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- PDB-3ef7: ZP-N domain of mammalian sperm receptor ZP3 (crystal form III) -

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Basic information

Entry
Database: PDB / ID: 3ef7
TitleZP-N domain of mammalian sperm receptor ZP3 (crystal form III)
ComponentsMaltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
KeywordsCELL ADHESION / Fertilization / oocyte / egg coat / zona pellucida / vitelline envelope / ZP domain / egg-sperm interaction / species-specific gamete recognition / speciation / biodiversity / infertility / extracellular matrix / immunoglobulin-like fold / glycoprotein / receptor / secreted / transmembrane
Function / homology
Function and homology information


positive regulation of type IV hypersensitivity / positive regulation of acrosomal vesicle exocytosis / positive regulation of antral ovarian follicle growth / positive regulation of ovarian follicle development / egg coat formation / positive regulation of humoral immune response / Interaction With Cumulus Cells And The Zona Pellucida / structural constituent of egg coat / egg coat / positive regulation of acrosome reaction ...positive regulation of type IV hypersensitivity / positive regulation of acrosomal vesicle exocytosis / positive regulation of antral ovarian follicle growth / positive regulation of ovarian follicle development / egg coat formation / positive regulation of humoral immune response / Interaction With Cumulus Cells And The Zona Pellucida / structural constituent of egg coat / egg coat / positive regulation of acrosome reaction / humoral immune response mediated by circulating immunoglobulin / binding of sperm to zona pellucida / blastocyst formation / oocyte development / regulation of signaling receptor activity / positive regulation of leukocyte migration / detection of maltose stimulus / maltose transport complex / positive regulation of interleukin-4 production / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / positive regulation of T cell proliferation / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / positive regulation of type II interferon production / positive regulation of inflammatory response / outer membrane-bounded periplasmic space / carbohydrate binding / : / periplasmic space / receptor ligand activity / negative regulation of DNA-templated transcription / DNA damage response / positive regulation of DNA-templated transcription / extracellular space / membrane / plasma membrane
Similarity search - Function
Zona pellucida, ZP-N domain / : / : / ZP-N domain / : / Zona pellucida domain, conserved site / ZP domain signature. / Zona pellucida, ZP-C domain / ZP-C domain / Zona pellucida (ZP) domain ...Zona pellucida, ZP-N domain / : / : / ZP-N domain / : / Zona pellucida domain, conserved site / ZP domain signature. / Zona pellucida, ZP-C domain / ZP-C domain / Zona pellucida (ZP) domain / ZP domain profile. / Zona pellucida domain / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Periplasmic binding protein-like II / D-Maltodextrin-Binding Protein; domain 2 / Immunoglobulin-like / Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
alpha-maltose / Maltose/maltodextrin-binding periplasmic protein / Zona pellucida sperm-binding protein 3
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT, ZN-SINGLE-WAVELENGTH ANOMALOUS DIFFRACTION / Resolution: 3.1 Å
AuthorsMonne, M. / Jovine, L.
Citation
Journal: Nature / Year: 2008
Title: Crystal structure of the ZP-N domain of ZP3 reveals the core fold of animal egg coats
Authors: Monne, M. / Han, L. / Schwend, T. / Burendahl, S. / Jovine, L.
#1: Journal: CELL(CAMBRIDGE,MASS.) / Year: 1980
Title: Mammalian sperm-egg interaction: identification of a glycoprotein in mouse egg zonae pellucidae possessing receptor activity for sperm
Authors: Bleil, J.D. / Wassarman, P.M.
#2: Journal: Febs Lett. / Year: 1992
Title: A large domain common to sperm receptors (Zp2 and Zp3) and TGF-beta type III receptor
Authors: Bork, P. / Sander, C.
#3: Journal: Nat Cell Biol / Year: 2002
Title: The ZP domain is a conserved module for polymerization of extracellular proteins.
Authors: Luca Jovine / Huayu Qi / Zev Williams / Eveline Litscher / Paul M Wassarman /
Abstract: Many eukaryotic extracellular proteins share a sequence of unknown function, called the zona pellucida (ZP) domain. Among these proteins are the mammalian sperm receptors ZP2 and ZP3, non-mammalian ...Many eukaryotic extracellular proteins share a sequence of unknown function, called the zona pellucida (ZP) domain. Among these proteins are the mammalian sperm receptors ZP2 and ZP3, non-mammalian egg coat proteins, Tamm-Horsfall protein (THP), glycoprotein-2 (GP-2), alpha- and beta-tectorins, transforming growth factor (TGF)-beta receptor III and endoglin, DMBT-1 (deleted in malignant brain tumour-1), NompA (no-mechanoreceptor-potential-A), Dumpy and cuticlin-1 (refs 1,2). Here, we report that the ZP domain of ZP2, ZP3 and THP is responsible for polymerization of these proteins into filaments of similar supramolecular structure. Most ZP domain proteins are synthesized as precursors with carboxy-terminal transmembrane domains or glycosyl phosphatidylinositol (GPI) anchors. Our results demonstrate that the C-terminal transmembrane domain and short cytoplasmic tail of ZP2 and ZP3 are not required for secretion, but are essential for assembly. Finally, we suggest a molecular basis for dominant human hearing disorders caused by point mutations within the ZP domain of alpha-tectorin.
#4: Journal: Proc Natl Acad Sci U S A / Year: 2004
Title: A duplicated motif controls assembly of zona pellucida domain proteins.
