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- PDB-5fob: Crystal Structure of Human Complement C3b in complex with Smallpo... -

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Basic information

Entry
Database: PDB / ID: 5fob
TitleCrystal Structure of Human Complement C3b in complex with Smallpox Inhibitor of Complement (SPICE)
Components
  • COMPLEMENT C3 BETA CHAIN
  • COMPLEMENT C3B ALPHA' CHAIN
  • SMALLPOX INHIBITOR OF COMPLEMENT SPICE, D15L
KeywordsLIPID BINDING PROTEIN / COMPLEMENT SYSTEM / IMMUNE SYSTEM / PLASMA PROTEIN / REGULATORS OF COMPLEMENT ACTIVITY / COFACTOR ACTIVITY / DECAY ACCELERATING ACTIVITY / IMMUNE EVASION
Function / homology
Function and homology information


negative regulation of complement activation / oviduct epithelium development / C5L2 anaphylatoxin chemotactic receptor binding / regulation of triglyceride biosynthetic process / complement binding / positive regulation of activation of membrane attack complex / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation ...negative regulation of complement activation / oviduct epithelium development / C5L2 anaphylatoxin chemotactic receptor binding / regulation of triglyceride biosynthetic process / complement binding / positive regulation of activation of membrane attack complex / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation / positive regulation of lipid storage / positive regulation of G protein-coupled receptor signaling pathway / positive regulation of phagocytosis, engulfment / complement receptor mediated signaling pathway / Activation of C3 and C5 / positive regulation of type IIa hypersensitivity / positive regulation of glucose transmembrane transport / complement-dependent cytotoxicity / complement activation, alternative pathway / complement activation / neuron remodeling / endopeptidase inhibitor activity / amyloid-beta clearance / positive regulation of vascular endothelial growth factor production / Purinergic signaling in leishmaniasis infection / complement activation, classical pathway / Peptide ligand-binding receptors / fatty acid metabolic process / Regulation of Complement cascade / Post-translational protein phosphorylation / response to bacterium / positive regulation of receptor-mediated endocytosis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / G alpha (i) signalling events / blood microparticle / secretory granule lumen / membrane => GO:0016020 / immune response / inflammatory response / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / signaling receptor binding / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Complement control protein C3/B5 / Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / S-adenosyl-L-methionine-dependent methyltransferases / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb ...Complement control protein C3/B5 / Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / S-adenosyl-L-methionine-dependent methyltransferases / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / : / : / Complement component 3, CUB domain 2 / Complement component 3, CUB domain 1 / Complement C3-like, NTR domain / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / : / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system domain / Anaphylatoxin domain signature. / Anaphylatoxin/fibulin / Anaphylatoxin, complement system / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Glycosyltransferase - #20 / Netrin domain / NTR domain profile. / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor binding domain / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor / Tissue inhibitor of metalloproteinases-like, OB-fold / Alpha-2-macroglobulin / Macroglobulin domain / Alpha-2-macroglobulin, bait region domain / Alpha-macroglobulin-like, TED domain / Alpha-2-macroglobulin family / MG2 domain / A-macroglobulin TED domain / Alpha-2-macroglobulin bait region domain / Alpha-2-Macroglobulin / Alpha-2-macroglobulin family / Other non-globular / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/SCR/CCP superfamily / Sushi/CCP/SCR domain profile. / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / Single Sheet / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Jelly Rolls / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
IODIDE ION / Complement C3 / D15L
Similarity search - Component
Biological speciesVARIOLA MAJOR VIRUS
HOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsForneris, F. / Wu, J. / Xue, X. / Gros, P.
CitationJournal: Embo J. / Year: 2016
Title: Regulators of Complement Activity Mediate Inhibitory Mechanisms Through a Common C3B-Binding Mode.
Authors: Forneris, F. / Wu, J. / Xue, X. / Ricklin, D. / Lin, Z. / Sfyroera, G. / Tzekou, A. / Volokhina, E. / Granneman, J.C. / Hauhart, R. / Bertram, P. / Liszewski, M.K. / Atkinson, J.P. / Lambris, J.D. / Gros, P.
History
DepositionNov 18, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 6, 2016Provider: repository / Type: Initial release
Revision 1.1Jun 1, 2016Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / 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_validate_chiral / 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.occupancy / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list / _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_label_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_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _struct_conn.conn_type_id / _struct_conn.id / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 10, 2024Group: 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
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: COMPLEMENT C3 BETA CHAIN
B: COMPLEMENT C3B ALPHA' CHAIN
C: SMALLPOX INHIBITOR OF COMPLEMENT SPICE, D15L
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,81543
Polymers202,3363
Non-polymers4,47940
Water3,729207
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21300 Å2
ΔGint-125.7 kcal/mol
Surface area79800 Å2
MethodPISA
Unit cell
Length a, b, c (Å)68.891, 83.311, 127.377
Angle α, β, γ (deg.)75.03, 76.20, 68.50
Int Tables number1
Space group name H-MP1

