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- PDB-5jpn: Structure of human complement C4 rebuilt using iMDFF -

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Basic information

Entry
Database: PDB / ID: 5jpn
TitleStructure of human complement C4 rebuilt using iMDFF
Components(Complement C4- ...) x 3
KeywordsIMMUNE SYSTEM / complement / blood
Function / homology
Function and homology information


complement component C1q complex binding / positive regulation of apoptotic cell clearance / Activation of C3 and C5 / complement activation / endopeptidase inhibitor activity / Initial triggering of complement / complement activation, classical pathway / Regulation of Complement cascade / Post-translational protein phosphorylation / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) ...complement component C1q complex binding / positive regulation of apoptotic cell clearance / Activation of C3 and C5 / complement activation / endopeptidase inhibitor activity / Initial triggering of complement / complement activation, classical pathway / Regulation of Complement cascade / Post-translational protein phosphorylation / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / blood microparticle / inflammatory response / endoplasmic reticulum lumen / axon / innate immune response / neuronal cell body / synapse / dendrite / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
: / Complement C4, MG1 domain / Jelly Rolls - #1540 / Anaphylotoxins (complement system) / N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / Influenza Virus Matrix Protein; Chain A, domain 1 ...: / Complement C4, MG1 domain / Jelly Rolls - #1540 / Anaphylotoxins (complement system) / N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / Influenza Virus Matrix Protein; Chain A, domain 1 / S-adenosyl-L-methionine-dependent methyltransferases / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / : / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system domain / Anaphylatoxin domain signature. / Anaphylatoxin, complement system / Anaphylatoxin/fibulin / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Glycosyltransferase - #20 / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor binding domain / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor / Netrin domain / NTR domain profile. / Tissue inhibitor of metalloproteinases-like, OB-fold / Alpha-2-macroglobulin / Macroglobulin domain / Alpha-2-macroglobulin, bait region domain / Alpha-macroglobulin-like, TED domain / Alpha-2-macroglobulin family / MG2 domain / A-macroglobulin TED domain / Alpha-2-macroglobulin bait region domain / Alpha-2-Macroglobulin / Alpha-2-macroglobulin family / Other non-globular / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / Single Sheet / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Jelly Rolls / Immunoglobulins / Immunoglobulin-like fold / Up-down Bundle / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
2-acetamido-2-deoxy-alpha-D-galactopyranose / TRIMETHYL LEAD ION / Complement C4-A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.6 Å
AuthorsCroll, T.I. / Andersen, G.R.
Funding support Denmark, 2items
OrganizationGrant numberCountry
Aarhus University Research Foundation Denmark
Danish Science Research Council for Nature and Universe Denmark
Citation
Journal: Acta Crystallogr D Struct Biol / Year: 2016
Title: Re-evaluation of low-resolution crystal structures via interactive molecular-dynamics flexible fitting (iMDFF): a case study in complement C4.
Authors: Croll, T.I. / Andersen, G.R.
#1: Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2012
Title: Structural basis for activation of the complement system by component C4 cleavage.
Authors: Kidmose, R.T. / Laursen, N.S. / Dobo, J. / Kjaer, T.R. / Sirotkina, S. / Yatime, L. / Sottrup-Jensen, L. / Thiel, S. / Gal, P. / Andersen, G.R.
History
DepositionMay 3, 2016Deposition site: RCSB / Processing site: PDBE
SupersessionAug 10, 2016ID: 4FXK
Revision 1.0Aug 10, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 14, 2016Group: Database references
Revision 1.2Sep 19, 2018Group: Data collection / Category: diffrn_radiation_wavelength / Item: _diffrn_radiation_wavelength.wavelength
Revision 1.3Nov 21, 2018Group: Data collection / Category: reflns / reflns_shell / Item: _reflns.pdbx_Rsym_value / _reflns_shell.d_res_high
Revision 1.4Jan 23, 2019Group: Advisory / Data collection / Derived calculations
Category: database_PDB_rev / database_PDB_rev_record ...database_PDB_rev / database_PDB_rev_record / pdbx_data_processing_status / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / struct_conn
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / diffrn_radiation_wavelength / 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 / 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.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.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 / _diffrn_radiation_wavelength.wavelength / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _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_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_symmetry / _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_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 / _struct_conn.ptnr2_symmetry / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Complement C4-A
B: Complement C4-A
C: Complement C4-A
hetero molecules


Theoretical massNumber of molelcules
Total (without water)193,08112
Polymers189,0183
Non-polymers4,0639
Water00
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21060 Å2
ΔGint-63 kcal/mol
Surface area76330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)85.450, 103.310, 256.030
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Complement C4- ... , 3 types, 3 molecules ABC

#1: Protein Complement C4-A / Acidic complement C4 / C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2


