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- PDB-5moi: Crystal structure of human IgE-Fc epsilon 3-4 -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 5moi
TitleCrystal structure of human IgE-Fc epsilon 3-4
ComponentsIg epsilon chain C region
KeywordsIMMUNE SYSTEM / immunoglobulin E / IgE / antibody
Function / homology
Function and homology information


IgE B cell receptor complex / adaptive immune memory response / primary adaptive immune response / type I hypersensitivity / B cell antigen processing and presentation / Fc receptor-mediated immune complex endocytosis / eosinophil degranulation / IgE immunoglobulin complex / macrophage activation / type 2 immune response ...IgE B cell receptor complex / adaptive immune memory response / primary adaptive immune response / type I hypersensitivity / B cell antigen processing and presentation / Fc receptor-mediated immune complex endocytosis / eosinophil degranulation / IgE immunoglobulin complex / macrophage activation / type 2 immune response / Fc epsilon receptor (FCERI) signaling / antibody-dependent cellular cytotoxicity / mast cell degranulation / B cell proliferation / macrophage differentiation / immunoglobulin complex, circulating / Role of LAT2/NTAL/LAB on calcium mobilization / immunoglobulin receptor binding / FCERI mediated Ca+2 mobilization / complement activation, classical pathway / antigen binding / FCERI mediated MAPK activation / B cell receptor signaling pathway / FCERI mediated NF-kB activation / antibacterial humoral response / Interleukin-4 and Interleukin-13 signaling / adaptive immune response / inflammatory response / immune response / extracellular space / extracellular region / plasma membrane
Similarity search - Function
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 / Immunoglobulin-like 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 / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / PHOSPHATE ION / Immunoglobulin heavy constant epsilon
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsDore, K.A. / Davies, A.M. / Drinkwater, N. / Beavil, A.J. / McDonnell, J.M. / Sutton, B.J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Medical Research Council (United Kingdom)G1100090 United Kingdom
CitationJournal: Biochim. Biophys. Acta / Year: 2017
Title: Thermal sensitivity and flexibility of the C epsilon 3 domains in immunoglobulin E.
Authors: Dore, K.A. / Davies, A.M. / Drinkwater, N. / Beavil, A.J. / McDonnell, J.M. / Sutton, B.J.
History
DepositionDec 14, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 10, 2018Provider: repository / Type: Initial release
Revision 1.1Apr 3, 2019Group: Data collection / Source and taxonomy / Category: entity_src_gen / Item: _entity_src_gen.pdbx_host_org_cell_line
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / 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 / struct_asym / struct_conn / 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 / _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_atom_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_atom_id / _pdbx_unobs_or_zero_occ_atoms.label_comp_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 17, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / 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_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)155,96925
Polymers149,5216
Non-polymers6,44819
Water3,837213
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)47.673, 90.296, 92.908
Angle α, β, γ (deg.)114.41, 90.63, 96.10
Int Tables number1
Space group name H-MP1

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Components

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Protein , 1 types, 6 molecules ABCDEF

#1: Protein
Ig epsilon chain C region


Mass: 24920.146 Da / Num. of mol.: 6
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

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Sugars , 4 types, 6 molecules

#2: 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


Type: oligosaccharide / Mass: 707.630 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-2-3-3/a4-b1_b3-c1_b6-d1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}LINUCSPDB-CARE
#3: 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)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-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_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]{}}}}}LINUCSPDB-CARE
#4: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_e6-g1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose


Type: oligosaccharide / Mass: 504.438 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a1122h-1b_1-5][a1122h-1a_1-5]/1-2-2/a3-b1_a6-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}LINUCSPDB-CARE

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Non-polymers , 4 types, 226 molecules

#6: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C4H10O3
#7: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: PO4
#8: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 213 / Source method: isolated from a natural source / Formula: H2O

