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- PDB-7xqa: Orf1-glycine complex -

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Basic information

Entry
Database: PDB / ID: 7xqa
TitleOrf1-glycine complex
Components(N-formimidoyl fortimicin A synthase) x 2
KeywordsOXIDOREDUCTASE / glycine complex cysteine-adduct
Function / homologyFAD dependent oxidoreductase / FAD dependent oxidoreductase / FAD/NAD(P)-binding domain superfamily / oxidoreductase activity / nucleotide binding / cytoplasm / FLAVIN-ADENINE DINUCLEOTIDE / GLYCINE / N-formimidoyl fortimicin A synthase
Function and homology information
Biological speciesStreptomyces luteocolor (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.93 Å
AuthorsWang, Y.L. / Li, T.L.
Funding support Taiwan, 1items
OrganizationGrant numberCountry
Other government Taiwan
CitationJournal: Nat Commun / Year: 2023
Title: N-Formimidoylation/-iminoacetylation modification in aminoglycosides requires FAD-dependent and ligand-protein NOS bridge dual chemistry.
Authors: Wang, Y.L. / Chang, C.Y. / Hsu, N.S. / Lo, I.W. / Lin, K.H. / Chen, C.L. / Chang, C.F. / Wang, Z.C. / Ogasawara, Y. / Dairi, T. / Maruyama, C. / Hamano, Y. / Li, T.L.
History
DepositionMay 7, 2022Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0May 31, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 29, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.2May 8, 2024Group: Database references / Category: citation
Item: _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: N-formimidoyl fortimicin A synthase
B: N-formimidoyl fortimicin A synthase
C: N-formimidoyl fortimicin A synthase
D: N-formimidoyl fortimicin A synthase
E: N-formimidoyl fortimicin A synthase
F: N-formimidoyl fortimicin A synthase
G: N-formimidoyl fortimicin A synthase
H: N-formimidoyl fortimicin A synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)447,54526
Polymers440,5108
Non-polymers7,03518
Water56,2433122
1
A: N-formimidoyl fortimicin A synthase
B: N-formimidoyl fortimicin A synthase
C: N-formimidoyl fortimicin A synthase
D: N-formimidoyl fortimicin A synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)223,72913
Polymers220,2124
Non-polymers3,5189
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area17430 Å2
ΔGint-97 kcal/mol
Surface area64880 Å2
MethodPISA
2
E: N-formimidoyl fortimicin A synthase
F: N-formimidoyl fortimicin A synthase
G: N-formimidoyl fortimicin A synthase
H: N-formimidoyl fortimicin A synthase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)223,81613
Polymers220,2994
Non-polymers3,5189
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area17480 Å2
ΔGint-96 kcal/mol
Surface area64980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)103.386, 107.803, 134.754
Angle α, β, γ (deg.)89.853, 89.989, 83.575
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
32A
42C
53A
63D
74A
84E
95A
105F
116A
126G
137A
147H
158A
168H
179B
189C
1910B
2010D
2111B
2211E
2312B
2412F
2513B
2613G
2714B
2814H
2915B
3015H
3116C
3216D
3317C
3417E
3518C
3618F
3719C
3819G
3920C
4020H
4121C
4221H
4322D
4422E
4523D
4623F
4724D
4824G
4925D
5025H
5126D
5226H
5327E
5427F
5528E
5628G
5729E
5829H
5930E
6030H
6131F
6231G
6332F
6432H
6533F
6633H
6734G
6834H
6935G
7035H

