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- PDB-1pvc: REFINEMENT OF THE SABIN STRAIN OF TYPE 3 POLIOVIRUS AT 2.4 ANGSTR... -

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Database: PDB / ID: 1pvc
TitleREFINEMENT OF THE SABIN STRAIN OF TYPE 3 POLIOVIRUS AT 2.4 ANGSTROMS AND THE CRYSTAL STRUCTURES OF ITS VARIANTS AT 2.9 ANGSTROMS RESOLUTION
Components(POLIOVIRUS TYPE 3, SABIN ...) x 5
KeywordsVIRUS / 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 / picornain 2A / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / symbiont-mediated suppression of host mRNA export from nucleus / ribonucleoside triphosphate phosphatase activity / 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 / picornain 2A / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / symbiont-mediated suppression of host mRNA export from nucleus / ribonucleoside triphosphate phosphatase activity / 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 / protein complex oligomerization / monoatomic ion channel activity / symbiont-mediated suppression of host gene expression / DNA replication / RNA helicase activity / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / cysteine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / 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) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / 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 / Viral coat protein subunit / Few Secondary Structures / Irregular / 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
Similarity search - Component
Biological speciesPoliovirus type 3
MethodX-RAY DIFFRACTION / Resolution: 2.4 Å
AuthorsSyed, R. / Filman, D.J. / Hogle, J.M.
Citation
Journal: To be Published
Title: Refinement of the Sabin Strain of Type 3 Poliovirus at 2.4 Angstroms and the Crystal Structures of its Variants at 2.9 Angstroms Resolution
Authors: Syed, R. / Filman, D.J. / Hogle, J.M.
#1: Journal: Use of X-Ray Crystallography in the Design of Antiviral Agents
Year: 1990
Title: Structural Determinants of Serotype Specificity Host Range and Thermostability in Poliovirus
Authors: Hogle, J.M. / Syed, R. / Yeates, T.O. / Jacobson, D. / Filman, D.J.
#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: Vaccines 89: Modern Approaches to New Vaccines Including Prevention of Aids
Year: 1989
Title: Structural Determinants of Serotype Specificity in Poliovirus
Authors: Hogle, J.M. / Filman, D.J. / Critchlow, T. / Jacobson, D. / Yeates, T.O. / Syed, R.
#5: Journal: Concepts in Viral Pathogenesis III / Year: 1989
Title: Structural Determinants of Serotype Specificity and Host Range in Poliovirus
Authors: Hogle, J.M. / Syed, R. / Yeates, T.O. / Jacobson, D. / Critchlow, T. / Filman, D.J.
#6: Journal: Molecular Aspects of Picornavirus Infection and Detection
Year: 1989
Title: Structural Basis for Serotypic Differences and Thermostability in Poliovirus
Authors: Hogle, J.M. / Filman, D.J. / Syed, R. / Chow, M. / Minor, P.D.
#7: Journal: Nucleic Acids Res. / Year: 1983
Title: The Nucleotide Sequence of Poliovirus Type 3 Leon 12A(1)B: Comparison with Poliovirus Type 1
Authors: Stanway, G. / Cann, A.J. / Hauptman, R. / Hughes, P. / Clarke, L.D. / Mountford, R.C. / Minor, P.D. / Schild, G.C. / Almond, J.W.
History
DepositionMar 30, 1995Processing site: BNL
Revision 1.0Sep 15, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jun 5, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_struct_oper_list / struct_conn / 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 / _pdbx_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700SHEET STRANDS 2, 3, AND 4 ARE COMMON TO SHEETS *1B1* AND *1B2*. THE SECOND STRAND OF SHEET *1B3* IS ...SHEET STRANDS 2, 3, AND 4 ARE COMMON TO SHEETS *1B1* AND *1B2*. THE SECOND STRAND OF SHEET *1B3* IS THE SAME AS THE THIRD STRAND OF SHEETS *1B1* AND *1B2*. STRANDS 1, 2, AND 3 ARE COMMON TO SHEETS *2B1*, *2B2*, AND *2B3*. STRANDS 1 AND 2 ARE COMMON TO SHEETS *2C1*, *2C2*, AND *2C3*. THE LAST FOUR STRANDS ARE COMMON TO SHEETS *3B1* AND *3B2*. SEQUENCE NUMBERING IS UNCERTAIN IN THE THIRD STRAND OF SHEET * 4N*. SHEET * 3C* CONSISTS OF SEVEN STRANDS. THE FIFTH AND SIXTH STRANDS OF SHEET * 3C* ARE FROM A THREEFOLD-RELATED PROTOMER. BECAUSE OF LIMITATIONS IMPOSED BY THE PROTEIN DATA BANK FORMAT IT IS NOT POSSIBLE TO PRESENT ALL OF THIS SHEET ON SHEET RECORDS. INSTEAD THE COMPLETE SHEET IS SPECIFIED IN THIS REMARK. 3C 7 LEU 3 83 LEU 3 87 0 3C 7 GLY 3 188 PHE 3 193 -1 O GLY 3 188 N LEU 3 87 3C 7 ALA 3 126 ALA 3 135 -1 O ALA 3 135 N TYR 3 189 3C 7 THR 3 152 TRP 3 156 -1 O THR 3 152 N TYR 3 134 3C 7 ASN 2 20 THR 2 25 1 O ASN 2 20 N HIS 3 153 3C 7 LEU 2 14 LEU 2 18 -1 O LEU 2 18 N SER 2 21 3C 7 ALA 1 36 SER 1 38 -1 N ALA 1 36 O THR 2 17 SHEET * TT* CONSISTS OF FIVE STRANDS. ALL FIVE STRANDS OF SHEET * TT* ARE FROM FIVE-FOLD-RELATED PROTOMERS. BECAUSE OF LIMITATIONS IMPOSED BY THE PROTEIN DATA BANK FORMAT IT IS NOT POSSIBLE TO PRESENT THIS SHEET ON SHEET RECORDS. INSTEAD THIS SHEET IS SPECIFIED IN THIS REMARK. TT 5 LEU 3 2 THR 3 7 0 TT 5 LEU 3 2 THR 3 7 1 N LEU 3 2 O PRO 3 3 TT 5 LEU 3 2 THR 3 7 1 N LEU 3 2 O PRO 3 3 TT 5 LEU 3 2 THR 3 7 1 N LEU 3 2 O PRO 3 3 TT 5 LEU 3 2 THR 3 7 1 N LEU 3 2 O PRO 3 3

