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- PDB-4wrl: Structure of the human CSF-1:CSF-1R complex -

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Basic information

Entry
Database: PDB / ID: 4wrl
TitleStructure of the human CSF-1:CSF-1R complex
Components(Macrophage colony-stimulating factor ...) x 2
KeywordsCYTOKINE/CYTOKINE RECEPTOR / cytokine-cytokine receptor complex
Function / homology
Function and homology information


regulation of macrophage derived foam cell differentiation / mammary gland fat development / positive regulation of macrophage colony-stimulating factor signaling pathway / monocyte homeostasis / macrophage homeostasis / macrophage colony-stimulating factor receptor binding / positive regulation of macrophage migration / osteoclast proliferation / positive regulation of odontogenesis of dentin-containing tooth / forebrain neuron differentiation ...regulation of macrophage derived foam cell differentiation / mammary gland fat development / positive regulation of macrophage colony-stimulating factor signaling pathway / monocyte homeostasis / macrophage homeostasis / macrophage colony-stimulating factor receptor binding / positive regulation of macrophage migration / osteoclast proliferation / positive regulation of odontogenesis of dentin-containing tooth / forebrain neuron differentiation / developmental process involved in reproduction / macrophage colony-stimulating factor receptor activity / CSF1-CSF1R complex / monocyte activation / macrophage colony-stimulating factor signaling pathway / regulation of macrophage migration / positive regulation of microglial cell migration / mammary duct terminal end bud growth / cellular response to macrophage colony-stimulating factor stimulus / cell-cell junction maintenance / microglial cell proliferation / positive regulation of mononuclear cell proliferation / positive regulation of macrophage differentiation / olfactory bulb development / mammary gland duct morphogenesis / myeloid leukocyte migration / neutrophil homeostasis / host-mediated activation of viral process / ruffle organization / positive regulation of monocyte differentiation / positive regulation of multicellular organism growth / positive regulation of osteoclast differentiation / positive regulation of macrophage proliferation / branching involved in mammary gland duct morphogenesis / positive regulation of macrophage derived foam cell differentiation / positive regulation of Ras protein signal transduction / regulation of bone resorption / positive regulation of cell motility / Other interleukin signaling / positive regulation of tyrosine phosphorylation of STAT protein / positive regulation of cell-matrix adhesion / growth factor binding / positive regulation of protein tyrosine kinase activity / positive regulation of macrophage chemotaxis / cytokine binding / cellular response to cytokine stimulus / Interleukin-10 signaling / positive regulation of protein metabolic process / regulation of MAPK cascade / hemopoiesis / Transcriptional Regulation by VENTX / macrophage differentiation / monocyte differentiation / regulation of ossification / positive regulation of chemokine production / Transcriptional and post-translational regulation of MITF-M expression and activity / homeostasis of number of cells within a tissue / axon guidance / cell surface receptor protein tyrosine kinase signaling pathway / osteoclast differentiation / peptidyl-tyrosine phosphorylation / response to ischemia / cytokine activity / regulation of actin cytoskeleton organization / Post-translational protein phosphorylation / growth factor activity / receptor protein-tyrosine kinase / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of protein phosphorylation / cytokine-mediated signaling pathway / Signaling by CSF1 (M-CSF) in myeloid cells / cell migration / regulation of cell shape / protein autophosphorylation / protein tyrosine kinase activity / protein phosphatase binding / Ras protein signal transduction / cell population proliferation / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / receptor complex / nuclear body / positive regulation of cell migration / endoplasmic reticulum lumen / inflammatory response / negative regulation of cell population proliferation / innate immune response / intracellular membrane-bounded organelle / positive regulation of cell population proliferation / positive regulation of gene expression / negative regulation of apoptotic process / perinuclear region of cytoplasm / cell surface / signal transduction / protein homodimerization activity / extracellular space / extracellular region / nucleoplasm / ATP binding / identical protein binding
Similarity search - Function
Macrophage colony stimulating factor-1 / Macrophage colony stimulating factor-1 (CSF-1) / Macrophage colony-stimulating factor 1 receptor / Platelet-derived growth factor receptor Ig-like domain 4 / Tyrosine-protein kinase, receptor class III, conserved site / Receptor tyrosine kinase class III signature. / Growth Hormone; Chain: A; - #10 / Four-helical cytokine-like, core / Growth Hormone; Chain: A; / Immunoglobulin ...Macrophage colony stimulating factor-1 / Macrophage colony stimulating factor-1 (CSF-1) / Macrophage colony-stimulating factor 1 receptor / Platelet-derived growth factor receptor Ig-like domain 4 / Tyrosine-protein kinase, receptor class III, conserved site / Receptor tyrosine kinase class III signature. / Growth Hormone; Chain: A; - #10 / Four-helical cytokine-like, core / Growth Hormone; Chain: A; / Immunoglobulin / Immunoglobulin domain / : / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Immunoglobulins / Protein kinase-like domain superfamily / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
3'-sialyl-N-acetyllactosamine / N-acetyl-alpha-neuraminic acid / Macrophage colony-stimulating factor 1 receptor / Macrophage colony-stimulating factor 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.802 Å
AuthorsFelix, J. / De Munck, S. / Elegheert, J. / Savvides, S.N.
CitationJournal: Structure / Year: 2015
Title: Structure and Assembly Mechanism of the Signaling Complex Mediated by Human CSF-1.
Authors: Jan Felix / Steven De Munck / Kenneth Verstraete / Leander Meuris / Nico Callewaert / Jonathan Elegheert / Savvas N Savvides /
Abstract: Human colony-stimulating factor 1 receptor (hCSF-1R) is unique among the hematopoietic receptors because it is activated by two distinct cytokines, CSF-1 and interleukin-34 (IL-34). Despite ever- ...Human colony-stimulating factor 1 receptor (hCSF-1R) is unique among the hematopoietic receptors because it is activated by two distinct cytokines, CSF-1 and interleukin-34 (IL-34). Despite ever-growing insights into the central role of hCSF-1R signaling in innate and adaptive immunity, inflammatory diseases, and cancer, the structural basis of the functional dichotomy of hCSF-1R has remained elusive. Here, we report crystal structures of ternary complexes between hCSF-1 and hCSF-1R, including their complete extracellular assembly, and propose a mechanism for the cooperative human CSF-1:CSF-1R complex that relies on the adoption by dimeric hCSF-1 of an active conformational state and homotypic receptor interactions. Furthermore, we trace the cytokine-binding duality of hCSF-1R to a limited set of conserved interactions mediated by functionally equivalent residues on CSF-1 and IL-34 that play into the geometric requirements of hCSF-1R activation, and map the possible mechanistic consequences of somatic mutations in hCSF-1R associated with cancer.
History
DepositionOct 24, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Aug 12, 2015Provider: repository / Type: Initial release
Revision 1.1Sep 9, 2015Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / 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_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / 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 / _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_unobs_or_zero_occ_atoms.label_asym_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_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_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 10, 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
Revision 2.2Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Macrophage colony-stimulating factor 1 receptor
C: Macrophage colony-stimulating factor 1 receptor
B: Macrophage colony-stimulating factor 1
D: Macrophage colony-stimulating factor 1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,02913
Polymers102,6824
Non-polymers4,3479
Water00
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8190 Å2
ΔGint21 kcal/mol
Surface area44790 Å2
MethodPISA
Unit cell
Length a, b, c (Å)142.997, 142.997, 138.323
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number80
Space group name H-MI41

