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- PDB-3cu7: Human Complement Component 5 -

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Basic information

Entry
Database: PDB / ID: 3cu7
TitleHuman Complement Component 5
ComponentsComplement C5Complement component 5
KeywordsIMMUNE SYSTEM / MG domain / complement / inflammation / anaphylatoxin / Cleavage on pair of basic residues / Complement alternate pathway / Complement pathway / Cytolysis / Glycoprotein / Immune response / Inflammatory response / Innate immunity / Membrane attack complex / Secreted
Function / homology
Function and homology information


Terminal pathway of complement / membrane attack complex / Activation of C3 and C5 / negative regulation of macrophage chemotaxis / complement activation, alternative pathway / chemokine activity / endopeptidase inhibitor activity / positive regulation of vascular endothelial growth factor production / complement activation, classical pathway / positive regulation of chemokine production ...Terminal pathway of complement / membrane attack complex / Activation of C3 and C5 / negative regulation of macrophage chemotaxis / complement activation, alternative pathway / chemokine activity / endopeptidase inhibitor activity / positive regulation of vascular endothelial growth factor production / complement activation, classical pathway / positive regulation of chemokine production / Peptide ligand-binding receptors / Regulation of Complement cascade / chemotaxis / G alpha (i) signalling events / killing of cells of another organism / cell surface receptor signaling pathway / inflammatory response / G protein-coupled receptor signaling pathway / signaling receptor binding / extracellular space / extracellular exosome / extracellular region
Similarity search - Function
Pheromone ER-1 / Pheromone ER-1 - #10 / Jelly Rolls - #1540 / Anaphylotoxins (complement system) / 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 ...Pheromone ER-1 / Pheromone ER-1 - #10 / Jelly Rolls - #1540 / Anaphylotoxins (complement system) / 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 / : / Complement component 5, CUB domain / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / Anaphylatoxin, complement system domain / Anaphylatoxin domain signature. / Anaphylatoxin/fibulin / Anaphylatoxin, complement system / 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 / Netrin domain / NTR domain profile. / 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 / 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 / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / Single Sheet / Helix non-globular / 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
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT, SAD / Resolution: 3.105 Å
AuthorsFredslund, F. / Andersen, G.R.
CitationJournal: Nat.Immunol. / Year: 2008
Title: Structure of and influence of a tick complement inhibitor on human complement component 5
Authors: Fredslund, F. / Laursen, N.S. / Roversi, P. / Jenner, L. / Oliveira, C.L.P. / Pedersen, J.S. / Nunn, M.A. / Lea, S.M. / Discipio, R. / Sottrup-Jensen, L. / Andersen, G.R.
History
DepositionApr 16, 2008Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Jun 10, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 1.2Nov 6, 2013Group: Data collection
Revision 1.3Oct 25, 2017Group: Data collection / Refinement description / Category: diffrn_source / software / Item: _diffrn_source.pdbx_synchrotron_site / _software.name
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 / 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.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_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _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_label_seq_id / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Nov 1, 2023Group: Data collection / Database references ...Data collection / Database references / 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_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_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_comp_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Complement C5
B: Complement C5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)379,35515
Polymers377,0522
Non-polymers2,30313
Water0
1
A: Complement C5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)189,7348
Polymers188,5261
Non-polymers1,2087
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Complement C5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)189,6217
Polymers188,5261
Non-polymers1,0956
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4570 Å2
ΔGint-62 kcal/mol
Surface area140330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)144.260, 144.260, 241.000
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number144
Space group name H-MP31
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11resid 20:120 and chain A
21resid 20:120 and chain B
12resid 121:224 and chain A
22resid 121:224 and chain B
13resid 225:349 and chain A
23resid 225:349 and chain B
14resid 350:460 and chain A
24resid 350:460 and chain B
15resid 461:566 and chain A
25resid 461:566 and chain B
16(resid 567:606 or resid 760:821) and chain A
26(resid 567:606 or resid 760:821) and chain B
17resid 822:930 and chain A and not(resid 892:896)
27resid 822:930 and chain B and not(resid 892:896)
18(resid 931:983 or resid 1305:1367) and chain A
28(resid 931:983 or resid 1305:1367) and chain B
19resid 984:1304 and chain A
29resid 984:1304 and chain B
110resid 1368:1512 and chain A
210resid 1368:1512 and chain B
111resid 679:743 and chain A
211resid 679:743 and chain B
112resid 607:673 and chain A
212resid 607:673 and chain B