Mass: 71761.688 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P0C0L4
#2: Protein Complement C4-A / Acidic complement C4 / C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2


Mass: 84270.055 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P0C0L4
#3: Protein Complement C4-A / Acidic complement C4 / C3 and PZP-like alpha-2-macroglobulin domain-containing protein 2


Mass: 32986.516 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P0C0L4

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Sugars , 4 types, 5 molecules

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


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#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 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.: 2
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
#8: Sugar ChemComp-A2G / 2-acetamido-2-deoxy-alpha-D-galactopyranose


Type: D-saccharide, alpha linking / Mass: 221.208 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGalpNAcaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-a-D-galactopyranosamineCOMMON NAMEGMML 1.0
a-D-GalpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GalNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 1 types, 4 molecules

#7: Chemical
ChemComp-PBM / TRIMETHYL LEAD ION


Mass: 252.304 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H9Pb

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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: 2.99 Å3/Da / Density % sol: 58.85 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.4
Details: 0.9 M sodium citrate pH 6.4, 0.25 M potassium chloride, 1% v/v ethanol, 3 % v/v acetonitrile, 6 % v/v ethylene glycol and 10 mM spermidine

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONSOLEIL PROXIMA 110.97892
SYNCHROTRONESRF ID2920.97892
Detector
TypeIDDetectorDate
ADSC QUANTUM 315r1CCDJun 14, 2011
PSI PILATUS 6M2PIXELJul 14, 2011
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray2
Radiation wavelength
IDWavelength (Å)Relative weight
10.978921
21
ReflectionResolution: 3.6→45.9 Å / Num. obs: 26960 / % possible obs: 99.6 % / Redundancy: 4.61 % / Rsym value: 0.097 / Net I/σ(I): 13.2
Reflection shellHighest resolution: 3.6 Å

