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- PDB-5ft8: Crystal structure of the complex between the cysteine desulfurase... -

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Basic information

Entry
Database: PDB / ID: 5ft8
TitleCrystal structure of the complex between the cysteine desulfurase CsdA and the sulfur-acceptor CsdE in the persulfurated state at 2.50 Angstroem resolution
Components
  • Cysteine desulfurase CsdA
  • Sulfur acceptor protein CsdE
KeywordsTRANSFERASE / L-CYSTEINE DESULFURASE / SULFUR ACCEPTOR / TRANSPERSULFURATION / SULFUR TRAFFICKING
Function / homology
Function and homology information


sulfur compound transport / cyclic threonylcarbamoyladenosine biosynthetic process / selenocysteine catabolic process / Hydrolases; Acting on carbon-sulfur bonds; Acting on carbon-sulfur bonds / cysteine sulfinate desulfinase activity / sulfur amino acid metabolic process / selenocysteine lyase / selenocysteine lyase activity / sulfurtransferase activity / L-cysteine desulfurase complex ...sulfur compound transport / cyclic threonylcarbamoyladenosine biosynthetic process / selenocysteine catabolic process / Hydrolases; Acting on carbon-sulfur bonds; Acting on carbon-sulfur bonds / cysteine sulfinate desulfinase activity / sulfur amino acid metabolic process / selenocysteine lyase / selenocysteine lyase activity / sulfurtransferase activity / L-cysteine desulfurase complex / sulfur carrier activity / L-cysteine catabolic process / cysteine desulfurase / cysteine desulfurase activity / iron-sulfur cluster assembly / pyridoxal phosphate binding / hydrolase activity
Similarity search - Function
Cysteine desulfurase, sulphur acceptor subunit CsdE / Cysteine desulphurase, catalytic subunit, CsdA / Fe-S metabolism associated domain, SufE-like / Fe-S metabolism associated domain / Cysteine desulfurase, SufS / Aminotransferase class-V, pyridoxal-phosphate binding site / Aminotransferases class-V pyridoxal-phosphate attachment site. / Aminotransferase class V domain / Aminotransferase class-V / Aspartate Aminotransferase, domain 1 ...Cysteine desulfurase, sulphur acceptor subunit CsdE / Cysteine desulphurase, catalytic subunit, CsdA / Fe-S metabolism associated domain, SufE-like / Fe-S metabolism associated domain / Cysteine desulfurase, SufS / Aminotransferase class-V, pyridoxal-phosphate binding site / Aminotransferases class-V pyridoxal-phosphate attachment site. / Aminotransferase class V domain / Aminotransferase class-V / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase, domain 1 / Aspartate Aminotransferase; domain 2 / Type I PLP-dependent aspartate aminotransferase-like (Major domain) / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase / Alpha-Beta Complex / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / PYRIDOXAL-5'-PHOSPHATE / Sulfur acceptor protein CsdE / Cysteine desulfurase CsdA
Similarity search - Component
Biological speciesEscherichia coli K-12 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsFernandez, F.J. / Arda, A. / Lopez-Estepa, M. / Aranda, J. / Penya-Soler, E. / Garces, F. / Round, A. / Campos-Oliva, R. / Bruix, M. / Coll, M. ...Fernandez, F.J. / Arda, A. / Lopez-Estepa, M. / Aranda, J. / Penya-Soler, E. / Garces, F. / Round, A. / Campos-Oliva, R. / Bruix, M. / Coll, M. / Tunon, I. / Jimenez-Barbero, J. / Vega, M.C.
CitationJournal: Acs Catalysis / Year: 2016
Title: Mechanism of Sulfur Transfer Across Protein-Protein Interfaces: The Cysteine Desulfurase Model System
Authors: Fernandez, F.J. / Arda, A. / Lopez-Estepa, M. / Aranda, J. / Penya-Soler, E. / Garces, F. / Quintana, J.F. / Round, A. / Campos-Oliva, R. / Bruix, M. / Coll, M. / Tunon, I. / Jimenez-Barbero, J. / Vega, M.C.
History
DepositionJan 11, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 23, 2016Provider: repository / Type: Initial release
Revision 1.1Jan 2, 2019Group: Data collection / Database references / Structure summary
Category: pdbx_database_related / struct / Item: _pdbx_database_related.details / _struct.title
