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- PDB-1rhi: HUMAN RHINOVIRUS 3 COAT PROTEIN -

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Basic information

Entry
Database: PDB / ID: 1rhi
TitleHUMAN RHINOVIRUS 3 COAT PROTEIN
Components(HUMAN RHINOVIRUS 3 COAT PROTEIN) x 4
KeywordsVIRUS / HUMAN RHINOVIRUS 3 / COAT PROTEIN / Icosahedral virus
Function / homology
Function and homology information


symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I 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 / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / channel activity ...symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I 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 / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / DNA replication / 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 / 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 / Picornavirus coat protein VP4 superfamily / 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 coat protein VP4 / Rhinovirus 14, subunit 4 / Picornavirus coat protein VP4 superfamily / 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 / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / 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
Biological speciesHuman rhinovirus 3
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsZhao, R. / Rossmann, M.G.
Citation
#1: Journal: Protein Sci. / Year: 1994
Title: Viral Cell Recognition and Entry
Authors: Rossmann, M.G.
#2: Journal: J.Mol.Biol. / Year: 1993
Title: A Comparison of the Anti-Rhinoviral Drug Binding Pocket in Hrv14 and Hrv1A
Authors: Kim, K.H. / Willingmann, P. / Gong, Z.X. / Kremer, M.J. / Chapman, M.S. / Minor, I. / Oliveira, M.A. / Rossmann, M.G. / Andries, K. / Diana, G.D. / al., et
#3: Journal: Structure / Year: 1993
Title: The Structure of Human Rhinovirus 16
Authors: Oliveira, M.A. / Zhao, R. / Lee, W.M. / Kremer, M.J. / Minor, I. / Rueckert, R.R. / Diana, G.D. / Pevear, D.C. / Dutko, F.J. / Mckinlay, M.A. / al., et
#4: Journal: J.Mol.Biol. / Year: 1989
Title: Crystal Structure of Human Rhinovirus Serotype 1A (Hrv1A)
Authors: Kim, S.S. / Smith, T.J. / Chapman, M.S. / Rossmann, M.C. / Pevear, D.C. / Dutko, F.J. / Felock, P.J. / Diana, G.D. / Mckinlay, M.A.
#5: Journal: Nature / Year: 1985
Title: Structure of a Human Common Cold Virus and Functional Relationship to Other Picornaviruses
Authors: Rossmann, M.G. / Arnold, E. / Erickson, J.W. / Frankenberger, E.A. / Griffith, J.P. / Hecht, H.J. / Johnson, J.E. / Kamer, G. / Luo, M. / Mosser, A.G. / al., et
History
DepositionJun 17, 1996Processing site: BNL
Revision 1.0Mar 12, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 16, 2012Group: Advisory
Revision 2.0Apr 19, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Other / Refinement description
Category: atom_site / cell ...atom_site / cell / database_2 / database_PDB_matrix / pdbx_database_remark / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_oper_list / pdbx_validate_rmsd_angle / pdbx_validate_rmsd_bond / pdbx_validate_torsion / struct_conn / struct_ncs_oper / struct_ref_seq_dif / struct_site
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_2.pdbx_DOI / _database_2.pdbx_database_accession / _database_PDB_matrix.origx[1][1] / _database_PDB_matrix.origx[1][3] / _database_PDB_matrix.origx[3][1] / _database_PDB_matrix.origx[3][3] / _database_PDB_matrix.origx_vector[2] / _pdbx_database_status.process_site / _pdbx_validate_rmsd_angle.angle_deviation / _pdbx_validate_rmsd_angle.angle_value / _pdbx_validate_rmsd_bond.bond_deviation / _pdbx_validate_rmsd_bond.bond_value / _pdbx_validate_torsion.phi / _pdbx_validate_torsion.psi / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Details: Coordinates and associated matrices have been transformed from the icosahedral point symmetry frame to the crystallographic frame
Provider: repository / Type: Remediation
Revision 2.1Apr 3, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
1: HUMAN RHINOVIRUS 3 COAT PROTEIN
2: HUMAN RHINOVIRUS 3 COAT PROTEIN
3: HUMAN RHINOVIRUS 3 COAT PROTEIN
4: HUMAN RHINOVIRUS 3 COAT PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,3475
Polymers94,3074
Non-polymers401
Water00
1
1: HUMAN RHINOVIRUS 3 COAT PROTEIN
2: HUMAN RHINOVIRUS 3 COAT PROTEIN
3: HUMAN RHINOVIRUS 3 COAT PROTEIN
4: HUMAN RHINOVIRUS 3 COAT PROTEIN
hetero molecules
x 60