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein COMPLEMENT C3 BETA CHAIN / C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PROTEIN 1


Mass: 71393.320 Da / Num. of mol.: 1 / Fragment: RESIDUES 23-667 / Source method: isolated from a natural source / Details: PURIFIED FROM HUMAN PLASMA / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P01024
#2: Protein COMPLEMENT C3B ALPHA' CHAIN


Mass: 104074.148 Da / Num. of mol.: 1 / Fragment: CCP DOMAINS, RESIDUES 749-1663 / Source method: isolated from a natural source / Details: PURIFIED FROM HUMAN PLASMA / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P01024
#3: Protein SMALLPOX INHIBITOR OF COMPLEMENT SPICE, D15L


Mass: 26868.223 Da / Num. of mol.: 1 / Fragment: RESIDUES 19-263
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) VARIOLA MAJOR VIRUS / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q76U65

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Sugars , 2 types, 2 molecules

#4: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...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: 732.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#5: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE

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Non-polymers , 5 types, 245 molecules

#6: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Cl
#7: Chemical...
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#9: Chemical
ChemComp-IOD / IODIDE ION / Iodide


Mass: 126.904 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: I
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 207 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsRESIDUE 1013 HAS BEEN CONVERTED FROM GLN TO GLU IN CONVERSION OF C3 PROTEIN TO C3B

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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: 3.25 Å3/Da / Density % sol: 64.22 % / Description: NONE
Crystal growDetails: 75MM AMMONIUM IODIDE, 3.5% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.939
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.939 Å / Relative weight: 1
ReflectionResolution: 2.5→47.8 Å / Num. obs: 84531 / % possible obs: 97.2 % / Observed criterion σ(I): 1.5 / Redundancy: 2 % / Biso Wilson estimate: 60.63 Å2 / Rmerge(I) obs: 0.11 / Net I/σ(I): 4.3
Reflection shellResolution: 2.5→2.55 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.39 / Mean I/σ(I) obs: 1 / % possible all: 96.3

