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- PDB-5jpm: Structure of the complex of human complement C4 with MASP-2 rebui... -

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Basic information

Entry
Database: PDB / ID: 5jpm
TitleStructure of the complex of human complement C4 with MASP-2 rebuilt using iMDFF
Components
  • (Complement C4- ...) x 3
  • (Mannan-binding lectin serine protease ...) x 2
KeywordsIMMUNE SYSTEM / complement / blood
Function / homology
Function and homology information


mannan-binding lectin-associated serine protease-2 / complement component C4b binding / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / complement component C1q complex binding / complement activation, lectin pathway / positive regulation of apoptotic cell clearance / Activation of C3 and C5 / complement activation / endopeptidase inhibitor activity ...mannan-binding lectin-associated serine protease-2 / complement component C4b binding / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / complement component C1q complex binding / complement activation, lectin pathway / 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) / calcium-dependent protein binding / peptidase activity / blood microparticle / inflammatory response / endoplasmic reticulum lumen / axon / innate immune response / serine-type endopeptidase activity / neuronal cell body / synapse / dendrite / calcium ion binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / proteolysis / extracellular space / extracellular exosome / extracellular region / identical protein binding / plasma membrane
Similarity search - Function
: / : / Complement C4, MG1 domain / Complement C4A/B CUB C-terminal domain / Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / Anaphylotoxins (complement system) / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Alpha-macroglobulin, receptor-binding domain / S-adenosyl-L-methionine-dependent methyltransferases ...: / : / Complement C4, MG1 domain / Complement C4A/B CUB C-terminal domain / Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / Anaphylotoxins (complement system) / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Alpha-macroglobulin, receptor-binding domain / S-adenosyl-L-methionine-dependent methyltransferases / Influenza Virus Matrix Protein; Chain A, domain 1 / Macroglobulin (MG2) domain / Immunoglobulin-like - #1940 / Peptidase S1A, complement C1r/C1S/mannan-binding / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Anaphylatoxin, complement system domain / Complement Module, domain 1 / : / Anaphylatoxin domain signature. / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system / Anaphylatoxin/fibulin / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Complement Module; domain 1 / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Macroglobulin domain MG4 / Macroglobulin domain MG4 / CUB domain / Domain first found in C1r, C1s, uEGF, and bone morphogenetic protein. / CUB domain / CUB domain profile. / Glycosyltransferase - #20 / Netrin domain / NTR domain profile. / Alpha-macroglobulin, receptor-binding / Spermadhesin, CUB domain superfamily / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG3 / : / A-macroglobulin receptor binding domain / Macroglobulin domain MG3 / A-macroglobulin receptor / 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 / : / Calcium-binding EGF domain / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / EGF-type aspartate/asparagine hydroxylation site / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Epidermal growth factor-like domain. / Single Sheet / EGF-like domain signature 2. / EGF-like domain / Special / Ribbon / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Trypsin-like serine proteases / Thrombin, subunit H / Jelly Rolls / Peptidase S1, PA clan, chymotrypsin-like fold / Immunoglobulin-like fold / Peptidase S1, PA clan / Immunoglobulins / Up-down Bundle / Beta Barrel
Similarity search - Domain/homology
Mannan-binding lectin serine protease 2 / Complement C4-A
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.75 Å
AuthorsCroll, T.I. / Andersen, G.R.
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: 4FXG
Revision 1.0Aug 10, 2016Provider: repository / Type: Initial release
Revision 1.1Sep 14, 2016Group: Database references
Revision 1.2Sep 28, 2016Group: Database references
Revision 1.3Feb 20, 2019Group: Advisory / Data collection / Derived calculations
Category: pdbx_data_processing_status / pdbx_unobs_or_zero_occ_atoms ...pdbx_data_processing_status / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / struct_conn
Revision 1.4Oct 16, 2019Group: Data collection / Category: reflns_shell
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 / 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 / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 23, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
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: Complement C4-A
B: Complement C4-A
C: Complement C4-A
D: Complement C4-A
E: Complement C4-A
F: Complement C4-A
G: Mannan-binding lectin serine protease 2
H: Mannan-binding lectin serine protease 2
I: Mannan-binding lectin serine protease 2
J: Mannan-binding lectin serine protease 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)468,73416
Polymers465,21510
Non-polymers3,5196
Water00
1
A: Complement C4-A
B: Complement C4-A
C: Complement C4-A
I: Mannan-binding lectin serine protease 2
J: Mannan-binding lectin serine protease 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)234,3678
Polymers232,6075
Non-polymers1,7603
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25380 Å2
ΔGint-107 kcal/mol
Surface area92970 Å2
MethodPISA
2
D: Complement C4-A
E: Complement C4-A
F: Complement C4-A
G: Mannan-binding lectin serine protease 2
H: Mannan-binding lectin serine protease 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)234,3678
Polymers232,6075
Non-polymers1,7603
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25130 Å2
ΔGint-114 kcal/mol
Surface area92340 Å2
MethodPISA
Unit cell
Length a, b, c (Å)99.010, 215.010, 142.860
Angle α, β, γ (deg.)90.00, 110.11, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Complement C4- ... , 3 types, 6 molecules ADBECF