Theoretical massNumber of molelcules
Total (without water)5,660,834300
Polymers5,658,430240
Non-polymers2,40560
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
1: HUMAN RHINOVIRUS 3 COAT PROTEIN
2: HUMAN RHINOVIRUS 3 COAT PROTEIN
3: HUMAN RHINOVIRUS 3 COAT PROTEIN
4: HUMAN RHINOVIRUS 3 COAT PROTEIN
hetero molecules
x 5


  • icosahedral pentamer
  • 472 kDa, 20 polymers
Theoretical massNumber of molelcules
Total (without water)471,73625
Polymers471,53620
Non-polymers2005
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation4
4
1: HUMAN RHINOVIRUS 3 COAT PROTEIN
2: HUMAN RHINOVIRUS 3 COAT PROTEIN
3: HUMAN RHINOVIRUS 3 COAT PROTEIN
4: HUMAN RHINOVIRUS 3 COAT PROTEIN
hetero molecules
x 6


  • icosahedral 23 hexamer
  • 566 kDa, 24 polymers
Theoretical massNumber of molelcules
Total (without water)566,08330
Polymers565,84324
Non-polymers2406
Water0
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
1: HUMAN RHINOVIRUS 3 COAT PROTEIN
2: HUMAN RHINOVIRUS 3 COAT PROTEIN
3: HUMAN RHINOVIRUS 3 COAT PROTEIN
4: HUMAN RHINOVIRUS 3 COAT PROTEIN
hetero molecules
x 30