Revision 2.0Dec 7, 2022Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Other / Polymer sequence / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / database_2 / entity / entity_name_com / entity_poly / entity_poly_seq / entity_src_gen / pdbx_database_status / pdbx_distant_solvent_atoms / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_mod_residue / pdbx_struct_sheet_hbond / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_rmsd_angle / pdbx_validate_torsion / struct_asym / struct_conf / struct_conn / struct_ref / struct_ref_seq / struct_ref_seq_dif / struct_sheet_range / 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.group_PDB / _atom_site.label_alt_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _atom_site.occupancy / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_alt_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.pdbx_label_seq_id / _atom_site_anisotrop.type_symbol / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_name_com.name / _entity_poly.nstd_monomer / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_strand_id / _entity_poly_seq.mon_id / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_gene / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_seq_type / _pdbx_database_status.status_code_sf / _pdbx_distant_solvent_atoms.auth_asym_id / _pdbx_distant_solvent_atoms.auth_seq_id / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.auth_seq_num / _pdbx_poly_seq_scheme.mon_id / _pdbx_poly_seq_scheme.pdb_ins_code / _pdbx_poly_seq_scheme.pdb_mon_id / _pdbx_poly_seq_scheme.pdb_seq_num / _pdbx_poly_seq_scheme.pdb_strand_id / _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_sheet_hbond.range_1_auth_asym_id / _pdbx_struct_sheet_hbond.range_2_auth_asym_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _pdbx_validate_rmsd_angle.auth_asym_id_1 / _pdbx_validate_rmsd_angle.auth_asym_id_2 / _pdbx_validate_rmsd_angle.auth_asym_id_3 / _struct_conf.beg_auth_asym_id / _struct_conf.beg_auth_seq_id / _struct_conf.end_auth_asym_id / _struct_conf.end_auth_seq_id / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_ref.pdbx_align_begin / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.pdbx_auth_seq_align_end / _struct_ref_seq.pdbx_strand_id / _struct_ref_seq_dif.pdbx_auth_seq_num / _struct_ref_seq_dif.pdbx_pdb_strand_id / _struct_sheet_range.beg_auth_asym_id / _struct_sheet_range.end_auth_asym_id / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id / _struct_site_gen.auth_asym_id / _struct_site_gen.auth_seq_id / _struct_site_gen.label_asym_id / _struct_site_gen.label_seq_id
Revision 2.1Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cysteine desulfurase CsdA
Q: Sulfur acceptor protein CsdE
C: Cysteine desulfurase CsdA
S: Sulfur acceptor protein CsdE
E: Cysteine desulfurase CsdA
U: Sulfur acceptor protein CsdE
G: Cysteine desulfurase CsdA
W: Sulfur acceptor protein CsdE
I: Cysteine desulfurase CsdA
Y: Sulfur acceptor protein CsdE
K: Cysteine desulfurase CsdA
a: Sulfur acceptor protein CsdE
M: Cysteine desulfurase CsdA
c: Sulfur acceptor protein CsdE
O: Cysteine desulfurase CsdA
e: Sulfur acceptor protein CsdE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)491,41691
Polymers483,04416
Non-polymers8,37275
Water18,3931021
1
A: Cysteine desulfurase CsdA
Q: Sulfur acceptor protein CsdE
C: Cysteine desulfurase CsdA
S: Sulfur acceptor protein CsdE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)124,49940
Polymers120,7614
Non-polymers3,73836
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
E: Cysteine desulfurase CsdA
U: Sulfur acceptor protein CsdE
G: Cysteine desulfurase CsdA
W: Sulfur acceptor protein CsdE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)123,64231
Polymers120,7614
Non-polymers2,88127
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
I: Cysteine desulfurase CsdA
Y: Sulfur acceptor protein CsdE
K: Cysteine desulfurase CsdA
a: Sulfur acceptor protein CsdE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,92813
Polymers120,7614
Non-polymers1,1679
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
M: Cysteine desulfurase CsdA
c: Sulfur acceptor protein CsdE
O: Cysteine desulfurase CsdA
e: Sulfur acceptor protein CsdE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,3477
Polymers120,7614
Non-polymers5863
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)74.863, 115.135, 604.966
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 2 types, 16 molecules ACEGIKMOQSUWYace

