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- PDB-4elm: Crystal structure of the mouse CD1d-lysosulfatide-Hy19.3 TCR complex -

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Basic information

Entry
Database: PDB / ID: 4elm
TitleCrystal structure of the mouse CD1d-lysosulfatide-Hy19.3 TCR complex
Components
  • Antigen-presenting glycoprotein CD1d1
  • Beta-2 microglobulin
  • Hy19.3 TCR alpha chain (mouse variable domain, human constant domain)
  • Hy19.3 TCR beta chain (mouse variable domain, human constant domain)
KeywordsIMMUNE SYSTEM / antigen presentation / glycolipid / NKT cells
Function / homology
Function and homology information


regulation of immature T cell proliferation in thymus / positive regulation of NK T cell activation / positive regulation of NK T cell differentiation / NK T cell differentiation / endogenous lipid antigen binding / antigen processing and presentation, exogenous lipid antigen via MHC class Ib / positive thymic T cell selection / positive regulation of macrophage activation / Endosomal/Vacuolar pathway / DAP12 interactions ...regulation of immature T cell proliferation in thymus / positive regulation of NK T cell activation / positive regulation of NK T cell differentiation / NK T cell differentiation / endogenous lipid antigen binding / antigen processing and presentation, exogenous lipid antigen via MHC class Ib / positive thymic T cell selection / positive regulation of macrophage activation / Endosomal/Vacuolar pathway / DAP12 interactions / Antigen Presentation: Folding, assembly and peptide loading of class I MHC / ER-Phagosome pathway / DAP12 signaling / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / antigen processing and presentation / positive regulation of interleukin-4 production / regulation of immune response / cellular defense response / T cell receptor binding / Neutrophil degranulation / positive regulation of interleukin-2 production / antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-dependent / cellular response to iron(III) ion / negative regulation of forebrain neuron differentiation / iron ion transport / peptide antigen assembly with MHC class I protein complex / regulation of erythrocyte differentiation / regulation of iron ion transport / response to molecule of bacterial origin / MHC class I peptide loading complex / HFE-transferrin receptor complex / T cell mediated cytotoxicity / antigen processing and presentation of endogenous peptide antigen via MHC class I / positive regulation of T cell cytokine production / MHC class I protein complex / positive regulation of receptor-mediated endocytosis / negative regulation of neurogenesis / positive regulation of T cell mediated cytotoxicity / cellular response to nicotine / multicellular organismal-level iron ion homeostasis / positive regulation of type II interferon production / phagocytic vesicle membrane / negative regulation of epithelial cell proliferation / sensory perception of smell / positive regulation of cellular senescence / late endosome / T cell differentiation in thymus / negative regulation of neuron projection development / protein refolding / protein homotetramerization / amyloid fibril formation / intracellular iron ion homeostasis / learning or memory / early endosome / endosome membrane / lysosome / lysosomal membrane / innate immune response / external side of plasma membrane / structural molecule activity / Golgi apparatus / protein homodimerization activity / extracellular space / cytosol
Similarity search - Function
MHC-I family domain / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site ...MHC-I family domain / MHC class I-like antigen recognition-like / Murine Class I Major Histocompatibility Complex, H2-DB; Chain A, domain 1 / Beta-2-Microglobulin / : / MHC class I-like antigen recognition-like / MHC class I-like antigen recognition-like superfamily / MHC classes I/II-like antigen recognition protein / : / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Immunoglobulins / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
PALMITIC ACID / Chem-SGF / Beta-2-microglobulin / Antigen-presenting glycoprotein CD1d1 / Beta-2-microglobulin
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.48 Å
AuthorsGirardi, E. / Maricic, I. / Wang, J. / Mac, T.T. / Iyer, P. / Kumar, V. / Zajonc, D.M.
CitationJournal: Nat.Immunol. / Year: 2012
Title: Type II natural killer T cells use features of both innate-like and conventional T cells to recognize sulfatide self antigens.
Authors: Girardi, E. / Maricic, I. / Wang, J. / Mac, T.T. / Iyer, P. / Kumar, V. / Zajonc, D.M.
History
DepositionApr 11, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 25, 2012Provider: repository / Type: Initial release
Revision 1.1Jan 9, 2013Group: Database references
Revision 1.2Feb 6, 2013Group: Non-polymer description
Revision 1.3Aug 12, 2015Group: Refinement description
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / 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_unobs_or_zero_occ_atoms / struct_asym / struct_conn / struct_ref_seq_dif / 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.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.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Antigen-presenting glycoprotein CD1d1
C: Antigen-presenting glycoprotein CD1d1
B: Beta-2 microglobulin
D: Beta-2 microglobulin
E: Hy19.3 TCR alpha chain (mouse variable domain, human constant domain)
F: Hy19.3 TCR beta chain (mouse variable domain, human constant domain)
G: Hy19.3 TCR alpha chain (mouse variable domain, human constant domain)
H: Hy19.3 TCR beta chain (mouse variable domain, human constant domain)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)194,63018
Polymers190,9928
Non-polymers3,63810
Water00
1
A: Antigen-presenting glycoprotein CD1d1
B: Beta-2 microglobulin
G: Hy19.3 TCR alpha chain (mouse variable domain, human constant domain)
H: Hy19.3 TCR beta chain (mouse variable domain, human constant domain)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,1619
Polymers95,4964
Non-polymers1,6655
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9250 Å2
ΔGint-30 kcal/mol
Surface area35840 Å2
MethodPISA
2
C: Antigen-presenting glycoprotein CD1d1
D: Beta-2 microglobulin
E: Hy19.3 TCR alpha chain (mouse variable domain, human constant domain)
F: Hy19.3 TCR beta chain (mouse variable domain, human constant domain)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)97,4699
Polymers95,4964
Non-polymers1,9735
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9980 Å2
ΔGint-22 kcal/mol
Surface area36560 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.514, 126.996, 104.349
Angle α, β, γ (deg.)90.00, 110.53, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.996656, 0.081685, 0.002243), (0.081468, 0.995395, -0.050514), (-0.006359, -0.050162, -0.998721)78.32824, -2.06952, 45.81529
Detailsassembly of CD1d, beta-2m, lipid, NKT TCR alpha and beta chains

