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- PDB-7q5t: The tandem SH2 domains of SYK with a bound FCER1G diphospho-ITAM ... -

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Basic information

Entry
Database: PDB / ID: 7q5t
TitleThe tandem SH2 domains of SYK with a bound FCER1G diphospho-ITAM peptide
Components
  • High affinity immunoglobulin epsilon receptor subunit gamma
  • Tyrosine-protein kinase SYK
KeywordsTRANSFERASE / Signalling / kinase
Function / homology
Function and homology information


IgE receptor activity / Fc-epsilon receptor I complex / Fc receptor mediated stimulatory signaling pathway / T cell differentiation involved in immune response / negative regulation of mast cell apoptotic process / mast cell apoptotic process / Fc-gamma receptor III complex / interleukin-15 receptor binding / regulation of superoxide anion generation / regulation of neutrophil degranulation ...IgE receptor activity / Fc-epsilon receptor I complex / Fc receptor mediated stimulatory signaling pathway / T cell differentiation involved in immune response / negative regulation of mast cell apoptotic process / mast cell apoptotic process / Fc-gamma receptor III complex / interleukin-15 receptor binding / regulation of superoxide anion generation / regulation of neutrophil degranulation / regulation of arachidonate secretion / positive regulation of interleukin-3 production / cellular response to lectin / B cell receptor complex / Toll-like receptor binding / regulation of platelet aggregation / positive regulation of alpha-beta T cell proliferation / serotonin secretion by platelet / leukocyte activation involved in immune response / neutrophil activation involved in immune response / lymph vessel development / positive regulation of mast cell degranulation / gamma-delta T cell differentiation / positive regulation of mast cell cytokine production / collagen-activated tyrosine kinase receptor signaling pathway / positive regulation of gamma-delta T cell differentiation / cell surface pattern recognition receptor signaling pathway / positive regulation of type III hypersensitivity / Fc-gamma receptor signaling pathway / regulation of platelet activation / cell activation / Platelet Adhesion to exposed collagen / positive regulation of type IIa hypersensitivity / beta selection / IgE binding / cellular response to molecule of fungal origin / FLT3 signaling through SRC family kinases / early phagosome / leukotriene biosynthetic process / regulation of phagocytosis / regulation of DNA-binding transcription factor activity / regulation of tumor necrosis factor-mediated signaling pathway / positive regulation of type I hypersensitivity / positive regulation of protein localization to cell surface / macrophage activation involved in immune response / interleukin-3-mediated signaling pathway / positive regulation of bone resorption / positive regulation of monocyte chemotactic protein-1 production / cellular response to lipid / Fc epsilon receptor (FCERI) signaling / Interleukin-2 signaling / positive regulation of granulocyte macrophage colony-stimulating factor production / positive regulation of alpha-beta T cell differentiation / blood vessel morphogenesis / positive regulation of cell adhesion mediated by integrin / IgG binding / positive regulation of B cell differentiation / T cell receptor complex / leukocyte cell-cell adhesion / phagocytosis, engulfment / mast cell degranulation / Dectin-2 family / antigen processing and presentation of exogenous peptide antigen via MHC class I / positive regulation of interleukin-4 production / Fc-epsilon receptor signaling pathway / stimulatory C-type lectin receptor signaling pathway / Fc-gamma receptor signaling pathway involved in phagocytosis / amyloid-beta clearance / immunoglobulin mediated immune response / tertiary granule membrane / positive regulation of interleukin-10 production / positive regulation of receptor internalization / FCGR activation / cellular response to low-density lipoprotein particle stimulus / ficolin-1-rich granule membrane / Role of LAT2/NTAL/LAB on calcium mobilization / positive regulation of type I interferon production / Role of phospholipids in phagocytosis / phosphatase binding / regulation of ERK1 and ERK2 cascade / phospholipase binding / GPVI-mediated activation cascade / Signaling by CSF3 (G-CSF) / positive regulation of superoxide anion generation / phosphotyrosine residue binding / neutrophil chemotaxis / Integrin signaling / positive regulation of interleukin-12 production / positive regulation of TORC1 signaling / FCERI mediated Ca+2 mobilization / SH2 domain binding / positive regulation of calcium-mediated signaling / FCGR3A-mediated IL10 synthesis / positive regulation of phagocytosis / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / osteoclast differentiation / peptidyl-tyrosine phosphorylation / B cell differentiation / animal organ morphogenesis / integrin-mediated signaling pathway
Similarity search - Function
High affinity immunoglobulin epsilon receptor subunit gamma / T-cell surface glycoprotein CD3 zeta subunit/High affinity IgE receptor gamma subunit / T-cell surface glycoprotein CD3 zeta chain / Tyrosine-protein kinase, non-receptor SYK/ZAP-70 / Tyrosine-protein kinase SYK/ZAP-70, inter-SH2 domain superfamily / SYK/ZAP-70, N-terminal SH2 domain / Immunoreceptor tyrosine-based activation motif / Phosphorylated immunoreceptor signalling ITAM / ITAM motif mammalian type profile. / Immunoreceptor tyrosine-based activation motif ...High affinity immunoglobulin epsilon receptor subunit gamma / T-cell surface glycoprotein CD3 zeta subunit/High affinity IgE receptor gamma subunit / T-cell surface glycoprotein CD3 zeta chain / Tyrosine-protein kinase, non-receptor SYK/ZAP-70 / Tyrosine-protein kinase SYK/ZAP-70, inter-SH2 domain superfamily / SYK/ZAP-70, N-terminal SH2 domain / Immunoreceptor tyrosine-based activation motif / Phosphorylated immunoreceptor signalling ITAM / ITAM motif mammalian type profile. / Immunoreceptor tyrosine-based activation motif / : / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / SH2 domain superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / PHOSPHATE ION / High affinity immunoglobulin epsilon receptor subunit gamma / Tyrosine-protein kinase SYK
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsBradshaw, W.J. / Katis, V.L. / Chen, Z. / Bountra, C. / von Delft, F. / Gileadi, O. / Brennan, P.E.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA)5U54AG065187-03 United States
CitationJournal: Structure / Year: 2024
Title: The mechanism of allosteric activation of SYK kinase derived from multiple phospho-ITAM-bound structures.
Authors: Bradshaw, W.J. / Harris, G. / Gileadi, O. / Katis, V.L.
History
DepositionNov 4, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 24, 2021Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Derived calculations / Refinement description
Category: atom_type / chem_comp_atom ...atom_type / chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z ..._atom_type.pdbx_N_electrons / _atom_type.pdbx_scat_Z / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.2Oct 30, 2024Group: Database references / Structure summary
Category: citation / citation_author ...citation / citation_author / pdbx_entry_details / pdbx_modification_feature
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year / _pdbx_entry_details.has_protein_modification
Revision 1.3Jan 29, 2025Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
AAA: Tyrosine-protein kinase SYK
BBB: Tyrosine-protein kinase SYK
CCC: Tyrosine-protein kinase SYK
DDD: Tyrosine-protein kinase SYK
EEE: Tyrosine-protein kinase SYK
FFF: Tyrosine-protein kinase SYK
GGG: High affinity immunoglobulin epsilon receptor subunit gamma
HHH: High affinity immunoglobulin epsilon receptor subunit gamma
III: High affinity immunoglobulin epsilon receptor subunit gamma
JJJ: High affinity immunoglobulin epsilon receptor subunit gamma
KKK: High affinity immunoglobulin epsilon receptor subunit gamma
LLL: High affinity immunoglobulin epsilon receptor subunit gamma
hetero molecules