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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: 2.42 Å3/Da / Density % sol: 49.12 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop
Details: 25% (v/v) PEG1500, 0.1M SPG (succinic acid, sodium dihydrogen phosphate and glycine in the ratio 2:7:7)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 2, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.2→81.61 Å / Num. obs: 70275 / % possible obs: 98.9 % / Redundancy: 5.7 % / CC1/2: 0.997 / Rmerge(I) obs: 0.13 / Net I/σ(I): 7.5
Reflection shellResolution: 2.2→2.25 Å / Redundancy: 3.8 % / Rmerge(I) obs: 1.103 / Mean I/σ(I) obs: 2 / CC1/2: 0.656 / % possible all: 97

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Processing

Software
NameVersionClassification
PHENIX(1.10_2155: ???)refinement
DIALSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3HA0

3ha0


Resolution: 2.2→42.223 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.02 / Phase error: 31.36
RfactorNum. reflection% reflection
Rfree0.2336 2992 4.98 %
Rwork0.2134 --
obs0.2144 60090 84.54 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.2→42.223 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8713 0 419 213 9345
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0039374
X-RAY DIFFRACTIONf_angle_d0.59112824
X-RAY DIFFRACTIONf_dihedral_angle_d13.9175676
X-RAY DIFFRACTIONf_chiral_restr0.041552
X-RAY DIFFRACTIONf_plane_restr0.0051586
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2-2.23610.2622670.2521430X-RAY DIFFRACTION44
2.2361-2.27460.2859800.26111612X-RAY DIFFRACTION50
2.2746-2.3160.3402800.28911727X-RAY DIFFRACTION54
2.316-2.36050.3043890.27541959X-RAY DIFFRACTION60
2.3605-2.40870.26831100.26062031X-RAY DIFFRACTION64
2.4087-2.46110.31141310.26772245X-RAY DIFFRACTION70
2.4611-2.51830.37841120.27172449X-RAY DIFFRACTION75
2.5183-2.58130.28851380.26982581X-RAY DIFFRACTION81
2.5813-2.65110.31071580.25912890X-RAY DIFFRACTION88
2.6511-2.72910.28521510.25452954X-RAY DIFFRACTION94
2.7291-2.81710.30541470.25663238X-RAY DIFFRACTION99
2.8171-2.91780.28061600.25583156X-RAY DIFFRACTION100
2.9178-3.03460.23981720.2573214X-RAY DIFFRACTION100
3.0346-3.17270.28441530.2473257X-RAY DIFFRACTION100
3.1727-3.33990.28121830.23113177X-RAY DIFFRACTION100
3.3399-3.5490.25751590.22363214X-RAY DIFFRACTION100
3.549-3.82290.22211810.20593203X-RAY DIFFRACTION100
3.8229-4.20730.23291620.18263213X-RAY DIFFRACTION100
4.2073-4.81530.17691830.15783220X-RAY DIFFRACTION100
4.8153-6.06390.19142070.18043176X-RAY DIFFRACTION100
6.0639-42.23070.19771690.20173152X-RAY DIFFRACTION98
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)
16.76582.6838-0.33137.6001-0.53266.97270.20110.0946-0.00030.88190.0652-0.1923-0.24611.4603-0.28760.35320.0006-0.12330.34650.05670.521310.7222-41.489823.5882
25.25992.430.54595.8496-1.65310.82271.0948-1.7014-0.89652.236-0.4017-1.52020.56940.0801-0.19991.222-0.2059-0.29110.72630.1930.800312.192-45.951536.5368
