[English] 日本語
Yorodumi
- PDB-3qwn: Crystal structure of a NigD-like immunity protein (BACCAC_03262) ... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 3qwn
TitleCrystal structure of a NigD-like immunity protein (BACCAC_03262) from Bacteroides caccae ATCC 43185 at 2.42 A resolution
ComponentsHypothetical nigD-like protein
KeywordsANTITOXIN / SH3-like barrel fold / Structural Genomics / Joint Center for Structural Genomics / JCSG / Protein Structure Initiative / PSI-biology
Function / homology
Function and homology information


NigD-like, C-terminal beta sandwich domain / NigD-like N-terminal OB domain / NigD-like, C-terminal beta sandwich domain / NigD-like, C-terminal domain superfamily / NigD-like N-terminal OB domain / NigD-like C-terminal beta sandwich domain / NigD-like N-terminal OB domain / NigD-like, N-terminal domain superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Immunoglobulin-like ...NigD-like, C-terminal beta sandwich domain / NigD-like N-terminal OB domain / NigD-like, C-terminal beta sandwich domain / NigD-like, C-terminal domain superfamily / NigD-like N-terminal OB domain / NigD-like C-terminal beta sandwich domain / NigD-like N-terminal OB domain / NigD-like, N-terminal domain superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta
Similarity search - Domain/homology
Uncharacterized protein
Similarity search - Component
Biological speciesBacteroides caccae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.42 Å
AuthorsJoint Center for Structural Genomics (JCSG)
CitationJournal: To be published
Title: Crystal structure of a Hypothetical nigD-like protein (BACCAC_03262) from Bacteroides caccae at 2.42 A resolution
Authors: Joint Center for Structural Genomics (JCSG)
History
DepositionFeb 28, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 23, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Dec 24, 2014Group: Structure summary
Revision 1.3Oct 25, 2017Group: Author supporting evidence / Refinement description / Category: pdbx_struct_assembly_auth_evidence / software / Item: _software.classification / _software.name
Revision 1.4Feb 1, 2023Group: Database references / Derived calculations
Category: database_2 / struct_conn ...database_2 / struct_conn / 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 / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Hypothetical nigD-like protein
B: Hypothetical nigD-like protein
C: Hypothetical nigD-like protein
D: Hypothetical nigD-like protein
E: Hypothetical nigD-like protein
F: Hypothetical nigD-like protein
G: Hypothetical nigD-like protein
H: Hypothetical nigD-like protein
I: Hypothetical nigD-like protein
J: Hypothetical nigD-like protein
K: Hypothetical nigD-like protein
L: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)289,44956
Polymers287,80912
Non-polymers1,64044
Water22,0141222
1
A: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,1265
Polymers23,9841
Non-polymers1424
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,1265
Polymers23,9841
Non-polymers1424
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0553
Polymers23,9841
Non-polymers712
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,2598
Polymers23,9841
Non-polymers2757
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,1616
Polymers23,9841
Non-polymers1775
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0553
Polymers23,9841
Non-polymers712
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,1616
Polymers23,9841
Non-polymers1775
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
H: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0553
Polymers23,9841
Non-polymers712
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
9
I: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,1525
Polymers23,9841
Non-polymers1684
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
10
J: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0904
Polymers23,9841
Non-polymers1063
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
11
K: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,0904
Polymers23,9841
Non-polymers1063
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
12
L: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)24,1174
Polymers23,9841
Non-polymers1333
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
13
A: Hypothetical nigD-like protein
D: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,38513
Polymers47,9682
Non-polymers41711
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3040 Å2
ΔGint-91 kcal/mol
Surface area20630 Å2
MethodPISA
14
B: Hypothetical nigD-like protein
C: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,1818
Polymers47,9682
Non-polymers2136
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2650 Å2
ΔGint-71 kcal/mol
Surface area20500 Å2
MethodPISA
15
E: Hypothetical nigD-like protein
H: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,2169
Polymers47,9682
Non-polymers2487
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2620 Å2
ΔGint-75 kcal/mol
Surface area20490 Å2
MethodPISA
16
F: Hypothetical nigD-like protein
G: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,2169
Polymers47,9682
Non-polymers2487
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2640 Å2
ΔGint-75 kcal/mol
Surface area20870 Å2
MethodPISA
17
I: Hypothetical nigD-like protein
L: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,2709
Polymers47,9682
Non-polymers3017
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2690 Å2
ΔGint-51 kcal/mol
Surface area20420 Å2
MethodPISA
18
J: Hypothetical nigD-like protein
K: Hypothetical nigD-like protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)48,1818
Polymers47,9682
Non-polymers2136
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2610 Å2
ΔGint-69 kcal/mol
Surface area20630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)132.310, 132.310, 163.350
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number144
Space group name H-MP31
DetailsLIGHT SCATTERING SUPPORTS THE ASSIGNMENT OF A MONOMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.

