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- PDB-3zlj: CRYSTAL STRUCTURE OF FULL-LENGTH E.COLI DNA MISMATCH REPAIR PROTE... -

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Basic information

Entry
Database: PDB / ID: 3zlj
TitleCRYSTAL STRUCTURE OF FULL-LENGTH E.COLI DNA MISMATCH REPAIR PROTEIN MUTS D835R MUTANT IN COMPLEX WITH GT MISMATCHED DNA
Components
  • (DNA MISMATCH REPAIR PROTEIN MUTS) x 2
  • 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP *AP*GP*TP*GP*TP*CP*AP)-3'
  • 5'-D(*TP*GP*AP*CP*AP*CP*TP*GP*GP*TP*GP*CP*TP*TP *GP*GP*CP*AP*GP*CP*TP)-3'
KeywordsDNA BINDING PROTEIN/DNA / DNA BINDING PROTEIN-DNA COMPLEX / DIMER MUTANT / MISMATCH REPAIR / DNA REPAIR PROTEIN / DNA DAMAGE / NUCLEOTIDE-BINDING / ATP-BINDING
Function / homology
Function and homology information


adenine/cytosine mispair binding / MutS complex / mismatch repair complex / regulation of DNA recombination / mismatched DNA binding / DNA binding, bending / ATP-dependent DNA damage sensor activity / mismatch repair / ADP binding / damaged DNA binding ...adenine/cytosine mispair binding / MutS complex / mismatch repair complex / regulation of DNA recombination / mismatched DNA binding / DNA binding, bending / ATP-dependent DNA damage sensor activity / mismatch repair / ADP binding / damaged DNA binding / DNA damage response / ATP hydrolysis activity / ATP binding / identical protein binding / cytosol
Similarity search - Function
MutS, DNA mismatch repair protein; Chain A, domain 3 / MutS, DNA mismatch repair protein; Chain A, domain 3 - #10 / MutS, connector domain / DNA repair protein MutS, domain I / DNA mismatch repair protein MutS / DNA mismatch repair protein MutS/MSH / DNA mismatch repair protein MutS-like, N-terminal / DNA mismatch repair protein MutS, connector domain / DNA mismatch repair protein MutS, clamp / DNA mismatch repair protein MutS, N-terminal ...MutS, DNA mismatch repair protein; Chain A, domain 3 / MutS, DNA mismatch repair protein; Chain A, domain 3 - #10 / MutS, connector domain / DNA repair protein MutS, domain I / DNA mismatch repair protein MutS / DNA mismatch repair protein MutS/MSH / DNA mismatch repair protein MutS-like, N-terminal / DNA mismatch repair protein MutS, connector domain / DNA mismatch repair protein MutS, clamp / DNA mismatch repair protein MutS, N-terminal / MutS, connector domain superfamily / MutS domain I / MutS domain II / MutS family domain IV / MutS domain III / DNA mismatch repair MutS family / DNA mismatch repair protein MutS, C-terminal / DNA mismatch repair protein MutS, core / DNA mismatch repair protein MutS, core domain superfamily / MutS domain V / DNA mismatch repair proteins mutS family signature. / DNA-binding domain of DNA mismatch repair MUTS family / ATPase domain of DNA mismatch repair MUTS family / MutS, DNA mismatch repair protein, domain I / Nucleotidyltransferase; domain 5 / P-loop containing nucleotide triphosphate hydrolases / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
DNA / DNA (> 10) / DNA mismatch repair protein MutS
Similarity search - Component
Biological speciesESCHERICHIA COLI K-12 (bacteria)
SYNTHETIC CONSTRUCT (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsGroothuizen, F.S. / Fish, A. / Petoukhov, M.V. / Reumer, A. / Manelyte, L. / Winterwerp, H.H.K. / Marinus, M.G. / Lebbink, J.H.G. / Svergun, D.I. / Friedhoff, P. / Sixma, T.K.
CitationJournal: Nucleic Acids Res / Year: 2013
Title: Using stable MutS dimers and tetramers to quantitatively analyze DNA mismatch recognition and sliding clamp formation.
Authors: Flora S Groothuizen / Alexander Fish / Maxim V Petoukhov / Annet Reumer / Laura Manelyte / Herrie H K Winterwerp / Martin G Marinus / Joyce H G Lebbink / Dmitri I Svergun / Peter Friedhoff / Titia K Sixma /
Abstract: The process of DNA mismatch repair is initiated when MutS recognizes mismatched DNA bases and starts the repair cascade. The Escherichia coli MutS protein exists in an equilibrium between dimers and ...The process of DNA mismatch repair is initiated when MutS recognizes mismatched DNA bases and starts the repair cascade. The Escherichia coli MutS protein exists in an equilibrium between dimers and tetramers, which has compromised biophysical analysis. To uncouple these states, we have generated stable dimers and tetramers, respectively. These proteins allowed kinetic analysis of DNA recognition and structural analysis of the full-length protein by X-ray crystallography and small angle X-ray scattering. Our structural data reveal that the tetramerization domains are flexible with respect to the body of the protein, resulting in mostly extended structures. Tetrameric MutS has a slow dissociation from DNA, which can be due to occasional bending over and binding DNA in its two binding sites. In contrast, the dimer dissociation is faster, primarily dependent on a combination of the type of mismatch and the flanking sequence. In the presence of ATP, we could distinguish two kinetic groups: DNA sequences where MutS forms sliding clamps and those where sliding clamps are not formed efficiently. Interestingly, this inability to undergo a conformational change rather than mismatch affinity is correlated with mismatch repair.
History
DepositionFeb 1, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 17, 2013Provider: repository / Type: Initial release
Revision 1.1Oct 30, 2013Group: Database references
Revision 1.2Jan 30, 2019Group: Data collection / Experimental preparation / Other
Category: exptl_crystal_grow / pdbx_database_proc ...exptl_crystal_grow / pdbx_database_proc / pdbx_database_status / pdbx_seq_map_depositor_info
Item: _exptl_crystal_grow.method / _pdbx_database_status.recvd_author_approval / _pdbx_seq_map_depositor_info.one_letter_code_mod
Revision 1.3Feb 6, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.temp
Revision 1.4Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / 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 / 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 / _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: DNA MISMATCH REPAIR PROTEIN MUTS
B: DNA MISMATCH REPAIR PROTEIN MUTS
C: DNA MISMATCH REPAIR PROTEIN MUTS
D: DNA MISMATCH REPAIR PROTEIN MUTS
E: 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP *AP*GP*TP*GP*TP*CP*AP)-3'
F: 5'-D(*TP*GP*AP*CP*AP*CP*TP*GP*GP*TP*GP*CP*TP*TP *GP*GP*CP*AP*GP*CP*TP)-3'


