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- PDB-1ar9: P1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT H2142Y -

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Basic information

Entry
Database: PDB / ID: 1ar9
TitleP1/MAHONEY POLIOVIRUS, SINGLE SITE MUTANT H2142Y
Components(P1/MAHONEY POLIOVIRUS) x 5
KeywordsVIRUS / PICORNAVIRUS / POLIOVIRUS / COAT PROTEIN / Icosahedral virus
Function / homology
Function and homology information


symbiont-mediated suppression of host translation initiation / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / ribonucleoside triphosphate phosphatase activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid ...symbiont-mediated suppression of host translation initiation / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MDA-5 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / ribonucleoside triphosphate phosphatase activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / symbiont-mediated suppression of host gene expression / RNA helicase activity / endocytosis involved in viral entry into host cell / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / : / host cell nucleus / virion attachment to host cell / structural molecule activity / proteolysis / RNA binding / ATP binding / membrane / metal ion binding
Similarity search - Function
Picornavirus coat protein VP4 / Rhinovirus 14, subunit 4 / Jelly Rolls - #20 / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A ...Picornavirus coat protein VP4 / Rhinovirus 14, subunit 4 / Jelly Rolls - #20 / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Picornavirus capsid / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / Picornavirus/Calicivirus coat protein / Few Secondary Structures / Irregular / Viral coat protein subunit / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / Reverse transcriptase/Diguanylate cyclase domain / Jelly Rolls / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / Sandwich / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
MYRISTIC ACID / SPHINGOSINE / Genome polyprotein / Genome polyprotein
Similarity search - Component
Biological speciesHuman poliovirus 1
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.9 Å
AuthorsWien, M.W. / Curry, S. / Filman, D.J. / Hogle, J.M.
Citation
Journal: Nat.Struct.Biol. / Year: 1997
Title: Structural studies of poliovirus mutants that overcome receptor defects.
Authors: Wien, M.W. / Curry, S. / Filman, D.J. / Hogle, J.M.
#1: Journal: Acta Crystallogr.,Sect.D / Year: 1996
Title: A Pseudo-Cell Based Approach to Efficient Crystallographic Refinement of Viruses
Authors: Jacobson, D.H. / Hogle, J.M. / Filman, D.J.
#2: Journal: Science / Year: 1985
Title: Three-Dimensional Structure of Poliovirus at 2.9 A Resolution
Authors: Hogle, J.M. / Chow, M. / Filman, D.J.
History
DepositionAug 11, 1997Processing site: BNL
Revision 1.0Dec 3, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3Nov 29, 2017Group: Derived calculations / Other
Category: pdbx_database_status / struct_conf / struct_conf_type
Item: _pdbx_database_status.process_site
Revision 1.4Nov 3, 2021Group: 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
Revision 2.0Apr 19, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Other / Refinement description
Category: atom_site / cell ...atom_site / cell / database_PDB_matrix / pdbx_database_remark / pdbx_struct_oper_list / pdbx_validate_close_contact / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / pdbx_validate_torsion / struct_conn / struct_ncs_oper
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _cell.Z_PDB / _database_PDB_matrix.origx[1][1] / _database_PDB_matrix.origx[1][2] / _database_PDB_matrix.origx[2][1] / _database_PDB_matrix.origx[2][2] / _database_PDB_matrix.origx_vector[3] / _pdbx_struct_oper_list.id / _pdbx_struct_oper_list.matrix[1][1] / _pdbx_struct_oper_list.matrix[1][2] / _pdbx_struct_oper_list.matrix[1][3] / _pdbx_struct_oper_list.matrix[2][1] / _pdbx_struct_oper_list.matrix[2][2] / _pdbx_struct_oper_list.matrix[2][3] / _pdbx_struct_oper_list.matrix[3][1] / _pdbx_struct_oper_list.matrix[3][2] / _pdbx_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type / _pdbx_struct_oper_list.vector[1] / _pdbx_struct_oper_list.vector[2] / _pdbx_struct_oper_list.vector[3] / _pdbx_validate_rmsd_angle.angle_deviation / _pdbx_validate_rmsd_angle.angle_value / _pdbx_validate_torsion.phi / _pdbx_validate_torsion.psi / _struct_conn.pdbx_dist_value
Details: Coordinates and associated matrices have been transformed from the icosahedral point symmetry frame to the crystallographic frame
Provider: repository / Type: Remediation
Revision 2.1Aug 9, 2023Group: Refinement description / Category: pdbx_initial_refinement_model
Revision 2.2Nov 6, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
0: P1/MAHONEY POLIOVIRUS
1: P1/MAHONEY POLIOVIRUS
2: P1/MAHONEY POLIOVIRUS
3: P1/MAHONEY POLIOVIRUS
4: P1/MAHONEY POLIOVIRUS
1: SPHINGOSINE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)98,4957
Polymers97,9675
Non-polymers5282
Water9,638535
1
0: P1/MAHONEY POLIOVIRUS
1: P1/MAHONEY POLIOVIRUS
2: P1/MAHONEY POLIOVIRUS
3: P1/MAHONEY POLIOVIRUS
4: P1/MAHONEY POLIOVIRUS
hetero molecules
x 60


