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- PDB-6vel: Crystal Structure of Human E-cadherin bound by mouse monoclonal a... -

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Basic information

Entry
Database: PDB / ID: 6vel
TitleCrystal Structure of Human E-cadherin bound by mouse monoclonal antibody 66E8Fab
Components
  • 66E8 Fab Heavy Chain
  • 66E8 Fab Light Chain
  • Ubiquitin-like protein SMT3,Cadherin-1
KeywordsCELL ADHESION/Immune System / SSGCID / cadherin / E-cadherin / antibody / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / CELL ADHESION / CELL ADHESION-Immune System complex
Function / homology
Function and homology information


SUMO is conjugated to E1 (UBA2:SAE1) / response to Gram-positive bacterium / SUMOylation of nuclear envelope proteins / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / SUMOylation of transcription factors / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of transcription cofactors / pituitary gland development ...SUMO is conjugated to E1 (UBA2:SAE1) / response to Gram-positive bacterium / SUMOylation of nuclear envelope proteins / SUMO is transferred from E1 to E2 (UBE2I, UBC9) / SUMO is proteolytically processed / regulation of protein catabolic process at postsynapse, modulating synaptic transmission / SUMOylation of transcription factors / Postmitotic nuclear pore complex (NPC) reformation / SUMOylation of transcription cofactors / pituitary gland development / gamma-catenin binding / SUMOylation of DNA damage response and repair proteins / negative regulation of axon extension / cell-cell adhesion mediated by cadherin / SUMOylation of DNA replication proteins / cellular response to indole-3-methanol / flotillin complex / septin ring / calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules / Formation of definitive endoderm / SUMOylation of SUMOylation proteins / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / SUMOylation of RNA binding proteins / Adherens junctions interactions / catenin complex / Apoptotic cleavage of cell adhesion proteins / GTPase activating protein binding / cell-cell junction assembly / adherens junction organization / SUMOylation of chromatin organization proteins / apical junction complex / ankyrin binding / negative regulation of cell-cell adhesion / cellular response to lithium ion / ubiquitin-like protein ligase binding / homophilic cell adhesion via plasma membrane adhesion molecules / protein sumoylation / lateral plasma membrane / RHO GTPases activate IQGAPs / Integrin cell surface interactions / cell adhesion molecule binding / synapse assembly / InlA-mediated entry of Listeria monocytogenes into host cells / Degradation of the extracellular matrix / negative regulation of cell migration / protein tyrosine kinase binding / condensed nuclear chromosome / protein localization to plasma membrane / adherens junction / cell morphogenesis / trans-Golgi network / cytoplasmic side of plasma membrane / response to toxic substance / PML body / beta-catenin binding / cell-cell adhesion / positive regulation of protein import into nucleus / protein tag activity / neuron projection development / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / actin cytoskeleton / lamellipodium / cell junction / postsynapse / regulation of gene expression / endosome / response to xenobiotic stimulus / cadherin binding / glutamatergic synapse / calcium ion binding / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / extracellular exosome / extracellular region / identical protein binding / membrane / nucleus / plasma membrane
Similarity search - Function
Cadherin prodomain like / Cadherin prodomain / Cadherin prodomain like / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Catenin binding domain superfamily / Cadherins / Cadherin / Rad60/SUMO-like domain / Ubiquitin-2 like Rad60 SUMO-like ...Cadherin prodomain like / Cadherin prodomain / Cadherin prodomain like / Cadherin, Y-type LIR-motif / Cadherin, Y-type LIR-motif / Catenin binding domain superfamily / Cadherins / Cadherin / Rad60/SUMO-like domain / Ubiquitin-2 like Rad60 SUMO-like / Cadherin conserved site / Cadherin domain signature. / Cadherin repeats. / Cadherin domain / Cadherins domain profile. / Cadherin-like / Cadherin-like superfamily / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Cadherin-1 / Ubiquitin-like protein SMT3
Similarity search - Component
Biological speciesMus musculus (house mouse)
Saccharomyces cerevisiae (brewer's yeast)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.65 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
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
