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- PDB-4ndz: Structure of Maltose Binding Protein fusion to 2-O-Sulfotransfera... -

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Basic information

Entry
Database: PDB / ID: 4ndz
TitleStructure of Maltose Binding Protein fusion to 2-O-Sulfotransferase with bound heptasaccharide and PAP
ComponentsMaltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
KeywordsTRANSPORT PROTEIN/TRANSFERASE / heparan sulfate / fusion / TRANSPORT PROTEIN-TRANSFERASE complex
Function / homology
Function and homology information


heparan sulfate 2-O-sulfotransferase activity / HS-GAG biosynthesis / Transferases; Transferring sulfur-containing groups; Sulfotransferases / ureteric bud formation / heparan sulfate proteoglycan biosynthetic process, enzymatic modification / heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process / heparin metabolic process / detection of maltose stimulus / maltose binding / maltose transport complex ...heparan sulfate 2-O-sulfotransferase activity / HS-GAG biosynthesis / Transferases; Transferring sulfur-containing groups; Sulfotransferases / ureteric bud formation / heparan sulfate proteoglycan biosynthetic process, enzymatic modification / heparan sulfate proteoglycan biosynthetic process, polysaccharide chain biosynthetic process / heparin metabolic process / detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / gene expression / outer membrane-bounded periplasmic space / periplasmic space / Golgi membrane / DNA damage response / membrane / identical protein binding
Similarity search - Function
Heparan sulphate 2-O-sulfotransferase / Sulfotransferase / Sulfotransferase family / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase ...Heparan sulphate 2-O-sulfotransferase / Sulfotransferase / Sulfotransferase family / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
alpha-maltose / ADENOSINE-3'-5'-DIPHOSPHATE / P-NITROPHENOL / Maltose/maltodextrin-binding periplasmic protein / Heparan sulfate 2-O-sulfotransferase 1
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Gallus gallus (chicken)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.45 Å
AuthorsLiu, C. / Sheng, J. / Krahn, J.M. / Perera, L. / Xu, Y. / Hsieh, P. / Liu, J. / Pedersen, L.C.
CitationJournal: To be Published
Title: Deciphering the role of 2-O-sulfotransferase in regulating heparan sulfate biosynthesis
Authors: Liu, C. / Sheng, J. / Krahn, J.M. / Perera, L. / Xu, Y. / Hsieh, P. / Liu, J. / Pedersen, L.C.
History
DepositionOct 28, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 19, 2014Provider: repository / Type: Initial release
Revision 1.1Aug 16, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.occupancy / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _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.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_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
B: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
C: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
D: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
E: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
F: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
hetero molecules


Theoretical massNumber of molelcules
Total (without water)458,28726
Polymers446,4156
Non-polymers11,87220
Water0
1
A: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
B: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
C: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
hetero molecules


Theoretical massNumber of molelcules
Total (without water)228,26812
Polymers223,2073
Non-polymers5,0619
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21150 Å2
ΔGint10 kcal/mol
Surface area61690 Å2
MethodPISA
2
D: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
E: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
F: Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion
hetero molecules


Theoretical massNumber of molelcules
Total (without water)230,01914
Polymers223,2073
Non-polymers6,81111
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25420 Å2
ΔGint32 kcal/mol
Surface area73240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)155.720, 170.690, 183.960
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
12
22
32
13
23
33
43
53
14
24
34
15
25
16
26
36
46
56

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111(chain B and (resid 1072:1335 or resid 1339:1355) and not...
211(chain A and (resid 1072:1335 or resid 1339:1355) ) or...
311(chain C and (resid 1072:1335 or resid 1339:1355) ) or (chain C and resName A3P)
411(chain D and (resid 1072:1335 or resid 1339:1355) ) or...
511(chain E and (resid 1072:1335 or resid 1339:1355) ) or...
611(chain F and (resid 1072:1335 or resid 1339:1355) ) or...
112(chain C and resid 1352:1355)
212(chain D and resid 1352:1355)
312(chain E and resid 1352:1355)
113chain B and resid 3001:3002 and not (name C8 or name C7 or name O7)
213chain A and resid 3001:3002 and not (name C8 or name C7 or name O7)
313chain D and resid 3001:3002 and not (name C8 or name C7 or name O7)
413chain E and resid 3001:3002 and not (name C8 or name C7 or name O7)
513chain F and resid 3001:3002 and not (name C8 or name C7 or name O7)
114chain B and resid 3003:3006
214chain A and resid 3003:3006
314chain D and resid 3003:3006
115chain E and resid 3003:3006
215chain F and resid 3003:3006
116(chain D and (resid 1:169 or resid 180:367) and not...
216(chain B and (resid 1:41 or resid 58:169 or resid 180:367) ) or (chain B and resName GLC)
316(chain C and (resid 1:169 or resid 180:367) ) or (chain C and resName GLC)
416(chain E and (resid 1:169 or resid 180:367) ) or (chain E and resName GLC)
516(chain F and (resid 1:169 or resid 180:367) ) or (chain F and resName GLC)

