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- PDB-1s78: Insights into ErbB signaling from the structure of the ErbB2-pert... -

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Basic information

Entry
Database: PDB / ID: 1s78
TitleInsights into ErbB signaling from the structure of the ErbB2-pertuzumab complex
Components
  • (Pertuzumab Fab ...) x 2
  • Receptor protein-tyrosine kinase erbB-2
KeywordsTRANSFERASE / receptor-antibody complex / Fab fragment / cysteine-rich domain / leucine-rich repeat
Function / homology
Function and homology information


negative regulation of immature T cell proliferation in thymus / ERBB3:ERBB2 complex / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / immature T cell proliferation in thymus / RNA polymerase I core binding / semaphorin receptor complex / regulation of microtubule-based process / ErbB-3 class receptor binding / motor neuron axon guidance ...negative regulation of immature T cell proliferation in thymus / ERBB3:ERBB2 complex / ERBB2-ERBB4 signaling pathway / GRB7 events in ERBB2 signaling / immature T cell proliferation in thymus / RNA polymerase I core binding / semaphorin receptor complex / regulation of microtubule-based process / ErbB-3 class receptor binding / motor neuron axon guidance / Sema4D induced cell migration and growth-cone collapse / PLCG1 events in ERBB2 signaling / ERBB2-EGFR signaling pathway / neurotransmitter receptor localization to postsynaptic specialization membrane / ERBB2 Activates PTK6 Signaling / neuromuscular junction development / enzyme-linked receptor protein signaling pathway / ERBB2-ERBB3 signaling pathway / positive regulation of Rho protein signal transduction / Drug-mediated inhibition of ERBB2 signaling / Resistance of ERBB2 KD mutants to trastuzumab / Resistance of ERBB2 KD mutants to sapitinib / Resistance of ERBB2 KD mutants to tesevatinib / Resistance of ERBB2 KD mutants to neratinib / Resistance of ERBB2 KD mutants to osimertinib / Resistance of ERBB2 KD mutants to afatinib / Resistance of ERBB2 KD mutants to AEE788 / Resistance of ERBB2 KD mutants to lapatinib / Drug resistance in ERBB2 TMD/JMD mutants / positive regulation of transcription by RNA polymerase I / ERBB2 Regulates Cell Motility / oligodendrocyte differentiation / semaphorin-plexin signaling pathway / PI3K events in ERBB2 signaling / positive regulation of protein targeting to membrane / regulation of angiogenesis / positive regulation of MAP kinase activity / regulation of ERK1 and ERK2 cascade / Schwann cell development / coreceptor activity / Signaling by ERBB2 / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / transmembrane receptor protein tyrosine kinase activity / myelination / GRB2 events in ERBB2 signaling / positive regulation of cell adhesion / SHC1 events in ERBB2 signaling / Downregulation of ERBB2:ERBB3 signaling / basal plasma membrane / cell surface receptor protein tyrosine kinase signaling pathway / Constitutive Signaling by Overexpressed ERBB2 / cellular response to epidermal growth factor stimulus / positive regulation of epithelial cell proliferation / positive regulation of translation / phosphatidylinositol 3-kinase/protein kinase B signal transduction / wound healing / peptidyl-tyrosine phosphorylation / Signaling by ERBB2 TMD/JMD mutants / receptor protein-tyrosine kinase / Signaling by ERBB2 ECD mutants / neuromuscular junction / Signaling by ERBB2 KD Mutants / receptor tyrosine kinase binding / cellular response to growth factor stimulus / ruffle membrane / Downregulation of ERBB2 signaling / epidermal growth factor receptor signaling pathway / neuron differentiation / Constitutive Signaling by Aberrant PI3K in Cancer / transmembrane signaling receptor activity / PIP3 activates AKT signaling / myelin sheath / presynaptic membrane / heart development / RAF/MAP kinase cascade / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cell growth / protein tyrosine kinase activity / basolateral plasma membrane / early endosome / cell population proliferation / cell surface receptor signaling pathway / receptor complex / positive regulation of MAPK cascade / endosome membrane / intracellular signal transduction / protein phosphorylation / apical plasma membrane / protein heterodimerization activity / signaling receptor binding / negative regulation of apoptotic process / perinuclear region of cytoplasm / signal transduction / extracellular region / nucleoplasm / ATP binding / identical protein binding / nucleus / membrane / plasma membrane