34.47153.44092.55926.4643-0.18483.69950.9673-0.1284-1.08620.6185-0.2377-1.17070.16030.2587-0.16050.8486-0.0116-0.21170.07970.06720.666412.9519-46.825228.5486
44.10570.6882.62653.2227-1.38984.33850.6146-0.8563-1.13040.8883-0.38-0.29860.7852-0.3587-0.72830.7326-0.1074-0.10740.40750.12240.77694.379-50.561625.6506
54.6253-0.15130.38873.9778-0.84774.5887-0.05190.43120.6714-0.22620.2870.3268-0.1182-0.1466-0.14390.16030.03620.01360.1931-0.01950.33751.1503-27.26029.3659
65.46962.8619-2.08594.8257-2.13434.123-0.0391-0.2538-0.9830.1041-0.1058-0.09830.31510.4765-0.01820.26630.016-0.00260.2033-0.05730.42673.6352-31.101715.6154
74.87491.00120.01466.0274-1.82493.3343-0.0540.51261.1295-0.21590.0481-0.3617-0.23630.1771-0.00740.2006-0.00710.01370.25240.00490.42696.5633-24.66138.9133
87.0051.9209-1.06872.9293-4.69488.22240.11980.7144-0.4307-0.8633-0.0607-0.07510.62440.3782-0.05370.27230.00060.0140.3561-0.1560.26527.6827-36.77326.804
96.8671-0.045-0.53673.8907-1.93075.00610.3155-0.7129-0.77420.4962-0.057-0.0691-0.0197-0.4964-0.05130.3309-0.0769-0.04520.4879-0.16950.443-24.1931-23.901629.9691
106.19190.42440.83635.8749-2.13465.74950.4254-1.34-0.94740.4782-0.1770.06090.5309-0.37340.28580.4195-0.0854-0.0450.8949-0.04890.5237-28.5565-28.210335.7849
116.13450.2903-1.85362.4092-1.54384.16760.1801-0.98010.31010.769-0.3484-0.4368-0.7237-0.0206-0.07250.534-0.1223-0.06180.5641-0.23810.5267-22.2731-17.742532.2271
126.0187-1.19550.37026.91581.8955.97290.30930.48680.1006-0.6656-0.2624-0.0032-0.17690.07110.01730.21810.0319-0.00360.2204-0.01320.2364-13.4895-26.27717.6172
135.4383-0.1861-0.50276.66570.22333.80640.31850.29870.3093-0.4843-0.2013-0.16280.2087-0.8739-0.06530.5278-0.01520.00680.4819-0.06870.23826.2924-40.6276-17.1819
145.81911.736-0.2957.8083-0.63085.01190.2550.84131.0074-1.072-0.1836-0.3219-0.3795-0.2037-0.0460.50880.13440.10620.49930.02490.233210.4012-32.3966-20.3282
154.1003-0.7395-0.52633.3611-1.49075.43440.60840.70210.6104-0.4535-0.46040.0606-0.37640.6025-0.03590.58820.14290.09760.54180.03650.40513.0387-29.8087-16.8789
165.3121-0.7773-1.18593.6991-0.60186.37270.340.05140.85270.1582-0.18160.137-0.5825-0.3348-0.06330.4610.06630.1270.3723-0.01220.35778.2775-32.4774-11.5441
174.06131.43271.06754.78850.29620.28480.40420.8911-0.67970.2102-0.63630.53890.6725-0.33310.09560.38110.0561-0.10410.7433-0.18290.6093-2.411-56.6166-26.9156
182.39711.10660.80833.4541.58563.96620.28630.7842-0.6995-0.0835-0.149-0.2036-0.01380.1147-0.12870.4705-0.0071-0.09620.5847-0.21050.45233.6478-54.7424-27.5207
199.415-3.1806-1.80594.34974.03273.95361.0382-0.1909-0.1196-0.0113-0.5430.5355-0.4559-1.0499-0.32160.612-0.17930.04350.7631-0.18660.5951-9.5215-48.5673-20.6392
202.75330.55550.30342.32481.53535.18890.35960.84-1.52070.0283-0.1001-0.32570.39270.3491-0.17860.5369-0.0181-0.04880.706-0.35130.72354.4142-59.9513-28.6202
213.7895-1.3584-0.69193.3929-1.9674.95050.48022.10190.6337-0.5676-0.4206-0.0339-0.14490.3932-0.27790.5250.17070.03831.13430.24550.522-20.2101-35.1723-36.3554
