[English] 日本語
Yorodumi
- PDB-6dz4: Crystal structure of Salmonella typhimurium Tryptophan Synthase w... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6dz4
TitleCrystal structure of Salmonella typhimurium Tryptophan Synthase with sodium ion at the metal coordination site and (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine at the beta-site
Components(Tryptophan synthase ...) x 2
KeywordsLYASE/LYASE Inhibitor / F9F / LYASE-LYASE Inhibitor complex
Function / homology
Function and homology information


tryptophan synthase / tryptophan synthase activity / L-tryptophan biosynthetic process / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Tryptophan synthase, alpha chain / Tryptophan synthase, alpha chain, active site / Tryptophan synthase alpha chain / Tryptophan synthase alpha chain signature. / Tryptophan synthase, beta chain, conserved site / Tryptophan synthase, beta chain / Tryptophan synthase beta chain/beta chain-like / Tryptophan synthase beta chain pyridoxal-phosphate attachment site. / Rossmann fold - #1100 / Pyridoxal-phosphate dependent enzyme ...Tryptophan synthase, alpha chain / Tryptophan synthase, alpha chain, active site / Tryptophan synthase alpha chain / Tryptophan synthase alpha chain signature. / Tryptophan synthase, beta chain, conserved site / Tryptophan synthase, beta chain / Tryptophan synthase beta chain/beta chain-like / Tryptophan synthase beta chain pyridoxal-phosphate attachment site. / Rossmann fold - #1100 / Pyridoxal-phosphate dependent enzyme / Pyridoxal-phosphate dependent enzyme / Tryptophan synthase beta subunit-like PLP-dependent enzyme / Ribulose-phosphate binding barrel / Aldolase class I / Aldolase-type TIM barrel / TIM Barrel / Alpha-Beta Barrel / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Chem-KOU / Tryptophan synthase alpha chain / Tryptophan synthase beta chain
Similarity search - Component
Biological speciesSalmonella typhimurium (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.45 Å
AuthorsHilario, E. / Dunn, M.F. / Mueller, L.J. / Fan, L.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)2R01GM097569-06A1 United States
CitationJournal: To be Published
Title: Crystal structure of Salmonella typhimurium Tryptophan Synthase with sodium ion at the metal coordination site and (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)- ...Title: Crystal structure of Salmonella typhimurium Tryptophan Synthase with sodium ion at the metal coordination site and (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine at the beta site
Authors: Hilario, E. / Dunn, M.F. / Mueller, L.J. / Fan, L.
History
DepositionJul 2, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 10, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0May 6, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / citation / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / struct / struct_keywords / struct_site
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.pdbx_synonyms / _chem_comp.type / _citation.title / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _struct.title / _struct_keywords.pdbx_keywords / _struct_keywords.text / _struct_site.details / _struct_site.pdbx_auth_comp_id
Revision 3.0Jun 10, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Author supporting evidence / Data collection / Derived calculations / Refinement description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / computing / diffrn / entity / pdbx_entity_instance_feature / pdbx_entity_nonpoly / pdbx_entry_details / pdbx_nonpoly_scheme / pdbx_refine_tls / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_validate_close_contact / refine / refine_hist / reflns / reflns_shell / struct_asym / struct_conn / struct_keywords / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_alt_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.occupancy / _atom_site.type_symbol / _diffrn.ambient_temp_details / _diffrn.pdbx_serial_crystal_experiment / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.auth_mon_id / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.entity_id / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_id / _pdbx_refine_tls.origin_x / _pdbx_refine_tls.origin_y / _pdbx_refine_tls.origin_z / _pdbx_struct_assembly_prop.value / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_validate_close_contact.auth_seq_id_1 / _refine.ls_wR_factor_R_free / _refine.ls_wR_factor_R_work / _refine.overall_FOM_work_R_set / _refine.overall_SU_R_free / _refine.pdbx_stereochemistry_target_values / _refine.solvent_model_details / _refine_hist.pdbx_B_iso_mean_ligand / _reflns.number_all / _reflns_shell.number_measured_all / _reflns_shell.pdbx_netI_over_sigmaI_obs / _struct_asym.entity_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_keywords.text / _struct_site.details / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id / _struct_site.pdbx_num_residues / _struct_site_gen.auth_asym_id / _struct_site_gen.auth_comp_id / _struct_site_gen.auth_seq_id / _struct_site_gen.label_asym_id / _struct_site_gen.label_comp_id / _struct_site_gen.label_seq_id / _struct_site_gen.pdbx_num_res / _struct_site_gen.site_id / _struct_site_gen.symmetry
Description: Model orientation/position
Details: We have flipped the side chain of residue Q114 from chain B and the current orientation makes more sense regarding local hydrogen bonding.
Provider: author / Type: Coordinate replacement
Revision 3.1Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
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_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Tryptophan synthase alpha chain
B: Tryptophan synthase beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)73,21925
Polymers71,6182
Non-polymers1,60123
Water13,295738
1
A: Tryptophan synthase alpha chain
B: Tryptophan synthase beta chain
hetero molecules

