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- PDB-2xwj: Crystal Structure of Complement C3b in Complex with Factor B -

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Basic information

Entry
Database: PDB / ID: 2xwj
TitleCrystal Structure of Complement C3b in Complex with Factor B
Components
  • (COMPLEMENT C3 ...) x 2
  • COMPLEMENT FACTOR B
KeywordsHYDROLASE / IMMUNE SYSTEM / PRO-CONVERTASE / SERINE PROTEASE / CONFORMATIONAL CHANGES / ALTERNATIVE PATHWAY
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 / complement binding / 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 ...alternative-complement-pathway C3/C5 convertase / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / complement binding / 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 / Activation of C3 and C5 / positive regulation of phagocytosis, engulfment / positive regulation of lipid storage / positive regulation of G protein-coupled receptor signaling pathway / positive regulation of type IIa hypersensitivity / complement receptor mediated signaling pathway / 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 / response to bacterium / Post-translational protein phosphorylation / fatty acid metabolic process / 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 protein phosphorylation / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / secretory granule lumen / G alpha (i) signalling events / blood microparticle / immune response / G protein-coupled receptor signaling pathway / receptor ligand activity / endoplasmic reticulum lumen / inflammatory response / 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
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 ...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 / 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 / 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 / Glycosyltransferase - #20 / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG3 / : / A-macroglobulin receptor binding domain / Macroglobulin domain MG3 / A-macroglobulin receptor / Netrin domain / NTR domain profile. / Alpha-2-macroglobulin / Macroglobulin domain / Tissue inhibitor of metalloproteinases-like, OB-fold / 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) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / 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 / VWFA domain profile. / von Willebrand factor (vWF) type A domain / von Willebrand factor, type A / Single Sheet / von Willebrand factor A-like domain superfamily / Special / Ribbon / 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 / Jelly Rolls / Immunoglobulin-like fold / Immunoglobulins / Peptidase S1, PA clan / Beta Barrel / Immunoglobulin-like / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
NICKEL (II) ION / Complement factor B / Complement C3
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4 Å
AuthorsForneris, F. / Ricklin, D. / Wu, J. / Tzekou, A. / Wallace, R.S. / Lambris, J.D. / Gros, P.
CitationJournal: Science / Year: 2010
Title: Structures of C3B in Complex with Factors B and D Give Insight Into Complement Convertase Formation.
Authors: Forneris, F. / Ricklin, D. / Wu, J. / Tzekou, A. / Wallace, R.S. / Lambris, J.D. / Gros, P.
History
DepositionNov 4, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 12, 2011Provider: repository / Type: Initial release
Revision 1.1Apr 11, 2012Group: Database references / Other ...Database references / Other / Refinement description / Version format compliance
Revision 1.2Jul 29, 2020Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _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.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Dec 20, 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
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.4Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification
Remark 700 SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "II" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "II" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "JH" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "KG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "LI" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL.

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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 C3 ALPHA CHAIN
C: COMPLEMENT C3 BETA CHAIN
D: COMPLEMENT C3 ALPHA CHAIN
E: COMPLEMENT C3 BETA CHAIN
F: COMPLEMENT C3 ALPHA CHAIN
G: COMPLEMENT C3 BETA CHAIN
H: COMPLEMENT C3 ALPHA CHAIN
I: COMPLEMENT FACTOR B
J: COMPLEMENT FACTOR B
K: COMPLEMENT FACTOR B
L: COMPLEMENT FACTOR B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)1,036,65424
Polymers1,034,64912
Non-polymers2,00412
Water1448
1
A: COMPLEMENT C3 BETA CHAIN
B: COMPLEMENT C3 ALPHA CHAIN
I: COMPLEMENT FACTOR B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)259,1636
Polymers258,6623
Non-polymers5013
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16430 Å2
ΔGint-61.5 kcal/mol
Surface area97180 Å2
MethodPISA
2
C: COMPLEMENT C3 BETA CHAIN
D: COMPLEMENT C3 ALPHA CHAIN
J: COMPLEMENT FACTOR B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)259,1636
Polymers258,6623
Non-polymers5013
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16600 Å2
ΔGint-59.5 kcal/mol
Surface area97190 Å2
MethodPISA
3
G: COMPLEMENT C3 BETA CHAIN
H: COMPLEMENT C3 ALPHA CHAIN
L: COMPLEMENT FACTOR B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)259,1636
Polymers258,6623
Non-polymers5013
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16810 Å2
ΔGint-60 kcal/mol
Surface area96610 Å2
MethodPISA
4
E: COMPLEMENT C3 BETA CHAIN
F: COMPLEMENT C3 ALPHA CHAIN
K: COMPLEMENT FACTOR B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)259,1636
Polymers258,6623
Non-polymers5013
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16560 Å2
ΔGint-59.5 kcal/mol
Surface area97370 Å2
MethodPISA
Unit cell
Length a, b, c (Å)262.160, 297.870, 341.440
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
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
310
410
111
211
311
411
112
212
113
213
114
214
314
414
115
215
116
216
117
217
118
218
119
219
120
220
121
221
122
222
123
223
323
423

