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- PDB-4gkh: Crystal structure of the aminoglycoside phosphotransferase APH(3'... -

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Basic information

Entry
Database: PDB / ID: 4gkh
TitleCrystal structure of the aminoglycoside phosphotransferase APH(3')-Ia, with substrate kanamycin and small molecule inhibitor 1-NA-PP1
ComponentsAminoglycoside 3'-phosphotransferase AphA1-IAB
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / PYRAZOLOPYRIMIDINE / 1-NA-PP1 / BUMPED KINASE INHIBITOR / BKI / PROTEIN KINASE INHIBITOR / CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES / CSGID / NIAID / NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES / TRANSFERASE-TRANSFERASE INHIBITOR COMPLEX / EUKARYOTIC PROTEIN KINASE-LIKE FOLD / ALPHA/BETA PROTEIN / TRANSFERASE / PHOSPHOTRANSFERASE / AMINOGLYCOSIDE PHOSPHOTRANSFERASE / ANTIBIOTIC RESISTANCE / AMINOGLYCOSIDES / KANAMYCIN / GTP / INTRACELLULAR
Function / homology
Function and homology information


kanamycin kinase / kanamycin kinase activity / phosphorylation / response to antibiotic / ATP binding / metal ion binding
Similarity search - Function
Aminoglycoside 3-phosphotransferase / Aminoglycoside phosphotransferase / Phosphotransferase enzyme family / Aminoglycoside 3'-phosphotransferase; Chain: A, domain 2 / Aminoglycoside phosphotransferase (APH), C-terminal lobe / 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
Chem-0J9 / ACETATE ION / KANAMYCIN A / DI(HYDROXYETHYL)ETHER / Aminoglycoside 3'-phosphotransferase
Similarity search - Component
Biological speciesAcinetobacter baumannii (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.863 Å
AuthorsStogios, P.J. / Evdokimova, E. / Wawrzak, Z. / Minasov, G. / Egorova, O. / Di Leo, R. / Shakya, T. / Spanogiannopoulos, P. / Todorovic, N. / Capretta, A. ...Stogios, P.J. / Evdokimova, E. / Wawrzak, Z. / Minasov, G. / Egorova, O. / Di Leo, R. / Shakya, T. / Spanogiannopoulos, P. / Todorovic, N. / Capretta, A. / Wright, G.D. / Savchenko, A. / Anderson, W.F. / Center for Structural Genomics of Infectious Diseases (CSGID)
CitationJournal: Biochem.J. / Year: 2013
Title: Structure-guided optimization of protein kinase inhibitors reverses aminoglycoside antibiotic resistance.
Authors: Stogios, P.J. / Spanogiannopoulos, P. / Evdokimova, E. / Egorova, O. / Shakya, T. / Todorovic, N. / Capretta, A. / Wright, G.D. / Savchenko, A.
History
DepositionAug 11, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 5, 2012Provider: repository / Type: Initial release
Revision 1.1Jun 26, 2013Group: Database references
Revision 1.2Aug 7, 2013Group: Database references
Revision 1.3Sep 4, 2013Group: Database references
Revision 1.4Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.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_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Dec 6, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.6Nov 20, 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: Aminoglycoside 3'-phosphotransferase AphA1-IAB
B: Aminoglycoside 3'-phosphotransferase AphA1-IAB
C: Aminoglycoside 3'-phosphotransferase AphA1-IAB
D: Aminoglycoside 3'-phosphotransferase AphA1-IAB
E: Aminoglycoside 3'-phosphotransferase AphA1-IAB
F: Aminoglycoside 3'-phosphotransferase AphA1-IAB
G: Aminoglycoside 3'-phosphotransferase AphA1-IAB
H: Aminoglycoside 3'-phosphotransferase AphA1-IAB
I: Aminoglycoside 3'-phosphotransferase AphA1-IAB
J: Aminoglycoside 3'-phosphotransferase AphA1-IAB
K: Aminoglycoside 3'-phosphotransferase AphA1-IAB
L: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)388,66491
Polymers376,20512
Non-polymers12,45979
Water51,7032870
1
A: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3527
Polymers31,3501
Non-polymers1,0026
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3167
Polymers31,3501
Non-polymers9666
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,7059
Polymers31,3501
Non-polymers1,3558
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,2838
Polymers31,3501
Non-polymers9337
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3527
Polymers31,3501
Non-polymers1,0026
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,4349
Polymers31,3501
Non-polymers1,0848
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3758
Polymers31,3501
Non-polymers1,0257
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
H: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3997
Polymers31,3501
Non-polymers1,0496
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
9
I: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3888
Polymers31,3501
Non-polymers1,0377
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
10
J: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,2114
Polymers31,3501
Non-polymers8613
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
11
K: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3758
Polymers31,3501
Non-polymers1,0257
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
12
L: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,4719
Polymers31,3501
Non-polymers1,1208
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
13
A: Aminoglycoside 3'-phosphotransferase AphA1-IAB
B: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,66914
Polymers62,7012
Non-polymers1,96812
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7210 Å2
ΔGint-50 kcal/mol
Surface area23660 Å2
MethodPISA
14
C: Aminoglycoside 3'-phosphotransferase AphA1-IAB
D: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,98917
Polymers62,7012
Non-polymers2,28815
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9270 Å2
ΔGint-41 kcal/mol
Surface area24110 Å2
MethodPISA
15
E: Aminoglycoside 3'-phosphotransferase AphA1-IAB
F: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,78716
Polymers62,7012
Non-polymers2,08614
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7970 Å2
ΔGint-44 kcal/mol
Surface area24120 Å2
MethodPISA
16
G: Aminoglycoside 3'-phosphotransferase AphA1-IAB
H: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,77515
Polymers62,7012
Non-polymers2,07413
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7230 Å2
ΔGint-54 kcal/mol
Surface area23530 Å2
MethodPISA
17
I: Aminoglycoside 3'-phosphotransferase AphA1-IAB
J: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,59912
Polymers62,7012
Non-polymers1,89810
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7710 Å2
ΔGint-43 kcal/mol
Surface area23850 Å2
MethodPISA
18
K: Aminoglycoside 3'-phosphotransferase AphA1-IAB
L: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,84617
Polymers62,7012
Non-polymers2,14515
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7430 Å2
ΔGint-53 kcal/mol
Surface area23840 Å2
MethodPISA
Unit cell
Length a, b, c (Å)97.185, 97.298, 112.738
Angle α, β, γ (deg.)102.97, 106.21, 112.66
Int Tables number1
Space group name H-MP1