Theoretical massNumber of molelcules
Total (without water)5,909,713420
Polymers5,878,042300
Non-polymers31,672120
Water5,405300
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation59
2


  • Idetical with deposited unit
  • icosahedral asymmetric unit
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
0: P1/MAHONEY POLIOVIRUS
1: P1/MAHONEY POLIOVIRUS
2: P1/MAHONEY POLIOVIRUS
3: P1/MAHONEY POLIOVIRUS
4: P1/MAHONEY POLIOVIRUS
hetero molecules
x 5


  • icosahedral pentamer
  • 492 kDa, 25 polymers
Theoretical massNumber of molelcules
Total (without water)492,47635
Polymers489,83725
Non-polymers2,63910
Water45025
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
0: P1/MAHONEY POLIOVIRUS
1: P1/MAHONEY POLIOVIRUS
2: P1/MAHONEY POLIOVIRUS
3: P1/MAHONEY POLIOVIRUS
4: P1/MAHONEY POLIOVIRUS
hetero molecules
x 6


  • icosahedral 23 hexamer
  • 591 kDa, 30 polymers
Theoretical massNumber of molelcules
Total (without water)590,97142
Polymers587,80430
Non-polymers3,16712
Water54030
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation5
5


  • Idetical with deposited unit in distinct coordinate
  • icosahedral asymmetric unit, std point frame
TypeNameSymmetry operationNumber
transform to point frame1
6
0: P1/MAHONEY POLIOVIRUS
1: P1/MAHONEY POLIOVIRUS
2: P1/MAHONEY POLIOVIRUS
3: P1/MAHONEY POLIOVIRUS
4: P1/MAHONEY POLIOVIRUS
hetero molecules
x 30


