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- PDB-2v6a: Crystal structure of Chlamydomonas reinhardtii Rubisco with large... -

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Basic information

Entry
Database: PDB / ID: 2v6a
TitleCrystal structure of Chlamydomonas reinhardtii Rubisco with large- subunit mutations V331A, G344S
Components(RIBULOSE BISPHOSPHATE CARBOXYLASE ...) x 2
KeywordsOXIDOREDUCTASE / LARGE SUBUNIT LOOP 6 MUTATION / CO2/O2 SPECIFICITY / CARBON DIOXIDE FIXATION / PHOTOSYNTHESIS / TRANSIT PEPTIDE / PHOTORESPIRATION / METAL-BINDING / HYDROXYLATION / METHYLATION / CHLOROPLAST / CALVIN CYCLE / MONOOXYGENASE / LYASE / RUBISCO / PLASTID / MAGNESIUM / ACETYLATION
Function / homology
Function and homology information


photorespiration / ribulose-bisphosphate carboxylase / ribulose-bisphosphate carboxylase activity / reductive pentose-phosphate cycle / monooxygenase activity / chloroplast / magnesium ion binding
Similarity search - Function
Ribulose bisphosphate carboxylase, small subunit / Ribulose 1,5 Bisphosphate Carboxylase/Oxygenase / Ribulose bisphosphate carboxylase, small subunit / Ribulose bisphosphate carboxylase, large subunit, C-terminal domain / RuBisCO large subunit, N-terminal domain / Ribulose bisphosphate carboxylase small subunit, domain / Ribulose bisphosphate carboxylase, small subunit superfamily / Ribulose bisphosphate carboxylase, small chain / Ribulose bisphosphate carboxylase, small chain / Ribulose bisphosphate carboxylase large subunit, type I ...Ribulose bisphosphate carboxylase, small subunit / Ribulose 1,5 Bisphosphate Carboxylase/Oxygenase / Ribulose bisphosphate carboxylase, small subunit / Ribulose bisphosphate carboxylase, large subunit, C-terminal domain / RuBisCO large subunit, N-terminal domain / Ribulose bisphosphate carboxylase small subunit, domain / Ribulose bisphosphate carboxylase, small subunit superfamily / Ribulose bisphosphate carboxylase, small chain / Ribulose bisphosphate carboxylase, small chain / Ribulose bisphosphate carboxylase large subunit, type I / Ribulose bisphosphate carboxylase, large chain, active site / Ribulose bisphosphate carboxylase large chain active site. / Ribulose bisphosphate carboxylase, large subunit, ferrodoxin-like N-terminal / Ribulose bisphosphate carboxylase large chain, N-terminal domain / Ribulose bisphosphate carboxylase, large subunit, C-terminal / RuBisCO / Ribulose bisphosphate carboxylase, large subunit, C-terminal domain superfamily / RuBisCO large subunit, N-terminal domain superfamily / Ribulose bisphosphate carboxylase large chain, catalytic domain / Alpha-Beta Plaits / TIM Barrel / Alpha-Beta Barrel / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
2-CARBOXYARABINITOL-1,5-DIPHOSPHATE / Ribulose bisphosphate carboxylase small subunit, chloroplastic 1 / Ribulose bisphosphate carboxylase large chain
Similarity search - Component
Biological speciesCHLAMYDOMONAS REINHARDTII (plant)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å
AuthorsKarkehabadi, S. / Satagopan, S. / Taylor, T.C. / Spreitzer, R.J. / Andersson, I.
CitationJournal: Biochemistry / Year: 2007
Title: Structural Analysis of Altered Large-Subunit Loop-6-Carboxy-Terminus Interactions that Influence Catalytic Efficiency and Co2-O2 Specificity of Ribulose-1,5-Bisphosphate Carboxylase Oxygenase
Authors: Karkehabadi, S. / Satagopan, S. / Taylor, T.C. / Spreitzer, R.J. / Andersson, I.
History
DepositionJul 14, 2007Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 31, 2007Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _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_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_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
B: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
C: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
D: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
E: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
F: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
G: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
H: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN
I: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1
J: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1
K: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1
L: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1
M: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1
N: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1
O: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1
P: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)558,56691
Polymers551,86116
Non-polymers6,70575
Water62,9083492
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area125620 Å2
ΔGint-755.1 kcal/mol
Surface area152130 Å2
MethodPQS
Unit cell
Length a, b, c (Å)129.906, 196.629, 201.950
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-IDDetails
11A
12B
22A
13C
23A
14D
24A
15E
25A
16F
26A
17G
27A
18H
28A
19I
110J
210I
111K
211I
112L
212I
113M
213I
114N
214I
115O
215I
116P
216I