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Components

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Macrophage colony-stimulating factor ... , 2 types, 4 molecules ACBD

#1: Protein Macrophage colony-stimulating factor 1 receptor / CSF-1 receptor / M-CSF-R / Proto-oncogene c-Fms


Mass: 31583.867 Da / Num. of mol.: 2 / Fragment: UNP residues 20-296 / Mutation: N240Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CSF1R, FMS / Cell line (production host): HEK-293S / Production host: Homo sapiens (human)
References: UniProt: P07333, receptor protein-tyrosine kinase
#2: Protein Macrophage colony-stimulating factor 1 / MCSF / Lanimostim


Mass: 19757.314 Da / Num. of mol.: 2 / Fragment: UNP residues 33-181
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CSF1 / Production host: Escherichia coli (E. coli) / References: UniProt: P09603

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Sugars , 5 types, 9 molecules

#3: Polysaccharide N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2- ...N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 820.744 Da / Num. of mol.: 2 / Source method: obtained synthetically
DescriptorTypeProgram
DNeup5Aca2-3DGalpb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,4,3/[a2122h-1b_1-5_2*NCC/3=O][a2112h-1b_1-5][Aad21122h-2a_2-6_5*NCC/3=O][a1221m-1a_1-5]/1-2-3-4/a4-b1_a6-d1_b3-c2WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{[(3+2)][a-D-Neup5Ac]{}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#4: Polysaccharide beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 383.349 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGalpb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a2112h-1b_1-5]/1-2/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{}}}LINUCSPDB-CARE
#5: Polysaccharide N-acetyl-alpha-neuraminic acid-(2-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / 3'-sialyl-N-acetyllactosamine


