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- PDB-4bld: Crystal structure of a human Suppressor of fused (SUFU)-GLI3p complex -

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Basic information

Entry
Database: PDB / ID: 4bld
TitleCrystal structure of a human Suppressor of fused (SUFU)-GLI3p complex
Components
  • MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
  • TRANSCRIPTIONAL ACTIVATOR GLI3
KeywordsSIGNALING PROTEIN / SUGAR BINDING PROTEIN-SIGNALING PROTEIN COMPLEX / CHIMERA / FUSION PROTEIN / HEDGEHOG SIGNALING / GENE REGULATION / TRANSCRIPTION FACTOR
Function / homology
Function and homology information


lateral ganglionic eminence cell proliferation / lambdoid suture morphogenesis / sagittal suture morphogenesis / mammary gland specification / anterior semicircular canal development / lateral semicircular canal development / larynx morphogenesis / nose morphogenesis / GLI proteins bind promoters of Hh responsive genes to promote transcription / smoothened signaling pathway involved in dorsal/ventral neural tube patterning ...lateral ganglionic eminence cell proliferation / lambdoid suture morphogenesis / sagittal suture morphogenesis / mammary gland specification / anterior semicircular canal development / lateral semicircular canal development / larynx morphogenesis / nose morphogenesis / GLI proteins bind promoters of Hh responsive genes to promote transcription / smoothened signaling pathway involved in dorsal/ventral neural tube patterning / smoothened signaling pathway involved in ventral spinal cord interneuron specification / smoothened signaling pathway involved in spinal cord motor neuron cell fate specification / positive regulation of cellular response to drug / forebrain dorsal/ventral pattern formation / GLI-SUFU complex / frontal suture morphogenesis / cell differentiation involved in kidney development / embryonic neurocranium morphogenesis / hindgut morphogenesis / optic nerve morphogenesis / negative regulation of alpha-beta T cell differentiation / tongue development / regulation of bone development / positive regulation of chondrocyte differentiation / proximal/distal pattern formation / limb morphogenesis / layer formation in cerebral cortex / embryonic digestive tract morphogenesis / ciliary tip / camera-type eye morphogenesis / embryonic digestive tract development / artery development / vocalization behavior / negative thymic T cell selection / mediator complex binding / melanocyte differentiation / forebrain radial glial cell differentiation / metanephros development / coronary vasculature development / negative regulation of chondrocyte differentiation / positive regulation of alpha-beta T cell differentiation / alpha-beta T cell differentiation / anterior/posterior pattern specification / aorta development / ventricular septum development / embryonic digit morphogenesis / branching involved in ureteric bud morphogenesis / smoothened signaling pathway / negative regulation of protein import into nucleus / skin development / thymocyte apoptotic process / negative regulation of neuron differentiation / positive regulation of neuroblast proliferation / histone acetyltransferase binding / ciliary base / heart looping / detection of maltose stimulus / RUNX2 regulates osteoblast differentiation / maltose transport complex / odontogenesis of dentin-containing tooth / carbohydrate transport / roof of mouth development / oligodendrocyte differentiation / axoneme / negative regulation of ubiquitin-dependent protein catabolic process / developmental growth / carbohydrate transmembrane transporter activity / spermatid development / neuroblast proliferation / maltose binding / maltose transport / chondrocyte differentiation / maltodextrin transmembrane transport / negative regulation of osteoblast differentiation / positive regulation of osteoblast differentiation / negative regulation of stem cell proliferation / Hedgehog 'off' state / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / transcription repressor complex / ATP-binding cassette (ABC) transporter complex / lung development / axon guidance / stem cell proliferation / cell chemotaxis / negative regulation of smoothened signaling pathway / neural tube closure / RNA polymerase II transcription regulatory region sequence-specific DNA binding / hippocampus development / Degradation of GLI1 by the proteasome / Hedgehog 'on' state / negative regulation of canonical Wnt signaling pathway / Degradation of GLI2 by the proteasome / GLI3 is processed to GLI3R by the proteasome / beta-catenin binding / protein processing / positive regulation of protein import into nucleus / histone deacetylase binding / protein import into nucleus / sequence-specific double-stranded DNA binding / osteoblast differentiation
Similarity search - Function