-
Components

#1: Protein
Hypothetical nigD-like protein


Mass: 23984.062 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacteroides caccae (bacteria) / Gene: BACCAC_03262 / Plasmid: SpeedET / Production host: Escherichia Coli (E. coli) / Strain (production host): HK100 / References: UniProt: A5ZK25
#2: Chemical...
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 41 / Source method: obtained synthetically / Formula: Cl
#3: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1222 / Source method: isolated from a natural source / Formula: H2O
Sequence detailsTHE CONSTRUCT (RESIDUES 23-235) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG ...THE CONSTRUCT (RESIDUES 23-235) WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.87 Å3/Da / Density % sol: 57.12 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 7.3
Details: 30.0% polyethylene glycol 3350, 0.2M di-sodium hydrogen phosphate, 0.1M HEPES pH 7.3, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL9-2 / Wavelength: 0.97901,0.97920,0.91837,0.97908
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jul 22, 2010 / Details: double crystal monochromator
RadiationMonochromator: double crystal / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.979011
20.97921
30.918371
40.979081
ReflectionResolution: 2.42→29.712 Å / Num. all: 121998 / Num. obs: 121998 / % possible obs: 99.9 % / Redundancy: 4.3 % / Rsym value: 0.096 / Net I/σ(I): 9.8
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured allNum. unique allRsym value% possible all
2.42-2.484.20.77913829990580.779100
2.48-2.554.20.6361.23739088240.636100
2.55-2.624.20.511.53610985330.51100
2.62-2.714.20.4031.93535083360.403100
2.71-2.794.20.3292.33404880220.329100
2.79-2.894.20.2682.83303377730.268100
2.89-34.30.2043.73226575830.204100
3-3.124.30.1774.33067071990.177100
3.12-3.264.30.1315.72953769160.131100
3.26-3.424.30.0997.32836566560.099100
3.42-3.614.30.0887.92701763270.088100
3.61-3.834.30.0778.82535759360.077100
3.83-4.094.30.06510.22412856310.065100
4.09-4.424.30.05611.52233452100.056100
4.42-4.844.30.0512.92048747800.05100
4.84-5.414.30.05411.61870143580.054100
5.41-6.254.30.06310.61640238210.063100
6.25-7.654.30.0689.31384832230.068100
7.65-10.824.30.052101072925060.052100
10.82-29.7124.20.04310.7550913060.04395.4

