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- PDB-3op0: Crystal structure of Cbl-c (Cbl-3) TKB domain in complex with EGF... -

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Basic information

Entry
Database: PDB / ID: 3op0
TitleCrystal structure of Cbl-c (Cbl-3) TKB domain in complex with EGFR pY1069 peptide
Components
  • Epidermal growth factor receptor
  • Signal transduction protein CBL-C
KeywordsSIGNALING PROTEIN/SIGNALING PROTEIN REGULATOR / Structural Genomics / Structural Genomics Consortium / SGC / Signal transduction protein / SH3-binding protein / SIGNALING PROTEIN-SIGNALING PROTEIN REGULATOR complex
Function / homology
Function and homology information


response to glial cell derived neurotrophic factor / multivesicular body, internal vesicle lumen / negative regulation of cardiocyte differentiation / Shc-EGFR complex / morphogenesis of an epithelial fold / positive regulation of protein kinase C signaling / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / epidermal growth factor binding ...response to glial cell derived neurotrophic factor / multivesicular body, internal vesicle lumen / negative regulation of cardiocyte differentiation / Shc-EGFR complex / morphogenesis of an epithelial fold / positive regulation of protein kinase C signaling / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / epidermal growth factor binding / epidermal growth factor receptor binding / response to UV-A / regulation of peptidyl-tyrosine phosphorylation / ubiquitin-dependent endocytosis / PLCG1 events in ERBB2 signaling / digestive tract morphogenesis / ERBB2-EGFR signaling pathway / PTK6 promotes HIF1A stabilization / eyelid development in camera-type eye / ERBB2 Activates PTK6 Signaling / Signaling by EGFR / intracellular vesicle / cerebral cortex cell migration / hair follicle development / ERBB2 Regulates Cell Motility / Developmental Lineage of Mammary Gland Myoepithelial Cells / protein insertion into membrane / protein tyrosine kinase activator activity / Signaling by ERBB4 / Respiratory syncytial virus (RSV) attachment and entry / embryonic placenta development / negative regulation of epidermal growth factor receptor signaling pathway / PI3K events in ERBB2 signaling / positive regulation of phosphorylation / positive regulation of peptidyl-serine phosphorylation / MAP kinase kinase kinase activity / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / GAB1 signalosome / salivary gland morphogenesis / xenobiotic transport / positive regulation of G1/S transition of mitotic cell cycle / positive regulation of epidermal growth factor receptor signaling pathway / epithelial cell proliferation / negative regulation of MAPK cascade / Signaling by ERBB2 / phosphotyrosine residue binding / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / transmembrane receptor protein tyrosine kinase activity / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / EGFR Transactivation by Gastrin / positive regulation of epithelial cell proliferation / GRB2 events in ERBB2 signaling / SHC1 events in ERBB2 signaling / ossification / cellular response to epidermal growth factor stimulus / basal plasma membrane / positive regulation of DNA replication / positive regulation of DNA repair / Signal transduction by L1 / positive regulation of protein localization to plasma membrane / cellular response to amino acid stimulus / cellular response to estradiol stimulus / phosphatidylinositol 3-kinase/protein kinase B signal transduction / sperm end piece / NOTCH3 Activation and Transmission of Signal to the Nucleus / clathrin-coated endocytic vesicle membrane / sperm principal piece / Signaling by ERBB2 TMD/JMD mutants / cell-cell adhesion / EGFR downregulation / Constitutive Signaling by EGFRvIII / receptor protein-tyrosine kinase / negative regulation of protein catabolic process / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / SH3 domain binding / positive regulation of protein phosphorylation / receptor tyrosine kinase binding / RING-type E3 ubiquitin transferase / positive regulation of miRNA transcription / cell morphogenesis / positive regulation of fibroblast proliferation / epidermal growth factor receptor signaling pathway / ruffle membrane / kinase binding / Downregulation of ERBB2 signaling / neuron differentiation / Constitutive Signaling by Aberrant PI3K in Cancer / HCMV Early Events / cell junction / positive regulation of canonical Wnt signaling pathway / actin filament binding / ubiquitin protein ligase activity / transmembrane signaling receptor activity / PIP3 activates AKT signaling / Cargo recognition for clathrin-mediated endocytosis / sperm midpiece / Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants / Clathrin-mediated endocytosis
