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- PDB-4nyt: L-Ficolin Complexed to Phosphocholine -

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Basic information

Entry
Database: PDB / ID: 4nyt
TitleL-Ficolin Complexed to Phosphocholine
ComponentsFicolin-2
KeywordsIMMUNE SYSTEM / Soluble innate immune recognition / Extracellular
Function / homology
Function and homology information


mannan binding / recognition of apoptotic cell / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / positive regulation of opsonization / opsonization / complement activation, lectin pathway / cell surface pattern recognition receptor signaling pathway / carbohydrate derivative binding / collagen trimer ...mannan binding / recognition of apoptotic cell / Ficolins bind to repetitive carbohydrate structures on the target cell surface / Lectin pathway of complement activation / positive regulation of opsonization / opsonization / complement activation, lectin pathway / cell surface pattern recognition receptor signaling pathway / carbohydrate derivative binding / collagen trimer / serine-type endopeptidase complex / proteoglycan binding / Initial triggering of complement / antigen binding / calcium-dependent protein binding / : / defense response to Gram-negative bacterium / blood microparticle / defense response to Gram-positive bacterium / external side of plasma membrane / signaling receptor binding / proteolysis / extracellular space / extracellular exosome / extracellular region / metal ion binding
Similarity search - Function
: / Gamma-fibrinogen Carboxyl Terminal Fragment; domain 2 / Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2 / Gamma Fibrinogen; Chain A, domain 1 / Gamma Fibrinogen, chain A, domain 1 / Fibrinogen, conserved site / Fibrinogen C-terminal domain signature. / Fibrinogen-related domains (FReDs) / Fibrinogen beta and gamma chains, C-terminal globular domain / Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 ...: / Gamma-fibrinogen Carboxyl Terminal Fragment; domain 2 / Gamma-fibrinogen Carboxyl Terminal Fragment, domain 2 / Gamma Fibrinogen; Chain A, domain 1 / Gamma Fibrinogen, chain A, domain 1 / Fibrinogen, conserved site / Fibrinogen C-terminal domain signature. / Fibrinogen-related domains (FReDs) / Fibrinogen beta and gamma chains, C-terminal globular domain / Fibrinogen, alpha/beta/gamma chain, C-terminal globular, subdomain 1 / Fibrinogen, alpha/beta/gamma chain, C-terminal globular domain / Fibrinogen-like, C-terminal / Fibrinogen C-terminal domain profile. / Collagen triple helix repeat / Collagen triple helix repeat (20 copies) / Few Secondary Structures / Irregular / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
ACETATE ION / PHOSPHOCHOLINE / PHOSPHATE ION / Ficolin-2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsLaffly, E. / Gaboriaud, C. / Martin, L. / Thielens, N.
CitationJournal: J.Immunol. / Year: 2014
Title: Human L-ficolin recognizes phosphocholine moieties of pneumococcal teichoic Acid
Authors: Vassal-Stermann, E. / Lacroix, M. / Gout, E. / Laffly, E. / Pedersen, C.M. / Martin, L. / Amoroso, A. / Schmidt, R.R. / Zahringer, U. / Gaboriaud, C. / Di Guilmi, A.M. / Thielens, N.M.
History
DepositionDec 11, 2013Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Oct 29, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 24, 2014Group: Database references
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_struct_conn_angle / pdbx_validate_chiral / 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.occupancy / _atom_site.type_symbol / _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_auth_seq_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_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Nov 13, 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 / _pdbx_entry_details.has_protein_modification / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
C: Ficolin-2
A: Ficolin-2
B: Ficolin-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,35713
Polymers73,8463
Non-polymers1,51110
Water1,26170
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)96.130, 96.130, 139.880
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11C
21B
31A
12C
22B
32A
13C
23B
33A
14C
24B
34A
15C
25A
16C
26A
17C
27A
18C
28A
19C
29A
110C
210A
111C
211A
112C
212A
312B
113C
213A
313B