C2H2-type zinc-finger protein GLI-like / Sufu, C-terminal domain / Suppressor of fused / Suppressor of fused, eukaryotic / Suppressor of fused C-terminal / Suppressor of fused, N-terminal / Suppressor of fused, C-terminal domain superfamily / Suppressor of Fused Gli/Ci N terminal binding domain / Suppressor of fused-like domain / Suppressor of fused protein (SUFU) ...C2H2-type zinc-finger protein GLI-like / Sufu, C-terminal domain / Suppressor of fused / Suppressor of fused, eukaryotic / Suppressor of fused C-terminal / Suppressor of fused, N-terminal / Suppressor of fused, C-terminal domain superfamily / Suppressor of Fused Gli/Ci N terminal binding domain / Suppressor of fused-like domain / Suppressor of fused protein (SUFU) / : / C2H2 zinc finger / Gyrase A; domain 2 / Zinc finger, C2H2 type / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / zinc finger / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Zinc finger C2H2 type domain profile. / Zinc finger C2H2 superfamily / Zinc finger C2H2 type domain signature. / Zinc finger C2H2-type / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
alpha-maltose / Maltose/maltodextrin-binding periplasmic protein / Transcriptional activator GLI3 / Suppressor of fused homolog
Similarity search - Component
Biological speciesESCHERICHIA COLI (E. coli)
HOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.802 Å
AuthorsCherry, A.L. / Finta, C. / Karlstrom, M. / De Sanctis, D. / Toftgard, R. / Jovine, L.
Citation
#1: Journal: Nat.Cell Biol. / Year: 1999
Title: Mammalian Suppressor-of-Fused Modulates Nuclear-Cytoplasmic Shuttling of GLI-1.
Authors: Kogerman, P. / Grimm, T. / Kogerman, L. / Krause, D. / Unden, A.B. / Sandstedt, B. / Toftgard, R. / Zaphiropoulos, P.G.
#2: Journal: J.Biol.Chem. / Year: 2003
Title: Characterization of the Physical Interaction of GLI Proteins with Sufu Proteins.
Authors: Dunaeva, M. / Michelson, P. / Kogerman, P. / Toftgard, R.
#3: Journal: Mol.Cell.Biol. / Year: 2004
Title: Suppressor of Fused Regulates GLI Activity Through a Dual Binding Mechanism.
Authors: Merchant, M. / Vajdos, F.F. / Ultsch, M. / Maun, H.R. / Wendt, U. / Cannon, J. / Desmarais, W. / Lazarus, R.A. / De Vos, A.M. / De Sauvage, F.J.
#4: Journal: Dev.Cell / Year: 2006
Title: Genetic Elimination of Suppressor of Fused Reveals an Essential Repressor Function in the Mammalian Hedgehog Signaling Pathway.
Authors: Svard, J. / Heby-Henricson, K. / Persson-Lek, M. / Rozell, B. / Lauth, M. / Bergstrom, A. / Ericson, J. / Toftgard, R. / Teglund, S.
History
DepositionMay 2, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 27, 2013Provider: repository / Type: Initial release
Revision 1.1Dec 11, 2013Group: Derived calculations / Other
Revision 1.2Dec 18, 2013Group: Database references
Revision 1.3Mar 15, 2017Group: Source and taxonomy
Revision 1.4May 8, 2019Group: Data collection / Experimental preparation
Category: database_PDB_rev / database_PDB_rev_record / exptl_crystal_grow
Item: _exptl_crystal_grow.method
Revision 1.5May 15, 2019Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.temp
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Other / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_conn_type / 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 / _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_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.type / _pdbx_database_status.status_code_sf / _pdbx_struct_assembly_gen.asym_id_list / _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_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_asym.entity_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 20, 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
B: MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
C: MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
D: MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
E: TRANSCRIPTIONAL ACTIVATOR GLI3
F: TRANSCRIPTIONAL ACTIVATOR GLI3
G: TRANSCRIPTIONAL ACTIVATOR GLI3
H: TRANSCRIPTIONAL ACTIVATOR GLI3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)342,48616
Polymers340,8558
Non-polymers1,6318
Water00
1
A: MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
E: TRANSCRIPTIONAL ACTIVATOR GLI3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,6214
Polymers85,2142
Non-polymers4082
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2100 Å2
ΔGint-26.3 kcal/mol
Surface area31570 Å2
MethodPISA
2
C: MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
G: TRANSCRIPTIONAL ACTIVATOR GLI3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,6214
Polymers85,2142
Non-polymers4082
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2060 Å2
ΔGint-25.8 kcal/mol
Surface area31260 Å2
MethodPISA
3
B: MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
F: TRANSCRIPTIONAL ACTIVATOR GLI3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,6214
Polymers85,2142
Non-polymers4082
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2110 Å2
ΔGint-24.7 kcal/mol
Surface area31000 Å2
MethodPISA
4
D: MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG
H: TRANSCRIPTIONAL ACTIVATOR GLI3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,6214
Polymers85,2142
Non-polymers4082
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2130 Å2
ΔGint-25.4 kcal/mol
Surface area31240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)116.610, 136.550, 116.740
Angle α, β, γ (deg.)90.00, 105.25, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
22
/ NCS ensembles :
ID
1
2