222.3563-0.81190.9791.2435-0.70473.35130.7041.22250.8266-0.3716-0.34190.0196-0.8941-0.36510.77520.97950.35450.36831.27190.81590.8612-25.3462-22.7633-36.5513
232.3205-0.1034-1.10240.0275-0.1727.05080.92350.88951.4313-0.5275-0.4914-0.5243-0.31620.4578-0.00710.8650.31070.21931.24970.48440.5575-21.2943-28.6927-32.8702
243.6359-1.1659-0.51853.2753-0.02041.83890.23871.07-0.2452-0.9437-0.2722-0.62470.20830.1416-0.05240.48830.10920.04891.0109-0.22910.4253-10.5677-55.0579-35.5579
254.7408-1.2837-0.40293.4633-1.59153.9140.43511.4417-0.6109-0.5057-0.29920.416-0.157-0.369-0.09320.51940.1429-0.05520.9372-0.32580.435-16.4234-54.8587-35.2823
266.0654-2.3862-0.89035.3561.33938.8288-0.34-0.2436-0.5312-0.11020.4731-0.1240.15251.4993-0.19530.3623-0.03030.05450.42610.04480.454916.2868-67.3199-1.2531
277.5748-0.42330.10415.6974-0.70666.83880.49270.95240.1354-0.4871-0.211-1.4097-0.25251.3423-0.19580.5914-0.07340.14411.0446-0.08510.535323.5886-66.0675-12.5835
281.1899-1.68690.28692.4310.04364.98350.07420.6853-1.30110.01260.3720.49892.27290.8636-0.46411.41550.5108-0.2080.9091-0.14581.451120.9945-82.6147-6.0293
297.0612-1.21710.56278.65372.56498.2305-0.05940.2965-0.0342-1.27970.5837-0.4955-1.40331.6815-0.35740.6513-0.19010.04610.5898-0.05090.35319.4478-63.6545-7.6401
303.59430.1685-1.08041.3478-0.85977.44590.02810.47050.4178-0.9940.04070.0309-1.09940.5581-0.09810.58410.0116-0.02720.45170.11060.423610.3281-63.9886-8.9451
315.863.7404-3.15224.8518-5.94498.64180.1918-1.0051-0.50070.61260.64651.9673-0.177-1.0537-0.84020.3661-0.0130.00330.99840.17880.6297-1.4514-74.268423.0867
323.87072.1274-1.91482.30361.10355.05990.139-0.6216-0.68290.40620.1660.799-0.5994-0.5431-0.29340.1520.05050.04950.43830.13350.58471.1028-69.775716.6279
335.23790.34240.67836.3882-2.54442.1768-0.29870.37450.2454-0.3451-0.00090.2184-0.728-0.1322-0.09270.31370.00450.03890.26110.05910.30237.8493-64.52429.3813
345.9810.85121.6874.8277-0.90158.46180.0854-0.78-0.70480.4978-0.0111-0.4268-0.02720.47940.0320.20980.0166-0.01070.45030.13550.449413.904-72.051618.5935
352.26982.34980.94325.6966-1.442.1759-0.00490.65040.0052-1.0018-0.03321.1909-0.2747-0.9681-0.06190.49250.0833-0.11470.61550.07390.5705-3.2559-66.24613.1778
365.48450.22880.55054.2528-0.38337.04160.0201-1.3249-0.24050.46470.10320.1685-0.4083-0.4329-0.07840.24090.07550.06470.49160.06510.34527.2592-67.484920.0277
376.3675-0.5287-3.27246.9896-1.21467.4715-0.31520.3959-1.5347-1.1039-0.61170.6570.7231-0.78061.00240.53450.0168-0.03730.5742-0.13161.2146-13.8639-89.28890.5601
382.0806-0.94351.39030.4274-0.6310.92460.02421.0298-0.5687-1.5249-0.2622-0.4572.09360.8010.09161.35620.16260.10010.7897-0.5031.3627-12.1201-94.5495-11.5588
396.4066-1.78693.16178.4498-3.13626.96790.5211.1242-1.3466-1.0494-0.40730.27671.44710.1707-0.05840.93490.05150.17290.5331-0.10821.5154-10.9186-92.3837-9.0201
401.8267-0.79712.00043.044-2.42073.07670.24310.2346-2.4059-0.6433-0.3449-0.05031.20880.73160.28740.58040.2715-0.06340.71230.23691.8486-4.0414-95.55198.1576
416.8507-0.9904-0.56334.10670.51813.72540.1955-1.0495-0.64070.1218-0.3137-0.3724-0.00320.29570.03480.2227-0.0337-0.00260.58250.12090.6234-8.8868-74.03314.7286