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 1:102 )
211CHAIN G AND (RESSEQ 1:102 )
112CHAIN C AND (RESSEQ 1:102 )
212CHAIN E AND (RESSEQ 1:102 )
113CHAIN A AND (RESSEQ 103:650 ) OR CHAIN B AND (RESSEQ 744:804 )
213CHAIN C AND (RESSEQ 103:650 ) OR CHAIN D AND (RESSEQ 744:804 )
313CHAIN E AND (RESSEQ 103:650 ) OR CHAIN F AND (RESSEQ 744:804 )
413CHAIN G AND (RESSEQ 103:650 ) OR CHAIN H AND (RESSEQ 744:804 )
114CHAIN B AND (RESSEQ 805:900 )
214CHAIN D AND (RESSEQ 805:900 )
314CHAIN F AND (RESSEQ 805:900 )
414CHAIN H AND (RESSEQ 805:900 )
115CHAIN B AND (RESSEQ 913:965 OR RESSEQ 1268:1331 )
215CHAIN D AND (RESSEQ 913:965 OR RESSEQ 1268:1331 )
315CHAIN F AND (RESSEQ 913:965 OR RESSEQ 1268:1331 )
415CHAIN H AND (RESSEQ 913:965 OR RESSEQ 1268:1331 )
116CHAIN B AND (RESSEQ 969:1102 )
216CHAIN D AND (RESSEQ 969:1102 )
316CHAIN F AND (RESSEQ 969:1102 )
416CHAIN H AND (RESSEQ 969:1102 )
117CHAIN B AND (RESSEQ 1108:1264 )
217CHAIN D AND (RESSEQ 1108:1264 )
317CHAIN F AND (RESSEQ 1108:1264 )
417CHAIN H AND (RESSEQ 1108:1264 )
118CHAIN B AND (RESSEQ 1332:1480 )
218CHAIN D AND (RESSEQ 1332:1480 )
318CHAIN F AND (RESSEQ 1332:1480 )
418CHAIN H AND (RESSEQ 1332:1480 )
119CHAIN B AND (RESSEQ 1485:1498 )
219CHAIN D AND (RESSEQ 1485:1498 )
319CHAIN F AND (RESSEQ 1485:1498 )
419CHAIN H AND (RESSEQ 1485:1498 )
1110CHAIN B AND (RESSEQ 1500:1531 )
2110CHAIN D AND (RESSEQ 1500:1531 )
3110CHAIN F AND (RESSEQ 1500:1531 )
4110CHAIN H AND (RESSEQ 1500:1531 )
1111CHAIN B AND (RESSEQ 1538:1638 )
2111CHAIN D AND (RESSEQ 1538:1638 )
3111CHAIN F AND (RESSEQ 1538:1638 )
4111CHAIN H AND (RESSEQ 1538:1638 )
1112CHAIN I AND (RESSEQ 10:68 )
2112CHAIN L AND (RESSEQ 10:68 )
1113CHAIN J AND (RESSEQ 10:68 )
2113CHAIN K AND (RESSEQ 10:68 )
1114CHAIN I AND (RESSEQ 78:220 )
2114CHAIN J AND (RESSEQ 78:220 )
3114CHAIN K AND (RESSEQ 78:220 )
4114CHAIN L AND (RESSEQ 78:220 )
1115CHAIN I AND (RESSEQ 244:250 )
2115CHAIN L AND (RESSEQ 244:250 )
1116CHAIN J AND (RESSEQ 244:250 )
2116CHAIN K AND (RESSEQ 244:250 )
1117CHAIN I AND (RESSEQ 260:324 )
2117CHAIN L AND (RESSEQ 260:324 )
1118CHAIN J AND (RESSEQ 260:324 )
2118CHAIN K AND (RESSEQ 260:324 )
1119CHAIN I AND (RESSEQ 330:340 )
2119CHAIN L AND (RESSEQ 330:340 )
1120CHAIN J AND (RESSEQ 330:340 )
2120CHAIN K AND (RESSEQ 330:340 )
1121CHAIN I AND (RESSEQ 360:455 )
2121CHAIN L AND (RESSEQ 360:455 )
1122CHAIN J AND (RESSEQ 360:455 )
2122CHAIN K AND (RESSEQ 360:455 )
1123CHAIN I AND (RESSEQ 485:741 )
2123CHAIN J AND (RESSEQ 485:741 )
3123CHAIN K AND (RESSEQ 485:741 )
4123CHAIN L AND (RESSEQ 485:741 )

