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- PDB-1vbe: POLIOVIRUS (TYPE 3, SABIN STRAIN, MUTANT 242-H2) COMPLEXED WITH R78206 -

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Basic information

Entry
Database: PDB / ID: 1vbe
TitlePOLIOVIRUS (TYPE 3, SABIN STRAIN, MUTANT 242-H2) COMPLEXED WITH R78206
Components(POLIOVIRUS TYPE ...) x 5
KeywordsVIRUS / VIRUS COAT PROTEIN / HYDROLASE / THIOL PROTEASE / Icosahedral virus
Function / homology
Function and homology information


caveolin-mediated endocytosis of virus by host cell / 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 ...caveolin-mediated endocytosis of virus by host cell / 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 / DNA replication / RNA helicase activity / 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 / virion attachment to host cell / host cell nucleus / structural molecule activity / proteolysis / RNA binding / zinc ion binding / ATP binding / membrane
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
Chem-J78 / MYRISTIC ACID / Genome polyprotein
Similarity search - Component
Biological speciesPoliovirus type 3
MethodX-RAY DIFFRACTION / Resolution: 2.8 Å
AuthorsGrant, R.A. / Hiremath, C.N. / Filman, D.J. / Syed, R. / Andries, K. / Hogle, J.M.
Citation
Journal: Curr.Biol. / Year: 1994
Title: Structures of poliovirus complexes with anti-viral drugs: implications for viral stability and drug design.
Authors: Grant, R.A. / Hiremath, C.N. / Filman, D.J. / Syed, R. / Andries, K. / Hogle, J.M.
#1: Journal: Acta Crystallogr.,Sect.D / Year: 1995
Title: Binding of the Antiviral Drug Win51711 to the Sabin Strain of Type 3 Poliovirus: Structural Comparison with Drug Binding in Rhinovirus 14
Authors: Hiremath, C.N. / Grant, R.A. / Filman, D.J. / Hogle, J.M.
#2: Journal: New Aspects of Positive-Strand RNA Viruses / Year: 1990
Title: Role of Conformational Transitions in Poliovirus Assembly and Cell Entry
Authors: Hogle, J.M. / Syed, R. / Fricks, C.E. / Icenogle, J.P. / Flore, O. / Filman, D.J.
#3: Journal: Embo J. / Year: 1989
Title: Structural Factors that Control Conformational Transitions and Serotype Specificity in Type 3 Poliovirus
Authors: Filman, D.J. / Syed, R. / Chow, M. / Macadam, A.J. / Minor, P.D. / Hogle, J.M.
#4: Journal: Nature / Year: 1987
Title: Myristylation of Picornavirus Capsid Protein Vp4 and its Structural Significance
Authors: Chow, M. / Newman, J.F. / Filman, D. / Hogle, J.M. / Rowlands, D.J. / Brown, F.
#5: Journal: Science / Year: 1985
Title: Three-Dimensional Structure of Poliovirus at 2.9 A Resolution
Authors: Hogle, J.M. / Chow, M. / Filman, D.J.
#6: Journal: Nucleic Acids Res. / Year: 1983
Title: The Nucleotide Sequence of Poliovirus Type 3 Leon 12 A1B: Comparison with Poliovirus Type 1
Authors: Stanway, G. / Cann, A.J. / Hauptmann, R. / Hughes, P. / Clarke, L.D. / Mountford, R.C. / Minor, P.D. / Schild, G.C. / Almond, J.W.
History
DepositionJan 2, 1996Processing site: BNL
Revision 1.0Jul 11, 1996Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / 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 / _pdbx_database_status.process_site / _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 1.4Nov 20, 2024Group: Data collection / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_oper_list
Item: _pdbx_entry_details.has_protein_modification / _pdbx_struct_oper_list.name ..._pdbx_entry_details.has_protein_modification / _pdbx_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
0: POLIOVIRUS TYPE 3
1: POLIOVIRUS TYPE 3
2: POLIOVIRUS TYPE 3
3: POLIOVIRUS TYPE 3
4: POLIOVIRUS TYPE 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,9567
Polymers97,3445
Non-polymers6122
Water00
1
0: POLIOVIRUS TYPE 3
1: POLIOVIRUS TYPE 3
2: POLIOVIRUS TYPE 3
3: POLIOVIRUS TYPE 3
4: POLIOVIRUS TYPE 3
hetero molecules
x 60