#1: Protein
Cysteine desulfurase CsdA / Cysteine sulfinate desulfinase / CSD / Selenocysteine lyase


Mass: 43434.172 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K-12 / Gene: csdA, ygdJ, b2810, JW2781 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q46925, cysteine desulfurase, Hydrolases; Acting on carbon-sulfur bonds; Acting on carbon-sulfur bonds, selenocysteine lyase
#2: Protein
Sulfur acceptor protein CsdE


Mass: 16946.336 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K-12 / Gene: csdE, ygdK, b2811, JW2782 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0AGF2

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Non-polymers , 4 types, 1096 molecules

#3: Chemical
ChemComp-PLP / PYRIDOXAL-5'-PHOSPHATE / VITAMIN B6 Phosphate


Mass: 247.142 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C8H10NO6P
#4: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 16 / Source method: obtained synthetically / Formula: C4H10O3
#5: Chemical...
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 51 / Source method: obtained synthetically / Formula: C3H8O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1021 / Source method: isolated from a natural source / Formula: H2O

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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: 2.71 Å3/Da / Density % sol: 54.72 % / Description: NONE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.98011
DetectorType: ADSC CCD / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98011 Å / Relative weight: 1
ReflectionResolution: 2.5→48.3 Å / Num. obs: 178722 / % possible obs: 98.9 % / Observed criterion σ(I): -3 / Redundancy: 1 % / Rmerge(I) obs: 0.13 / Net I/σ(I): 7.4
Reflection shellResolution: 2.5→2.63 Å / Redundancy: 1 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 1.6 / % possible all: 97.9

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Processing

Software
NameVersionClassification
REFMAC5.6.0117refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 5FT4 AND 5FT7

