[English] 日本語
Yorodumi
- PDB-2q04: Crystal structure of acetoin utilization protein (ZP_00540088.1) ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2q04
TitleCrystal structure of acetoin utilization protein (ZP_00540088.1) from Exiguobacterium sibiricum 255-15 at 2.33 A resolution
ComponentsAcetoin utilization protein
KeywordsTRANSFERASE / ZP_00540088.1 / acetoin utilization protein / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-2
Function / homology
Function and homology information


acetoin dehydrogenase activity / acetoin catabolic process / N-acetyltransferase activity / metal ion binding
Similarity search - Function
Acetoin utilization protein AcuA / Acetyltransferase (GNAT) family / Gcn5-related N-acetyltransferase (GNAT) / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / Acyl-CoA N-acyltransferase / Aminopeptidase / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
ACETIC ACID / Acetoin utilization protein / :
Similarity search - Component
Biological speciesExiguobacterium sibiricum (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.33 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: To be published
Title: Crystal structure of acetoin utilization protein (ZP_00540088.1) from Exiguobacterium sibiricum 255-15 at 2.33 A resolution
Authors: Joint Center for Structural Genomics (JCSG)
History
DepositionMay 18, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 12, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Source and taxonomy / Version format compliance
Revision 1.3Oct 18, 2017Group: Refinement description / Category: software / Item: _software.classification / _software.name
Revision 1.4Oct 25, 2017Group: Author supporting evidence / Category: pdbx_struct_assembly_auth_evidence
Revision 1.5Jul 24, 2019Group: Data collection / Derived calculations / Refinement description
Category: software / struct_conn
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.language / _software.location / _software.name / _software.type / _software.version / _struct_conn.pdbx_leaving_atom_flag
Revision 1.6Jan 25, 2023Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.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 / _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 / _struct_conn_type.id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH ... BIOMOLECULE: 1, 2, 3, 4, 5, 6 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT WHICH CONSISTS OF 6 CHAIN(S). SEE REMARK 350 FOR INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S). SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORT THE ASSIGNMENT OF A MONOMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.
Remark 999 SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS ... SEQUENCE THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Acetoin utilization protein
B: Acetoin utilization protein
C: Acetoin utilization protein
D: Acetoin utilization protein
E: Acetoin utilization protein
F: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)148,12824
Polymers147,1736
Non-polymers95518
Water4,324240
1
A: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,8557
Polymers24,5291
Non-polymers3266
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,5692
Polymers24,5291
Non-polymers401
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,6313
Polymers24,5291
Non-polymers1022
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,6934
Polymers24,5291
Non-polymers1643
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,6894
Polymers24,5291
Non-polymers1603
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,6914
Polymers24,5291
Non-polymers1623
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12210 Å2
ΔGint-114 kcal/mol
Surface area52560 Å2
MethodPISA
8
C: Acetoin utilization protein
D: Acetoin utilization protein
E: Acetoin utilization protein
F: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)98,70415
Polymers98,1154
Non-polymers58911
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6000 Å2
ΔGint-55 kcal/mol
Surface area37230 Å2
MethodPISA
9
A: Acetoin utilization protein
B: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)49,4249
Polymers49,0582
Non-polymers3667
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2180 Å2
ΔGint-30 kcal/mol
Surface area19370 Å2
MethodPISA
10
A: Acetoin utilization protein
C: Acetoin utilization protein
D: Acetoin utilization protein
E: Acetoin utilization protein
F: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)123,55922
Polymers122,6445
Non-polymers91517
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8910 Å2
ΔGint-82 kcal/mol
Surface area45430 Å2
MethodPISA
11
B: Acetoin utilization protein
C: Acetoin utilization protein
D: Acetoin utilization protein
E: Acetoin utilization protein
F: Acetoin utilization protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)123,27317
Polymers122,6445
Non-polymers62912
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7820 Å2
ΔGint-80 kcal/mol
Surface area45840 Å2
MethodPISA
Unit cell
Length a, b, c (Å)70.870, 128.580, 108.430
Angle α, β, γ (deg.)90.000, 108.430, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61A
71B
81C
91D
101E
111F
121A
131B
141C
151D
161E
171F
181A
191B
201C
211D
221E
231F
241A
251B
261C
271D
281E
291F
301A
311B
321C
331D
341E
351F
361A
371B
381C
391D
401E
411F