Type: oligosaccharide, Oligosaccharide / Class: Substrate analog / Mass: 674.604 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: oligosaccharide / References: 3'-sialyl-N-acetyllactosamine
DescriptorTypeProgram
DNeup5Aca2-3DGalpb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,3,2/[a2122h-1b_1-5_2*NCC/3=O][a2112h-1b_1-5][Aad21122h-2a_2-6_5*NCC/3=O]/1-2-3/a4-b1_b3-c2WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{[(3+2)][a-D-Neup5Ac]{}}}}LINUCSPDB-CARE
#6: Sugar ChemComp-SIA / N-acetyl-alpha-neuraminic acid / N-acetylneuraminic acid / sialic acid / alpha-sialic acid / O-SIALIC ACID


Type: D-saccharide, alpha linking / Mass: 309.270 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H19NO9
IdentifierTypeProgram
DNeup5AcaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-a-D-neuraminic acidCOMMON NAMEGMML 1.0
a-D-Neup5AcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
Neu5AcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#7: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 3.44 Å3/Da / Density % sol: 64.28 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 0.2 M Lithium sulfate monohydrate, 0.1 M Tris pH 8.5 and 28% w/v PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.97625 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Apr 25, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 2.8→49.71 Å / Num. obs: 34125 / % possible obs: 99.8 % / Redundancy: 6.9 % / Biso Wilson estimate: 82.26 Å2 / Rmerge(I) obs: 0.064 / Net I/σ(I): 20.73
Reflection shellResolution: 2.8→2.97 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.815 / Mean I/σ(I) obs: 2.32 / % possible all: 99.2