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLUGLUTHRTHRAA20 - 12020 - 120
21GLUGLUTHRTHRBB20 - 12020 - 120
12TYRTYRLEULEUAA121 - 224121 - 224
22TYRTYRLEULEUBB121 - 224121 - 224
13PROPROLEULEUAA225 - 349225 - 349
23PROPROLEULEUBB225 - 349225 - 349
14SERSERLEULEUAA350 - 460350 - 460
24SERSERLEULEUBB350 - 460350 - 460
15SERSERLYSLYSAA461 - 566461 - 566
25SERSERLYSLYSBB461 - 566461 - 566
16CYSCYSASPASPAA567 - 606567 - 606
26VALVALLYSLYSAA760 - 821760 - 821
17ASPASPVALVALAA822 - 930822 - 930
27ASPASPVALVALBB822 - 930822 - 930
18PROPROLEULEUAA931 - 983931 - 983
28LYSLYSLYSLYSAA1305 - 13671305 - 1367
19VALVALVALVALAA984 - 1304984 - 1304
29VALVALVALVALBB984 - 1304984 - 1304
110THRTHRSERSERAA1368 - 15121368 - 1512
210THRTHRSERSERBB1368 - 15121368 - 1512
111LEULEUSERSERAA679 - 743679 - 743
211LEULEUSERSERBB679 - 743679 - 743
112SERSERLEULEUAA607 - 673607 - 673
212SERSERLEULEUBB607 - 673607 - 673

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12

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Components

#1: Protein Complement C5 / Complement component 5 / C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4


Mass: 188526.125 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / Tissue: Blood / References: UniProt: P01031
#2: 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.: 2
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
#3: 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 / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
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
#4: Chemical
ChemComp-CD / CADMIUM ION


Mass: 112.411 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Cd
Sequence detailsTHE RESIDUE AT POSITION 802 IS A VARIANT AS REFERRED IN UNP ENTRY, P01031.

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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: 3.84 Å3/Da / Density % sol: 67.97 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6.8
Details: 100mM NaCl, 1.5-3mM MES pH 5.5, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: MAX II / Beamline: I711 / Wavelength: 0.989 Å
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Oct 20, 1998 / Details: MIRRORS
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.989 Å / Relative weight: 1
ReflectionResolution: 3.1→30 Å / Num. all: 101804 / Num. obs: 98600 / % possible obs: 96.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 1.36 % / Biso Wilson estimate: 94.23 Å2 / Rmerge(I) obs: 0.04 / Rsym value: 0.04 / Net I/σ(I): 13.5
Reflection shellResolution: 3.1→3.21 Å / Redundancy: 1.1 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 1.3 / Num. unique all: 8671 / Rsym value: 0.57 / % possible all: 86

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine)refinement
MAR345345 (ESD) Version 1.1.7data collection
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT, SAD
Starting model: PDB Entry 2B39