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg label comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLYLYS6AA0 - 41 - 5
21PHELYS6BB2 - 43 - 5
31PHELYS6CC2 - 43 - 5
41GLYLYS6DD0 - 41 - 5
51GLYLYS6EE0 - 41 - 5
62GLNPRO4AA5 - 366 - 37
72GLNPRO4BB5 - 366 - 37
82GLNPRO4CC5 - 366 - 37
92GLNPRO4DD5 - 366 - 37
102GLNPRO4EE5 - 366 - 37
112GLNPRO4FF5 - 366 - 37
123GLYPRO6AA37 - 4438 - 45
133GLYPRO6BB37 - 4438 - 45
143GLYPRO6CC37 - 4438 - 45
153GLYPRO6DD37 - 4438 - 45
163GLYPRO6EE37 - 4438 - 45
173GLYPRO6FF37 - 4438 - 45
184ALATYR4AA45 - 13546 - 136
194ALATYR4BB45 - 13546 - 136
204ALATYR4CC45 - 13546 - 136
214ALATYR4DD45 - 13546 - 136
224ALATYR4EE45 - 13546 - 136
234ALATYR4FF45 - 13546 - 136
245TYRSER6AA136 - 147137 - 148
255TYRSER6BB136 - 147137 - 148
265TYRSER6CC136 - 147137 - 148
275TYRSER6DD136 - 147137 - 148
285TYRSER6EE136 - 147137 - 148
295TYRSER6FF136 - 147137 - 148
306VALLEU2AA148 - 203149 - 204
316VALLEU2BB148 - 203149 - 204
326VALLEU2CC148 - 203149 - 204
336VALLEU2DD148 - 203149 - 204
346VALLEU2EE148 - 203149 - 204
356VALLEU2FF148 - 203149 - 204
367ARGASP6AA204 - 210205 - 211
377ARGMSE6BB204 - 208205 - 209
387ARGTYR6CC204 - 209205 - 210
397ARGTYR6DD204 - 209205 - 210
407ARGTYR6EE204 - 209205 - 210
417ARGMSE6FF204 - 208205 - 209
DetailsSIZE EXCLUSION WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A MONOMER AS A BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE.

-
Components

#1: Protein
Acetoin utilization protein


Mass: 24528.775 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Exiguobacterium sibiricum (bacteria) / Strain: 255-15 / Gene: ZP_00540088.1, ExigDRAFT_0571 / Plasmid: speedET / Production host: Escherichia coli (E. coli) / Strain (production host): HK100 / References: UniProt: Q41BL0, UniProt: B1YKD7*PLUS
#2: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Ca
#3: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C2H6O2
#4: Chemical
ChemComp-ACY / ACETIC ACID / Acetic acid


Mass: 60.052 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H4O2
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 240 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.18 Å3/Da / Density % sol: 61.36 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: NANODROP, 5.7% PEG 8000, 0.2M Calcium acetate, 0.1M Imidazole pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.91162, 0.97936, 0.97925
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Mar 15, 2007 / Details: Flat collimating mirror, toroid focusing mirror
RadiationMonochromator: Double crystal / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.911621
20.979361
30.979251
ReflectionResolution: 2.33→29.336 Å / Num. obs: 73748 / % possible obs: 88.6 % / Observed criterion σ(I): -3 / Biso Wilson estimate: 50.785 Å2 / Rmerge(I) obs: 0.052 / Net I/σ(I): 7.53
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
2.33-2.410.451.481131345289.7
2.41-2.510.3691.688811443389.7
2.51-2.620.3141.984241349189.3
2.62-2.760.2392.587281405189.6
2.76-2.930.1683.587091370089
2.93-3.160.1075.289441400688.8
3.16-3.480.0648.189671390488.5
3.48-3.980.03513.488681368688.4
3.98-50.02418.390881356987.8
50.0212091461343885.1