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Components

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Protein , 1 types, 12 molecules ABCDEFGHIJKL

#1: Protein
Aminoglycoside 3'-phosphotransferase AphA1-IAB


Mass: 31350.404 Da / Num. of mol.: 12
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Acinetobacter baumannii (bacteria) / Strain: AYE / Gene: ABAYE3578, APHA1-IAB / Plasmid: P15TV LIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: B0VD92, kanamycin kinase

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Non-polymers , 7 types, 2949 molecules

#2: Chemical
ChemComp-KAN / KANAMYCIN A


Mass: 484.499 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C18H36N4O11 / Comment: antibiotic*YM
#3: Chemical
ChemComp-0J9 / 1-tert-butyl-3-(naphthalen-1-yl)-1H-pyrazolo[3,4-d]pyrimidin-4-amine


Mass: 317.388 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C19H19N5
#4: Chemical
ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 14 / Source method: obtained synthetically / Formula: Na
#5: Chemical...
ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 36 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#7: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C4H10O3
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2870 / 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: 2.33 Å3/Da / Density % sol: 47.17 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 0.1 M SODIUM ACETATE pH 4.5, 7% PEG3350, 3% DMSO, 2 MM KANAMYCIN, 3 mM 1-NA-PP1, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97856 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Apr 21, 2012
RadiationMonochromator: DIAMOND(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97856 Å / Relative weight: 1
ReflectionResolution: 1.86→80.87 Å / Num. obs: 275562 / % possible obs: 97.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -2 / Redundancy: 3.9 % / Rmerge(I) obs: 0.061 / Net I/σ(I): 11.1
Reflection shellResolution: 1.86→1.96 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.401 / Mean I/σ(I) obs: 2.8 / % possible all: 96.5

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Processing

Software
NameVersionClassification
HKL-3000data collection
PHENIXmodel building
PHENIX(phenix.refine: 1.8_1069)refinement
XDSdata reduction
SCALAdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4EJ7