#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.: 2 / 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: 84430.180 Da / Num. of mol.: 2 / 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: 33115.629 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P0C0L4

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Mannan-binding lectin serine protease ... , 2 types, 4 molecules GIHJ

#4: Protein Mannan-binding lectin serine protease 2 / MBL-associated serine protease 2 / Mannose-binding protein-associated serine protease 2 / MASP-2


Mass: 16773.002 Da / Num. of mol.: 2 / Mutation: Q298H, P299A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MASP2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: O00187, mannan-binding lectin-associated serine protease-2
#5: Protein Mannan-binding lectin serine protease 2 / MBL-associated serine protease 2 / Mannose-binding protein-associated serine protease 2 / MASP-2


Mass: 26526.971 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MASP2 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: O00187, mannan-binding lectin-associated serine protease-2

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Sugars , 1 types, 6 molecules

#6: 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.: 6
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

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Details

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: 3.07 Å3/Da / Density % sol: 59.93 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 100 mM Tris-HCl pH 8.0, 2% v/v 1,4-dioxane and 12-14% w/v PEG3350

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONESRF ID2910.97625
SYNCHROTRONSOLEIL PROXIMA 120.9883
Detector
TypeIDDetectorDate
PSI PILATUS 6M1PIXELJul 4, 2011
ADSC QUANTUM 315r2CCDJun 14, 2011
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray2
Radiation wavelength
IDWavelength (Å)Relative weight
10.976251
20.98831
ReflectionResolution: 3.75→48.98 Å / Num. obs: 56637 / % possible obs: 98.45 % / Redundancy: 3.92 % / Net I/σ(I): 9.45

