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- PDB-4gko: Crystal structure of the calcium2+-bound human IgE-Fc(epsilon)3-4... -

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Basic information

Entry
Database: PDB / ID: 4gko
TitleCrystal structure of the calcium2+-bound human IgE-Fc(epsilon)3-4 bound to its B cell receptor derCD23
Components
  • Ig epsilon chain C region
  • Low affinity immunoglobulin epsilon Fc receptor
KeywordsIMMUNE SYSTEM / IMMUNOGLOBULIN FOLD LECTIN / ANTIBODY RECEPTOR
Function / homology
Function and homology information


low-affinity IgE receptor activity / adaptive immune memory response / primary adaptive immune response / IgE B cell receptor complex / type I hypersensitivity / B cell antigen processing and presentation / Fc receptor-mediated immune complex endocytosis / positive regulation of humoral immune response mediated by circulating immunoglobulin / NOTCH2 intracellular domain regulates transcription / eosinophil degranulation ...low-affinity IgE receptor activity / adaptive immune memory response / primary adaptive immune response / IgE B cell receptor complex / type I hypersensitivity / B cell antigen processing and presentation / Fc receptor-mediated immune complex endocytosis / positive regulation of humoral immune response mediated by circulating immunoglobulin / NOTCH2 intracellular domain regulates transcription / eosinophil degranulation / IgE immunoglobulin complex / macrophage activation / IgE binding / positive regulation of killing of cells of another organism / type 2 immune response / Fc epsilon receptor (FCERI) signaling / antibody-dependent cellular cytotoxicity / mast cell degranulation / B cell proliferation / positive regulation of nitric-oxide synthase biosynthetic process / Interleukin-10 signaling / macrophage differentiation / Role of LAT2/NTAL/LAB on calcium mobilization / immunoglobulin complex, circulating / immunoglobulin receptor binding / FCERI mediated Ca+2 mobilization / complement activation, classical pathway / positive regulation of nitric-oxide synthase activity / antigen binding / FCERI mediated MAPK activation / B cell receptor signaling pathway / FCERI mediated NF-kB activation / integrin binding / antibacterial humoral response / carbohydrate binding / protease binding / Interleukin-4 and Interleukin-13 signaling / adaptive immune response / inflammatory response / immune response / external side of plasma membrane / extracellular space / extracellular exosome / extracellular region / metal ion binding / plasma membrane
Similarity search - Function
CD209-like, C-type lectin-like domain / : / C-type lectin, conserved site / C-type lectin domain signature. / Mannose-Binding Protein A; Chain A / Mannose-Binding Protein A, subunit A / Lectin C-type domain / C-type lectin domain profile. / C-type lectin-like / C-type lectin (CTL) or carbohydrate-recognition domain (CRD) ...CD209-like, C-type lectin-like domain / : / C-type lectin, conserved site / C-type lectin domain signature. / Mannose-Binding Protein A; Chain A / Mannose-Binding Protein A, subunit A / Lectin C-type domain / C-type lectin domain profile. / C-type lectin-like / C-type lectin (CTL) or carbohydrate-recognition domain (CRD) / C-type lectin-like/link domain superfamily / C-type lectin fold / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Roll / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
alpha-D-mannopyranose / Immunoglobulin heavy constant epsilon / Low affinity immunoglobulin epsilon Fc receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å
AuthorsYuan, D. / Sutton, B.J. / Dhaliwal, B.
CitationJournal: J.Biol.Chem. / Year: 2013
Title: Ca2+-dependent Structural Changes in the B-cell Receptor CD23 Increase Its Affinity for Human Immunoglobulin E.
Authors: Yuan, D. / Keeble, A.H. / Hibbert, R.G. / Fabiane, S. / Gould, H.J. / McDonnell, J.M. / Beavil, A.J. / Sutton, B.J. / Dhaliwal, B.
History
DepositionAug 13, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 26, 2013Provider: repository / Type: Initial release
Revision 1.1Aug 14, 2013Group: Database references
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_struct_conn_angle / 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.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _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_comp_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_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.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_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ig epsilon chain C region
B: Ig epsilon chain C region
C: Ig epsilon chain C region
D: Ig epsilon chain C region
E: Ig epsilon chain C region
F: Ig epsilon chain C region
G: Low affinity immunoglobulin epsilon Fc receptor
H: Low affinity immunoglobulin epsilon Fc receptor
I: Low affinity immunoglobulin epsilon Fc receptor
J: Low affinity immunoglobulin epsilon Fc receptor
K: Low affinity immunoglobulin epsilon Fc receptor
L: Low affinity immunoglobulin epsilon Fc receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)252,57726
Polymers246,51112
Non-polymers6,06614
Water00
1
A: Ig epsilon chain C region
B: Ig epsilon chain C region
G: Low affinity immunoglobulin epsilon Fc receptor
H: Low affinity immunoglobulin epsilon Fc receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,0728
Polymers82,1704
Non-polymers1,9024
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Ig epsilon chain C region
D: Ig epsilon chain C region
I: Low affinity immunoglobulin epsilon Fc receptor
J: Low affinity immunoglobulin epsilon Fc receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,43210
Polymers82,1704
Non-polymers2,2626
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Ig epsilon chain C region
F: Ig epsilon chain C region
K: Low affinity immunoglobulin epsilon Fc receptor
L: Low affinity immunoglobulin epsilon Fc receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,0728
Polymers82,1704
Non-polymers1,9024
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)62.830, 110.130, 367.410
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14A
24E
15A
25F
16B
26C
17B
27D
18B
28E
19B
29F
110C
210D
111C
211E
112C
212F
113D
213E
114D
214F
115E
215F
116G
216H
117G
217I
118G
218J
119G
219K
120G
220L
121H
221I
122H
222J
123H
223K
124H
224L
125I
225J
126I
226K
127I
227L
128J
228K
129J
229L
130K
230L