NCS domain segments:

Refine code: 2

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111PHEPHEPROPROAA13 - 8913 - 89
121TYRTYRCAPCAPAA - R97 - 147797
112PHEPHEPROPROBB13 - 8913 - 89
212PHEPHEPROPROAA13 - 8913 - 89
122TYRTYRCAPCAPBB - AA97 - 147797
222TYRTYRCAPCAPAA - R97 - 147797
113PHEPHEPROPROCC13 - 8913 - 89
213PHEPHEPROPROAA13 - 8913 - 89
123TYRTYRCAPCAPCC - HA97 - 147797
223TYRTYRCAPCAPAA - R97 - 147797
114PHEPHEPROPRODD13 - 8913 - 89
214PHEPHEPROPROAA13 - 8913 - 89
124TYRTYRCAPCAPDD - PA97 - 147797
224TYRTYRCAPCAPAA - R97 - 147797
115PHEPHEPROPROEE13 - 8913 - 89
215PHEPHEPROPROAA13 - 8913 - 89
125TYRTYRCAPCAPEE - WA97 - 147797
225TYRTYRCAPCAPAA - R97 - 147797
116PHEPHEPROPROFF13 - 8913 - 89
216PHEPHEPROPROAA13 - 8913 - 89
126TYRTYRCAPCAPFF - CB97 - 147797
226TYRTYRCAPCAPAA - R97 - 147797
117PHEPHEPROPROGG13 - 8913 - 89
217PHEPHEPROPROAA13 - 8913 - 89
127TYRTYRCAPCAPGG - KB97 - 147797
227TYRTYRCAPCAPAA - R97 - 147797
118PHEPHEPROPROHH13 - 8913 - 89
218PHEPHEPROPROAA13 - 8913 - 89
128TYRTYRCAPCAPHH - RB97 - 147797
228TYRTYRCAPCAPAA - R97 - 147797
119MMEMMEVALVALII1 - 1401 - 140
1110MMEMMEVALVALJJ1 - 1401 - 140
2110MMEMMEVALVALII1 - 1401 - 140
1111MMEMMEVALVALKK1 - 1401 - 140
2111MMEMMEVALVALII1 - 1401 - 140
1112MMEMMEVALVALLL1 - 1401 - 140
2112MMEMMEVALVALII1 - 1401 - 140
1113MMEMMEVALVALMM1 - 1401 - 140
2113MMEMMEVALVALII1 - 1401 - 140
1114MMEMMEVALVALNN1 - 1401 - 140
2114MMEMMEVALVALII1 - 1401 - 140
1115MMEMMEVALVALOO1 - 1401 - 140
2115MMEMMEVALVALII1 - 1401 - 140
1116MMEMMEVALVALPP1 - 1401 - 140
2116MMEMMEVALVALII1 - 1401 - 140