Similarity search - Function
Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Alpha-Beta Horseshoe ...Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / 24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / : / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Alpha-Beta Horseshoe / : / 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 / Growth factor receptor cysteine-rich domain superfamily / : / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Ribbon / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Tyrosine-protein kinase, active site / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Immunoglobulins / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Receptor tyrosine-protein kinase erbB-2 / Ig-like domain-containing protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.25 Å
AuthorsFranklin, M.C. / Carey, K.D. / Vajdos, F.F. / Leahy, D.J. / de Vos, A.M. / Sliwkowski, M.X.
Citation
Journal: Cancer Cell / Year: 2004
Title: Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex.
Authors: Franklin, M.C. / Carey, K.D. / Vajdos, F.F. / Leahy, D.J. / De Vos, A.M. / Sliwkowski, M.X.
#1: Journal: Nature / Year: 2003
Title: Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab
Authors: Cho, H.S. / Mason, K. / Ramyar, K.X. / Stanley, A.M. / Gabelli, S.B. / Denney Jr., D.W. / Leahy, D.J.
#2: Journal: J.Mol.Biol. / Year: 2002
Title: Comprehensive functional maps of the antigen-binding site of an anti-ErbB2 antibody obtained with shotgun scanning mutagenesis
Authors: Vajdos, F.F. / Adams, C.W. / Breece, T.N. / Presta, L.G. / de Vos, A.M. / Sidhu, S.S.
#3: Journal: Cancer Cell / Year: 2002
Title: Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth
Authors: Agus, D.B. / Akita, R.W. / Fox, W.D. / Lewis, G.D. / Higgins, B. / Pisacane, P.I. / Lofgren, J.A. / Tindell, C. / Evans, D.P. / Maiese, K. / Scher, H.I. / Sliwkowski, M.X.
History
DepositionJan 29, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 27, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_chiral / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Aug 23, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 30, 2024Group: Refinement description / Structure summary
Category: pdbx_entry_details / pdbx_modification_feature / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_asym_id / _struct_ncs_dom_lim.beg_auth_comp_id ..._struct_ncs_dom_lim.beg_auth_asym_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_auth_seq_id / _struct_ncs_dom_lim.end_auth_asym_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_auth_seq_id
Remark 999SEQUENCE The sequences of the chains C,E and D,F were not deposited into any sequence database. ...SEQUENCE The sequences of the chains C,E and D,F were not deposited into any sequence database. Residues C110-C214 and D113-D216 lie in a region of very poor electron density and have not been well refined.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Receptor protein-tyrosine kinase erbB-2
B: Receptor protein-tyrosine kinase erbB-2
C: Pertuzumab Fab light chain
D: Pertuzumab Fab heavy chain
E: Pertuzumab Fab light chain
F: Pertuzumab Fab heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)235,72713
Polymers233,0006
Non-polymers2,7277
Water00
1
A: Receptor protein-tyrosine kinase erbB-2
C: Pertuzumab Fab light chain
D: Pertuzumab Fab heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,5706
Polymers116,5003
Non-polymers1,0703
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7480 Å2
ΔGint-19 kcal/mol
Surface area45800 Å2
MethodPISA
2
B: Receptor protein-tyrosine kinase erbB-2
E: Pertuzumab Fab light chain
F: Pertuzumab Fab heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)118,1577
Polymers116,5003
Non-polymers1,6574
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7810 Å2
ΔGint-15 kcal/mol
Surface area46650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)139.412, 139.412, 356.873
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
31A
41B
12A
22B
32A
42B
13A
23B
14A
24B
34A
44B