Authors: Luca Jovine / Huayu Qi / Zev Williams / Eveline S Litscher / Paul M Wassarman /
Abstract: Many secreted eukaryotic glycoproteins that play fundamental roles in development, hearing, immunity, and cancer polymerize into filaments and extracellular matrices through zona pellucida (ZP) ...Many secreted eukaryotic glycoproteins that play fundamental roles in development, hearing, immunity, and cancer polymerize into filaments and extracellular matrices through zona pellucida (ZP) domains. ZP domain proteins are synthesized as precursors containing C-terminal propeptides that are cleaved at conserved sites. However, the consequences of this processing and the mechanism by which nascent proteins assemble are unclear. By microinjection of mutated DNA constructs into growing oocytes and mammalian cell transfection, we have identified a conserved duplicated motif [EHP (external hydrophobic patch)/IHP (internal hydrophobic patch)] regulating the assembly of mouse ZP proteins. Whereas the transmembrane domain (TMD) of ZP3 can be functionally replaced by an unrelated TMD, mutations in either EHP or IHP do not hinder secretion of full-length ZP3 but completely abolish its assembly. Because mutants truncated before the TMD are not processed, we conclude that the conserved TMD of mammalian ZP proteins does not engage them in specific interactions but is essential for C-terminal processing. Cleavage of ZP precursors results in loss of the EHP, thereby activating secreted polypeptides to assemble by using the IHP within the ZP domain. Taken together, these findings suggest a general mechanism for assembly of ZP domain proteins.
#5: Journal: Annu Rev Biochem / Year: 2005
Title: Zona pellucida domain proteins.
Authors: Luca Jovine / Costel C Darie / Eveline S Litscher / Paul M Wassarman /
Abstract: Many eukaryotic proteins share a sequence designated as the zona pellucida (ZP) domain. This structural element, present in extracellular proteins from a wide variety of organisms, from nematodes to ...Many eukaryotic proteins share a sequence designated as the zona pellucida (ZP) domain. This structural element, present in extracellular proteins from a wide variety of organisms, from nematodes to mammals, consists of approximately 260 amino acids with eight conserved cysteine (Cys) residues and is located close to the C terminus of the polypeptide. ZP domain proteins are often glycosylated, modular structures consisting of multiple types of domains. Predictions can be made about some of the structural features of the ZP domain and ZP domain proteins. The functions of ZP domain proteins vary tremendously, from serving as structural components of egg coats, appendicularian mucous houses, and nematode dauer larvae, to serving as mechanotransducers in flies and receptors in mammals and nonmammals. Generally, ZP domain proteins are present in filaments and/or matrices, which is consistent with the role of the domain in protein polymerization. A general mechanism for assembly of ZP domain proteins has been presented. It is likely that the ZP domain plays a common role despite its presence in proteins of widely diverse functions.
#6: Journal: Bmc Biochem. / Year: 2006
Title: The PLAC1-homology region of the ZP domain is sufficient for protein polymerisation
Authors: Jovine, L. / Janssen, W.G. / Litscher, E.S. / Wassarman, P.M.
History
DepositionSep 8, 2008Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Dec 2, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.2Jun 28, 2017Group: Source and taxonomy / Category: entity_src_gen
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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.occupancy / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _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_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_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 / _pdbx_struct_special_symmetry.label_asym_id / _struct_asym.entity_id / _struct_ref_seq_dif.details
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Revision 2.1Nov 10, 2021Group: Database references / Structure summary / Category: chem_comp / database_2 / struct_ref_seq_dif
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 2.2Nov 1, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 2.3Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature
Remark 650HELIX DETERMINATION METHOD: AUTHOR DETERMINED
Remark 700SHEET DETERMINATION METHOD: AUTHOR DETERMINED
Remark 40MOLPROBITY STRUCTURE VALIDATION PROGRAMS: MOLPROBITY (KING, REDUCE, AND PROBE) AUTHORS: I.W.DAVIS,V. ...MOLPROBITY STRUCTURE VALIDATION PROGRAMS: MOLPROBITY (KING, REDUCE, AND PROBE) AUTHORS: I.W.DAVIS,V.B.CHEN, R.M.IMMORMINO, J.J.HEADD,W.B.ARENDALL,J.M.WORD AUTHORS: I.W.DAVIS,A.LEAVER-FAY,V.B.CHEN,J.N.BLOCK, G.J.KAPRAL,X.WANG,L.W.MURRAY,W.B.ARENDALL, J.SNOEYINK,J.S.RICHARDSON,D.C.RICHARDSON REFERENCE: MOLPROBITY: ALL-ATOM CONTACTS AND STRUCTURE VALIDATION FOR PROTEINS AND NUCLEIC ACIDS NUCLEIC ACIDS RESEARCH. 2007;35:W375-83.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
B: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)107,59321
Polymers105,8982
Non-polymers1,69519
Water362
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A: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,6989
Polymers52,9491
Non-polymers7498
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)53,89512
Polymers52,9491
Non-polymers94611
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
A: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
B: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
hetero molecules

