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- PDB-4knl: Crystal structure of Staphylococcus aureus hydrolase AmiA in comp... -

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Basic information

Entry
Database: PDB / ID: 4knl
TitleCrystal structure of Staphylococcus aureus hydrolase AmiA in complex with its ligand
Components
  • Bifunctional autolysin
  • Muramyl tetrapeptide
KeywordsHYDROLASE/SUBSTRATE / peptidoglycan / ligand complex / autolysin / amidase / N-acetylmuramoyl-L-alanine amidase / HYDROLASE-SUBSTRATE complex
Function / homology
Function and homology information


mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase / mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity / N-acetylmuramoyl-L-alanine amidase / amidase activity / N-acetylmuramoyl-L-alanine amidase activity / peptidoglycan catabolic process / cell wall organization / extracellular region
Similarity search - Function
Lysozyme subfamily 2 / Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain / GW domain / GW domain superfamily / Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase / GW (Gly-Tryp) dipeptide domain / GW domain profile. / Lysozyme-like / Peptidoglycan recognition protein-like / Ami_2 ...Lysozyme subfamily 2 / Mannosyl-glycoprotein endo-beta-N-acetylglucosamidase-like domain / GW domain / GW domain superfamily / Mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase / GW (Gly-Tryp) dipeptide domain / GW domain profile. / Lysozyme-like / Peptidoglycan recognition protein-like / Ami_2 / N-acetylmuramoyl-L-alanine amidase / N-acetylmuramoyl-L-alanine amidase domain / N-acetylmuramoyl-L-alanine amidase/PGRP domain superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Muramyl tetrapeptide / FORMIC ACID / IMIDAZOLE / N-acetyl-alpha-muramic acid / OXAMIC ACID / D(-)-TARTARIC ACID / Bifunctional autolysin
Similarity search - Component
Biological speciesStaphylococcus aureus subsp. aureus NCTC 8325 (bacteria)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å
AuthorsBuettner, F.M. / Stehle, T.
CitationJournal: J.Biol.Chem. / Year: 2014
Title: Structure-function analysis of Staphylococcus aureus amidase reveals the determinants of peptidoglycan recognition and cleavage.
Authors: Buttner, F.M. / Zoll, S. / Nega, M. / Gotz, F. / Stehle, T.
History
DepositionMay 10, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 12, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 3, 2014Group: Database references
Revision 1.2Jul 29, 2020Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / pdbx_chem_comp_identifier ...chem_comp / pdbx_chem_comp_identifier / pdbx_struct_conn_angle / pdbx_validate_polymer_linkage / struct_conn / struct_conn_type / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _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 / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _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_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 / _struct_conn_type.id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.0Mar 1, 2023Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Source and taxonomy / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_2 / entity / entity_name_com / entity_poly / entity_poly_seq / entity_src_gen / pdbx_entity_nonpoly / pdbx_entity_src_syn / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_struct_mod_residue / struct_asym / struct_conn / struct_ref / struct_ref_seq
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_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.pdbx_formal_charge / _atom_site.type_symbol / _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.pdbx_beg_seq_num / _entity_src_gen.pdbx_end_seq_num / _entity_src_gen.pdbx_gene_src_scientific_name / _entity_src_gen.pdbx_seq_type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_mod_residue.label_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_seq_id / _struct_ref.pdbx_seq_one_letter_code / _struct_ref_seq.db_align_beg / _struct_ref_seq.pdbx_auth_seq_align_beg / _struct_ref_seq.seq_align_end
Revision 2.1Sep 20, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 3.0Nov 15, 2023Group: Atomic model / Data collection / Derived calculations
Category: atom_site / chem_comp_atom ...atom_site / chem_comp_atom / chem_comp_bond / pdbx_validate_main_chain_plane / pdbx_validate_peptide_omega / pdbx_validate_torsion / struct_conn
Item: _atom_site.auth_atom_id / _atom_site.label_atom_id ..._atom_site.auth_atom_id / _atom_site.label_atom_id / _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_1 / _chem_comp_bond.atom_id_2 / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_label_atom_id
Revision 3.1Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Bifunctional autolysin
B: Bifunctional autolysin
C: Bifunctional autolysin
D: Bifunctional autolysin
F: Muramyl tetrapeptide
G: Muramyl tetrapeptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)103,47325
Polymers101,9766
Non-polymers1,49619
Water11,349630
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A: Bifunctional autolysin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,4275
Polymers25,2661
Non-polymers1614
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Bifunctional autolysin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,5166
Polymers25,2661
Non-polymers2505
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Bifunctional autolysin
F: Muramyl tetrapeptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,3998
Polymers25,7222
Non-polymers6776
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2440 Å2
ΔGint-30 kcal/mol
Surface area9300 Å2
MethodPISA
4
D: Bifunctional autolysin
G: Muramyl tetrapeptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)26,1316
Polymers25,7222
Non-polymers4084
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2030 Å2
ΔGint-21 kcal/mol
Surface area9120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.810, 82.830, 77.430
Angle α, β, γ (deg.)90.00, 96.18, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein / Protein/peptide / Sugars , 3 types, 8 molecules ABCDFG

