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- PDB-5wb7: Crystal structure of the epidermal growth factor receptor extrace... -

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Basic information

Entry
Database: PDB / ID: 5wb7
TitleCrystal structure of the epidermal growth factor receptor extracellular region in complex with epiregulin
Components
  • Epidermal growth factor receptor
  • Proepiregulin
KeywordsSIGNALING PROTEIN / Receptor tyrosine kinase / growth factor / signaling / membrane protein
Function / homology
Function and homology information


luteinizing hormone signaling pathway / ovulation / ovarian cumulus expansion / ERBB4-ERBB4 signaling pathway / negative regulation of smooth muscle cell differentiation / ERBB2-ERBB4 signaling pathway / primary follicle stage / female meiotic nuclear division / PI3K events in ERBB4 signaling / transmembrane receptor protein tyrosine kinase activator activity ...luteinizing hormone signaling pathway / ovulation / ovarian cumulus expansion / ERBB4-ERBB4 signaling pathway / negative regulation of smooth muscle cell differentiation / ERBB2-ERBB4 signaling pathway / primary follicle stage / female meiotic nuclear division / PI3K events in ERBB4 signaling / transmembrane receptor protein tyrosine kinase activator activity / positive regulation of innate immune response / mRNA transcription / oocyte maturation / multivesicular body, internal vesicle lumen / negative regulation of cardiocyte differentiation / epidermal growth factor receptor binding / Shc-EGFR complex / positive regulation of protein kinase C signaling / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / regulation of peptidyl-tyrosine phosphorylation / epidermal growth factor binding / response to UV-A / PLCG1 events in ERBB2 signaling / ERBB2-EGFR signaling pathway / morphogenesis of an epithelial fold / PTK6 promotes HIF1A stabilization / ERBB2 Activates PTK6 Signaling / digestive tract morphogenesis / Signaling by EGFR / intracellular vesicle / negative regulation of epidermal growth factor receptor signaling pathway / eyelid development in camera-type eye / cerebral cortex cell migration / protein insertion into membrane / ERBB2 Regulates Cell Motility / positive regulation of protein kinase activity / protein tyrosine kinase activator activity / Respiratory syncytial virus (RSV) attachment and entry / positive regulation of cell division / Signaling by ERBB4 / PI3K events in ERBB2 signaling / keratinocyte proliferation / positive regulation of phosphorylation / anatomical structure morphogenesis / positive regulation of peptidyl-serine phosphorylation / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / SHC1 events in ERBB4 signaling / hair follicle development / MAP kinase kinase kinase activity / GAB1 signalosome / positive regulation of G1/S transition of mitotic cell cycle / embryonic placenta development / salivary gland morphogenesis / Nuclear signaling by ERBB4 / keratinocyte differentiation / Signaling by ERBB2 / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / transmembrane receptor protein tyrosine kinase activity / EGFR Transactivation by Gastrin / positive regulation of smooth muscle cell proliferation / positive regulation of mitotic nuclear division / GRB2 events in ERBB2 signaling / ossification / SHC1 events in ERBB2 signaling / basal plasma membrane / positive regulation of DNA repair / cellular response to epidermal growth factor stimulus / positive regulation of cytokine production / animal organ morphogenesis / positive regulation of DNA replication / epithelial cell proliferation / positive regulation of epithelial cell proliferation / Signal transduction by L1 / positive regulation of protein localization to plasma membrane / NOTCH3 Activation and Transmission of Signal to the Nucleus / cellular response to amino acid stimulus / growth factor activity / phosphatidylinositol 3-kinase/protein kinase B signal transduction / cellular response to estradiol stimulus / EGFR downregulation / wound healing / clathrin-coated endocytic vesicle membrane / Signaling by ERBB2 TMD/JMD mutants / Constitutive Signaling by EGFRvIII / cell-cell adhesion / response to peptide hormone / receptor protein-tyrosine kinase / Signaling by ERBB2 ECD mutants / negative regulation of protein catabolic process / Signaling by ERBB2 KD Mutants / positive regulation of interleukin-6 production / positive regulation of miRNA transcription / kinase binding / ruffle membrane / Downregulation of ERBB2 signaling / epidermal growth factor receptor signaling pathway
Similarity search - Function
Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Alpha-Beta Horseshoe / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV ...Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Alpha-Beta Horseshoe / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Laminin / Laminin / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / Furin-like repeat / Furin-like repeats / EGF-like domain profile. / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 1. / EGF-like domain signature 2. / : / EGF-like domain / Ribbon / 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 / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Proepiregulin / Epidermal growth factor receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.941 Å
AuthorsFreed, D.M. / Bessman, N.J. / Ferguson, K.M. / Lemmon, M.A.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)R01-CA198164 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)U54-CA193417 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)F32-GM109688 United States
CitationJournal: Cell / Year: 2017
Title: EGFR Ligands Differentially Stabilize Receptor Dimers to Specify Signaling Kinetics.
Authors: Freed, D.M. / Bessman, N.J. / Kiyatkin, A. / Salazar-Cavazos, E. / Byrne, P.O. / Moore, J.O. / Valley, C.C. / Ferguson, K.M. / Leahy, D.J. / Lidke, D.S. / Lemmon, M.A.
History
DepositionJun 28, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 18, 2017Provider: repository / Type: Initial release
Revision 1.1Oct 25, 2017Group: Database references / Category: citation
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_PubMed / _citation.title
Revision 1.2Nov 1, 2017Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
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_validate_close_contact / pdbx_validate_symm_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 / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_symm_contact.auth_asym_id_2 / _pdbx_validate_symm_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 2.1Oct 4, 2023Group: 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 20, 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: Epidermal growth factor receptor
B: Epidermal growth factor receptor
C: Epidermal growth factor receptor
D: Epidermal growth factor receptor
E: Proepiregulin
F: Proepiregulin
G: Proepiregulin
H: Proepiregulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)260,39822
Polymers254,2578
Non-polymers6,14114
Water73941
1
A: Epidermal growth factor receptor
D: Epidermal growth factor receptor
E: Proepiregulin
H: Proepiregulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)129,93511
Polymers127,1284
Non-polymers2,8077
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11260 Å2
ΔGint17 kcal/mol
Surface area49980 Å2
MethodPISA
2
B: Epidermal growth factor receptor
C: Epidermal growth factor receptor
F: Proepiregulin
G: Proepiregulin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)130,46311
Polymers127,1284
Non-polymers3,3347
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10400 Å2
ΔGint-5 kcal/mol
Surface area49750 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.647, 199.288, 87.916
Angle α, β, γ (deg.)90.000, 96.740, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 2 types, 8 molecules ABCDEFGH