Theoretical massNumber of molelcules
Total (without water)195,54826
Polymers194,29412
Non-polymers1,25314
Water6,017334
1
AAA: Tyrosine-protein kinase SYK
JJJ: High affinity immunoglobulin epsilon receptor subunit gamma
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,6345
Polymers32,3822
Non-polymers2523
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2790 Å2
ΔGint-17 kcal/mol
Surface area14730 Å2
MethodPISA
2
BBB: Tyrosine-protein kinase SYK
KKK: High affinity immunoglobulin epsilon receptor subunit gamma
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,6785
Polymers32,3822
Non-polymers2963
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2940 Å2
ΔGint-12 kcal/mol
Surface area14650 Å2
MethodPISA
3
CCC: Tyrosine-protein kinase SYK
HHH: High affinity immunoglobulin epsilon receptor subunit gamma
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,6966
Polymers32,3822
Non-polymers3144
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2670 Å2
ΔGint-18 kcal/mol
Surface area14790 Å2
MethodPISA
4
DDD: Tyrosine-protein kinase SYK
III: High affinity immunoglobulin epsilon receptor subunit gamma
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,6675
Polymers32,3822
Non-polymers2853
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2910 Å2
ΔGint-23 kcal/mol
Surface area14690 Å2
MethodPISA
5
EEE: Tyrosine-protein kinase SYK
GGG: High affinity immunoglobulin epsilon receptor subunit gamma
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,4893
Polymers32,3822
Non-polymers1061
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2380 Å2
ΔGint-11 kcal/mol
Surface area14460 Å2
MethodPISA
6
FFF: Tyrosine-protein kinase SYK
LLL: High affinity immunoglobulin epsilon receptor subunit gamma


