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- PDB-3tgx: IL-21:IL21R complex -

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Basic information

Entry
Database: PDB / ID: 3tgx
TitleIL-21:IL21R complex
Components
  • Interleukin-21
  • Interleukin-21 receptor
KeywordsCYTOKINE/CYTOKINE RECEPTOR / Class I cytokine / Class I cytokine Receptor / sugarbridge / Fibronectin domain / Signaling / CYTOKINE-CYTOKINE RECEPTOR complex
Function / homology
Function and homology information


interleukin-21 receptor activity / T follicular helper cell differentiation / interleukin-2 receptor binding / germinal center B cell differentiation / positive regulation of tissue remodeling / Interleukin-21 signaling / positive regulation of natural killer cell mediated cytotoxicity / cytokine receptor binding / tyrosine phosphorylation of STAT protein / natural killer cell activation ...interleukin-21 receptor activity / T follicular helper cell differentiation / interleukin-2 receptor binding / germinal center B cell differentiation / positive regulation of tissue remodeling / Interleukin-21 signaling / positive regulation of natural killer cell mediated cytotoxicity / cytokine receptor binding / tyrosine phosphorylation of STAT protein / natural killer cell activation / cytokine receptor activity / positive regulation of immunoglobulin production / positive regulation of interleukin-17 production / immunoglobulin mediated immune response / positive regulation of tyrosine phosphorylation of STAT protein / positive regulation of B cell proliferation / positive regulation of T cell proliferation / cell maturation / positive regulation of cytokine production / cytokine activity / cellular response to virus / cytokine-mediated signaling pathway / positive regulation of inflammatory response / positive regulation of type II interferon production / transmembrane signaling receptor activity / defense response to virus / external side of plasma membrane / positive regulation of cell population proliferation / signal transduction / extracellular space / extracellular region / membrane / plasma membrane
Similarity search - Function
Interleukin-15/Interleukin-21 / Interleukin-15/Interleukin-21 family / Interleukin 15 / Short hematopoietin receptor family 1 signature. / Short hematopoietin receptor, family 1, conserved site / Growth Hormone; Chain: A; / Four-helical cytokine-like, core / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily ...Interleukin-15/Interleukin-21 / Interleukin-15/Interleukin-21 family / Interleukin 15 / Short hematopoietin receptor family 1 signature. / Short hematopoietin receptor, family 1, conserved site / Growth Hormone; Chain: A; / Four-helical cytokine-like, core / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulins / Immunoglobulin-like fold / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
alpha-D-mannopyranose / NICKEL (II) ION / Interleukin-21 / Interleukin-21 receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 2.8 Å
AuthorsHamming, O.J. / Kang, L. / Svenson, A. / Karlsen, J.L. / Rahbek-Nielsen, H. / Paludan, S.R. / Hjort, S.A. / Bondensgaard, K. / Hartmann, R.
CitationJournal: J.Biol.Chem. / Year: 2012
Title: The crystal structure of the interleukin 21 receptor bound to interleukin 21 reveals that a sugar chain interacting with the WSXWS motif is an integral part of the interleukin 21 receptor.
Authors: Hamming, O.J. / Kang, L. / Svensson, A. / Karlsen, J.L. / Rahbek-Nielsen, H. / Paludan, S.R. / Hjorth, S.A. / Bondensgaard, K. / Hartmann, R.
History
DepositionAug 18, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 15, 2012Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2017Group: Advisory / Database references / Category: pdbx_unobs_or_zero_occ_atoms / struct_ref_seq_dif
Item: _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _struct_ref_seq_dif.details
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_unobs_or_zero_occ_atoms.auth_asym_id / _pdbx_unobs_or_zero_occ_atoms.auth_comp_id / _pdbx_unobs_or_zero_occ_atoms.auth_seq_id / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _pdbx_unobs_or_zero_occ_atoms.label_comp_id / _pdbx_unobs_or_zero_occ_atoms.label_seq_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_atom_id_1 / _pdbx_validate_close_contact.auth_atom_id_2 / _pdbx_validate_close_contact.auth_comp_id_1 / _pdbx_validate_close_contact.auth_comp_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _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_asym_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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 27, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_validate_close_contact / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Nov 6, 2024Group: Structure summary / Category: 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
A: Interleukin-21 receptor
B: Interleukin-21
C: Interleukin-21 receptor
D: Interleukin-21
E: Interleukin-21 receptor
F: Interleukin-21
G: Interleukin-21 receptor
H: Interleukin-21
I: Interleukin-21 receptor
J: Interleukin-21
K: Interleukin-21 receptor
L: Interleukin-21
M: Interleukin-21 receptor
N: Interleukin-21
O: Interleukin-21 receptor
P: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)343,28275
Polymers328,59416
Non-polymers14,68959
Water00
1
A: Interleukin-21 receptor
B: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,9169
Polymers41,0742
Non-polymers1,8427
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4800 Å2
ΔGint-14 kcal/mol
Surface area17150 Å2
MethodPISA
2
C: Interleukin-21 receptor
D: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,05010
Polymers41,0742
Non-polymers1,9768
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5000 Å2
ΔGint-26 kcal/mol
Surface area17440 Å2
MethodPISA
3
E: Interleukin-21 receptor
F: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,9169
Polymers41,0742
Non-polymers1,8427
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4750 Å2
ΔGint-10 kcal/mol
Surface area17100 Å2
MethodPISA
4
G: Interleukin-21 receptor
H: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,10911
Polymers41,0742
Non-polymers2,0349
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4920 Å2
ΔGint-22 kcal/mol
Surface area17540 Å2
MethodPISA
5
I: Interleukin-21 receptor
J: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,8588
Polymers41,0742
Non-polymers1,7846
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4760 Å2
ΔGint-9 kcal/mol
Surface area17340 Å2
MethodPISA
6
K: Interleukin-21 receptor
L: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,88810
Polymers41,0742
Non-polymers1,8138
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4710 Å2
ΔGint-36 kcal/mol
Surface area17310 Å2
MethodPISA
7
M: Interleukin-21 receptor
N: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,6968
Polymers41,0742
Non-polymers1,6216
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4370 Å2
ΔGint-16 kcal/mol
Surface area17020 Å2
MethodPISA
8
O: Interleukin-21 receptor
P: Interleukin-21
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,85010
Polymers41,0742
Non-polymers1,7768
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4550 Å2
ΔGint-25 kcal/mol
Surface area17090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.230, 151.120, 364.820
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
12
22
32
42
52
62
72
82