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLNGLNHISHISAA10 - 49131 - 512
221GLNGLNHISHISBB10 - 49131 - 512
332GLNGLNHISHISAA10 - 49131 - 512
442GLNGLNHISHISCC10 - 49131 - 512
553VALVALTRPTRPAA13 - 49034 - 511
663VALVALTRPTRPDD13 - 49034 - 511
774GLNGLNHISHISAA10 - 49131 - 512
884GLNGLNHISHISEE10 - 49131 - 512
995GLNGLNHISHISAA10 - 49131 - 512
10105GLNGLNHISHISFF10 - 49131 - 512
11116GLNGLNHISHISAA10 - 49131 - 512
12126GLNGLNHISHISGG10 - 49131 - 512
13137VALVALPHEPHEAA13 - 27934 - 300
14147VALVALALAALAHH13 - 28034 - 301
15158GLYGLYTRPTRPAA282 - 490303 - 511
16168GQIGQIGQIGQIHH492302
17179GLNGLNHISHISBB10 - 49131 - 512
18189GLNGLNHISHISCC10 - 49131 - 512
191910VALVALTRPTRPBB13 - 49034 - 511
202010VALVALTRPTRPDD13 - 49034 - 511
212111GLNGLNHISHISBB10 - 49131 - 512
222211GLNGLNHISHISEE10 - 49131 - 512
232312GLNGLNHISHISBB10 - 49131 - 512
242412GLNGLNHISHISFF10 - 49131 - 512
252513GLNGLNHISHISBB10 - 49131 - 512
262613GLNGLNHISHISGG10 - 49131 - 512
272714VALVALPHEPHEBB13 - 27934 - 300
282814VALVALALAALAHH13 - 28034 - 301
292915GLYGLYTRPTRPBB282 - 490303 - 511
303015GQIGQIGQIGQIHH492302
313116VALVALTRPTRPCC13 - 49034 - 511
323216VALVALTRPTRPDD13 - 49034 - 511
333317GLNGLNHISHISCC10 - 49131 - 512
343417GLNGLNHISHISEE10 - 49131 - 512
353518GLNGLNHISHISCC10 - 49131 - 512
363618GLNGLNHISHISFF10 - 49131 - 512
373719GLNGLNHISHISCC10 - 49131 - 512
383819GLNGLNHISHISGG10 - 49131 - 512
393920VALVALPHEPHECC13 - 27934 - 300
404020VALVALALAALAHH13 - 28034 - 301
414121GLYGLYTRPTRPCC282 - 490303 - 511
424221GQIGQIGQIGQIHH492302
434322VALVALTRPTRPDD13 - 49034 - 511
444422VALVALTRPTRPEE13 - 49034 - 511
454523VALVALTRPTRPDD13 - 49034 - 511
464623VALVALTRPTRPFF13 - 49034 - 511
474724VALVALTRPTRPDD13 - 49034 - 511
484824VALVALTRPTRPGG13 - 49034 - 511
494925VALVALPHEPHEDD13 - 27934 - 300
505025VALVALALAALAHH13 - 28034 - 301
515126GLYGLYTRPTRPDD282 - 490303 - 511
525226GQIGQIGQIGQIHH492302
535327GLNGLNHISHISEE10 - 49131 - 512
545427GLNGLNHISHISFF10 - 49131 - 512
555528GLNGLNHISHISEE10 - 49131 - 512
565628GLNGLNHISHISGG10 - 49131 - 512
575729VALVALPHEPHEEE13 - 27934 - 300
585829VALVALALAALAHH13 - 28034 - 301
595930GLYGLYTRPTRPEE282 - 490303 - 511
606030GQIGQIGQIGQIHH492302
616131GLNGLNHISHISFF10 - 49131 - 512
626231GLNGLNHISHISGG10 - 49131 - 512
636332VALVALPHEPHEFF13 - 27934 - 300
646432VALVALALAALAHH13 - 28034 - 301
656533GLYGLYTRPTRPFF282 - 490303 - 511
666633GQIGQIGQIGQIHH492302
676734VALVALPHEPHEGG13 - 27934 - 300
686834VALVALALAALAHH13 - 28034 - 301
696935GLYGLYTRPTRPGG282 - 490303 - 511
707035GQIGQIGQIGQIHH492302

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12
7Local NCS retraints between domains: 13 14
8Local NCS retraints between domains: 15 16
9Local NCS retraints between domains: 17 18
10Local NCS retraints between domains: 19 20
11Local NCS retraints between domains: 21 22
12Local NCS retraints between domains: 23 24
13Local NCS retraints between domains: 25 26
14Local NCS retraints between domains: 27 28
15Local NCS retraints between domains: 29 30
16Local NCS retraints between domains: 31 32
17Local NCS retraints between domains: 33 34
18Local NCS retraints between domains: 35 36
19Local NCS retraints between domains: 37 38
20Local NCS retraints between domains: 39 40
21Local NCS retraints between domains: 41 42
22Local NCS retraints between domains: 43 44
23Local NCS retraints between domains: 45 46
24Local NCS retraints between domains: 47 48
25Local NCS retraints between domains: 49 50
26Local NCS retraints between domains: 51 52
27Local NCS retraints between domains: 53 54
28Local NCS retraints between domains: 55 56
29Local NCS retraints between domains: 57 58
30Local NCS retraints between domains: 59 60
31Local NCS retraints between domains: 61 62
32Local NCS retraints between domains: 63 64
33Local NCS retraints between domains: 65 66
34Local NCS retraints between domains: 67 68
35Local NCS retraints between domains: 69 70