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
111THRTHRARGARG1AA1 - 1951 - 195
211THRTHRARGARG1BB1 - 1951 - 195
321NAGNAGNAGNAG1GG1
421NAGNAGNAGNAG1JJ1
112THRTHRCYSCYS1AA196 - 320196 - 320
212THRTHRCYSCYS1BB196 - 320196 - 320
322NAGNAGNAGNAG1HH1
422NAGNAGNAGNAG1KK1
113TYRTYRALAALA1AA321 - 488321 - 488
213TYRTYRALAALA1BB321 - 488321 - 488
114CYSCYSALAALA4AA489 - 564489 - 564
214CYSCYSALAALA4BB489 - 564489 - 564
324NAGNAGNAGNAG4II1
424NAGNAGNAGNAG4AL1006

NCS ensembles :
ID
1
2
3
4

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Receptor protein-tyrosine kinase erbB-2 / p185erbB2 / NEU proto-oncogene / C-erbB-2 / Tyrosine kinase-type cell surface receptor HER2 / MLN 19


Mass: 68794.086 Da / Num. of mol.: 2 / Fragment: extracellular domain (residues 23-646)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ERBB2, HER2, NGL, NEU / Organ (production host): ovary / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P04626, EC: 2.7.1.112

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Antibody , 2 types, 4 molecules CEDF

#2: Antibody Pertuzumab Fab light chain


Mass: 23548.152 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: 2C4574 / Production host: Escherichia coli (E. coli) / Strain (production host): 16C9 / References: UniProt: Q7Z3Y4*PLUS
#3: Antibody Pertuzumab Fab heavy chain


Mass: 24158.006 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: 2C4574 / Production host: Escherichia coli (E. coli) / Strain (production host): 16C9

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Sugars , 3 types, 7 molecules

#4: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#6: 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.: 2
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 4 Å3/Da / Density % sol: 69.01 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: PEG 3350, ammonium formate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Nov 19, 2001
RadiationMonochromator: single crystal Si(220) monochromator, cylindrically bent
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.25→30 Å / Num. all: 56393 / Num. obs: 56351 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 8.2 % / Biso Wilson estimate: 97.8 Å2 / Rmerge(I) obs: 0.116 / Rsym value: 0.116 / Net I/σ(I): 19.3
Reflection shellResolution: 3.25→3.37 Å / Redundancy: 8.3 % / Rmerge(I) obs: 0.691 / Mean I/σ(I) obs: 3.3 / Num. unique all: 5496 / Rsym value: 0.691 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: Rat ErbB2 extracellular domain (PDB code 1N8Y) and uncomplexed pertuzumab Fab (PDB code 1L7I)

1n8y

1l7i


Resolution: 3.25→15 Å / Cor.coef. Fo:Fc: 0.909 / Cor.coef. Fo:Fc free: 0.88 / SU B: 22.571 / SU ML: 0.381 / TLS residual ADP flag: LIKELY RESIDUAL / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.479 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.26772 2835 5.1 %SHELLS (A): 3.289 - 3.285, 3.370 - 3.366, 3.459 - 3.454, 3.559 - 3.554, 3.670 - 3.664, 3.798 - 3.791, 3.944 - 3.937, 4.117 - 4.107, 4.323 - 4.313, 4.577 - 4.564, 4.904 - 4.886, 5.345 - 5.319, 6.000 - 5.960, 7.157 - 7.073, 10.465 - 10.120
Rwork0.22429 ---
all0.2265 55651 --
obs0.22655 52816 100 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 10.586 Å2
Baniso -1Baniso -2Baniso -3
1-2.21 Å20 Å20 Å2
2--2.21 Å20 Å2
3----4.43 Å2
Refinement stepCycle: LAST / Resolution: 3.25→15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15302 0 179 0 15481
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.02115906
X-RAY DIFFRACTIONr_angle_refined_deg1.2731.96821684
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.5251987
X-RAY DIFFRACTIONr_chiral_restr0.0830.22428
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0212074
X-RAY DIFFRACTIONr_nbd_refined0.2080.26438
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1370.2404
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2270.233
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.1760.23
X-RAY DIFFRACTIONr_mcbond_it1.6572.59931
X-RAY DIFFRACTIONr_mcangle_it2.717516033
X-RAY DIFFRACTIONr_scbond_it1.812.55975
X-RAY DIFFRACTIONr_scangle_it2.8355651
Refine LS restraints NCS

