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- PDB-2win: C3 convertase (C3bBb) stabilized by SCIN -

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Basic information

Entry
Database: PDB / ID: 2win
TitleC3 convertase (C3bBb) stabilized by SCIN
Components
  • COMPLEMENT C3 BETA CHAIN
  • COMPLEMENT C3B ALPHA' CHAIN
  • COMPLEMENT FACTOR B
  • STAPHYLOCOCCAL COMPLEMENT INHIBITOR
KeywordsIMMUNE SYSTEM / SERINE PROTEASE / IMMUNE RESPONSE / INNATE IMMUNITY / ZYMOGEN / SECRETED / PROTEASE / GLYCATION / ALTERNATIVE PATHWAY / DISEASE MUTATION / HYDROLASE / CONVERTASE / COMPLEMENT / POLYMORPHISM / IMMUNE EVASION
Function / homology
Function and homology information


alternative-complement-pathway C3/C5 convertase / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / complement binding / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation ...alternative-complement-pathway C3/C5 convertase / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / complement binding / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation / Activation of C3 and C5 / positive regulation of phagocytosis, engulfment / positive regulation of lipid storage / positive regulation of G protein-coupled receptor signaling pathway / complement receptor mediated signaling pathway / positive regulation of type IIa hypersensitivity / complement-dependent cytotoxicity / positive regulation of D-glucose transmembrane transport / complement activation / complement activation, alternative pathway / endopeptidase inhibitor activity / neuron remodeling / amyloid-beta clearance / B cell activation / positive regulation of vascular endothelial growth factor production / complement activation, classical pathway / Purinergic signaling in leishmaniasis infection / 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 / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / positive regulation of protein phosphorylation / G alpha (i) signalling events / secretory granule lumen / blood microparticle / immune response / G protein-coupled receptor signaling pathway / inflammatory response / receptor ligand activity / endoplasmic reticulum lumen / signaling receptor binding / serine-type endopeptidase activity / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Staphylococcal complement inhibitor SCIN / Staphylococcal complement inhibitor SCIN / Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / Complement factor B / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Alpha-macroglobulin, receptor-binding domain / Complement B/C2 / S-adenosyl-L-methionine-dependent methyltransferases / Macroglobulin (MG2) domain ...Staphylococcal complement inhibitor SCIN / Staphylococcal complement inhibitor SCIN / Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / Complement factor B / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Alpha-macroglobulin, receptor-binding domain / Complement B/C2 / S-adenosyl-L-methionine-dependent methyltransferases / Macroglobulin (MG2) domain / Immunoglobulin-like - #1940 / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / Substrate Binding Domain Of Dnak; Chain:A; Domain 2 - #10 / 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 / Anaphylatoxin, complement system domain / : / 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 / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Macroglobulin domain MG4 / Macroglobulin domain MG4 / Glycosyltransferase - #20 / Netrin domain / NTR domain profile. / Alpha-macroglobulin, receptor-binding / 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 / von Willebrand factor, type A domain / Other non-globular / Sushi repeat (SCR repeat) / Heat shock protein 70kD, C-terminal domain superfamily / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Substrate Binding Domain Of Dnak; Chain:A; Domain 2 / von Willebrand factor type A domain / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / Single Sheet / von Willebrand factor A-like domain superfamily / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine 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 / Immunoglobulin-like fold / Peptidase S1, PA clan / Immunoglobulins / Up-down Bundle / Beta Barrel / Immunoglobulin-like / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta
Similarity search - Domain/homology
beta-D-mannopyranose / alpha-D-mannopyranose / Complement factor B / Complement C3 / Staphylococcal complement inhibitor
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
STAPHYLOCOCCUS AUREUS (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.9 Å
AuthorsWu, J. / Janssen, B.J. / Gros, P.
CitationJournal: Nat. Immunol. / Year: 2009
Title: Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor.
Authors: Rooijakkers, S.H. / Wu, J. / Ruyken, M. / van Domselaar, R. / Planken, K.L. / Tzekou, A. / Ricklin, D. / Lambris, J.D. / Janssen, B.J. / van Strijp, J.A. / Gros, P.
History
DepositionMay 13, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 9, 2009Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Jan 17, 2018Group: Advisory / Database references / Source and taxonomy
Category: citation / citation_author ...citation / citation_author / entity_src_gen / pdbx_unobs_or_zero_occ_residues
Item: _citation.journal_abbrev / _citation.journal_id_ISSN ..._citation.journal_abbrev / _citation.journal_id_ISSN / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name / _entity_src_gen.pdbx_host_org_strain
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Non-polymer description / 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_struct_conn_angle / 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.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.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_label_asym_id / _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 / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_comp_id_2 / _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 / _struct_conn.ptnr2_label_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Dec 13, 2023Group: Advisory / Data collection ...Advisory / 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 / pdbx_unobs_or_zero_occ_residues
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "IB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "IB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "JB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "KB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "LB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 5-STRANDED BARREL THIS IS REPRESENTED BY A 6-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: COMPLEMENT C3 BETA CHAIN
B: COMPLEMENT C3B ALPHA' CHAIN
C: COMPLEMENT C3 BETA CHAIN
D: COMPLEMENT C3B ALPHA' CHAIN
E: COMPLEMENT C3 BETA CHAIN
F: COMPLEMENT C3B ALPHA' CHAIN
G: COMPLEMENT C3 BETA CHAIN
H: COMPLEMENT C3B ALPHA' CHAIN
I: COMPLEMENT FACTOR B
J: COMPLEMENT FACTOR B
K: COMPLEMENT FACTOR B
L: COMPLEMENT FACTOR B
M: STAPHYLOCOCCAL COMPLEMENT INHIBITOR
N: STAPHYLOCOCCAL COMPLEMENT INHIBITOR
P: STAPHYLOCOCCAL COMPLEMENT INHIBITOR
Q: STAPHYLOCOCCAL COMPLEMENT INHIBITOR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)984,82938
Polymers974,01616
Non-polymers10,81322
Water1448
1
A: COMPLEMENT C3 BETA CHAIN
B: COMPLEMENT C3B ALPHA' CHAIN
G: COMPLEMENT C3 BETA CHAIN
H: COMPLEMENT C3B ALPHA' CHAIN
J: COMPLEMENT FACTOR B
L: COMPLEMENT FACTOR B
N: STAPHYLOCOCCAL COMPLEMENT INHIBITOR
Q: STAPHYLOCOCCAL COMPLEMENT INHIBITOR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)491,96819
Polymers487,0088
Non-polymers4,96011
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area38830 Å2
ΔGint-227.2 kcal/mol
Surface area238000 Å2
MethodPQS
2
C: COMPLEMENT C3 BETA CHAIN
D: COMPLEMENT C3B ALPHA' CHAIN
E: COMPLEMENT C3 BETA CHAIN
F: COMPLEMENT C3B ALPHA' CHAIN
I: COMPLEMENT FACTOR B
K: COMPLEMENT FACTOR B
M: STAPHYLOCOCCAL COMPLEMENT INHIBITOR
P: STAPHYLOCOCCAL COMPLEMENT INHIBITOR
hetero molecules