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Processing

SoftwareName: PHENIX / Version: (dev_2376) / Classification: refinement
RefinementResolution: 3.75→48.973 Å / SU ML: 0.48 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 28.58
RfactorNum. reflection% reflectionSelection details
Rfree0.2682 1727 3.05 %Random selection
Rwork0.2116 ---
obs0.2133 56608 98.56 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 3.75→48.973 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms31980 0 234 0 32214
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00232994
X-RAY DIFFRACTIONf_angle_d0.544852
X-RAY DIFFRACTIONf_dihedral_angle_d13.82819894
X-RAY DIFFRACTIONf_chiral_restr0.045012
X-RAY DIFFRACTIONf_plane_restr0.0035816
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.75-3.86030.3421670.30544491X-RAY DIFFRACTION97
3.8603-3.98480.33481480.28834452X-RAY DIFFRACTION97
3.9848-4.12720.29561350.26694384X-RAY DIFFRACTION95
4.1272-4.29230.31361410.24554555X-RAY DIFFRACTION99
4.2923-4.48760.25931290.22244613X-RAY DIFFRACTION99
4.4876-4.7240.29061540.20974594X-RAY DIFFRACTION99
4.724-5.01970.32561170.20364610X-RAY DIFFRACTION99
5.0197-5.40680.27051520.21634624X-RAY DIFFRACTION100
5.4068-5.95010.3141420.22354636X-RAY DIFFRACTION100
5.9501-6.80910.26971670.22864601X-RAY DIFFRACTION100
6.8091-8.57120.21671320.19784644X-RAY DIFFRACTION99
8.5712-48.97730.21041430.1554677X-RAY DIFFRACTION99
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)
14.7199-1.03792.47135.24920.79814.5757-0.0787-0.70910.52960.5238-0.13790.5946-0.1533-0.90390.17631.1730.15280.09672.30570.05291.236414.3338-10.1189-1.2817
24.43681.12941.78833.7901-1.08867.60040.0816-0.6432-0.47980.00380.05520.125-0.026-0.209-0.16710.99820.0682-0.10221.24250.00391.211112.7807-14.0353-39.8648
35.94986.3674-5.3936.8242-5.79424.93761.27520.23063.6235-0.20650.7085-3.38340.10370.8616-2.251.8655-1.0774-0.14222.12890.17482.238920.0397-0.79-30.9125
45.17811.75133.7583.85621.59244.8112-0.234-0.2933-0.3375-0.0190.0803-0.2306-0.08390.65690.15911.2515-0.03020.22711.72290.18081.360945.524-4.0284-56.6527
52.9533-0.903-1.81112.11420.06446.99950.16640.50670.38260.07280.1168-0.3371-0.10860.2803-0.24311.2595-0.236-0.06491.44760.21691.417151.7576-7.0831-19.0564
62.53281.8709-1.69374.378-0.45334.64710.1223-0.039-0.9311-0.8188-0.12040.3451.01750.49310.06771.61460.1817-0.24311.54890.12171.637823.1877-32.4761-45.4373
76.9384-1.50370.64565.605-0.02837.4287-0.2025-0.2272-0.1880.0660.3757-0.32910.17220.151-0.19420.9845-0.0623-0.08381.070.16921.017936.2103-18.6858-6.0445
80.78240.80881.57941.54791.73483.0938-0.18090.17730.528-0.649-0.40740.0836-2.2737-2.18070.61331.70140.2353-0.13381.8030.13081.432327.8331-9.2882-19.9974
95.24331.21650.43323.4983-1.61225.29520.3399-0.53060.2657-0.6828-0.45-0.09980.27220.68310.21681.10010.1266-0.07810.96040.00361.182131.791310.7113-70.9887
109.0712-5.05631.61766.247-2.23193.80350.0691-0.3811-0.6350.17290.02-0.08510.28950.4361-0.1131.4789-0.0539-0.071.129-0.09181.206622.3388-30.7385-79.3287
110.20531.1042-0.19216.1533-1.88183.3960.69330.468-0.0233-0.6215-2.175-0.65951.1681-0.69941.3533.04111.26420.33966.59180.53021.964849.2235-30.1275-80.5101