Similarity search - Function
Adaptor protein Cbl, N-terminal domain / Adaptor protein Cbl, N-terminal helical / Adaptor protein Cbl, EF hand-like / Adaptor protein Cbl, SH2-like domain / Adaptor protein Cbl, PTB domain / Adaptor protein Cbl / CBL proto-oncogene N-terminal domain 1 / CBL proto-oncogene N-terminus, EF hand-like domain / CBL proto-oncogene N-terminus, SH2-like domain / Cbl-type phosphotyrosine-binding (Cbl-PTB) domain profile. ...Adaptor protein Cbl, N-terminal domain / Adaptor protein Cbl, N-terminal helical / Adaptor protein Cbl, EF hand-like / Adaptor protein Cbl, SH2-like domain / Adaptor protein Cbl, PTB domain / Adaptor protein Cbl / CBL proto-oncogene N-terminal domain 1 / CBL proto-oncogene N-terminus, EF hand-like domain / CBL proto-oncogene N-terminus, SH2-like domain / Cbl-type phosphotyrosine-binding (Cbl-PTB) domain profile. / Adaptor protein Cbl, N-terminal domain superfamily / Transcription Elongation Factor S-II; Chain A / SH2 domain / SHC Adaptor Protein / Zinc finger, C3HC4 type (RING finger) / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / 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 / EF-hand / Recoverin; domain 1 / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Growth factor receptor cysteine-rich domain superfamily / Ring finger / : / SH2 domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / EF-hand domain pair / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Zinc finger, RING/FYVE/PHD-type / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Up-down Bundle / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
NICKEL (II) ION / Epidermal growth factor receptor / E3 ubiquitin-protein ligase CBL-C
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.52 Å
AuthorsChaikuad, A. / Guo, K. / Cooper, C.D.O. / Ayinampudi, V. / Krojer, T. / Ugochukwu, E. / Muniz, J.R.C. / Vollmar, M. / Canning, P. / von Delft, F. ...Chaikuad, A. / Guo, K. / Cooper, C.D.O. / Ayinampudi, V. / Krojer, T. / Ugochukwu, E. / Muniz, J.R.C. / Vollmar, M. / Canning, P. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A.M. / Bountra, C. / Bullock, A. / Structural Genomics Consortium (SGC)
CitationJournal: To be Published
Title: Crystal structure of Cbl-c (Cbl-3) TKB domain in complex with EGFR pY1069 peptide
Authors: Chaikuad, A. / Guo, K. / Cooper, C.D.O. / Ayinampudi, V. / Krojer, T. / Ugochukwu, E. / Muniz, J.R.C. / Vollmar, M. / Canning, P. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, ...Authors: Chaikuad, A. / Guo, K. / Cooper, C.D.O. / Ayinampudi, V. / Krojer, T. / Ugochukwu, E. / Muniz, J.R.C. / Vollmar, M. / Canning, P. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A.M. / Bountra, C. / Bullock, A.
History
DepositionAug 31, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 20, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software
Revision 1.3Sep 6, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_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_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Dec 6, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.5Nov 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: Signal transduction protein CBL-C
B: Signal transduction protein CBL-C
C: Epidermal growth factor receptor
D: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,0848
Polymers74,9214
Non-polymers1634
Water5,080282
1
A: Signal transduction protein CBL-C
C: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,5424
Polymers37,4612
Non-polymers822
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1340 Å2
ΔGint-23 kcal/mol
Surface area15470 Å2
MethodPISA
2
B: Signal transduction protein CBL-C
D: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,5424
Polymers37,4612
Non-polymers822
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1340 Å2
ΔGint-25 kcal/mol
Surface area15440 Å2
MethodPISA
3


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4450 Å2
ΔGint-61 kcal/mol
Surface area29140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)90.250, 90.250, 191.581
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number170
Space group name H-MP65
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails (eV)
11A
21B
12C
22D