Theoretical massNumber of molelcules
Total (without water)492,86119
Polymers487,0088
Non-polymers5,85311
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area40640 Å2
ΔGint-236.7 kcal/mol
Surface area236850 Å2
MethodPQS
Unit cell
Length a, b, c (Å)228.632, 121.491, 280.783
Angle α, β, γ (deg.)90.00, 91.64, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
12
22
32
42
13
23
33
43
14
24
34
44
15
25
35
45
16
26
36
46
17
27
37
47
18
28
38
48
19
29
39
49
110
210
111
211
112
212
312
113
213
114
214
115
215
315
415
116
216
316
416
117
217
317
417
118
218
119
219
120
220
320
420

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 1:72 OR RESSEQ 78: 104 )
211CHAIN E AND (RESSEQ 1:72 OR RESSEQ 78: 104 )
311CHAIN C AND (RESSEQ 1:72 OR RESSEQ 78: 104 )
411CHAIN G AND (RESSEQ 1:72 OR RESSEQ 78: 104 )
112CHAIN A AND (RESSEQ 105:209 )
212CHAIN E AND (RESSEQ 105:209 )
312CHAIN C AND (RESSEQ 105:209 )
412CHAIN G AND (RESSEQ 105:209 )
113CHAIN A AND (RESSEQ 210:289 )
213CHAIN E AND (RESSEQ 210:289 )
313CHAIN C AND (RESSEQ 210:289 )
413CHAIN G AND (RESSEQ 210:289 )
114CHAIN A AND (RESSEQ 297:328 )
214CHAIN E AND (RESSEQ 297:328 )
314CHAIN C AND (RESSEQ 297:328 )
414CHAIN G AND (RESSEQ 297:328 )
115CHAIN A AND (RESSEQ 329:369 )
215CHAIN E AND (RESSEQ 329:369 )
315CHAIN C AND (RESSEQ 329:369 )
415CHAIN G AND (RESSEQ 329:369 )
116CHAIN A AND (RESSEQ 377:426 )
216CHAIN E AND (RESSEQ 377:426 )
316CHAIN C AND (RESSEQ 377:426 )
416CHAIN G AND (RESSEQ 377:426 )
117CHAIN A AND (RESSEQ 427:485 OR RESSEQ 492:534 )
217CHAIN E AND (RESSEQ 427:485 OR RESSEQ 492:534 )
317CHAIN C AND (RESSEQ 427:485 OR RESSEQ 492:534 )
417CHAIN G AND (RESSEQ 427:485 OR RESSEQ 492:534 )
118CHAIN A AND (RESSEQ 535:642 )
218CHAIN E AND (RESSEQ 535:642 )
318CHAIN C AND (RESSEQ 535:642 )
418CHAIN G AND (RESSEQ 535:642 )
119CHAIN B AND (RESSEQ 746:806 )
219CHAIN F AND (RESSEQ 746:806 )
319CHAIN D AND (RESSEQ 746:806 )
419CHAIN H AND (RESSEQ 746:806 )
1110CHAIN F AND (RESSEQ 1331:1349 OR RESSEQ 1359:1480 )
2110CHAIN H AND (RESSEQ 1331:1349 OR RESSEQ 1359:1480 )
1111CHAIN B AND (RESSEQ 1331:1351 OR RESSEQ 1358:1480 )
2111CHAIN D AND (RESSEQ 1331:1349 OR RESSEQ 1356:1480 )
1112CHAIN B AND (RESSEQ 971:1041 OR RESSEQ 1046:1262 )
2112CHAIN D AND (RESSEQ 971:1041 OR RESSEQ 1046:1262 )
3112CHAIN F AND (RESSEQ 971:1041 OR RESSEQ 1046:1262 )
1113CHAIN B AND (RESSEQ 1481:1498 OR RESSEQ 1501:1637 )
2113CHAIN D AND (RESSEQ 1481:1498 OR RESSEQ 1501:1637 )
1114CHAIN F AND (RESSEQ 1505:1636 )
2114CHAIN H AND (RESSEQ 1505:1636 )
1115CHAIN L AND (RESSEQ 235:449 )
2115CHAIN J AND (RESSEQ 235:449 )
3115CHAIN K AND (RESSEQ 235:449 )
4115CHAIN I AND (RESSEQ 235:449 )
1116CHAIN L AND (RESSEQ 450:741 )
2116CHAIN J AND (RESSEQ 450:741 )
3116CHAIN K AND (RESSEQ 450:741 )
4116CHAIN I AND (RESSEQ 450:741 )
1117CHAIN M AND (RESSEQ 2:85 )
2117CHAIN N AND (RESSEQ 2:85 )
3117CHAIN P AND (RESSEQ 2:85 )
4117CHAIN Q AND (RESSEQ 2:85 )
1118CHAIN B AND (RESSEQ 915:963 OR RESSEQ 1271:1330 )
2118CHAIN D AND (RESSEQ 915:963 OR RESSEQ 1271:1330 )
1119CHAIN F AND (RESSEQ 915:963 OR RESSEQ 1271:1330 )
2119CHAIN H AND (RESSEQ 915:963 OR RESSEQ 1271:1330 )
1120CHAIN B AND (RESSEQ 729:745 OR RESSEQ 807:911 )
2120CHAIN F AND (RESSEQ 729:745 OR RESSEQ 807:911 )
3120CHAIN D AND (RESSEQ 729:745 OR RESSEQ 807:911 )
4120CHAIN H AND (RESSEQ 729:745 OR RESSEQ 807:911 )

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20

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Components

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Protein , 4 types, 16 molecules ACEGBDFHIJKLMNPQ