#1: Protein
Epidermal growth factor receptor / Proto-oncogene c-ErbB-1 / Receptor tyrosine-protein kinase erbB-1


Mass: 56522.199 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EGFR, ERBB, ERBB1, HER1 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Sf9
References: UniProt: P00533, receptor protein-tyrosine kinase
#2: Protein
Proepiregulin


Mass: 7042.026 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EREG / Production host: Drosophila melanogaster (fruit fly) / Strain (production host): S2 / References: UniProt: O14944

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Sugars , 5 types, 14 molecules

#3: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...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: 748.682 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam 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]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#4: 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.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam 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
[]{[(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]{}}}}}LINUCSPDB-CARE
#5: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#6: 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.: 2
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
#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.: 7
Source method: isolated from a genetically manipulated source
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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Non-polymers , 1 types, 41 molecules

#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 41 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.71 Å3/Da / Density % sol: 54.61 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 7.6
Details: 0.03 M citric acid, 0.07 M Bis-Tris propane, 16% PEG3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.03 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jun 17, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03 Å / Relative weight: 1
ReflectionResolution: 2.94→50 Å / Num. obs: 53585 / % possible obs: 97.2 % / Redundancy: 2.8 % / Biso Wilson estimate: 71.36 Å2 / Rmerge(I) obs: 0.131 / Rpim(I) all: 0.09 / Rrim(I) all: 0.16 / Χ2: 1.081 / Net I/σ(I): 5.3
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.94-2.992.30.4581.724550.7490.3340.570.91589.8
2.99-3.052.50.4240.7810.3030.5230.93493.5
3.05-3.12.70.4160.790.2890.5090.96596.9
3.1-3.172.80.3740.8320.2630.4590.94397.8
3.17-3.242.80.3310.8470.230.4040.94897
3.24-3.312.90.2840.8990.1970.3471.01997.6
3.31-3.392.80.2460.9150.170.31.02396.8
3.39-3.492.80.2160.9320.1520.2651.03197.5
3.49-3.592.80.190.9490.1320.2321.03398
3.59-3.730.2090.9370.1430.2541.29497.3
3.7-3.8430.170.950.1140.2051.1198.3
3.84-3.992.90.1510.9640.1030.1841.16197.5
3.99-4.172.90.1370.9650.0940.1661.16997.2
4.17-4.392.80.1310.9630.090.1591.18598.2
4.39-4.6730.1230.9680.0830.1491.20698.3
4.67-5.0330.1240.9580.0830.1491.21998.3
5.03-5.532.90.1150.9720.0780.1391.11498.4
5.53-6.332.90.1170.9680.0780.1411.14298.8
6.33-7.9730.1050.9740.070.1261.11598.5
7.97-502.90.090.9750.0630.1110.93398.3