  • crystal asymmetric unit, crystal frame
  • 120-MERIC
  • 2.83 MDa, 120 polymers
Theoretical massNumber of molelcules
Total (without water)2,830,417150
Polymers2,829,215120
Non-polymers1,20230
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
point symmetry operation29
Unit cell
Length a, b, c (Å)397.900, 341.800, 301.700
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21221
SymmetryPoint symmetry: (Hermann–Mauguin notation: 532 / Schoenflies symbol: I (icosahedral))
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2generate(0.81609459, 0.49064786, -0.30537569), (-0.49064782, 0.30901699, -0.81472273), (-0.30537569, 0.8147228, 0.4929224)-41.99294, 59.13897, -69.72945
3generate(0.51852939, 0.30323705, -0.79948393), (-0.30323702, -0.80901699, -0.50352634), (-0.79948393, 0.50352639, -0.32754638)-25.95306, 154.82783, -43.09517
4generate(0.51852939, -0.30323705, -0.79948393), (0.30323702, -0.80901699, 0.50352634), (-0.79948393, -0.50352639, -0.32754638)25.95306, 154.82783, 43.09517
5generate(0.81609459, -0.49064786, -0.30537569), (0.49064782, 0.30901699, 0.81472273), (-0.30537569, -0.8147228, 0.4929224)41.99294, 59.13897, 69.72945
6generate(0.32038678, 0.81252289, -0.48698965), (0.81252282, -0.5, -0.29967749), (-0.48698965, -0.29967752, -0.82038678)-69.54117, 128.38008, 25.64842
7generate(0.01151814, 0.0115189, -0.99986731), (0.99993361, 0.0115189), (0.00013269, -0.9999337, -0.01151814)-0.98586, 85.58672, 85.58105
8generate(0.30908333, -0.80540382, -0.50575907), (0.81252282, 0.5, -0.29967749), (0.49424093, -0.31831549, 0.80895065)68.93187, 42.79336, 27.24358
9generate(0.80185739, -0.50928584, 0.31249429), (0.50928579, 0.30901699, -0.80320383), (0.31249428, 0.8032039, 0.5071596)43.5881, 59.13897, -68.74359
10generate(0.8088433, 0.49064786, 0.32409443), (0.50928579, -0.30901699, -0.80320383), (-0.29393955, 0.8147228, -0.49982631)-41.99294, 112.03447, -69.72945
11generate(-0.80185739, -0.50928584, -0.31249429), (-0.50928579, 0.30901699, 0.80320383), (-0.31249428, 0.8032039, -0.5071596)43.5881, 59.13897, -68.74359
12generate(-0.30908333, -0.80540382, 0.50575907), (-0.81252282, 0.5, 0.29967749), (-0.49424093, -0.31831549, -0.80895065)68.93187, 42.79336, 27.24358
13generate(-0.01151814, 0.0115189, 0.99986731), (-0.99993361, -0.0115189), (-0.00013269, -0.9999337, 0.01151814)-0.98586, 85.58672, 85.58105
14generate(-0.32038678, 0.81252289, 0.48698965), (-0.81252282, -0.5, 0.29967749), (0.48698965, -0.29967752, 0.82038678)-69.54117, 128.38008, 25.64842
15generate(-0.8088433, 0.49064786, -0.32409443), (-0.50928579, -0.30901699, 0.80320383), (0.29393955, 0.8147228, 0.49982631)-41.99294, 112.03447, -69.72945
16generate(0.8088433, -0.50928584, -0.29393955), (-0.49064782, -0.30901699, -0.81472273), (0.32409443, 0.8032039, -0.49982631)43.5881, 112.03447, -68.74359
17generate(0.99973463, 0.02303627), (-1), (0.02303627, -0.99973463)171.17344
18generate(0.8088433, 0.50928584, -0.29393955), (0.49064782, -0.30901699, 0.81472273), (0.32409443, -0.8032039, -0.49982631)-43.5881, 112.03447, 68.74359
19generate(0.49997466, 0.31475595, -0.80681722), (0.30323702, 0.80901699, 0.50352634), (0.81121676, -0.49640731, 0.30904233)-26.93893, 16.34561, 42.48587
20generate(0.49997466, -0.31475595, -0.80681722), (-0.30323702, 0.80901699, -0.50352634), (0.81121676, 0.49640731, 0.30904233)26.93893, 16.34561, -42.48587
21generate(-0.01151814, 0.9999337, -0.00013269), (-0.0115189, 0.99993361), (0.99986731, 0.0115189, 0.01151814)-85.58105, 85.58672, -0.98586
22generate(-0.49997466, 0.30323705, -0.81121676), (-0.31475592, 0.80901699, 0.49640727), (0.80681722, 0.50352639, -0.30904233)-25.95306, 16.34561, -43.09517
23generate(-0.30908333, -0.81252289, -0.49424093), (-0.80540374, 0.5, -0.31831546), (0.50575907, 0.29967752, -0.80895065)69.54117, 42.79336, -25.64842
24generate(0.29735051, -0.80540382, 0.51274498), (-0.80540374, -0.5, -0.31831546), (0.51274498, -0.31831549, -0.79735051)68.93187, 128.38008, 27.24358
25generate(0.48125592, 0.31475595, 0.81812067), (-0.31475592, -0.80901699, 0.49640727), (0.81812067, -0.49640731, -0.29027291)-26.93893, 154.82783, 42.48587
26generate(-0.29735051, -0.80540382, -0.51274498), (0.80540374, -0.5, 0.31831546), (-0.51274498, -0.31831549, 0.79735051)68.93187, 128.38008, 27.24358
27generate(0.30908333, -0.81252289, 0.49424093), (0.80540374, 0.5, 0.31831546), (-0.50575907, 0.29967752, 0.80895065)69.54117, 42.79336, -25.64842
28generate(0.49997466, 0.30323705, 0.81121676), (0.31475592, 0.80901699, -0.49640727), (-0.80681722, 0.50352639, 0.30904233)-25.95306, 16.34561, -43.09517
29generate(0.01151814, 0.9999337, 0.00013269), (0.0115189, -0.99993361), (-0.99986731, 0.0115189, -0.01151814)-85.58105, 85.58672, -0.98586
30generate(-0.48125592, 0.31475595, -0.81812067), (0.31475592, -0.80901699, -0.49640727), (-0.81812067, -0.49640731, 0.29027291)-26.93893, 154.82783, 42.48587

