890.2334-0.02641.5266-0.01960.1581-0.0383-0.07010.022-0.00610.03160.00570.00320.089-0.01150.00480.0710.00570.0568-84.837727.394194.2589
71.8744-0.05620.2340.74420.21081.5606-0.0280.14060.1458-0.03750.0241-0.1561-0.13760.2132-0.00060.0982-0.0356-0.00960.08820.02110.1063-70.441335.7516105.1648
80.95930.03590.60271.5073-0.02651.186-0.0503-0.1106-0.00230.10360.0331-0.0275-0.0433-0.01820.01810.06490.0060.00870.07840.00890.0622-77.372928.2025119.7603
93.25110.41930.04492.8554-0.50992.1929-0.0101-0.0035-0.5392-0.0112-0.0458-0.05980.22840.0760.06340.10620.0251-0.00040.07620.01070.1253-71.926313.0987111.0548
101.4919-0.18370.29050.99020.47932.03020.0281-0.0557-0.16220.0077-0.050.04670.1333-0.12660.0470.0721-0.02290.00410.04730.02190.1029-109.993316.6379136.163
110.9233-0.23630.12540.40470.24571.0309-0.0279-0.1749-0.20150.1493-0.0287-0.0680.13760.1720.03860.13790.0041-0.02110.13540.05520.1208-86.068616.3693147.6163
121.45520.43370.6411.12210.85192.15530.01040.05520.09240.02440.0246-0.1391-0.03840.3172-0.030.0894-0.0189-0.00140.17130.03180.1181-76.021327.5612138.5038
131.5448-0.26670.3241.00370.31731.19270.024-0.0880.1480.0958-0.0533-0.1449-0.09380.18870.03540.1146-0.0499-0.02870.13810.02110.0951-83.580934.7337151.5281
141.38230.27080.72650.68860.19030.9740.0614-0.1752-0.0740.1301-0.0316-0.06880.01910.0444-0.03690.0997-0.0086-0.00290.10590.00870.0574-96.288427.4988150.9535
151.41360.1820.26510.7564-0.05411.4661-0.0261-0.10720.13450.0196-0.01010.0506-0.1647-0.12550.02310.09620.0147-0.00530.0564-0.00890.0786-109.376635.0008137.299
160.79140.09710.29620.95570.0120.868-0.02670.06120.0339-0.09710.02090.012-0.06860.0650.00420.0758-0.00690.0080.0523-0.00460.0612-105.734125.1982124.2604
172.9195-1.6734-0.89842.87940.8581.77450.0047-0.0678-0.39290.1324-0.09440.02180.2274-0.06950.10930.0993-0.01830.00240.06260.02050.1056-110.535613.9111135.5535
181.69370.4994-0.92190.5225-0.41971.35770.1058-0.13490.20360.1244-0.0321-0.0546-0.25870.1139-0.07580.1551-0.0201-0.01220.0828-0.03780.1444-85.448371.5804142.8719
191.5714-0.84190.08710.8178-0.57641.1478-0.0252-0.1560.34680.1174-0.0255-0.0532-0.2309-0.050.08470.2136-0.00590.00390.0971-0.03770.1961-97.065977.6615144.2432
201.58860.27260.24950.8511-0.36391.1585-0.0092-0.18150.24990.14140.04630.0458-0.2278-0.1526-0.03820.1190.02090.01590.1-0.03080.1272-105.810171.4614141.2294
212.33360.4176-0.75991.2392-0.82281.82750.01260.0365-0.0123-0.03330.09530.0843-0.0144-0.1873-0.09410.0593-0.0072-0.00980.0914-0.00910.0753-108.859861.2294134.4035
221.9348-0.25890.03390.997-0.27311.19510.0002-0.134-0.13470.07560.03980.10680.036-0.1989-0.0270.0824-0.01440.0040.0958-0.00060.0832-103.965154.7947148.8012
231.3617-0.0444-0.62190.4698-0.14521.3013-0.0354-0.1521-0.02770.0686-0.0138-0.0938-0.00080.17870.04550.0887-0.0055-0.0110.0778-0.00850.0865-79.91456.4527142.4718
241.1238-0.3088-0.56081.4238-0.00840.90740.02640.08310.0602-0.1331-0.0166-0.1052-0.00620.0489-0.00770.0746-0.01920.00060.0853-0.00250.0854-77.198463.0175125.5538
254.18080.3912-0.23952.73140.38532.2710.1181-0.21920.49450.0991-0.0896-0.0737-0.40620.37110.04060.1411-0.0682-0.00240.1571-0.01970.1628-74.47875.1386136.8205
261.1004-0.0985-0.40420.33490.20.58470.07220.10120.2432-0.1202-0.0046-0.0087-0.17340.022-0.06050.1655-0.00990.01780.08480.0440.1428-87.512571.571199.8688
272.1558-0.6546-1.02920.97730.95491.75110.0111-0.14930.03960.0110.1072-0.0438-0.02520.271-0.11080.0737-0.0128-0.00870.10660.01110.0799-73.3960.3774108.8277