4ej7


Resolution: 1.863→54.779 Å / SU ML: 0.19 / σ(F): 1.96 / Phase error: 23.78 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2159 13290 5.06 %
Rwork0.1639 --
obs0.1665 262197 94.6 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.863→54.779 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25478 0 865 2870 29213
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00827382
X-RAY DIFFRACTIONf_angle_d1.17337201
X-RAY DIFFRACTIONf_dihedral_angle_d13.4710115
X-RAY DIFFRACTIONf_chiral_restr0.0774030
X-RAY DIFFRACTIONf_plane_restr0.0054827
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8631-1.88430.28919070.257917014X-RAY DIFFRACTION95
1.8843-1.90640.29419100.247517171X-RAY DIFFRACTION95
1.9064-1.92970.28569580.245416884X-RAY DIFFRACTION95
1.9297-1.95410.27769740.225117102X-RAY DIFFRACTION95
1.9541-1.97980.27098980.219217273X-RAY DIFFRACTION96
1.9798-2.0070.25498830.209216940X-RAY DIFFRACTION95
2.007-2.03560.25869170.205417172X-RAY DIFFRACTION96
2.0356-2.0660.25799970.197717142X-RAY DIFFRACTION96
2.066-2.09830.24739650.190716889X-RAY DIFFRACTION95
2.0983-2.13270.24299680.182217156X-RAY DIFFRACTION96
2.1327-2.16950.22729310.179717218X-RAY DIFFRACTION96
2.1695-2.20890.23919620.177117161X-RAY DIFFRACTION96
2.2089-2.25140.23639280.176417038X-RAY DIFFRACTION95
2.2514-2.29740.2339250.177517097X-RAY DIFFRACTION95
2.2974-2.34730.23399330.174717193X-RAY DIFFRACTION96
2.3473-2.40190.2199860.160617061X-RAY DIFFRACTION96
2.4019-2.4620.21939260.161717017X-RAY DIFFRACTION95
2.462-2.52860.2279230.161517139X-RAY DIFFRACTION96
2.5286-2.6030.23089090.165517138X-RAY DIFFRACTION95
2.603-2.6870.22267960.160917193X-RAY DIFFRACTION95
2.687-2.7830.25918710.169816947X-RAY DIFFRACTION95
2.783-2.89440.23168790.165416924X-RAY DIFFRACTION94
2.8944-3.02620.22288560.165816902X-RAY DIFFRACTION94
3.0262-3.18570.22567820.165216722X-RAY DIFFRACTION93
3.1857-3.38530.20038760.147516734X-RAY DIFFRACTION93
3.3853-3.64660.19028330.145416662X-RAY DIFFRACTION92
3.6466-4.01350.16618760.125916730X-RAY DIFFRACTION93
4.0135-4.5940.15198450.119516774X-RAY DIFFRACTION93
4.594-5.78690.1839190.14216858X-RAY DIFFRACTION94
5.7869-54.8030.20098120.171216087X-RAY DIFFRACTION89
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)
13.44811.0762-0.30315.270.79050.4277-0.08410.2978-0.104-0.29140.01310.1279-0.0319-0.03650.09740.27060.0103-0.02610.30040.04640.178574.730251.6367-39.0333
22.141-0.7101-0.5211.25360.07861.1926-0.0961-0.1957-0.07670.1145-0.0008-0.14080.03580.15120.10270.2809-0.008-0.0290.28390.03960.297887.787654.2819-19.3391
33.2686-0.949-1.34943.39711.32942.00230.13730.47950.0603-0.5808-0.19930.5843-0.2254-0.2856-0.00660.3311-0.0079-0.10970.31710.01260.325462.516162.5543-39.5162
42.56-0.8530.11711.6284-0.36550.803-0.0306-0.1330.13320.13410.0277-0.0842-0.1017-0.03-0.00180.29450.016-0.00690.2394-0.0270.231966.056885.1398-24.7506
52.1077-0.7579-0.34262.5268-0.32962.2907-0.01220.53-0.2841-0.5761-0.03410.2740.3992-0.2686-0.01230.3961-0.0815-0.03320.3331-0.05310.257462.35983.5865-35.9997
61.3644-0.69140.28661.7372-0.11640.883-0.0584-0.00980.2017-0.00270.0377-0.1245-0.0018-0.0070.02230.2076-0.01090.03130.2141-0.02080.225770.777323.6389-21.3278
73.0826-1.22180.45062.5266-0.1143.2769-0.12370.4587-0.4903-0.41580.05060.32560.6272-0.10160.06840.5472-0.12870.07320.3535-0.0740.330763.3864-8.6696-29.7246
83.29830.5026-0.89642.4423-0.80691.3093-0.0274-0.1554-0.21410.1206-0.014-0.02580.08190.01280.04320.3454-0.03830.03310.26030.00920.217859.8057-7.7573-2.6432