Theoretical massNumber of molelcules
Total (without water)203,7356
Polymers203,7356
Non-polymers00
Water00
1
A: DNA MISMATCH REPAIR PROTEIN MUTS
B: DNA MISMATCH REPAIR PROTEIN MUTS
E: 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP *AP*GP*TP*GP*TP*CP*AP)-3'
F: 5'-D(*TP*GP*AP*CP*AP*CP*TP*GP*GP*TP*GP*CP*TP*TP *GP*GP*CP*AP*GP*CP*TP)-3'


Theoretical massNumber of molelcules
Total (without water)192,1124
Polymers192,1124
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10360 Å2
ΔGint-70.2 kcal/mol
Surface area69490 Å2
MethodPISA
2
C: DNA MISMATCH REPAIR PROTEIN MUTS
D: DNA MISMATCH REPAIR PROTEIN MUTS


Theoretical massNumber of molelcules
Total (without water)11,6232
Polymers11,6232
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1610 Å2
ΔGint-19.6 kcal/mol
Surface area4670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)110.288, 91.152, 112.855
Angle α, β, γ (deg.)90.00, 101.79, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12C
22D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUILEILEAA26 - 79926 - 799
21GLUGLUILEILEBB26 - 79926 - 799
12SERSERVALVALCC823 - 85323 - 53
22SERSERVALVALDD823 - 85323 - 53

NCS ensembles :
ID
1
2

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Components

#1: Protein DNA MISMATCH REPAIR PROTEIN MUTS


Mass: 89604.359 Da / Num. of mol.: 2 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ESCHERICHIA COLI K-12 (bacteria) / Production host: ESCHERICHIA COLI B (bacteria) / Strain (production host): B834(DE3) / Variant (production host): PLYSS / References: UniProt: P23909
#2: Protein DNA MISMATCH REPAIR PROTEIN MUTS