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11VALVALPROPROAA336 - 54512 - 221
21VALVALPROPROBB336 - 54512 - 221
12VALVALPROPROAA336 - 54512 - 221
22VALVALPROPROCC336 - 54512 - 221
13GLYGLYVALVALAA335 - 54111 - 217
23GLYGLYVALVALDD335 - 54111 - 217
14GLYGLYALAALAAA335 - 54011 - 216
24GLYGLYALAALAEE335 - 54011 - 216
15VALVALARGARGAA336 - 53912 - 215
25VALVALARGARGFF336 - 53912 - 215
16VALVALPROPROBB336 - 54512 - 221
26VALVALPROPROCC336 - 54512 - 221
17VALVALVALVALBB336 - 54112 - 217
27VALVALVALVALDD336 - 54112 - 217
18VALVALALAALABB336 - 54012 - 216
28VALVALALAALAEE336 - 54012 - 216
19VALVALARGARGBB336 - 53912 - 215
29VALVALARGARGFF336 - 53912 - 215
110VALVALVALVALCC336 - 54112 - 217
210VALVALVALVALDD336 - 54112 - 217
111VALVALALAALACC336 - 54012 - 216
211VALVALALAALAEE336 - 54012 - 216
112VALVALARGARGCC336 - 53912 - 215
212VALVALARGARGFF336 - 53912 - 215
113GLYGLYALAALADD335 - 54011 - 216
213GLYGLYALAALAEE335 - 54011 - 216
114VALVALARGARGDD336 - 53912 - 215
214VALVALARGARGFF336 - 53912 - 215
115VALVALARGARGEE336 - 53912 - 215
215VALVALARGARGFF336 - 53912 - 215
116PHEPHETHRTHRGG158 - 2893 - 134
216PHEPHETHRTHRHH158 - 2893 - 134
117PHEPHEPROPROGG158 - 2903 - 135
217PHEPHEPROPROII158 - 2903 - 135
118PHEPHEALAALAGG158 - 2923 - 137
218PHEPHEALAALAJJ158 - 2923 - 137
119PHEPHEPROPROGG158 - 2903 - 135
219PHEPHEPROPROKK158 - 2903 - 135
120PHEPHEPROPROGG158 - 2913 - 136
220PHEPHEPROPROLL158 - 2913 - 136
121PHEPHETHRTHRHH158 - 2893 - 134
221PHEPHETHRTHRII158 - 2893 - 134
122PHEPHETHRTHRHH158 - 2893 - 134
222PHEPHETHRTHRJJ158 - 2893 - 134
123PHEPHETHRTHRHH158 - 2893 - 134
223PHEPHETHRTHRKK158 - 2893 - 134
124PHEPHETHRTHRHH158 - 2893 - 134
224PHEPHETHRTHRLL158 - 2893 - 134
125PHEPHEPROPROII158 - 2903 - 135
225PHEPHEPROPROJJ158 - 2903 - 135
126PHEPHEPROPROII158 - 2903 - 135
226PHEPHEPROPROKK158 - 2903 - 135
127PHEPHEPROPROII158 - 2903 - 135
227PHEPHEPROPROLL158 - 2903 - 135
128PHEPHEPROPROJJ158 - 2903 - 135
228PHEPHEPROPROKK158 - 2903 - 135
129PHEPHEPROPROJJ158 - 2913 - 136
229PHEPHEPROPROLL158 - 2913 - 136
130PHEPHEPROPROKK158 - 2903 - 135
230PHEPHEPROPROLL158 - 2903 - 135