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and (resseq 1:157 or resseq 162: 171 or resseq 174:207 or resseq 569:572 or resseq 580)
211chain C and (resseq 1:157 or resseq 162: 171 or resseq 174:207 or resseq 569:572 or resseq 580)
311chain E and (resseq 1:157 or resseq 162: 171 or resseq 174:207 or resseq 569:572 or resseq 580)
411chain G and (resseq 1:157 or resseq 162: 171 or resseq 174:207 or resseq 569:572 or resseq 580)
511chain I and (resseq 1:157 or resseq 162: 171 or resseq 174:207 or resseq 569:572 or resseq 580)
611chain K and (resseq 1:157 or resseq 162: 171 or resseq 174:207 or resseq 569:572 or resseq 580)
711chain M and (resseq 1:157 or resseq 162: 171 or resseq 174:207 or resseq 569:572 or resseq 580)
811chain O and (resseq 1:157 or resseq 162: 171 or resseq 174:207 or resseq 569:572 or resseq 580)
112chain B and (resseq 5:81 or resseq 93:119 or resseq 600:602 )
212chain D and (resseq 5:81 or resseq 93:119 or resseq 600:602 )
312chain F and (resseq 5:81 or resseq 93:119 or resseq 600:602 )
412chain H and (resseq 5:81 or resseq 93:119 or resseq 600:602 )
512chain J and (resseq 5:81 or resseq 93:119 or resseq 600:602 )
612chain L and (resseq 5:81 or resseq 93:119 or resseq 600:602 )
712chain N and (resseq 5:81 or resseq 93:119 or resseq 600:602 )
812chain P and (resseq 5:81 or resseq 93:119 or resseq 600:602 )