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Components

#1: Protein
N-formimidoyl fortimicin A synthase


Mass: 55052.918 Da / Num. of mol.: 7
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptomyces luteocolor (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: A0A125SZC1
#2: Protein N-formimidoyl fortimicin A synthase


Mass: 55139.953 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptomyces luteocolor (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: A0A125SZC1
#3: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE / Flavin adenine dinucleotide


Mass: 785.550 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: FAD*YM
#4: Chemical
ChemComp-GLY / GLYCINE / Glycine


Type: peptide linking / Mass: 75.067 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C2H5NO2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 3122 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 3.39 Å3/Da / Density % sol: 59.15 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 0.1 M Tris-HCl pH8.5, 0.2 M KBr, 8 % PEG 550 MME and 8 % PEG 20000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: NSRRC / Beamline: TPS 05A / Wavelength: 1 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Apr 13, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.93→30 Å / Num. obs: 424903 / % possible obs: 97.9 % / Redundancy: 5.3 % / Rmerge(I) obs: 0.043 / Rpim(I) all: 0.021 / Rrim(I) all: 0.048 / Χ2: 0.936 / Net I/σ(I): 35.8 / Num. measured all: 2253992
Reflection shell

Diffraction-ID: 1 / Redundancy: 5.3 %

Resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
1.93-20.285.9418870.9620.1350.3110.92896.5
2-2.080.212420190.9740.1020.2360.97496.9
2.08-2.170.158421750.9850.0760.1750.99697.2
2.17-2.290.118422940.990.0570.1311.01497.4
2.29-2.430.09423820.9930.0430.11.0197.7
2.43-2.620.069425540.9960.0340.0771.00998
2.62-2.880.053426630.9970.0260.0590.9898.3
2.88-3.30.04427870.9980.020.0450.92598.7
3.3-4.150.032430300.9980.0160.0360.84199
4.15-300.028431120.9980.0140.0310.68199.4