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLNGLNCYSCYS1AA11 - 324 - 25
211GLNGLNCYSCYS1BB11 - 324 - 25
121CYSCYSSERSER1AA32 - 4025 - 33
221CYSCYSSERSER1BB32 - 4025 - 33
131PROPROARGARG1AA41 - 6334 - 56
231PROPROARGARG1BB41 - 6334 - 56
141GLUGLUPROPRO4AA64 - 7057 - 63
241GLUGLUPROPRO4BB64 - 7057 - 63
151GLYGLYPROPRO1AA71 - 9964 - 92
251GLYGLYPROPRO1BB71 - 9964 - 92
161PHEPHEGLNGLN1AA111 - 330104 - 323
261PHEPHEGLNGLN1BB111 - 330104 - 323
171PROPROLEULEU1AA100 - 11093 - 103
271PROPROLEULEU1BB100 - 11093 - 103
112LEULEUARGARG1CC1066 - 10681 - 3
212LEULEUARGARG1DD1066 - 10681 - 3
122SERSERGLYGLY1CC1070 - 10755 - 10
222SERSERGLYGLY1DD1070 - 10755 - 10

NCS ensembles :
ID
1
2

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Components

#1: Protein Signal transduction protein CBL-C / SH3-binding protein CBL-C / SH3-binding protein CBL-3 / RING finger protein 57


Mass: 36185.320 Da / Num. of mol.: 2 / Fragment: CBL N-terminal, UNP residues 9-323 / Mutation: A64E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CBL3, CBLC, RNF57 / Plasmid: pNIC-CTHF / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-R3-pRARE2 / References: UniProt: Q9ULV8
#2: Protein/peptide Epidermal growth factor receptor / Receptor tyrosine-protein kinase erbB-1 / Proto-oncogene c-ErbB-1


Mass: 1275.240 Da / Num. of mol.: 2 / Fragment: EGFR, UNP residues 1066-1076 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P00533
#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#4: Chemical ChemComp-NI / NICKEL (II) ION


Mass: 58.693 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ni
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 282 / Source method: isolated from a natural source / Formula: H2O
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: 3.01 Å3/Da / Density % sol: 59.08 %
Crystal growTemperature: 277.15 K / pH: 7.5
Details: 20% Jeffamine M-600, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 277.15K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795
DetectorType: ADSC Q315 3X3 CCD / Detector: CCD / Date: May 26, 2010 / Details: KIRKPATRICK BAEZ BIMORPH MIRROR PAIR
RadiationMonochromator: SI (111) DOUBLE CRYSTAL MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.52→49.45 Å / Num. obs: 29742 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 5.7 % / Biso Wilson estimate: 49 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 9.1
Reflection shellResolution: 2.52→2.66 Å / Redundancy: 5.6 % / Rmerge(I) obs: 0.745 / Mean I/σ(I) obs: 2 / % possible all: 100

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Processing

Software
NameVersionClassification
PHASERphasing
REFMAC5.5.0109refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ID: 1FBV CHAIN A