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23
24
25
26
27
28
29
30

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Components

#1: Protein
Ig epsilon chain C region


Mass: 24920.146 Da / Num. of mol.: 6 / Fragment: UNP residues 209-428
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGHE / Cell line (production host): HEK293 / Production host: Homo Sapiens (human) / References: UniProt: P01854
#2: Protein
Low affinity immunoglobulin epsilon Fc receptor / BLAST-2 / C-type lectin domain family 4 member J / Fc-epsilon-RII / Immunoglobulin E-binding factor ...BLAST-2 / C-type lectin domain family 4 member J / Fc-epsilon-RII / Immunoglobulin E-binding factor / Lymphocyte IgE receptor / Low affinity immunoglobulin epsilon Fc receptor membrane-bound form / Low affinity immunoglobulin epsilon Fc receptor soluble form


Mass: 16164.986 Da / Num. of mol.: 6 / Fragment: UNP residues 156-298
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FCER2, CD23A, CLEC4J, FCE2, IGEBF / Production host: Escherichia coli (E. coli) / References: UniProt: P06734
#3: Polysaccharide
alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#4: Sugar ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 2
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
#5: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / 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: 1

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Sample preparation

CrystalDensity Matthews: 2.58 Å3/Da / Density % sol: 52.29 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 0.2 M sodium acetate trihydrate, 0.1 M Tris pH 8.5, 16% PEG 4000, 10 mM CaCl2, VAPOR DIFFUSION, SITTING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.9173 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Sep 24, 2011
RadiationMonochromator: Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9173 Å / Relative weight: 1
ReflectionResolution: 3.3→73.5 Å / Num. all: 39116 / Num. obs: 33757 / % possible obs: 86.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0
Reflection shellResolution: 3.3→3.48 Å / % possible all: 86.3

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Processing

Software
NameVersionClassificationNB
REFMAC5.6.0117refinement
PDB_EXTRACT3.11data extraction
HKL-2000data collection
MOSFLMdata reduction
SCALAdata scaling
PHASESphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4EZM