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
HKL-2000data reduction
HKL-2000data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1ng3
Resolution: 1.93→29.718 Å / Cor.coef. Fo:Fc: 0.944 / Cor.coef. Fo:Fc free: 0.935 / WRfactor Rfree: 0.211 / WRfactor Rwork: 0.195 / SU B: 2.876 / SU ML: 0.082 / Average fsc free: 0.9294 / Average fsc work: 0.9354 / Cross valid method: FREE R-VALUE / ESU R: 0.132 / ESU R Free: 0.118
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.2083 21320 5.018 %
Rwork0.1921 403562 -
all0.193 --
obs-424882 97.733 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 23.627 Å2
Baniso -1Baniso -2Baniso -3
1-0.079 Å2-0.071 Å20 Å2
2--0.017 Å2-0.058 Å2
3----0.112 Å2
Refinement stepCycle: LAST / Resolution: 1.93→29.718 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29178 0 486 3122 32786
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01330413
X-RAY DIFFRACTIONr_bond_other_d0.0010.01728306
X-RAY DIFFRACTIONr_angle_refined_deg1.3711.63841513
X-RAY DIFFRACTIONr_angle_other_deg1.3081.57464943
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.71153850
X-RAY DIFFRACTIONr_dihedral_angle_2_deg27.73720.5471608
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.981154558
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.64215281
X-RAY DIFFRACTIONr_chiral_restr0.0680.23918
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0234910
X-RAY DIFFRACTIONr_gen_planes_other0.0010.026932
X-RAY DIFFRACTIONr_nbd_refined0.1930.26083
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1830.227241
X-RAY DIFFRACTIONr_nbtor_refined0.1540.214649
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.080.214058
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1550.22667
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.10.29
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.2620.232
X-RAY DIFFRACTIONr_nbd_other0.2710.281
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1660.249
X-RAY DIFFRACTIONr_mcbond_it1.5692.35115442
X-RAY DIFFRACTIONr_mcbond_other1.5692.35115440
X-RAY DIFFRACTIONr_mcangle_it2.4463.51719278
X-RAY DIFFRACTIONr_mcangle_other2.4463.51719278
X-RAY DIFFRACTIONr_scbond_it2.0252.59914971
X-RAY DIFFRACTIONr_scbond_other2.0242.59914971
X-RAY DIFFRACTIONr_scangle_it3.2743.79822235
X-RAY DIFFRACTIONr_scangle_other3.2743.79822235
X-RAY DIFFRACTIONr_lrange_it5.2528.29934764
X-RAY DIFFRACTIONr_lrange_other4.99927.8633887
X-RAY DIFFRACTIONr_ncsr_local_group_10.0590.0515424
X-RAY DIFFRACTIONr_ncsr_local_group_20.0650.0515288
X-RAY DIFFRACTIONr_ncsr_local_group_30.0580.0515198
X-RAY DIFFRACTIONr_ncsr_local_group_40.0420.0515657
X-RAY DIFFRACTIONr_ncsr_local_group_50.0610.0515404
X-RAY DIFFRACTIONr_ncsr_local_group_60.0640.0515290
X-RAY DIFFRACTIONr_ncsr_local_group_70.0590.057615
X-RAY DIFFRACTIONr_ncsr_local_group_80.0630.056253
X-RAY DIFFRACTIONr_ncsr_local_group_90.0540.0515478
X-RAY DIFFRACTIONr_ncsr_local_group_100.0540.0515310
X-RAY DIFFRACTIONr_ncsr_local_group_110.0560.0515514
X-RAY DIFFRACTIONr_ncsr_local_group_120.040.0515680
X-RAY DIFFRACTIONr_ncsr_local_group_130.0570.0515441
X-RAY DIFFRACTIONr_ncsr_local_group_140.0520.057691
X-RAY DIFFRACTIONr_ncsr_local_group_150.0640.056255
X-RAY DIFFRACTIONr_ncsr_local_group_160.0540.0515168
X-RAY DIFFRACTIONr_ncsr_local_group_170.0630.0515266
X-RAY DIFFRACTIONr_ncsr_local_group_180.0560.0515371
X-RAY DIFFRACTIONr_ncsr_local_group_190.0360.0515609
X-RAY DIFFRACTIONr_ncsr_local_group_200.0530.057606
X-RAY DIFFRACTIONr_ncsr_local_group_210.060.056217
X-RAY DIFFRACTIONr_ncsr_local_group_220.0590.0515170
X-RAY DIFFRACTIONr_ncsr_local_group_230.0570.0515208
X-RAY DIFFRACTIONr_ncsr_local_group_240.0550.0515165
X-RAY DIFFRACTIONr_ncsr_local_group_250.0310.057722
X-RAY DIFFRACTIONr_ncsr_local_group_260.0440.056286
X-RAY DIFFRACTIONr_ncsr_local_group_270.0590.0515436
X-RAY DIFFRACTIONr_ncsr_local_group_280.0660.0515283
X-RAY DIFFRACTIONr_ncsr_local_group_290.0560.057646