-
Phasing

PhasingMethod: MAD

-
Processing

Software
NameVersionClassificationNB
MolProbity3beta29model building
PDB_EXTRACT3.1data extraction
SOLVEphasing
SCALA3.3.15data scaling
BUSTER-TNT2.8.0refinement
MOSFLMdata reduction
BUSTER2.8.0refinement
RefinementMethod to determine structure: MAD / Resolution: 2.42→29.712 Å / Cor.coef. Fo:Fc: 0.9393 / Cor.coef. Fo:Fc free: 0.9259 / Occupancy max: 1 / Occupancy min: 0.5 / Cross valid method: THROUGHOUT / σ(F): 0
Details: 1. 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 ...Details: 1. 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. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT. 4. CHLORIDE (CL) AND ETHYLENE GLYCOL (EDO) MODELED ARE PRESENT PROTEIN BUFFER. 5. NCS RESTRAINTS WERE APPLIED USING BUSTER'S LSSR RESTRAINT REPRESENTATION (-AUTONCS).
RfactorNum. reflection% reflectionSelection details
Rfree0.2131 6123 5.02 %RANDOM
Rwork0.1754 ---
obs0.1773 121938 --
Displacement parametersBiso max: 191.72 Å2 / Biso mean: 59.0428 Å2 / Biso min: 18.68 Å2
Baniso -1Baniso -2Baniso -3
1--5.8298 Å20 Å20 Å2
2---5.8298 Å20 Å2
3---11.6597 Å2
Refinement stepCycle: LAST / Resolution: 2.42→29.712 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18959 0 53 1222 20234
Refine LS restraints
Refine-IDTypeNumberRestraint functionWeightDev ideal
X-RAY DIFFRACTIONt_dihedral_angle_d8681SINUSOIDAL2
X-RAY DIFFRACTIONt_trig_c_planes509HARMONIC2
X-RAY DIFFRACTIONt_gen_planes2825HARMONIC5
X-RAY DIFFRACTIONt_it19419HARMONIC20
X-RAY DIFFRACTIONt_nbd5SEMIHARMONIC5
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_chiral_improper_torsion2585SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact20836SEMIHARMONIC4
X-RAY DIFFRACTIONt_bond_d19419HARMONIC20.01
X-RAY DIFFRACTIONt_angle_deg26472HARMONIC21.11
X-RAY DIFFRACTIONt_omega_torsion3.83
X-RAY DIFFRACTIONt_other_torsion2.84
LS refinement shellResolution: 2.42→2.48 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2558 430 4.76 %
Rwork0.2137 8612 -
all0.2157 9042 -
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)
11.6569-0.1557-0.0021.9457-0.14432.8948-0.1504-0.07220.04230.2374-0.0861-0.0934-0.85470.31360.23650.0759-0.1794-0.0976-0.18230.0553-0.2149145.033320.22165.5051
21.96950.3544-0.08050.8503-0.39432.0779-0.11230.01370.0680.09120.00780.0831-0.6128-0.25220.10450.070.124-0.0109-0.1701-0.0237-0.1249120.180419.989446.2706
30.6501-0.44010.37561.2702-0.59363.13940.0538-0.0691-0.1099-0.09090.04340.11090.1835-0.5094-0.0971-0.1505-0.0655-0.0112-0.01990.0271-0.0631117.5143-14.520851.5108
40.7137-0.1065-0.09591.10580.53282.299-0.0123-0.0219-0.1514-0.0063-0.0034-0.02050.03150.38280.0157-0.15680.00720.0027-0.001-0.0017-0.0229147.839-14.440760.0508
52.7137-0.4478-0.43221.404-0.01662.7358-0.10960.11710.11970.4535-0.2183-0.2709-0.53430.4440.3279-0.0516-0.2839-0.179-0.07770.1286-0.214376.82158.628963.4452
61.97910.454-0.19072.656-0.11173.02780.09440.15650.0609-0.0464-0.37970.2849-0.4113-0.24840.2853-0.24130.0509-0.03510.0256-0.119-0.181351.642857.330544.5388
70.6838-0.09680.17791.2026-0.48871.18720.0432-0.1775-0.2080.0362-0.1463-0.01620.221-0.28580.1031-0.1062-0.14960.03330.09250.0021-0.1151.396522.766949.9789
80.0150.27740.53161.36361.09595.561-0.00730.2196-0.08830.0985-0.0246-0.04620.65731.03850.0319-0.17550.1480.03290.1059-0.0213-0.237581.368724.86158.023
92.3449-0.4675-0.30930.90770.78532.9488-0.22340.15080.0137-0.07310.2191-0.0001-0.54030.36540.0042-0.1475-0.24510.04440.081-0.029-0.22514.055795.814663.6625
101.81940.0789-0.29191.3290.11752.9993-0.0832-0.00020.0366-0.2393-0.03110.0879-0.7899-0.02380.1144-0.0704-0.0324-0.0434-0.0468-0.0169-0.2031-10.513697.657744.0361
110.3723-0.35390.12341.4883-0.4083.1211-0.0033-0.0132-0.1124-0.1350.14680.20410.3855-0.5599-0.1434-0.2291-0.1598-0.0750.0930.0626-0.1006-16.306363.523849.7093
120.54780.19260.52461.82161.31483.741-0.04460.1323-0.10070.00640.4272-0.16270.22630.9073-0.3826-0.28790.0351-0.00670.1849-0.147-0.160814.001661.110958.1851
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1{ A|28 - 333 }A28 - 333
2X-RAY DIFFRACTION2{ B|27 - 333 }B27 - 333
3X-RAY DIFFRACTION3{ C|31 - 333 }C31 - 333
4X-RAY DIFFRACTION4{ D|30 - 333 }D30 - 333
5X-RAY DIFFRACTION5{ E|29 - 333 }E29 - 333
6X-RAY DIFFRACTION6{ F|29 - 333 }F29 - 333
7X-RAY DIFFRACTION7{ G|25 - 333 }G25 - 333
8X-RAY DIFFRACTION8{ H|28 - 333 }H28 - 333
9X-RAY DIFFRACTION9{ I|29 - 333 }I29 - 333
10X-RAY DIFFRACTION10{ J|26 - 333 }J26 - 333
11X-RAY DIFFRACTION11{ K|28 - 333 }K28 - 333
12X-RAY DIFFRACTION12{ L|31 - 333 }L31 - 333

+
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