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- PDB-3pfv: Crystal structure of Cbl-b TKB domain in complex with EGFR pY1069... -

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Basic information

Entry
Database: PDB / ID: 3pfv
TitleCrystal structure of Cbl-b TKB domain in complex with EGFR pY1069 peptide
Components
  • 11-meric peptide from Epidermal growth factor receptor
  • E3 ubiquitin-protein ligase CBL-B
KeywordsLIGASE/PROTEIN BINDING / Structural Genomics / Structural Genomics Consortium / SGC / Signal transduction protein / CBL-B / SH3-binding protein / LIGASE-PROTEIN BINDING complex
Function / homology
Function and homology information


regulation of platelet-derived growth factor receptor-alpha signaling pathway / T cell anergy / positive regulation of T cell anergy / CD4-positive, alpha-beta T cell proliferation / negative regulation of CD4-positive, alpha-beta T cell proliferation / response to hydroxyisoflavone / multivesicular body, internal vesicle lumen / positive regulation of prolactin secretion / negative regulation of cardiocyte differentiation / positive regulation of protein kinase C activity ...regulation of platelet-derived growth factor receptor-alpha signaling pathway / T cell anergy / positive regulation of T cell anergy / CD4-positive, alpha-beta T cell proliferation / negative regulation of CD4-positive, alpha-beta T cell proliferation / response to hydroxyisoflavone / multivesicular body, internal vesicle lumen / positive regulation of prolactin secretion / negative regulation of cardiocyte differentiation / positive regulation of protein kinase C activity / diterpenoid metabolic process / Shc-EGFR complex / ovulation cycle / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / positive regulation of mucus secretion / response to UV-A / epidermal growth factor binding / PLCG1 events in ERBB2 signaling / tongue development / negative regulation of T cell receptor signaling pathway / midgut development / ERBB2-EGFR signaling pathway / hydrogen peroxide metabolic process / PTK6 promotes HIF1A stabilization / digestive tract morphogenesis / regulation of nitric-oxide synthase activity / morphogenesis of an epithelial fold / ERBB2 Activates PTK6 Signaling / NLS-bearing protein import into nucleus / intracellular vesicle / Signaling by EGFR / response to cobalamin / transmembrane receptor protein tyrosine kinase activator activity / protein tyrosine kinase activator activity / negative regulation of epidermal growth factor receptor signaling pathway / Signaling by ERBB4 / regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / eyelid development in camera-type eye / protein insertion into membrane / cerebral cortex cell migration / ERBB2 Regulates Cell Motility / regulation of JNK cascade / : / PI3K events in ERBB2 signaling / positive regulation of cyclin-dependent protein serine/threonine kinase activity / negative regulation of mitotic cell cycle / hair follicle development / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / MAP kinase kinase kinase activity / embryonic placenta development / positive regulation of bone resorption / positive regulation of G1/S transition of mitotic cell cycle / GAB1 signalosome / positive regulation of nitric oxide mediated signal transduction / salivary gland morphogenesis / peptidyl-tyrosine autophosphorylation / regulation of peptidyl-tyrosine phosphorylation / positive regulation of phosphorylation / positive regulation of glial cell proliferation / positive regulation of vasoconstriction / Signaling by ERBB2 / cellular response to epidermal growth factor stimulus / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / cellular response to cadmium ion / positive regulation of DNA repair / EGFR Transactivation by Gastrin / GRB2 events in ERBB2 signaling / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / phosphotyrosine residue binding / transmembrane receptor protein tyrosine kinase activity / SHC1 events in ERBB2 signaling / positive regulation of synaptic