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Components

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Protein , 4 types, 8 molecules ACBDEGFH

#1: Protein Antigen-presenting glycoprotein CD1d1


Mass: 32632.668 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Cd1.1, CD1d, Cd1d1 / Plasmid: pBACp10pH / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Sf9 / References: UniProt: P11609
#2: Protein Beta-2 microglobulin / Uncharacterized protein


Mass: 11660.350 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse)
Gene: B2m, beta-2-microglobulin, mCG_11606, RP23-34E24.5-001
Plasmid: pBACp10pH / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): Sf9 / References: UniProt: Q91XJ8, UniProt: P01887*PLUS
#3: Protein Hy19.3 TCR alpha chain (mouse variable domain, human constant domain)


Mass: 23209.518 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Valpha1 (mouse variable domain, human constant domain / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
#4: Protein Hy19.3 TCR beta chain (mouse variable domain, human constant domain)


Mass: 27993.633 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse)
Gene: Vbeta16 (mouse variable domain, human constant domain)
Plasmid: pET30a / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)

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Sugars , 3 types, 6 molecules

#5: 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.: 1
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)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#6: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 732.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#7: 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.: 4
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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Non-polymers , 2 types, 4 molecules

#8: Chemical ChemComp-SGF / (2S,3R,4E)-2-amino-3-hydroxyoctadec-4-en-1-yl 3-O-sulfo-beta-D-galactopyranoside / Sphingosine-1-galactoside-3-sulfate


Mass: 541.696 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C24H47NO10S
#9: Chemical ChemComp-PLM / PALMITIC ACID


Mass: 256.424 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C16H32O2

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Details

Has protein modificationY
Sequence detailsAUTHOR INDICATES THIS IS A NATURE VARIANT