5ft4

5ft7
PDB Unreleased entry


Resolution: 2.5→48.3 Å / Cor.coef. Fo:Fc: 0.904 / Cor.coef. Fo:Fc free: 0.889 / SU B: 30.717 / SU ML: 0.307 / Cross valid method: THROUGHOUT / ESU R: 0.601 / ESU R Free: 0.311 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED.
RfactorNum. reflection% reflectionSelection details
Rfree0.27876 2000 1.1 %RANDOM
Rwork0.25363 ---
obs0.25391 176559 97.74 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 58.429 Å2
Baniso -1Baniso -2Baniso -3
1-3.23 Å20 Å20 Å2
2---0.19 Å20 Å2
3----3.04 Å2
Refinement stepCycle: LAST / Resolution: 2.5→48.3 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms32578 0 643 1021 34242
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01933951
X-RAY DIFFRACTIONr_bond_other_d0.0060.0222558
X-RAY DIFFRACTIONr_angle_refined_deg1.1871.97146076
X-RAY DIFFRACTIONr_angle_other_deg1.388355025
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.28754306
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.7724.1981465
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.296155282
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.97915209
X-RAY DIFFRACTIONr_chiral_restr0.0620.25244
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02137986
X-RAY DIFFRACTIONr_gen_planes_other0.0040.026767
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_it
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.498→2.563 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.476 108 -
Rwork0.412 9708 -
obs--77.78 %
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)
10.6877-0.1207-0.15320.84740.31541.95770.0087-0.10240.01130.1519-0.0064-0.10870.070.2399-0.00240.1614-0.0687-0.0680.30130.02640.2958-29.6222-21.7956115.2277
26.36160.74361.39474.75231.18085.10840.0230.6787-0.1501-0.2313-0.00540.20610.1079-0.0468-0.01750.3341-0.0206-0.02440.26560.0410.2377-66.4665-24.9019128.0015
30.95390.40070.132.00930.14920.9832-0.04060.07490.2137-0.2613-0.0370.1878-0.1534-0.00410.07760.2059-0.0138-0.03880.24240.01590.3235-44.3734-6.509892.0542
44.2815-2.1518-0.77015.81091.62452.22150.0260.0718-0.3512-0.1534-0.00110.18470.3730.1645-0.02490.57460.0111-0.02380.47790.01520.402-7.52342.198182.6839
50.7082-0.11610.2451.8601-0.38511.1867-0.089-0.04010.0130.07280.10510.1128-0.1713-0.1595-0.01610.25370.00520.01560.22430.03390.2383-12.366936.4163117.4701
610.26-0.7518-1.737.31382.26635.8922-0.1512-0.2011-1.40390.41530.0006-1.54730.70421.1610.15060.68810.0367-0.07350.93860.15311.081221.726550.2786106.5695
70.7548-0.2217-0.12120.90060.32942.4349-0.0791-0.0690.02830.13570.0355-0.1616-0.06260.10610.04360.2208-0.0149-0.01170.19960.01920.30026.589118.7434135.184
83.48511.82551.31135.77232.96246.3121-0.03920.5224-0.1213-0.5309-0.22940.59880.1377-0.73070.26860.5840.0374-0.0610.5126-0.08540.4005-28.24168.4715152.5449
91.82530.5501-0.34411.1462-0.08381.0868-0.03140.21910.1081-0.12770.03850.0961-0.07-0.1318-0.00710.4217-0.019-0.05570.24570.04010.1959-4.8891-41.922977.9259
108.1344-1.11370.32397.371.59344.6904-0.07080.8753-0.5718-1.34220.2313-1.07860.14420.4521-0.16041.0069-0.10730.17710.4635-0.06360.6054-5.4488-79.63772.4465
111.072-0.32250.19871.418-0.58342.31090.03990.4166-0.0185-0.3208-0.03250.02790.0835-0.0764-0.00730.7548-0.0925-0.00190.62570.02740.2561.1877-43.669647.168
