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- PDB-2a74: Human Complement Component C3c -

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Basic information

Entry
Database: PDB / ID: 2a74
TitleHuman Complement Component C3c
Components(Complement Component ...) x 3
KeywordsIMMUNE SYSTEM
Function / homology
Function and homology information


C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation / positive regulation of lipid storage / positive regulation of phagocytosis, engulfment ...C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation / positive regulation of lipid storage / positive regulation of phagocytosis, engulfment / positive regulation of G protein-coupled receptor signaling pathway / Activation of C3 and C5 / complement receptor mediated signaling pathway / positive regulation of type IIa hypersensitivity / positive regulation of D-glucose transmembrane transport / complement-dependent cytotoxicity / complement activation / complement activation, alternative pathway / endopeptidase inhibitor activity / neuron remodeling / B cell activation / amyloid-beta clearance / positive regulation of vascular endothelial growth factor production / Purinergic signaling in leishmaniasis infection / complement activation, classical pathway / Peptide ligand-binding receptors / Regulation of Complement cascade / fatty acid metabolic process / Post-translational protein phosphorylation / response to bacterium / positive regulation of receptor-mediated endocytosis / positive regulation of angiogenesis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / G alpha (i) signalling events / secretory granule lumen / blood microparticle / receptor ligand activity / inflammatory response / immune response / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / signaling receptor binding / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / S-adenosyl-L-methionine-dependent methyltransferases / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / Complement C3-like, NTR domain / : ...N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / S-adenosyl-L-methionine-dependent methyltransferases / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / Complement C3-like, NTR domain / : / : / Complement component 3, CUB domain, second segment / Complement component 3, CUB domain, first segment / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / : / 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 / 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. / 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 / Tissue inhibitor of metalloproteinases-like, OB-fold / Other non-globular / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Single Sheet / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta
Similarity search - Domain/homology
NITRATE ION / Complement C3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD, SIRAS / Resolution: 2.4 Å
AuthorsJanssen, B.J.C. / Huizinga, E.G. / Raaijmakers, H.C.A. / Roos, A. / Daha, M.R. / Nilsson-Ekdahl, K. / Nilsson, B. / Gros, P.
CitationJournal: Nature / Year: 2005
Title: Structures of complement component C3 provide insights into the function and evolution of immunity.
Authors: Janssen, B.J. / Huizinga, E.G. / Raaijmakers, H.C. / Roos, A. / Daha, M.R. / Nilsson-Ekdahl, K. / Nilsson, B. / Gros, P.
History
DepositionJul 4, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 27, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Advisory / Version format compliance
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 / database_PDB_caveat / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_chiral / 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 / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_unobs_or_zero_occ_atoms.auth_asym_id / _pdbx_unobs_or_zero_occ_atoms.auth_atom_id / _pdbx_unobs_or_zero_occ_atoms.auth_seq_id / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _pdbx_unobs_or_zero_occ_atoms.label_atom_id / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 16, 2024Group: 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_entry_details / pdbx_modification_feature / 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.end_auth_comp_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Complement Component C3c
B: Complement Component C3c
C: Complement Component C3c
D: Complement Component C3c
E: Complement Component C3c
F: Complement Component C3c
hetero molecules


Theoretical massNumber of molelcules
Total (without water)266,88524
Polymers264,6536
Non-polymers2,23218
Water11,007611
1
A: Complement Component C3c
B: Complement Component C3c
C: Complement Component C3c
hetero molecules


Theoretical massNumber of molelcules
Total (without water)133,45712
Polymers132,3263
Non-polymers1,1319
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12890 Å2
ΔGint-54 kcal/mol
Surface area49660 Å2
MethodPISA
2
D: Complement Component C3c
E: Complement Component C3c
F: Complement Component C3c
hetero molecules


