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- PDB-6cey: Aminoglycoside Phosphotransferase (2'')-Ia in complex with GMPPNP... -

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Basic information

Entry
Database: PDB / ID: 6cey
TitleAminoglycoside Phosphotransferase (2'')-Ia in complex with GMPPNP, Magnesium, and Lividomycin moieties
ComponentsBifunctional AAC/APH
KeywordsTRANSFERASE/Antibiotic / Kinase / Antibiotic / Aminoglycoside / Resistance / Transferase / TRANSFERASE-Antibiotic complex
Function / homology
Function and homology information


aminoglycoside 2''-phosphotransferase / aminoglycoside phosphotransferase activity / N-acyltransferase activity / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / response to antibiotic / ATP binding / cytoplasm
Similarity search - Function
Acetyltransferase (GNAT) domain / Aminoglycoside phosphotransferase / Phosphotransferase enzyme family / Aminoglycoside 3'-phosphotransferase; Chain: A, domain 2 / Aminoglycoside phosphotransferase (APH), C-terminal lobe / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / Acyl-CoA N-acyltransferase / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 ...Acetyltransferase (GNAT) domain / Aminoglycoside phosphotransferase / Phosphotransferase enzyme family / Aminoglycoside 3'-phosphotransferase; Chain: A, domain 2 / Aminoglycoside phosphotransferase (APH), C-terminal lobe / Gcn5-related N-acetyltransferase (GNAT) domain profile. / GNAT domain / Acyl-CoA N-acyltransferase / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Protein kinase-like domain superfamily / Alpha-Beta Complex / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Chem-LIV / Bifunctional AAC/APH
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.4 Å
AuthorsCaldwell, S.J. / Berghuis, A.M.
Funding support Canada, 1items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)MOP-13107 Canada
CitationJournal: Antimicrob. Agents Chemother. / Year: 2018
Title: Plasticity of Aminoglycoside Binding to Antibiotic Kinase APH(2′′)-Ia.
Authors: Caldwell, S.J. / Berghuis, A.M.
History
DepositionFeb 13, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 11, 2018Provider: repository / Type: Initial release
Revision 1.1May 2, 2018Group: Data collection / Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jul 4, 2018Group: Data collection / Database references / Category: citation / Item: _citation.journal_volume / _citation.title
Revision 1.3Feb 20, 2019Group: Author supporting evidence / Data collection / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Jan 8, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Oct 4, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_entity_nonpoly / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _chem_comp.name / _chem_comp.pdbx_synonyms ..._chem_comp.name / _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_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.pdbx_dist_value / _struct_conn.pdbx_ptnr1_label_alt_id / _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_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
A: Bifunctional AAC/APH
B: Bifunctional AAC/APH
C: Bifunctional AAC/APH
D: Bifunctional AAC/APH
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,96821
Polymers143,7934
Non-polymers3,17617
Water9,746541
1
A: Bifunctional AAC/APH
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,5545
Polymers35,9481
Non-polymers6064
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: Bifunctional AAC/APH
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,5545
Polymers35,9481
Non-polymers6064
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: Bifunctional AAC/APH
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,5796
Polymers35,9481
Non-polymers6315
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: Bifunctional AAC/APH
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,2815
Polymers35,9481
Non-polymers1,3334
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)90.250, 100.240, 94.010
Angle α, β, γ (deg.)90.00, 105.17, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12A
22C
13A
23D
14B
24C
15B
25D
16C
26D

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ASNASNTYRTYRAA185 - 47711 - 303
21ASNASNTYRTYRBB185 - 47711 - 303
12ASNASNTYRTYRAA185 - 47711 - 303
22ASNASNTYRTYRCC185 - 47711 - 303
13ASNASNARGARGAA185 - 47511 - 301
23ASNASNARGARGDD185 - 47511 - 301
14THRTHRTYRTYRBB184 - 47710 - 303
24THRTHRTYRTYRCC184 - 47710 - 303
15TYRTYRARGARGBB179 - 4755 - 301
25TYRTYRARGARGDD179 - 4755 - 301
16THRTHRARGARGCC184 - 47510 - 301
26THRTHRARGARGDD184 - 47510 - 301