NCS ensembles :
ID
1
2
3
4
5
6

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Components

#1: Protein
Maltose-binding periplasmic protein, Heparan sulfate 2-O-sulfotransferase 1 fusion


Mass: 74402.477 Da / Num. of mol.: 6 / Mutation: E359A, K362A, D363A, R367N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli), (gene. exp.) Gallus gallus (chicken)
Strain: UMEA 3304-1 / Gene: G962_03763, HS2ST1, HS2ST / Production host: Escherichia coli (E. coli)
References: UniProt: P0AEX9, UniProt: Q76KB1, Transferases; Transferring sulfur-containing groups; Sulfotransferases
#2: Polysaccharide
beta-D-glucopyranuronic acid-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-beta-D- ...beta-D-glucopyranuronic acid-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranuronic acid-(1-4)-2-deoxy-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-beta-D-glucopyranuronic acid


Type: oligosaccharide / Mass: 1408.141 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpAb1-4DGlcpNAca1-4DGlcpAb1-4DGlcpNSa1-4LIdopAa1-4DGlcpNSa1-4DGlcpAb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/4,7,6/[a2122A-1b_1-5][a2122h-1a_1-5_2*NSO/3=O/3=O][a2121A-1a_1-5][a2122h-1a_1-5_2*NCC/3=O]/1-2-3-2-1-4-1/a4-b1_b4-c1_c4-d1_d4-e1_e4-f1_f4-g1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpA]{[(4+1)][a-D-GlcpNSO3]{[(4+1)][a-L-IdopA]{[(4+1)][a-D-GlcpNSO3]{[(4+1)][b-D-GlcpA]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpA]{}}}}}}}LINUCSPDB-CARE
#3: Polysaccharide
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#4: Chemical
ChemComp-A3P / ADENOSINE-3'-5'-DIPHOSPHATE / cHS2ST / Adenosine 3',5'-bisphosphate


Type: RNA linking / Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H15N5O10P2
#5: Chemical
ChemComp-NPO / P-NITROPHENOL / 4-Nitrophenol


Mass: 139.109 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H5NO3

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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: 2.73 Å3/Da / Density % sol: 55 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 5.6
Details: 17.9% PEG 4000, 60mM sodium citrate, 120mM ammonium acetate, 10.5% glycerol, 10mM hexamine cobalt chloride, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 5, 2012
RadiationMonochromator: SAGITALLY FOCUSED Si220 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.45→50 Å / Num. all: 64322 / Num. obs: 64322 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 6 % / Rsym value: 0.107
Reflection shellResolution: 3.45→3.51 Å / Redundancy: 5.6 % / Mean I/σ(I) obs: 2.3 / Rsym value: 0.638 / % possible all: 93.8

