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- PDB-7stz: Crystal Structure of Human E-cadherin EC1-5 bound by mouse monocl... -

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Basic information

Entry
Database: PDB / ID: 7stz
TitleCrystal Structure of Human E-cadherin EC1-5 bound by mouse monoclonal antibody Fab mAb-1_19A11
Components
  • Cadherin-1
  • mAb-1_19A11 Heavy Chain
  • mAb-1_19A11 Light Chain
Keywordscell adhesion/immune system / SSGCID / Cadherin-1 / cell adhesion / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / cell adhesion-immune system complex
Function / homology
Function and homology information


response to heparin / desmosome assembly / response to Gram-positive bacterium / pituitary gland development / gamma-catenin binding / Regulation of MITF-M-dependent genes involved in extracellular matrix, focal adhesion and epithelial-to-mesenchymal transition / negative regulation of axon extension / desmosome / cellular response to indole-3-methanol / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules ...response to heparin / desmosome assembly / response to Gram-positive bacterium / pituitary gland development / gamma-catenin binding / Regulation of MITF-M-dependent genes involved in extracellular matrix, focal adhesion and epithelial-to-mesenchymal transition / negative regulation of axon extension / desmosome / cellular response to indole-3-methanol / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / flotillin complex / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / cell-cell adhesion mediated by cadherin / Formation of definitive endoderm / catenin complex / Apoptotic cleavage of cell adhesion proteins / adherens junction organization / GTPase activating protein binding / cell-cell junction assembly / Adherens junctions interactions / ankyrin binding / negative regulation of cell-cell adhesion / apical junction complex / cellular response to lithium ion / homophilic cell adhesion via plasma membrane adhesion molecules / Integrin cell surface interactions / lateral plasma membrane / RHO GTPases activate IQGAPs / synapse assembly / positive regulation of protein localization / cell adhesion molecule binding / Degradation of the extracellular matrix / Transcriptional and post-translational regulation of MITF-M expression and activity / InlA-mediated entry of Listeria monocytogenes into host cells / negative regulation of cell migration / protein tyrosine kinase binding / protein localization to plasma membrane / adherens junction / trans-Golgi network / cell morphogenesis / beta-catenin binding / cell-cell adhesion / cytoplasmic side of plasma membrane / positive regulation of protein import into nucleus / response to toxic substance / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / neuron projection development / cell junction / cell migration / lamellipodium / actin cytoskeleton / regulation of gene expression / postsynapse / endosome / cadherin binding / response to xenobiotic stimulus / calcium ion binding / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / glutamatergic synapse / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane / cytoplasm
Similarity search - Function
Cadherin prodomain like / Cadherin prodomain / Cadherin prodomain like / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Cadherin / Catenin binding domain superfamily / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. ...Cadherin prodomain like / Cadherin prodomain / Cadherin prodomain like / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Cadherin / Catenin binding domain superfamily / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherin-like / Cadherins domain profile. / Cadherin-like superfamily
Similarity search - Domain/homology
beta-D-mannopyranose / alpha-D-mannopyranose / Cadherin-1
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.95 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: Pnas Nexus / Year: 2022
Title: Regulation of multiple dimeric states of E-cadherin by adhesion activating antibodies revealed through Cryo-EM and X-ray crystallography.
Authors: Maker, A. / Bolejack, M. / Schecterson, L. / Hammerson, B. / Abendroth, J. / Edwards, T.E. / Staker, B. / Myler, P.J. / Gumbiner, B.M.
History