#1: Protein
COMPLEMENT C3 BETA CHAIN


Mass: 71393.320 Da / Num. of mol.: 4 / Fragment: COMPLEMENT C3B BETA CHAIN, RESIDUES 23-667 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P01024
#2: Protein
COMPLEMENT C3B ALPHA' CHAIN


Mass: 104073.164 Da / Num. of mol.: 4 / Fragment: COMPLEMENT C3B ALPHA' CHAIN, RESIDUES 749-1663 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / References: UniProt: P01024
#3: Protein
COMPLEMENT FACTOR B


Mass: 57258.277 Da / Num. of mol.: 4 / Fragment: COMPLEMENT FACTOR B BB FRAGMENT, RESIDUES 260-764
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PUPE06.08-FBWT / Cell line (production host): HEK293ES / Production host: HOMO SAPIENS (human) / Variant (production host): GNTI-
References: UniProt: P00751, alternative-complement-pathway C3/C5 convertase
#4: Protein
STAPHYLOCOCCAL COMPLEMENT INHIBITOR


Mass: 10779.215 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) STAPHYLOCOCCUS AUREUS (bacteria) / Plasmid: PRSETB / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q6GFB4

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Sugars , 11 types, 18 molecules

#5: Polysaccharide
beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4) ...beta-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: 748.682 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2/a4-b1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][b-D-Manp]{}}}}}LINUCSPDB-CARE
#6: Polysaccharide beta-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2- ...beta-D-mannopyranose-(1-3)-beta-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
DManpb1-3DManpb1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2-2/a4-b1_b4-c1_c6-d1_d3-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}}}}}}LINUCSPDB-CARE
#7: Polysaccharide beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-6)-beta-D- ...beta-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]beta-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: 1072.964 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-3[DManpb1-6]DManpb1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2-2-2-2/a4-b1_b4-c1_c6-d1_d3-e1_d6-f1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}[(6+1)][b-D-Manp]{}}}}}}LINUCSPDB-CARE
#8: Polysaccharide alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2/a4-b1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][b-D-Manp]{}}}}}LINUCSPDB-CARE
#9: Polysaccharide alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...alpha-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.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_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
#10: 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)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#11: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-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]DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2-2/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][a-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][b-D-Manp]{}[(6+1)][b-D-Manp]{}}}}}LINUCSPDB-CARE
#12: 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
#13: Sugar ChemComp-BMA / beta-D-mannopyranose / beta-D-mannose / D-mannose / mannose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-mannopyranoseCOMMON NAMEGMML 1.0
b-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0
#14: Sugar ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0
#16: 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