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Processing

Software
NameVersionClassification
HKL-3000data scaling
PHENIX1.11.1_2575refinement
PDB_EXTRACT3.22data extraction
HKL-3000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: EGFR domains I and III from PDB entry 3NJP

3njp


Resolution: 2.941→47.684 Å / SU ML: 0.49 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 32.1
RfactorNum. reflection% reflection
Rfree0.2675 2596 4.85 %
Rwork0.2246 --
obs0.2267 53542 96.52 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 277.25 Å2 / Biso mean: 92.8633 Å2 / Biso min: 27.95 Å2
Refinement stepCycle: final / Resolution: 2.941→47.684 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16658 0 404 41 17103
Biso mean--133.6 66.74 -
Num. residues----2186
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00417485
X-RAY DIFFRACTIONf_angle_d0.90223776
X-RAY DIFFRACTIONf_chiral_restr0.0652714
X-RAY DIFFRACTIONf_plane_restr0.0173061
X-RAY DIFFRACTIONf_dihedral_angle_d14.0526664
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 19

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.941-2.99440.46821170.36862144226178
2.9944-3.0520.44071260.34922595272193
3.052-3.11430.43591240.32152687281197
3.1143-3.1820.38061560.29792681283798
3.182-3.2560.32161330.28542704283797
3.256-3.33740.31551120.26332746285897
3.3374-3.42760.30211290.25632664279397
3.4276-3.52840.36131330.26682712284597
3.5284-3.64230.31731450.26612721286698
3.6423-3.77240.27461400.2372688282898
3.7724-3.92340.25921190.22772744286398
3.9234-4.10190.24191430.20472693283697
4.1019-4.3180.23691390.19362711285098
4.318-4.58830.24631490.17982729287898
4.5883-4.94230.21761470.17982731287898
4.9423-5.4390.25421420.19192753289599
5.439-6.22450.23351500.20852718286898
6.2245-7.83660.27781480.22842768291699
7.8366-47.69060.2151440.20442757290198
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)
15.956-2.1195-1.01766.12182.52094.1077-0.0350.11350.2189-0.2425-0.08850.42890.3194-0.34220.0890.5839-0.0904-0.13730.42450.01360.403176.945-8.51777.292
22.69930.2856-0.06231.08830.65151.6391-0.1862-0.50610.70510.21040.0623-0.0673-0.0450.06720.0540.8185-0.0319-0.25250.5115-0.12360.798690.2148.24291.377
33.3052-0.93260.51192.575-0.16933.0405-0.03540.28420.2089-0.00280.1113-0.13260.0347-0.0098-0.06990.4765-0.0726-0.06630.43840.0520.3314111.753-11.61669.822
46.7261-1.1431-3.04217.21161.79883.5876-0.3163-0.78660.40590.8590.64-1.9583-0.04111.0234-0.51380.6666-0.0573-0.26260.6327-0.1430.6244128.139-22.19275.774
56.5095-1.56240.70816.02611.43413.5799-0.05740.13740.1474-0.10130.04480.2880.1121-0.0131-0.00580.3179-0.0067-0.01580.36790.02460.340151.272-19.7221.624
62.8431-1.22511.0422.47470.58642.5468-0.3982-0.72281.2520.12470.0308-0.0137-0.3621-0.21510.37670.5772-0.0193-0.0460.4511-0.14030.606358.475-3.22140.425
73.1065-0.79050.29364.90550.59083.9064-0.00740.09270.08570.04120.0703-0.4397-0.16980.0854-0.07470.26990.0091-0.06330.35590.00650.389985.781-23.41329.436
88.05332.4514-1.57235.5970.9620.7615-0.081-1.104-0.47581.14580.2523-0.3410.62370.8246-0.10950.85160.101-0.3310.8233-0.02790.710698.01-35.03844.045