-
Phasing

PhasingMethod: MAD

-
Processing

Software
NameVersionClassificationNB
REFMAC5.2.0005refinement
PHENIXrefinement
SHELXphasing
MolProbity3beta29model building
XSCALEdata scaling
PDB_EXTRACT3data extraction
MAR345CCDdata collection
XDSdata reduction
autoSHARPphasing
RefinementMethod to determine structure: MAD / Resolution: 2.33→29.336 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.924 / SU B: 19.82 / SU ML: 0.227 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.325 / ESU R Free: 0.24
Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES
Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN ...Details: 1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. CALCIUM AND ACETATE FROM THE CRYSTALLIZATION SOLUTIONS WERE MODELED INTO THE STRUCTURE. 5. ETHYLENE GLYCOL USED AS A CRYOPROTECTANT WAS MODELED INTO THE STRUCTURE. 6. UNEXPLAINED DIFFERENCE ELECTRON DENSITIES NEAR GLY 112 IN THE D AND E SUBUNITS WERE NOT MODELED. 7. ARG B205, PHE B207, ASP C35, AND PRO C36 WERE MODELED INTO ELECTRON DENSITY BUT ARE RAMACHANDRAN OUTLIERS.
RfactorNum. reflection% reflectionSelection details
Rfree0.26 3696 5 %RANDOM
Rwork0.229 ---
obs0.231 73722 93.65 %-
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: 54.794 Å2
Baniso -1Baniso -2Baniso -3
1--1.73 Å20 Å2-2.01 Å2
2---0.88 Å20 Å2
3---1.33 Å2
Refinement stepCycle: LAST / Resolution: 2.33→29.336 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9788 0 51 240 10079
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.02210152
X-RAY DIFFRACTIONr_bond_other_d0.0030.029122
X-RAY DIFFRACTIONr_angle_refined_deg0.7561.95113809
X-RAY DIFFRACTIONr_angle_other_deg0.562321065
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.29751260
X-RAY DIFFRACTIONr_dihedral_angle_2_deg28.89423.608474
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.214151577
X-RAY DIFFRACTIONr_dihedral_angle_4_deg13.0061562
X-RAY DIFFRACTIONr_chiral_restr0.0660.21486
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0211428
X-RAY DIFFRACTIONr_gen_planes_other0.0020.022114
X-RAY DIFFRACTIONr_nbd_refined0.2010.32290
X-RAY DIFFRACTIONr_nbd_other0.180.39503
X-RAY DIFFRACTIONr_nbtor_refined0.1840.54959
X-RAY DIFFRACTIONr_nbtor_other0.0850.55600
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2020.5537
X-RAY DIFFRACTIONr_xyhbond_nbd_other0.0670.53
X-RAY DIFFRACTIONr_metal_ion_refined0.1130.59
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1830.313
X-RAY DIFFRACTIONr_symmetry_vdw_other0.2320.349
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1530.58
X-RAY DIFFRACTIONr_mcbond_it0.71526399
X-RAY DIFFRACTIONr_mcbond_other0.19722542
X-RAY DIFFRACTIONr_mcangle_it1.181410025
X-RAY DIFFRACTIONr_scbond_it2.31264304
X-RAY DIFFRACTIONr_scangle_it3.07483777
Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A327TIGHT POSITIONAL0.070.05
2B327TIGHT POSITIONAL0.070.05
3C327TIGHT POSITIONAL0.040.05
4D327TIGHT POSITIONAL0.080.05
5E327TIGHT POSITIONAL0.060.05
11F327TIGHT POSITIONAL0.050.05
1A2136MEDIUM POSITIONAL0.470.5
2B2136MEDIUM POSITIONAL0.50.5
3C2136MEDIUM POSITIONAL0.450.5
4D2136MEDIUM POSITIONAL0.570.5
5E2136MEDIUM POSITIONAL0.470.5
11F2136MEDIUM POSITIONAL0.510.5
1A302LOOSE POSITIONAL1.325
2B302LOOSE POSITIONAL1.535
3C302LOOSE POSITIONAL1.675
4D302LOOSE POSITIONAL1.455
5E302LOOSE POSITIONAL1.585
11F302LOOSE POSITIONAL1.435
1A327TIGHT THERMAL0.090.5
2B327TIGHT THERMAL0.070.5
3C327TIGHT THERMAL0.080.5
4D327TIGHT THERMAL0.110.5
5E327TIGHT THERMAL0.080.5
11F327TIGHT THERMAL0.070.5
1A2136MEDIUM THERMAL0.52
2B2136MEDIUM THERMAL0.512
3C2136MEDIUM THERMAL0.442
4D2136MEDIUM THERMAL0.652
5E2136MEDIUM THERMAL0.552
11F2136MEDIUM THERMAL0.452
1A302LOOSE THERMAL4.0610
2B302LOOSE THERMAL3.7210
3C302LOOSE THERMAL1.5710
4D302LOOSE THERMAL5.3110
5E302LOOSE THERMAL3.4510
11F302LOOSE THERMAL2.2510
LS refinement shellResolution: 2.33→2.39 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.322 266 -
Rwork0.332 5278 -
obs-5544 95.8 %
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)
13.67492.08821.8853.94441.16324.2849-0.06430.129-0.0285-0.26210.1262-0.198-0.24520.3183-0.0619-0.16030.00080.0325-0.2154-0.1191-0.18193.98181.98542.2773
24.974-2.35231.32734.5461-1.15533.6792-0.0897-0.1310.14850.38070.1157-0.0188-0.1121-0.2582-0.026-0.10430.06820.0079-0.21520.0757-0.1683-20.172885.29579.2964
34.00751.55840.18552.99140.73135.13430.1064-0.63980.7350.3886-0.57650.86330.0237-1.16650.4701-0.1118-0.07390.15530.3785-0.3440.0217-25.074262.019953.9416
45.7428-1.62491.32373.27580.03182.8354-0.119-0.3895-0.2606-0.0170.13620.32440.1268-0.0259-0.0172-0.32410.0430.0736-0.2601-0.0041-0.3718.103844.30135.4481
54.78012.15441.53432.92430.15652.4913-0.14210.3713-0.18310.00760.1386-0.20340.15240.21730.0035-0.2936-0.0413-0.002-0.1893-0.0016-0.2526-25.695245.405716.2946
65.918-3.34760.46895.128-0.76584.66580.63251.04040.9857-0.8094-0.7107-0.9557-0.33080.65920.07820.04330.08140.15390.13170.2199-0.01067.908663.6393-1.3784
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA0 - 2101 - 211
2X-RAY DIFFRACTION2BB2 - 2063 - 207
3X-RAY DIFFRACTION3CC2 - 2093 - 210
4X-RAY DIFFRACTION4DD2 - 2093 - 210
5X-RAY DIFFRACTION5EE0 - 2091 - 210
6X-RAY DIFFRACTION6FF5 - 2086 - 209

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

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

-
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

Read more