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14
15
16
17
18
19
20
21
22
23

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Components

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COMPLEMENT C3 ... , 2 types, 8 molecules ACEGBDFH

#1: Protein
COMPLEMENT C3 BETA CHAIN


Mass: 71393.320 Da / Num. of mol.: 4 / Fragment: RESIDUES 23-667 / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Organ: BLOOD / References: UniProt: P01024
#2: Protein
COMPLEMENT C3 ALPHA CHAIN


Mass: 104074.148 Da / Num. of mol.: 4 / Fragment: RESIDUES 749-1663 / Mutation: YES / Source method: isolated from a natural source / Source: (natural) HOMO SAPIENS (human) / Organ: BLOOD / References: UniProt: P01024

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Protein / Sugars , 2 types, 12 molecules IJKL

#3: Protein
COMPLEMENT FACTOR B / C3/C5 CONVERTASE / GLYCINE-RICH BETA GLYCOPROTEIN / GBG / PBF2 / PROPERDIN FACTOR B


Mass: 83194.859 Da / Num. of mol.: 4 / Fragment: COMPLEMENT FACTOR B / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Organ: BLOOD / Plasmid: PUPE.05.05 / Cell line (production host): HEK293-ES / Production host: HOMO SAPIENS (human) / References: UniProt: P00751
#4: 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.: 8
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

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Non-polymers , 2 types, 12 molecules

#5: Chemical
ChemComp-NI / NICKEL (II) ION


Mass: 58.693 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ni
#6: Water ChemComp-HOH / water


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

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN B, GLN1013 TO GLU ENGINEERED RESIDUE IN CHAIN D, GLN1013 TO GLU ...ENGINEERED RESIDUE IN CHAIN B, GLN1013 TO GLU ENGINEERED RESIDUE IN CHAIN D, GLN1013 TO GLU ENGINEERED RESIDUE IN CHAIN F, GLN1013 TO GLU ENGINEERED RESIDUE IN CHAIN H, GLN1013 TO GLU ENGINEERED RESIDUE IN CHAIN I, ASP 279 TO GLY ENGINEERED RESIDUE IN CHAIN I, ASN 285 TO ASP ENGINEERED RESIDUE IN CHAIN J, ASP 279 TO GLY ENGINEERED RESIDUE IN CHAIN J, ASN 285 TO ASP ENGINEERED RESIDUE IN CHAIN K, ASP 279 TO GLY ENGINEERED RESIDUE IN CHAIN K, ASN 285 TO ASP ENGINEERED RESIDUE IN CHAIN L, ASP 279 TO GLY ENGINEERED RESIDUE IN CHAIN L, ASN 285 TO ASP
Has protein modificationY
Sequence detailsMUTANT D254G N260D, PLUS TWO ADDITIONAL ALANINES AT C-TER. RESIDUE 991 FOR CHAINS B,D,F,H HAS BEEN ...MUTANT D254G N260D, PLUS TWO ADDITIONAL ALANINES AT C-TER. RESIDUE 991 FOR CHAINS B,D,F,H HAS BEEN CONVERTED FROM GLN TO GLU IN THE CONVERSION OF C3 TO C3B

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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: 2.78 Å3/Da / Density % sol: 55.7 % / Description: NONE
Crystal growpH: 4 / Details: pH 4.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID14-4 / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD / Date: Mar 12, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 4→75 Å / Num. obs: 104810 / % possible obs: 93.4 % / Observed criterion σ(I): 3.5 / Redundancy: 4.3 % / Biso Wilson estimate: 78.22 Å2 / Rmerge(I) obs: 0.16 / Net I/σ(I): 7.2
Reflection shellResolution: 4→4.22 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 3.2 / % possible all: 79