Mass: 5811.530 Da / Num. of mol.: 2 / Mutation: YES
Source method: isolated from a genetically manipulated source
Details: CHAINS C AND D ARE THE C-TERMINAL PORTION OF CHAINS A AND B, HOWEVER THE MISSING REGION 800-822 MAKES UNAMBIGUOUS ASSIGNMENT TO THE CORRECT CHAIN IMPOSSIBLE
Source: (gene. exp.) ESCHERICHIA COLI K-12 (bacteria) / Production host: ESCHERICHIA COLI B (bacteria) / Strain (production host): B834(DE3) / Variant (production host): PLYSS / References: UniProt: P23909
#3: DNA chain 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*GP*GP*CP*AP*CP*CP *AP*GP*TP*GP*TP*CP*AP)-3'


Mass: 6433.162 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others)
#4: DNA chain 5'-D(*TP*GP*AP*CP*AP*CP*TP*GP*GP*TP*GP*CP*TP*TP *GP*GP*CP*AP*GP*CP*TP)-3'


Mass: 6470.169 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others)

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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: 2.72 Å3/Da / Density % sol: 59.7 % / Description: NONE
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 5MM TRIS PH8, 750MM NACL, 12% PEG 6000, 10MM MGCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.976
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: May 2, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.976 Å / Relative weight: 1
ReflectionResolution: 3.1→47.24 Å / Num. obs: 40031 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 4.4 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 9.9
Reflection shellResolution: 3.1→3.27 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 2.4 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.7.0032refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1E3M

1e3m


Resolution: 3.1→46.49 Å / Cor.coef. Fo:Fc: 0.917 / Cor.coef. Fo:Fc free: 0.884 / SU B: 49.479 / SU ML: 0.38 / Cross valid method: THROUGHOUT / ESU R Free: 0.49 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.26283 2006 5 %RANDOM
Rwork0.22734 ---
obs0.22912 37981 99.84 %-
Solvent computationIon probe radii: 0.9 Å / Shrinkage radii: 0.9 Å / VDW probe radii: 1 Å / Solvent model: MASK
Displacement parametersBiso mean: 61.792 Å2
Baniso -1Baniso -2Baniso -3
1-3.55 Å20 Å2-0.71 Å2
2---4.3 Å20 Å2
3---0.82 Å2
Refinement stepCycle: LAST / Resolution: 3.1→46.49 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12499 734 0 0 13233
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0060.01913527
X-RAY DIFFRACTIONr_bond_other_d0.0030.0212824
X-RAY DIFFRACTIONr_angle_refined_deg1.0021.92418463
X-RAY DIFFRACTIONr_angle_other_deg0.919329418
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.01151575
X-RAY DIFFRACTIONr_dihedral_angle_2_deg32.73523.471605
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.262152266
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.19215131
X-RAY DIFFRACTIONr_chiral_restr0.0540.22067
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02114800
X-RAY DIFFRACTIONr_gen_planes_other0.0020.023063
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