Dom-ID: 1 / Auth asym-ID: A / Refine-ID: X-RAY DIFFRACTION

Ens-IDNumberTypeRms dev position (Å)Weight position
11498tight positional0.030.05
2941tight positional0.030.05
31316tight positional0.030.05
4592medium positional0.290.5
11498tight thermal0.060.5
2941tight thermal0.050.5
31316tight thermal0.060.5
4592medium thermal0.52
LS refinement shellResolution: 3.25→3.33 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.397 189 -
Rwork0.331 3708 -
obs-3708 100 %
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)
18.1541-0.7112-1.24823.8111-0.45584.29180.0164-0.6025-0.22310.2585-0.1664-0.0344-0.32210.08150.150.32820.1187-0.09030.3497-0.00790.279750.814664.4207217.161
22.95330.3437-1.24793.5179-0.47115.6454-0.022-0.83720.75470.5839-0.0193-0.2326-0.99960.72450.04130.9610.051-0.2190.334-0.14710.537560.973891.1703212.4541
34.6119-0.9412-0.1285.1052-0.83564.682-0.00680.207-0.2034-0.0555-0.08340.0157-0.30530.17550.09020.1956-0.0221-0.11790.31390.0380.276478.413264.5571196.5325
426.625411.2059-9.93089.7618-4.818115.19930.953-0.77933.3216-0.30280.0129-0.6317-3.45953.6272-0.96591.3333-0.79240.09671.70010.0571.3954107.893874.4499199.1873
54.93650.27062.39884.67830.52746.6367-0.2511-0.38480.4705-0.0098-0.15480.3979-0.6068-0.77560.40590.20780.31150.00850.5371-0.16780.465321.248960.2082207.0842
63.06530.109-0.37793.8276-0.62582.7017-0.016-0.5385-0.04930.2442-0.1131.0809-0.1483-1.14090.1290.20260.12240.16480.89840.08450.536810.101934.5373214.5874
73.7897-0.66031.07696.15330.02915.6096-0.0143-0.06630.029-0.2414-0.0084-0.0043-0.212-0.08670.02270.12410.105-0.02740.3717-0.02280.370811.937641.173179.7694
813.005713.12923.817120.39786.92743.6376-0.1521-0.4122-2.3614-0.27590.1274-0.72750.7782-0.10440.02470.71030.4-0.0820.88330.11381.2723-14.363423.6989169.1663
93.212-0.69911.14222.1977-0.83878.95530.13910.38010.6882-0.0834-0.1490.1628-1.07090.38130.00990.977-0.0297-0.09380.09730.06410.539159.2854104.7732177.6731
108.1035-3.17481.22334.1635-1.30462.8854-0.0027-0.45670.54410.16690.14520.4931-0.5833-0.3368-0.14250.97050.0894-0.05230.1703-0.080.521448.1018100.3724196.5645
115.1573-2.962-1.1694.61160.41036.04940.3404-0.4462-0.6168-0.125-0.20580.25371.00390.0846-0.13460.4836-0.0457-0.01350.39090.16570.48228.54043.1198205.1855
125.6269-2.5782.24613.7517-0.59893.792-0.0471-1.02460.02940.21290.2125-0.2772-0.00920.029-0.16540.152-0.07460.11360.79430.07580.388527.521320.7101219.047
1330.7116-4.7048-8.824115.24780.979515.65942.38455.1091.61691.8285-2.80333.5391-1.8008-5.85630.41881.39870.9150.47672.7895-0.55541.976325.8744112.5158163.9545
143.6061-4.5102-0.094314.34477.263513.50980.53842.3612-1.6467-0.8897-2.37541.89331.8244-2.48381.8371.9025-0.05470.31421.682-0.70162.029423.376298.9991171.5865
156.9041-2.9565.09696.7464-0.739213.45810.732-0.8789-0.40930.2284-0.4218-1.08131.11130.968-0.31020.51820.2288-0.09161.49230.43391.008856.9009-7.5915224.4427
1613.811-3.8288-2.22347.67421.571711.86160.3416-0.60681.85020.3369-0.3212-2.7345-0.11371.3929-0.02040.1358-0.02640.05791.58190.25461.537662.30137.1213222.5789
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1 - 1951 - 195
2X-RAY DIFFRACTION1AG1001 - 1002
3X-RAY DIFFRACTION2AA196 - 320196 - 320
4X-RAY DIFFRACTION2AH1003 - 1004
5X-RAY DIFFRACTION3AA321 - 488321 - 488
6X-RAY DIFFRACTION4AA489 - 564489 - 564
7X-RAY DIFFRACTION4AI1006
8X-RAY DIFFRACTION5BB1 - 1951 - 195
9X-RAY DIFFRACTION5BJ1001 - 1002
10X-RAY DIFFRACTION6BB196 - 320196 - 320
11X-RAY DIFFRACTION6BK1003 - 1005
12X-RAY DIFFRACTION7BB321 - 488321 - 488
13X-RAY DIFFRACTION8BB489 - 577489 - 577
14X-RAY DIFFRACTION8BM1007 - 1008
15X-RAY DIFFRACTION9CC1 - 1091 - 109
16X-RAY DIFFRACTION10DD1 - 1131 - 119
17X-RAY DIFFRACTION11EE1 - 1091 - 109
18X-RAY DIFFRACTION12FF1 - 1131 - 119
19X-RAY DIFFRACTION13CC110 - 214110 - 214
20X-RAY DIFFRACTION14DD114 - 216120 - 222
21X-RAY DIFFRACTION15EE110 - 214110 - 214
22X-RAY DIFFRACTION16FF114 - 216120 - 222

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