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 16 molecules ACEGIKMOBDFHJLNP

#1: Protein
Interleukin-21 receptor / IL-21 receptor / IL-21R / Novel interleukin receptor


Mass: 25451.297 Da / Num. of mol.: 8 / Fragment: Interleukin 21 receptor extracellular domain / Mutation: N78Q, N85Q, N106D, N116Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL21R, NILR, UNQ3121/PRO10273 / Cell line (production host): HEK293 / Production host: Homo Sapiens (human) / References: UniProt: Q9HBE5
#2: Protein
Interleukin-21 / IL-21 / Za11


Mass: 15622.893 Da / Num. of mol.: 8 / Fragment: unp RESIDUES 23-155
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL21 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9HBE4

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Sugars , 4 types, 16 molecules

#3: Polysaccharide
alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-beta-D- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1219.105 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpa1-6DManpa1-6DManpb1-4DGlcpNAcb1-4[LFucpb1-6]DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/4,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1b_1-5]/1-1-2-3-3-3-4/a4-b1_a6-g1_b4-c1_c6-d1_d6-e1_e6-f1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{[(6+1)][a-D-Manp]{[(6+1)][a-D-Manp]{}}}}}[(6+1)][b-L-Fucp]{}}LINUCSPDB-CARE
#4: Polysaccharide alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1056.964 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpa1-6DManpb1-4DGlcpNAcb1-4[LFucpb1-6]DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/4,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1b_1-5]/1-1-2-3-3-4/a4-b1_a6-f1_b4-c1_c6-d1_d6-e1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{[(6+1)][a-D-Manp]{}}}}[(6+1)][b-L-Fucp]{}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1056.964 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpa1-6DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/4,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-3-4/a4-b1_a6-f1_b4-c1_c6-d1_d6-e1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{[(6+1)][a-D-Manp]{}}}}[(6+1)][a-L-Fucp]{}}LINUCSPDB-CARE
#6: Sugar
ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 2 types, 43 molecules

#7: Chemical
ChemComp-NI / NICKEL (II) ION


Mass: 58.693 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ni
#8: Chemical...
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 39 / Source method: obtained synthetically / Formula: SO4

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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: 3

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Sample preparation

CrystalDensity Matthews: 3.45 Å3/Da / Density % sol: 64.34 %
Crystal growTemperature: 291.3 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 1,8-1,9 M di-Ammonium sulphate and 0.1 M Sodium acetate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 291.3K

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.98 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 2.8→94.7 Å / % possible obs: 99.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5.2 % / Rmerge(I) obs: 0.187 / Net I/σ(I): 30.1
Reflection shellResolution: 2.8→3 Å / Rmerge(I) obs: 0.483 / Mean I/σ(I) obs: 3.6 / % possible all: 69.1