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PARTIAL MODEL FROM 2XWB

2xwb


Resolution: 4→72.757 Å / SU ML: 0.52 / σ(F): 1.34 / Phase error: 29.83 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2808 5237 5 %
Rwork0.2275 --
obs0.2301 104583 93.07 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 59.838 Å2 / ksol: 0.303 e/Å3
Displacement parametersBiso mean: 126.15 Å2
Baniso -1Baniso -2Baniso -3
1--5.1812 Å20 Å20 Å2
2---48.1353 Å20 Å2
3----13.3221 Å2
Refinement stepCycle: LAST / Resolution: 4→72.757 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms71136 0 116 8 71260
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00172836
X-RAY DIFFRACTIONf_angle_d0.35798559
X-RAY DIFFRACTIONf_dihedral_angle_d7.17326931
X-RAY DIFFRACTIONf_chiral_restr0.02411024
X-RAY DIFFRACTIONf_plane_restr0.00212755
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A771X-RAY DIFFRACTIONPOSITIONAL
12G771X-RAY DIFFRACTIONPOSITIONAL0.091
21C771X-RAY DIFFRACTIONPOSITIONAL
22E771X-RAY DIFFRACTIONPOSITIONAL0.009
31A4709X-RAY DIFFRACTIONPOSITIONAL
32C4709X-RAY DIFFRACTIONPOSITIONAL0.017
33E4709X-RAY DIFFRACTIONPOSITIONAL0.018
34G4709X-RAY DIFFRACTIONPOSITIONAL0.015
41B790X-RAY DIFFRACTIONPOSITIONAL
42D790X-RAY DIFFRACTIONPOSITIONAL0.015
43F790X-RAY DIFFRACTIONPOSITIONAL0.018
44H790X-RAY DIFFRACTIONPOSITIONAL0.008
51B908X-RAY DIFFRACTIONPOSITIONAL
52D908X-RAY DIFFRACTIONPOSITIONAL0.057
53F908X-RAY DIFFRACTIONPOSITIONAL0.052
54H908X-RAY DIFFRACTIONPOSITIONAL0.049
61B1048X-RAY DIFFRACTIONPOSITIONAL
62D1048X-RAY DIFFRACTIONPOSITIONAL0.026
63F1048X-RAY DIFFRACTIONPOSITIONAL0.02
64H1048X-RAY DIFFRACTIONPOSITIONAL0.02
71B1238X-RAY DIFFRACTIONPOSITIONAL
72D1238X-RAY DIFFRACTIONPOSITIONAL0.014
73F1238X-RAY DIFFRACTIONPOSITIONAL0.012
74H1238X-RAY DIFFRACTIONPOSITIONAL0.014
81B1133X-RAY DIFFRACTIONPOSITIONAL
82D1133X-RAY DIFFRACTIONPOSITIONAL0.034
83F1133X-RAY DIFFRACTIONPOSITIONAL0.033
84H1133X-RAY DIFFRACTIONPOSITIONAL0.028
91B115X-RAY DIFFRACTIONPOSITIONAL
92D115X-RAY DIFFRACTIONPOSITIONAL0.03
93F115X-RAY DIFFRACTIONPOSITIONAL0.047
94H115X-RAY DIFFRACTIONPOSITIONAL0.014
101B246X-RAY DIFFRACTIONPOSITIONAL
102D246X-RAY DIFFRACTIONPOSITIONAL0.107
103F246X-RAY DIFFRACTIONPOSITIONAL0.107
104H246X-RAY DIFFRACTIONPOSITIONAL0.106
111B827X-RAY DIFFRACTIONPOSITIONAL
112D827X-RAY DIFFRACTIONPOSITIONAL0.014
113F827X-RAY DIFFRACTIONPOSITIONAL0.015
114H827X-RAY DIFFRACTIONPOSITIONAL0.012
121I453X-RAY DIFFRACTIONPOSITIONAL
122L453X-RAY DIFFRACTIONPOSITIONAL0.009
131J436X-RAY DIFFRACTIONPOSITIONAL
132K436X-RAY DIFFRACTIONPOSITIONAL0.136
141I1115X-RAY DIFFRACTIONPOSITIONAL
142J1115X-RAY DIFFRACTIONPOSITIONAL0.053
143K1115X-RAY DIFFRACTIONPOSITIONAL0.053
144L1115X-RAY DIFFRACTIONPOSITIONAL0.052
151I59X-RAY DIFFRACTIONPOSITIONAL
152L59X-RAY DIFFRACTIONPOSITIONAL0.021
161J59X-RAY DIFFRACTIONPOSITIONAL
162K59X-RAY DIFFRACTIONPOSITIONAL0.011
171I523X-RAY DIFFRACTIONPOSITIONAL
172L523X-RAY DIFFRACTIONPOSITIONAL0.008
181J523X-RAY DIFFRACTIONPOSITIONAL
182K523X-RAY DIFFRACTIONPOSITIONAL0.01
191I85X-RAY DIFFRACTIONPOSITIONAL
192L85X-RAY DIFFRACTIONPOSITIONAL0.01
201J85X-RAY DIFFRACTIONPOSITIONAL