NCS ensembles :
ID
1
2
3
4
5
6

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Bifunctional AAC/APH


Mass: 35948.199 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: aacA-aphD, R015, VRA0030 / Plasmid: pET-22b-APH(2'')-Ia / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(LDE3)
References: UniProt: P0A0C1, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups, aminoglycoside 2''-phosphotransferase

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Non-polymers , 5 types, 558 molecules

#2: Chemical
ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER


Mass: 522.196 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H17N6O13P3
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#5: Chemical ChemComp-LIV / (2R,3S,4S,5S,6R)-2-((2S,3S,4R,5R,6R)-5-AMINO-2-(AMINOMETHYL)-6-((2R,3S,4R,5S)-5-((1R,2R,3S,5R,6S)-3,5-DIAMINO-2-((2S,3R ,5S,6R)-3-AMINO-5-HYDROXY-6-(HYDROXYMETHYL)-TETRAHYDRO-2H-PYRAN-2-YLOXY)-6-HYDROXYCYCLOHEXYLOXY)-4-HYDROXY-2-(HYDROXYMET HYL)-TETRAHYDROFURAN-3-YLOXY)-4-HYDROXY-TETRAHYDRO-2H-PYRAN-3-YLOXY)-6-(HYDROXYMETHYL)-TETRAHYDRO-2H-PYRAN-3,4,5-TRIOL / LIVIDOMYCIN A / O-2-AMINO-2,3-DIDEOXY-ALPHA-D-GLUCOPYRANOSYL-(1,4)-O-[BETA-D-MANNOPYRANOSYL-(1,4)-O-2,6-DIAMINO-2,6-DIDEOXY-BETA-L-IDOPY RANOSYL-(1,3)-BETA-D-RIBOFURANOSYL-(1,5)-2-DEOXY-D-STREPTAMINE


Mass: 761.770 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C29H55N5O18 / Comment: antibiotic*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 541 / 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: 2.87 Å3/Da / Density % sol: 56.91 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 80-120mM MgCl2, 8% glycerol, 10% PEG 3350, 100mM HEPES pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.9795 Å
DetectorType: RAYONIX MX-300 / Detector: CCD / Date: Nov 26, 2013
RadiationMonochromator: ACCEL/BRUKER double crystal monochromator (DCM), featuring indirectly cryo-cooled first crystal and sagittally focusing second crystal
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.4→90.73 Å / Num. obs: 63302 / % possible obs: 100 % / Redundancy: 4.2 % / Biso Wilson estimate: 50.686 Å2 / CC1/2: 0.988 / Rmerge(I) obs: 0.11 / Rpim(I) all: 0.084 / Rrim(I) all: 0.127 / Net I/σ(I): 10
Reflection shellResolution: 2.4→2.46 Å / Redundancy: 4.2 % / Rmerge(I) obs: 1.345 / Mean I/σ(I) obs: 1.8 / Num. unique obs: 4441 / CC1/2: 0.287 / Rpim(I) all: 1.011 / Rrim(I) all: 1.538 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0189refinement
iMOSFLM0.1.27data reduction
Aimless0.3.11data scaling
Coot0.7.2model building
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: PDB 5IQA