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDRefine codeAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11THRTHRTYRTYR2CA79 - 978 - 26
21THRTHRTYRTYR2BC79 - 978 - 26
31THRTHRTYRTYR2AB79 - 978 - 26
12PROPROMETMET2CA103 - 11032 - 39
22PROPROMETMET2BC103 - 11032 - 39
32PROPROMETMET2AB103 - 11032 - 39
13THRTHRARGARG2CA112 - 14441 - 73
23THRTHRARGARG2BC112 - 14441 - 73
33THRTHRARGARG2AB112 - 14441 - 73
14GLUGLUTHRTHR2CA147 - 15976 - 88
24GLUGLUTHRTHR2BC147 - 15976 - 88
34GLUGLUTHRTHR2AB147 - 15976 - 88
15LEULEUPHEPHE2CA166 - 17395 - 102
25LEULEUPHEPHE2AB166 - 17395 - 102
16GLNGLNTYRTYR2CA178 - 182107 - 111
26GLNGLNTYRTYR2AB178 - 182107 - 111
17VALVALALAALA2CA187 - 191116 - 120
27VALVALALAALA2AB187 - 191116 - 120
18TYRTYRTHRTHR4CA194 - 211123 - 140
28TYRTYRTHRTHR4AB194 - 211123 - 140
19SERSERASPASP2CA217 - 222146 - 151
29SERSERASPASP2AB217 - 222146 - 151
110GLYGLYPHEPHE2CA230 - 236159 - 165
210GLYGLYPHEPHE2AB230 - 236159 - 165
111GLYGLYTYRTYR2CA238 - 242167 - 171
211GLYGLYTYRTYR2AB238 - 242167 - 171
112THRTHRGLYGLY2CA247 - 252176 - 181
212THRTHRGLYGLY2AB247 - 252176 - 181
312THRTHRGLYGLY2BC247 - 252176 - 181
113TRPTRPPROPRO2CA268 - 287197 - 216
213TRPTRPPROPRO2AB268 - 287197 - 216
313TRPTRPPROPRO2BC268 - 287197 - 216

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(-0.43333, 0.899702, 0.052547), (-0.706134, -0.375173, 0.600517), (0.56, 0.223117, 0.797884)91.54861, -27.63839, -12.64726
3given(-0.437006, -0.748574, 0.498661), (0.899359, -0.371903, 0.229872), (0.013378, 0.54893, 0.835761)25.8399, -89.85398, 21.51406

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Components

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Protein , 1 types, 3 molecules CAB

#1: Protein Ficolin-2 / 37 kDa elastin-binding protein / Collagen/fibrinogen domain-containing protein 2 / EBP-37 / Ficolin- ...37 kDa elastin-binding protein / Collagen/fibrinogen domain-containing protein 2 / EBP-37 / Ficolin-B / Ficolin-beta / Hucolin / L-ficolin / Serum lectin p35


Mass: 24615.219 Da / Num. of mol.: 3
Fragment: Fibrinogen-like Ligand Binding Domain, Residues 97-313
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FCN2 / Cell line (production host): High Five / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q15485

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Sugars , 2 types, 2 molecules

#2: Polysaccharide alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 732.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#6: 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.: 1
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 , 5 types, 78 molecules

#3: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H3O2
#4: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#5: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: PO4
#7: Chemical ChemComp-PC / PHOSPHOCHOLINE


Mass: 184.151 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C5H15NO4P
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 70 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Sequence detailsTHERE IS A DIFFERENCE BECAUSE IT EXISTS POINTS OF POLYMORPHISM IN L FICOLIN FOR 272 AND 193. THE ...THERE IS A DIFFERENCE BECAUSE IT EXISTS POINTS OF POLYMORPHISM IN L FICOLIN FOR 272 AND 193. THE CDNA USED CORRESPONDS TO ONE WIDESPREAD ALLELE AND THE SEQUENCE IN UNP TO ANOTHER