Theoretical massNumber of molelcules
Total (without water)5,877,333420
Polymers5,840,622300
Non-polymers36,711120
Water0
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: POLIOVIRUS TYPE 3
1: POLIOVIRUS TYPE 3
2: POLIOVIRUS TYPE 3
3: POLIOVIRUS TYPE 3
4: POLIOVIRUS TYPE 3
hetero molecules
x 5


  • icosahedral pentamer
  • 490 kDa, 25 polymers
Theoretical massNumber of molelcules
Total (without water)489,77835
Polymers486,71825
Non-polymers3,05910
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
0: POLIOVIRUS TYPE 3
1: POLIOVIRUS TYPE 3
2: POLIOVIRUS TYPE 3
3: POLIOVIRUS TYPE 3
4: POLIOVIRUS TYPE 3
hetero molecules
x 6


  • icosahedral 23 hexamer
  • 588 kDa, 30 polymers
Theoretical massNumber of molelcules
Total (without water)587,73342
Polymers584,06230
Non-polymers3,67112
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation5
5


  • Idetical with deposited unit
  • icosahedral asymmetric unit, std point frame
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
0: POLIOVIRUS TYPE 3
1: POLIOVIRUS TYPE 3
2: POLIOVIRUS TYPE 3
3: POLIOVIRUS TYPE 3
4: POLIOVIRUS TYPE 3
hetero molecules
x 15


  • crystal asymmetric unit, crystal frame
  • 1.47 MDa, 75 polymers
Theoretical massNumber of molelcules
Total (without water)1,469,333105
Polymers1,460,15575
Non-polymers9,17830
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z2
point symmetry operation14
Unit cell
Length a, b, c (Å)321.060, 358.620, 381.820
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222
SymmetryPoint symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral))
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrix
1given(1), (1), (1)
2generate(0.30901699, -0.80901699, 0.5), (0.80901699, 0.5, 0.30901699), (-0.5, 0.30901699, 0.80901699)
3generate(-0.80901699, -0.5, 0.30901699), (0.5, -0.30901699, 0.80901699), (-0.30901699, 0.80901699, 0.5)
4generate(-0.80901699, 0.5, -0.30901699), (-0.5, -0.30901699, 0.80901699), (0.30901699, 0.80901699, 0.5)
5generate(0.30901699, 0.80901699, -0.5), (-0.80901699, 0.5, 0.30901699), (0.5, 0.30901699, 0.80901699)
6generate(1), (1), (1)
7generate(-0.5, 0.30901699, 0.80901699), (0.30901699, -0.80901699, 0.5), (0.80901699, 0.5, 0.30901699)
8generate(-0.30901699, 0.80901699, 0.5), (-0.80901699, -0.5, 0.30901699), (0.5, -0.30901699, 0.80901699)
9generate(0.30901699, 0.80901699, 0.5), (-0.80901699, 0.5, -0.30901699), (-0.5, -0.30901699, 0.80901699)
10generate(0.5, 0.30901699, 0.80901699), (0.30901699, 0.80901699, -0.5), (-0.80901699, 0.5, 0.30901699)
11generate(1), (1), (1)
12generate(0.80901699, 0.5, 0.30901699), (-0.5, 0.30901699, 0.80901699), (0.30901699, -0.80901699, 0.5)
13generate(0.5, -0.30901699, 0.80901699), (-0.30901699, 0.80901699, 0.5), (-0.80901699, -0.5, 0.30901699)
14generate(-0.5, -0.30901699, 0.80901699), (0.30901699, 0.80901699, 0.5), (-0.80901699, 0.5, -0.30901699)
15generate(-0.80901699, 0.5, 0.30901699), (0.5, 0.30901699, 0.80901699), (0.30901699, 0.80901699, -0.5)

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Components

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POLIOVIRUS TYPE ... , 5 types, 5 molecules 01234

#1: Protein/peptide POLIOVIRUS TYPE 3


Mass: 446.495 Da / Num. of mol.: 1 / Mutation: CHAIN 1, F124L, F134L / Source method: isolated from a natural source
Details: P3/242-H2 DERIVED FROM A LOW-PASSAGE SEED STOCK OF A PLAQUE ISOLATE PROVIDED BY A. MACADAM (NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Species: Poliovirus / Strain: P3-242-H2
#2: Protein POLIOVIRUS TYPE 3


Mass: 33455.641 Da / Num. of mol.: 1 / Mutation: CHAIN 1, F124L, F134L / Source method: isolated from a natural source
Details: P3/242-H2 DERIVED FROM A LOW-PASSAGE SEED STOCK OF A PLAQUE ISOLATE PROVIDED BY A. MACADAM (NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Organ: SEED / Species: Poliovirus / Strain: P3-242-H2 / References: UniProt: P03302
#3: Protein POLIOVIRUS TYPE 3