Theoretical massNumber of molelcules
Total (without water)32,3822
Polymers32,3822
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2100 Å2
ΔGint-14 kcal/mol
Surface area14100 Å2
MethodPISA
Unit cell
Length a, b, c (Å)144.136, 88.035, 158.486
Angle α, β, γ (deg.)90.000, 113.575, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11AAA
21BBB
32AAA
42CCC
53AAA
63DDD
74AAA
84EEE
95AAA
105FFF
116BBB
126CCC
137BBB
147DDD
158BBB
168EEE
179BBB
189FFF
1910CCC
2010DDD
2111CCC
2211EEE
2312CCC
2412FFF
2513DDD
2613EEE
2714DDD
2814FFF
2915EEE
3015FFF
3116GGG
3216III
3317GGG
3417LLL
3518HHH
3618JJJ
3719HHH
3819KKK
3920III
4020LLL
4121JJJ
4221KKK

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ASPASPLYSLYSAAAA8 - 2614 - 257
221ASPASPLYSLYSBBBB8 - 2614 - 257
332SERSERLYSLYSAAAA9 - 2615 - 257
442SERSERLYSLYSCCCC9 - 2615 - 257
553ALAALAILEILEAAAA10 - 2626 - 258
663ALAALAILEILEDDDD10 - 2626 - 258
774SERSERLYSLYSAAAA9 - 2615 - 257
884SERSERLYSLYSEEEE9 - 2615 - 257
995SERSERILEILEAAAA9 - 2625 - 258
10105SERSERILEILEFFFF9 - 2625 - 258
11116SERSERGLYGLYBBBB9 - 2635 - 259
12126SERSERGLYGLYCCCC9 - 2635 - 259
13137ALAALAGLYGLYBBBB10 - 2636 - 259
14147ALAALAGLYGLYDDDD10 - 2636 - 259
15158SERSERLYSLYSBBBB9 - 2615 - 257
16168SERSERLYSLYSEEEE9 - 2615 - 257
17179SERSERILEILEBBBB9 - 2625 - 258
18189SERSERILEILEFFFF9 - 2625 - 258
191910ALAALAILEILECCCC10 - 2626 - 258
202010ALAALAILEILEDDDD10 - 2626 - 258
212111SERSERLYSLYSCCCC9 - 2615 - 257
222211SERSERLYSLYSEEEE9 - 2615 - 257
232312SERSERILEILECCCC9 - 2625 - 258
242412SERSERILEILEFFFF9 - 2625 - 258
252513ALAALAILEILEDDDD10 - 2626 - 258
262613ALAALAILEILEEEEE10 - 2626 - 258
272714ALAALAILEILEDDDD10 - 2626 - 258
282814ALAALAILEILEFFFF10 - 2626 - 258
292915SERSERILEILEEEEE9 - 2625 - 258
303015SERSERILEILEFFFF9 - 2625 - 258
313116GLYGLYLEULEUGGGG63 - 792 - 18
323216GLYGLYLEULEUIIII63 - 792 - 18
333317PTRPTRTHRTHRGGGG65 - 784 - 17
343417PTRPTRTHRTHRLLLL65 - 784 - 17
353518VALVALLEULEUHHHH64 - 793 - 18
363618VALVALLEULEUJJJJ64 - 793 - 18
373719GLYGLYLEULEUHHHH63 - 792 - 18
383819GLYGLYLEULEUKKKK63 - 792 - 18
393920PTRPTRTHRTHRIIII65 - 784 - 17
404020PTRPTRTHRTHRLLLL65 - 784 - 17
414121VALVALLEULEUJJJJ64 - 793 - 18
424221VALVALLEULEUKKKK64 - 793 - 18