A: Tryptophan synthase alpha chain
B: Tryptophan synthase beta chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,43850
Polymers143,2354
Non-polymers3,20346
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-x,y,-z1
Buried area14350 Å2
ΔGint-158 kcal/mol
Surface area44610 Å2
MethodPISA
Unit cell
Length a, b, c (Å)182.509, 59.300, 67.325
Angle α, β, γ (deg.)90.000, 94.690, 90.000
Int Tables number5
Space group name H-MC121

-
Components

-
Tryptophan synthase ... , 2 types, 2 molecules AB

#1: Protein Tryptophan synthase alpha chain


Mass: 28698.797 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (bacteria)
Strain: LT2 / SGSC1412 / ATCC 700720 / Gene: trpA, STM1727 / Plasmid: PEBA-10 / Production host: Escherichia coli (E. coli) / Strain (production host): CB149 / References: UniProt: P00929, tryptophan synthase
#2: Protein Tryptophan synthase beta chain


Mass: 42918.879 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (bacteria)
Strain: LT2 / SGSC1412 / ATCC 700720 / Gene: trpB, STM1726 / Plasmid: PEBA-10 / Production host: Escherichia coli (E. coli) / Strain (production host): CB149 / References: UniProt: P0A2K1, tryptophan synthase

-
Non-polymers , 5 types, 761 molecules

#3: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Cl
#4: Chemical
ChemComp-DMS / DIMETHYL SULFOXIDE


Mass: 78.133 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#5: Chemical ChemComp-KOU / (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-serine


Mass: 334.219 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H15N2O8P / Feature type: SUBJECT OF INVESTIGATION
#6: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na / Feature type: SUBJECT OF INVESTIGATION
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 738 / Source method: isolated from a natural source / Formula: H2O

-
Details

Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.54 Å3/Da / Density % sol: 51.48 % / Description: Large plate-like crystal.
Crystal growTemperature: 297 K / Method: vapor diffusion, sitting drop / pH: 7.8
Details: 50mM Bicine-NaOH, pH 7.8, containing 9% PEG3350, 50mM NaCl, 2mM spermine
PH range: 7.6-8.0

-
Data collection

DiffractionMean temperature: 100 K / Ambient temp details: constant / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 12.3.1 / Wavelength: 0.9793 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 19, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 1.45→30 Å / Num. all: 126505 / Num. obs: 126505 / % possible obs: 99.5 % / Redundancy: 5.6 % / CC1/2: 0.998 / Rmerge(I) obs: 0.085 / Rpim(I) all: 0.039 / Rrim(I) all: 0.094 / Rsym value: 0.085 / Net I/σ(I): 9.9 / Num. measured all: 710786
Reflection shellResolution: 1.45→1.53 Å / Redundancy: 5.3 % / Rmerge(I) obs: 0.632 / Num. measured all: 96459 / Num. unique obs: 18128 / CC1/2: 0.859 / Rpim(I) all: 0.018 / Rrim(I) all: 0.045 / Rsym value: 0.041 / Net I/σ(I) obs: 2.2 / % possible all: 98.1

-
Processing

Software
NameVersionClassification
REFMAC5.8.0230refinement
MOSFLM7.2.2data reduction
SCALA3.2.22data scaling
MOLREP11.6.03phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4HN4