X-RAY DIFFRACTIONr_ncsr_local_group_300.0720.056227
X-RAY DIFFRACTIONr_ncsr_local_group_310.0560.0515421
X-RAY DIFFRACTIONr_ncsr_local_group_320.0550.057636
X-RAY DIFFRACTIONr_ncsr_local_group_330.0620.056285
X-RAY DIFFRACTIONr_ncsr_local_group_340.0520.057598
X-RAY DIFFRACTIONr_ncsr_local_group_350.0570.056248
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AX-RAY DIFFRACTIONLocal ncs0.058630.0501
12BX-RAY DIFFRACTIONLocal ncs0.058630.0501
23AX-RAY DIFFRACTIONLocal ncs0.064980.05009
24CX-RAY DIFFRACTIONLocal ncs0.064980.05009
35AX-RAY DIFFRACTIONLocal ncs0.058410.05009
36DX-RAY DIFFRACTIONLocal ncs0.058410.05009
47AX-RAY DIFFRACTIONLocal ncs0.042110.0501
48EX-RAY DIFFRACTIONLocal ncs0.042110.0501
59AX-RAY DIFFRACTIONLocal ncs0.061190.0501
510FX-RAY DIFFRACTIONLocal ncs0.061190.0501
611AX-RAY DIFFRACTIONLocal ncs0.064040.05009
612GX-RAY DIFFRACTIONLocal ncs0.064040.05009
713AX-RAY DIFFRACTIONLocal ncs0.059320.05009
714HX-RAY DIFFRACTIONLocal ncs0.059320.05009
815AX-RAY DIFFRACTIONLocal ncs0.06320.05009
816HX-RAY DIFFRACTIONLocal ncs0.06320.05009
917BX-RAY DIFFRACTIONLocal ncs0.054410.05009
918CX-RAY DIFFRACTIONLocal ncs0.054410.05009
1019BX-RAY DIFFRACTIONLocal ncs0.054310.05009
1020DX-RAY DIFFRACTIONLocal ncs0.054310.05009
1121BX-RAY DIFFRACTIONLocal ncs0.055860.0501
1122EX-RAY DIFFRACTIONLocal ncs0.055860.0501
1223BX-RAY DIFFRACTIONLocal ncs0.040480.0501
1224FX-RAY DIFFRACTIONLocal ncs0.040480.0501
1325BX-RAY DIFFRACTIONLocal ncs0.057260.05009
1326GX-RAY DIFFRACTIONLocal ncs0.057260.05009
1427BX-RAY DIFFRACTIONLocal ncs0.05210.05009
1428HX-RAY DIFFRACTIONLocal ncs0.05210.05009
1529BX-RAY DIFFRACTIONLocal ncs0.064090.05009
1530HX-RAY DIFFRACTIONLocal ncs0.064090.05009
1631CX-RAY DIFFRACTIONLocal ncs0.053860.05009
1632DX-RAY DIFFRACTIONLocal ncs0.053860.05009
1733CX-RAY DIFFRACTIONLocal ncs0.062980.05009
1734EX-RAY DIFFRACTIONLocal ncs0.062980.05009
1835CX-RAY DIFFRACTIONLocal ncs0.056250.05009
1836FX-RAY DIFFRACTIONLocal ncs0.056250.05009
1937CX-RAY DIFFRACTIONLocal ncs0.035790.0501
1938GX-RAY DIFFRACTIONLocal ncs0.035790.0501
2039CX-RAY DIFFRACTIONLocal ncs0.052720.05009
2040HX-RAY DIFFRACTIONLocal ncs0.052720.05009
2141CX-RAY DIFFRACTIONLocal ncs0.059840.05009
2142HX-RAY DIFFRACTIONLocal ncs0.059840.05009
2243DX-RAY DIFFRACTIONLocal ncs0.059340.05009
2244EX-RAY DIFFRACTIONLocal ncs0.059340.05009
2345DX-RAY DIFFRACTIONLocal ncs0.056830.05009
2346FX-RAY DIFFRACTIONLocal ncs0.056830.05009
2447DX-RAY DIFFRACTIONLocal ncs0.054720.05009
2448GX-RAY DIFFRACTIONLocal ncs0.054720.05009
2549DX-RAY DIFFRACTIONLocal ncs0.030720.0501
2550HX-RAY DIFFRACTIONLocal ncs0.030720.0501
2651DX-RAY DIFFRACTIONLocal ncs0.043670.05009
2652HX-RAY DIFFRACTIONLocal ncs0.043670.05009
2753EX-RAY DIFFRACTIONLocal ncs0.058850.0501
2754FX-RAY DIFFRACTIONLocal ncs0.058850.0501
2855EX-RAY DIFFRACTIONLocal ncs0.065740.05009
2856GX-RAY DIFFRACTIONLocal ncs0.065740.05009
2957EX-RAY DIFFRACTIONLocal ncs0.056240.05009
2958HX-RAY DIFFRACTIONLocal ncs0.056240.05009
3059EX-RAY DIFFRACTIONLocal ncs0.072230.05009
3060HX-RAY DIFFRACTIONLocal ncs0.072230.05009
3161FX-RAY DIFFRACTIONLocal ncs0.056110.05009
3162GX-RAY DIFFRACTIONLocal ncs0.056110.05009
3263FX-RAY DIFFRACTIONLocal ncs0.055430.05009
3264HX-RAY DIFFRACTIONLocal ncs0.055430.05009
3365FX-RAY DIFFRACTIONLocal ncs0.06220.05009
3366HX-RAY DIFFRACTIONLocal ncs0.06220.05009
3467GX-RAY DIFFRACTIONLocal ncs0.052130.05009
3468HX-RAY DIFFRACTIONLocal ncs0.052130.05009
3569GX-RAY DIFFRACTIONLocal ncs0.056730.05009
3570HX-RAY DIFFRACTIONLocal ncs0.056730.05009
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.93-1.980.26915230.24628974X-RAY DIFFRACTION94.8467
1.98-2.0350.25815150.23828848X-RAY DIFFRACTION96.7683
2.035-2.0940.25915240.23228023X-RAY DIFFRACTION97.0345
2.094-2.1580.25513480.22327470X-RAY DIFFRACTION97.1153
2.158-2.2290.23514460.21326411X-RAY DIFFRACTION97.3783
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