#1: Protein
Bifunctional autolysin


Mass: 25265.828 Da / Num. of mol.: 4 / Fragment: UNP residues 198-421
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus subsp. aureus NCTC 8325 (bacteria)
Strain: NCTC 8325 / Gene: atl, nag, SAOUHSC_00994 / Plasmid: pGEX-4T3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q2FZK7, N-acetylmuramoyl-L-alanine amidase, mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase
#2: Protein/peptide Muramyl tetrapeptide


Type: Peptide-like / Class: Unknown / Mass: 456.516 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) / References: Muramyl tetrapeptide
#9: Sugar ChemComp-MUB / N-acetyl-alpha-muramic acid / N-acetyl-muramic acid / N-ACETYLMURAMIC ACID


Type: D-saccharide, alpha linking / Mass: 293.270 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C11H19NO8
IdentifierTypeProgram
a-D-GlcpNAc3IUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
MurNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 7 types, 647 molecules

#3: Chemical
ChemComp-IMD / IMIDAZOLE


Mass: 69.085 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H5N2
#4: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Na
#5: Chemical ChemComp-FMT / FORMIC ACID


Mass: 46.025 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: CH2O2
#6: Chemical ChemComp-OXM / OXAMIC ACID


Mass: 89.050 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H3NO3
#7: Chemical ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#8: Chemical ChemComp-TAR / D(-)-TARTARIC ACID


Mass: 150.087 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H6O6
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 630 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.11 Å3/Da / Density % sol: 41.68 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 0.1 M MES/imidazole, pH 6.5, 0.02 M sodium formate, 0.02 M ammonium acetate, 0.02 M sodium citrate, 0.02 M racemic sodium/potassium tartrate, 0.02 M sodium oxamate, 12.5% w/v PEG1000, 12.5% ...Details: 0.1 M MES/imidazole, pH 6.5, 0.02 M sodium formate, 0.02 M ammonium acetate, 0.02 M sodium citrate, 0.02 M racemic sodium/potassium tartrate, 0.02 M sodium oxamate, 12.5% w/v PEG1000, 12.5% w/v PEG3350, 12.5% w/v MPD, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00605 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 16, 2012
RadiationMonochromator: Fixed-exit LN2 cooled double crystal Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00605 Å / Relative weight: 1
ReflectionResolution: 1.55→48.21 Å / Num. obs: 122961 / % possible obs: 99.1 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.6 % / Biso Wilson estimate: 24.5 Å2 / Net I/σ(I): 13.9
Reflection shellResolution: 1.55→1.59 Å / Redundancy: 3 % / Mean I/σ(I) obs: 1.7 / Num. unique all: 8927 / % possible all: 98.1

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Processing

Software
NameVersionClassification
RemDAqdata collection
PHASERphasing
PHENIX(phenix.refine: 1.8_1069)refinement
XDSdata reduction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 4KNK