NCS ensembles :
IDDetails
1Local NCS retraints between domains: 1 2
2Local NCS retraints between domains: 3 4
3Local NCS retraints between domains: 5 6
4Local NCS retraints between domains: 7 8
5Local NCS retraints between domains: 9 10
6Local NCS retraints between domains: 11 12
7Local NCS retraints between domains: 13 14
8Local NCS retraints between domains: 15 16
9Local NCS retraints between domains: 17 18
10Local NCS retraints between domains: 19 20
11Local NCS retraints between domains: 21 22
12Local NCS retraints between domains: 23 24
13Local NCS retraints between domains: 25 26
14Local NCS retraints between domains: 27 28
15Local NCS retraints between domains: 29 30
16Local NCS retraints between domains: 31 32
17Local NCS retraints between domains: 33 34
18Local NCS retraints between domains: 35 36
19Local NCS retraints between domains: 37 38
20Local NCS retraints between domains: 39 40
21Local NCS retraints between domains: 41 42

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Components

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Protein / Protein/peptide , 2 types, 12 molecules AAABBBCCCDDDEEEFFFGGGHHHIIIJJJKKKLLL

#1: Protein
Tyrosine-protein kinase SYK / Spleen tyrosine kinase / p72-Syk


Mass: 29906.971 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SYK / Plasmid: pNIC28-Bsa4 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: P43405, non-specific protein-tyrosine kinase
#2: Protein/peptide
High affinity immunoglobulin epsilon receptor subunit gamma / Fc receptor gamma-chain / FcRgamma / Fc-epsilon RI-gamma / IgE Fc receptor subunit gamma / FceRI gamma


Mass: 2475.431 Da / Num. of mol.: 6 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P30273

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Non-polymers , 4 types, 348 molecules

#3: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: PO4
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 334 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
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: 2.37 Å3/Da / Density % sol: 48.14 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulphate, 100 mM Tris/BICINE, 10% PEG 20,000, 20% PEG 500 MME

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9762 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Jan 20, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
ReflectionResolution: 2.2→73.26 Å / Num. obs: 90843 / % possible obs: 98.3 % / Redundancy: 8.3 % / CC1/2: 0.995 / Rmerge(I) obs: 0.145 / Rpim(I) all: 0.077 / Rrim(I) all: 0.164 / Χ2: 0.93 / Net I/σ(I): 7.5
Reflection shellResolution: 2.2→2.24 Å / Redundancy: 4.9 % / Rmerge(I) obs: 1.672 / Mean I/σ(I) obs: 0.7 / Num. unique obs: 3838 / CC1/2: 0.31 / Rpim(I) all: 1.1 / Rrim(I) all: 2.018 / Χ2: 0.97 / % possible all: 83.8

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Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
DIALSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1A81