DepositionNov 15, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 26, 2022Provider: repository / Type: Initial release
Revision 1.1Feb 1, 2023Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.3Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: Cadherin-1
H: mAb-1_19A11 Heavy Chain
L: mAb-1_19A11 Light Chain
D: Cadherin-1
I: mAb-1_19A11 Heavy Chain
M: mAb-1_19A11 Light Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)239,27856
Polymers234,1126
Non-polymers5,16750
Water9,620534
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)85.340, 131.620, 201.760
Angle α, β, γ (deg.)90.000, 100.860, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain H and (resid 1 through 14 or resid 16...
21(chain I and (resid 1 through 14 or resid 16...
12(chain L and (resid 1 through 10 or resid 12...
22(chain M and (resid 1 through 10 or resid 12...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLNGLNPROPRO(chain H and (resid 1 through 14 or resid 16...HB1 - 1420 - 33
121GLNGLNSERSER(chain H and (resid 1 through 14 or resid 16...HB16 - 3035 - 49
131TYRTYRMETMET(chain H and (resid 1 through 14 or resid 16...HB32 - 5151 - 70
141SERSERTHRTHR(chain H and (resid 1 through 14 or resid 16...HB84 - 87103 - 106
151GLNGLNMETMET(chain H and (resid 1 through 14 or resid 16...HB1 - 8220 - 101
161ASPASPGLYGLY(chain H and (resid 1 through 14 or resid 16...HB89 - 110108 - 129
171GLNGLNEDOEDO(chain H and (resid 1 through 14 or resid 16...HB - FA1 - 30120
181GLNGLNGLNGLN(chain H and (resid 1 through 14 or resid 16...HB137156
191GLNGLNEDOEDO(chain H and (resid 1 through 14 or resid 16...HB - FA1 - 30120
1101GLNGLNEDOEDO(chain H and (resid 1 through 14 or resid 16...HB - FA1 - 30120
1111GLNGLNEDOEDO(chain H and (resid 1 through 14 or resid 16...HB - FA1 - 30120
1121GLNGLNEDOEDO(chain H and (resid 1 through 14 or resid 16...HB - FA1 - 30120
211GLNGLNPROPRO(chain I and (resid 1 through 14 or resid 16...IE1 - 1420 - 33
221GLNGLNSERSER(chain I and (resid 1 through 14 or resid 16...IE16 - 3035 - 49
231TYRTYRMETMET(chain I and (resid 1 through 14 or resid 16...IE32 - 5151 - 70
241GLYGLYTHRTHR(chain I and (resid 1 through 14 or resid 16...IE53 - 5772 - 76
251TYRTYRMETMET(chain I and (resid 1 through 14 or resid 16...IE59 - 8278 - 101
261SERSERTHRTHR(chain I and (resid 1 through 14 or resid 16...IE84 - 87103 - 106
271ASPASPGLYGLY(chain I and (resid 1 through 14 or resid 16...IE89 - 110108 - 129
281GLYGLYVALVAL(chain I and (resid 1 through 14 or resid 16...IE112 - 148131 - 167
291GLYGLYPROPRO(chain I and (resid 1 through 14 or resid 16...IE150 - 193169 - 212
2101ARGARGARGARG(chain I and (resid 1 through 14 or resid 16...IE194213
2111GLNGLNEDOEDO(chain I and (resid 1 through 14 or resid 16...IE - BB1 - 30220
2121GLNGLNEDOEDO(chain I and (resid 1 through 14 or resid 16...IE - BB1 - 30220
2131GLNGLNEDOEDO(chain I and (resid 1 through 14 or resid 16...IE - BB1 - 30220
2141GLNGLNEDOEDO(chain I and (resid 1 through 14 or resid 16...IE - BB1 - 30220
112ASPASPSERSER(chain L and (resid 1 through 10 or resid 12...LC1 - 1021 - 30
122ALAALATYRTYR(chain L and (resid 1 through 10 or resid 12...LC12 - 9832 - 118
132ASPASPHOHHOH(chain L and (resid 1 through 10 or resid 12...LC - GB1 - 30121
142ASPASPHOHHOH(chain L and (resid 1 through 10 or resid 12...LC - GB1 - 30121
152CYSCYSCYSCYS(chain L and (resid 1 through 10 or resid 12...LC220240
162ASPASPHOHHOH(chain L and (resid 1 through 10 or resid 12...LC - GB1 - 30121
172ASPASPHOHHOH(chain L and (resid 1 through 10 or resid 12...LC - GB1 - 30121
182ASPASPHOHHOH(chain L and (resid 1 through 10 or resid 12...LC - GB1 - 30121
192ASPASPHOHHOH(chain L and (resid 1 through 10 or resid 12...LC - GB1 - 30121
212ASPASPSERSER(chain M and (resid 1 through 10 or resid 12...MF1 - 1021 - 30
222ALAALATYRTYR(chain M and (resid 1 through 10 or resid 12...MF12 - 9832 - 118
232THRTHRASPASP(chain M and (resid 1 through 10 or resid 12...MF100 - 1120 - 21
242ASPASPCACA(chain M and (resid 1 through 10 or resid 12...MF - DB1 - 30121
252ASPASPCACA(chain M and (resid 1 through 10 or resid 12...MF - DB1 - 30121
262ASPASPCACA(chain M and (resid 1 through 10 or resid 12...MF - DB1 - 30121
272ASPASPCACA(chain M and (resid 1 through 10 or resid 12...MF - DB1 - 30121
282ASPASPCACA(chain M and (resid 1 through 10 or resid 12...MF - DB1 - 30121