4hn4


Resolution: 1.45→28.94 Å / Cor.coef. Fo:Fc: 0.976 / Cor.coef. Fo:Fc free: 0.963 / WRfactor Rfree: 0.1828 / WRfactor Rwork: 0.1429 / FOM work R set: 0.8487 / SU B: 2.779 / SU ML: 0.045 / SU R Cruickshank DPI: 0.0646 / SU Rfree: 0.0609 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.065 / ESU R Free: 0.061 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.1856 6241 4.9 %RANDOM
Rwork0.1469 ---
obs0.1488 120118 99.46 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 117.81 Å2 / Biso mean: 23.82 Å2 / Biso min: 8.51 Å2
Baniso -1Baniso -2Baniso -3
1--0.41 Å20 Å20.05 Å2
2--0.11 Å2-0 Å2
3---0.29 Å2
Refinement stepCycle: final / Resolution: 1.45→28.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4922 0 80 767 5769
Biso mean--43.27 37.78 -
Num. residues----650
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0125244
X-RAY DIFFRACTIONr_angle_refined_deg1.3761.6447106
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.0525681
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.40122.124259
X-RAY DIFFRACTIONr_dihedral_angle_3_deg11.99715873
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.2621535
X-RAY DIFFRACTIONr_chiral_restr0.0910.2691
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.023965
X-RAY DIFFRACTIONr_rigid_bond_restr1.78835244
X-RAY DIFFRACTIONr_sphericity_free27.0235463
X-RAY DIFFRACTIONr_sphericity_bonded13.01855457
LS refinement shellResolution: 1.45→1.488 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.303 509 -
Rwork0.282 8577 -
all-9086 -
obs--97.58 %
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)
15.35761.07521.97690.338-0.31534.88840.2396-0.1172-0.14560.03140.01710.0010.2103-0.4172-0.25670.0188-0.01-0.00020.1173-0.01160.0993-59.667-21.55425.797
20.0564-0.08830.0550.327-0.49040.93210.07040.0510.0587-0.063-0.0683-0.0514-0.03430.0103-0.00210.09650.07460.06660.07670.01630.1196-41.559-12.1619.076
30.7057-0.7184-0.24560.94620.36770.19830.09190.0020.0216-0.0143-0.08010.0008-0.0016-0.0406-0.01180.0539-0.00650.02320.0809-0.01080.0646-41.664-24.09827.57
40.5082-0.17790.50521.6122-0.77420.8120.0980.0765-0.1225-0.09960.02760.11330.0774-0.0491-0.12560.04610.0656-0.04930.1546-0.0380.0781-52.122-32.29513.462
53.08352.0421.14892.03570.37110.68040.1030.05070.0262-0.0402-0.0590.0650.04710.0145-0.0440.10340.11820.03930.14020.04040.0584-48.787-13.259.411
64.58913.60011.90534.31381.41860.90610.00460.13770.3377-0.0623-0.08810.2349-0.0923-0.04540.08360.10710.11190.02340.14310.06480.1004-51.809-4.89512.807
70.85220.0345-0.52380.02970.02460.408-0.00460.0793-0.07890.029-0.0492-0.00230.0378-0.16070.05380.0474-0.026-0.01160.1645-0.01990.0363-30.482-42.63413.985
80.18340.0041-0.21040.12120.15470.4594-0.05170.0309-0.01650.01740.03390.01430.07260.04580.01780.0598-0.0039-0.01520.0901-0.0070.0461-3.965-47.115.706
90.0985-0.03710.07550.01730.0030.42130.01690.04670.0024-0.0075-0.0179-0.00540.0216-0.00030.00090.0573-0.0026-0.01120.0893-0.00750.0444-8.765-41.5035.789
100.12250.07640.13720.50870.17680.90060.07750.0229-0.032-0.04740.0405-0.0898-0.1793-0.139-0.1180.13340.0480.0220.10250.00950.0276-17.435-26.6330.82
110.07280.0994-0.20190.1519-0.33320.82610.0430.07860.01850.05060.0730.0353-0.042-0.1515-0.1160.06880.0431-0.00890.17940.02040.035-27.006-31.5437.907
120.22290.0051-0.03220.0280.07990.25090.0069-0.02040.0214-0.0006-0.00350.00830.01040.0019-0.00340.0562-0.0005-0.00370.0756-0.00060.0528-8.115-36.28720.313
130.2869-0.2423-0.19080.2885-0.0050.59120.1006-0.00970.0324-0.06970.03330.0067-0.08820.0686-0.13390.0717-0.01470.02330.1039-0.0290.03834.35-30.33315.503
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 13
2X-RAY DIFFRACTION2A14 - 77
3X-RAY DIFFRACTION3A78 - 159
4X-RAY DIFFRACTION4A160 - 216
5X-RAY DIFFRACTION5A217 - 247
6X-RAY DIFFRACTION6A248 - 267
7X-RAY DIFFRACTION7B2 - 37
8X-RAY DIFFRACTION8B38 - 70
9X-RAY DIFFRACTION9B71 - 100
10X-RAY DIFFRACTION10B101 - 165
11X-RAY DIFFRACTION11B166 - 196
12X-RAY DIFFRACTION12B197 - 364
13X-RAY DIFFRACTION13B365 - 396

+
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