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- PDB-6fgo: Fc in complex with engineered calcium binding domain Z -

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Basic information

Entry
Database: PDB / ID: 6fgo
TitleFc in complex with engineered calcium binding domain Z
Components
  • Immunoglobulin gamma-1 heavy chain
  • Z-Ca
KeywordsIMMUNE SYSTEM / Antibody / Protein A / EF-hand / calcium-binding
Function / homology
Function and homology information


immunoglobulin complex / immunoglobulin binding / : / adaptive immune response / extracellular region / plasma membrane
Similarity search - Function
Immunoglobulin FC, subunit C / Protein A, Ig-binding domain / B domain / Immunoglobulin/albumin-binding domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulin ...Immunoglobulin FC, subunit C / Protein A, Ig-binding domain / B domain / Immunoglobulin/albumin-binding domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulin / 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 / Immunoglobulins / Immunoglobulin-like fold / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Protein A / Immunoglobulin gamma-1 heavy chain
Similarity search - Component
Biological speciesHomo sapiens (human)
Staphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.5 Å
AuthorsVenskutonyte, R. / Kanje, S. / Hober, S. / Lindkvist-Petersson, K.
Funding support Sweden, 1items
OrganizationGrant numberCountry
Vinnova Sweden
CitationJournal: J. Mol. Biol. / Year: 2018
Title: Protein Engineering Allows for Mild Affinity-based Elution of Therapeutic Antibodies.
Authors: Kanje, S. / Venskutonyte, R. / Scheffel, J. / Nilvebrant, J. / Lindkvist-Petersson, K. / Hober, S.
History
DepositionJan 11, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 20, 2018Provider: repository / Type: Initial release
Revision 1.1Aug 29, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
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 / 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_struct_conn_angle / pdbx_validate_close_contact / 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_struct_conn_angle.ptnr2_label_asym_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_atom_id_1 / _pdbx_validate_close_contact.auth_atom_id_2 / _pdbx_validate_close_contact.auth_comp_id_1 / _pdbx_validate_close_contact.auth_comp_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.conn_type_id / _struct_conn.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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 17, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Immunoglobulin gamma-1 heavy chain
E: Z-Ca
B: Immunoglobulin gamma-1 heavy chain
F: Z-Ca
C: Immunoglobulin gamma-1 heavy chain
G: Z-Ca
D: Immunoglobulin gamma-1 heavy chain
H: Z-Ca
hetero molecules


Theoretical massNumber of molelcules
Total (without water)133,43445
Polymers125,9458
Non-polymers7,48937
Water3,225179
1
A: Immunoglobulin gamma-1 heavy chain
E: Z-Ca
C: Immunoglobulin gamma-1 heavy chain
G: Z-Ca
hetero molecules


Theoretical massNumber of molelcules
Total (without water)67,33225
Polymers62,9734
Non-polymers4,35921
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Immunoglobulin gamma-1 heavy chain
F: Z-Ca
D: Immunoglobulin gamma-1 heavy chain
H: Z-Ca
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,10220
Polymers62,9734
Non-polymers3,13016
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)90.229, 120.296, 126.330
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain E and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))
21(chain F and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))
31(chain G and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))
41(chain H and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))
12(chain A and resid 237 through 444)
22(chain B and resid 237 through 444)
32chain C
42chain D

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111LEULEUASNASN(chain E and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))EB5 - 235 - 23
121GLUGLUGLNGLN(chain E and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))EB25 - 2625 - 26
131LYSLYSARGARG(chain E and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))EB28 - 6628 - 66
211LEULEUASNASN(chain F and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))FD5 - 235 - 23
221GLUGLUGLNGLN(chain F and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))FD25 - 2625 - 26
231LYSLYSARGARG(chain F and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))FD28 - 6628 - 66
311LEULEUASNASN(chain G and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))GF5 - 235 - 23
321GLUGLUGLNGLN(chain G and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))GF25 - 2625 - 26
331LYSLYSARGARG(chain G and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))GF28 - 6628 - 66
411LEULEUASNASN(chain H and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))HH5 - 235 - 23
421GLUGLUGLNGLN(chain H and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))HH25 - 2625 - 26
431LYSLYSARGARG(chain H and (resid 5 through 23 or resid 25 through 26 or resid 28 through 66))HH28 - 6628 - 66
112GLYGLYSERSER(chain A and resid 237 through 444)AA237 - 4441 - 208
212GLYGLYSERSER(chain B and resid 237 through 444)BC237 - 4441 - 208
312GLYGLYSERSERchain CCE237 - 4441 - 208
412GLYGLYSERSERchain DDG237 - 4441 - 208