NCS ensembles :
ID
1
2

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Components

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Protein , 1 types, 2 molecules CD

#1: Protein Cadherin-1 / CAM 120/80 / Epithelial cadherin / E-cadherin / Uvomorulin


Mass: 64179.281 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CDH1, CDHE, UVO / Plasmid: HosaA.19747.a.LS31 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P12830

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Antibody , 2 types, 4 molecules HILM

#2: Antibody mAb-1_19A11 Heavy Chain


Mass: 26346.926 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: I6L985 / Source: (gene. exp.) Mus musculus (house mouse) / Gene: Igh / Production host: Escherichia coli BL21(DE3) (bacteria)
#3: Antibody mAb-1_19A11 Light Chain


Mass: 26529.557 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: A0A0C6EL31 / Source: (gene. exp.) Mus musculus (house mouse) / Gene: LC / Production host: Escherichia coli BL21(DE3) (bacteria)

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Sugars , 3 types, 16 molecules

#5: 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.: 1 / 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
#7: Sugar ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C6H12O6
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0
#8: Sugar
ChemComp-BMA / beta-D-mannopyranose / beta-D-mannose / D-mannose / mannose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C6H12O6
IdentifierTypeProgram
DManpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-mannopyranoseCOMMON NAMEGMML 1.0
b-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 4 types, 568 molecules

#4: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical
ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#9: Chemical...
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 24 / Source method: obtained synthetically / Formula: Ca
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 534 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
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: 4.75 Å3/Da / Density % sol: 74.12 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop / pH: 7
Details: HosaA.19747.a.LS31.PC00180 at 11.5 mg/mL was mixed 2:1 (0.2 uL protein and 0.1 uL precipitant) with 0.1M sodium HEPES pH 7.0 and 15% w/v PEG4000 (ProPlex B11) and stored at 14C. The crystal ...Details: HosaA.19747.a.LS31.PC00180 at 11.5 mg/mL was mixed 2:1 (0.2 uL protein and 0.1 uL precipitant) with 0.1M sodium HEPES pH 7.0 and 15% w/v PEG4000 (ProPlex B11) and stored at 14C. The crystal was cryoprotected with 15% ethylene glycol. Tray: 321285b11, puck: ygq5-2.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.9787 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jun 24, 2021 / Details: Beryllium Lenses
RadiationMonochromator: Diamond [111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9787 Å / Relative weight: 1
ReflectionResolution: 2.95→49.54 Å / Num. obs: 92265 / % possible obs: 99.9 % / Redundancy: 7.431 % / Biso Wilson estimate: 53.51 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.118 / Rrim(I) all: 0.127 / Χ2: 0.912 / Net I/σ(I): 14.25 / Num. measured all: 685577 / Scaling rejects: 78
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
2.95-3.037.4860.6313.267830.8970.678100
3.03-3.117.4880.508466360.9260.546100
3.11-3.27.4810.4134.9264660.9520.44399.9
3.2-3.37.4640.3196.2462490.9720.34399.9
3.3-3.417.4650.267.6460690.980.279100
3.41-3.537.4590.18810.0458540.9880.20299.9
3.53-3.667.4550.16211.5656840.9910.17499.9
3.66-3.817.4580.14113.0754220.9920.152100
3.81-3.987.450.12514.5352610.9930.13499.9
3.98-4.177.4410.10117.4550030.9950.109100
4.17-4.47.4430.08719.4747960.9960.093100
4.4-4.667.4370.07921.5645010.9960.085100
4.66-4.997.4230.07223.2542540.9970.077100
4.99-5.397.4240.07223.1439740.9970.07799.8
5.39-5.97.4150.07722.1236100.9970.082100
5.9-6.67.3870.07522.6233420.9970.0899.9
6.6-7.627.3780.06525.2628930.9970.07100
7.62-9.337.3120.0530.624980.9980.05499.9
9.33-13.197.20.04335.0819200.9980.04699.8
13.19-49.546.4290.04234.7710500.9980.04696.1