DepositionJan 2, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 29, 2020Provider: repository / Type: Initial release
Revision 2.0Aug 12, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Polymer sequence / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / entity_poly / entity_poly_seq / entity_src_gen / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_struct_special_symmetry / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / pdbx_validate_torsion / refine / refine_hist / refine_ls_restr / refine_ls_shell / software / struct_asym / struct_conf / struct_conn / struct_mon_prot_cis / struct_ref_seq / struct_sheet_range / 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.label_seq_id / _atom_site.occupancy / _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_label_seq_id / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.pdbx_end_seq_num / _pdbx_nonpoly_scheme.asym_id / _pdbx_nonpoly_scheme.auth_mon_id / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.entity_id / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.ndb_seq_num / _pdbx_nonpoly_scheme.pdb_mon_id / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_refine_tls.L[1][1] / _pdbx_refine_tls.L[1][2] / _pdbx_refine_tls.L[1][3] / _pdbx_refine_tls.L[2][2] / _pdbx_refine_tls.L[2][3] / _pdbx_refine_tls.L[3][3] / _pdbx_refine_tls.S[1][1] / _pdbx_refine_tls.S[1][2] / _pdbx_refine_tls.S[1][3] / _pdbx_refine_tls.S[2][1] / _pdbx_refine_tls.S[2][2] / _pdbx_refine_tls.S[2][3] / _pdbx_refine_tls.S[3][1] / _pdbx_refine_tls.S[3][2] / _pdbx_refine_tls.S[3][3] / _pdbx_refine_tls.T[1][1] / _pdbx_refine_tls.T[1][2] / _pdbx_refine_tls.T[1][3] / _pdbx_refine_tls.T[2][2] / _pdbx_refine_tls.T[2][3] / _pdbx_refine_tls.T[3][3] / _pdbx_refine_tls.origin_x / _pdbx_refine_tls.origin_y / _pdbx_refine_tls.origin_z / _pdbx_struct_assembly_prop.value / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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_struct_sheet_hbond.range_1_auth_comp_id / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_comp_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _pdbx_struct_special_symmetry.auth_seq_id / _pdbx_struct_special_symmetry.label_asym_id / _pdbx_unobs_or_zero_occ_atoms.label_seq_id / _pdbx_validate_torsion.phi / _pdbx_validate_torsion.psi / _refine.B_iso_max / _refine.B_iso_mean / _refine.B_iso_min / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.overall_SU_ML / _refine.pdbx_overall_phase_error / _refine_hist.pdbx_B_iso_mean_ligand / _refine_hist.pdbx_B_iso_mean_solvent / _refine_ls_shell.R_factor_R_free / _refine_ls_shell.R_factor_R_work / _software.version / _struct_asym.entity_id / _struct_conf.beg_label_seq_id / _struct_conf.end_label_seq_id / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_seq_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 / _struct_mon_prot_cis.label_seq_id / _struct_mon_prot_cis.pdbx_label_seq_id_2 / _struct_mon_prot_cis.pdbx_omega_angle / _struct_ref_seq.db_align_beg / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.seq_align_end / _struct_sheet_range.beg_auth_comp_id / _struct_sheet_range.beg_auth_seq_id / _struct_sheet_range.beg_label_comp_id / _struct_sheet_range.beg_label_seq_id / _struct_sheet_range.end_auth_comp_id / _struct_sheet_range.end_auth_seq_id / _struct_sheet_range.end_label_comp_id / _struct_sheet_range.end_label_seq_id / _struct_site.details / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_num_residues / _struct_site_gen.auth_asym_id / _struct_site_gen.auth_comp_id / _struct_site_gen.auth_seq_id / _struct_site_gen.label_asym_id / _struct_site_gen.label_comp_id / _struct_site_gen.label_seq_id / _struct_site_gen.pdbx_num_res / _struct_site_gen.site_id / _struct_site_gen.symmetry
Description: Sequence discrepancy / Details: Replaced incorrect Na ion with Ca / Provider: author / Type: Coordinate replacement
Revision 2.1Feb 1, 2023Group: Database references / Category: citation / citation_author / database_2
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 / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 25, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
H: 66E8 Fab Heavy Chain
L: 66E8 Fab Light Chain
C: Ubiquitin-like protein SMT3,Cadherin-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,54112
Polymers88,8443
Non-polymers6979
Water2,306128
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6160 Å2
ΔGint-137 kcal/mol
Surface area29380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)142.170, 142.170, 90.320
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121
Components on special symmetry positions
IDModelComponents
11C-403-