  • crystal asymmetric unit, crystal frame
  • 2.95 MDa, 150 polymers
Theoretical massNumber of molelcules
Total (without water)2,954,857210
Polymers2,939,021150
Non-polymers15,83660
Water2,702150
TypeNameSymmetry operationNumber
identity operation1_555x,y,z2
point symmetry operation29
Unit cell
Length a, b, c (Å)319.950, 355.150, 377.050
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
SymmetryPoint symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral))
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2generate(0.30923344, -0.81767247, 0.48623159), (0.80040263, 0.49978355, 0.33034972), (-0.51276242, 0.28700732, 0.80901699)45.77764, 31.10171, -17.98063
3generate(-0.80816317, -0.5219589, 0.27361081), (0.47814841, -0.30987081, 0.82154294), (-0.34367538, 0.79490706, 0.5)25.75986, 77.34648, -47.07391
4generate(-0.8079857, 0.47847462, -0.34402764), (-0.52141829, -0.31004828, 0.79476733), (0.27358857, 0.82179903, 0.5)-32.38945, 74.82561, -47.07391
5generate(0.30952059, 0.80106295, -0.51312843), (-0.81693026, 0.4994964, 0.28702586), (0.48599165, 0.33051945, 0.80901699)-48.30992, 27.02286, -17.98063
6generate(-0.99622977, -0.08696857), (-0.08653977, 0.99622977), (-1)-188.29564
7generate(-0.37767743, 0.7711242, -0.51312843), (0.77062394, 0.56866044, 0.28702586), (0.51276242, -0.28700732, -0.80901699)-48.30992, 27.02286, -170.31501
8generate(0.76353233, 0.54694002, -0.34402764), (0.54628393, -0.26353233, 0.79476733), (0.34367538, -0.79490706, -0.5)-32.38945, 74.82561, -141.22173
9generate(0.85028641, -0.4497062, 0.27361081), (-0.44952954, -0.35028641, 0.82154294), (-0.27358857, -0.82179903, -0.5)25.75986, 77.34648, -141.22173
10generate(-0.23730637, -0.84148325, 0.48623159), (-0.84063609, 0.42828938, 0.33034972), (-0.48599165, -0.33051945, -0.80901699)45.77764, 31.10171, -170.31501
11generate(-0.04346578, -0.00189365, 0.99936002), (0.99769009, 0.04346578, 0.04332386), (-0.04331603, 0.99917932)94.08757, 4.07885, -94.14782
12generate(-0.52739102, 0.321418, 0.78673924), (0.32109441, -0.78162597, 0.53451708), (0.786351, 0.53479171, 0.30901699)74.06978, 50.32362, -65.05454
13generate(-0.30923344, 0.81767247, 0.48623159), (-0.80040263, -0.49978355, 0.33034972), (0.51276242, -0.28700732, 0.80901699)45.77764, 31.10171, -17.98063
14generate(0.30952059, 0.80106295, 0.51312843), (-0.81693026, 0.4994964, -0.28702586), (-0.48599165, -0.33051945, 0.80901699)48.30992, -27.02286, -17.98063
15generate(0.47377405, 0.29454323, 0.83025924), (0.29435215, 0.83524294, -0.46441761), (-0.82966703, 0.46438761, 0.30901699)78.1671, -43.72391, -65.05454
16generate(0.04346578, 0.00189365, 0.99936002), (-0.99769009, -0.04346578, 0.04332386), (0.04331603, -0.99917932)94.08757, 4.07885, -94.14782
17generate(-0.49747751, 0.25222929, 0.83025924), (-0.36552411, 0.8064945, -0.46441761), (-0.786351, -0.53479171, -0.30901699)78.1671, -43.72391, -123.2411
18generate(-0.37767743, 0.7711242, 0.51312843), (0.77062394, 0.56866044, -0.28702586), (-0.51276242, 0.28700732, -0.80901699)48.30992, -27.02286, -170.31501
19generate(0.23730637, 0.84148325, 0.48623159), (0.84063609, -0.42828938, 0.33034972), (0.48599165, 0.33051945, -0.80901699)45.77764, 31.10171, -170.31501
20generate(0.4975872, 0.36607262, 0.78673924), (-0.25224208, -0.80660418, 0.53451708), (0.82966703, -0.46438761, -0.30901699)74.06978, 50.32362, -123.2411
21generate(-0.04328831, 0.99853987, -0.04352), (-0.00187662, 0.0432883, 0.99893469), (0.99875407, 0.04351213)-4.09731, 94.04752, -94.14782
22generate(0.80816317, 0.5219589, 0.27361081), (-0.47814841, 0.30987081, 0.82154294), (0.34367538, -0.79490706, 0.5)25.75986, 77.34648, -47.07391
23generate(0.52739102, -0.321418, 0.78673924), (-0.32109441, 0.78162597, 0.53451708), (-0.786351, -0.53479171, 0.30901699)74.06978, 50.32362, -65.05454
24generate(-0.4975872, -0.36607262, 0.78673924), (0.25224208, 0.80660418, 0.53451708), (-0.82966703, 0.46438761, -0.30901699)74.06978, 50.32362, -123.2411
25generate(-0.85028641, 0.4497062, 0.27361081), (0.44952954, 0.35028641, 0.82154294), (0.27358857, 0.82179903, -0.5)25.75986, 77.34648, -141.22173
26generate(0.04328831, -0.99853987, -0.04352), (0.00187662, -0.0432883, 0.99893469), (-0.99875407, -0.04351213)-4.09731, 94.04752, -94.14782
27generate(-0.76353233, -0.54694002, -0.34402764), (-0.54628393, 0.26353233, 0.79476733), (-0.34367538, 0.79490706, -0.5)-32.38945, 74.82561, -141.22173
28generate(-0.49747751, 0.25222929, -0.83025924), (-0.36552411, 0.8064945, 0.46441761), (0.786351, 0.53479171, -0.30901699)-78.1671, 43.72391, -123.2411
29generate(0.47377405, 0.29454323, -0.83025924), (0.29435215, 0.83524294, 0.46441761), (0.82966703, -0.46438761, 0.30901699)-78.1671, 43.72391, -65.05454
30generate(0.8079857, -0.47847462, -0.34402764), (0.52141829, 0.31004828, 0.79476733), (-0.27358857, -0.82179903, 0.5)-32.38945, 74.82561, -47.07391

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Components

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Protein/peptide , 1 types, 1 molecules 0

#1: Protein/peptide P1/MAHONEY POLIOVIRUS


Mass: 437.404 Da / Num. of mol.: 1 / Fragment: VIRUS PROTOMER / Mutation: CHAIN 2, H142Y
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 1 / Genus: Enterovirus / Species: Poliovirus / Strain: Mahoney

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Protein , 4 types, 4 molecules 1234