A: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
B: Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)215,18642
Polymers211,7964
Non-polymers3,39038
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_455-x-1,-y,z1
MethodPQS
Unit cell
Length a, b, c (Å)86.200, 98.580, 143.680
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11A-490-

ZN

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Components

#1: Protein Maltose-binding periplasmic protein, LINKER, Zona pellucida protein 3 / Maltose-binding protein/ZP3 ZP-N domain chimera / MBP / Zona pellucida glycoprotein ZP3 / Sperm ...Maltose-binding protein/ZP3 ZP-N domain chimera / MBP / Zona pellucida glycoprotein ZP3 / Sperm receptor / Zona pellucida protein C


Mass: 52948.945 Da / Num. of mol.: 2
Fragment: ZP3 ZP-N domain, UNP residues 27-393, UNP residues 42-143
Mutation: I3T, E360A, K363A, D364A, R368N
Source method: isolated from a genetically manipulated source
Details: This protein is a chimera. residues 2-368 are from e. coli maltose binding protein (MBP), correspond to residues 27-393 of swiss-prot database entry P0AEX9 and contain mutations I3T, E360A, ...Details: This protein is a chimera. residues 2-368 are from e. coli maltose binding protein (MBP), correspond to residues 27-393 of swiss-prot database entry P0AEX9 and contain mutations I3T, E360A, K363A, D364A, R368N (corresponding to I28T, E385A, K388A, D389A and R393N IN P0AEX9). residues 372-473 are from mouse ZP3 protein and correspond to residues 42-143 of swiss-prot database entry P10761.
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria), (gene. exp.) Mus musculus (house mouse)
Cellular location: Extracellular matrix / Gene: ZP3, ZP-3, ZPC / Plasmid: PLJMBP4C, PLJDIS1 / Production host: Escherichia coli (E. coli) / Strain (production host): Origami B (DE3) / References: UniProt: P0AEX9, UniProt: P10761
#2: Polysaccharide alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 2
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
#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: Zn
#4: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2 / 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: 2.89 Å3/Da / Density % sol: 57.38 % / Description: The file contains friedel pairs
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.8
Details: Sample: 15mg/ml protein in 0.05M sodium chloride, 0.01M Tris-HCL, PH7.2, 0.001M Maltose. Reservoir: 12% PEG6000, 0.15M calcium chloride, 0.0025M zinc chloride, 0.1M Tris-HCL, PH8.2. Sample ...Details: Sample: 15mg/ml protein in 0.05M sodium chloride, 0.01M Tris-HCL, PH7.2, 0.001M Maltose. Reservoir: 12% PEG6000, 0.15M calcium chloride, 0.0025M zinc chloride, 0.1M Tris-HCL, PH8.2. Sample to reservoir ratio in drop: 1:1, PH8.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.0K, pH7.8

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1.28235 / Wavelength: 1.28235 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 17, 2007
RadiationMonochromator: SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.28235 Å / Relative weight: 1
ReflectionResolution: 3.1→500 Å / Num. all: 42949 / Num. obs: 42898 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 7.6 % / Biso Wilson estimate: 82.58 Å2 / Rsym value: 0.095 / Net I/σ(I): 17.7
Reflection shellResolution: 3.1→3.17 Å / Redundancy: 7.6 % / Mean I/σ(I) obs: 3.1 / Num. unique all: 2688 / Rsym value: 0.768 / % possible all: 100