202K85X-RAY DIFFRACTIONPOSITIONAL0.011
211I764X-RAY DIFFRACTIONPOSITIONAL
212L764X-RAY DIFFRACTIONPOSITIONAL0.009
221J764X-RAY DIFFRACTIONPOSITIONAL
222K764X-RAY DIFFRACTIONPOSITIONAL0.083
231I2030X-RAY DIFFRACTIONPOSITIONAL
232J2030X-RAY DIFFRACTIONPOSITIONAL0.009
233K2030X-RAY DIFFRACTIONPOSITIONAL0.01
234L2030X-RAY DIFFRACTIONPOSITIONAL0.008
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4-4.04550.34631310.28622766X-RAY DIFFRACTION77
4.0455-4.0930.30831420.27522789X-RAY DIFFRACTION79
4.093-4.1430.35891450.26342753X-RAY DIFFRACTION78
4.143-4.19540.31391530.25982815X-RAY DIFFRACTION80
4.1954-4.25060.29031540.24272816X-RAY DIFFRACTION80
4.2506-4.30880.31071400.24712888X-RAY DIFFRACTION81
4.3088-4.37040.26791460.23822916X-RAY DIFFRACTION83
4.3704-4.43560.28441680.23043029X-RAY DIFFRACTION85
4.4356-4.50490.28511500.23643064X-RAY DIFFRACTION87
4.5049-4.57870.31221670.22763149X-RAY DIFFRACTION89
4.5787-4.65770.28111620.22683234X-RAY DIFFRACTION92
4.6577-4.74240.26531640.2183367X-RAY DIFFRACTION94
4.7424-4.83360.29691720.20913443X-RAY DIFFRACTION97
4.8336-4.93220.26011820.20623469X-RAY DIFFRACTION98
4.9322-5.03940.25841910.2163464X-RAY DIFFRACTION99
5.0394-5.15660.29381850.20683514X-RAY DIFFRACTION99
5.1566-5.28550.25941980.21043526X-RAY DIFFRACTION100
5.2855-5.42840.25591810.20843546X-RAY DIFFRACTION100
5.4284-5.58810.26451740.22113544X-RAY DIFFRACTION99
5.5881-5.76840.30662030.22223523X-RAY DIFFRACTION100
5.7684-5.97440.30332020.22453546X-RAY DIFFRACTION100
5.9744-6.21350.31881900.22123560X-RAY DIFFRACTION100
6.2135-6.49620.27031880.2273517X-RAY DIFFRACTION100
6.4962-6.83840.29581820.23243585X-RAY DIFFRACTION100
6.8384-7.26650.30731770.2173571X-RAY DIFFRACTION100
7.2665-7.82690.23571870.20133568X-RAY DIFFRACTION100
7.8269-8.61350.22592130.18763567X-RAY DIFFRACTION100
8.6135-9.85720.19651840.17653609X-RAY DIFFRACTION100
9.8572-12.40910.21011990.18293606X-RAY DIFFRACTION99
12.4091-72.76930.35772070.30953602X-RAY DIFFRACTION96
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)
10.29850.15160.25570.4901-0.43750.97610.01170.240.0686-0.0432-0.4405-0.1749-0.26550.18630.31850.3520.290.0170.4920.12320.286779.0641-50.9825-12.3543
20.26440.13840.39280.6364-0.3370.53660.01560.15830.1623-0.2197-0.2098-0.40270.1130.45680.33380.27660.34540.21420.52180.32920.4681100.684-49.2548-33.7788
30.9659-0.19560.42091.196-0.76140.4957-0.39430.22970.0058-0.31650.0082-0.24690.260.1930.31310.32360.22320.07590.52030.06680.260684.2614-50.7048-28.3451
41.03920.3953-0.68320.6176-0.52690.77690.19720.2531-0.17-0.4362-0.1803-0.24060.2275-0.3927-0.03550.75770.12380.01510.34010.09470.288164.74-30.3653-54.5326
50.2660.02790.07940.53090.08140.0251-0.1485-0.3583-0.00570.2431-0.28830.0655-0.08670.51260.39991.03230.2440.02130.76990.12960.269267.6876-10.0123-14.4835
60.0643-0.0431-0.0280.07440.09710.17060.0881-0.0501-0.2073-0.26750.145-0.388-0.14810.28250.3627-0.25690.4513-0.4298-0.19910.60910.112486.7805-43.242824.8602
70.49140.30810.42750.89410.5460.5355-0.2041-0.4556-0.0848-0.19650.03870.23670.0563-0.41140.26380.6720.28720.06730.73860.01620.092965.6953-15.743-14.4057