127.23072.3226-4.6963.6522-2.69766.2292-0.458-0.0815-0.4817-0.72950.12940.62190.8018-0.91020.28991.2165-0.1303-0.18281.3097-0.0821.1549-19.5116-17.4793-77.6024
130.5566-0.5323-1.35335.31255.11046.31260.44110.7139-1.39870.53890.0826-0.26170.43740.6812-0.69571.4363-0.6734-0.13224.49950.64422.656-38.707-30.48-66.0314
145.17830.54070.94345.22541.29593.0816-0.2831-0.3080.5612-0.08730.07540.5996-0.5717-0.70380.17291.01310.1854-0.04181.1358-0.03790.8777-13.18633.2433-56.3693
157.1109-2.0455-2.05776.78421.55156.36810.10320.14440.6315-0.6010.0147-0.2177-0.460.287-0.10581.0561-0.0354-0.1920.8270.0390.859312.9004-0.0238-79.4628
166.3226-1.214-1.03743.58342.3867.91230.0145-0.2095-0.03-0.17580.0931-0.09660.03940.1434-0.10181.006-0.124-0.0670.71190.04620.8345-1.4928-22.5627-110.0949
177.29190.4095-0.27356.6275-1.90764.0233-0.1948-0.3283-0.19570.41590.2241-0.55740.65930.6747-0.09060.96980.1089-0.14821.398-0.03971.1488-15.110139.7573-58.7419
184.08040.91291.43794.47673.07358.14350.1922-0.24580.19730.1079-0.1462-0.36410.15210.3456-0.09071.03750.06240.13571.1160.18861.2123-13.964343.2885-97.1483
195.0771.16344.16712.3677-1.03866.84990.5484-0.3994-2.32911.94810.3595.13311.1497-0.2589-0.6491.3319-0.19720.2652.79140.87762.4078-21.262131.0737-87.7293
208.83331.5809-1.84495.4416-0.06623.8564-0.14250.4275-0.55440.03590.0191-0.04780.3016-0.55970.061.1805-0.0672-0.08281.60290.01131.3372-46.939334.0147-113.3469
213.13830.62562.27272.6090.20427.3166-0.47140.58570.1736-0.26460.4832-0.0629-0.0939-0.57830.01831.1142-0.14970.07261.3927-0.1091.195-52.704137.0517-75.9609
223.7147-0.0071-1.3126.74160.54434.2887-0.1278-0.17820.2061-0.09550.2022-0.21310.0616-0.4795-0.0710.85340.06510.00650.8515-0.12121.0879-36.746648.3804-63.0604
232.7918-0.70353.33794.55711.65186.7702-0.07270.19840.8221-0.452-0.5298-0.17-1.3388-0.08890.63431.4237-0.01830.19441.17410.14011.4992-23.993261.955-102.7674
241.052-0.2299-0.71240.742-1.17677.78420.13220.79320.0148-0.5645-0.38790.08592.06280.7280.31511.38980.11120.17191.5301-0.01091.3914-28.840739.07-77.1766
259.4555-4.6413-3.34.30691.85643.6961-0.67770.2705-0.8777-0.36950.07560.83511.1427-0.85190.59461.4392-0.18720.10141.5126-0.14391.5918-33.7618.1927-127.2773
267.0872-3.5045-2.36444.63111.63785.8285-0.00620.06820.32480.31020.06730.2901-0.7617-0.3876-0.11121.44580.17350.1351.30950.17821.161-23.600159.5682-136.5042
279.2654-2.8243-1.3397.8786-4.40164.2525-0.16220.20410.3309-5.2104-2.61642.72260.736-0.6442.72813.14380.2418-0.7842.6805-0.52272.3093-49.694159.8283-139.0623
285.95462.97233.97913.8912.73697.7030.20860.25180.3101-0.4422-0.1603-0.9035-0.44920.7007-0.08171.24070.21550.27481.29080.2041.402818.182345.5475-134.5932
292.3358-2.3361-0.62325.5601-0.73354.81440.47171.2418-2.17170.06861.6098-0.9855-1.318-1.6652-1.74021.5865-0.62230.21393.5198-0.38442.606837.558258.2532-122.021
304.52230.6838-0.97664.6341-1.36664.5893-0.3798-0.0237-0.8388-0.05120.0144-0.77950.92730.63580.26321.03040.27340.07330.93720.10230.97811.324825.0403-113.162
318.3902-0.19562.04558.2465-3.17417.76720.02780.4523-0.5976-0.7921-0.02630.02330.9978-0.37650.04121.1311-0.04730.28880.957-0.09490.8899-14.72328.6228-136.3421