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Components

#1: Protein
MALTOSE-BINDING PERIPLASMIC PROTEIN, SUPPRESSOR OF FUSED HOMOLOG / SUFUH / LINKER / SUPPRESOR OF FUSED


Mass: 83634.141 Da / Num. of mol.: 4
Fragment: MBPP RESIDUES 29-392,SUFUH RESIDUES 32-278,361-483
Mutation: YES
Source method: isolated from a genetically manipulated source
Details: DELETION OF RESIDUES 279-360 AND REPLACEMENT WITH PSRGEDP LINKER. DELETION OF RESIDUES 454-456. W61D, L62S, G63F, P453A, K457A
Source: (gene. exp.) ESCHERICHIA COLI (E. coli), (gene. exp.) HOMO SAPIENS (human)
Plasmid: PLJMBP4C / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): JM109 (DE3) / References: UniProt: P0AEX9, UniProt: Q9UMX1
#2: Protein/peptide
TRANSCRIPTIONAL ACTIVATOR GLI3 / GLI3 FORM OF 190 KDA / GLI3-190 / GLI3 FULL LENGTH PROTEIN / G LI3FL / GLI3 C-TERMINALLY TRUNCATED ...GLI3 FORM OF 190 KDA / GLI3-190 / GLI3 FULL LENGTH PROTEIN / G LI3FL / GLI3 C-TERMINALLY TRUNCATED FORM / GLI3 FORM OF 83 KDA / GLI3-8 GLI3


Mass: 1579.648 Da / Num. of mol.: 4 / Fragment: RESIDUES 328-344 / Source method: obtained synthetically / Source: (synth.) HOMO SAPIENS (human) / References: UniProt: P10071
#3: Polysaccharide
alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
Sequence detailsRESIDUES 216 AND 220 OF MALTOSE-BINDING PERIPLASMIC PROTEIN ARE MUTATED TO HISTIDINES. RESIDUES 372- ...RESIDUES 216 AND 220 OF MALTOSE-BINDING PERIPLASMIC PROTEIN ARE MUTATED TO HISTIDINES. RESIDUES 372-618 OF THIS FUSION CONSTRUCT REPRESENT UNIPROT Q9UMX1 RESIDUES 32- 278. RESIDUES 61-63 OF UNIPROT Q9UMX1 HAVE BEEN MUTATED ( FROM WLG) TO DSF. RESIDUES 619-625 REPRESENT AN ARTIFICIAL LINKER. RESIDUES 626-718 REPRESENT UNIPROT Q9UMX1 RESIDUES 361-453. RESIDUES 454-456 OF UNIPROT Q9UMX1 HAVE BEEN DELETED AND RESIDUES 453 AND 457 MUTATED TO ALANINES. RESIDUES 719-745 REPRESENT UNIPROT Q9UMX1 RESIDUES 457-483. THIS MOLECULE IS A PEPTIDE CONTAINING RESIDUES 328-344