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Processing

Software
NameVersionClassification
PHENIXdev_2376refinement
PDB_EXTRACT3.2data extraction
RefinementResolution: 3.6→45.896 Å / SU ML: 0.45 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 28.12
RfactorNum. reflection% reflectionSelection details
Rfree0.2629 1348 5 %Random selection
Rwork0.2147 ---
obs0.2172 26948 99.63 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 240.27 Å2 / Biso mean: 130.4851 Å2 / Biso min: 67.71 Å2
Refinement stepCycle: final / Resolution: 3.6→45.896 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12684 0 207 0 12891
Biso mean--190.43 --
Num. residues----1638
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00213192
X-RAY DIFFRACTIONf_angle_d0.60517932
X-RAY DIFFRACTIONf_chiral_restr0.0432047
X-RAY DIFFRACTIONf_plane_restr0.0042312
X-RAY DIFFRACTIONf_dihedral_angle_d15.6847992
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.6-3.72860.36351330.289425222655100
3.7286-3.87780.3481320.274625162648100
3.8778-4.05420.35121330.255325302663100
4.0542-4.26780.24641330.232725152648100
4.2678-4.5350.24411340.201225452679100
4.535-4.88480.25671330.189525312664100
4.8848-5.37570.23531350.198525662701100
5.3757-6.1520.29581360.219425872723100
6.152-7.74480.28191370.22632590272799
7.7448-45.89980.21331420.1872698284098
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)
16.7037-1.3155-0.02034.29120.06744.13580.1613-0.38560.21361.1646-0.29640.6672-0.6288-0.42980.17221.38070.080.15141.2845-0.08490.9403-60.2648-45.53362.2309
24.05751.9471-1.17874.1226-0.85925.0411-0.0142-0.13550.2270.3468-0.1346-0.1123-0.4516-0.15930.01310.96020.1175-0.00220.77270.0020.9299-43.4603-26.668133.7551
31.22751.1564-0.96192.4520.26231.81720.04080.017-0.54780.1359-0.1984-0.4959-0.3651.03440.04311.60050.15950.30552.2247-0.00112.308-7.3302-37.774727.5952
44.91982.0046-0.44441.39581.01832.525-0.32120.1763-0.3557-0.44150.0771-0.6890.77750.60620.36611.59440.33610.05881.51870.01741.7594-25.0698-63.612749.8141
56.37090.0367-0.00674.93211.95234.8480.0091-0.0236-0.67640.04890.17810.14050.85780.1374-0.11380.9570.0058-0.03420.7195-0.00850.9912-47.6974-63.142951.593
63.5491.8583-0.02383.761-0.97313.7843-0.03680.8395-0.2772-0.6099-0.0198-0.66510.38310.4932-0.03391.13670.18240.01131.0534-0.06551.0613-39.5203-39.476419.0792
73.4507-0.62260.9942.76891.77132.31250.5973-0.39851.28050.2534-0.2478-1.0068-0.93220.6392-0.26451.2363-0.07250.02661.07920.04271.253-44.0291-49.541361.3541
81.9306-0.0206-0.29652.29190.16570.90360.23750.16530.30530.6518-0.2015-1.1544-0.25691.4034-0.14941.3520.2443-0.17912.2996-0.18461.683-5.7575-6.748630.501
93.7338-0.0463-0.90983.7495-2.15173.4365-0.2792-0.093-0.5761-0.57510.18020.61370.7680.08370.02361.4083-0.04980.18161.1526-0.04151.1978-26.4675-24.1653-7.9646
100.26710.87340.45524.2951-0.78114.3610.2846-0.0504-1.0048-0.04620.6544-1.7103-0.08890.1609-0.88661.98630.0456-0.11351.88930.04622.2481-3.792-39.9952-12.0816
114.92750.454-1.09812.1519-0.55132.69010.10030.2279-0.1106-0.5601-0.04660.3327-0.4424-0.39930.05731.44790.0936-0.06481.1891-0.06021.1789-51.769910.74212.6049
121.19870.1081-0.22360.855-0.11261.7026-0.21-0.4620.3432-0.0334-0.00820.31410.1481-0.97370.15232.1763-0.0482-0.46462.0008-0.51043.8688-75.558711.06184.1782
136.933-0.71640.08213.06730.0312.56111.02050.6581.74090.24140.52980.7120.6868-1.45-1.64712.06810.00180.05052.54040.23242.4091-33.717526.7977-3.1846
142.3396-0.94390.60992.76110.17725.245-0.0888-0.00540.22740.1086-0.0110.0314-0.6035-0.1576-0.01440.92710.02540.06590.7953-0.0590.9017-45.87138.783731.8999
153.3912-0.573-4.04152.02622.1326.1658-0.1688-0.21120.25130.03340.2575-0.5401-0.06250.9909-0.09711.0131-0.097-0.01141.0178-0.03941.0235-18.8262-0.782911.837
163.19410.3168-1.73374.1032-1.70794.72040.01910.2682-0.26260.03350.06010.6274-0.1362-0.4954-0.13051.1318-0.02990.04661.1551-0.11241.1178-27.404911.9555-25.5789
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resid 20:137A20 - 137
2X-RAY DIFFRACTION2(chain A and (resid 138:238 or resid 701:703)) or (chain D and resid 2)A138 - 238
3X-RAY DIFFRACTION2(chain A and (resid 138:238 or resid 701:703)) or (chain D and resid 2)A701 - 703
4X-RAY DIFFRACTION3chain A and resid 239:364A239 - 364
5X-RAY DIFFRACTION4chain A and resid 365:468A365 - 468
6X-RAY DIFFRACTION5chain A and resid 469:568A469 - 568
7X-RAY DIFFRACTION6(chain A and resid 569:631) or (chain B and resid 768:831) or (chain D and resid 3)A569 - 631
8X-RAY DIFFRACTION6(chain A and resid 569:631) or (chain B and resid 768:831) or (chain D and resid 3)B768 - 831
9X-RAY DIFFRACTION6(chain A and resid 569:631) or (chain B and resid 768:831) or (chain D and resid 3)D3
10X-RAY DIFFRACTION7chain A and resid 632:670A632 - 670
11X-RAY DIFFRACTION8chain B and resid 697:745B697 - 745
12X-RAY DIFFRACTION9chain B and (resid 832:934)B832 - 934
13X-RAY DIFFRACTION10chain B and resid 1801:1809B1801 - 1809
14X-RAY DIFFRACTION11(chain B and (resid 935:982 or resid 1321:1392)) or (chain D and resid 4)B935 - 982
15X-RAY DIFFRACTION11(chain B and (resid 935:982 or resid 1321:1392)) or (chain D and resid 4)B1321 - 1392
16X-RAY DIFFRACTION12(chain B and resid 1810:1811)B1810 - 1811
17X-RAY DIFFRACTION13(chain B and resid 1820:1824)B1820 - 1824
18X-RAY DIFFRACTION14(chain B and resid 983:1320) or (chain B and resid 1830)B983 - 1320
19X-RAY DIFFRACTION14(chain B and resid 983:1320) or (chain B and resid 1830)B1830
20X-RAY DIFFRACTION15(chain B and resid 1393:1415) or (chain C and resid 1455:1581)B1393 - 1415
21X-RAY DIFFRACTION15(chain B and resid 1393:1415) or (chain C and resid 1455:1581)C1455 - 1581
22X-RAY DIFFRACTION16(chain C and resid 1582:1744) or (chain D and resid 1)C1582 - 1744
23X-RAY DIFFRACTION16(chain C and resid 1582:1744) or (chain D and resid 1)D1

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