SO4

21C-403-

SO4

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Components

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Protein , 1 types, 1 molecules C

#3: Protein Ubiquitin-like protein SMT3,Cadherin-1 / CAM 120/80 / Epithelial cadherin / E-cadherin / Uvomorulin


Mass: 36625.715 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast), (gene. exp.) Homo sapiens (human)
Strain: ATCC 204508 / S288c / Gene: SMT3, YDR510W, D9719.15, CDH1, CDHE, UVO / Plasmid: pET-21a_modified
Details (production host): N-term His/SUMO-tagged human E-cadherin subunits EC1-EC2 in pET-21a from Barry Gumbiner
Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q12306, UniProt: P12830

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Antibody , 2 types, 2 molecules HL

#1: Antibody 66E8 Fab Heavy Chain


Mass: 26407.775 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pET-21a_modified
Details (production host): plasmid: N-term His/SUMO-tagged human E-cadherin subunits EC1-EC2 in pET-21a from Barry Gumbiner
Production host: Escherichia coli BL21(DE3) (bacteria)
#2: Antibody 66E8 Fab Light Chain


Mass: 25810.666 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: LH
Details (production host): full Fab, mouse mAb 66E8, light chain; vector unknown; construct sequence significantly different from reference; from Gumbiner lab, Wei Wang
Production host: Escherichia coli BL21(DE3) (bacteria)

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Non-polymers , 3 types, 137 molecules

#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 128 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 3.04 Å3/Da / Density % sol: 59.52 %
Crystal growTemperature: 290 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: A complex of HosaA.19747.a.KW2, MumuA.20194.a.LG23, and MumuA.20195.a.LH23 was crystallized at 10.4 mg/ml at 14C and mixed 1:1 with 12.5% (w/v) PEG 4000, 20% (v/v) 1,2,6-hexanetriol, 0.1M ...Details: A complex of HosaA.19747.a.KW2, MumuA.20194.a.LG23, and MumuA.20195.a.LH23 was crystallized at 10.4 mg/ml at 14C and mixed 1:1 with 12.5% (w/v) PEG 4000, 20% (v/v) 1,2,6-hexanetriol, 0.1M GlyGly/AMPD pH 8.5, 0.03M of each Lithium sulfate, Sodium sulfate, and Potassium sulfate. Tray 307437a10: puck ckt8-9.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Jul 18, 2019 / Details: Beryllium Lenses
RadiationMonochromator: Diamond [111] / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.65→46.54 Å / Num. obs: 30906 / % possible obs: 99.9 % / Redundancy: 8.734 % / Biso Wilson estimate: 60.262 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.061 / Rrim(I) all: 0.065 / Χ2: 1.057 / Net I/σ(I): 24.68 / Num. measured all: 269932
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.65-2.728.9840.5953.5620150224422430.920.631100
2.72-2.798.9460.4474.7119798221322130.9580.473100
2.79-2.878.9790.3466.1519215214021400.9680.366100
2.87-2.968.9510.2647.8718726209220920.9830.28100
2.96-3.068.9720.19410.8818150202320230.9910.205100
3.06-3.178.8880.16113.1217304194719470.9920.171100
3.17-3.298.920.12616.1916940189918990.9960.133100
3.29-3.428.7840.09919.9715846180418040.9970.105100
3.42-3.578.7880.07525.915405175317530.9980.079100
3.57-3.758.720.06530.1214755169216920.9980.069100
3.75-3.958.6580.05634.413705158315830.9990.059100
3.95-4.198.5470.04739.9712897151015090.9990.0599.9
4.19-4.488.5110.0444.5312136142614260.9990.043100
4.48-4.848.4610.03847.0911295133513350.9990.04100
4.84-5.38.5170.03847.9810476123012300.9990.04100
5.3-5.938.4740.03746.989491112011200.9990.039100
5.93-6.848.4570.03548.1783729909900.9990.037100
6.84-8.388.3650.02952.3371358538530.9990.031100
8.38-11.858.0420.02356.64539667167110.025100
11.85-46.547.1540.02354.3927403993830.9990.02596