4knk


Resolution: 1.55→48.209 Å / SU ML: 0.16 / σ(F): 1.99 / Phase error: 22.14 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.1981 6129 5 %RANDOM
Rwork0.1712 ---
obs0.1725 122657 99.48 %-
all-124130 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.55→48.209 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6628 0 58 630 7316
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0126879
X-RAY DIFFRACTIONf_angle_d1.3829390
X-RAY DIFFRACTIONf_dihedral_angle_d15.2292390
X-RAY DIFFRACTIONf_chiral_restr0.095965
X-RAY DIFFRACTIONf_plane_restr0.0081239
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.55-1.56760.31291990.31133776X-RAY DIFFRACTION97
1.5676-1.5860.32192010.28153818X-RAY DIFFRACTION99
1.586-1.60540.31492030.26753845X-RAY DIFFRACTION99
1.6054-1.62570.27742040.25683890X-RAY DIFFRACTION99
1.6257-1.64710.25652040.23643872X-RAY DIFFRACTION99
1.6471-1.66960.27422040.23123871X-RAY DIFFRACTION100
1.6696-1.69350.25162060.22823907X-RAY DIFFRACTION100
1.6935-1.71880.25992030.23483860X-RAY DIFFRACTION100
1.7188-1.74560.27262040.22483880X-RAY DIFFRACTION100
1.7456-1.77430.25742040.21623865X-RAY DIFFRACTION100
1.7743-1.80480.24242040.20653883X-RAY DIFFRACTION100
1.8048-1.83770.23482030.19263873X-RAY DIFFRACTION100
1.8377-1.8730.2312040.18453881X-RAY DIFFRACTION100
1.873-1.91120.20532060.17113896X-RAY DIFFRACTION100
1.9112-1.95280.23752040.17593891X-RAY DIFFRACTION100
1.9528-1.99820.19052060.15993905X-RAY DIFFRACTION100
1.9982-2.04820.21252040.1623864X-RAY DIFFRACTION100
2.0482-2.10360.19852020.15543885X-RAY DIFFRACTION100
2.1036-2.16550.22050.15053900X-RAY DIFFRACTION100
2.1655-2.23540.17372060.15163901X-RAY DIFFRACTION100
2.2354-2.31530.18882050.16113888X-RAY DIFFRACTION100
2.3153-2.4080.20182040.1573885X-RAY DIFFRACTION99
2.408-2.51760.21142050.16143911X-RAY DIFFRACTION100
2.5176-2.65030.17842040.15653875X-RAY DIFFRACTION100
2.6503-2.81630.17912040.15923901X-RAY DIFFRACTION100
2.8163-3.03370.17972060.16063896X-RAY DIFFRACTION100
3.0337-3.3390.15942060.1523913X-RAY DIFFRACTION100
3.339-3.82190.15852050.14483906X-RAY DIFFRACTION99
3.8219-4.81460.14982060.13833919X-RAY DIFFRACTION99
4.8146-48.23190.20342080.17983971X-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)
10.8593-1.2048-0.90642.12930.86721.3590.09160.0956-0.08750.0582-0.041-1.11470.04370.6590.12310.21450.1309-0.06450.2696-0.06370.488738.05514.991582.9532
21.08620.55090.39690.53470.370.45970.0428-0.14860.12520.0636-0.06940.0555-0.0368-0.09780.03270.15020.00610.00970.1323-0.01680.223212.209312.263478.2249
30.90990.51330.37250.72730.27970.60390.0170.0323-0.0284-0.02280.0021-0.0167-0.02260.0462-0.01830.1607-0.00240.00320.1299-0.01070.227519.337311.984275.3694
41.60760.56020.31460.57710.09591.5950.01390.0351-0.0132-0.01140.0332-0.0335-0.02110.1331-0.03860.1261-0.0130.00440.105-0.01920.219126.22115.528577.1841
52.65871.4230.06712.0165-0.83212.14860.49680.0125-0.3036-0.2719-0.4180.72040.1714-0.4068-0.04440.2648-0.0132-0.05280.36760.04820.429-16.87043.802332.7878