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)98,4067
Polymers97,8785
Non-polymers5282
Water7,620423
1
0: POLIOVIRUS TYPE 3, SABIN STRAIN
1: POLIOVIRUS TYPE 3, SABIN STRAIN
2: POLIOVIRUS TYPE 3, SABIN STRAIN
3: POLIOVIRUS TYPE 3, SABIN STRAIN
4: POLIOVIRUS TYPE 3, SABIN STRAIN
hetero molecules
x 60


Theoretical massNumber of molelcules
Total (without water)5,904,367420
Polymers5,872,696300
Non-polymers31,672120
Water4,324240
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, SABIN STRAIN
1: POLIOVIRUS TYPE 3, SABIN STRAIN
2: POLIOVIRUS TYPE 3, SABIN STRAIN
3: POLIOVIRUS TYPE 3, SABIN STRAIN
4: POLIOVIRUS TYPE 3, SABIN STRAIN
hetero molecules
x 5


  • icosahedral pentamer
  • 492 kDa, 25 polymers
Theoretical massNumber of molelcules
Total (without water)492,03135
Polymers489,39125
Non-polymers2,63910
Water36020
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
0: POLIOVIRUS TYPE 3, SABIN STRAIN
1: POLIOVIRUS TYPE 3, SABIN STRAIN
2: POLIOVIRUS TYPE 3, SABIN STRAIN
3: POLIOVIRUS TYPE 3, SABIN STRAIN
4: POLIOVIRUS TYPE 3, SABIN STRAIN
hetero molecules
x 6


  • icosahedral 23 hexamer
  • 590 kDa, 30 polymers
Theoretical massNumber of molelcules
Total (without water)590,43742
Polymers587,27030
Non-polymers3,16712
Water43224
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, SABIN STRAIN
1: POLIOVIRUS TYPE 3, SABIN STRAIN
2: POLIOVIRUS TYPE 3, SABIN STRAIN
3: POLIOVIRUS TYPE 3, SABIN STRAIN
4: POLIOVIRUS TYPE 3, SABIN STRAIN
hetero molecules
x 15


  • crystal asymmetric unit, crystal frame
  • 1.48 MDa, 75 polymers
Theoretical massNumber of molelcules
Total (without water)1,476,092105
Polymers1,468,17475
Non-polymers7,91830
Water1,08160
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
Atom site foot note1: CIS PROLINE - PRO 2 83
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 3, SABIN ... , 5 types, 5 molecules 01234

#1: Protein/peptide POLIOVIRUS TYPE 3, SABIN STRAIN


Mass: 446.495 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: SEED STOCK OBTAINED FROM P.D.MINOR (NATIONAL INSTITUTE OF BIOLOGICAL STANDARDS AND CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Species: Poliovirus
Strain: DERIVED FROM LABORATORY STRAIN P3/LEON/12A(1)B PLACQUE 411
#2: Protein POLIOVIRUS TYPE 3, SABIN STRAIN


Mass: 33651.801 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: SEED STOCK OBTAINED FROM P.D.MINOR (NATIONAL INSTITUTE OF BIOLOGICAL STANDARDS AND CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Species: Poliovirus
Strain: DERIVED FROM LABORATORY STRAIN P3/LEON/12A(1)B PLACQUE 411
References: PIR: S03822, UniProt: P03302*PLUS
#3: Protein POLIOVIRUS TYPE 3, SABIN STRAIN