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4DKD, 3UF2

4dkd

3uf2


Resolution: 2.802→49.71 Å / SU ML: 0.52 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 30.59 / Stereochemistry target values: ML
Details: Galactose 403 and Galactose 408 on chain C failed to be fitted in the exo-anomeric conformation of their glycosidic bond
RfactorNum. reflection% reflection
Rfree0.2613 1706 5 %
Rwork0.2231 --
obs0.225 34117 99.83 %
Solvent computationShrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.802→49.71 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6370 0 287 0 6657
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0066827
X-RAY DIFFRACTIONf_angle_d1.0949324
X-RAY DIFFRACTIONf_dihedral_angle_d13.4462424
X-RAY DIFFRACTIONf_chiral_restr0.0521125
X-RAY DIFFRACTIONf_plane_restr0.0141181
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8016-2.88410.521380.38952638X-RAY DIFFRACTION98
2.8841-2.97710.40031420.34352709X-RAY DIFFRACTION100
2.9771-3.08350.36061420.30312686X-RAY DIFFRACTION100
3.0835-3.2070.31141420.2772710X-RAY DIFFRACTION100
3.207-3.35290.35311400.2812660X-RAY DIFFRACTION100
3.3529-3.52960.31821440.24362722X-RAY DIFFRACTION100
3.5296-3.75070.32641430.24862712X-RAY DIFFRACTION100
3.7507-4.04020.23041410.21392683X-RAY DIFFRACTION100
4.0402-4.44650.21861430.19212720X-RAY DIFFRACTION100
4.4465-5.08940.2241420.18322707X-RAY DIFFRACTION100
5.0894-6.40990.23161430.20672713X-RAY DIFFRACTION100
6.4099-49.7180.2281460.2042751X-RAY DIFFRACTION100
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)
12.04951.12660.67514.57181.35782.8965-0.26510.2951-0.2415-0.26350.3831-0.3601-0.01590.13650.00240.4579-0.19280.0810.6725-0.01880.49999.93840.3851-31.0206
20.6902-1.54610.52593.70090.33671.8101-0.12740.7808-1.2759-0.13850.3654-0.3956-0.10690.14990.04330.5787-0.1620.12040.7533-0.30070.74285.2551-17.6289-37.1975
30.6052-0.3862-0.11370.3652-0.50860.4428-0.1698-0.0323-0.43910.48250.28040.4974-0.00670.084101.3968-0.19380.45081.1787-0.23961.599-20.0162-41.5512-32.524
41.9839-0.7686-0.4444.53841.73753.4121-0.3053-0.38790.19350.2490.3642-0.2645-0.00040.21990.00220.46650.2062-0.08630.6569-0.01190.53389.9514-71.8339-93.0482
50.5320.5857-0.23612.26852.01912.2243-0.0595-0.76690.2964-0.41350.3784-0.2014-0.570.25850.02410.73320.3196-0.20890.9233-0.13910.6914.7987-54.159-85.9649
60.4720.58610.31360.32590.469-0.1453-0.54060.24920.4013-0.01190.43650.2238-0.2084-0.2765-01.25990.1868-0.28161.3673-0.191.4065-23.8003-30.7563-86.8703
70.38620.3680.08130.17290.08550.0115-0.47690.30120.6201-1.3439-0.86780.1882-0.6276-1.3306-0.01391.56260.1902-0.34511.0267-0.13550.785-0.7174-33.0247-80.5741
80.98020.04020.24131.46431.130.6458-0.22310.55140.0911-1.04070.235-0.5656-0.72130.9547-01.0645-0.17350.13921.0965-0.01150.777916.297-33.4447-78.218
91.9611-0.7519-0.05631.90391.14610.7378-0.191-0.045-0.1112-0.2786-0.21460.3517-0.17510.264700.63460.0704-0.04730.5137-0.14450.69683.8785-42.4387-74.8677
100.38250.3704-0.00311.5379-0.05250.7067-0.03010.82840.7001-1.99210.1378-0.8437-2.02430.86870.01721.3736-0.16610.10031.0359-0.08090.698612.5449-31.5687-81.6448
110.25850.2494-0.23010.78660.14360.51150.40430.7234-0.0023-2.0307-0.161-1.0221-0.9860.2719-0.14023.5515-0.42140.87581.47610.2643-0.307712.9308-31.2862-95.9154
120.6197-0.34440.04420.4053-0.18070.19640.1298-0.738-0.79631.2805-0.11490.70360.4185-1.5855-01.3166-0.05340.28370.9408-0.03050.84990.0795-38.1582-42.8784
131.85240.3964-0.54891.25380.90710.5504-0.1097-0.8076-0.19481.01180.1947-0.59450.7521.176800.99660.244-0.09931.08720.03430.809516.7402-37.9355-46.1865
141.1551-0.252-0.43641.5120.78040.5878-0.20630.09540.16010.3755-0.09810.401-0.1272-0.124500.669-0.06040.04180.5633-0.10740.67093.9359-29.0358-50.3681
150.6006-0.43830.06832.0638-0.27991.0246-0.0116-0.923-0.51331.84050.2061-0.55961.9731.33480.02491.31550.10520.01450.95310.00230.754312.9626-39.456-42.1615
160.1040.302-0.0291.863-0.10750.03230.1599-1.22260.22372.8827-0.51450.10871.39111.21990.07582.52510.1621-0.27341.87870.03040.710614.5039-40.3146-28.2403
170.1509-0.1636-0.24721.55170.8832-0.4553-0.1745-0.63770.06790.2839-0.0622-0.0098-0.3868-0.21840.0011.36210.3863-0.00571.5109-0.02331.4183-0.7765-61.0911-97.5169
180.03710.5298-0.89930.78740.64591.1836-0.2504-0.00330.1011-0.42890.0810.16920.1767-0.42870.00011.5058-0.1573-0.28581.69230.10191.33860.1541-9.2536-29.8537
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 20 through 174 )
2X-RAY DIFFRACTION2chain 'A' and (resid 175 through 208 )
3X-RAY DIFFRACTION3chain 'A' and (resid 209 through 296 )
4X-RAY DIFFRACTION4chain 'C' and (resid 20 through 174 )
5X-RAY DIFFRACTION5chain 'C' and (resid 175 through 208 )
6X-RAY DIFFRACTION6chain 'C' and (resid 209 through 296)
7X-RAY DIFFRACTION7chain 'B' and (resid 2 through 24 )
8X-RAY DIFFRACTION8chain 'B' and (resid 25 through 63 )
9X-RAY DIFFRACTION9chain 'B' and (resid 64 through 89 )
10X-RAY DIFFRACTION10chain 'B' and (resid 90 through 130 )
11X-RAY DIFFRACTION11chain 'B' and (resid 131 through 146 )
12X-RAY DIFFRACTION12chain 'D' and (resid 2 through 24 )
13X-RAY DIFFRACTION13chain 'D' and (resid 25 through 63 )
14X-RAY DIFFRACTION14chain 'D' and (resid 64 through 87 )
15X-RAY DIFFRACTION15chain 'D' and (resid 88 through 130 )
16X-RAY DIFFRACTION16chain 'D' and (resid 131 through 146 )
17X-RAY DIFFRACTION17chain 'C' and (resid 401 through 409)
18X-RAY DIFFRACTION18chain 'A' and (resid 401 through 411)

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