4ezm


Resolution: 3.3→73.5 Å / Cor.coef. Fo:Fc: 0.897 / Cor.coef. Fo:Fc free: 0.891 / Occupancy max: 1 / Occupancy min: 0.5 / SU B: 135.444 / SU ML: 0.9 / σ(F): 0 / ESU R Free: 0.787 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.3118 1684 5 %RANDOM THROUGHOUT
Rwork0.2725 ---
all0.2745 39116 --
obs0.2745 33653 85.13 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 503.43 Å2 / Biso mean: 150.7958 Å2 / Biso min: 88.75 Å2
Baniso -1Baniso -2Baniso -3
1-1.62 Å20 Å20 Å2
2---2.03 Å20 Å2
3---0.41 Å2
Refinement stepCycle: LAST / Resolution: 3.3→73.5 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15820 0 394 0 16214
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.0216706
X-RAY DIFFRACTIONr_angle_refined_deg1.9631.95222649
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.85951959
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.72922.752763
X-RAY DIFFRACTIONr_dihedral_angle_3_deg19.331152640
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.66815149
X-RAY DIFFRACTIONr_chiral_restr0.1150.22471
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.02112553
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: LOCAL / Weight: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms
11A2410.11
12B2410.11
21A2330.06
22C2330.06
31A2210.11
32D2210.11
41A2050.05
42E2050.05
51A2340.12
52F2340.12
61B2340.06
62C2340.06
71B2160.12
72D2160.12
81B2070.09
82E2070.09
91B2380.08
92F2380.08
101C2020.06
102D2020.06
111C2020.06
112E2020.06
121C2250.08
122F2250.08
131D1920.16
132E1920.16
141D2140.15
142F2140.15
151E2050.09
152F2050.09
161G1850.06
162H1850.06
171G1870.09
172I1870.09
181G1900.07
182J1900.07
191G1890.05
192K1890.05
201G1910.07
202L1910.07
211H1860.08
212I1860.08
221H1890.08
222J1890.08
231H1860.03
232K1860.03
241H1870.04
242L1870.04
251I1910.06
252J1910.06
261I1880.07
262K1880.07
271I1900.07
272L1900.07
281J1900.07
282K1900.07
291J1930.07
292L1930.07
301K1890.03
302L1890.03
LS refinement shellResolution: 3.3→3.386 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.444 103 -
Rwork0.357 2077 -
all-2180 -
obs--82.58 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
11.524-0.4201-0.70251.82450.12321.0848-0.0849-0.1349-0.1059-0.23140.0599-0.13840.0075-0.07640.0251.17010.02630.65891.10440.0141.1751-3.343-5.802388.4552
21.61761.3372-0.96221.4101-0.56590.8918-0.27120.05880.1488-0.44730.21540.16030.3659-0.08960.05581.4056-0.09150.47131.23650.10921.1386-29.1562-3.45290.1647
30.52471.0577-0.05664.58080.99631.7649-0.04350.20390.22170.41750.06580.02420.42420.1287-0.02230.85390.09990.43431.2539-0.52771.2572-17.8507-10.727227.6166
41.9069-2.2455-1.92474.03173.12.45250.51740.2252-0.5808-0.499-0.81850.2171-0.5184-0.6370.30110.74970.24720.31371.4632-0.63761.5453-32.275410.363631.7088
54.03820.18490.63423.04291.45890.79280.05740.39970.06020.70280.235-0.59280.16910.1161-0.29242.3475-0.03530.55040.9139-0.8090.97032.364462.346430.0938
61.89450.50560.56521.06540.31980.8194-0.4276-0.2160.11790.35460.51110.4849-0.280.2611-0.08351.67470.25470.08151.0297-0.62331.411912.829437.876428.7197
74.381-0.8669-0.12990.27110.20973.6555-0.53070.0764-0.2252-0.18010.219-0.1531-0.0085-0.21150.31171.7266-0.18981.1171.0714-0.31570.838115.214-9.06658.2976
82.2140.1317-2.03432.947-0.73493.0969-0.1039-0.3573-0.05880.11890.2157-0.170.23080.3945-0.11181.102-0.12140.52451.26250.29181.1758-47.0491-8.9433120.2228
91.4029-2.9848-3.21887.83085.89118.58780.37810.7073-0.1594-0.4428-1.2111-0.3737-0.3728-1.54980.8331.09380.13580.1171.3931-0.84721.0002-17.4795-30.6915-2.1867
104.1298-2.2225-0.12682.4782-0.02552.8197-0.20770.2322-0.34541.0227-0.0880.11670.1274-0.07410.29570.9810.05750.53511.3203-0.38471.176-40.338126.344461.481
111.5684-0.4906-2.348825.95-8.45716.98911.3752-0.6724-0.41212.8797-2.4893-1.1599-2.58222.24241.11413.8192-1.00770.12361.8505-0.52510.8724-11.064976.952558.7266
121.1391-1.257-1.13175.87210.09781.55550.12120.0338-0.0813-0.5645-0.08990.0671-0.1954-0.1208-0.03131.55730.0091-0.36830.868-0.64881.098120.829718.70860.1171
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A335 - 545
2X-RAY DIFFRACTION1A601 - 605
3X-RAY DIFFRACTION2B336 - 545
4X-RAY DIFFRACTION2B601 - 605
5X-RAY DIFFRACTION3C336 - 545
6X-RAY DIFFRACTION3C601 - 607
7X-RAY DIFFRACTION4D335 - 541
8X-RAY DIFFRACTION4D601 - 605
9X-RAY DIFFRACTION5E335 - 540
10X-RAY DIFFRACTION5E601 - 605
11X-RAY DIFFRACTION6F336 - 539
12X-RAY DIFFRACTION6F601 - 605
13X-RAY DIFFRACTION7G158 - 292
14X-RAY DIFFRACTION7G301
15X-RAY DIFFRACTION8H158 - 290
16X-RAY DIFFRACTION8H301
17X-RAY DIFFRACTION9I158 - 291
18X-RAY DIFFRACTION9I301
19X-RAY DIFFRACTION10J158 - 292
20X-RAY DIFFRACTION10J301
21X-RAY DIFFRACTION11K157 - 291
22X-RAY DIFFRACTION11K301
23X-RAY DIFFRACTION12L158 - 293
24X-RAY DIFFRACTION12L301

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