1a81


Resolution: 2.2→73.26 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.93 / SU B: 9.783 / SU ML: 0.226 / Cross valid method: FREE R-VALUE / ESU R: 0.288 / ESU R Free: 0.222
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.255 1981 2.183 %
Rwork0.2075 88775 -
all0.209 --
obs-90756 98.264 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 63.047 Å2
Baniso -1Baniso -2Baniso -3
1--1.865 Å20 Å21.846 Å2
2---2.006 Å20 Å2
3---1.636 Å2
Refinement stepCycle: LAST / Resolution: 2.2→73.26 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13083 0 71 334 13488
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01313448
X-RAY DIFFRACTIONr_bond_other_d0.0010.01512654
X-RAY DIFFRACTIONr_angle_refined_deg1.5061.6518152
X-RAY DIFFRACTIONr_angle_other_deg1.2661.58429176
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.16451622
X-RAY DIFFRACTIONr_dihedral_angle_2_deg30.60622.378719
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.039152367
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.9561584
X-RAY DIFFRACTIONr_chiral_restr0.0690.21669
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0215127
X-RAY DIFFRACTIONr_gen_planes_other0.0010.023125
X-RAY DIFFRACTIONr_nbd_refined0.2110.22336
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1840.210817
X-RAY DIFFRACTIONr_nbtor_refined0.1630.26194
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0770.26386
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1590.2364
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_other0.0660.27
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.1790.252
X-RAY DIFFRACTIONr_nbd_other0.2180.2182
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.3340.27
X-RAY DIFFRACTIONr_mcbond_it5.6816.3556512
X-RAY DIFFRACTIONr_mcbond_other5.6816.3546511
X-RAY DIFFRACTIONr_mcangle_it8.3689.5118117
X-RAY DIFFRACTIONr_mcangle_other8.3689.5128118
X-RAY DIFFRACTIONr_scbond_it6.1956.9426936
X-RAY DIFFRACTIONr_scbond_other6.1946.9426937
X-RAY DIFFRACTIONr_scangle_it9.32810.15210032
X-RAY DIFFRACTIONr_scangle_other9.32810.15210033
X-RAY DIFFRACTIONr_lrange_it12.52272.04514151
X-RAY DIFFRACTIONr_lrange_other12.52972.05614125
X-RAY DIFFRACTIONr_ncsr_local_group_10.1110.057753
X-RAY DIFFRACTIONr_ncsr_local_group_20.1060.057746
X-RAY DIFFRACTIONr_ncsr_local_group_30.1220.057464
X-RAY DIFFRACTIONr_ncsr_local_group_40.1230.057529
X-RAY DIFFRACTIONr_ncsr_local_group_50.1240.057331
X-RAY DIFFRACTIONr_ncsr_local_group_60.10.057859
X-RAY DIFFRACTIONr_ncsr_local_group_70.120.057511
X-RAY DIFFRACTIONr_ncsr_local_group_80.1190.057593
X-RAY DIFFRACTIONr_ncsr_local_group_90.110.057416
X-RAY DIFFRACTIONr_ncsr_local_group_100.1190.057524
X-RAY DIFFRACTIONr_ncsr_local_group_110.1220.057563
X-RAY DIFFRACTIONr_ncsr_local_group_120.1180.057380
X-RAY DIFFRACTIONr_ncsr_local_group_130.1250.057381
X-RAY DIFFRACTIONr_ncsr_local_group_140.1060.057309
X-RAY DIFFRACTIONr_ncsr_local_group_150.1110.057339
X-RAY DIFFRACTIONr_ncsr_local_group_160.2060.05335
X-RAY DIFFRACTIONr_ncsr_local_group_170.2360.05262
X-RAY DIFFRACTIONr_ncsr_local_group_180.1970.05331
X-RAY DIFFRACTIONr_ncsr_local_group_190.2250.05329
X-RAY DIFFRACTIONr_ncsr_local_group_200.2050.05272