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX1.18.2-3874refinement
XDSdata reduction
XSCALEdata scaling
PDB_EXTRACT3.25data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2o72

2o72


Resolution: 2.65→46.54 Å / SU ML: 0.35 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 24.66 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2358 1542 4.99 %
Rwork0.194 29330 -
obs0.1961 30872 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 218.3 Å2 / Biso mean: 74.6742 Å2 / Biso min: 36.85 Å2
Refinement stepCycle: final / Resolution: 2.65→46.54 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4723 0 33 128 4884
Biso mean--117.65 56.83 -
Num. residues----630
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 11 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2.65-2.740.31341570.279126322789
2.74-2.830.31551220.251926272749
2.83-2.950.26891340.254126492783
2.95-3.080.30171300.240226362766
3.08-3.240.24831500.237926602810
3.24-3.450.2681690.219226012770
3.45-3.710.2541310.207526532784
3.71-4.090.23331420.186526792821
4.09-4.680.19191300.148726882818
4.68-5.890.18741390.162227082847
5.89-46.540.23191380.183727972935
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)
12.0286-0.3195-0.41987.11630.69482.78160.1496-0.01260.30320.0652-0.0126-0.032-0.2598-0.0048-0.15140.40160.01510.07640.4238-0.0030.3189-60.719550.881611.0364
25.92251.36521.20228.97121.01692.23260.3130.75010.5154-0.18140.23760.5979-1.2001-1.38-0.56650.96430.24450.27880.80880.21430.7685-61.669276.5386-13.2612
32.26650.0949-0.31144.5958-1.38675.81010.1550.45850.5163-0.19440.50210.6917-1.3723-0.9691-0.60.9180.22150.21260.89860.2310.8061-63.092375.6493-14.7998
43.29070.41190.39624.7505-2.14887.61510.00660.27480.1581-0.2129-0.0106-0.17330.0840.29070.02120.29360.01910.03450.3515-0.03660.3006-49.753840.3831-6.5177
51.30190.2588-0.61560.37650.46441.40.2499-0.00820.47640.260.18470.0609-1.02220.0673-0.38560.7111-0.05520.13810.3998-0.00520.5111-50.597562.2723-9.566
63.59390.3747-0.68429.07291.79356.23760.4834-0.22630.66661.1110.53430.2115-1.14890.3865-0.86080.8128-0.18240.22990.6219-0.04080.6912-46.785670.5925-15.2492
71.3970.26750.65222.5154-0.73450.54730.480.05941.50660.03130.6057-0.6882-1.91560.7579-0.57271.5389-0.40960.47610.6784-0.0741.3038-43.457180.5537-17.2175
86.14820.6877-1.55313.1036-0.36622.5170.49012.2589-0.7806-0.0464-0.0258-0.8059-0.23620.565-0.45940.6150.2324-0.03281.2289-0.280.8857-17.673622.89695.3579
96.67321.4175-1.75650.79290.44312.5-0.30.5341-1.22840.17020.2487-0.41640.49140.31220.12260.71920.1308-0.09290.4382-0.08590.6194-41.931518.660812.9592
102.48260.6113-2.56622.3324-0.43953.16910.10480.22590.02580.39920.03870.1890.5301-0.3565-0.15990.6801-0.0330.00350.44010.00620.3452-65.816524.87520.0299
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'H' and (resid 20 through 141 )H20 - 141
2X-RAY DIFFRACTION2chain 'H' and (resid 142 through 179 )H142 - 179
3X-RAY DIFFRACTION3chain 'H' and (resid 180 through 235 )H180 - 235
4X-RAY DIFFRACTION4chain 'L' and (resid 20 through 109 )L20 - 109
5X-RAY DIFFRACTION5chain 'L' and (resid 110 through 147 )L110 - 147
6X-RAY DIFFRACTION6chain 'L' and (resid 148 through 193 )L148 - 193
7X-RAY DIFFRACTION7chain 'L' and (resid 194 through 229 )L194 - 229
8X-RAY DIFFRACTION8chain 'C' and (resid 102 through 173 )C102 - 173
9X-RAY DIFFRACTION9chain 'C' and (resid 174 through 247 )C174 - 247
10X-RAY DIFFRACTION10chain 'C' and (resid 248 through 314 )C248 - 314

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