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

-
Non-polymers , 2 types, 12 molecules

#15: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#17: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.1 Å3/Da / Density % sol: 68 % / Description: NONE
Crystal growpH: 6.5
Details: 75 MM SODIUM/POTASSIUM TARTRATE, 8.0% PEG 3350, 50 MM BIS-TRIS PROPANE, PH 6.5

-
Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 0.975
DetectorType: ADSC CCD / Detector: CCD / Date: Mar 2, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.975 Å / Relative weight: 1
ReflectionResolution: 3.9→40 Å / Num. obs: 137476 / % possible obs: 97.6 % / Observed criterion σ(I): -3.7 / Redundancy: 3.5 % / Biso Wilson estimate: 125.23 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 10.4
Reflection shellResolution: 3.9→4.1 Å / Redundancy: 3.4 % / Rmerge(I) obs: 0.69 / Mean I/σ(I) obs: 1.8 / % possible all: 92

-
Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2A74, 2I07,1RRK, 2QFF

2a74

2i07

1rrk

2qff


Resolution: 3.9→39.675 Å / SU ML: 0.57 / σ(F): 1.34 / Phase error: 26.44 / Stereochemistry target values: ML
Details: OCCUPANCY OF RESIDUES 968-1267 OF CHAIN H ARE SET TO 0.00
RfactorNum. reflection% reflection
Rfree0.2679 2088 1.5 %
Rwork0.2531 --
obs0.2533 137444 97.63 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 69.409 Å2 / ksol: 0.295 e/Å3
Displacement parametersBiso mean: 158.8 Å2
Baniso -1Baniso -2Baniso -3
1--8.266 Å20 Å2-4.9722 Å2
2---10.927 Å2-0 Å2
3---19.193 Å2
Refinement stepCycle: LAST / Resolution: 3.9→39.675 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms67266 0 715 8 67989
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00269445
X-RAY DIFFRACTIONf_angle_d0.51994103
X-RAY DIFFRACTIONf_dihedral_angle_d14.37925971
X-RAY DIFFRACTIONf_chiral_restr0.03410771
X-RAY DIFFRACTIONf_plane_restr0.00212013
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A759X-RAY DIFFRACTIONPOSITIONAL
12E759X-RAY DIFFRACTIONPOSITIONAL0.005
13C759X-RAY DIFFRACTIONPOSITIONAL0.003
14G759X-RAY DIFFRACTIONPOSITIONAL0.008
21A847X-RAY DIFFRACTIONPOSITIONAL
22E847X-RAY DIFFRACTIONPOSITIONAL0.005
23C847X-RAY DIFFRACTIONPOSITIONAL0.003
24G847X-RAY DIFFRACTIONPOSITIONAL0.008
31A636X-RAY DIFFRACTIONPOSITIONAL
32E636X-RAY DIFFRACTIONPOSITIONAL0.004
33C636X-RAY DIFFRACTIONPOSITIONAL0.001
34G636X-RAY DIFFRACTIONPOSITIONAL0.005
41A232X-RAY DIFFRACTIONPOSITIONAL
42E232X-RAY DIFFRACTIONPOSITIONAL0.008
43C232X-RAY DIFFRACTIONPOSITIONAL0.002
44G232X-RAY DIFFRACTIONPOSITIONAL0.011
51A328X-RAY DIFFRACTIONPOSITIONAL
52E328X-RAY DIFFRACTIONPOSITIONAL0.007
53C328X-RAY DIFFRACTIONPOSITIONAL0.001
54G328X-RAY DIFFRACTIONPOSITIONAL0.01
61A380X-RAY DIFFRACTIONPOSITIONAL
62E380X-RAY DIFFRACTIONPOSITIONAL0.006
63C380X-RAY DIFFRACTIONPOSITIONAL0.003
64G380X-RAY DIFFRACTIONPOSITIONAL0.01
71A817X-RAY DIFFRACTIONPOSITIONAL
72E817X-RAY DIFFRACTIONPOSITIONAL0.007
73C817X-RAY DIFFRACTIONPOSITIONAL0.004
74G817X-RAY DIFFRACTIONPOSITIONAL0.018
81A799X-RAY DIFFRACTIONPOSITIONAL
82E799X-RAY DIFFRACTIONPOSITIONAL0.006
83C799X-RAY DIFFRACTIONPOSITIONAL0.004
84G799X-RAY DIFFRACTIONPOSITIONAL0.019
91B485X-RAY DIFFRACTIONPOSITIONAL
92F485X-RAY DIFFRACTIONPOSITIONAL0.005
93D485X-RAY DIFFRACTIONPOSITIONAL0.002
94H485X-RAY DIFFRACTIONPOSITIONAL0.007
101F1142X-RAY DIFFRACTIONPOSITIONAL
102H1142X-RAY DIFFRACTIONPOSITIONAL0.007
111B1143X-RAY DIFFRACTIONPOSITIONAL