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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: 2.69 Å3/Da / Density % sol: 54.26 % / Description: NONE
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: PROTEIN (10 MG/ML IN 10 MM TRIS-HCL PH 7.5, 50 MM NACL, 1 MM DTT, 1 MM MALTOSE) WAS MIXED IN A 1:1 MOLAR RATIO WITH ZN(OAC)2 AND A 1:4 MOLAR RATIO WITH GLI3 PEPTIDE. THE COMPLEX WAS ...Details: PROTEIN (10 MG/ML IN 10 MM TRIS-HCL PH 7.5, 50 MM NACL, 1 MM DTT, 1 MM MALTOSE) WAS MIXED IN A 1:1 MOLAR RATIO WITH ZN(OAC)2 AND A 1:4 MOLAR RATIO WITH GLI3 PEPTIDE. THE COMPLEX WAS CRYSTALLISED BY HANGING DROP VAPOUR DIFFUSION AT 4C WITH 1:1 OR 2:1 DROPS OF PROTEIN:WELL SOLUTION (14-18% (V/V) PEG 3350 AND 0.2 M NA FORMATE)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.97625
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 24, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 2.8→46.36 Å / Num. obs: 85722 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 3.4 % / Biso Wilson estimate: 75.469 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 9.6
Reflection shellResolution: 2.8→2.87 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.67 / Mean I/σ(I) obs: 1.6 / % possible all: 95.7

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
xia2- XDSdata reduction
xia2- XDSdata scaling
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4BL9