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Components

#1: Protein HUMAN RHINOVIRUS 3 COAT PROTEIN


Mass: 32328.193 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus 3 / Genus: Rhinovirus / Cell line: HELA CELL / Species: Human rhinovirus B / References: UniProt: Q82081
#2: Protein HUMAN RHINOVIRUS 3 COAT PROTEIN


Mass: 28700.510 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus 3 / Genus: Rhinovirus / Cell line: HELA CELL / Species: Human rhinovirus B / References: UniProt: Q82081
#3: Protein HUMAN RHINOVIRUS 3 COAT PROTEIN


Mass: 26058.602 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus 3 / Genus: Rhinovirus / Cell line: HELA CELL / Species: Human rhinovirus B / References: UniProt: Q82081
#4: Protein HUMAN RHINOVIRUS 3 COAT PROTEIN


Mass: 7219.854 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human rhinovirus 3 / Genus: Rhinovirus / Cell line: HELA CELL / Species: Human rhinovirus B / References: UniProt: Q82081
#5: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 45

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Sample preparation

CrystalDensity Matthews: 2.5 Å3/Da / Density % sol: 49 %
Crystal growMethod: vapor diffusion, hanging drop / pH: 7.2
Details: RESERVOIR SOLUTION: 10MM CACL2 AND 0.75% PEG8000 IN A 0.25M HEPES/0.75M NACL/PH7.2 BUFFER HANGING DROP: 5UL OF 10MG/ML VIRUS + 5UL OF RESERVOIR SOLUTION, vapor diffusion - hanging drop
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
15 mg/mlvirus1drop
25 mM1dropCaCl2
30.375 %PEG80001drop
40.125 MHEPES1drop
50.375 M1dropNaCl
610 mM1reservoirCaCl2
70.75 %PEG80001reservoir
80.25 MHEPES1reservoir
90.75 M1reservoirNaCl

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: F1 / Wavelength: 0.918
DetectorType: FUJI / Detector: IMAGE PLATE / Date: Sep 16, 1993
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.918 Å / Relative weight: 1
ReflectionResolution: 2.8→30 Å / Num. obs: 730925 / % possible obs: 73.1 % / Observed criterion σ(I): 3 / Redundancy: 2.6 % / Rmerge(I) obs: 0.12 / Net I/σ(I): 3
Reflection shellResolution: 2.8→3.12 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.189 / Mean I/σ(I) obs: 3 / % possible all: 47
Reflection shell
*PLUS
% possible obs: 47 % / Num. unique obs: 139901

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
MGROSCdata reduction
MGRSCLdata scaling
X-PLOR3.1phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: HUMAN RHINOVIRUS 14

Resolution: 3→5 Å / σ(F): 3
Details: REFINEMENT WAS CARRIED OUT PRIMARILY TO OBTAIN REASONABLE GEOMETRY AND TO AVOID UNACCEPTABLE NON-BONDED ATOMIC CONTACTS. ICOSAHEDRAL SYMMETRY WAS RETAINED BY CONSTRAINING THE NON- ...Details: REFINEMENT WAS CARRIED OUT PRIMARILY TO OBTAIN REASONABLE GEOMETRY AND TO AVOID UNACCEPTABLE NON-BONDED ATOMIC CONTACTS. ICOSAHEDRAL SYMMETRY WAS RETAINED BY CONSTRAINING THE NON-CRYSTALLOGRAPHICALLY RELATED SUBUNITS DURING CONJUGATE GRADIENT ENERGY MINIMIZATION. THE PUTATIVE CALCIUM ION WAS NOT INCLUDED IN THE REFINEMENTS.
RfactorNum. reflection% reflection
Rfree0.288 -20 %
Rwork0.284 --
obs0.284 397586 64 %
Displacement parametersBiso mean: 15 Å2
Refinement stepCycle: LAST / Resolution: 3→5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6287 0 1 0 6288
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.01
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg1.769
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d27.08
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.211
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Refine LS restraints NCSNCS model details: ICOSAHEDRON
LS refinement shellResolution: 3→3.1 Å
RfactorNum. reflection% reflection
Rfree0.349 -20 %
Rwork0.345 41869 -
obs--56 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPH19.PEP
X-RAY DIFFRACTION2TOPHCSDX.PRO
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refinement
*PLUS
Rfactor obs: 0.281
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.009
X-RAY DIFFRACTIONx_angle_deg1.8
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg27.08
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.211

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