transmission, glutamatergic / ossification / cellular response to dexamethasone stimulus / basal plasma membrane / neurogenesis / regulation of ERK1 and ERK2 cascade / neuron projection morphogenesis / positive regulation of superoxide anion generation / epithelial cell proliferation / positive regulation of DNA replication / positive regulation of protein ubiquitination / Signal transduction by L1 / cell surface receptor protein tyrosine kinase signaling pathway / cellular response to estradiol stimulus / NOTCH3 Activation and Transmission of Signal to the Nucleus / positive regulation of epithelial cell proliferation / astrocyte activation / liver regeneration / positive regulation of protein localization to plasma membrane / EGFR downregulation / cellular response to amino acid stimulus / positive regulation of smooth muscle cell proliferation / Signaling by ERBB2 TMD/JMD mutants / positive regulation of MAP kinase activity / lung development / clathrin-coated endocytic vesicle membrane
Similarity search - Function
E3 ubiquitin-protein ligase CBL-B, RING finger, HC subclass / 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 ...E3 ubiquitin-protein ligase CBL-B, RING finger, HC subclass / 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 / Ubiquitin associated domain / Zinc finger, C3HC4 RING-type / Zinc finger, C3HC4 type (RING finger) / Ubiquitin-associated domain / Ubiquitin-associated domain (UBA) profile. / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / SH2 domain / SHC Adaptor Protein / 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 / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Recoverin; domain 1 / Ring finger / Growth factor receptor cysteine-rich domain superfamily / Zinc finger RING-type profile. / Zinc finger, RING-type / SH2 domain superfamily / 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
Epidermal growth factor receptor / E3 ubiquitin-protein ligase CBL-B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.27 Å
AuthorsChaikuad, A. / Guo, K. / Cooper, C.D.O. / Ayinampudi, V. / Krojer, T. / Muniz, J.R.C. / Vollmar, M. / Canning, P. / Gileadi, O. / von Delft, F. ...Chaikuad, A. / Guo, K. / Cooper, C.D.O. / Ayinampudi, V. / Krojer, T. / Muniz, J.R.C. / Vollmar, M. / Canning, P. / Gileadi, O. / 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-b TKB domain in complex with EGFR pY1069 peptide
Authors: Chaikuad, A. / Guo, K. / Cooper, C.D.O. / Ayinampudi, V. / Krojer, T. / Muniz, J.R.C. / Vollmar, M. / Canning, P. / Gileadi, O. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A. ...Authors: Chaikuad, A. / Guo, K. / Cooper, C.D.O. / Ayinampudi, V. / Krojer, T. / Muniz, J.R.C. / Vollmar, M. / Canning, P. / Gileadi, O. / von Delft, F. / Arrowsmith, C.H. / Weigelt, J. / Edwards, A.M. / Bountra, C. / Bullock, A. / Structural Genomics Consortium (SGC)
History
DepositionOct 29, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Apr 2, 2014Group: Source and taxonomy
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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: E3 ubiquitin-protein ligase CBL-B
B: E3 ubiquitin-protein ligase CBL-B
C: 11-meric peptide from Epidermal growth factor receptor
D: 11-meric peptide from Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,58319
Polymers76,4134
Non-polymers1,17015
Water3,963220
1
A: E3 ubiquitin-protein ligase CBL-B
C: 11-meric peptide from Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,87112
Polymers38,2072
Non-polymers66410
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2140 Å2
ΔGint-73 kcal/mol
Surface area15570 Å2
MethodPISA
2
B: E3 ubiquitin-protein ligase CBL-B
D: 11-meric peptide from Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,7127
Polymers38,2072
Non-polymers5055
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2520 Å2
ΔGint-61 kcal/mol
Surface area15740 Å2
MethodPISA
Unit cell
Length a, b, c (Å)60.063, 98.934, 61.978
Angle α, β, γ (deg.)90.00, 110.63, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12C
22D
13B
23A

