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- PDB-4cr7: Crystal structure of the N-acetyl-D-mannosamine dehydrogenase wit... -

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Basic information

Entry
Database: PDB / ID: 4cr7
TitleCrystal structure of the N-acetyl-D-mannosamine dehydrogenase with n-acetylmannosamine
ComponentsN-ACYLMANNOSAMINE 1-DEHYDROGENASE
KeywordsOXIDOREDUCTASE / N-ACETYL-D-MANNOSAMINE DEHYDROGENASE / SHORT-CHAIN DEHYDROGENASE/REDUCTASE / SUBSTRATE SELECTIVITY
Function / homology
Function and homology information


N-acylmannosamine 1-dehydrogenase / N-acylmannosamine 1-dehydrogenase activity
Similarity search - Function
Short-chain dehydrogenase/reductase, conserved site / Short-chain dehydrogenases/reductases family signature. / Enoyl-(Acyl carrier protein) reductase / Short-chain dehydrogenase/reductase SDR / NAD(P)-binding Rossmann-like Domain / NAD(P)-binding domain superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
2-acetamido-2-deoxy-alpha-D-mannopyranose / alpha-D-mannopyranose / N-acylmannosamine 1-dehydrogenase
Similarity search - Component
Biological speciesFLAVOBACTERIUM SP. 141-8 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å
AuthorsGil-Ortiz, F. / Sola-Carvajal, A. / Garcia-Carmona, F. / Sanchez-Ferrer, A. / Rubio, V.
CitationJournal: Biochem.J. / Year: 2014
Title: Crystal Structures and Functional Studies Clarify Substrate Selectivity and Catalytic Residues for the Unique Orphan Enzyme N-Acetyl-D-Mannosamine Dehydrogenase.
Authors: Sola-Carvajal, A. / Gil-Ortiz, F. / Garcia-Carmona, F. / Rubio, V. / Sanchez-Ferrer, A.
History
DepositionFeb 25, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 9, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 3, 2014Group: Atomic model / Database references
Revision 1.2Jul 29, 2020Group: Advisory / Data collection ...Advisory / Data collection / Derived calculations / Other / Structure summary
Category: chem_comp / database_PDB_caveat ...chem_comp / database_PDB_caveat / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Dec 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
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.
Remark 700 SHEET DETERMINATION METHOD: AUTHOR PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
B: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
C: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
D: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
E: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
F: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
G: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
H: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
I: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
J: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
K: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
L: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
M: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
N: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
O: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
P: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)446,90550
Polymers439,92616
Non-polymers6,97934
Water14,610811
1
N: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

H: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

A: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
K: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,62912
Polymers109,9814
Non-polymers1,6488
Water724
TypeNameSymmetry operationNumber
crystal symmetry operation1_544x,y-1,z-11
crystal symmetry operation1_444x-1,y-1,z-11
identity operation1_555x,y,z1
Buried area22080 Å2
ΔGint-79.7 kcal/mol
Surface area31120 Å2
MethodPISA
2
N: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

H: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

A: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
K: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,62912
Polymers109,9814
Non-polymers1,6488
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_455x-1,y,z1
crystal symmetry operation1_566x,y+1,z+11
Buried area22080 Å2
ΔGint-79.7 kcal/mol
Surface area31120 Å2
MethodPISA
3
H: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

N: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

A: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
K: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,62912
Polymers109,9814
Non-polymers1,6488
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_655x+1,y,z1
crystal symmetry operation1_666x+1,y+1,z+11
Buried area22080 Å2
ΔGint-79.7 kcal/mol
Surface area31120 Å2
MethodPISA
4
G: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

B: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
L: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
M: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,43511
Polymers109,9814
Non-polymers1,4537
Water724
TypeNameSymmetry operationNumber
crystal symmetry operation1_455x-1,y,z1
identity operation1_555x,y,z1
Buried area21610 Å2
ΔGint-82.4 kcal/mol
Surface area31290 Å2
MethodPISA
5
G: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

B: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
L: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
M: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,43511
Polymers109,9814
Non-polymers1,4537
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_655x+1,y,z1
Buried area21610 Å2
ΔGint-82.4 kcal/mol
Surface area31290 Å2
MethodPISA
6
D: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
F: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

I: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
O: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,21215
Polymers109,9814
Non-polymers2,23011
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_556x,y,z+11
Buried area23410 Å2
ΔGint-67.6 kcal/mol
Surface area30720 Å2
MethodPISA
7
I: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
O: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

D: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
F: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)112,21215
Polymers109,9814
Non-polymers2,23011
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_554x,y,z-11
Buried area23410 Å2
ΔGint-67.6 kcal/mol
Surface area30720 Å2
MethodPISA
8
J: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
P: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