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2I07, 3O8E, 2WII

2i07

3o8e

2wii


Resolution: 2.6→42.356 Å / SU ML: 0.35 / σ(F): 1.96 / Phase error: 28.53 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2295 2249 3 %
Rwork0.198 --
obs0.1989 75190 97.29 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 80 Å2
Refinement stepCycle: LAST / Resolution: 2.6→42.356 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14003 0 235 207 14445
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00514563
X-RAY DIFFRACTIONf_angle_d0.87919706
X-RAY DIFFRACTIONf_dihedral_angle_d18.7345472
X-RAY DIFFRACTIONf_chiral_restr0.0612215
X-RAY DIFFRACTIONf_plane_restr0.0052523
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6-2.65650.31911320.30544511X-RAY DIFFRACTION96
2.6565-2.71830.36161440.30414493X-RAY DIFFRACTION96
2.7183-2.78630.32591400.26984546X-RAY DIFFRACTION97
2.7863-2.86160.30071360.25464557X-RAY DIFFRACTION97
2.8616-2.94580.31711420.2424507X-RAY DIFFRACTION97
2.9458-3.04080.30281510.2424532X-RAY DIFFRACTION97
3.0408-3.14950.28831320.23054616X-RAY DIFFRACTION98
3.1495-3.27550.26861410.21494546X-RAY DIFFRACTION98
3.2755-3.42460.25661110.20354626X-RAY DIFFRACTION98
3.4246-3.6050.2231530.19914605X-RAY DIFFRACTION98
3.605-3.83080.2241410.19064530X-RAY DIFFRACTION98
3.8308-4.12630.22191330.18774575X-RAY DIFFRACTION98
4.1263-4.54110.20561480.16254604X-RAY DIFFRACTION98
4.5411-5.19720.18671550.1564550X-RAY DIFFRACTION98
5.1972-6.5440.19091490.19774553X-RAY DIFFRACTION98
6.544-42.3620.211410.18864590X-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)
12.32150.5457-1.07123.4067-0.54093.7321-0.2696-1.33510.06470.4337-0.0636-0.7283-0.0940.49170.34280.80260.4527-0.23021.53140.02660.679612.5582-15.591860.9615
22.87210.45730.82881.58870.68935.58540.0314-0.4103-0.41140.24490.08290.05490.54990.1643-0.08580.27890.01690.03180.28640.07860.37716.174-28.265126.9021
36.1358-0.9952-2.42742.30441.06745.77670.08240.10110.14560.1485-0.31250.1006-0.0748-0.57650.2070.1936-0.0364-0.09250.2979-0.0550.4631-22.2526-13.198113.0015
43.46420.89223.37452.55650.30187.361-0.6205-0.72490.4860.33020.5093-0.0886-1.0844-0.4249-0.06080.72970.2332-0.15650.6448-0.25640.7262-17.95343.055943.4639
52.9462-0.67540.44322.49970.98882.8417-0.4118-10.38670.66310.4384-0.2997-0.63050.2513-0.06771.00390.1692-0.33110.9839-0.36370.86381.41893.714556.1052
60.2626-0.7129-0.64911.54641.68426.8086-0.3686-0.64270.05240.62360.0387-0.05620.35-0.49710.33880.53140.0593-0.06410.838-0.09770.5584-1.8461-13.213545.8287
72.88530.74460.65811.48360.21774.6886-0.0382-0.13630.5254-0.03610.072-0.1697-0.51920.34560.00640.2624-0.0794-0.01090.2665-0.00480.535713.8122-10.197514.7184
85.04310.6174-2.72197.2211-1.99463.19980.24040.94310.1512-0.9622-0.235-0.60660.30850.36810.42010.33940.00560.06690.62070.10610.420811.553-21.1893-13.4102
92.47411.1815-0.22236.2754-1.16473.157-0.07270.61890.1567-0.4677-0.1576-0.1483-0.01380.18380.26380.28260.0645-0.020.47670.01780.31940.7846-25.7851-11.8116
103.995-0.48311.45211.6145-3.16888.31940.2297-0.3056-0.6367-0.44920.22880.06741.431-0.5525-0.36611.2108-0.01320.00680.51210.07980.6115-1.9592-55.963423.1994
114.9159-0.4713-1.84533.88920.29874.0763-0.02020.5856-0.2021-0.5045-0.10520.40310.1369-0.15660.10440.28930.0524-0.14630.5467-0.08970.429-20.6778-28.8722-12.3541
123.6611-1.20830.19284.21050.13233.77730.43451.1404-0.2028-0.1621-0.5850.2461-0.1995-0.71430.07050.47380.1656-0.03621.0156-0.12770.27195.0201-48.113877.4121
137.3386-3.97050.7882.3350.05852.1084-0.42040.221-0.5521-0.9316-0.57850.52040.9136-0.54371.05720.8337-0.00910.23240.6756-0.18890.696-1.0943-49.4185-15.2102
146.2382-2.8213-1.06924.49071.76851.6153-0.33690.1641-0.80870.2754-0.05020.67050.33730.18350.40160.68350.06010.22980.7518-0.15510.629613.0074-64.008-23.631
155.5477-0.83651.73645.4792-3.92713.162-0.2530.0437-0.2047-0.4943-0.3725-0.72490.25310.64420.50710.51290.02840.08220.49870.0510.505229.1952-12.3709-28.5086
163.8158-0.3507-2.54614.8645-3.59456.5703-0.2528-0.7725-0.0692-0.32040.1236-0.16010.81670.75220.20530.39320.10840.03670.80570.10570.530123.6583-27.3163.3691
174.01910.34362.46183.343-0.34411.9112-0.6527-0.1987-1.24760.2487-0.675-0.14012.69461.15570.24071.17340.38690.31091.12160.42310.895823.0293-41.737939.1877
180.05760.05270.02680.01590.01450.00340.21590.08070.6564-0.4891-0.30520.461-0.343-0.12590.21031.77650.26430.15251.78960.43810.993732.9861-30.391366.3667
190.23570.4162-0.58661.57-2.00142.62220.2373-0.41170.15491.9837-0.5178-0.03940.98040.9538-0.38011.82970.1575-0.18191.60970.42410.918624.281-34.738668.4768
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND RESID 1:104
2X-RAY DIFFRACTION2CHAIN A AND RESID 105:209
3X-RAY DIFFRACTION3CHAIN A AND RESID 210:328
4X-RAY DIFFRACTION4CHAIN A AND RESID 329:426
5X-RAY DIFFRACTION5CHAIN A AND RESID 427:534
6X-RAY DIFFRACTION6CHAIN A AND RESID 579:642
7X-RAY DIFFRACTION7CHAIN A AND RESID 535:578 OR CHAIN B AND RESID 746:806
8X-RAY DIFFRACTION8CHAIN B AND RESID 730:745
9X-RAY DIFFRACTION9CHAIN B AND RESID 807:911
10X-RAY DIFFRACTION10CHAIN B AND RESID 912:967 OR CHAIN A AND RESID 1266:1330
11X-RAY DIFFRACTION11CHAIN B AND RESID 1331:1480
12X-RAY DIFFRACTION12CHAIN B AND RESID 968:1265
13X-RAY DIFFRACTION13CHAIN B AND RESID 1481:1494
14X-RAY DIFFRACTION14CHAIN B AND RESID 1495:1641
15X-RAY DIFFRACTION15CHAIN C AND RESID 1:64
16X-RAY DIFFRACTION16CHAIN C AND RESID 65:127
17X-RAY DIFFRACTION17CHAIN C AND RESID 128:184
18X-RAY DIFFRACTION18CHAIN C AND RESID 220:239
19X-RAY DIFFRACTION19CHAIN C AND RESID 185:212

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