112D1143X-RAY DIFFRACTIONPOSITIONAL0.023
121B2267X-RAY DIFFRACTIONPOSITIONAL
122D2267X-RAY DIFFRACTIONPOSITIONAL0.003
123F2267X-RAY DIFFRACTIONPOSITIONAL0.002
131B1260X-RAY DIFFRACTIONPOSITIONAL
132D1260X-RAY DIFFRACTIONPOSITIONAL0.007
141F1081X-RAY DIFFRACTIONPOSITIONAL
142H1081X-RAY DIFFRACTIONPOSITIONAL0.003
151L1694X-RAY DIFFRACTIONPOSITIONAL
152J1694X-RAY DIFFRACTIONPOSITIONAL0.007
153K1694X-RAY DIFFRACTIONPOSITIONAL0.008
154I1694X-RAY DIFFRACTIONPOSITIONAL0.003
161L2310X-RAY DIFFRACTIONPOSITIONAL
162J2310X-RAY DIFFRACTIONPOSITIONAL0.004
163K2310X-RAY DIFFRACTIONPOSITIONAL0.004
164I2310X-RAY DIFFRACTIONPOSITIONAL0.002
171M682X-RAY DIFFRACTIONPOSITIONAL
172N682X-RAY DIFFRACTIONPOSITIONAL0.001
173P682X-RAY DIFFRACTIONPOSITIONAL0.001
174Q682X-RAY DIFFRACTIONPOSITIONAL0.001
181B847X-RAY DIFFRACTIONPOSITIONAL
182D847X-RAY DIFFRACTIONPOSITIONAL0.007
191F847X-RAY DIFFRACTIONPOSITIONAL
192H847X-RAY DIFFRACTIONPOSITIONAL0.011
201B986X-RAY DIFFRACTIONPOSITIONAL
202F986X-RAY DIFFRACTIONPOSITIONAL0.005
203D986X-RAY DIFFRACTIONPOSITIONAL0.004
204H986X-RAY DIFFRACTIONPOSITIONAL0.005
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.9-3.99070.34761320.33788356X-RAY DIFFRACTION91
3.9907-4.09040.33371300.32328440X-RAY DIFFRACTION92
4.0904-4.20080.28921250.30768671X-RAY DIFFRACTION94
4.2008-4.32430.31271370.29128738X-RAY DIFFRACTION95
4.3243-4.46370.2771290.26958929X-RAY DIFFRACTION97
4.4637-4.6230.25361390.25819034X-RAY DIFFRACTION99
4.623-4.80780.27371370.25129103X-RAY DIFFRACTION99
4.8078-5.02620.2371240.24469239X-RAY DIFFRACTION100
5.0262-5.29060.27461350.24189202X-RAY DIFFRACTION100
5.2906-5.62120.26991680.24679171X-RAY DIFFRACTION100
5.6212-6.05390.28241320.26219238X-RAY DIFFRACTION100
6.0539-6.66050.29811410.26029262X-RAY DIFFRACTION100
6.6605-7.61840.27991660.24699261X-RAY DIFFRACTION100
7.6184-9.5760.22411350.20499311X-RAY DIFFRACTION100
9.576-39.67730.21831580.21619401X-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)
11.54641.76210.10213.19530.92172.68390.16080.06250.1212-0.25170.0223-0.253-0.9798-0.0571-01.28580.1784-0.09641.44620.13591.3959117.05224.9421122.6966
21.70230.7532-0.65794.79180.82634.438-0.7430.1161-0.05820.58950.1076-0.1188-1.29060.6135-01.76930.23730.08621.5508-0.12171.2722.490697.263538.622
32.98641.761-1.94364.54660.02433.7197-0.17980.0772-0.8639-0.3436-0.01160.32771.1576-0.08-01.0550.3776-0.05611.28420.03590.932-7.057266.2038-17.7124
4-1.2970.757-0.31174.0501-0.092.319-0.76820.1069-0.54880.64150.0666-0.63951.2068-0.2716-0.00022.17130.226-0.48531.9184-0.15422.253887.0796-5.7896180.0393
53.80821.4175-0.42984.03690.78515.3290.06730.7354-0.2366-0.4414-0.0906-0.53770.22710.49350.00031.04010.1323-0.19380.99220.08021.01982.705928.6367106.957
64.26110.9621.6375.1971-1.26564.8515-0.2191-0.94950.17520.78160.3324-0.0374-0.7683-0.096-0.00021.09120.0480.15121.2387-0.14250.930951.582572.542836.9076
74.48221.65430.08764.72291.41865.69230.19170.92940.059-0.4208-0.30320.4396-0.1887-0.72510.00020.91130.31060.14670.9360.11550.717327.242362.75-33.8021
83.671.0032-0.54953.12330.44054.2855-0.387-0.7976-0.17341.15190.3714-0.8490.47650.3647-0.00041.36260.0255-0.20961.29570.22011.078758.081419.2852178.1859
93.6742-2.3195-0.7118.57990.30771.0238-0.15490.085-0.2711-0.0868-0.08-0.36810.3574-0.21870.00011.2634-0.2376-0.22890.8833-0.01011.167361.4413.7216119.9884