5iqa


Resolution: 2.4→90.73 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.947 / SU B: 16.142 / SU ML: 0.18 / Cross valid method: THROUGHOUT / ESU R: 0.312 / ESU R Free: 0.219 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: Author states that the ligand modelled is their best interpretation of the observed electron density with the tools available at deposition, but remains subject to some ambiguity in absolute ...Details: Author states that the ligand modelled is their best interpretation of the observed electron density with the tools available at deposition, but remains subject to some ambiguity in absolute configuration. The difference density was observed following the soaking of lividomycin to antibiotic-free crystals. Observed electron density likely reflects the superimposition of multiple weak binding modes, which would explain to low-level off-target activity of the enzyme as reported in studies of enzymatic regiospecificity.
RfactorNum. reflection% reflectionSelection details
Rfree0.21598 3190 5 %RANDOM
Rwork0.1714 ---
obs0.17368 60081 99.93 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 59.493 Å2
Baniso -1Baniso -2Baniso -3
1--0.15 Å2-0 Å2-0.05 Å2
2--0.16 Å2-0 Å2
3---0.02 Å2
Refinement stepCycle: 1 / Resolution: 2.4→90.73 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9588 0 192 541 10321
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.0199980
X-RAY DIFFRACTIONr_bond_other_d0.0020.028861
X-RAY DIFFRACTIONr_angle_refined_deg2.0381.96913513
X-RAY DIFFRACTIONr_angle_other_deg1.073320659
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.08551157
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.12125.606528
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.669151791
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.7531532
X-RAY DIFFRACTIONr_chiral_restr0.1230.21484
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0211157
X-RAY DIFFRACTIONr_gen_planes_other0.0010.021995
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_it2.0713.3434652
X-RAY DIFFRACTIONr_mcbond_other2.0713.3434651
X-RAY DIFFRACTIONr_mcangle_it3.0565.0115801
X-RAY DIFFRACTIONr_mcangle_other3.0565.0115802
X-RAY DIFFRACTIONr_scbond_it2.893.6485328
X-RAY DIFFRACTIONr_scbond_other2.893.6485329
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other4.4815.3587713
X-RAY DIFFRACTIONr_long_range_B_refined6.8839.6311423
X-RAY DIFFRACTIONr_long_range_B_other6.89239.59111411
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 / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A189260.07
12B189260.07
21A189760.07
22C189760.07
31A186720.08
32D186720.08
41B189080.08
42C189080.08
51B192060.07
52D192060.07
61C186440.08
62D186440.08
LS refinement shellResolution: 2.4→2.462 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.326 229 -
Rwork0.291 4416 -
obs--99.85 %
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)
18.6785-5.5466.76984.0034-4.8315.84140.40210.2130.0931-0.5318-0.15530.23540.61160.2248-0.24690.34080.0065-0.09230.30090.00530.249646.335-3.17655.846
215.39028.6463-16.085820.34722.17824.93350.26350.2831-0.5001-0.1181-1.24840.3659-0.4821-1.3190.98490.34770.0544-0.03290.350.00120.224646.818-1.91236.44