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A439890.12
12B439890.12
21C13650.2
22D13650.2
LS refinement shellResolution: 3.1→3.181 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.353 156 -
Rwork0.31 2790 -
obs--100 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.77220.0090.64791.75770.52234.0585-0.01330.05130.2990.09350.14570.3649-0.4976-0.037-0.13240.32930.02070.0120.1741-0.01240.2959-34.214640.2064-15.3162
22.89590.84280.54363.8686-0.79794.16330.2265-0.1954-0.17070.2851-0.04590.1518-0.10150.0738-0.18050.07730.00990.02660.1128-0.02620.124-23.67615.1968-2.8096
33.9778-1.6151.08271.0363-0.92761.99480.20250.2859-0.2719-0.2612-0.03370.37560.2761-0.0744-0.16880.2318-0.0584-0.07070.1876-0.04990.3205-31.83313.0839-22.8611
44.79721.73531.26134.3179-0.35275.8192-0.16870.1713-0.0589-0.85460.12980.54360.0511-0.47010.0390.52970.0532-0.29430.5155-0.0960.5338-59.592439.5033-50.4545
50.71070.36920.39590.5646-0.42682.22260.09990.1538-0.0904-0.03540.26470.36550.2766-0.253-0.36460.0635-0.0904-0.02480.30650.04960.6441-39.11677.2112-23.0204
64.97330.85741.76682.08550.94761.8860.10170.3822-0.1776-0.1712-0.0539-0.3559-0.18810.2377-0.04780.24170.06960.12270.20010.03530.19695.2443-4.3576-11.4122
73.1057-0.89120.29592.7228-5.329413.27780.1465-0.3248-0.3578-0.017-0.0125-0.24060.36550.5924-0.13410.50660.04710.22180.2698-0.17250.818331.19033.4852-21.7749
85.2977-1.1278-0.89180.30970.17440.1642-0.09870.3606-0.34310.35430.0086-0.0139-0.0275-0.17660.09011.57260.0045-0.46451.10660.0491.0793-15.702728.4125-42.6905
94.9864-3.1258-0.37594.3907-1.04343.69120.84711.0308-0.6573-1.3813-0.58580.21580.6150.1919-0.26121.09280.1346-0.07790.4778-0.16260.22969.905331.4544-47.5947
102.6634-2.20361.79113.2591-1.63381.61-0.00870.21760.2098-0.4379-0.0262-0.0817-0.03510.07990.03480.4315-0.01370.04580.24770.0180.05945.035852.5363-35.2365
117.47451.9152-3.39164.3015-1.51382.1866-0.02670.50660.4594-0.11330.01830.3967-0.236-0.15510.00840.570.0392-0.40850.4470.04290.6071-46.279861.5681-44.9135
120.6685-1.080.12852.1029-0.52060.90590.11480.29640.1708-0.4735-0.3471-0.15190.3240.13650.23240.4359-0.0604-0.02980.28470.18450.2445-0.25655.354-41.1571
131.7399-0.64860.25555.7613-0.83552.3624-0.14860.0235-0.4182-0.0938-0.0341-0.49080.09340.00030.18270.11480.02040.16260.28460.01760.299126.406825.5175-15.6982
1411.16864.6217-1.02316.30353.76446.02770.507-1.0537-0.7670.7055-0.836-1.05040.12920.23070.32910.4376-0.0252-0.21230.34610.42010.652619.14067.37644.3429
154.1781.0221-1.12290.3132-0.29150.3065-0.02580.010.3312-0.20570.0694-0.04820.0524-0.013-0.04351.2477-0.011-0.14311.00330.02140.905231.4669-20.1371-34.9909
161.63771.4412-0.10384.98158.712922.64990.19430.0013-0.3565-0.3378-0.6506-0.4324-0.7352-0.2780.45631.1250.05880.02011.41310.18691.068522.7167-15.5933-37.5698
170.4308-1.57760.59285.7862-2.16010.8425-0.17560.04950.1360.7305-0.1183-0.4603-0.20010.21930.29391.27350.2651-0.06211.48440.02381.02528.4267-5.6683-38.9888
183.11885.211-1.5918.7095-2.66310.82630.2947-0.223-0.20670.5724-0.3559-0.3564-0.29390.12030.06121.66240.2273-0.13031.3002-0.13240.782831.8592-14.4216-43.5517
195.1641-2.72645.16111.8353-2.98655.33140.37091.22630.2028-0.7422-0.6375-0.26320.75861.20180.26650.93390.0903-0.0180.6217-0.10550.3953-37.736640.8508-42.5196
202.91291.55710.97481.9584-1.3894.4983-0.2981-0.20161.44410.7854-0.03890.5953-1.6174-1.20780.3370.95630.2842-0.07150.73340.03991.1632-48.431156.4959-22.1969
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A2 - 115
2X-RAY DIFFRACTION2A116 - 266
3X-RAY DIFFRACTION3A267 - 443
4X-RAY DIFFRACTION4A444 - 512
5X-RAY DIFFRACTION5A513 - 567
6X-RAY DIFFRACTION6A568 - 768
7X-RAY DIFFRACTION7A769 - 800
8X-RAY DIFFRACTION8B14 - 115
9X-RAY DIFFRACTION9B116 - 266
10X-RAY DIFFRACTION10B267 - 443
11X-RAY DIFFRACTION11B444 - 512
12X-RAY DIFFRACTION12B513 - 567
13X-RAY DIFFRACTION13B568 - 768
14X-RAY DIFFRACTION14B769 - 800
15X-RAY DIFFRACTION15C820 - 838
16X-RAY DIFFRACTION16C839 - 853
17X-RAY DIFFRACTION17D820 - 838
18X-RAY DIFFRACTION18D839 - 853
19X-RAY DIFFRACTION19E1 - 8
20X-RAY DIFFRACTION19F14 - 21
21X-RAY DIFFRACTION20E9 - 20
22X-RAY DIFFRACTION20F2 - 13

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  • 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

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