Mass: 30169.920 Da / Num. of mol.: 1 / Mutation: CHAIN 1, F124L, F134L / Source method: isolated from a natural source
Details: P3/242-H2 DERIVED FROM A LOW-PASSAGE SEED STOCK OF A PLAQUE ISOLATE PROVIDED BY A. MACADAM (NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Organ: SEED / Species: Poliovirus / Strain: P3-242-H2 / References: UniProt: P03302
#4: Protein POLIOVIRUS TYPE 3


Mass: 25950.723 Da / Num. of mol.: 1 / Mutation: CHAIN 1, F124L, F134L / Source method: isolated from a natural source
Details: P3/242-H2 DERIVED FROM A LOW-PASSAGE SEED STOCK OF A PLAQUE ISOLATE PROVIDED BY A. MACADAM (NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Organ: SEED / Species: Poliovirus / Strain: P3-242-H2 / References: UniProt: P03302
#5: Protein POLIOVIRUS TYPE 3


Mass: 7320.917 Da / Num. of mol.: 1 / Mutation: CHAIN 1, F124L, F134L / Source method: isolated from a natural source
Details: P3/242-H2 DERIVED FROM A LOW-PASSAGE SEED STOCK OF A PLAQUE ISOLATE PROVIDED BY A. MACADAM (NATIONAL INSTITUTE FOR BIOLOGICAL STANDARDS CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Organ: SEED / Species: Poliovirus / Strain: P3-242-H2 / References: UniProt: P03302

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Non-polymers , 2 types, 2 molecules

#6: Chemical ChemComp-J78 / (METHYLPYRIDAZINE PIPERIDINE PROPYLOXYPHENYL)ETHYLACETATE / R78206


Mass: 383.484 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C22H29N3O3
#7: Chemical ChemComp-MYR / MYRISTIC ACID


Mass: 228.371 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C14H28O2

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Details

Has protein modificationY
Sequence detailsTHE APPROPRIATE SEQUENCE FOR THIS VIRUS CORRESPONDS TO THE STANWAY ET AL. REFERENCE ABOVE EXCEPT ...THE APPROPRIATE SEQUENCE FOR THIS VIRUS CORRESPONDS TO THE STANWAY ET AL. REFERENCE ABOVE EXCEPT FOR TWO MUTATIONS. THE FIRST MUTATION IS A PHE-TO-LEU SUBSTITUTION AT RESIDUE 124 OF VP1. THE SECOND MUTATION IS ANOTHER PHE-TO-LEU SUBSTITUTION AT RESIDUE 134 OF VP1. THE NUMBERING OF THE VP1 RESIDUES HAS BEEN ALTERED TO FACILITATE COMPARISON WITH THE STRUCTURE OF THE MAHONEY STRAIN OF TYPE 1 POLIOVIRUS (PDB ENTRY 2PLV). MAHONEY HAS A TWO RESIDUE INSERTION, RELATIVE TO P3/SABIN, LOCATED IN THE DISORDERED N-TERMINUS OF VP1. THUS THE RESIDUES NUMBERED 24 - 302 IN THIS ENTRY ARE ACTUALLY RESIDUES 22 - 300. VP4 HAS A MYRISTATE MOIETY COVALENTLY LINKED TO ITS N-TERMINUS. THIS MYRISTATE HAS BEEN DESIGNATED RESIDUE 1 OF VP4 AND THE AMINO ACID RESIDUES OF VP4 ARE NUMBERED 2 - 69.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.59 Å3/Da / Density % sol: 30 %
Crystal grow
*PLUS
Method: other / Details: Filman, D.J., (1989) EMBO, J., 8, 1567.

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Data collection

RadiationScattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 2.8→30 Å / Num. obs: 161423 / % possible obs: 30 % / Observed criterion σ(I): 0
Reflection
*PLUS
Num. measured all: 349922