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Processing

Software
NameVersionClassification
SERGUIdata collection
PHASERphasing
PHENIXmodel building
PHENIX(phenix.refine: 1.8.2_1309)refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3F5F
Resolution: 3.45→49.661 Å / SU ML: 0.41 / σ(F): 1.34 / Phase error: 23.43 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2275 1959 3.05 %
Rwork0.1759 --
obs0.1775 64165 98.52 %
all-64322 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.45→49.661 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27976 0 778 0 28754
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00529548
X-RAY DIFFRACTIONf_angle_d0.84140243
X-RAY DIFFRACTIONf_dihedral_angle_d11.15710768
X-RAY DIFFRACTIONf_chiral_restr0.0544451
X-RAY DIFFRACTIONf_plane_restr0.0035085
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11B2272X-RAY DIFFRACTIONPOSITIONAL
12A2272X-RAY DIFFRACTIONPOSITIONAL0.07
13C2239X-RAY DIFFRACTIONPOSITIONAL0.082
14D2272X-RAY DIFFRACTIONPOSITIONAL0.067
15E2252X-RAY DIFFRACTIONPOSITIONAL0.076
16F2250X-RAY DIFFRACTIONPOSITIONAL0.081
21C30X-RAY DIFFRACTIONPOSITIONAL
22D30X-RAY DIFFRACTIONPOSITIONAL0.034
23E30X-RAY DIFFRACTIONPOSITIONAL0.031
31B23X-RAY DIFFRACTIONPOSITIONAL
32A23X-RAY DIFFRACTIONPOSITIONAL0.201
33D23X-RAY DIFFRACTIONPOSITIONAL0.182
34E23X-RAY DIFFRACTIONPOSITIONAL0.157
35F23X-RAY DIFFRACTIONPOSITIONAL0.206
41B54X-RAY DIFFRACTIONPOSITIONAL
42A54X-RAY DIFFRACTIONPOSITIONAL0.075
43D54X-RAY DIFFRACTIONPOSITIONAL0.069
51E54X-RAY DIFFRACTIONPOSITIONAL
52F54X-RAY DIFFRACTIONPOSITIONAL0.197
61D2532X-RAY DIFFRACTIONPOSITIONAL
62B2532X-RAY DIFFRACTIONPOSITIONAL0.042
63C2635X-RAY DIFFRACTIONPOSITIONAL0.061
64E2635X-RAY DIFFRACTIONPOSITIONAL0.061
65F2635X-RAY DIFFRACTIONPOSITIONAL0.045
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.45-3.53620.37311200.2733911X-RAY DIFFRACTION88
3.5362-3.63180.27751380.23854339X-RAY DIFFRACTION98
3.6318-3.73870.29711360.21674396X-RAY DIFFRACTION99
3.7387-3.85930.26891420.19734441X-RAY DIFFRACTION100
3.8593-3.99720.23231410.1854491X-RAY DIFFRACTION100
3.9972-4.15710.23471420.17854456X-RAY DIFFRACTION100
4.1571-4.34620.2291440.16684470X-RAY DIFFRACTION100
4.3462-4.57520.20451430.14614475X-RAY DIFFRACTION100
4.5752-4.86160.18911450.13554496X-RAY DIFFRACTION100
4.8616-5.23660.20331340.13594511X-RAY DIFFRACTION100
5.2366-5.76290.19791480.15094504X-RAY DIFFRACTION100
5.7629-6.59520.22721380.17664565X-RAY DIFFRACTION100
6.5952-8.30290.21331440.18544582X-RAY DIFFRACTION100
8.3029-49.66630.22041440.18434569X-RAY DIFFRACTION96
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)
11.0365-0.041-0.51290.1757-0.02880.37560.12590.2003-0.5525-0.55-0.4916-0.29480.40270.4153-02.96060.26710.17812.41090.39071.894722.677435.0942.6856
21.13260.4670.84271.2115-0.08391.3927-0.97450.32640.6326-0.17720.04590.4354-0.7161-0.5246-0.92370.9730.525-0.55541.189-0.27490.9937-17.393541.153129.9137
30.78750.3444-0.59530.7354-0.38860.7885-0.0340.3898-0.36530.36380.25530.69030.6996-0.05590.02941.3233-0.36040.20150.8539-0.0261.5983-12.6851-8.395996.4001
40.9446-0.7362-0.29151.3547-1.35471.8387-0.2113-0.0797-0.22731.32760.26030.5002-0.6058-0.19630.03571.41860.14480.47530.61370.12120.6989-22.452838.7102114.8551
50.8904-0.38620.6880.69310.31960.6613-0.4113-1.1751-0.48620.25220.1723-0.29480.5546-0.057402.60980.36820.24042.16140.45461.383722.01318.675139.5139
62.212-0.3071-0.42772.15710.45051.1344-0.17050.0878-0.151-0.4041-0.1423-0.1110.0405-0.2191-0.02140.52440.00380.12630.5318-0.08710.488111.0772-12.982718.0748