120.37020.2161-0.12551.82393.10457.8236-0.1717-0.02850.4456-0.37960.08250.3085-1.01370.1560.08931.4607-0.03310.13631.25210.02590.9665-1.1242-4.558649.8746
131.1136-0.21850.43831.744-0.70541.69650.24460.043-0.2959-0.17310.07190.03790.6138-0.2078-0.31651.1595-0.0342-0.21060.88590.13180.4587-28.1554-49.5652-6.4494
148.3292-0.8373-2.45860.16210.41063.4054-0.2642-0.4796-0.1967-0.0130.2989-0.21370.78570.6057-0.03461.730.10830.09291.75030.05061.1618-0.1431-35.576-30.365
151.28290.07840.31231.5140.13381.87660.28090.0629-0.5139-0.0872-0.123-0.5670.9160.4063-0.1581.6270.2565-0.23760.99150.0820.9444-3.4864-66.97273.3087
161.85440.132-0.68110.0504-0.03120.3389-0.2718-0.1749-0.69090.1882-0.14510.0909-0.1122-0.22980.41692.6441-0.2164-0.11331.6219-0.18391.3972-25.9428-69.405436.1454
170.02160.03410.03030.11280.01070.0952-0.00970.00610.0474-0.04120.00110.0130.0153-0.02610.00860.0275-0.0648-0.02360.44770.01490.5307-18.0342-4.6743107.5956
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A3 - 54
2X-RAY DIFFRACTION1A55 - 110
3X-RAY DIFFRACTION1A111 - 167
4X-RAY DIFFRACTION1A168 - 203
5X-RAY DIFFRACTION1A204 - 229
6X-RAY DIFFRACTION1A230 - 262
7X-RAY DIFFRACTION1A263 - 293
8X-RAY DIFFRACTION1A294 - 327
9X-RAY DIFFRACTION1A328 - 359
10X-RAY DIFFRACTION1A360 - 401
11X-RAY DIFFRACTION2B6 - 16
12X-RAY DIFFRACTION2B17 - 29
13X-RAY DIFFRACTION2B30 - 42
14X-RAY DIFFRACTION2B43 - 51
15X-RAY DIFFRACTION2B52 - 64
16X-RAY DIFFRACTION2B65 - 85
17X-RAY DIFFRACTION2B86 - 111
18X-RAY DIFFRACTION2B112 - 118
19X-RAY DIFFRACTION2B119 - 129
20X-RAY DIFFRACTION2B130 - 148
21X-RAY DIFFRACTION3C3 - 32
22X-RAY DIFFRACTION3C33 - 54
23X-RAY DIFFRACTION3C55 - 110
24X-RAY DIFFRACTION3C111 - 167
25X-RAY DIFFRACTION3C168 - 203
26X-RAY DIFFRACTION3C204 - 229
27X-RAY DIFFRACTION3C230 - 262
28X-RAY DIFFRACTION3C263 - 293
29X-RAY DIFFRACTION3C294 - 327
30X-RAY DIFFRACTION3C328 - 359
31X-RAY DIFFRACTION3C360 - 401
32X-RAY DIFFRACTION4D8 - 16
33X-RAY DIFFRACTION4D17 - 29
34X-RAY DIFFRACTION4D30 - 42
35X-RAY DIFFRACTION4D43 - 51
36X-RAY DIFFRACTION4D52 - 64
37X-RAY DIFFRACTION4D65 - 85
38X-RAY DIFFRACTION4D86 - 111
39X-RAY DIFFRACTION4D112 - 118
40X-RAY DIFFRACTION4D119 - 129
41X-RAY DIFFRACTION4D130 - 148
42X-RAY DIFFRACTION5E3 - 32
43X-RAY DIFFRACTION5E33 - 54
44X-RAY DIFFRACTION5E55 - 110
45X-RAY DIFFRACTION5E111 - 167
46X-RAY DIFFRACTION5E168 - 203
47X-RAY DIFFRACTION5E204 - 229
48X-RAY DIFFRACTION5E230 - 262
49X-RAY DIFFRACTION5E263 - 293
50X-RAY DIFFRACTION5E294 - 327
51X-RAY DIFFRACTION5E328 - 359
52X-RAY DIFFRACTION5E360 - 401
53X-RAY DIFFRACTION6F9 - 16
54X-RAY DIFFRACTION6F17 - 29
55X-RAY DIFFRACTION6F30 - 42
56X-RAY DIFFRACTION6F43 - 51
57X-RAY DIFFRACTION6F52 - 64
58X-RAY DIFFRACTION6F65 - 85
59X-RAY DIFFRACTION6F86 - 111
60X-RAY DIFFRACTION6F112 - 118
61X-RAY DIFFRACTION6F119 - 129
62X-RAY DIFFRACTION6F130 - 144
63X-RAY DIFFRACTION7G3 - 32
64X-RAY DIFFRACTION7G33 - 54
65X-RAY DIFFRACTION7G55 - 110
66X-RAY DIFFRACTION7G111 - 167
67X-RAY DIFFRACTION7G168 - 203
68X-RAY DIFFRACTION7G204 - 229
69X-RAY DIFFRACTION7G230 - 262
70X-RAY DIFFRACTION7G263 - 293
71X-RAY DIFFRACTION7G294 - 327
72X-RAY DIFFRACTION7G328 - 359
73X-RAY DIFFRACTION7G360 - 401
74X-RAY DIFFRACTION8H6 - 16
75X-RAY DIFFRACTION8H17 - 29
76X-RAY DIFFRACTION8H30 - 42
77X-RAY DIFFRACTION8H43 - 51
78X-RAY DIFFRACTION8H52 - 64
79X-RAY DIFFRACTION8H65 - 85