2b39
PDB Unreleased entry


Resolution: 3.105→29.286 Å / SU ML: 0.44 / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 1.97 / Phase error: 31.59 / Stereochemistry target values: ML / Details: Used TLS and NCS
RfactorNum. reflection% reflectionSelection details
Rfree0.2805 4921 4.99 %random
Rwork0.2357 93649 --
obs0.2379 98570 97.46 %-
all-101139 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 95.161 Å2 / ksol: 0.297 e/Å3
Displacement parametersBiso max: 59.61 Å2 / Biso mean: 141 Å2 / Biso min: 316.64 Å2
Baniso -1Baniso -2Baniso -3
1-9.864 Å2-0 Å2-0 Å2
2--9.864 Å2-0 Å2
3----19.728 Å2
Refinement stepCycle: LAST / Resolution: 3.105→29.286 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24562 0 93 0 24655
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00425237
X-RAY DIFFRACTIONf_angle_d0.84634167
X-RAY DIFFRACTIONf_chiral_restr0.0593905
X-RAY DIFFRACTIONf_plane_restr0.0044334
X-RAY DIFFRACTIONf_dihedral_angle_d16.9789137
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A800X-RAY DIFFRACTIONPOSITIONAL0.003
12B800X-RAY DIFFRACTIONPOSITIONAL0.003
21A853X-RAY DIFFRACTIONPOSITIONAL0.005
22B853X-RAY DIFFRACTIONPOSITIONAL0.005
31A1018X-RAY DIFFRACTIONPOSITIONAL0.005
32B1018X-RAY DIFFRACTIONPOSITIONAL0.005
41A844X-RAY DIFFRACTIONPOSITIONAL0.008
42B844X-RAY DIFFRACTIONPOSITIONAL0.008
51A863X-RAY DIFFRACTIONPOSITIONAL0.005
52B863X-RAY DIFFRACTIONPOSITIONAL0.005
61A790X-RAY DIFFRACTIONPOSITIONAL0.004
62B790X-RAY DIFFRACTIONPOSITIONAL0.004
71A744X-RAY DIFFRACTIONPOSITIONAL0.005
72B744X-RAY DIFFRACTIONPOSITIONAL0.005
81A918X-RAY DIFFRACTIONPOSITIONAL0.007
82B918X-RAY DIFFRACTIONPOSITIONAL0.007
91A2548X-RAY DIFFRACTIONPOSITIONAL0.006
92B2548X-RAY DIFFRACTIONPOSITIONAL0.006
101A1056X-RAY DIFFRACTIONPOSITIONAL0.006
102B1056X-RAY DIFFRACTIONPOSITIONAL0.006
111A498X-RAY DIFFRACTIONPOSITIONAL0.003
112B498X-RAY DIFFRACTIONPOSITIONAL0.003
121A501X-RAY DIFFRACTIONPOSITIONAL0.004
122B501X-RAY DIFFRACTIONPOSITIONAL0.004
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.105-3.1410.4011480.3632348249674
3.141-3.1780.3451460.3453189333599
3.178-3.2160.3481940.3393139333399
3.216-3.2570.3831790.3423146332599
3.257-3.30.3821450.3173246339199
3.3-3.3450.3661690.313183335299
3.345-3.3930.2961380.2923184332299
3.393-3.4430.391610.2993191335299
3.443-3.4970.3341740.3063157333199
3.497-3.5540.3481670.29832113378100
3.554-3.6150.3491780.2853184336299
3.615-3.6810.3121820.2713078326098
3.681-3.7520.3651870.2653169335699
3.752-3.8280.3221570.2583195335299
3.828-3.9110.3141480.2443190333898
3.911-4.0020.2641680.2373184335299
4.002-4.1020.2781640.2183171333599
4.102-4.2120.2541850.22531683353100
4.212-4.3360.2971460.2133173331999
4.336-4.4750.2341640.1893211337599
4.475-4.6350.211690.1843200336999
4.635-4.8190.221770.1813164334199
4.819-5.0380.2521760.1823124330099
5.038-5.3020.2021560.183247340399
5.302-5.6320.2071700.2023131330199
5.632-6.0630.2791750.2163159333498
6.063-6.6670.2791310.233140327197
6.667-7.6170.2731760.2333078325496
7.617-9.5410.2581550.1982986314193
9.541-29.2870.2411360.2232703283984
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)