Theoretical massNumber of molelcules
Total (without water)133,42712
Polymers132,3263
Non-polymers1,1019
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12830 Å2
ΔGint-53 kcal/mol
Surface area50110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)126.866, 246.863, 87.383
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21D
31A
41D
51A
61D
71A
81D
12A
22D
32A
42D
52A
62D
13B
23E
33B
43E
14B
24E
15C
25F

NCS domain segments:

Refine code: 5

Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111SERSERGLNGLNAA1 - 1041 - 104
211PROPROGLNGLNDD2 - 1042 - 104
321ASPASPALAALAAA602 - 636602 - 636
421ASPASPALAALADD602 - 636602 - 636
531SERSERTYRTYRAA329 - 424329 - 424
631SERSERTYRTYRDD329 - 424329 - 424
741SERSERLYSLYSAA430 - 534430 - 534
841SERSERLYSLYSDD430 - 534430 - 534
112SERSERGLUGLUAA105 - 204105 - 204
212SERSERGLUGLUDD105 - 204105 - 204
322ASPASPALAALAAA535 - 601535 - 601
422ASPASPALAALADD535 - 601535 - 601
532PHEPHETHRTHRAA210 - 328210 - 328
632PHEPHETHRTHRDD210 - 328210 - 328
113PHEPHEGLUGLUBB808 - 91282 - 186
213PHEPHEGLUGLUEE808 - 91282 - 186
323ASPASPSERSERBB730 - 7414 - 15
423GLUGLUSERSEREE731 - 7415 - 15
114GLUGLUASPASPBB744 - 80618 - 80
214GLUGLUASPASPEE744 - 80618 - 80
115THRTHRASNASNCC1335 - 164137 - 343
215THRTHRASNASNFF1335 - 164137 - 343

NCS ensembles :
ID
1
2
3
4
5
DetailsThere are 2 biological units in the asymmetric unit

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Components

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Complement Component ... , 3 types, 6 molecules ADBECF

#1: Protein Complement Component C3c


Mass: 71267.203 Da / Num. of mol.: 2 / Fragment: residues 23-665 / Source method: isolated from a natural source / Details: serum / Source: (natural) Homo sapiens (human) / References: UniProt: P01024
#2: Protein Complement Component C3c


Mass: 21521.756 Da / Num. of mol.: 2 / Fragment: residues 749-936 / Source method: isolated from a natural source / Details: serum / Source: (natural) Homo sapiens (human) / References: UniProt: P01024
#3: Protein Complement Component C3c


Mass: 39537.418 Da / Num. of mol.: 2 / Fragment: esidues 1321-1663 / Source method: isolated from a natural source / Details: serum / Source: (natural) Homo sapiens (human) / References: UniProt: P01024

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Sugars , 1 types, 2 molecules

#4: Polysaccharide 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-alpha-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAca1-4DGlcpNAca1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE

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Non-polymers , 3 types, 627 molecules

#5: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical ChemComp-NO3 / NITRATE ION


Mass: 62.005 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: NO3
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 611 / Source method: isolated from a natural source / Formula: H2O

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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: 2.5 Å3/Da / Density % sol: 51 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7
Details: PEG3000, lithium nitrate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.9393 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Sep 7, 2003
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9393 Å / Relative weight: 1
ReflectionResolution: 2.4→40 Å / Num. all: 107630 / Num. obs: 105155 / % possible obs: 97.7 % / Observed criterion σ(F): -999 / Observed criterion σ(I): -3.7 / Redundancy: 3.7 % / Rmerge(I) obs: 0.073 / Net I/σ(I): 13.4
Reflection shellResolution: 2.4→2.53 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.331 / Mean I/σ(I) obs: 2.5 / % possible all: 90.2