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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: 2.53 Å3/Da / Density % sol: 51.32 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 7
Details: 15%(w/v) PEG 8000, 200mM Ca acetate, 0.1M Hepes, pH 7.0, VAPOR DIFFUSION, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.97887 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 2, 2011
RadiationMonochromator: Toroidal mirror Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97887 Å / Relative weight: 1
ReflectionResolution: 2.2→20 Å / Num. all: 38564 / Num. obs: 38356 / % possible obs: 99.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3
Reflection shell
Resolution (Å)Diffraction-ID% possible all
2.2-2.26199.5
2.26-2.32199.6
2.32-2.39199.7
2.39-2.46199.7
2.46-2.54199.9
2.54-2.63199.7
2.63-2.73199.7
2.73-2.84199.8
2.84-2.97199.9
2.97-3.11199.9
3.11-3.28199.8
3.28-3.48199.8
3.48-3.72199.7
3.72-4.02199.5
4.02-4.4199.6
4.4-4.92199.3
4.92-5.68199.8
5.68-6.96199.5
6.96-9.84199.4
9.84-20180.9

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
REFMAC5.7.0032refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.25→19.95 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.919 / SU B: 13.789 / SU ML: 0.175 / Cross valid method: THROUGHOUT / ESU R: 0.317 / ESU R Free: 0.221 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.24293 1795 5 %RANDOM
Rwork0.21285 ---
all0.21439 34287 --
obs0.21439 34099 99.45 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 60.17 Å2
Baniso -1Baniso -2Baniso -3
1--0.02 Å2-0.02 Å20 Å2
2---0.02 Å20 Å2
3---0.05 Å2
Refinement stepCycle: LAST / Resolution: 2.25→19.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5134 0 91 70 5295
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0180.0195429
X-RAY DIFFRACTIONr_bond_other_d0.0050.024791
X-RAY DIFFRACTIONr_angle_refined_deg1.8981.9277365
X-RAY DIFFRACTIONr_angle_other_deg1.3313.00310937
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.2335649
X-RAY DIFFRACTIONr_dihedral_angle_2_deg29.67323.552290
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.07115830
X-RAY DIFFRACTIONr_dihedral_angle_4_deg23.5981538
X-RAY DIFFRACTIONr_chiral_restr0.1870.2741
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.026325
X-RAY DIFFRACTIONr_gen_planes_other0.0070.021447
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.6940.8892589
X-RAY DIFFRACTIONr_mcbond_other0.6940.8892588
X-RAY DIFFRACTIONr_mcangle_it1.1671.3283239
X-RAY DIFFRACTIONr_mcangle_other1.1671.3283240
X-RAY DIFFRACTIONr_scbond_it1.2761.0712840
X-RAY DIFFRACTIONr_scbond_other1.2761.0712841
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other1.9731.5724127
X-RAY DIFFRACTIONr_long_range_B_refined3.8747.556248
X-RAY DIFFRACTIONr_long_range_B_other3.8717.5266240
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11C35TIGHT POSITIONAL0.040.05
11C29TIGHT POSITIONAL0.030.05
11C29TIGHT POSITIONAL0.040.05
12B29TIGHT POSITIONAL0.040.05
13A29TIGHT POSITIONAL0.050.05