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Processing

SoftwareName: PHENIX / Version: (phenix.refine: 1.7.1_743) / Classification: refinement
RefinementMethod to determine structure: SIRAS / Resolution: 2.8→80.22 Å / SU ML: 0.87 / σ(F): 1.99 / Phase error: 28.93 / Stereochemistry target values: MLHL
RfactorNum. reflection% reflection
Rfree0.273 5632 5 %
Rwork0.242 --
obs0.244 112594 99.7 %
Solvent computationShrinkage radii: 0.72 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 41.47 Å2 / ksol: 0.33 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-3.8538 Å2-0 Å20 Å2
2--2.0307 Å20 Å2
3----6.5072 Å2
Refinement stepCycle: LAST / Resolution: 2.8→80.22 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20920 0 910 0 21830
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.02522436
X-RAY DIFFRACTIONf_angle_d1.7930487
X-RAY DIFFRACTIONf_dihedral_angle_d21.4118591
X-RAY DIFFRACTIONf_chiral_restr0.1693402
X-RAY DIFFRACTIONf_plane_restr0.0063786
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A1683X-RAY DIFFRACTIONPOSITIONAL
12C1683X-RAY DIFFRACTIONPOSITIONAL0.656
13E1694X-RAY DIFFRACTIONPOSITIONAL0.68
14G1694X-RAY DIFFRACTIONPOSITIONAL0.655
15I1683X-RAY DIFFRACTIONPOSITIONAL0.566
16K1683X-RAY DIFFRACTIONPOSITIONAL0.682
17M1694X-RAY DIFFRACTIONPOSITIONAL0.655
18O1683X-RAY DIFFRACTIONPOSITIONAL0.817
21B850X-RAY DIFFRACTIONPOSITIONAL
22D850X-RAY DIFFRACTIONPOSITIONAL0.927
23F850X-RAY DIFFRACTIONPOSITIONAL0.93
24H850X-RAY DIFFRACTIONPOSITIONAL0.912
25J850X-RAY DIFFRACTIONPOSITIONAL0.866
26L850X-RAY DIFFRACTIONPOSITIONAL0.964
27N850X-RAY DIFFRACTIONPOSITIONAL0.924
28P850X-RAY DIFFRACTIONPOSITIONAL0.961
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.83180.39681860.3663530X-RAY DIFFRACTION99
2.8318-2.86510.38221850.35653504X-RAY DIFFRACTION99
2.8651-2.90010.37011840.3463508X-RAY DIFFRACTION100
2.9001-2.93680.3641860.34113526X-RAY DIFFRACTION99
2.9368-2.97540.42221830.3413479X-RAY DIFFRACTION100
2.9754-3.01620.40621880.32833567X-RAY DIFFRACTION100
3.0162-3.05930.39611850.31063518X-RAY DIFFRACTION100
3.0593-3.1050.36761840.31643490X-RAY DIFFRACTION100
3.105-3.15350.33821880.29263574X-RAY DIFFRACTION100
3.1535-3.20520.3161830.29763491X-RAY DIFFRACTION100
3.2052-3.26040.37411870.28783543X-RAY DIFFRACTION100
3.2604-3.31970.30711850.2793526X-RAY DIFFRACTION100
3.3197-3.38360.31171860.26623529X-RAY DIFFRACTION100
3.3836-3.45270.28911880.26013571X-RAY DIFFRACTION100
3.4527-3.52770.25261850.25153521X-RAY DIFFRACTION100
3.5277-3.60980.25271870.23443550X-RAY DIFFRACTION100
3.6098-3.70010.27591860.23293540X-RAY DIFFRACTION100
3.7001-3.80010.27061870.23363548X-RAY DIFFRACTION100
3.8001-3.91190.28281880.23543576X-RAY DIFFRACTION100
3.9119-4.03820.24491850.22923514X-RAY DIFFRACTION100
4.0382-4.18250.24911890.20163594X-RAY DIFFRACTION100
4.1825-4.350.21251890.19043588X-RAY DIFFRACTION100
4.35-4.54790.19821880.18323580X-RAY DIFFRACTION100
4.5479-4.78770.21491880.1873567X-RAY DIFFRACTION100
4.7877-5.08760.22491900.18943613X-RAY DIFFRACTION100
5.0876-5.48030.24851910.21293626X-RAY DIFFRACTION100
5.4803-6.03160.23051900.23153614X-RAY DIFFRACTION100
6.0316-6.9040.3011930.24043662X-RAY DIFFRACTION100
6.904-8.69670.2061940.22543676X-RAY DIFFRACTION100
8.6967-80.25040.26182040.243837X-RAY DIFFRACTION98

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