65.2411-1.42540.91311.8961.17254.61370.28220.9866-0.38280.179-0.07510.05310.24380.0567-0.19220.3210.0939-0.05050.5314-0.02990.2246-6.28625.576424.2372
73.28221.0027-0.17412.74772.37023.5797-0.11430.46510.2034-0.16760.0328-0.0684-0.10680.35060.0660.19290.017-0.00780.29050.06120.300317.66677.127342.251
81.7941-0.44890.48441.36970.25730.1860.01160.50230.3469-0.2098-0.1141-0.1794-0.03340.14510.05390.17370.01670.00280.23450.07770.2615.478913.479943.5158
94.0836-0.86980.78781.1922-1.46952.7534-0.04240.92770.5376-0.0732-0.1975-0.5772-0.12770.40690.22290.2003-0.00460.05870.62550.24030.418817.343315.328433.1915
100.6973-0.7171-0.81723.19410.55564.14710.13150.63310.3243-0.1805-0.1749-0.413-0.13570.12020.00150.13250.02230.01630.30640.09350.26212.421411.359540.0011
112.1248-0.72970.8241.4153-0.65982.52970.11180.69670.1251-0.2394-0.1414-0.0845-0.00970.07880.0580.1740.05390.01510.33010.04840.18332.28911.357935.3487
125.7153-5.59392.0665.6967-2.20460.879-0.1266-0.0822-0.06450.25330.14390.2721-0.1332-0.1747-0.03830.23320.03250.01120.21320.00070.2318-7.0411.786846.6636
132.1052-0.27480.96122.23060.61013.7186-0.02440.56530.6568-0.052-0.0553-0.1727-0.27760.02010.12790.18430.0394-0.00860.24570.08730.2791-1.658922.062439.1365
143.45260.0806-0.16758.9096-3.18844.56750.15980.3485-0.3375-0.4274-0.04560.33960.3675-0.1191-0.10780.17960.0243-0.03720.2374-0.0180.2024-8.89314.625436.2913
152.7235-1.9531.37774.8967-0.09961.33010.2413-0.06730.16440.43510.16950.4483-0.4285-0.6882-0.07240.20430.10250.16090.38370.03440.4168-20.4927-2.566382.6717
162.02331.0051-0.93540.7465-0.56590.64760.1955-0.29850.27060.1787-0.0630.0627-0.0680.0116-0.15870.1893-0.00110.01840.2051-0.03510.24752.2389-5.484881.3413
172.90980.61060.34560.29460.39841.2730.02850.0151-0.1123-0.11040.14090.17810.1989-0.1701-0.20330.16160.00810.02140.1256-0.04740.18711.1568-11.109970.1266
183.1511-0.2-0.6942.70570.6671.73970.089-0.1505-0.1126-0.0132-0.0066-0.20820.11430.0044-0.09880.12490.0037-0.01130.11050.00820.186210.7084-13.059277.5358
191.58010.3414-0.56650.6659-0.59031.22630.0583-0.10530.07650.0459-0.0370.09230.0418-0.0456-0.02260.1519-0.01970.00640.1384-0.01780.18520.411-9.246676.0966
201.72821.2227-0.50055.9032-2.61342.6613-0.15020.26250.0682-0.27860.38470.47170.2205-0.2455-0.24240.1874-0.0495-0.00760.24840.00840.2482-12.5366-10.277767.7152
211.9061-0.2442-0.98830.7064-0.52133.2049-0.0380.0928-0.4059-0.1236-0.00790.06250.2505-0.10140.05550.1788-0.0702-0.01070.1571-0.03040.2525-5.9385-20.094673.6522
222.9939-0.4752-0.46173.6219-0.26954.92410.0798-0.19670.23970.21050.03560.1265-0.3759-0.263-0.10450.14380.00350.03160.1948-0.01210.2176-12.6776-2.526479.8666
233.24272.4350.07062.1532-1.15864.54840.39640.784-0.17440.048-0.2424-0.2584-0.32750.0586-0.13560.269-0.01290.06370.5632-0.05860.624541.8892-5.86633.7311
244.6128-1.2765-1.94111.83420.28352.32480.16291.20740.4528-0.48170.0462-0.4118-0.17520.1884-0.23050.35450.02610.13130.6440.01860.349930.8838-8.022725.3978
253.24450.0621-0.89081.6152-0.46623.05810.05040.42220.0608-0.07410.02580.02-0.0902-0.1227-0.08430.1850.01120.00190.2145-0.00510.20837.5497-6.253244.1145