327.3199-0.8849-0.192.9063-2.05858.2782-0.0317-0.32650.03010.03830.11760.1228-0.167-0.3763-0.07170.93710.00280.0570.7936-0.08660.9140.16351.305-166.8624
332.52531.7348-0.7764.3151-1.07093.3813-0.62360.42850.3964-0.65970.2543-0.4566-0.0243-0.31840.27141.9286-0.0141-0.08171.52730.13511.4290.66167.2792-204.3743
345.21581.3905-4.13482.791-0.34563.4881-0.03-0.3556-0.4548-0.24540.02920.10410.569-0.8855-0.07441.3531-0.2603-0.02711.94710.00061.4617-24.512446.277-186.827
351.4174-0.3674-3.36568.4626-2.87699.6349-0.2939-0.5593-0.14050.7416-0.0349-0.092-0.2623-0.16620.29791.3696-0.1613-0.14362.62540.21391.5881-46.638733.6607-158.4469
364.5104-2.27510.09436.3361-0.24691.5933-0.60610.9004-0.9921-1.12280.94280.34720.8297-0.3129-0.31112.2839-0.5107-0.05251.5509-0.1861.3017-2.1192-37.8645-147.7808
375.05253.35182.58365.33210.76334.1163-0.07471.15170.0603-0.02330.7479-0.24710.64221.166-0.58181.429-0.06360.02872.0697-0.05321.223523.2308-17.3762-129.8477
388.11061.36580.42097.66421.44026.3817-0.55990.3261-0.30590.47660.8065-0.88410.64491.4154-0.12470.94860.2218-0.06351.4358-0.10321.121245.2182-5.7124-100.8677
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A and resid 20:139
2X-RAY DIFFRACTION2chain A and resid 140:238
3X-RAY DIFFRACTION3chain A and resid 701:703
4X-RAY DIFFRACTION4chain A and resid 239:362
5X-RAY DIFFRACTION5chain A and resid 363:468
6X-RAY DIFFRACTION6(chain A and resid 569:605) or (chain B and resid 773:831)
7X-RAY DIFFRACTION7chain A and resid 469:568
8X-RAY DIFFRACTION8chain A and resid 606:670
9X-RAY DIFFRACTION9chain B and resid 681:772
10X-RAY DIFFRACTION10chain B and resid 832:934
11X-RAY DIFFRACTION11chain B and resid 1501:1503
12X-RAY DIFFRACTION12chain B and (resid 935:982 or resid 1321:1392)
13X-RAY DIFFRACTION13chain B and resid 1504:1506
14X-RAY DIFFRACTION14chain B and resid 983:1320
15X-RAY DIFFRACTION15(chain B and resid 1393:1420) or (chain C and resid 1458:1581)
16X-RAY DIFFRACTION16chain C and resid 1582:1744
17X-RAY DIFFRACTION17chain D and resid 20:139
18X-RAY DIFFRACTION18chain D and resid 140:238
19X-RAY DIFFRACTION19chain D and resid 701:703
20X-RAY DIFFRACTION20chain D and resid 239:362
21X-RAY DIFFRACTION21chain D and resid 363:468
22X-RAY DIFFRACTION22chain D and resid 469:568
23X-RAY DIFFRACTION23(chain D and resid 569:605) or (chain E and resid 773:831)
24X-RAY DIFFRACTION24chain D and resid 606:670
25X-RAY DIFFRACTION25chain E and resid 681:772
26X-RAY DIFFRACTION26chain E and resid 832:934
27X-RAY DIFFRACTION27chain E and resid 1501:1503
28X-RAY DIFFRACTION28chain E and (resid 935:982 or resid 1321:1392)
29X-RAY DIFFRACTION29chain E and resid 1504:1506
30X-RAY DIFFRACTION30chain E and resid 983:1320
31X-RAY DIFFRACTION31(chain E and resid 1393:1420) or (chain F and resid 1458:1581)
32X-RAY DIFFRACTION32chain F and resid 1582:1744
33X-RAY DIFFRACTION33chain G and resid 296:364
34X-RAY DIFFRACTION34chain G and resid 365:432
35X-RAY DIFFRACTION35(chain G and resid 433:440) or (chain H and resid 445:686)
36X-RAY DIFFRACTION36chain I and resid 296:364
37X-RAY DIFFRACTION37chain I and resid 365:432
38X-RAY DIFFRACTION38(chain I and resid 433:440) or (chain J and resid 445:686)

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