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.2 Å3/Da / Density % sol: 61.57 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6
Details: 11% PEG4000, 4% tacsimate, pH 6, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.3 / Wavelength: 0.9765 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Nov 19, 2011
RadiationMonochromator: Single crystal, cylindrically bent, Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9765 Å / Relative weight: 1
ReflectionResolution: 3.48→92.26 Å / Num. all: 31189 / Num. obs: 30877 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.3 % / Rmerge(I) obs: 0.24 / Net I/σ(I): 8.3
Reflection shellResolution: 3.5→3.69 Å / Redundancy: 8.5 % / Rmerge(I) obs: 0.814 / Mean I/σ(I) obs: 2.8 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHASERphasing
REFMAC5.6.0104refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.48→92.26 Å / Cor.coef. Fo:Fc: 0.906 / Cor.coef. Fo:Fc free: 0.865 / SU B: 63.833 / SU ML: 0.451 / Cross valid method: THROUGHOUT / ESU R Free: 0.589 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT
RfactorNum. reflection% reflectionSelection details
Rfree0.26494 1541 5 %RANDOM
Rwork0.20877 ---
obs0.21163 29051 99.05 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 74.926 Å2
Baniso -1Baniso -2Baniso -3
1-1.34 Å20 Å22.14 Å2
2--0.57 Å2-0 Å2
3----0.41 Å2
Refinement stepCycle: LAST / Resolution: 3.48→92.26 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11120 0 240 0 11360
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.02111702
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.1051.94316026
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.55251492
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.74224.021475
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.387151399
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.3361536
X-RAY DIFFRACTIONr_chiral_restr0.070.21769
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0219135
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 3.484→3.574 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.331 106 -
Rwork0.249 1818 -
obs--86.94 %
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)
12.59640.45030.36751.68382.47433.67330.19370.26640.1478-0.2177-0.19310.0067-0.3282-0.3027-0.00070.29760.13370.13420.32050.02750.27239.3701-30.8199-5.5928
26.74421.14462.89743.7938-0.27272.7888-0.0378-0.08870.8282-0.29050.1125-0.6807-0.98060.3182-0.07470.8098-0.22370.50840.3458-0.17590.574456.215-14.23288.5596
33.8235-0.2733-0.23860.7965-1.76494.1230.0106-0.00060.0991-0.0458-0.1242-0.05960.15810.29210.11360.1489-0.00590.00180.099-0.00520.250837.0391-29.486952.5528
47.6586-1.07953.72323.7991-0.11553.279-0.06860.29340.4518-0.0084-0.1030.1787-0.43010.17570.17160.2283-0.0067-0.00180.0229-0.01550.120821.5342-11.51938.0108
54.839-1.58151.26593.95-1.18143.93870.0705-0.10010.21110.01910.08440.01180.10580.469-0.15490.2565-0.0665-0.00610.1286-0.02870.155450.8844-52.268170.741
65.73272.5758-4.5164.4682-2.63678.3590.4967-0.90970.52190.6146-0.24870.6792-0.49920.0336-0.2480.3948-0.08340.1250.2605-0.12850.266432.779-44.704783.3181
78.89083.58622.26123.03491.30982.79350.16780.1547-0.6482-0.06140.2577-0.23620.6916-0.2877-0.42550.38060.0139-0.06280.3986-0.12230.341223.4723-53.406-23.1137
82.6504-1.6519-3.77824.21962.03719.89460.03180.77860.0724-0.95990.1533-0.7373-0.08610.4745-0.18510.4002-0.12240.21521.0625-0.1160.52242.2271-47.3791-35.9492
92.48681.0361-0.374.48024.894314.2623-0.0388-0.41950.04870.03660.00130.1939-0.08190.36590.03750.1568-0.0206-0.05130.3058-0.04250.242353.579-25.450126.5455
103.2028-1.9675-1.4713.8538-1.599911.65810.30450.62990.0544-0.2753-0.4497-0.55430.22910.21270.14520.22350.0283-0.05080.1833-0.0150.202223.0202-24.066120.1594
118.0086-6.247-3.76085.32142.66046.1638-1.1547-2.0239-0.35160.20111.2441-0.11430.78621.1085-0.08941.36640.1310.14491.61010.60651.192166.1732-64.127198.1616
1215.7895-2.8904-3.15594.24681.91891.505-1.6301-2.06470.98750.29381.19150.16520.10640.67280.43871.1717-0.1398-0.42071.93810.03770.660452.5668-52.0618105.5074
1311.7405-3.20820.6274.4301-4.98226.6019-1.00622.3176-0.6292-0.17690.95040.04580.7868-1.82880.05591.161-0.0379-0.3611.7208-0.66981.09517.3505-64.2915-49.4
1418.14350.4767-2.85233.1561-0.95421.4512-1.70672.7878-0.365-0.38820.979-0.2281-0.0364-0.890.72771.4014-0.118-0.17872.2044-0.34920.50521.5901-54.4341-56.9021
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 180
2X-RAY DIFFRACTION1A301 - 306
3X-RAY DIFFRACTION2B2 - 99
4X-RAY DIFFRACTION3C1 - 180
5X-RAY DIFFRACTION3C501 - 508
6X-RAY DIFFRACTION4D1 - 99
7X-RAY DIFFRACTION5E1 - 114
8X-RAY DIFFRACTION6F1 - 116
9X-RAY DIFFRACTION7G1 - 114
10X-RAY DIFFRACTION8H1 - 116
11X-RAY DIFFRACTION9A181 - 280
12X-RAY DIFFRACTION10C181 - 280
13X-RAY DIFFRACTION11E115 - 210
14X-RAY DIFFRACTION12F117 - 250
15X-RAY DIFFRACTION13G115 - 210
16X-RAY DIFFRACTION14H117 - 250

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