NCS ensembles :
ID
1
2

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Components

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Antibody / Protein , 2 types, 8 molecules ABCDEFGH

#1: Antibody
Immunoglobulin gamma-1 heavy chain / Immunoglobulin gamma-1 heavy chain NIE


Mass: 23820.906 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P0DOX5
#2: Protein
Z-Ca


Mass: 7665.391 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: A0A0U3TLJ6*PLUS

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Sugars , 3 types, 4 molecules

#3: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)]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: 1463.349 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-2DManpa1-3[DGlcpNAcb1-2DManpa1-6]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,8,7/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-1-3-1-4/a4-b1_a6-h1_b4-c1_c3-d1_c6-f1_d2-e1_f2-g1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{}}[(6+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{}}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]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: 1260.157 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-2DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-3-1-4/a4-b1_a6-g1_b4-c1_c3-d1_c6-e1_e2-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{}}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE

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Non-polymers , 5 types, 212 molecules

#6: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C4H10O3
#7: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#9: Chemical
ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Cl
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 179 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.72 Å3/Da / Density % sol: 54.81 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6 / Details: 24 % PEG3350, 0.1 M LiCl2, 0.1 M MES pH 6.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jun 24, 2017 / Details: Toroidal mirror
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.5→47.53 Å / Num. obs: 47055 / % possible obs: 98 % / Redundancy: 4.4 % / Biso Wilson estimate: 52.03 Å2 / Rpim(I) all: 0.03 / Rrim(I) all: 0.067 / Rsym value: 0.06 / Net I/av σ(I): 10.2 / Net I/σ(I): 13.8
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsRpim(I) allRrim(I) allRsym value% possible all
2.5-2.644.40.421.868820.2130.4740.4299.3
2.64-2.84.30.2822.765080.1450.3190.28298.9
2.8-2.994.30.1734.461010.0890.1960.17398.8
2.99-3.234.50.1126.656880.0560.1260.11298.5
3.23-3.544.40.06910.552130.0340.0770.06998.1
3.54-3.954.30.0531347100.0270.060.05397.7
3.95-4.564.60.04315.541700.0220.0480.04397.1
4.56-5.594.20.03916.935000.020.0440.03996.3
5.59-7.914.50.03617.927410.0180.0410.03696.1
7.91-46.5294.20.03118.415420.0160.0350.03193.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
XDSdata reduction
SCALA3.3.21data scaling
PHASERphasing
PHENIX1.12-2829refinement
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5U4Y

5u4y


Resolution: 2.5→46.529 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 0.99 / Phase error: 23.72
Details: NCS and TLS used. Riding hydrogens were used during refinement, but were removed prior deposition.
RfactorNum. reflection% reflection
Rfree0.2319 2256 4.8 %
Rwork0.2035 --
obs0.2048 47032 97.4 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 157.85 Å2 / Biso mean: 65.1984 Å2 / Biso min: 24.81 Å2
Refinement stepCycle: final / Resolution: 2.5→46.529 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8705 0 482 181 9368
Biso mean--73.66 44.13 -
Num. residues----1094
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0039414
X-RAY DIFFRACTIONf_angle_d0.57512714
X-RAY DIFFRACTIONf_chiral_restr0.0421433
X-RAY DIFFRACTIONf_plane_restr0.0031606
X-RAY DIFFRACTIONf_dihedral_angle_d17.9045747
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11E1379X-RAY DIFFRACTION10.404TORSIONAL
12F1379X-RAY DIFFRACTION10.404TORSIONAL
13G1379X-RAY DIFFRACTION10.404TORSIONAL
14H1379X-RAY DIFFRACTION10.404TORSIONAL
21A5196X-RAY DIFFRACTION10.404TORSIONAL
22B5196X-RAY DIFFRACTION10.404TORSIONAL
23C5196X-RAY DIFFRACTION10.404TORSIONAL
24D5196X-RAY DIFFRACTION10.404TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 16