81.90250.4664-0.17880.5003-0.00810.0621-0.3454-0.3738-0.2597-0.3278-0.0203-0.2304-0.15610.11590.22460.39280.05180.0850.31070.13640.228677.5506-6.1388-62.3836
90.7814-0.62970.41480.6217-0.42191.3081-0.23230.19190.07030.0321-0.1085-0.10310.09430.15290.14970.21930.0935-0.09250.2343-0.01720.183737.65928.1842-60.0688
100.44720.2676-0.11920.42520.07240.2102-0.0376-0.0677-0.1122-0.183-0.1710.3569-0.0013-0.06280.16270.1335-0.06010.11730.1988-0.18721.0232152.1216-20.4689-65.6906
110.0937-0.0098-0.15760.21720.0141.07210.2577-0.07450.24830.09020.35780.1158-0.0110.1288-0.53860.0737-0.05180.00190.3416-0.07250.618152.6082-56.2246-54.8602
120.2448-0.2175-0.46430.82560.07730.44780.00380.06120.19990.27170.04150.5440.0181-0.08920.10140.1920.00520.16430.2534-0.14460.8566138.2187-37.4162-36.9194
130.30140.1702-0.30861.91830.05950.5109-0.24670.12270.26760.01630.10731.04180.19110.0850.0325-0.032-0.0315-0.03630.1704-0.04220.4325132.5885-80.2555-46.6951
140.0812-0.08040.13290.80760.28980.4680.1329-0.2093-0.10120.110.1041-0.5042-0.04760.4248-0.10780.1507-0.09930.07410.4270.08820.3899177.0192-71.7956-50.1961
150.42750.4212-0.1160.4038-0.12320.18740.0307-0.1794-0.1562-0.0155-0.0151-0.178-0.06320.30630.01430.20010.00630.23040.3503-0.04380.3391192.3748-23.8333-64.091
161.20180.23570.72850.21510.1810.51880.32420.1187-0.3401-0.18040.0366-0.1736-0.07630.1846-0.2540.12560.12910.11330.61430.06080.4731173.0738-70.6314-54.3403
170.256-0.05250.09681.3467-0.1130.0547-0.1748-0.181-0.12240.73640.19520.01590.1934-0.134-0.00740.5356-0.06730.10830.5703-0.05770.3001140.8412-92.3193-22.4668
180.4652-0.5027-0.43271.2078-0.2981.2164-0.1243-0.0034-0.14840.3032-0.1031-0.0105-0.1506-0.34440.15970.1136-0.0205-0.10410.22650.01920.1271150.6198-123.9547-48.6416
190.60960.33890.23390.47960.15590.11050.0924-0.005-0.05350.1903-0.1511-0.61050.03980.02710.00720.1338-0.1269-0.28870.21450.27090.9225110.9091-39.946861.2661
200.1540.1096-0.02660.50460.00170.2097-0.0594-0.18610.07690.0149-0.275-0.7197-0.09820.01640.27320.38140.014-0.07220.35560.51351.3385119.8014-66.432227.5704
210.47080.42130.23431.1785-0.37161.08370.12890.09580.4792-0.1895-0.535-0.0237-0.04590.32780.30530.3799-0.0267-0.12780.37760.50481.217125.5388-29.982433.2112
220.053-0.00240.13420.01610.03070.33830.06430.18410.21030.09460.1474-0.1453-0.00520.1414-0.15810.0963-0.1461-0.23890.39860.49031.6836129.5344-41.570551.41
230.5282-0.7201-0.00442.0978-0.37140.1242-0.09590.03630.29070.35860.32660.8201-0.04320.0547-0.20020.34440.1822-0.09740.25290.18040.9763113.5471-36.80246.1976
240.20220.0638-0.37160.6755-0.19160.2953-0.20370.07230.26780.1897-0.1143-0.76910.15860.11040.19260.11230.0008-0.17590.26380.29110.9864120.2845-84.091446.6531
251.2912-0.2525-0.06420.7461-0.23570.30410.28390.023-0.2060.3652-0.1672-0.0486-0.0637-0.0045-0.03970.1973-0.0981-0.06860.41540.22870.388370.2718-29.49263.4081
260.73750.1090.17190.9907-0.43760.3687-0.0414-0.20690.2305-0.2344-0.0013-0.18150.2355-0.00210.01290.15310.05010.03220.22310.27360.6402113.3889-94.732432.4994
270.27490.3628-0.06250.5309-0.13420.28880.00410.00830.1387-0.2481-0.03820.18920.10330.27550.00030.1276-0.091-0.12410.45890.26030.5578110.3371-129.28847.2656