263.0817-0.56460.67390.9271-0.47341.48020.06530.225-0.1906-0.05680.0397-0.19090.13440.1318-0.13370.1415-0.00130.00910.17280.01470.163219.8889-11.987846.2842
276.54221.2216-2.21055.2111-0.97473.85910.22780.1014-0.2937-0.1763-0.03730.07270.21320.0369-0.2280.2171-0.008-0.04210.2535-0.05090.23057.2012-16.195437.3761
282.82641.119-1.33215.2667-2.04394.53150.14050.395-0.0202-0.20830.02160.11170.08290.0438-0.14070.11120.0214-0.01420.1973-0.02780.122312.8576-12.284539.1404
292.1485-0.3948-0.15771.74370.35881.42550.07420.4204-0.0374-0.2202-0.0274-0.17040.0750.146-0.04380.16650.02640.00870.2407-0.00780.166620.7153-10.452940.2659
304.6988-3.77280.59468.5388-0.84372.4143-0.0915-0.10580.15160.2864-0.0841-1.07960.12430.34520.15790.16460.02710.00980.26080.01580.280833.5986-11.211148.7952
311.7388-0.45380.02461.91130.60045.73170.13170.3626-0.344-0.1481-0.0003-0.07460.4960.1891-0.10820.19310.0695-0.01240.2234-0.04450.272226.8562-21.23443.3858
321.99290.37060.6196.22431.46632.58760.01190.36790.2075-0.30180.129-0.8069-0.14910.288-0.12070.2110.00810.08560.37540.02240.310733.8877-4.819737.0267
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 213 through 223 )
2X-RAY DIFFRACTION2chain 'A' and (resid 224 through 301 )
3X-RAY DIFFRACTION3chain 'A' and (resid 302 through 366 )
4X-RAY DIFFRACTION4chain 'A' and (resid 367 through 417 )
5X-RAY DIFFRACTION5chain 'B' and (resid 213 through 223 )
6X-RAY DIFFRACTION6chain 'B' and (resid 224 through 238 )
7X-RAY DIFFRACTION7chain 'B' and (resid 239 through 251 )
8X-RAY DIFFRACTION8chain 'B' and (resid 252 through 273 )
9X-RAY DIFFRACTION9chain 'B' and (resid 274 through 283 )
10X-RAY DIFFRACTION10chain 'B' and (resid 284 through 312 )
11X-RAY DIFFRACTION11chain 'B' and (resid 313 through 351 )
12X-RAY DIFFRACTION12chain 'B' and (resid 352 through 366 )
13X-RAY DIFFRACTION13chain 'B' and (resid 367 through 395 )
14X-RAY DIFFRACTION14chain 'B' and (resid 396 through 417 )
15X-RAY DIFFRACTION15chain 'C' and (resid 213 through 223 )
16X-RAY DIFFRACTION16chain 'C' and (resid 224 through 251 )
17X-RAY DIFFRACTION17chain 'C' and (resid 252 through 273 )
18X-RAY DIFFRACTION18chain 'C' and (resid 274 through 301 )
19X-RAY DIFFRACTION19chain 'C' and (resid 302 through 352 )
20X-RAY DIFFRACTION20chain 'C' and (resid 353 through 366 )
21X-RAY DIFFRACTION21chain 'C' and (resid 367 through 395 )
22X-RAY DIFFRACTION22chain 'C' and (resid 396 through 419 )
23X-RAY DIFFRACTION23chain 'D' and (resid 214 through 223 )
24X-RAY DIFFRACTION24chain 'D' and (resid 224 through 238 )
25X-RAY DIFFRACTION25chain 'D' and (resid 239 through 251 )
26X-RAY DIFFRACTION26chain 'D' and (resid 252 through 273 )
27X-RAY DIFFRACTION27chain 'D' and (resid 274 through 284 )
28X-RAY DIFFRACTION28chain 'D' and (resid 285 through 301 )
29X-RAY DIFFRACTION29chain 'D' and (resid 302 through 352 )
30X-RAY DIFFRACTION30chain 'D' and (resid 353 through 366 )
31X-RAY DIFFRACTION31chain 'D' and (resid 367 through 395 )
32X-RAY DIFFRACTION32chain 'D' and (resid 396 through 417 )

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