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.5-2.55440.29031360.27552814295099
2.5544-2.61380.33741640.27672770293499
2.6138-2.67910.32191400.27022799293999
2.6791-2.75160.28781590.26162794295399
2.7516-2.83250.28761450.25862750289598
2.8325-2.92390.34951540.25672802295699
2.9239-3.02840.28341430.26082788293198
3.0284-3.14960.27531230.24782816293998
3.1496-3.2930.25431520.23622796294898
3.293-3.46650.2331300.22832781291198
3.4665-3.68360.24931290.20772802293197
3.6836-3.96790.20331280.18432817294597
3.9679-4.36690.20091260.17182797292397
4.3669-4.99820.20171320.14822794292696
4.9982-6.29470.21921470.17662795294295
6.2947-46.53710.1731480.18452861300993
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)
12.2708-0.8611-0.58162.30831.82263.5233-0.08280.0150.31090.0512-0.04210.1474-0.1831-0.15440.12170.3157-0.0037-0.0030.19560.00320.436396.094135.836557.8989
23.46642.6752-1.56065.7648-3.25015.03270.0658-0.0301-0.26510.1978-0.05830.03330.0967-0.0501-0.02310.28370.00560.00850.1769-0.03070.4328108.27628.660568.0387
32.07390.9329-1.74935.4689-5.44726.9164-0.0534-0.0176-0.32330.0562-0.2356-0.34660.0988-0.290.3170.4041-0.0127-0.03230.2619-0.06220.5206105.41483.289760.6851
47.55394.5109-1.13763.24340.42926.56290.1942-0.2746-0.24710.0339-0.22050.02150.41450.42620.18060.46560.0673-0.04170.3271-0.03920.473699.686710.054946.4066
53.96834.25330.09336.435-0.18454.9424-0.17640.49380.1588-0.60310.12980.3346-0.21460.21250.08920.49060.0539-0.03010.3367-0.01930.330495.530916.630738.1645
68.36363.7527-2.77225.1445-5.62276.62170.14211.2737-0.1644-0.61320.28770.28660.2117-0.0413-0.28120.64580.06510.02810.5837-0.20240.4839100.037410.90432.7752
71.7407-1.2832-2.54152.44181.67753.99330.34751.3499-0.3278-0.5924-0.40050.29360.1974-0.02630.1720.55890.1429-0.06840.5993-0.31040.4663124.849626.872733.9817
82.25961.24160.84153.0553.00847.0878-0.11670.3913-1.0313-0.2767-0.42310.26331.5298-0.10240.14060.92470.16140.01950.5933-0.28220.8549129.785312.700434.3166
91.22081.05062.60221.13962.61896.7120.01030.2827-0.52611.58350.4426-0.46361.5676-0.4768-0.52840.87180.1413-0.17481.0471-0.57541.0564118.584110.604923.1197
100.3404-0.6343-0.83796.58262.39542.7429-0.080.7987-0.6029-0.2990.0315-0.410.50980.58580.00930.58960.2040.05790.7114-0.24930.6553132.920320.874934.8273
115.1913-2.22131.17485.9564-0.31616.1002-0.49460.16371.2477-0.03440.1912-0.4845-0.7857-0.12340.28640.4798-0.0490.15540.53730.12510.316119.428451.406426.7528
125.2818-4.63552.64888.7633-2.88227.04910.44850.3301-0.217-0.2102-0.09810.3704-0.05550.0708-0.3640.4496-0.01560.03590.5007-0.0330.3417118.569646.738929.2431
133.787-0.49021.61362.1271-0.94795.4056-0.01180.17480.31230.06130.15850.2534-0.1805-0.5406-0.17940.37540.03260.05940.41350.05970.4182114.690248.761530.6655
142.92541.821-3.82917.6123-0.61856.45160.10250.1618-0.02590.59370.10530.41240.0126-0.3826-0.35210.35470.05350.06790.2940.00940.3733120.152841.833847.9828
157.4951-0.4536-1.69751.8153-1.05231.6329-0.3959-0.5176-0.35160.00810.1224-0.23040.2720.21850.14270.46010.0219-0.01140.2955-0.04730.3565125.277834.168855.7185
166.14373.0552-1.98477.2940.47297.28460.198-0.51990.48880.2717-0.04260.2295-0.53760.2529-0.22350.48580.0609-0.00980.3225-0.04870.3909128.135341.610760.3202
173.367-0.09560.25594.2662-1.50054.4730.08180.09660.3496-0.03560.1229-0.00870.282-0.5123-0.20940.3411-0.00980.00260.5005-0.03070.3128119.288340.883686.4865
183.0417-2.0489-1.15655.28262.77174.25790.1503-0.3305-0.26310.25820.0982-0.3604-0.05720.2499-0.20770.4696-0.0927-0.00330.29350.03710.5113117.239310.797677.5253
194.523-1.9041-2.39815.54673.47217.5364-0.0401-0.6452-0.43130.9556-0.094-0.17660.05150.9022-0.19580.5565-0.1065-0.09210.47680.05230.5067121.76657.814585.4839