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Processing

Software
NameVersionClassificationNB
REFMACrefinement
PDB_EXTRACT1.7data extraction
MOSFLMdata reduction
CCP4(SCALA)data scaling
SOLVEphasing
RefinementMethod to determine structure: MAD, SIRAS / Resolution: 2.4→40 Å / Cor.coef. Fo:Fc: 0.947 / Cor.coef. Fo:Fc free: 0.918 / SU B: 18.332 / SU ML: 0.22 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.423 / ESU R Free: 0.286 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.27527 3123 3 %RANDOM
Rwork0.21476 ---
obs0.21653 101981 97.37 %-
all-107630 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 45.606 Å2
Baniso -1Baniso -2Baniso -3
1--1.61 Å20 Å20 Å2
2---0.47 Å20 Å2
3---2.09 Å2
Refinement stepCycle: LAST / Resolution: 2.4→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17632 0 146 611 18389
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.02218139
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2011.96124585
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.96352212
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.47824.851808
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.813153211
X-RAY DIFFRACTIONr_dihedral_angle_4_deg20.7881594
X-RAY DIFFRACTIONr_chiral_restr0.1170.22805
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0213462
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2460.27652
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined0.3180.211999
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1880.2884
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2040.275
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2410.210
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.731.511361
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it1.242218122
X-RAY DIFFRACTIONr_scbond_it1.94437545
X-RAY DIFFRACTIONr_scangle_it3.1034.56462
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Dom-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Ens-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
1A1320medium positional0.230.5
2A1132medium positional0.260.5
3B464medium positional0.240.5
4B252medium positional0.240.5
5C1184medium positional0.340.5
1A1242loose positional0.815
2A1087loose positional0.695
3B475loose positional0.675
4B253loose positional0.595
5C1223loose positional0.745
1A1320medium thermal0.562
2A1132medium thermal0.712
3B464medium thermal0.622
4B252medium thermal1.142
5C1184medium thermal0.582
1A1242loose thermal1.3410
2A1087loose thermal1.6110
3B475loose thermal1.5710
4B253loose thermal1.8610
5C1223loose thermal1.3510
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.361 201 -
Rwork0.291 6602 -
obs--86.66 %
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)
13.9682-1.1918-0.2925.1669-0.59551.7508-0.15610.0601-0.3732-0.35790.0805-0.69760.11350.30470.07560.0198-0.00840.0078-0.1267-0.0864-0.170145.71-37.23585.121
24.9418-2.38050.36075.97050.44021.92120.02650.10650.1482-0.36620.12380.8341-0.0716-0.3465-0.15030.1461-0.0236-0.0159-0.05370.0803-0.081716.85137.37942.478
32.1413-1.55220.743710.1387-1.17021.64850.08670.5217-0.1177-1.0857-0.1275-0.27470.17390.19930.0408-0.0172-0.02390.0755-0.0546-0.0288-0.326850.3670.03381.701
42.2859-0.97120.228511.85082.25462.88750.05660.37550.2814-1.0361-0.25320.8002-0.2925-0.32490.1965-0.0412-0.0314-0.09650.0442-0.0153-0.18611.6860.15140.105