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Processing

Software
NameClassification
MxCuBEdata collection
PHASERphasing
PHENIXrefinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT, ZN-SINGLE-WAVELENGTH ANOMALOUS DIFFRACTION
Starting model: PDB ENTRY 3D4G

3d4g


Resolution: 3.1→33.16 Å / SU ML: 0.45 / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 25.85
Stereochemistry target values: PHASED MAXIMUM LIKELIHOOD (MLHL)
Details: The file contains friedel pairs, Number of anomalous scatterer groups: 1. Anomalous scatterer group: 1. Selection: name ZN. FP: -8.2100. FDP: 4.7500
RfactorNum. reflection% reflectionSelection details
Rfree0.256 2191 5.108 %Random
Rwork0.208 ---
all0.21 42949 --
obs0.21 42895 99.9 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 56.4 Å2 / ksol: 0.28 e/Å3
Displacement parametersBiso mean: 112.96 Å2
Baniso -1Baniso -2Baniso -3
1-0.5421 Å20 Å2-0 Å2
2--5.1846 Å20 Å2
3----22.089 Å2
Refinement stepCycle: LAST / Resolution: 3.1→33.16 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7246 0 63 2 7311
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0117488
X-RAY DIFFRACTIONf_angle_d1.03910138
X-RAY DIFFRACTIONf_dihedral_angle_d17.5972696
X-RAY DIFFRACTIONf_chiral_restr0.0571132
X-RAY DIFFRACTIONf_plane_restr0.0041308
LS refinement shellResolution: 3.1→3.17 Å / Total num. of bins used: 16
RfactorNum. reflection% reflection
Rfree0.363 126 -
Rwork0.321 2562 -
obs-2688 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)
1-0.1360.54450.1262.4125-0.29721.2989-0.17831.04130.5846-0.40710.0347-0.09-0.46240.15150.03560.57030.04730.05081.0523-0.03880.8853-9.8517-16.290343.9019
22.3757-0.58080.52130.83920.4982.6553-0.0459-0.0901-0.1570.25780.0724-0.11440.27350.2933-0.00410.62780.0707-0.03670.35220.0540.7274-20.1804-16.13763.3926
32.8889-0.0471.46922.71821.05383.3066-0.28310.155-0.3128-0.7062-0.0187-0.11650.6595-0.04340.31131.00890.030.07850.7038-0.09120.8036-44.5222-14.461247.683
40.7511-1.969-0.37851.766-1.5421.2915-0.05670.69280.04190.2603-0.2184-0.52090.03110.60280.23360.7718-0.08110.07321.8328-0.07350.971-17.0783-10.151421.5731
50.21380.1077-0.31630.2613-0.02570.08090.78890.80360.0013-0.65950.0753-0.4660.7422-0.0574-0.74461.13070.13320.28762.4785-0.09920.7708-18.5794-10.23994.1976
61.1304-0.6130.76651.4044-0.11961.5570.17420.0838-0.3366-0.3276-0.34831.16310.08090.77520.22330.92810.05760.02551.2562-0.65271.301-27.9148-40.897217.0507
75.1426-0.20680.63710.91451.95661.3860.0671.6999-0.9748-0.36660.10980.12690.28140.836-0.0611.03810.01670.11121.3808-0.56221.0736-31.2568-32.587513.3671
81.28220.20430.8041.2383-0.33941.74990.35191.2948-0.3085-0.1758-0.2297-0.21930.20110.5927-0.07510.87120.07880.10921.9036-0.52240.9306-22.5495-20.936111.4349
91.2017-1.0551-0.40771.95721.6290.9104-0.24040.47440.02870.2569-0.14870.35290.1286-0.55750.40971.1045-0.22360.17151.7517-0.16761.0529-48.6357-9.109819.9639
10-0.57320.0397-1.21070.6746-0.54931.4633-0.40190.2836-0.129-0.3204-0.06390.30410.82980.3890.52210.8566-0.10560.03741.3006-0.25670.8476-38.6896-16.474526.318
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A 1-50
2X-RAY DIFFRACTION2chain A 51-372, 482
3X-RAY DIFFRACTION3chain A 373-480, 485, 492, 490, chain B 487
4X-RAY DIFFRACTION4chain B 1-66, 482
5X-RAY DIFFRACTION5chain B 67-109
6X-RAY DIFFRACTION6chain B 110-158
7X-RAY DIFFRACTION7chain B 159-255
8X-RAY DIFFRACTION8chain B 256-370, 493
9X-RAY DIFFRACTION9chain B 371-436
10X-RAY DIFFRACTION10chain B 437-480, 484, 486, 489

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