Mass: 30169.920 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: SEED STOCK OBTAINED FROM P.D.MINOR (NATIONAL INSTITUTE OF BIOLOGICAL STANDARDS AND CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Species: Poliovirus
Strain: DERIVED FROM LABORATORY STRAIN P3/LEON/12A(1)B PLACQUE 411
References: UniProt: P03302
#4: Protein POLIOVIRUS TYPE 3, SABIN STRAIN


Mass: 26289.127 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: SEED STOCK OBTAINED FROM P.D.MINOR (NATIONAL INSTITUTE OF BIOLOGICAL STANDARDS AND CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Species: Poliovirus
Strain: DERIVED FROM LABORATORY STRAIN P3/LEON/12A(1)B PLACQUE 411
References: PIR: S03822, UniProt: P03302*PLUS
#5: Protein POLIOVIRUS TYPE 3, SABIN STRAIN


Mass: 7320.917 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Details: SEED STOCK OBTAINED FROM P.D.MINOR (NATIONAL INSTITUTE OF BIOLOGICAL STANDARDS AND CONTROL, LONDON)
Source: (natural) Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)
Genus: Enterovirus / Species: Poliovirus
Strain: DERIVED FROM LABORATORY STRAIN P3/LEON/12A(1)B PLACQUE 411
References: UniProt: P03302

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Non-polymers , 3 types, 425 molecules

#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.: 423 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsTHE MYRISTOYL MOIETY, MYR, IS COVALENTLY LINKED TO GLY 2 OF CHAIN 4 VIA AN AMIDE BOND.
Nonpolymer detailsALTHOUGH ALL OF THE SOLVENT MOLECULES IN THIS FILE HAVE BEEN DESIGNATED TO BE WATER MOLECULES, ...ALTHOUGH ALL OF THE SOLVENT MOLECULES IN THIS FILE HAVE BEEN DESIGNATED TO BE WATER MOLECULES, SEVERAL OF THESE SITES HAVE REFINED OCCUPANCY VALUES GREATER THAN 1.0, AND ARE BELIEVED TO CORRESPOND TO LARGER BOUND ANIONS AND CATIONS. SOLVENT MOLECULE HOH 901 IS THE LARGE FIVE-FOLD PEAK AND PROBABLY AN ANION. SOLVENT MOLECULE HOH 902 IS ANOTHER FIVE-FOLD. SOLVENT MOLECULES HOH 903 AND HOH 904 ARE NEAR THREE-FOLD AXES. SOLVENT MOLECULES HOH 905 AND HOH 906 ARE NEAR TWO-FOLD AXES. SOLVENT MOLECULE HOH 2 IS POSSIBLY A ZN 2+ SITE AND SOLVENT MOLECULE HOH 40 IS ITS TETRAHEDRAL LIGAND. SOLVENT MOLECULES THAT LIE ON N-FOLD SYMMETRY AXES HAVE BEEN ASSIGNED OCCUPANCIES 1/NTH OF THEIR ACTUAL VALUES, TO FACILITATE CALCULATION OF THEIR FOURIER TRANSFORM. (THIS NOTE APPLIES TO ALL SOLVENT MOLECULES).

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Data collection

ReflectionResolution: 2.4→30 Å / Num. obs: 520979 / % possible obs: 61.6 %

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Processing

Software
NameClassification
X-PLORmodel building
X-PLORrefinement
X-PLORphasing
RefinementResolution: 2.4→10 Å / σ(F): 0
Details: THE POLYPEPTIDE DESIGNATED IN THIS FILE AS RESIDUES 7 - 10 OF CHAIN 0 REPRESENTS A FEATURE IN THE ELECTRON DENSITY MAP WHICH APPEARS TO BE A BETA STRAND. ALTHOUGH THE SIDE CHAINS OF THIS ...Details: THE POLYPEPTIDE DESIGNATED IN THIS FILE AS RESIDUES 7 - 10 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. SOLVENT MOLECULES HAVE BEEN ASSIGNED INDIVIDUAL OCCUPANCY VALUES BY THE PSEUDO-REAL-SPACE REFINEMENT PROCEDURE AND AN OVERALL TEMPERATURE FACTOR BY THE XPLOR PROGRAM. RESIDUE 1000 IS IDENTIFIED AS A SPHINGOSINE MOLECULE (SPH). THE PROVISIONAL IDENTIFICATION OF ELECTRON DENSITY AS SPHINGOSINE IS NOT BASED ON DIRECT CHEMICAL EVIDENCE.
RfactorNum. reflection% reflection
obs0.205 511849 61.4 %
Refinement stepCycle: LAST / Resolution: 2.4→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6631 0 21 423 7075
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_deg2.86
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

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