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.1053, 0.7043, -0.7021), (0.7036, -0.5517, -0.4479), (-0.7028, -0.4468, -0.5536)51.25, 150, 231
3given(0.4309, -0.05809, 0.9005), (-0.8029, 0.4308, 0.412), (-0.4119, -0.9006, 0.139)-43.37, 66.21, 193.1
4given(-0.6287, -0.06755, -0.7747), (-0.06845, -0.9875, 0.1417), (-0.7746, 0.1421, 0.6162)178, 184.9, 69.14
5given(-0.1394, -0.8606, 0.4898), (-0.8606, -0.1394, -0.4898), (0.4898, -0.4898, -0.7213)107.8, 209.2, 178.1
6given(-0.9646, 0.1562, 0.2127), (0.1564, -0.3107, 0.9375), (0.2125, 0.9376, 0.2753)84.8, 31.03, -36.92
7given(0.4303, -0.8034, -0.4117), (-0.05574, 0.4315, -0.9004), (0.901, 0.4104, 0.1409)151.3, 142.5, -15.06
8given(-0.2322, 0.9293, 0.2873), (0.9303, 0.1259, 0.3446), (0.2841, 0.3473, -0.8937)-42.22, -3.615, 125
9given(0.1037, 0.7051, -0.7015), (0.7046, -0.5499, -0.4485), (-0.7019, -0.4478, -0.5539)51.09, 149.9, 231.1
10given(0.4295, -0.05976, 0.9011), (-0.8038, 0.4295, 0.4116), (-0.4116, -0.9011, 0.1365)-43.19, 66.39, 193.4
11given(-0.6291, -0.06781, -0.7744), (-0.06893, -0.9874, 0.1425), (-0.7743, 0.143, 0.6165)178, 184.7, 69.03
12given(-0.1391, -0.8603, 0.4905), (-0.861, -0.1396, -0.4891), (0.4893, -0.4903, -0.7212)107.7, 209.1, 178.2
13given(-0.9645, 0.157, 0.2123), (0.156, -0.31, 0.9378), (0.213, 0.9377, 0.2745)84.77, 30.94, -36.88
14given(0.4305, -0.8024, -0.4133), (-0.05484, 0.4338, -0.8993), (0.9009, 0.4098, 0.1428)151.4, 142.2, -15.17
15given(-0.2304, 0.9293, 0.2885), (0.9301, 0.1233, 0.3459), (0.2859, 0.3481, -0.8928)-42.37, -3.381, 124.7

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Components

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RIBULOSE BISPHOSPHATE CARBOXYLASE ... , 2 types, 16 molecules ABCDEFGHIJKLMNOP

#1: Protein
RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN / RIBULOSE-1 / 5-BISPHOSPHATE CARBOXYLASE LARGE CHAIN


Mass: 52698.816 Da / Num. of mol.: 8 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Strain: 2137 / Production host: ESCHERICHIA COLI (E. coli)
References: UniProt: P00877, ribulose-bisphosphate carboxylase
#2: Protein
RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1 / RUBISCO SMALL SUBUNIT 1 / RIBULOSE-1 / 5-BISPHOSPHATE CARBOXYLASE SMALL CHAIN


Mass: 16283.806 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Strain: 2137 / Production host: ESCHERICHIA COLI (E. coli)
References: UniProt: P00873, ribulose-bisphosphate carboxylase

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Sugars , 1 types, 8 molecules

#4: Sugar
ChemComp-CAP / 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE


Type: saccharide / Mass: 356.115 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C6H14O13P2

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Non-polymers , 3 types, 3559 molecules

#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Mg
#5: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 59 / Source method: obtained synthetically / Formula: C2H6O2
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 3492 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN A, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN A, GLY 344 TO SER ...ENGINEERED RESIDUE IN CHAIN A, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN A, GLY 344 TO SER ENGINEERED RESIDUE IN CHAIN B, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN B, GLY 344 TO SER ENGINEERED RESIDUE IN CHAIN C, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN C, GLY 344 TO SER ENGINEERED RESIDUE IN CHAIN D, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN D, GLY 344 TO SER ENGINEERED RESIDUE IN CHAIN E, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN E, GLY 344 TO SER ENGINEERED RESIDUE IN CHAIN F, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN F, GLY 344 TO SER ENGINEERED RESIDUE IN CHAIN G, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN G, GLY 344 TO SER ENGINEERED RESIDUE IN CHAIN H, VAL 331 TO ALA ENGINEERED RESIDUE IN CHAIN H, GLY 344 TO SER
Sequence detailsTHE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877) HAS A VARIANT (LEU46PRO) WHICH OCCURS IN ...THE UNIPROT DATABASE ENTRY FOR THIS SEQUENCE (P00877) HAS A VARIANT (LEU46PRO) WHICH OCCURS IN STRAIN 21GR AND 2137.