80X-RAY DIFFRACTION8H86 - 111
81X-RAY DIFFRACTION8H112 - 118
82X-RAY DIFFRACTION8H119 - 129
83X-RAY DIFFRACTION8H130 - 148
84X-RAY DIFFRACTION9I3 - 32
85X-RAY DIFFRACTION9I33 - 54
86X-RAY DIFFRACTION9I55 - 110
87X-RAY DIFFRACTION9I111 - 167
88X-RAY DIFFRACTION9I168 - 203
89X-RAY DIFFRACTION9I204 - 229
90X-RAY DIFFRACTION9I230 - 262
91X-RAY DIFFRACTION9I263 - 293
92X-RAY DIFFRACTION9I294 - 327
93X-RAY DIFFRACTION9I328 - 359
94X-RAY DIFFRACTION9I360 - 401
95X-RAY DIFFRACTION10J6 - 16
96X-RAY DIFFRACTION10J17 - 29
97X-RAY DIFFRACTION10J30 - 42
98X-RAY DIFFRACTION10J43 - 51
99X-RAY DIFFRACTION10J52 - 64
100X-RAY DIFFRACTION10J65 - 85
101X-RAY DIFFRACTION10J86 - 111
102X-RAY DIFFRACTION10J112 - 118
103X-RAY DIFFRACTION10J119 - 129
104X-RAY DIFFRACTION10J130 - 147
105X-RAY DIFFRACTION11K3 - 32
106X-RAY DIFFRACTION11K33 - 54
107X-RAY DIFFRACTION11K55 - 110
108X-RAY DIFFRACTION11K111 - 167
109X-RAY DIFFRACTION11K168 - 203
110X-RAY DIFFRACTION11K204 - 229
111X-RAY DIFFRACTION11K230 - 262
112X-RAY DIFFRACTION11K263 - 293
113X-RAY DIFFRACTION11K294 - 327
114X-RAY DIFFRACTION11K328 - 359
115X-RAY DIFFRACTION11K360 - 401
116X-RAY DIFFRACTION12L8 - 16
117X-RAY DIFFRACTION12L17 - 29
118X-RAY DIFFRACTION12L30 - 42
119X-RAY DIFFRACTION12L43 - 51
120X-RAY DIFFRACTION12L52 - 64
121X-RAY DIFFRACTION12L65 - 85
122X-RAY DIFFRACTION12L86 - 111
123X-RAY DIFFRACTION12L112 - 118
124X-RAY DIFFRACTION12L119 - 129
125X-RAY DIFFRACTION12L130 - 147
126X-RAY DIFFRACTION13M3 - 32
127X-RAY DIFFRACTION13M33 - 54
128X-RAY DIFFRACTION13M55 - 110
129X-RAY DIFFRACTION13M111 - 167
130X-RAY DIFFRACTION13M168 - 203
131X-RAY DIFFRACTION13M204 - 229
132X-RAY DIFFRACTION13M230 - 262
133X-RAY DIFFRACTION13M263 - 293
134X-RAY DIFFRACTION13M294 - 327
135X-RAY DIFFRACTION13M328 - 359
136X-RAY DIFFRACTION13M360 - 401
137X-RAY DIFFRACTION14N8 - 16
138X-RAY DIFFRACTION14N17 - 29
139X-RAY DIFFRACTION14N30 - 42
140X-RAY DIFFRACTION14N43 - 51
141X-RAY DIFFRACTION14N52 - 64
142X-RAY DIFFRACTION14N65 - 85
143X-RAY DIFFRACTION14N86 - 111
144X-RAY DIFFRACTION14N112 - 118
145X-RAY DIFFRACTION14N119 - 129
146X-RAY DIFFRACTION14N130 - 147
147X-RAY DIFFRACTION15O3 - 32
148X-RAY DIFFRACTION15O33 - 54
149X-RAY DIFFRACTION15O55 - 110
150X-RAY DIFFRACTION15O111 - 167
151X-RAY DIFFRACTION15O168 - 203
152X-RAY DIFFRACTION15O204 - 229
153X-RAY DIFFRACTION15O230 - 262
154X-RAY DIFFRACTION15O263 - 293
155X-RAY DIFFRACTION15O294 - 327
156X-RAY DIFFRACTION15O328 - 359
157X-RAY DIFFRACTION15O360 - 401
158X-RAY DIFFRACTION16P9 - 16
159X-RAY DIFFRACTION16P17 - 29
160X-RAY DIFFRACTION16P30 - 41
161X-RAY DIFFRACTION16P81 - 85
162X-RAY DIFFRACTION16P86 - 111
163X-RAY DIFFRACTION16P112 - 118
164X-RAY DIFFRACTION16P119 - 129
165X-RAY DIFFRACTION16P130 - 144
166X-RAY DIFFRACTION17A2001 - 2197
167X-RAY DIFFRACTION17B2001 - 2057
168X-RAY DIFFRACTION17C2001 - 2132
169X-RAY DIFFRACTION17D2001 - 2034
170X-RAY DIFFRACTION17E2001 - 2180
171X-RAY DIFFRACTION17F2001 - 2015
172X-RAY DIFFRACTION17G2001 - 2169
173X-RAY DIFFRACTION17H2001 - 2038
174X-RAY DIFFRACTION17I2001 - 2127
175X-RAY DIFFRACTION17J2001 - 2014
176X-RAY DIFFRACTION17K2001 - 2038
177X-RAY DIFFRACTION17L2001 - 2003
178X-RAY DIFFRACTION17M2001 - 2013
179X-RAY DIFFRACTION17N2001 - 2002
180X-RAY DIFFRACTION17O2001 - 2002

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