282.64440.2297-0.66221.43320.31051.4201-0.0533-0.0122-0.1086-0.00710.0522-0.07110.07030.16740.01170.06530.0026-0.00510.07730.00950.0586-75.736352.009297.1923
291.689-0.0995-0.81970.34490.31090.8370.10560.30850.0863-0.1229-0.05130.0195-0.1337-0.1331-0.05110.12460.0131-0.01340.10840.02760.0656-92.846158.766192.3796
302.1588-0.0327-0.69661.01130.15061.696-0.00140.2799-0.179-0.1536-0.07040.19980.0852-0.29680.04880.1177-0.0133-0.02510.1204-0.02740.1379-108.826251.2722101.0967
311.3058-0.2349-0.43591.38360.07020.83070.0065-0.00230.03320.0315-0.02030.02880.0051-0.03880.00970.0666-0.0078-0.00720.05490.00620.0734-104.923662.449114.2432
322.077-0.59910.23641.8458-0.02241.1477-0.0244-0.11950.04780.12960.02620.0539-0.0202-0.09840.00610.10990.00650.01080.11280.00720.0977-93.429230.7522107.958
331.85760.4391-0.4851.6427-0.73691.286-0.03370.15510.0267-0.26390.0023-0.1234-0.16110.15390.03380.1551-0.02810.0080.15860.00880.0974-89.105231.8213137.3808
340.9269-0.04490.33341.41520.72560.9790.01550.0573-0.0924-0.12450.0856-0.0223-0.045-0.0399-0.10080.1089-0.0101-0.01340.0927-0.00130.1075-95.614457.2276136.0242
352.0672-0.12720.49930.8459-0.45680.88010.01-0.044-0.04760.05920.0680.0642-0.07380.0359-0.09290.1247-0.00550.00170.07240.00330.1187-86.822756.2075107.4786
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid -3 through 21 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 22 through 71 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 72 through 106 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 107 through 148 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 149 through 191 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 192 through 262 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 263 through 306 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 307 through 401 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 402 through 421 )A0
10X-RAY DIFFRACTION10chain 'B' and (resid -3 through 21 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 22 through 106 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 107 through 148 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 149 through 214 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 215 through 247 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 248 through 335 )B0
16X-RAY DIFFRACTION16chain 'B' and (resid 336 through 401 )B0
17X-RAY DIFFRACTION17chain 'B' and (resid 402 through 421 )B0
18X-RAY DIFFRACTION18chain 'C' and (resid -3 through 47 )C0
19X-RAY DIFFRACTION19chain 'C' and (resid 48 through 71 )C0
20X-RAY DIFFRACTION20chain 'C' and (resid 72 through 106 )C0
21X-RAY DIFFRACTION21chain 'C' and (resid 107 through 148 )C0
22X-RAY DIFFRACTION22chain 'C' and (resid 149 through 214 )C0
23X-RAY DIFFRACTION23chain 'C' and (resid 215 through 335 )C0
24X-RAY DIFFRACTION24chain 'C' and (resid 336 through 401 )C0
25X-RAY DIFFRACTION25chain 'C' and (resid 402 through 421 )C0
26X-RAY DIFFRACTION26chain 'D' and (resid -3 through 106 )D0
27X-RAY DIFFRACTION27chain 'D' and (resid 107 through 148 )D0
28X-RAY DIFFRACTION28chain 'D' and (resid 149 through 191 )D0
29X-RAY DIFFRACTION29chain 'D' and (resid 192 through 262 )D0
30X-RAY DIFFRACTION30chain 'D' and (resid 263 through 306 )D0
31X-RAY DIFFRACTION31chain 'D' and (resid 307 through 421 )D0
32X-RAY DIFFRACTION32chain 'A' and resid 500A500
33X-RAY DIFFRACTION33chain 'B' and resid 500B500
34X-RAY DIFFRACTION34chain 'C' and resid 500C500
35X-RAY DIFFRACTION35chain 'D' and resid 500D500

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