95.17611.41410.75927.76832.96693.0435-0.05-0.0536-0.21430.4204-0.30520.30640.0605-0.1820.31450.4204-0.01250.05540.3451-0.01160.367645.17432.28658.003
103.5175-3.2452-1.9512.64351.58882.2945-0.0495-0.07030.1462-0.1162-0.14330.276-0.15520.10250.12930.6118-0.0547-0.11380.5105-0.14350.765353.73116.96543.108
117.8676-0.1845-4.52543.7790.84095.39320.0867-1.12191.35420.57770.7744-1.31690.31880.5961-0.61690.60870.1243-0.38010.6986-0.25381.155479.08635.98964.097
122.3948-1.4642-1.31872.6814-1.42313.49790.172-1.10673.3172-0.22940.28931.2397-0.61560.7991-0.59660.7801-0.1188-0.1290.8662-0.47542.399994.68145.80855.434
134.8882.31950.37987.55431.49821.99960.6135-0.446-0.22841.4119-0.7663-0.22680.2202-0.16010.08441.0167-0.1813-0.28350.58110.00680.489985.61944.996111.062
141.7247-2.2958-1.24774.67632.86423.1470.47620.00680.1728-0.0369-0.2818-0.4465-0.0468-0.1238-0.18960.8529-0.02-0.32540.5401-0.08691.110587.36628.56595.073
154.73330.5935-1.07433.18491.60682.36460.609-0.0586-1.81750.31880.2915-1.30650.23450.6115-0.61661.03490.108-0.43820.7951-0.1562.2196119.32547.776102.994
167.06870.6557-1.43633.6127-2.33871.64960.453-0.30690.9809-0.7770.0947-1.24770.57160.47520.20261.7732-0.02170.3580.9734-0.39071.8625131.29255.88288.727
177.909-1.3533-3.84646.37350.16112.30680.52920.3419-0.4636-0.0389-0.50350.2320.1283-0.65320.0720.6994-0.1072-0.23810.7379-0.02870.492788.269-15.18860.45
182.377-1.61943.2827.8297-2.28534.81560.16030.91090.0667-1.0522-0.30480.24460.74510.04980.20690.6590.09250.00540.7711-0.00750.311568.43-25.96110.903
198.70772.3399-3.09411.91660.4222.54030.0471-2.82770.5320.3989-0.07230.01511.08990.22220.19031.11890.139-0.09211.23880.0290.543357.6337.5776.174
202.93310.25680.55230.7707-0.37140.4960.4229-0.71230.0841.7779-0.2689-0.8027-0.57680.0014-0.20241.741-0.3381-0.8091.33790.09011.2548104.48851.513123.098
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 2:164 )A2 - 164
2X-RAY DIFFRACTION2( CHAIN A AND RESID 165:311 )A165 - 311
3X-RAY DIFFRACTION3( CHAIN A AND RESID 312:479 )A312 - 479
4X-RAY DIFFRACTION4( CHAIN A AND RESID 480:501 )A480 - 501
5X-RAY DIFFRACTION5( CHAIN B AND RESID 2:164 )B2 - 164
6X-RAY DIFFRACTION6( CHAIN B AND RESID 165:311 )B165 - 311
7X-RAY DIFFRACTION7( CHAIN B AND RESID 312:479 )B312 - 479
8X-RAY DIFFRACTION8( CHAIN B AND RESID 480:505 )B480 - 505
9X-RAY DIFFRACTION9( CHAIN C AND RESID 2:164 )C2 - 164
10X-RAY DIFFRACTION10( CHAIN C AND RESID 165:311 )C165 - 311
11X-RAY DIFFRACTION11( CHAIN C AND RESID 312:479 )C312 - 479
12X-RAY DIFFRACTION12( CHAIN C AND RESID 480:501 )C480 - 501
13X-RAY DIFFRACTION13( CHAIN D AND RESID 2:164 )D2 - 164
14X-RAY DIFFRACTION14( CHAIN D AND RESID 165:311 )D165 - 311
15X-RAY DIFFRACTION15( CHAIN D AND RESID 312:479 )D312 - 479
16X-RAY DIFFRACTION16( CHAIN D AND RESID 480:500 )D480 - 500
17X-RAY DIFFRACTION17( CHAIN E AND RESID 10:48 )E10 - 48
18X-RAY DIFFRACTION18( CHAIN F AND RESID 10:46 )F10 - 46
19X-RAY DIFFRACTION19( CHAIN G AND RESID 10:48 )G10 - 48
20X-RAY DIFFRACTION20( CHAIN H AND RESID 10:45 )H10 - 45

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