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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: 2.17 Å3/Da / Density % sol: 42.92 % / Description: NONE
Crystal growpH: 7.5 / Details: pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-3 / Wavelength: 0.931
DetectorType: ADSC CCD / Detector: CCD / Date: Nov 20, 2004
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.931 Å / Relative weight: 1
ReflectionResolution: 1.5→30 Å / Num. obs: 781039 / % possible obs: 96 % / Redundancy: 31.2 % / Rmerge(I) obs: 0.08 / Net I/σ(I): 20
Reflection shellResolution: 1.5→1.54 Å / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 1.9 / % possible all: 89.9

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Processing

Software
NameVersionClassification
REFMAC5.2.0019refinement
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1GK8

1gk8


Resolution: 1.5→30 Å / Cor.coef. Fo:Fc: 0.97 / Cor.coef. Fo:Fc free: 0.965 / SU B: 1.204 / SU ML: 0.045 / Cross valid method: THROUGHOUT / ESU R: 0.074 / ESU R Free: 0.071 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.192 39244 5 %RANDOM
Rwork0.176 ---
obs0.177 740735 95.7 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 19.23 Å2
Baniso -1Baniso -2Baniso -3
1-0.34 Å20 Å20 Å2
2--0.49 Å20 Å2
3----0.84 Å2
Refinement stepCycle: LAST / Resolution: 1.5→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms38207 0 412 3492 42111
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.02239827
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2861.9653897
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.96354833
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.13623.2481878
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.021156460
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.4515312
X-RAY DIFFRACTIONr_chiral_restr0.0880.25701
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0230552
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1990.220657
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3090.227474
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1080.23474
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2140.263
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1710.216
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.7191.524714
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.122238792
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.832317315
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it2.8014.515105
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

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

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1825tight positional00.05
2B1825tight positional0.030.05
3C1825tight positional0.020.05
4D1825tight positional0.030.05
5E1825tight positional0.020.05
6F1825tight positional0.020.05
7G1825tight positional0.050.05
8H1825tight positional0.030.05
9I560tight positional00.05
10J560tight positional0.050.05
11K560tight positional0.020.05
12L560tight positional0.020.05
13M560tight positional0.030.05
14N560tight positional0.020.05
15O560tight positional0.020.05
16P560tight positional0.040.05
1A1783medium positional00.5
2B1782medium positional0.150.5
3C1774medium positional0.180.5
4D1777medium positional0.20.5
5E1780medium positional0.180.5
6F1780medium positional0.180.5
7G1780medium positional0.20.5
8H1773medium positional0.180.5
9I587medium positional00.5
10J579medium positional0.250.5
11K569medium positional0.230.5
12L566medium positional0.240.5
13M567medium positional0.460.5
14N565medium positional0.250.5
15O573medium positional0.230.5
16P569medium positional0.280.5
1A1825tight thermal00.5
2B1825tight thermal0.140.5
3C1825tight thermal0.180.5
4D1825tight thermal0.160.5
5E1825tight thermal0.140.5
6F1825tight thermal0.130.5
7G1825tight thermal0.20.5
8H1825tight thermal0.150.5
9I560tight thermal00.5
10J560tight thermal0.160.5
11K560tight thermal0.140.5
12L560tight thermal0.110.5
13M560tight thermal0.240.5
14N560tight thermal0.110.5
15O560tight thermal0.130.5
16P560tight thermal0.140.5
1A1783medium thermal02
2B1782medium thermal0.432
3C1774medium thermal0.482
4D1777medium thermal0.472
5E1780medium thermal0.422
6F1780medium thermal0.42
7G1780medium thermal0.462
8H1773medium thermal0.432
9I587medium thermal02
10J579medium thermal0.432
11K569medium thermal0.362
12L566medium thermal0.372
13M567medium thermal0.552
14N565medium thermal0.362
15O573medium thermal0.412
16P569medium thermal0.412
LS refinement shellResolution: 1.5→1.54 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.269 2655
Rwork0.255 50643

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