4bl9


Resolution: 2.802→19.94 Å / SU ML: 0.39 / σ(F): 1.37 / Phase error: 28.6 / Stereochemistry target values: ML
Details: RESIDUES 372-618 OF THIS FUSION CONSTRUCT REPRESENT UNIPROT Q9UMX1 RESIDUES 32-278. RESIDUES 619-625 REPRESENT AN ARTIFICIAL LINKER. RESIDUES 626-718 REPRESENT UNIPROT Q9UMX1 RESIDUES 361- ...Details: RESIDUES 372-618 OF THIS FUSION CONSTRUCT REPRESENT UNIPROT Q9UMX1 RESIDUES 32-278. RESIDUES 619-625 REPRESENT AN ARTIFICIAL LINKER. RESIDUES 626-718 REPRESENT UNIPROT Q9UMX1 RESIDUES 361-453. RESIDUES 719-745 REPRESENT UNIPROT Q9UMX1 RESIDUES 457-483. THEREFORE, TO OBTAIN THE CORRECT NUMBERING, 340 SHOULD BE SUBTRACTED FROM RESIDUES 372-618, 265 SHOULD BE SUBTRACTED FROM RESIDUES 626-718 AND 262 SHOULD BE SUBTRACTED FROM RESIDUES 719-745.
RfactorNum. reflection% reflection
Rfree0.2343 1975 2.3 %
Rwork0.2011 --
obs0.2019 85322 98.78 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 96.568 Å2
Refinement stepCycle: LAST / Resolution: 2.802→19.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23020 0 96 0 23116
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00623757
X-RAY DIFFRACTIONf_angle_d1.14232309
X-RAY DIFFRACTIONf_dihedral_angle_d12.4838594
X-RAY DIFFRACTIONf_chiral_restr0.0693488
X-RAY DIFFRACTIONf_plane_restr0.0064190
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8024-2.87230.34971350.29985599X-RAY DIFFRACTION94
2.8723-2.94970.30971410.29466012X-RAY DIFFRACTION100
2.9497-3.03620.35181430.28875979X-RAY DIFFRACTION100
3.0362-3.13380.34671580.27795959X-RAY DIFFRACTION100
3.1338-3.24540.28121390.26546001X-RAY DIFFRACTION100
3.2454-3.37470.28131420.24225976X-RAY DIFFRACTION100
3.3747-3.52750.31181320.23055970X-RAY DIFFRACTION99
3.5275-3.71240.25071270.20866001X-RAY DIFFRACTION99
3.7124-3.94330.26421410.20255962X-RAY DIFFRACTION99
3.9433-4.2450.20181380.17456001X-RAY DIFFRACTION99
4.245-4.66730.18111430.15845966X-RAY DIFFRACTION99
4.6673-5.33130.20161490.16375947X-RAY DIFFRACTION99
5.3313-6.67480.23771360.20325984X-RAY DIFFRACTION99
6.6748-19.94070.19161510.18175990X-RAY DIFFRACTION97
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)
12.23470.17690.0030.7849-0.40614.5832-0.13530.2724-0.0622-0.1015-0.0455-0.04250.53030.5822-0.00010.6940.10490.07060.61930.03860.64471.1273-36.6058-133.2049
22.5425-0.89350.16144.39140.1221.5204-0.2250.03420.2718-0.02670.1549-0.0597-0.2905-0.08600.5847-0.02460.00480.60180.07980.536240.421-9.5119-128.0002
31.8172-0.21850.45131.71250.17711.28120.1325-0.24370.0072-0.05830.14210.38230.3415-0.357400.911-0.0094-0.16680.75580.15740.911513.0806-0.1887-138.4745
46.0610.06760.14622.07720.41973.4989-0.33420.1273-0.07160.00810.16710.19280.0663-0.1071-0.00040.5699-0.0204-0.02060.51510.02670.61876.3571-37.1309-129.9197
52.33490.24410.23163.43530.72523.4279-0.46220.41280.61450.03050.03440.1336-0.81510.0574-0.00190.8663-0.0035-0.260.82830.21630.8448.4944-12.9819-97.8036
60.26-0.1374-0.33110.3097-0.07360.65970.2094-1.2367-0.10830.3088-0.03030.271-0.7447-0.093301.57390.12950.0181.3216-0.15851.544-2.6118-4.2243-71.0806
73.8834-0.4011.14432.05120.48895.03330.1814-1.0958-0.58860.39570.06370.25950.7962-0.79030.0230.9479-0.1410.00870.96150.17380.741910.6754-41.7602-64.9374
83.9989-0.8044-0.21093.86360.31893.45080.18830.29151.0919-0.1703-0.07720.0747-0.8437-0.30310.01460.82030.22610.06180.67590.07090.956440.1621-13.6736-66.268
90.7206-0.34210.04560.16020.00260.6653-0.142-0.58040.86770.3365-0.2532-0.5828-1.47921.320301.5706-0.4585-0.08131.3614-0.04221.549365.7425-6.3006-50.3338
104.84650.3663-0.21431.86060.09232.7188-0.01170.02940.0160.137-0.0156-0.316-0.08640.459900.53440.0911-0.03450.5460.05010.641975.07-39.684-68.4622
111.198-0.3304-0.56424.2748-0.05382.3280.0409-0.00970.2670.0497-0.0455-0.0624-0.37150.093900.65130.03770.03160.84680.08350.700472.2854-10.8077-96.7634
120.39320.41320.01670.93440.03561.0409-0.08320.5686-0.0463-0.62150.0996-0.247-0.20540.608701.1071-0.110.17061.44270.1771.046482.86451.8301-122.8699
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESI 1:371 OR RESI 900)
2X-RAY DIFFRACTION2(CHAIN A AND (RESI 372:605 OR RESI 748:753 OR RESI 910)) OR (CHAIN E)
3X-RAY DIFFRACTION3CHAIN A AND RESI 606:740
4X-RAY DIFFRACTION4CHAIN B AND (RESI 5:371 OR RESI 900)
5X-RAY DIFFRACTION5(CHAIN B AND (RESI 372:605 OR RESI 747:753 OR RESI 910)) OR (CHAIN F)
6X-RAY DIFFRACTION6CHAIN B AND RESI 606:739
7X-RAY DIFFRACTION7CHAIN C AND (RESI 6:371 OR RESI 900)
8X-RAY DIFFRACTION8(CHAIN C AND (RESI 372:605 OR RESI 746:753 OR RESI 910)) OR (CHAIN G)
9X-RAY DIFFRACTION9CHAIN C AND RESI 606:735
10X-RAY DIFFRACTION10CHAIN D AND (RESI 6:371 OR RESI 900)
11X-RAY DIFFRACTION11(CHAIN D AND (RESI 372:605 OR RESI 747:753 OR RESI 910)) OR (CHAIN H)
12X-RAY DIFFRACTION12CHAIN D AND RESI 606:741

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