201.9957-1.66661.33895.231.99384.9862-0.36230.1657-0.09360.25640.4272-0.52710.34210.795-0.0441.1053-0.0318-0.03670.5311-0.03040.4834123.897715.794699.3456
218.8746-1.5226-7.9643.72091.05977.206-0.25340.34110.59710.93370.3644-0.0793-0.1461-1.3247-0.05170.9546-0.0913-0.11130.8839-0.0380.3601119.419624.6358108.4982
228.2883-2.4924-0.0248.9165-3.7689.38430.2362-1.45370.51511.0586-0.7144-1.1210.58821.210.3180.79590.0202-0.20140.86510.01010.6721136.255720.7936104.527
237.69260.199-4.7162.85881.16463.47140.0206-2.19090.04280.77540.0535-0.25510.92850.57230.1511.29530.1009-0.03541.01410.19120.5385122.575415.8247112.4936
244.0492-1.9773-0.58124.1914-1.62290.9123-0.1737-0.12470.07910.0521-0.0245-0.63310.41570.44490.13030.87260.2145-0.06681.0805-0.04790.446133.108830.3235-0.1403
251.90530.76321.22653.15280.90484.03720.11450.43240.3486-0.2749-0.0461-0.0395-0.63840.2679-0.0830.5909-0.02880.05290.73090.13070.483119.412154.188113.2059
268.5828-0.42884.54842.18433.29638.5421-0.13660.57661.5566-0.8957-0.8309-0.4495-0.9387-0.49260.72810.88760.1171-0.01991.03030.21660.6892116.860352.2351-9.0989
275.8694-1.46344.45577.04762.5976.0780.37740.8849-0.2099-0.6175-0.1581-0.28651.0932-0.2242-0.12760.69320.01330.09571.22530.09610.3612114.520642.2446-16.6904
286.05072.7655-3.23815.128-4.65024.8686-0.63592.10842.3595-1.2831-0.1497-1.49360.16771.33430.91850.6554-0.11290.0781.44540.39471.093126.826254.5552-19.8039
293.29530.233.70537.00863.82948.6834-0.0052-0.1870.2004-0.7367-0.4892-0.5591-0.7231-1.07790.54550.7790.21940.04440.91680.2080.4972110.78450.9539-20.1344
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 237 through 336 )A237 - 336
2X-RAY DIFFRACTION2chain 'A' and (resid 337 through 418 )A337 - 418
3X-RAY DIFFRACTION3chain 'A' and (resid 419 through 445 )A419 - 445
4X-RAY DIFFRACTION4chain 'E' and (resid 3 through 18 )E3 - 18
5X-RAY DIFFRACTION5chain 'E' and (resid 19 through 48 )E19 - 48
6X-RAY DIFFRACTION6chain 'E' and (resid 49 through 66 )E49 - 66
7X-RAY DIFFRACTION7chain 'B' and (resid 237 through 263 )B237 - 263
8X-RAY DIFFRACTION8chain 'B' and (resid 264 through 290 )B264 - 290
9X-RAY DIFFRACTION9chain 'B' and (resid 291 through 301 )B291 - 301
10X-RAY DIFFRACTION10chain 'B' and (resid 302 through 336 )B302 - 336
11X-RAY DIFFRACTION11chain 'B' and (resid 337 through 361 )B337 - 361
12X-RAY DIFFRACTION12chain 'B' and (resid 362 through 383 )B362 - 383
13X-RAY DIFFRACTION13chain 'B' and (resid 384 through 445 )B384 - 445
14X-RAY DIFFRACTION14chain 'F' and (resid 1 through 18 )F1 - 18
15X-RAY DIFFRACTION15chain 'F' and (resid 19 through 48 )F19 - 48
16X-RAY DIFFRACTION16chain 'F' and (resid 49 through 67 )F49 - 67
17X-RAY DIFFRACTION17chain 'C' and (resid 237 through 336 )C237 - 336
18X-RAY DIFFRACTION18chain 'C' and (resid 337 through 418 )C337 - 418
19X-RAY DIFFRACTION19chain 'C' and (resid 419 through 444 )C419 - 444
20X-RAY DIFFRACTION20chain 'G' and (resid 4 through 18 )G4 - 18
21X-RAY DIFFRACTION21chain 'G' and (resid 19 through 34 )G19 - 34
22X-RAY DIFFRACTION22chain 'G' and (resid 35 through 48 )G35 - 48
23X-RAY DIFFRACTION23chain 'G' and (resid 49 through 68 )G49 - 68
24X-RAY DIFFRACTION24chain 'D' and (resid 237 through 336 )D237 - 336
25X-RAY DIFFRACTION25chain 'D' and (resid 337 through 444 )D337 - 444
26X-RAY DIFFRACTION26chain 'H' and (resid 5 through 18 )H5 - 18
27X-RAY DIFFRACTION27chain 'H' and (resid 19 through 34 )H19 - 34
28X-RAY DIFFRACTION28chain 'H' and (resid 35 through 48 )H35 - 48
29X-RAY DIFFRACTION29chain 'H' and (resid 49 through 68 )H49 - 68

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