32.5112-0.10030.83952.893-1.29927.44490.02640.03980.2205-0.3222-0.1871-0.28490.0180.64450.16070.12280.0060.07930.29960.02810.144654.542.25951.487
415.0023-4.61.93562.01230.77525.0127-0.1719-0.329-0.6259-0.11360.09240.5592-0.1014-0.41640.07950.3972-0.0727-0.15260.33920.11660.544841.534-0.01849.752
560.8829341.3369123.69081913.709693.474251.2955-0.58941.9915-5.2892-3.684411.3061-29.7397-1.3344.0868-10.71660.62580.08010.95342.09660.72522.224347.31212.01856.809
63.0114-1.4614-0.26766.2016-1.41953.33030.0810.0687-0.10050.0678-0.07540.28510.0007-0.0943-0.00560.0723-0.03760.03380.1913-0.0030.042745.743-6.02371.102
75.9877-3.64592.04643.2931-0.57152.6997-0.06630.04970.28670.3274-0.00670.1024-0.42460.12650.0730.2939-0.03410.15470.131-0.01670.168328.7511.14971.196
810.94675.4011-4.07518.0262-4.33327.8687-0.14030.5085-0.2983-0.60550.0871-0.33640.3080.06190.05320.21960.05620.08520.245-0.06570.200724.2476.8358.639
911.49926.60131.53027.7313-5.02359.04080.2447-1.3182-0.06480.4616-0.384-0.1276-0.4553-0.71160.13920.24760.0894-0.00760.2266-0.00240.00336.7684.62720.806
102.94780.26350.09020.02920.00940.00640.0071-0.0468-0.3991-0.0169-0.01410.00820.0273-0.02970.0070.4844-0.02640.0150.4735-0.03460.456937.5772.61641.25
111.63820.14040.68531.4877-0.65947.3534-0.1128-0.23350.3340.1615-0.0336-0.0713-0.66080.06050.14640.34290.06030.01640.0859-0.03220.161343.05312.83724.241
121.1805-3.55630.732114.5216-1.41370.97380.0907-0.0299-0.4932-0.1027-0.00251.11220.2565-0.0833-0.08820.3342-0.00430.05010.2790.00830.500339.6440.28727.255
136.97746.22-4.841238.7377-9.12884.0584-0.1909-1.3431-0.3819-1.26070.14331.20460.31390.74680.04750.52750.0687-0.02010.57310.01380.421152.7662.14923.923
146.0052-1.35380.77353.0329-0.1472.6515-0.0940.144-0.2279-0.02890.11630.3191-0.0083-0.2218-0.02230.18950.04230.01370.06930.02120.102733.7922.765.745
152.383-2.01930.85316.1734-1.50592.57890.09850.1946-0.134-0.0913-0.1618-0.0268-0.11250.03360.06330.0742-0.0190.06060.1028-0.07790.120649.901-15.257.848
165.28782.5423.883510.32713.48076.72210.209-0.45030.21170.8081-0.29830.6996-0.0939-0.57480.08930.2330.01860.15520.175-0.05780.208144.968-18.45120.782
1717.8797-4.5478-0.73795.17294.3224.29020.1033-0.1236-0.0305-0.49530.0043-0.0969-0.4726-0.0496-0.10760.223-0.0166-0.00910.2689-0.01720.168564.26135.89975.063
1810.66477.34320.48376.22973.939411.1069-0.07830.1529-0.5969-0.21660.1208-0.4193-0.52050.0764-0.04250.4336-0.0052-0.0350.34470.00560.414565.234.41155.751
193.1082-0.187-0.63411.97520.65558.2006-0.09740.2398-0.2175-0.34690.00530.18070.296-0.64890.09210.1393-0.0576-0.00150.2784-0.02920.248856.30330.22870.653
2010.882-3.1172-3.28811.01791.34894.976-0.2478-0.38070.70850.05920.2208-0.35790.1850.35180.0270.2719-0.0541-0.0030.3404-0.1090.486469.15332.53669.323
21253.60843.4169165.79790.22847.4912259.973-2.8047-2.4032-1.47220.0307-0.10370.11080.1588-3.70642.90850.61170.0382-0.06810.5109-0.23170.671169.60719.17766.71
223.0469-1.45020.69394.6541-1.90524.8814-0.078-0.10190.24070.1976-0.007-0.1615-0.3632-0.10290.0850.08630.05810.00520.2343-0.06430.197964.26439.40690.162
235.8471-2.7928-2.32262.50530.75112.3412-0.256-0.1332-0.4281-0.01480.09760.18960.2486-0.20540.15840.1335-0.01930.06010.06590.0130.129781.8822.47791.838
249.67863.26722.64357.55733.81098.9086-0.18490.38530.3495-0.674-0.11540.6579-0.1636-0.67660.30030.13980.01150.01650.16710.00780.134186.53825.85379.257