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
111THRTHRASNASN4AA49 - 6213 - 26
211THRTHRASNASN4BB49 - 6213 - 26
121ASNASNLYSLYS3AA69 - 9133 - 55
221ASNASNLYSLYS3BB69 - 9133 - 55
131ALAALAILEILE4AA99 - 12263 - 86
231ALAALAILEILE4BB99 - 12263 - 86
141SERSERGLYGLY3AA137 - 164101 - 128
241SERSERGLYGLY3BB137 - 164101 - 128
112ARGARGTHRTHR4CC1068 - 10743 - 9
212ARGARGTHRTHR4DD1068 - 10743 - 9
113THRTHRPROPRO3BB174 - 311138 - 275
213THRTHRPROPRO3AA174 - 311138 - 275

NCS ensembles :
ID
1
2
3

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Components

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Protein / Protein/peptide , 2 types, 4 molecules ABCD

#1: Protein E3 ubiquitin-protein ligase CBL-B / Casitas B-lineage lymphoma proto-oncogene b / RING finger protein 56 / SH3-binding protein CBL-B / ...Casitas B-lineage lymphoma proto-oncogene b / RING finger protein 56 / SH3-binding protein CBL-B / Signal transduction protein CBL-B


Mass: 36931.402 Da / Num. of mol.: 2 / Fragment: N-terminal TKB domain (UNP residues 38-344)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CBLB, Nbla00127, RNF56 / Plasmid: pNIC-CTHF / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)-R3-pRARE2
References: UniProt: Q13191, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)
#2: Protein/peptide 11-meric peptide from Epidermal growth factor receptor / Proto-oncogene c-ErbB-1 / Receptor tyrosine-protein kinase erbB-1


Mass: 1275.240 Da / Num. of mol.: 2 / Fragment: UNP residues 1066-1076 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P00533

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Non-polymers , 6 types, 235 molecules

#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#5: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: SO4
#6: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 220 / Source method: isolated from a natural source / Formula: H2O

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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: 2.26 Å3/Da / Density % sol: 45.46 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 30% PEG 3350, 0.3M Ammonium sulfate, 0.1M Bis-Tris, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.15K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 6, 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: 0.9763 Å / Relative weight: 1
ReflectionResolution: 2.27→49.47 Å / Num. all: 30233 / Num. obs: 30186 / % possible obs: 96.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 43.2 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 8
Reflection shellResolution: 2.27→2.39 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.604 / Mean I/σ(I) obs: 2.1 / Num. unique all: 4455 / % possible all: 96.6

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Processing

Software
NameVersionClassification
GDAdata collection
PHASERphasing
REFMAC5.5.0110refinement
XDSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ID 3BUO

3buo


Resolution: 2.27→49.47 Å / Cor.coef. Fo:Fc: 0.938 / Cor.coef. Fo:Fc free: 0.909 / SU B: 15.54 / SU ML: 0.194 / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 2 / ESU R Free: 0.267 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.26201 1524 5 %RANDOM
Rwork0.21624 ---
obs0.21861 28661 96.09 %-
all-30186 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 40.207 Å2
Baniso -1Baniso -2Baniso -3
1--0.44 Å20 Å2-0.81 Å2
2--0.54 Å20 Å2
3----0.67 Å2
Refine analyzeLuzzati coordinate error obs: 0.319 Å
Refinement stepCycle: LAST / Resolution: 2.27→49.47 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5104 0 64 220 5388
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONr_bond_refined_d0.015
X-RAY DIFFRACTIONr_bond_other_d0.005
X-RAY DIFFRACTIONr_angle_refined_deg1.567
X-RAY DIFFRACTIONr_angle_other_deg1.198
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.499
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.703
X-RAY DIFFRACTIONr_dihedral_angle_3_deg15.268
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.486
X-RAY DIFFRACTIONr_chiral_restr0.079
X-RAY DIFFRACTIONr_gen_planes_refined0.008
X-RAY DIFFRACTIONr_gen_planes_other0.004
X-RAY DIFFRACTIONr_mcbond_it2.76
X-RAY DIFFRACTIONr_mcbond_other0.74
X-RAY DIFFRACTIONr_mcangle_it4.514
X-RAY DIFFRACTIONr_scbond_it7.11
X-RAY DIFFRACTIONr_scangle_it8.946
Refine LS restraints NCS