280.1832-0.043-0.02290.3939-0.20940.1205-0.1186-0.2220.25210.38790.14590.0822-0.6041-0.2606-0.13241.11340.57310.35970.41820.35030.006351.2331-94.233-13.4427
291.6185-1.0613-0.36751.2281-0.06281.12890.03730.0098-0.2973-0.05970.15940.3991-0.8731-0.8759-0.19790.64740.68030.24590.89650.27190.334231.8108-94.7129-35.8139
300.23990.280.12091.3830.85450.52160.21240.37060.2101-0.16630.6687-0.0733-0.4590.1006-0.67550.85260.3310.29460.765-0.06450.390937.0458-92.7027-18.2648
310.1112-0.119-0.07990.4980.22880.65560.07760.16990.1663-0.34680.19620.1237-0.2324-0.2511-0.21220.82970.08930.21880.40350.07350.158466.3329-113.8353-54.3964
321.1449-0.17340.02640.36430.06130.0080.19770.8148-0.09320.1451-0.1604-0.036-0.5294-0.3098-0.03471.06030.16790.27680.83730.07220.166563.1439-134.7039-14.0261
33-0.0466-0.0138-0.00150.1819-0.29981.4612-0.36230.06480.1176-0.0597-0.15030.0708-0.2401-0.621-0.8885-0.0826-0.02970.4026-0.20230.8105-1.29145.1057-104.675125.6968
341.2660.46310.35322.9445-1.30770.8698-0.015-0.61350.04490.3271-0.1433-0.322-0.6641-0.38790.11440.84460.18670.00190.66480.20360.190866.0153-129.2054-14.3853
352.441-0.09010.02271.1229-0.16840.27620.223-0.5030.0562-0.3157-0.29930.28280.1264-0.08840.03150.4233-0.03850.05090.4323-0.03130.37355.0244-137.963-62.9953
360.51480.4826-0.3351.6890.34991.1549-0.11360.25560.29550.26580.02040.63490.0239-0.184-0.05890.17990.11980.1720.28050.21470.410593.7133-152.0937-59.1545
370.4618-0.0849-0.00880.2567-0.17560.0776-0.05660.2333-0.0838-0.00580.0295-0.07750.39070.09620.00620.41420.0462-0.08280.3161-0.06780.190942.3316-27.4327-49.4428
380.9891-0.6469-0.59861.62240.74610.9279-0.18520.3954-0.33710.20660.03440.53230.4461-0.1578-0.01610.12670.0216-0.07610.22530.10240.161923.008-15.4543-36.2586
390.21680.1074-0.36110.1224-0.06161.5938-0.0366-0.2306-0.24820.09650.0263-0.02690.40480.45660.18060.88850.44830.24590.63480.33490.335141.2639-37.4295-5.5094
401.6453-2.0494-1.04652.68381.3571.793-0.4888-0.1449-0.68460.24460.15940.6972-0.06540.01330.19950.28120.00170.10870.38090.20350.4029125.538-110.8853-65.4836
410.0531-0.06740.0230.53930.28110.3660.0925-0.22230.2865-0.28360.29930.04740.0462-0.185-0.33260.1971-0.1246-0.11050.6347-0.09730.608143.4736-82.3134-65.3801
421.3740.79360.80661.12830.80730.68110.245-0.4677-0.40.4879-0.2367-0.11360.2489-0.4587-0.03430.27620.1085-0.02910.4538-0.00170.0219154.8606-105.7368-79.5243
430.97240.259-0.55411.1103-0.15460.4469-0.040.07020.2534-0.60260.1827-0.2163-0.0348-0.0988-0.09020.42910.05630.27560.20690.02110.2705166.4268-65.9908-87.3892
440.689-1.2203-0.54962.34740.89662.9813-0.681-0.14910.00840.4369-0.1108-0.1109-0.07370.02860.8450.56750.2327-0.05030.2932-0.03481.1911136.3965-116.303565.2369
451.3816-0.74790.75350.4196-0.34850.4026-0.09820.06850.18450.2757-0.0262-0.3933-0.18220.00150.1270.36920.0337-0.33030.36790.32360.9607119.2273-88.075164.7497
460.4516-0.1668-0.05390.1709-0.07590.7132-0.04560.1541-0.20850.0406-0.1180.00250.33180.0364-0.1910.3885-0.1004-0.28340.3140.13370.2295107.3295-111.025279.1887
470.7387-0.24770.07440.18870.12690.42040.0771-0.02680.21530.91980.144-0.05040.05260.0162-0.22510.7930.0887-0.0080.16370.12350.840295.8384-71.170286.2962