10.02491.2105-1.16952.17082.2884-0.5551-0.19810.73920.1681-0.0559-0.07990.3281-0.1676-0.88580.0061.63560.9984-0.39332.73630.07121.4331-89.661164.06983.0426
20.60180.3254-1.55822.69320.45181.85410.07690.5524-0.0903-0.4683-0.1399-0.08190.1597-0.74580.02511.24840.6234-0.28751.8047-0.32721.1557-59.671841.00346.2659
33.1195-0.8985-1.23483.69712.53514.97850.57960.4253-0.03560.04830.792-1.11220.37130.6285-1.21731.08290.6145-0.30030.8132-0.40291.2552-32.794451.629425.5865
43.9275-1.3804-0.48082.25740.761.92850.59910.50090.40350.096-0.01950.17250.0621-0.5804-0.28091.00240.55370.43140.90480.43110.8479-62.159276.582432.211
51.33310.28220.31783.53421.59520.47190.49360.5873-0.1840.0629-1.03960.85960.0264-1.03420.32750.98410.69850.03541.90360.0941.1428-85.005469.370725.8706
61.751-2.1266-0.89833.34251.4833.4330.12480.5975-0.22370.766-0.01390.33480.3903-0.5712-0.11351.21030.2412-0.1261.3733-0.14311.3477-62.734931.296824.1632
71.04990.5073-0.4553-0.7309-0.27032.88640.26130.5276-0.42780.2492-0.04690.05670.0367-0.6611-0.30051.71220.444-0.6031.211-0.46711.5687-33.692611.972130.0493
80.44440.8317-0.40261.80550.10751.8316-0.2365-0.21790.10960.61320.6419-0.43470.297-0.1679-0.21220.71950.3874-0.23071.3257-0.69091.0392-38.5619-1.231-10.5584
90.71531.3210.72562.9829-0.11232.5032-0.39720.0876-0.2790.31190.5771-0.4484-0.38850.1274-0.22650.41790.1632-0.09081.0747-0.52930.8069-39.222826.8861-20.0206
100.1624-0.00610.07462.0087-0.82472.32930.06940.2327-0.02820.19610.0499-1.1028-0.18520.8735-0.30230.87210.1556-0.41011.4804-0.81531.5604-18.564325.28142.1265
110.89250.7977-0.9868-0.32220.14651.53420.660.08620.2413-0.3076-0.00390.9552-0.36370.4993-0.23751.7606-0.1593-0.11691.5966-0.72812.2145-17.057150.89137.5668
12-0.54710.3231-1.69670.1921.14041.90680.62031.0115-0.3552-0.0332-0.16320.0053-0.531-0.8966-0.31011.220.5782-0.26791.81830.02181.2108-70.059963.19316.2272
131.6577-0.4499-0.8741-0.10291.14144.7025-0.9270.4985-0.70480.0158-0.32810.2555-0.59290.19030.49342.17390.3267-0.51731.8897-0.43531.8774-13.5511.20521.9298
141.4143-1.2913-1.71562.80110.32050.699-0.4190.27-0.08471.30060.3288-0.68370.3744-0.2385-0.12832.36650.5457-0.52961.9215-0.23922.0225-11.778913.969441.5599
152.651-0.89711.4609-1.4196-1.88380.49440.4052-0.1940.4930.4142-0.56380.236-0.62730.22040.01763.1309-0.0164-0.10450.88-0.31311.282-10.6494109.685677.2202
162.9941-0.9515-0.21850.2892-0.44771.86340.0571-0.4251-0.18060.8607-0.03830.1369-0.55030.33280.04322.1110.0498-0.44260.7379-0.08861.0617-5.660672.173374.0023
174.6092-1.2671.16681.0384-2.28665.05371.0058-0.3021-1.44970.1440.51330.69481.005-0.0135-1.32341.55520.4412-0.56040.5414-0.05641.4323-28.323554.205254.6868
182.2685-0.11650.73133.2967-1.19142.65280.49030.15430.54040.73630.1230.3048-0.78950.1475-0.46651.48880.28440.62590.50550.15290.9152-35.245892.13448.0594
192.9712-0.75761.70180.8241-1.16880.8531-0.28260.3370.77141.1219-0.159-0.2742-1.13520.25610.41312.3127-0.01980.15760.7376-0.03561.2598-17.5619108.299554.4017
201.2438-0.91171.31290.6139-0.81842.78720.60170.3270.06210.3134-0.43840.0032-0.09390.656-0.16981.46170.0257-0.1340.9705-0.0191.2834.257969.973756.1183
21-0.20181.0231-0.48580.12330.05832.22710.41420.0839-0.21980.6233-0.1931-0.2042-0.71490.4026-0.12891.50710.4466-0.7631.0163-0.27761.35886.466535.156150.2288