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

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A299TIGHT POSITIONAL0.030.05
1A511MEDIUM POSITIONAL0.030.5
1A386LOOSE POSITIONAL0.115
1A299TIGHT THERMAL0.150.5
1A511MEDIUM THERMAL0.12
1A386LOOSE THERMAL0.1110
2C104MEDIUM POSITIONAL0.570.5
2C104MEDIUM THERMAL0.762
3B812TIGHT POSITIONAL0.040.05
3B1070LOOSE POSITIONAL0.135
3B812TIGHT THERMAL0.190.5
3B1070LOOSE THERMAL0.1310
LS refinement shellResolution: 2.27→2.329 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.343 113 -
Rwork0.272 2150 -
obs--96.18 %
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)
18.02112.70761.240829.58461.26688.12180.43010.3745-0.0562.1306-0.0446-1.70450.46812.6193-0.38550.27520.1523-0.30391.0294-0.2040.416335.233616.065628.6796
21.3793-0.20712.41792.65870.46994.5096-0.18110.1647-0.00830.19590.4411-0.5751-0.23340.4189-0.260.2252-0.0302-0.18310.3795-0.03490.578725.714424.366529.108
36.8701-3.30185.84927.0827-2.71275.00470.1213-0.0266-0.28750.14980.0290.02910.0690.001-0.15030.26720.1787-0.09210.44150.06990.279628.1050.060335.6667
44.83124.4708-1.501918.2633-7.19236.3398-0.24430.3296-0.03370.39230.3284-1.35230.30840.8337-0.08410.16150.1429-0.16090.6945-0.08750.404231.953913.451219.6091
50.84251.3983-1.96466.4135-5.4397.69780.06080.06730.2550.76220.144-0.4641-0.63130.5006-0.20480.263-0.0455-0.12970.42120.00250.418823.759719.274921.1047
61.16730.0410.57980.7760.15013.29220.0301-0.0936-0.09660.17210.01770.1240.4721-0.0401-0.04780.3801-0.00830.0030.29270.04340.24889.72411.111419.1672
71.5848-0.4443-0.01132.4736-0.17620.7058-0.099-0.05020.04870.14380.02670.1431-0.04-0.07650.07230.28680.0404-0.01440.30010.01690.25942.224423.657516.7899
82.98940.63460.896712.9056-0.29030.2942-0.1610.4127-1.04270.46730.4054-1.7423-0.06780.1867-0.24440.0287-0.0077-0.00230.8491-0.09550.554343.24956.46150.3587
91.3165-0.61951.21786.88491.52041.79530.11430.64770.1415-0.76320.1181-0.9972-0.07330.7943-0.23250.1448-0.11660.16220.8078-0.04880.691544.210613.6551-9.5044
101.39761.958-1.170410.9598-5.284.6885-0.0449-0.35020.05910.21570.171-0.6692-0.08870.5913-0.12610.1237-0.0768-0.10650.4564-0.06410.456736.545510.01964.076
110.7088-0.34040.00491.7562-0.97852.52860.0479-0.03810.07-0.12530.1206-0.4481-0.11450.4604-0.16850.2262-0.1090.01460.4229-0.01440.438332.749312.9319-8.2098
121.12020.0143-0.60681.9849-0.1151.57790.05310.03170.1325-0.16420.0607-0.0621-0.32980.0303-0.11380.3078-0.0460.00990.31450.00920.268216.69218.5387-6.7589
131.61941.0357-0.22392.76870.41251.3441-0.04850.1753-0.1317-0.26690.1357-0.22130.02540.1219-0.08720.2804-0.03010.01040.3163-0.02770.290316.4815-3.2456-12.2585
142.2699-0.70521.57754.0778-1.39582.081-0.19470.11720.1205-0.19530.13310.2134-0.0019-0.2110.06160.26-0.062-0.05990.38570.00680.28693.64030.253-12.5775
153.6699-2.17610.83776.5608-5.01324.101-0.3482-0.01050.14660.9210.192-0.1649-0.597-0.24020.15620.4513-0.00230.02640.504-0.16340.27451.430926.975628.145
164.2286-2.673-6.38596.8082-1.063514.83230.1015-0.44920.0895-0.83960.2259-0.00240.43390.9632-0.32750.4284-0.2330.15630.7302-0.18550.316420.5654-4.574-19.8928
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A45 - 61
2X-RAY DIFFRACTION2A62 - 82
3X-RAY DIFFRACTION3A83 - 109
4X-RAY DIFFRACTION4A110 - 128
5X-RAY DIFFRACTION5A129 - 161
6X-RAY DIFFRACTION6A162 - 250
7X-RAY DIFFRACTION7A251 - 345
8X-RAY DIFFRACTION8B40 - 71
9X-RAY DIFFRACTION9B72 - 97
10X-RAY DIFFRACTION10B98 - 138
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13X-RAY DIFFRACTION13B265 - 323
14X-RAY DIFFRACTION14B324 - 349
15X-RAY DIFFRACTION15C1066 - 1075
16X-RAY DIFFRACTION16D1066 - 1075

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