480.3975-0.20490.24310.0652-0.150.20860.1728-0.0956-0.06930.0065-0.00770.1206-0.1239-0.3001-0.20.6666-0.09410.1720.47690.1560.305288.4394-116.3766-49.0474
491.01091.0745-1.4391.9695-0.92162.5779-0.36890.2766-0.3125-0.14590.2487-0.50250.5154-0.42760.11420.12940.01980.07150.21330.06270.1784107.5709-128.3525-36.4414
500.4655-0.0794-0.1810.6894-0.1190.05190.0321-0.08610.08810.20680.26240.0287-0.0743-0.0659-0.22510.75890.1418-0.09350.454-0.05410.111288.9334-106.7173-5.3892
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 1:190)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 191:546)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 547:642)
4X-RAY DIFFRACTION4(CHAIN B AND RESID 730:911)
5X-RAY DIFFRACTION5(CHAIN B AND RESID 912:969)
6X-RAY DIFFRACTION6(CHAIN B AND RESID 970:1262)
7X-RAY DIFFRACTION7(CHAIN B AND RESID 1263:1337)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 1338:1499)
9X-RAY DIFFRACTION9(CHAIN B AND RESID 1500:1641)
10X-RAY DIFFRACTION10(CHAIN C AND RESID 1:103)
11X-RAY DIFFRACTION11(CHAIN C AND RESID 104:204)
12X-RAY DIFFRACTION12(CHAIN C AND RESID 205:642)
13X-RAY DIFFRACTION13(CHAIN D AND RESID 730:914)
14X-RAY DIFFRACTION14(CHAIN D AND RESID 915:968)
15X-RAY DIFFRACTION15(CHAIN D AND RESID 969:1265)
16X-RAY DIFFRACTION16(CHAIN D AND RESID 1266:1336)
17X-RAY DIFFRACTION17(CHAIN D AND RESID 1337:1500)
18X-RAY DIFFRACTION18(CHAIN D AND RESID 1503:1641)
19X-RAY DIFFRACTION19(CHAIN E AND RESID 1:170)
20X-RAY DIFFRACTION20(CHAIN E AND RESID 171:317)
21X-RAY DIFFRACTION21(CHAIN E AND RESID 318:477)
22X-RAY DIFFRACTION22(CHAIN E AND RESID 478:581)
23X-RAY DIFFRACTION23(CHAIN E AND RESID 582:642)
24X-RAY DIFFRACTION24(CHAIN F AND RESID 730:968)
25X-RAY DIFFRACTION25(CHAIN F AND RESID 969:1269)
26X-RAY DIFFRACTION26(CHAIN F AND RESID 1270:1518)
27X-RAY DIFFRACTION27(CHAIN F AND RESID 1519:1641)
28X-RAY DIFFRACTION28(CHAIN G AND RESID 1:204)
29X-RAY DIFFRACTION29(CHAIN G AND RESID 205:580)
30X-RAY DIFFRACTION30(CHAIN G AND RESID 581:642)
31X-RAY DIFFRACTION31(CHAIN H AND RESID 730:914)
32X-RAY DIFFRACTION32(CHAIN H AND RESID 915:968)
33X-RAY DIFFRACTION33(CHAIN H AND RESID 969:1266)
34X-RAY DIFFRACTION34(CHAIN H AND RESID 1267:1334)
35X-RAY DIFFRACTION35(CHAIN H AND RESID 1335:1505)
36X-RAY DIFFRACTION36(CHAIN H AND RESID 1506:1641)
37X-RAY DIFFRACTION37(CHAIN I AND RESID 10:197)
38X-RAY DIFFRACTION38(CHAIN I AND RESID 198:454)
39X-RAY DIFFRACTION39(CHAIN I AND RESID 455:741)
40X-RAY DIFFRACTION40(CHAIN J AND RESID 10:74)
41X-RAY DIFFRACTION41(CHAIN J AND RESID 75:193)
42X-RAY DIFFRACTION42(CHAIN J AND RESID 194:450)
43X-RAY DIFFRACTION43(CHAIN J AND RESID 451:741)
44X-RAY DIFFRACTION44(CHAIN K AND RESID 10:74)
45X-RAY DIFFRACTION45(CHAIN K AND RESID 75:196)
46X-RAY DIFFRACTION46(CHAIN K AND RESID 197:450)
47X-RAY DIFFRACTION47(CHAIN K AND RESID 451:741)
48X-RAY DIFFRACTION48(CHAIN L AND RESID 10:192)
49X-RAY DIFFRACTION49(CHAIN L AND RESID 193:446)
50X-RAY DIFFRACTION50(CHAIN L AND RESID 447:741)

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