11C117TIGHT POSITIONAL0.050.05
12B117TIGHT POSITIONAL0.050.05
13A117TIGHT POSITIONAL0.050.05
11C195MEDIUM POSITIONAL0.040.5
12B195MEDIUM POSITIONAL0.030.5
13A195MEDIUM POSITIONAL0.030.5
11C112TIGHT THERMAL4.520.5
12B112TIGHT THERMAL5.390.5
13A112TIGHT THERMAL2.480.5
11C195MEDIUM THERMAL5.62
12B195MEDIUM THERMAL7.212
13A195MEDIUM THERMAL3.792
21C61MEDIUM POSITIONAL0.060.5
22B61MEDIUM POSITIONAL0.050.5
23A61MEDIUM POSITIONAL0.030.5
21C41TIGHT THERMAL1.970.5
22B41TIGHT THERMAL4.830.5
23A41TIGHT THERMAL3.580.5
21C61MEDIUM THERMAL2.132
22B61MEDIUM THERMAL5.222
23A61MEDIUM THERMAL4.32
31C315MEDIUM POSITIONAL0.250.5
32B315MEDIUM POSITIONAL0.120.5
33A315MEDIUM POSITIONAL0.150.5
31C192TIGHT THERMAL1.820.5
32B192TIGHT THERMAL3.280.5
33A192TIGHT THERMAL1.690.5
31C315MEDIUM THERMAL2.632
32B315MEDIUM THERMAL4.362
33A315MEDIUM THERMAL2.312
41C127MEDIUM POSITIONAL0.040.5
42B127MEDIUM POSITIONAL0.030.5
43A127MEDIUM POSITIONAL0.030.5
41C77TIGHT THERMAL0.880.5
42B77TIGHT THERMAL3.340.5
43A77TIGHT THERMAL3.130.5
41C127MEDIUM THERMAL1.632
42B127MEDIUM THERMAL3.932
43A127MEDIUM THERMAL2.972
51C87MEDIUM POSITIONAL0.050.5
51C48TIGHT THERMAL0.810.5
51C87MEDIUM THERMAL1.042
61C59MEDIUM POSITIONAL0.040.5
61C30TIGHT THERMAL0.770.5
61C59MEDIUM THERMAL1.852
71C33MEDIUM POSITIONAL0.060.5
71C30TIGHT THERMAL2.260.5
71C33MEDIUM THERMAL2.12
81C244MEDIUM POSITIONAL0.330.5
81C244MEDIUM THERMAL0.942
91C51MEDIUM POSITIONAL0.060.5
91C36TIGHT THERMAL0.660.5
91C51MEDIUM THERMAL1.072
101C43MEDIUM POSITIONAL0.050.5
101C35TIGHT THERMAL1.090.5
101C43MEDIUM THERMAL1.332
111C56MEDIUM POSITIONAL0.050.5
111C29TIGHT THERMAL0.910.5
111C56MEDIUM THERMAL0.692
121C35MEDIUM POSITIONAL0.050.5
122A35MEDIUM POSITIONAL0.040.5
123B35MEDIUM POSITIONAL0.040.5
121C29TIGHT THERMAL0.760.5
122A29TIGHT THERMAL1.260.5
123B29TIGHT THERMAL0.790.5
121C35MEDIUM THERMAL0.522
122A35MEDIUM THERMAL1.462
123B35MEDIUM THERMAL1.432
131C215MEDIUM POSITIONAL0.050.5
132A215MEDIUM POSITIONAL0.050.5
133B215MEDIUM POSITIONAL0.040.5
131C117TIGHT THERMAL1.130.5
132A117TIGHT THERMAL1.340.5
133B117TIGHT THERMAL1.340.5
131C215MEDIUM THERMAL1.382
132A215MEDIUM THERMAL2.072
133B215MEDIUM THERMAL1.992
LS refinement shellResolution: 2.25→2.308 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.317 129 -
Rwork0.25 2456 -
obs--99.54 %
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)
13.52020.748-2.51641.6896-1.2225.32470.00430.93510.6219-0.20470.31480.2105-0.2628-0.7044-0.31910.2335-0.0118-0.02930.37780.14790.126741.872-56.07715.877
212.24155.56911.709723.15493.05762.5351.4634-0.3542-0.0614-1.0312-1.7587-2.89310.069-0.22860.29530.31620.06310.24150.65610.27460.589724.158-26.24111.277
34.11360.28890.50512.2421-0.42831.96870.1602-0.0663-0.3343-0.04360.21640.65990.2026-0.5978-0.37650.2055-0.0361-0.02460.3010.13960.261157.007-27.8434.388
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A76 - 287
2X-RAY DIFFRACTION2B76 - 287
3X-RAY DIFFRACTION3C72 - 287

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