C: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
E: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,62912
Polymers109,9814
Non-polymers1,6488
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_565x,y+1,z1
Buried area22130 Å2
ΔGint-77.5 kcal/mol
Surface area30930 Å2
MethodPISA
9
C: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
E: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules

J: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
P: N-ACYLMANNOSAMINE 1-DEHYDROGENASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,62912
Polymers109,9814
Non-polymers1,6488
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_545x,y-1,z1
Buried area22130 Å2
ΔGint-77.5 kcal/mol
Surface area30930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.390, 100.120, 111.600
Angle α, β, γ (deg.)67.43, 89.75, 72.46
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31C
41D
51E
61F
71G
81H
91I
101J
111K
121L
131M
141N
151O
161P

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1113A1 - 500
2113B1 - 500
3113C1 - 500
4113D1 - 500
5113E1 - 500
6113F1 - 500
7113G1 - 500
8113H1 - 500
9113I1 - 500
10113J1 - 500
11113K1 - 500
12113L1 - 500
13113M1 - 500
14113N1 - 500
15113O1 - 500
16113P1 - 500

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.99871, -0.00714, -0.050279), (0.005444, 0.999414, -0.033785), (0.050491, 0.033468, 0.998164)-11.68071, -67.89104, -54.214
3given(0.998691, 0.048073, -0.017497), (-0.048819, 0.997793, -0.045016), (0.015294, 0.045812, 0.998833)-51.22853, -16.53643, -52.74891
4given(0.998148, 0.053407, 0.029135), (-0.052974, 0.998476, -0.015452), (-0.029916, 0.01388, 0.999456)-74.72613, -86.75063, -101.32802
5given(0.025226, 0.741576, 0.670394), (0.741597, -0.463581, 0.484899), (0.670372, 0.48493, -0.561645)-71.38992, -38.44244, -0.59922
6given(-0.010081, 0.721302, 0.692548), (0.722577, -0.473494, 0.503671), (0.691216, 0.505497, -0.516423)-156.43539, -41.93259, -24.66767
7given(0.088371, 0.732222, 0.675308), (0.730653, -0.508437, 0.455674), (0.677006, 0.453148, -0.579931)-115.6572, -57.05662, -63.70566
8given(0.048947, 0.709299, 0.703207), (0.708241, -0.521086, 0.476303), (0.704272, 0.474726, -0.52786)-197.74393, -53.41129, -88.80441
9given(-0.071517, -0.416546, -0.906297), (-0.36657, -0.834061, 0.412272), (-0.927638, 0.361706, -0.093044)45.46278, 84.90735, 55.73668
10given(-0.118753, -0.445896, -0.887172), (-0.349346, -0.817604, 0.457692), (-0.929438, 0.364282, -0.058679)128.21492, 121.57657, 47.19343
11given(-0.11779, -0.39809, -0.909753), (-0.398455, -0.8202, 0.410493), (-0.909593, 0.410848, -0.062009)21.12457, 21.14448, 11.21591
12given(-0.172252, -0.429009, -0.886724), (-0.379483, -0.801799, 0.461639), (-0.909022, 0.416015, -0.02469)98.9671, 58.76855, -3.10885
13given(-0.916305, -0.297398, 0.268215), (-0.358499, 0.310604, -0.880343), (0.178504, -0.902817, -0.391226)24.21751, 52.42711, 114.6111
14given(-0.928235, -0.312552, 0.201718), (-0.308366, 0.343215, -0.887194), (0.208062, -0.885728, -0.414965)55.65431, 75.56592, 194.71234
15given(-0.915291, -0.35946, 0.181743), (-0.301063, 0.310776, -0.901543), (0.267587, -0.87989, -0.39267)81.77698, 28.87226, 58.14145
16given(-0.907763, -0.345525, 0.237864), (-0.342501, 0.283103, -0.895849), (0.242198, -0.894687, -0.375332)105.86407, 64.17863, 138.37762

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Components

#1: Protein
N-ACYLMANNOSAMINE 1-DEHYDROGENASE / / NAMDH / NAM-DH / N-ACETYL-D-MANNOSAMINE DEHYDROGENASE


Mass: 27495.346 Da / Num. of mol.: 16
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) FLAVOBACTERIUM SP. 141-8 (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA2
References: UniProt: P22441, N-acylmannosamine 1-dehydrogenase
#2: Chemical
ChemComp-PG4 / TETRAETHYLENE GLYCOL / Polyethylene glycol