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Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHENIX1.20rc3-4406refinement
PDB_EXTRACT3.27data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6cxy

6cxy


Resolution: 2.95→49.54 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 21.01 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2077 1997 2.17 %
Rwork0.1819 90211 -
obs0.1824 92208 99.91 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 231.22 Å2 / Biso mean: 80.0732 Å2 / Biso min: 5.87 Å2
Refinement stepCycle: final / Resolution: 2.95→49.54 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13767 0 288 534 14589
Biso mean--117.12 49.72 -
Num. residues----1837
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11H0X-RAY DIFFRACTION10.644TORSIONAL
12I0X-RAY DIFFRACTION10.644TORSIONAL
21L2022X-RAY DIFFRACTION10.644TORSIONAL
22M2022X-RAY DIFFRACTION10.644TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.95-3.020.30571430.28164026545100
3.02-3.110.29261470.235563866533100
3.11-3.20.24651420.21364756617100
3.2-3.30.22631380.211563986536100
3.3-3.420.24951440.218264696613100
3.42-3.550.25181450.183464096554100
3.55-3.720.19891410.176763996540100
3.72-3.910.24371400.179864386578100
3.91-4.160.1791410.164564316572100
4.16-4.480.17951430.144764816624100
4.48-4.930.17331410.141964186559100
4.93-5.640.15081380.155265086646100
5.64-7.10.22041480.199664846632100
7.1-49.540.19141460.18976513665999
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)
12.90861.4272-0.26764.7037-1.31432.2106-0.20440.53580.1416-0.46240.2793-0.0125-0.09-0.0503-0.08020.3614-0.01730.07740.45820.06740.395-2.23617.842571.9608
25.21430.486-5.18452.7371-2.53186.7527-0.0190.10581.3990.4869-0.5568-1.222-2.14952.09160.62730.8029-0.22520.05070.57230.08381.016829.499543.989379.1152
38.00132.31684.15630.88311.9195.2004-0.0830.15690.6583-0.2235-0.0280.10990.2408-0.13420.17280.4785-0.02680.14860.35530.16490.735317.202437.365575.5658
47.74171.70995.12926.66730.87379.2929-0.27291.10.6362-0.49720.3515-1.18720.16671.3908-0.14060.61090.13940.26030.61150.01910.847328.172437.556570.9501
56.41914.33010.94644.47682.40722.23050.1612-0.0572-0.03670.1466-0.1098-0.1701-0.01920.0132-0.05360.32180.02890.07670.22710.08990.40340.360614.050294.5466
61.90751.16720.33152.22540.12810.4662-0.02890.00870.3163-0.3985-0.1169-0.2613-0.10520.08550.13350.39560.02860.14710.27450.03290.58999.047429.22287.7863
71.69761.416-0.26284.3725-3.37147.2794-0.25640.09480.8807-0.3334-0.0753-0.6145-0.3957-0.47610.3420.4430.10310.12670.41920.00631.118417.639949.987185.5771
81.97090.00030.05511.97551.10032.7760.0174-0.0618-0.58980.2958-0.12650.12780.2862-0.14140.09620.37190.04660.09260.27730.06960.6119-21.6203-13.515599.9701
9-0.06550.12541.0119-0.2177-0.98621.1409-0.07830.0115-0.09040.7121-0.2761-0.0637-0.72430.58920.2042.15110.0702-0.48171.74450.1470.844712.3697-1.9851172.6646
101.4835-0.1769-0.17943.61182.36893.3247-0.0588-0.2312-0.33270.24870.04570.18380.18350.18010.01820.2485-0.00890.08830.28790.05810.4347-35.0158.7026112.5295
117.1980.7043-1.99859.75532.46867.0475-0.12650.06011.3525-1.0185-0.16421.226-0.9036-1.87890.16230.47070.1032-0.04920.6103-0.10180.9336-64.9736.4748118.1603