221.75410.14330.22380.1961-0.09142.31980.62210.2769-0.4931-0.6864-0.18740.50450.32210.3947-0.32231.5818-0.0795-0.69750.61530.14321.119420.343132.785990.833
233.1043-0.21320.02920.4920.25262.50490.5257-0.1155-0.3962-0.5194-0.306-0.016-0.1589-0.4166-0.2021.1223-0.2216-0.51310.5120.18660.8475-3.674547.4196100.299
241.4076-1.3161-0.34560.75620.27082.37670.34650.1826-0.97270.0728-0.20090.47950.8326-0.3787-0.41611.4795-0.2032-0.91520.89190.03951.5357-12.625128.722178.153
25-1.02410.3099-1.73070.4714-0.17791.05180.45170.18420.31290.34610.4803-0.11790.139-0.7008-0.47441.489-0.0396-0.64631.9230.27962.2137-35.523140.230372.7127
260.8632-0.5160.2152-0.5795-0.9442-0.43280.0419-0.2416-0.34391.32020.2639-0.1214-0.75780.1689-0.19232.39480.1551-0.02070.9302-0.18141.1961-19.676692.282664.0334
27-0.8721.444-0.64654.47780.8173-0.98270.62421.0573-1.49871.5544-0.0315-2.1073-0.7331-0.5174-0.30132.40760.3477-0.55651.3941-0.20362.30665.065512.992255.8969
280.63110.0030.0952-0.02810.08230.179-0.22770.026-0.04140.10540.0950.13470.156-0.09740.0125.35480.2283-0.73492.66510.31051.572321.261539.489354.806
290.54460.5730.11840.2828-0.1823-0.4377-0.30680.03110.262-0.14470.0508-0.12160.23690.02310.12723.10040.62110.70524.7678-0.561.5897-45.00351.20425.5603
305.81782.0003-3.55261.999922-0.30320.6155-0.0067-2.51191.1513-0.93832.7105-1.5188-0.70323.0981-0.30450.36792.1923-0.32512.9027-3.160256.016921.3646
318.25183.0822-3.4508-2.25963.4888.13570.8373-1.34820.80771.43970.35331.24660.83843.6646-1.06042.49290.98521.36624.21061.6462.5947-46.907130.904958.8615
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1resid 20:120 and chain A
2X-RAY DIFFRACTION2resid 121:224 and chain A
3X-RAY DIFFRACTION3resid 225:349 and chain A
4X-RAY DIFFRACTION4resid 350:460 and chain A
5X-RAY DIFFRACTION5resid 461:566 and chain A
6X-RAY DIFFRACTION6(resid 567:606 or resid 760:821) and chain a
7X-RAY DIFFRACTION7resid 822:930 and chain A
8X-RAY DIFFRACTION8(resid 931:983 or resid 1305:1367) and chain A
9X-RAY DIFFRACTION9resid 984:1304 and chain A
10X-RAY DIFFRACTION10resid 1368:1514 and chain A
11X-RAY DIFFRACTION11resid 679:759 and chain A
12X-RAY DIFFRACTION12resid 607:673 and chain A
13X-RAY DIFFRACTION13resid 1515:1532 and chain A
14X-RAY DIFFRACTION14resid 1533:1678 and chain A
15X-RAY DIFFRACTION15resid 20:120 and chain B
16X-RAY DIFFRACTION16resid 121:224 and chain B
17X-RAY DIFFRACTION17resid 225:349 and chain B
18X-RAY DIFFRACTION18resid 350:460 and chain B
19X-RAY DIFFRACTION19resid 461:566 and chain B
20X-RAY DIFFRACTION20(resid 567:606 or resid 760:821) and chain B
21X-RAY DIFFRACTION21resid 822:930 and chain B
22X-RAY DIFFRACTION22(resid 931:983 or resid 1305:1367) and chain B
23X-RAY DIFFRACTION23resid 984:1304 and chain B
24X-RAY DIFFRACTION24resid 1368:1514 and chain B
25X-RAY DIFFRACTION25resid 679:759 and chain B
26X-RAY DIFFRACTION26resid 607:673 and chain B
27X-RAY DIFFRACTION27resid 1515:1532 and chain B
28X-RAY DIFFRACTION28resid 2001:2002 and chain B
29X-RAY DIFFRACTION29resid 2001:2002 and chain A
30X-RAY DIFFRACTION30resid 2003 and chain A
31X-RAY DIFFRACTION31resid 2003 and chain B

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