Mass: 194.226 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#3: Sugar
ChemComp-BM3 / 2-acetamido-2-deoxy-alpha-D-mannopyranose / N-acetyl-alpha-D-mannosamine / 2-acetamido-2-deoxy-alpha-D-mannose / 2-acetamido-2-deoxy-D-mannose / 2-acetamido-2-deoxy-mannose / 2-(ACETYLAMINO)-2-DEOXY-ALPHA-D-MANNOPYRANOSE


Type: D-saccharide, alpha linking / Mass: 221.208 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DManpNAcaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-a-D-mannopyranosamineCOMMON NAMEGMML 1.0
a-D-ManpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#4: Sugar
ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose / Mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 811 / 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: 2.2 Å3/Da / Density % sol: 44 % / Description: NONE
Crystal growpH: 8
Details: 0.1 M HEPES, PH 7.5 AND 30% (W/V) PEG [POLY(ETHYLENE GLYCOL)] 300

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Data collection

DiffractionMean temperature: 294 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9724
DetectorType: ADSC QUANTUM 210r / Detector: CCD / Date: Jun 8, 2011
RadiationMonochromator: CHANEL-CUT / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9724 Å / Relative weight: 1
ReflectionResolution: 2.15→15 Å / Num. obs: 189715 / % possible obs: 96.9 % / Observed criterion σ(I): 2 / Redundancy: 2.5 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 5.2
Reflection shellResolution: 2.15→2.27 Å / Redundancy: 2.6 % / Rmerge(I) obs: 0.36 / Mean I/σ(I) obs: 1.7 / % possible all: 97.8

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Processing

Software
NameVersionClassification
REFMAC5.6.0117refinement
MOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2D1Y

2d1y


Resolution: 2.15→15 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.935 / SU B: 5.059 / SU ML: 0.132 / Cross valid method: THROUGHOUT / ESU R: 0.295 / ESU R Free: 0.204 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
RfactorNum. reflection% reflectionSelection details
Rfree0.23102 10032 5 %RANDOM
Rwork0.20074 ---
obs0.20225 189715 97.73 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 22.534 Å2
Baniso -1Baniso -2Baniso -3
1--0.38 Å22 Å20.21 Å2
2---1.81 Å21.34 Å2
3----0.06 Å2
Refinement stepCycle: LAST / Resolution: 2.15→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms29105 0 392 811 30308
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01929861
X-RAY DIFFRACTIONr_bond_other_d0.0030.0219585
X-RAY DIFFRACTIONr_angle_refined_deg1.3331.98540446
X-RAY DIFFRACTIONr_angle_other_deg1.0683.00647567
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.18454120
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.80422.4671046
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.254154414
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.48715290
X-RAY DIFFRACTIONr_chiral_restr0.0810.24796
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02134281
X-RAY DIFFRACTIONr_gen_planes_other0.0020.026077
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
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

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

Dom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1417loose positional0.065
2B1417loose positional0.035
3C1417loose positional0.035
4D1417loose positional0.035
5E1417loose positional0.035
6F1417loose positional0.035
7G1417loose positional0.035
8H1417loose positional0.035
9I1417loose positional0.035
10J1417loose positional0.035
11K1417loose positional0.035
12L1417loose positional0.035
13M1417loose positional0.035
14N1417loose positional0.035
15O1417loose positional0.035
16P1417loose positional0.035
1A1473tight thermal2.930.5
2B1473tight thermal2.060.5
3C1473tight thermal2.160.5
4D1473tight thermal2.830.5
5E1473tight thermal2.520.5
6F1473tight thermal3.490.5
7G1473tight thermal2.340.5
8H1473tight thermal2.440.5
9I1473tight thermal2.520.5
10J1473tight thermal2.610.5
11K1473tight thermal2.420.5
12L1473tight thermal2.530.5
13M1473tight thermal2.610.5
14N1473tight thermal2.480.5
15O1473tight thermal1.950.5
16P1473tight thermal2.590.5
1A1417loose thermal2.9410
2B1417loose thermal2.7510
3C1417loose thermal2.6710
4D1417loose thermal3.0310
5E1417loose thermal2.8210
6F1417loose thermal4.0110
7G1417loose thermal2.7410
8H1417loose thermal2.7910
9I1417loose thermal2.7710
10J1417loose thermal2.8910
11K1417loose thermal2.810
12L1417loose thermal2.8910
13M1417loose thermal2.9810
14N1417loose thermal2.6910
15O1417loose thermal2.8910
16P1417loose thermal310
LS refinement shellResolution: 2.15→2.205 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.291 699 -
Rwork0.266 13616 -
obs--96.82 %

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