426.3098-1.0876-0.60193.43491.33393.5685-0.3975-0.5594-0.78860.29710.1237-0.23460.3190.5752-0.03870.30840.1335-0.06080.50030.14110.6776-10.2482-77.20318.6031
436.9432-0.98160.60746.32860.05472.82960.11-1.0407-0.26120.1988-0.34910.2125-0.0771-0.09320.26150.2178-0.0449-0.03760.67520.14190.6579-14.2892-75.505215.4457
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 339 through 354 )
2X-RAY DIFFRACTION2chain 'A' and (resid 355 through 399 )
3X-RAY DIFFRACTION3chain 'A' and (resid 400 through 411 )
4X-RAY DIFFRACTION4chain 'A' and (resid 412 through 443 )
5X-RAY DIFFRACTION5chain 'A' and (resid 444 through 480 )
6X-RAY DIFFRACTION6chain 'A' and (resid 481 through 502 )
7X-RAY DIFFRACTION7chain 'A' and (resid 503 through 527 )
8X-RAY DIFFRACTION8chain 'A' and (resid 528 through 544 )
9X-RAY DIFFRACTION9chain 'B' and (resid 338 through 376 )
10X-RAY DIFFRACTION10chain 'B' and (resid 377 through 398 )
11X-RAY DIFFRACTION11chain 'B' and (resid 399 through 443 )
12X-RAY DIFFRACTION12chain 'B' and (resid 444 through 544 )
13X-RAY DIFFRACTION13chain 'C' and (resid 336 through 349 )
14X-RAY DIFFRACTION14chain 'C' and (resid 350 through 370 )
15X-RAY DIFFRACTION15chain 'C' and (resid 371 through 396 )
16X-RAY DIFFRACTION16chain 'C' and (resid 397 through 433 )
17X-RAY DIFFRACTION17chain 'C' and (resid 434 through 458 )
18X-RAY DIFFRACTION18chain 'C' and (resid 459 through 492 )
19X-RAY DIFFRACTION19chain 'C' and (resid 493 through 502 )
20X-RAY DIFFRACTION20chain 'C' and (resid 503 through 544 )
21X-RAY DIFFRACTION21chain 'D' and (resid 335 through 361 )
22X-RAY DIFFRACTION22chain 'D' and (resid 362 through 385 )
23X-RAY DIFFRACTION23chain 'D' and (resid 386 through 433 )
24X-RAY DIFFRACTION24chain 'D' and (resid 434 through 458 )
25X-RAY DIFFRACTION25chain 'D' and (resid 459 through 544 )
26X-RAY DIFFRACTION26chain 'E' and (resid 336 through 361 )
27X-RAY DIFFRACTION27chain 'E' and (resid 362 through 384 )
28X-RAY DIFFRACTION28chain 'E' and (resid 385 through 396 )
29X-RAY DIFFRACTION29chain 'E' and (resid 397 through 421 )
30X-RAY DIFFRACTION30chain 'E' and (resid 422 through 443 )
31X-RAY DIFFRACTION31chain 'E' and (resid 444 through 458 )
32X-RAY DIFFRACTION32chain 'E' and (resid 459 through 469 )
33X-RAY DIFFRACTION33chain 'E' and (resid 470 through 479 )
34X-RAY DIFFRACTION34chain 'E' and (resid 480 through 492 )
35X-RAY DIFFRACTION35chain 'E' and (resid 493 through 502 )
36X-RAY DIFFRACTION36chain 'E' and (resid 503 through 544 )
37X-RAY DIFFRACTION37chain 'F' and (resid 339 through 354 )
38X-RAY DIFFRACTION38chain 'F' and (resid 355 through 384 )
39X-RAY DIFFRACTION39chain 'F' and (resid 385 through 433 )
40X-RAY DIFFRACTION40chain 'F' and (resid 434 through 443 )
41X-RAY DIFFRACTION41chain 'F' and (resid 444 through 480 )
42X-RAY DIFFRACTION42chain 'F' and (resid 481 through 502 )
43X-RAY DIFFRACTION43chain 'F' and (resid 503 through 544 )

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