2513.78846.5029-8.73245.9017-1.0188.9234-0.0289-0.648-0.49210.4167-0.2763-0.23830.48460.41590.30520.22980.02050.0320.32610.00790.085574.49728.93140.372
260.2953-0.78342.87252.1145-7.77128.7285-0.12380.11680.05990.1941-0.342-0.1675-0.64231.01050.46580.52150.04610.02970.55880.0260.833373.03241.71335.618
272.56870.5125-0.54552.9340.9150.49070.2818-0.12350.060.2029-0.1799-0.3473-0.0126-0.0423-0.10190.5087-0.0492-0.02890.4711-0.00670.420173.49329.8660.753
282.2297-0.4967-0.85222.6841-0.44767.3966-0.1123-0.2427-0.3806-0.0163-0.0150.02150.3805-0.00650.12730.2551-0.05840.02380.287-0.0050.358668.50220.38743.154
290.7727-0.83791.7719.8144-0.81994.36780.01890.02410.1828-0.1787-0.189-0.5911-0.15330.07650.17020.4084-0.04770.06270.368-0.00040.400571.48532.82946.875
304.0413-8.39922.290954.501147.960576.3422-0.4332-0.1664-0.0769-0.4225-0.12120.593-2.1492-0.79320.55440.2082-0.01950.05940.3792-00.430958.69430.8743.232
316.2579-0.3398-0.1362.3061-1.0572.8102-0.00540.1794-0.0539-0.188-0.0362-0.21820.16630.18330.04150.2744-0.00080.12680.3049-0.06160.213278.00231.72225.587
324.8012-3.4591-1.03995.97430.78291.8254-0.09410.13650.50710.31590.167-0.2537-0.0680.083-0.07290.2344-0.0522-0.02630.36960.06960.228161.49949.19528.111
336.01542.6457-0.55436.37040.19928.5993-0.1052-0.45980.11720.9998-0.0404-0.73010.21020.92630.14570.62030.174-0.13490.5683-0.0210.387865.75451.12641.336
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A500
2X-RAY DIFFRACTION1A700 - 702
3X-RAY DIFFRACTION1A900 - 909
4X-RAY DIFFRACTION2A185 - 187
5X-RAY DIFFRACTION3A188 - 207
6X-RAY DIFFRACTION3A217 - 229
7X-RAY DIFFRACTION3A237 - 277
8X-RAY DIFFRACTION4A208 - 216
9X-RAY DIFFRACTION5A236
10X-RAY DIFFRACTION6A278 - 318
11X-RAY DIFFRACTION6A367 - 431
12X-RAY DIFFRACTION7A319 - 366
13X-RAY DIFFRACTION7A432 - 447
14X-RAY DIFFRACTION8A448 - 478
15X-RAY DIFFRACTION9B500
16X-RAY DIFFRACTION9B700 - 702
17X-RAY DIFFRACTION9B900 - 909
18X-RAY DIFFRACTION10B179 - 187
19X-RAY DIFFRACTION11B188 - 207
20X-RAY DIFFRACTION11B217 - 229
21X-RAY DIFFRACTION11B237 - 277
22X-RAY DIFFRACTION12B208 - 216
23X-RAY DIFFRACTION13B230 - 236
24X-RAY DIFFRACTION14B278 - 318
25X-RAY DIFFRACTION14B367 - 431
26X-RAY DIFFRACTION15B319 - 366
27X-RAY DIFFRACTION15B432 - 447
28X-RAY DIFFRACTION16B448 - 478
29X-RAY DIFFRACTION17C500
30X-RAY DIFFRACTION17C700 - 702
31X-RAY DIFFRACTION17C900 - 909
32X-RAY DIFFRACTION18C184 - 187
33X-RAY DIFFRACTION19C188 - 207
34X-RAY DIFFRACTION19C217 - 229
35X-RAY DIFFRACTION19C237 - 277
36X-RAY DIFFRACTION20C208 - 216
37X-RAY DIFFRACTION21C230
38X-RAY DIFFRACTION22C278 - 318
39X-RAY DIFFRACTION22C367 - 431
40X-RAY DIFFRACTION23C319 - 366
41X-RAY DIFFRACTION23C432 - 447
42X-RAY DIFFRACTION24C448 - 478
43X-RAY DIFFRACTION25D500
44X-RAY DIFFRACTION25D700 - 702
45X-RAY DIFFRACTION25D900 - 911
46X-RAY DIFFRACTION26D600
47X-RAY DIFFRACTION27D179 - 187
48X-RAY DIFFRACTION28D188 - 207
49X-RAY DIFFRACTION28D217 - 229
50X-RAY DIFFRACTION28D237 - 277
51X-RAY DIFFRACTION29D208 - 216
52X-RAY DIFFRACTION30D230 - 236
53X-RAY DIFFRACTION31D278 - 318
54X-RAY DIFFRACTION31D367 - 431
55X-RAY DIFFRACTION32D319 - 366
56X-RAY DIFFRACTION32D432 - 447
57X-RAY DIFFRACTION33D448 - 476

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