107.56623.9501-3.02126.5623-0.490.91870.29280.41-0.20830.1741-0.14140.4166-0.273-0.2328-0.00010.76010.014-0.08680.94310.15220.751340.177842.672721.7879
112.0295-1.67830.91558.4357-0.53252.39740.0821-0.10730.2349-0.5425-0.0091-0.3038-0.3608-0.12320.00031.1778-0.00420.32130.85670.16531.149648.501287.8521-21.143
125.17735.01293.24677.04442.19432.60520.2390.1184-0.04540.2851-0.1903-0.76560.51010.1914-0.00020.978-0.12820.00921.06870.06991.205469.896349.0158162.9193
133.13932.2233-0.59232.5308-0.15612.1390.0422-0.7339-0.72511.1501-0.44480.1107-0.28010.4827-0.00011.8012-0.0329-0.2081.17810.10081.409790.6351-0.8113138.2199
141.11640.0975-1.58814.56570.68370.8945-0.13910.0258-0.3351-0.72610.10240.5242-0.527-0.7287-0.00021.24170.0483-0.03741.47510.2231.554912.81463.447919.0067
154.76853.0159-0.03290.98840.43161.54840.0579-0.830.37370.22940.036-0.6808-0.1657-0.0037-0.00011.34620.16430.05311.01320.09241.054119.640192.0545-2.4626
16-1.9626-1.4598-2.13180.9006-0.5198-0.9798-0.43250.5469-0.05070.0026-0.1179-2.51270.74560.37960.00011.7232-0.12030.11331.9561-0.22993.574897.312527.8222160.4619
172.6843-0.2356-0.39383.1206-0.82431.8003-0.0318-1.2732-0.72510.5771-0.0276-0.20020.0354-0.4106-0.00021.29560.1615-0.41381.42790.3571.2446107.632915.0783141.1012
183.64250.95252.45714.2058-0.89444.31690.3990.67330.237-0.5544-0.10240.3363-0.3666-0.3824-01.23520.31990.19231.44170.12731.219412.988487.248720.3874
195.6041-0.45151.79895.96250.32777.8588-0.4256-1.25760.43520.40890.6038-0.13060.24660.47380.00020.96560.30560.12590.9758-0.01720.48062.537675.95710.654
200.6360.1476-1.2219-2.5723-0.01580.58190.19990.45330.32210.0114-0.0314-1.3749-0.08230.52330.00171.56780.3435-0.08842.12470.03473.08796.87714.2796162.1222
218.40460.79210.63963.9227-0.17332.3647-0.0863-0.84990.33840.3199-0.00750.2028-0.63680.0173-0.00031.0551-0.0664-0.1570.7793-0.00090.929672.372937.5812125.6686
225.044-2.6501-0.00496.2110.40163.260.2140.32640.47450.01560.0344-0.4808-0.5452-0.1023-0.00021.1152-0.15730.23351.11190.08740.794855.334274.75614.1863
238.6868-0.1153-1.40163.81860.95772.8214-0.0236-0.7894-0.7253-0.0727-0.1656-0.16570.2684-0.1622-0.00020.91480.10670.14040.81440.18690.718637.813953.8105-15.2087
243.4664-3.75010.50025.7010.37411.45860.17440.3697-0.6659-0.22420.01620.33040.54310.33930.00021.2609-0.1593-0.12321.21590.02281.158954.674317.0213155.4373
253.70910.2327-0.05273.829-1.14926.52240.18250.25690.12950.0331-0.07210.4247-0.1346-0.27790.00020.8482-0.1061-0.36760.8885-0.01491.110543.785534.2234109.1812
263.358-0.12721.43272.0310.64824.9161-0.0568-0.1761-0.141-0.11470.0702-0.4228-0.54120.4565-00.81210.06060.09321.2224-0.06321.186876.059949.166816.8554
275.8072-0.66080.82963.07172.51963.81270.07820.45440.2126-0.1814-0.2163-0.63940.14950.36110.00020.95550.02830.47221.0080.11551.07566.177857.4282-31.9557
284.15310.2092-2.12632.4770.26275.6464-0.2782-0.15330.29530.05540.00330.54280.2007-0.0835-0.00010.8715-0.0352-0.11431.03060.15521.197633.997342.7677157.8216
293.4277-1.7498-1.51683.2047-0.19412.0359-0.14310.73120.77750.0623-0.271-1.2884-0.16350.0876-0.00031.6050.2474-0.14882.16480.23311.506684.731624.226881.4638
303.5479-0.8342-2.92415.65262.12075.23080.0929-0.3480.51250.31690.4359-0.1882-0.72870.41460.00081.76070.1808-0.19381.9426-0.22281.192658.854566.212660.8317
312.6581-2.17330.94083.4606-0.63394.87570.17640.7741-0.5148-0.2119-0.57850.97040.444-0.3627-0.00061.47740.2950.11711.8864-0.17251.246824.974367.4928-59.3016