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Processing

Software
NameVersionClassification
X-PLORmodel building
X-PLOR2.1refinement
X-PLORphasing
RefinementRfactor Rwork: 0.295 / Highest resolution: 2.8 Å
Details: STEREOCHEMICAL CONSTRAINTS BASED ON PARAM19 AND TOP19 FILES USED IN X-PLOR VERSIONS PREVIOUS TO VERSION 3.1 ATOMIC MODELS FOR THE VIRUS AND THE DRUG WERE BUILT TO FIT ICOSAHEDRALLY ...Details: STEREOCHEMICAL CONSTRAINTS BASED ON PARAM19 AND TOP19 FILES USED IN X-PLOR VERSIONS PREVIOUS TO VERSION 3.1 ATOMIC MODELS FOR THE VIRUS AND THE DRUG WERE BUILT TO FIT ICOSAHEDRALLY CONSTRAINED 'FO' MAP USING THE GRAPHICS PROGRAM FRODO (JONES, 1978) MODIFIED TO INCORPORATE T = 1 ICOSAHEDRAL SYMMETRY. ATOMIC MODELS WERE OPTIMIZED WITH RESPECT TO THIS MAP BY A PSEUDO-REAL-SPACE REFINEMENT PROCEDURE, MINIMIZING A RESIDUAL WITH A STEREOCHEMICAL AND A CRYSTALLOGRAPHIC COMPONENT. THE GRADIENT OF THE STEREOCHEMICAL COMPONENT WAS PROVIDED BY THE X-PLOR PROGRAM (A. BRUNGER, X-PLOR VERSION 2.1 YALE UNIVERSITY 1990). THE CRYSTALLOGRAPHIC COMPONENT AND ITS GRADIENT WERE EVALUATED OVER THE VOLUME OF AN ARBITRARY PSEUDO-CELL (THE PROTOMER BOX) WHICH IS SUFFICIENTLY LARGE TO COMFORTABLY ENCLOSE A COMPLETE CHEMICALLY CONTINUOUS POLIOVIRUS PROTOMER, TOGETHER WITH WHATEVER FRAGMENTS OF SYMMETRY-RELATED PROTOMERS HAPPEN TO LIE SUFFICIENTLY CLOSE TO THE BOX TO CONTRIBUTE TO IT. THIS REFINEMENT SEEKS TO MINIMIZE THE DISCREPANCY BETWEEN THE 'PHASED' FOURIER TRANSFORMS OF MODEL-BASED ELECTRON DENSITY AND AUTHENTIC SYMMETRY-CONSTRAINED ELECTRON DENSITY, WHEN EACH TRANSFORM IS CALCULATED IN THE ARBITRARY PROTOMER BOX VOLUME, SCALED IN A RESOLUTION-DEPENDENT FASHION. SEE JRNL REFERENCE FOR MORE DETAILS. THE DISORDERED RESIDUES ABSENT FROM THE MODEL INCLUDE THE AMINO TERMINUS OF VP1 PRIOR TO THE RESIDUE LABELED GLN 24, 1 - 5 IN VP2, 236 - 238 IN VP3, AND THE RESIDUES LABELED 17 - 22 IN VP4. THE POLYPEPTIDE DESIGNATED IN THIS FILE AS RESIDUES 6 - 9 OF CHAIN 0 REPRESENTS A FEATURE IN THE ELECTRON DENSITY MAP WHICH APPEARS TO BE A BETA STRAND. ALTHOUGH THE SIDE CHAINS OF THIS STRAND CANNOT BE CORRELATED RELIABLY WITH THE SEQUENCE OF THE PROTEIN, THE FEATURE IS BELIEVED LIKELY TO CORRESPOND TO SOME PORTION OF THE AMINO TERMINAL EXTENSION OF VP1. NO SOLVENT MOLECULES ARE INCLUDED. THE POLYPEPTIDE DESIGNATED IN THIS FILE AS RESIDUES 6 - 9 OF CHAIN 0 REPRESENTS A FEATURE IN THE ELECTRON DENSITY MAP WHICH APPEARS TO BE A BETA STRAND. ALTHOUGH THE SIDE CHAINS OF THIS STRAND CANNOT BE CORRELATED RELIABLY WITH THE SEQUENCE OF THE PROTEIN, THE FEATURE IS BELIEVED LIKELY TO CORRESPOND TO SOME PORTION OF THE AMINO TERMINAL EXTENSION OF VP1.
Refinement stepCycle: LAST / Highest resolution: 2.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6597 0 43 0 6640
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONo_bond_d0.011
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_deg2.51
X-RAY DIFFRACTIONo_angle_deg_na
X-RAY DIFFRACTIONo_angle_deg_prot
X-RAY DIFFRACTIONo_dihedral_angle_d
X-RAY DIFFRACTIONo_dihedral_angle_d_na
X-RAY DIFFRACTIONo_dihedral_angle_d_prot
X-RAY DIFFRACTIONo_improper_angle_d
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
Software
*PLUS
Name: 'PSEUDO-REAL SPACE PROCEDURE' / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.295
Solvent computation
*PLUS
Displacement parameters
*PLUS

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