X-RAY DIFFRACTIONr_ncsr_local_group_210.1970.05319
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)Weight position
11AAAX-RAY DIFFRACTIONLocal ncs0.111350.05008
12BBBX-RAY DIFFRACTIONLocal ncs0.111350.05008
23AAAX-RAY DIFFRACTIONLocal ncs0.106090.05008
24CCCX-RAY DIFFRACTIONLocal ncs0.106090.05008
35AAAX-RAY DIFFRACTIONLocal ncs0.122060.05008
36DDDX-RAY DIFFRACTIONLocal ncs0.122060.05008
47AAAX-RAY DIFFRACTIONLocal ncs0.123180.05007
48EEEX-RAY DIFFRACTIONLocal ncs0.123180.05007
59AAAX-RAY DIFFRACTIONLocal ncs0.124190.05008
510FFFX-RAY DIFFRACTIONLocal ncs0.124190.05008
611BBBX-RAY DIFFRACTIONLocal ncs0.100040.05008
612CCCX-RAY DIFFRACTIONLocal ncs0.100040.05008
713BBBX-RAY DIFFRACTIONLocal ncs0.119590.05008
714DDDX-RAY DIFFRACTIONLocal ncs0.119590.05008
815BBBX-RAY DIFFRACTIONLocal ncs0.119430.05008
816EEEX-RAY DIFFRACTIONLocal ncs0.119430.05008
917BBBX-RAY DIFFRACTIONLocal ncs0.110160.05008
918FFFX-RAY DIFFRACTIONLocal ncs0.110160.05008
1019CCCX-RAY DIFFRACTIONLocal ncs0.119190.05008
1020DDDX-RAY DIFFRACTIONLocal ncs0.119190.05008
1121CCCX-RAY DIFFRACTIONLocal ncs0.12180.05008
1122EEEX-RAY DIFFRACTIONLocal ncs0.12180.05008
1223CCCX-RAY DIFFRACTIONLocal ncs0.117740.05008
1224FFFX-RAY DIFFRACTIONLocal ncs0.117740.05008
1325DDDX-RAY DIFFRACTIONLocal ncs0.125010.05008
1326EEEX-RAY DIFFRACTIONLocal ncs0.125010.05008
1427DDDX-RAY DIFFRACTIONLocal ncs0.105960.05008
1428FFFX-RAY DIFFRACTIONLocal ncs0.105960.05008
1529EEEX-RAY DIFFRACTIONLocal ncs0.111390.05008
1530FFFX-RAY DIFFRACTIONLocal ncs0.111390.05008
1631GGGX-RAY DIFFRACTIONLocal ncs0.205560.05005
1632IIIX-RAY DIFFRACTIONLocal ncs0.205560.05005
1733GGGX-RAY DIFFRACTIONLocal ncs0.236370.05003
1734LLLX-RAY DIFFRACTIONLocal ncs0.236370.05003
1835HHHX-RAY DIFFRACTIONLocal ncs0.196810.05009
1836JJJX-RAY DIFFRACTIONLocal ncs0.196810.05009
1937HHHX-RAY DIFFRACTIONLocal ncs0.224810.05007
1938KKKX-RAY DIFFRACTIONLocal ncs0.224810.05007
2039IIIX-RAY DIFFRACTIONLocal ncs0.204950.05003
2040LLLX-RAY DIFFRACTIONLocal ncs0.204950.05003
2141JJJX-RAY DIFFRACTIONLocal ncs0.196730.05006
2142KKKX-RAY DIFFRACTIONLocal ncs0.196730.05006
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2-2.2570.3391190.3585684X-RAY DIFFRACTION85.1629
2.257-2.3190.3241350.3375997X-RAY DIFFRACTION92.6004
2.319-2.3860.3141330.3116212X-RAY DIFFRACTION98.7088
2.386-2.460.341320.2896111X-RAY DIFFRACTION99.984
2.46-2.540.3261050.2635982X-RAY DIFFRACTION99.9672
2.54-2.6290.2651500.2395741X-RAY DIFFRACTION99.9491
2.629-2.7290.3081360.2295529X-RAY DIFFRACTION99.9118
2.729-2.840.2721310.235320X-RAY DIFFRACTION99.9817
2.84-2.9660.3131260.2315079X-RAY DIFFRACTION99.9616
2.966-3.1110.29880.2264932X-RAY DIFFRACTION99.9801
3.111-3.2790.27980.2174679X-RAY DIFFRACTION100
3.279-3.4780.2621070.2124396X-RAY DIFFRACTION100
3.478-3.7180.2721070.2044143X-RAY DIFFRACTION100
3.718-4.0160.24680.1833927X-RAY DIFFRACTION100
4.016-4.3990.199820.1663541X-RAY DIFFRACTION100
4.399-4.9170.199760.1443232X-RAY DIFFRACTION100
4.917-5.6770.185670.1622866X-RAY DIFFRACTION100
5.677-6.950.267480.192439X-RAY DIFFRACTION100
6.95-9.8170.242520.1591885X-RAY DIFFRACTION100
9.817-73.260.214210.1941082X-RAY DIFFRACTION99.7288

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