324.449-1.1405-1.5311.52160.77864.3722-1.0179-0.3363-0.2539-0.01070.8025-0.23831.07480.42090.00042.9133-0.02550.11892.12930.17641.582849.918425.7162201.842
332.4722-0.994-0.46035.8795-1.47854.86690.24770.506-0.3208-0.3507-0.1235-0.27470.4139-0.53820.00041.1971-0.3238-0.32331.2906-0.1851.318338.102614.2055101.8551
345.7370.3811.24092.48050.79493.2814-0.0592-0.58890.01670.26370.056-0.27840.3980.55310.00031.02290.1499-0.03911.17710.17791.165468.242930.282724.7946
353.0466-0.5640.02574.77262.03014.87770.20030.53020.115-0.276-0.08430.1299-0.2060.5262-0.00021.2957-0.12540.54641.38870.24621.379871.593477.3212-39.2435
366.18240.1793-1.18573.448-1.38894.4027-0.0769-0.55730.21160.48130.0605-0.0181-0.6612-0.35030.00061.25110.0558-0.04241.0972-0.261.341241.802561.6409165.7767
374.31170.86770.03071.294-0.73651.4589-0.16171.6668-0.0691-0.7448-0.1692-0.30490.09120.1988-01.61560.1599-0.07511.89610.07721.6108134.292711.125291.9492
387.58240.8403-1.48192.07420.21313.2734-0.21521.3771-0.0654-0.37420.06590.16670.228-0.17540.00010.88890.107-0.01851.0792-0.04210.7899-24.413581.7021-48.469
393.6570.15030.11233.0256-0.74624.52620.2533-1.13140.42931.379-0.4014-0.128-2.3627-0.9643-03.17270.53490.17882.3075-0.14141.60617.699594.830375.8399
402.4154-0.4097-1.12064.16090.74192.94-0.0810.68570.8152-0.5707-0.29931.4451-0.3134-0.1277-0.00021.90270.0085-0.71741.74820.02841.776631.07251.113577.1802
412.25010.29230.24813.42570.63223.2621-0.03390.60280.1085-0.244-0.2496-1.1105-0.0270.68410.00012.13320.15580.50872.02260.14721.597679.352140.7795-63.6735
427.75631.02921.77284.6067-1.35613.66850.1474-1.3347-0.31640.30590.2576-0.23640.22750.56580.00021.47170.1340.03232.02820.0221.9326108.263740.308732.5085
435.93580.50510.21073.07511.2461-0.6285-0.1604-0.72950.12060.63380.2219-0.2702-0.3528-0.52980.00011.44380.13110.17162.0091-0.07991.88071.773451.9385172.7879
444.48521.0639-2.2474.4844-1.18648.37960.03790.5480.3474-1.00650.1265-0.25771.0104-0.047301.38860.08260.19940.9379-0.0880.640256.728123.8242-42.1504
455.87120.1518-0.12585.7621.42643.25120.018-0.95560.31870.8536-0.45560.47880.1113-0.5404-01.446-0.38680.14081.72770.04821.39259.808516.3612163.9418
464.7295-0.3492-0.02294.3148-0.42684.93830.0053-0.8136-0.32160.8237-0.1649-0.4132-0.14460.7678-0.00011.4221-0.42830.00011.8036-0.03641.584799.987275.556622.97
476.75150.30710.83733.88781.12977.03550.27490.8073-0.0618-0.82740.00850.2018-0.97480.3490.00011.3432-0.0743-0.16140.90930.20540.864453.613567.753598.9073
484.39480.9299-1.36856.18-1.353.9072-0.1659-0.2697-0.28250.178-0.08030.02350.80110.139601.2291-0.08120.26880.8190.00081.021641.45676.3862-7.5643
493.3460.31840.83114.24211.26374.23280.33540.3349-0.90560.2968-0.1573-0.54130.55790.3796-01.3072-0.1955-0.17731.33680.03772.000320.9931-13.809137.4953
501.90080.3442-0.71922.6881-0.43962.76340.33270.2411.02730.1704-0.19310.4781-0.7913-0.4271-01.5402-0.1640.45461.68290.10922.417888.9973105.809-3.4462
513.30640.97991.02875.43430.97163.3274-0.1327-0.29760.20540.5428-0.1088-0.3292-0.4521-0.203501.2863-0.1114-0.31090.89510.09371.250768.874485.0904133.4295
524.72360.69111.86995.65420.0716.28820.01370.0875-0.15870.709-0.0769-0.55720.15850.4177-0.00040.92510.17410.32070.8302-0.08090.730767.634337.0996-11.936
535.4348-0.1546-1.75523.36230.13355.60330.1045-0.0752-0.16650.9213-0.28370.29680.1168-0.296-0.00021.1685-0.0182-0.31830.72330.22121.149142.553654.5814129.0454