1fbv


Resolution: 2.52→49.45 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.902 / SU B: 19.618 / SU ML: 0.238 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.301 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.266 1505 5.1 %RANDOM
Rwork0.214 ---
all0.255 29663 --
obs0.216 28157 99.7 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 35.9 Å2
Baniso -1Baniso -2Baniso -3
1-2.68 Å21.34 Å20 Å2
2--2.68 Å20 Å2
3----4.03 Å2
Refine analyzeLuzzati coordinate error obs: 0.253 Å
Refinement stepCycle: LAST / Resolution: 2.52→49.45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5163 0 4 282 5449
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0140.0215358
X-RAY DIFFRACTIONr_bond_other_d0.0020.023708
X-RAY DIFFRACTIONr_angle_refined_deg1.5431.9727260
X-RAY DIFFRACTIONr_angle_other_deg1.1738949
X-RAY DIFFRACTIONr_dihedral_angle_1_deg14.7085.118678
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.3322.571245
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.61515831
X-RAY DIFFRACTIONr_dihedral_angle_4_deg18.521550
X-RAY DIFFRACTIONr_chiral_restr0.0720.2774
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0216008
X-RAY DIFFRACTIONr_gen_planes_other0.0020.021146
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.321.53316
X-RAY DIFFRACTIONr_mcbond_other0.11.51338
X-RAY DIFFRACTIONr_mcangle_it0.54625285
X-RAY DIFFRACTIONr_scbond_it1.16232042
X-RAY DIFFRACTIONr_scangle_it1.5734.51969
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A4251TIGHT POSITIONAL0.040.05
1A64MEDIUM POSITIONAL0.010.5
1A4251TIGHT THERMAL0.040.5
1A64MEDIUM THERMAL0.022
2C114TIGHT POSITIONAL0.010.05
2C114TIGHT THERMAL0.020.5
LS refinement shellResolution: 2.52→2.58 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.327 99 -
Rwork0.337 2084 -
obs--99.95 %
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)
17.6107-3.25772.95387.8327-3.17277.5313-0.12950.2645-0.75760.307-0.0682-0.69660.28420.35170.19770.20770.0242-0.00960.2078-0.0450.24579.647240.35343.7005
26.18488.62462.811914.51146.46243.9505-0.5123-0.31980.8656-1.85880.15760.9235-1.43320.36410.35470.8477-0.0141-0.15470.4649-0.07520.65212.264960.207335.1401
33.1022-0.2586-0.34866.12570.81438.63820.0691-0.1628-0.24230.4461-0.0064-0.03110.37960.0071-0.06270.0549-0.0078-0.0310.1439-0.01110.07521.325941.6340
40.2976-1.9435-0.520723.57182.32271.0320.2361-0.06640.34211.6670.139-4.147-0.7490.0654-0.37511.16120.0186-0.32721.0044-0.06360.84998.596263.020928.2185
52.4219-0.42670.55871.17890.77351.65840.00970.0657-0.0673-0.0226-0.01610.120.0562-0.17450.00640.1409-0.03750.01990.1787-0.00360.0328-9.925438.665525.5468
63.8586-0.38671.47083.9917-0.04493.0189-0.04070.270.4659-0.336-0.17590.1039-0.5571-0.08330.21660.25860.0696-0.02230.2188-0.01880.1776-16.406857.076521.6195
71.27663.19671.31198.85213.35761.5613-0.0921-0.14190.4530.0377-0.21720.8403-0.1845-0.28310.30920.3110.0926-0.05970.4222-0.03440.3478-26.915250.647517.3411
86.63851.58730.25515.00922.86565.754-0.2588-0.1336-0.6972-0.10780.0840.5780.4538-0.32340.17480.229-0.0176-0.02440.21250.05040.2097-9.659140.3668-12.509
93.3329-6.10013.804811.702-7.42154.7463-0.650.30610.66671.79520.0238-0.8849-1.2553-0.11080.62621.01440.2571-0.01860.68640.1770.6424-2.263560.2289-3.9535
102.9642-0.2321-0.44926.34790.1028.81950.03050.3306-0.25-0.3463-0.01230.11410.4361-0.1821-0.01820.0477-0.0054-0.02990.1689-0.00270.0869-1.333341.6366-8.8054
117.77342.0996-5.78310.5925-1.56234.30310.97831.08932.14490.03590.43330.725-0.581-0.8157-1.41161.64720.1153-0.70870.65970.01681.4831-8.565363.00692.8742
122.29940.33490.42771.2705-0.61111.8539-0.014-0.0415-0.07520.0566-0.0056-0.07920.06090.18690.01960.13680.030.01180.16760.00720.0419.92938.66675.6403
134.00330.67581.87534.31360.31442.8503-0.1015-0.24710.44930.2981-0.1094-0.1578-0.67450.12890.21090.301-0.0611-0.02950.21660.02290.160516.412957.08189.5686
141.395-3.47671.72828.749-4.3362.293-0.0570.14740.39730.0365-0.2446-0.8821-0.14650.32080.30160.3815-0.1609-0.02680.53590.0070.407826.923350.649713.8417
1551.01782.7342.88313.1312-1.352111.9261-0.5356-0.24052.32951.05930.06681.7128-1.1709-1.09990.46880.6510.2070.08740.4392-0.1150.3984-23.931158.705229.8097
1637.62892.6199-0.77117.53739.38112.1629-0.26620.07070.7599-1.39920.9606-0.601-1.67221.2242-0.69440.619-0.18210.20890.60310.2140.6924.068958.53151.445
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A10 - 26
2X-RAY DIFFRACTION2A27 - 42
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