#2: Protein P1/MAHONEY POLIOVIRUS


Mass: 33488.613 Da / Num. of mol.: 1 / Fragment: VIRUS PROTOMER / Mutation: CHAIN 2, H142Y
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 1 / Genus: Enterovirus / Species: Poliovirus / Strain: Mahoney / References: UniProt: P03300
#3: Protein P1/MAHONEY POLIOVIRUS


Mass: 30100.811 Da / Num. of mol.: 1 / Fragment: VIRUS PROTOMER / Mutation: CHAIN 2, H142Y
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 1 / Genus: Enterovirus / Species: Poliovirus / Strain: Mahoney / References: UniProt: P03300
#4: Protein P1/MAHONEY POLIOVIRUS


Mass: 26547.482 Da / Num. of mol.: 1 / Fragment: VIRUS PROTOMER / Mutation: CHAIN 2, H142Y
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 1 / Genus: Enterovirus / Species: Poliovirus / Strain: Mahoney / References: UniProt: P03300
#5: Protein P1/MAHONEY POLIOVIRUS


Mass: 7393.050 Da / Num. of mol.: 1 / Fragment: VIRUS PROTOMER / Mutation: CHAIN 2, H142Y
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human poliovirus 1 / Genus: Enterovirus / Species: Poliovirus / Strain: Mahoney / References: UniProt: P03299, UniProt: P03300*PLUS

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Non-polymers , 3 types, 537 molecules 1

#6: Chemical ChemComp-SPH / SPHINGOSINE


Mass: 299.492 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H37NO2
#7: Chemical ChemComp-MYR / MYRISTIC ACID


Mass: 228.371 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H28O2
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 535 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 2.59 Å3/Da / Density % sol: 30 %
Crystal growMethod: microdiaylsis / pH: 7.5
Details: VIRUS WAS CRYSTALLIZED BY MICRODIALYSIS AGAINST 10MM PIPES, 0-70 MM NACL, PH 7.5, 2% PEG 400, microdiaylsis
Crystal grow
*PLUS
Temperature: 4 ℃ / Method: microdialysis
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
170 mM11NaCl
22 %PEG40011

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Data collection

DiffractionMean temperature: 113 K
Diffraction sourceSource: ROTATING ANODE / Type: ELLIOTT GX-13 / Wavelength: 1.5418
DetectorType: MARRESEARCH / Detector: AREA DETECTOR / Date: Dec 1, 1995 / Details: SUPPER LONG MIRRORS
RadiationMonochromator: SUPPER LONG MIRRORS / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 2.9→40 Å / Num. obs: 777630 / % possible obs: 82 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Rmerge(I) obs: 0.15
Reflection
*PLUS
Num. measured all: 2807335

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Processing

Software
NameVersionClassification
X-PLOR3model building
X-PLOR3refinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLOR3phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2PLV

2plv


Resolution: 2.9→11 Å
Details: OTHER PROGRAMS USED PROGRAM : X-PLOR 3.0 AUTHORS : BRUNGER
RfactorNum. reflection% reflection
Rwork0.244 --
obs-777630 81 %
Refinement stepCycle: LAST / Resolution: 2.9→11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6634 0 36 535 7205
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.013
X-RAY DIFFRACTIONo_bond_d_na
X-RAY DIFFRACTIONo_bond_d_prot
X-RAY DIFFRACTIONo_angle_d
X-RAY DIFFRACTIONo_angle_d_na
X-RAY DIFFRACTIONo_angle_d_prot
X-RAY DIFFRACTIONo_angle_deg2.54
X-RAY DIFFRACTIONo_angle_deg_na
X-RAY DIFFRACTIONo_angle_deg_prot
X-RAY DIFFRACTIONo_dihedral_angle_d25.8
X-RAY DIFFRACTIONo_dihedral_angle_d_na
X-RAY DIFFRACTIONo_dihedral_angle_d_prot
X-RAY DIFFRACTIONo_improper_angle_d1.29
X-RAY DIFFRACTIONo_improper_angle_d_na
X-RAY DIFFRACTIONo_improper_angle_d_prot
X-RAY DIFFRACTIONo_mcbond_it
X-RAY DIFFRACTIONo_mcangle_it
X-RAY DIFFRACTIONo_scbond_it
X-RAY DIFFRACTIONo_scangle_it
LS refinement shellResolution: 2.9→2.99 Å / Total num. of bins used: 16 /
RfactorNum. reflection
Rwork0.347 67285
Software
*PLUS
Name: 'PROTOMER-BOX-BASED PSEUDO-REAL-SPACE' / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.244
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg25.8
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.29
LS refinement shell
*PLUS
Rfactor obs: 0.347

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Jul 12, 2017. Major update of PDB

Major update of PDB

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External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

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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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