542.04180.5286-0.80581.36660.32735.23620.3380.01280.8092-0.22140.0164-0.7033-0.3024-0.1592-00.8429-0.08230.20831.1436-0.01051.35282.613465.8206-5.3156
553.0746-0.37060.78482.4599-0.28373.71450.11880.2189-0.4873-0.24130.39450.4285-0.21570.281300.7849-0.2025-0.03870.9622-0.0451.391727.413226.0213135.7657
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND RESID 1:104
2X-RAY DIFFRACTION2CHAIN E AND RESID 1:104
3X-RAY DIFFRACTION3CHAIN C AND RESID 1:104
4X-RAY DIFFRACTION4CHAIN G AND RESID 1:104
5X-RAY DIFFRACTION5CHAIN A AND RESID 105:209
6X-RAY DIFFRACTION6CHAIN E AND RESID 105:209
7X-RAY DIFFRACTION7CHAIN C AND RESID 105:209
8X-RAY DIFFRACTION8CHAIN G AND RESID 105:209
9X-RAY DIFFRACTION9CHAIN A AND RESID 210:328
10X-RAY DIFFRACTION10CHAIN E AND RESID 210:328
11X-RAY DIFFRACTION11CHAIN C AND RESID 210:328
12X-RAY DIFFRACTION12CHAIN G AND RESID 210:328
13X-RAY DIFFRACTION13CHAIN A AND RESID 329:426
14X-RAY DIFFRACTION14CHAIN E AND RESID 329:426
15X-RAY DIFFRACTION15CHAIN C AND RESID 329:426
16X-RAY DIFFRACTION16CHAIN G AND RESID 329:426
17X-RAY DIFFRACTION17CHAIN A AND RESID 427:534
18X-RAY DIFFRACTION18CHAIN E AND RESID 427:534
19X-RAY DIFFRACTION19CHAIN C AND RESID 427:534
20X-RAY DIFFRACTION20CHAIN G AND RESID 427:534
21X-RAY DIFFRACTION21(CHAIN A AND RESID 535:578) OR (CHAIN B AND RESID 746:806)
22X-RAY DIFFRACTION22(CHAIN E AND RESID 535:578) OR (CHAIN F AND RESID 746:806)
23X-RAY DIFFRACTION23(CHAIN C AND RESID 535:578) OR (CHAIN D AND RESID 746:806)
24X-RAY DIFFRACTION24(CHAIN G AND RESID 535:578) OR (CHAIN H AND RESID 746:806)
25X-RAY DIFFRACTION25CHAIN B AND (RESID 807:911 OR RESID 727-745)
26X-RAY DIFFRACTION26CHAIN F AND (RESID 807:911 OR RESID 727-745)
27X-RAY DIFFRACTION27CHAIN D AND (RESID 807:911 OR RESID 727-745)
28X-RAY DIFFRACTION28CHAIN H AND (RESID 807:911 OR RESID 727-745)
29X-RAY DIFFRACTION29(CHAIN B AND RESID 912:969) OR (CHAIN B AND RESID 1269:1330)
30X-RAY DIFFRACTION30(CHAIN F AND RESID 912:969) OR (CHAIN F AND RESID 1269:1330)
31X-RAY DIFFRACTION31(CHAIN D AND RESID 912:969) OR (CHAIN D AND RESID 1269:1330)
32X-RAY DIFFRACTION32(CHAIN H AND RESID 912:969) OR (CHAIN H AND RESID 1269:1330)
33X-RAY DIFFRACTION33CHAIN B AND RESID 1331:1495
34X-RAY DIFFRACTION34CHAIN F AND RESID 1331:1495
35X-RAY DIFFRACTION35CHAIN D AND RESID 1331:1495
36X-RAY DIFFRACTION36CHAIN H AND RESID 1331:1495
37X-RAY DIFFRACTION37CHAIN B AND RESID 970:1268
38X-RAY DIFFRACTION38CHAIN D AND RESID 970:1268
39X-RAY DIFFRACTION39CHAIN F AND RESID 970:1268
40X-RAY DIFFRACTION40CHAIN B AND RESID 1496:1641
41X-RAY DIFFRACTION41CHAIN D AND RESID 1496:1641
42X-RAY DIFFRACTION42CHAIN F AND RESID 1496:1641
43X-RAY DIFFRACTION43CHAIN H AND RESID 1496:1641
44X-RAY DIFFRACTION44CHAIN I AND RESID 235:449
45X-RAY DIFFRACTION45CHAIN J AND RESID 235:449
46X-RAY DIFFRACTION46CHAIN K AND RESID 235:449
47X-RAY DIFFRACTION47CHAIN L AND RESID 235:449
48X-RAY DIFFRACTION48CHAIN I AND RESID 450:739
49X-RAY DIFFRACTION49CHAIN J AND RESID 450:739
50X-RAY DIFFRACTION50CHAIN K AND RESID 450:739
51X-RAY DIFFRACTION51CHAIN L AND RESID 450:739
52X-RAY DIFFRACTION52CHAIN M AND RESID 2:82
53X-RAY DIFFRACTION53CHAIN N AND RESID 2:82
54X-RAY DIFFRACTION54CHAIN P AND RESID 2:82
55X-RAY DIFFRACTION55CHAIN Q AND RESID 2:82

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