70.7238-0.3395-0.22311.42440.45432.1688-0.0532-0.2050.24770.06810.0892-0.268-0.1248-0.072900.43660.1131-0.05550.6961-0.17370.658417.363210.853444.5076
80.87990.3523-0.2591.88870.55571.4139-0.0983-0.24140.04540.2082-0.3250.40780.0201-0.5883-0.08080.37110.02460.12991.1005-0.26640.7219-13.9887-5.269542.817
90.6706-0.92430.44322.10450.33171.75770.1840.2358-0.146-0.1762-0.33360.3033-0.2971-0.3041-0.0010.49090.1032-0.10510.6322-0.09630.55996.824933.413177.8741
102.0685-1.44320.272.7715-0.47340.1709-0.4293-0.27250.44120.87890.2923-0.4548-0.3286-0.1581-0.01720.89790.0571-0.28880.4382-0.14820.572925.681343.5642106.7297
111.755-1.07050.16371.06490.11282.4560.06190.0406-0.43880.35520.02540.04640.3923-0.0546-0.01660.6336-0.0254-0.14360.3651-0.00630.73927.08899.364995.8343
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN B AND ( RESID 1:370 OR RESID 2001:2002 ) )B1 - 370
2X-RAY DIFFRACTION1( CHAIN B AND ( RESID 1:370 OR RESID 2001:2002 ) )B2001 - 2002
3X-RAY DIFFRACTION2( CHAIN C AND ( RESID 1:370 OR RESID 2001:2002 ) )C1 - 370
4X-RAY DIFFRACTION2( CHAIN C AND ( RESID 1:370 OR RESID 2001:2002 ) )C2001 - 2002
5X-RAY DIFFRACTION3( CHAIN D AND ( RESID 1:370 OR RESID 2001:2002 ) )D1 - 370
6X-RAY DIFFRACTION3( CHAIN D AND ( RESID 1:370 OR RESID 2001:2002 ) )D2001 - 2002
7X-RAY DIFFRACTION4( CHAIN E AND ( RESID 1:370 OR RESID 2001:2002 ) )E1 - 370
8X-RAY DIFFRACTION4( CHAIN E AND ( RESID 1:370 OR RESID 2001:2002 ) )E2001 - 2002
9X-RAY DIFFRACTION5( CHAIN F AND ( RESID 1:370 OR RESID 2001:2002 ) )F1 - 370
10X-RAY DIFFRACTION5( CHAIN F AND ( RESID 1:370 OR RESID 2001:2002 ) )F2001 - 2002
11X-RAY DIFFRACTION6( CHAIN A AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )A1069 - 1355
12X-RAY DIFFRACTION6( CHAIN A AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )A2003
13X-RAY DIFFRACTION6( CHAIN A AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )A2004
14X-RAY DIFFRACTION7( CHAIN B AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2010 ) ) OR ( CHAIN B AND RESID 2011:2011 )B1069 - 1355
15X-RAY DIFFRACTION7( CHAIN B AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2010 ) ) OR ( CHAIN B AND RESID 2011:2011 )B2003
16X-RAY DIFFRACTION7( CHAIN B AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2010 ) ) OR ( CHAIN B AND RESID 2011:2011 )B2004 - 2010
17X-RAY DIFFRACTION7( CHAIN B AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2010 ) ) OR ( CHAIN B AND RESID 2011:2011 )B2011
18X-RAY DIFFRACTION8( CHAIN C AND ( RESID 1069:1356 OR RESID 2003:2003 ) )C1069 - 1356
19X-RAY DIFFRACTION8( CHAIN C AND ( RESID 1069:1356 OR RESID 2003:2003 ) )C2003
20X-RAY DIFFRACTION9( CHAIN D AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )D1069 - 1355
21X-RAY DIFFRACTION9( CHAIN D AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )D2003
22X-RAY DIFFRACTION9( CHAIN D AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )D2004 - 2011
23X-RAY DIFFRACTION10( CHAIN E AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )E1069 - 1355
24X-RAY DIFFRACTION10( CHAIN E AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )E2003
25X-RAY DIFFRACTION10( CHAIN E AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2011 ) )E2004 - 2011
26X-RAY DIFFRACTION11( CHAIN F AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2010 ) )F1069 - 1355
27X-RAY DIFFRACTION11( CHAIN F AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2010 ) )F2003
28X-RAY DIFFRACTION11( CHAIN F AND ( RESID 1069:1355 OR RESID 2003:2003 OR RESID 2004:2010 ) )F2004 - 2010

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