123.8391-0.93181.34722.3472-0.65073.63910.0984-0.47430.01710.07390.04780.550.1651-0.5089-0.09250.3036-0.0530.1390.4305-0.02140.5554-58.557427.8968118.4269
137.9961-3.7474-0.93.6178-0.39521.82340.14980.28410.0963-0.2945-0.12840.1225-0.0805-0.0167-0.02050.2879-0.02760.01730.2103-0.02890.335-37.488914.72290.4042
142.0007-0.7274-0.51131.97370.13360.82540.0787-0.18730.2017-0.0198-0.06740.099-0.1142-0.056-0.00540.2682-0.04260.02910.265-0.06470.4484-45.649225.6837102.6141
152.4782-0.1050.20782.33951.30547.8211-0.0674-0.40870.78570.1268-0.04250.0681-0.9043-0.18220.03450.38590.03350.07720.3408-0.11040.8654-53.812844.0789113.0806
162.4897-1.63461.00923.062-1.36512.17460.07830.3935-0.4581-0.27680.00870.21010.01020.0568-0.10550.325-0.00520.03390.3623-0.1230.4913-15.5776-8.255374.3599
171.3343-1.53171.70770.5171-0.82161.226-0.0730.0758-0.4231-0.40680.19730.3113-0.7164-0.8905-0.25811.36090.4017-0.39861.44930.03430.7474-48.246721.223441.2059
180.40680.2890.5030.08960.31560.655-0.2394-0.1767-0.58240.15550.3151-0.25-0.8968-0.5504-0.03872.11131.112-0.70812.036-0.1318-0.0657-70.706338.282-7.6225
190.057-0.1709-0.54631.10362.43286.0266-0.8211-0.61220.35470.64380.2765-0.1174-0.96410.14130.12671.58190.4105-0.34161.5717-0.36130.4565-70.393437.2943-39.4101
208.8614-0.7891-2.73715.6770.31628.6002-0.5445-0.5669-0.24410.2443-0.1541-0.51510.2477-0.02420.55480.31-0.0087-0.06650.37290.06050.4597-65.84221.9654-68.0493
212.0835-0.5813-3.25335.60140.48168.30840.0912-0.0190.3211-0.1278-0.4862-0.7201-0.55950.15990.30880.3517-0.0198-0.05670.47460.02680.633-61.729726.2919-72.6934
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'H' and (resid 1 through 125 )H1 - 125
2X-RAY DIFFRACTION2chain 'H' and (resid 126 through 141 )H126 - 141
3X-RAY DIFFRACTION3chain 'H' and (resid 142 through 189 )H142 - 189
4X-RAY DIFFRACTION4chain 'H' and (resid 190 through 222 )H190 - 222
5X-RAY DIFFRACTION5chain 'L' and (resid 1 through 81 )L1 - 81
6X-RAY DIFFRACTION6chain 'L' and (resid 82 through 134 )L82 - 134
7X-RAY DIFFRACTION7chain 'L' and (resid 135 through 220 )L135 - 220
8X-RAY DIFFRACTION8chain 'D' and (resid 1 through 125 )D1 - 125
9X-RAY DIFFRACTION9chain 'D' and (resid 126 through 437 )D126 - 437
10X-RAY DIFFRACTION10chain 'I' and (resid 1 through 125 )I1 - 125
11X-RAY DIFFRACTION11chain 'I' and (resid 126 through 140 )I126 - 140
12X-RAY DIFFRACTION12chain 'I' and (resid 141 through 220 )I141 - 220
13X-RAY DIFFRACTION13chain 'M' and (resid 1 through 81 )M1 - 81
14X-RAY DIFFRACTION14chain 'M' and (resid 82 through 134 )M82 - 134
15X-RAY DIFFRACTION15chain 'M' and (resid 135 through 220 )M135 - 220
16X-RAY DIFFRACTION16chain 'C' and (resid 1 through 125 )C1 - 125
17X-RAY DIFFRACTION17chain 'C' and (resid 126 through 268 )C126 - 268
18X-RAY DIFFRACTION18chain 'C' and (resid 269 through 390 )C269 - 390
19X-RAY DIFFRACTION19chain 'C' and (resid 391 through 444 )C391 - 444
20X-RAY DIFFRACTION20chain 'C' and (resid 445 through 494 )C445 - 494
21X-RAY DIFFRACTION21chain 'C' and (resid 495 through 540 )C495 - 540

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