56.99633.96542.01455.62450.83891.343-0.00180.1157-0.0417-0.15470.09310.53270.0425-0.0534-0.0913-0.18340.01380.0278-0.1005-0.01940.008319.4614.34292.857
64.043.3725-2.19224.7839-1.37372.9530.21190.06750.15150.2-0.0275-0.0757-0.06420.0024-0.1843-0.1469-0.0021-0.0638-0.0382-0.0123-0.238444.485-13.45145.843
73.3283-3.7442-0.95413.3432.57911.9605-0.0769-0.19160.22340.48220.16871.08720.2438-0.2336-0.0917-0.1393-0.056-0.0091-0.04220.03410.002415.149-19.73795.816
82.1892-3.22990.56439.035-2.57092.6986-0.008-0.06140.24540.44040.0202-0.8183-0.34650.4822-0.0122-0.0511-0.11650.02440.0485-0.12280.081748.34920.13950.069
94.56613.20760.08238.0869-0.49752.76790.0175-0.2379-0.21460.1753-0.02470.21030.2138-0.15510.0072-0.1406-0.0096-0.0461-0.13870.0223-0.3532.244-35.33498.787
103.84252.8392-0.312410.06540.02432.1055-0.0427-0.18740.4020.36450.0734-0.4685-0.19820.1874-0.0307-0.024-0.0127-0.0113-0.0582-0.1012-0.202331.56135.64254.839
110.725-0.59550.13382.7914-0.94690.3576-0.0428-0.18280.06640.2948-0.02550.04180.04290.01150.0683-0.1193-0.03710.029-0.1152-0.0195-0.276449.7083.649102.115
121.11660.4512-0.067510.2973-0.83710.13630.0937-0.37330.07541.6581-0.17380.6282-0.1513-0.01240.08010.213-0.11590.0930.0477-0.0602-0.250715.826-3.85659.926
132.81640.4478-0.84573.3958-1.11824.6127-0.066-0.1810.30760.4575-0.0028-0.0919-0.23630.10580.0688-0.0577-0.0037-0.0194-0.2336-0.0463-0.15347.64737.12898.025
142.84661.08820.68075.03720.09684.13890.2003-0.3424-0.11130.8263-0.1230.17290.2328-0.1604-0.07730.0333-0.08350.0026-0.1135-0.0012-0.224517.333-36.98354.613
156.77110.96640.19767.3415-0.30752.7950.0494-0.15270.13410.26610.12660.3526-0.0912-0.2058-0.176-0.13590.07060.0028-0.10680.051-0.084926.75342.13289.161
166.2462.1512-0.13375.8534-1.02672.8456-0.0252-0.0888-0.26650.3450.0604-0.18650.05380.1027-0.0352-0.08250.0467-0.0675-0.0784-0.0417-0.259737.193-41.6443.529
175.08312.10050.72494.5631-0.04253.4047-0.1122-0.14620.33050.1711-0.02720.1454-0.1918-0.07990.1394-0.07050.0359-0.042-0.20250.0403-0.190461.24664.4281.638
185.27873.4439-1.08865.967-1.16913.2381-0.1395-0.1676-0.4360.2434-0.0981-0.44780.08390.13210.2376-0.05970.02030.0206-0.1564-0.0249-0.19032.361-64.57239.207
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1 - 1041 - 104
2X-RAY DIFFRACTION1AA602 - 636602 - 636
3X-RAY DIFFRACTION1AG644 - 6451 - 2
4X-RAY DIFFRACTION2DD2 - 1042 - 104
5X-RAY DIFFRACTION2DD602 - 636602 - 636
6X-RAY DIFFRACTION2DH644 - 6451 - 2
7X-RAY DIFFRACTION3AA105 - 204105 - 204
8X-RAY DIFFRACTION4DD105 - 204105 - 204
9X-RAY DIFFRACTION5AA210 - 328210 - 328
10X-RAY DIFFRACTION6DD210 - 328210 - 328
11X-RAY DIFFRACTION7AA329 - 424329 - 424
12X-RAY DIFFRACTION8DD329 - 424329 - 424
13X-RAY DIFFRACTION9AA430 - 534430 - 534
14X-RAY DIFFRACTION10DD430 - 534430 - 534
15X-RAY DIFFRACTION11AA535 - 601535 - 601
16X-RAY DIFFRACTION11BB744 - 80618 - 80
17X-RAY DIFFRACTION12DD535 - 601535 - 601
18X-RAY DIFFRACTION12EE744 - 80618 - 80
19X-RAY DIFFRACTION13BB808 - 91282 - 186
20X-RAY DIFFRACTION13BB730 - 7414 - 15
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22X-RAY DIFFRACTION14EE731 - 7415 - 15
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24X-RAY DIFFRACTION16FF1335 - 147437 - 176
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26X-RAY DIFFRACTION18FF1475 - 1641177 - 343

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