93.50520.6283-0.61043.00570.37560.6886-0.09240.5294-0.084-0.44250.07150.2070.0354-0.16230.04740.3246-0.0162-0.05190.33490.03820.184560.207627.2144-90.9389
102.5547-0.3997-0.58241.09970.12391.3119-0.0331-0.2340.01310.06860.0248-0.13620.01230.11490.01470.26780.0039-0.02670.26550.00260.257274.155629.1132-70.1253
113.616-0.3882-1.66653.27450.76022.38990.08580.59760.2098-0.46270.03580.5977-0.1205-0.4678-0.12890.3102-0.0392-0.10630.37470.06630.345848.729437.4859-90.3574
122.39-0.55430.05621.8546-0.39220.9628-0.0062-0.11150.07330.09360.0144-0.0497-0.0458-0.0229-0.01030.26160.0154-0.00270.2312-0.0150.245852.207759.9041-74.9332
132.31760.50750.90582.2065-0.31641.3675-0.02080.8767-0.1931-0.43890.0009-0.46770.07720.51620.0360.35490.06230.06850.61640.0260.340115.004710.1627-76.2737
142.22280.4413-0.71651.5414-0.68611.4961-0.0019-0.10880.15980.11170.05490.1061-0.0638-0.0002-0.06070.23190.01160.01350.2843-0.02070.245735.044215.1537-57.7089
155.48520.00882.36292.3628-0.98932.6354-0.07510.3594-0.0756-0.19430.11490.00110.08470.1932-0.04020.23070.01740.02680.2743-0.0370.20940.58375.8591-69.7626
163.1610.4221-0.35842.374-0.43871.8543-0.00850.1890.46090.08190.0230.1743-0.1712-0.1623-0.01210.21550.05160.00660.26330.01840.2758-1.614414.2141-47.612
171.6119-0.28940.22821.8556-0.50192.5451-0.14030.3855-0.3615-0.27850.12050.22450.4109-0.1675-0.00690.2788-0.10450.00630.3262-0.08470.333676.817427.538914.296
181.7895-0.48260.21232.0831-0.39170.8938-0.09310.01850.1699-0.05870.0569-0.0786-0.0134-0.02410.03760.2396-0.01810.00370.2643-0.02720.245885.172547.632728.7765
191.9016-1.0666-0.00061.6896-0.39234.1857-0.16570.2564-0.581-0.22370.04180.27490.8604-0.23280.08830.4774-0.10880.11390.3549-0.12980.509477.781515.888121.2615
203.31751.0586-1.21443.0087-1.14722.9084-0.1857-0.3864-0.51470.1789-0.0224-0.14040.46790.14090.15890.40950.01750.07690.33490.06550.329373.542916.899548.2071
212.79651.02910.72422.2078-0.23251.753-0.13810.9129-0.3048-0.4140.1709-0.37110.04620.490.00210.33520.00450.03280.5572-0.03820.284929.005335.2741-25.5964
222.25990.29-0.79491.5349-0.56491.32280.0234-0.14290.02240.0256-0.015-0.0967-0.03560.0752-0.01010.1923-0.01480.00450.2466-0.02560.201248.825140.0183-6.972
236.24840.24962.39312.1181-1.19923.3064-0.03540.5042-0.0168-0.25740.1220.06530.08240.0853-0.09080.2240.00740.02690.263-0.04180.212614.140531.1666-19.1641
242.8110.7955-0.60241.6501-0.27051.57140.02390.11070.28820.05010.02540.2235-0.1207-0.1124-0.04760.19940.018-0.00080.21810.01230.240812.10638.78243.2797
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A and resi 0:102
2X-RAY DIFFRACTION2chain A and resi 103:271
3X-RAY DIFFRACTION3chain B and resi 0:102
4X-RAY DIFFRACTION4chain B and resi 103:271
5X-RAY DIFFRACTION5chain C and resi 0:102
6X-RAY DIFFRACTION6chain C and resi 103:271
7X-RAY DIFFRACTION7chain D and resi 0:102
8X-RAY DIFFRACTION8chain D and resi 103:271
9X-RAY DIFFRACTION9chain E and resi 0:102
10X-RAY DIFFRACTION10chain E and resi 103:271
11X-RAY DIFFRACTION11chain F and resi 0:102
12X-RAY DIFFRACTION12chain F and resi 103:271
13X-RAY DIFFRACTION13chain G and resi 0:102
14X-RAY DIFFRACTION14chain G and resi 103:271
15X-RAY DIFFRACTION15chain H and resi 0:102
16X-RAY DIFFRACTION16chain H and resi 103:271
17X-RAY DIFFRACTION17chain I and resi 0:102
18X-RAY DIFFRACTION18chain I and resi 103:271
19X-RAY DIFFRACTION19chain J and resi 0:102
20X-RAY DIFFRACTION20chain J and resi 103:271
21X-RAY DIFFRACTION21chain K and resi 0:102
22X-RAY DIFFRACTION22chain K and resi 103:271
23X-RAY DIFFRACTION23chain L and resi 0:102
24X-RAY DIFFRACTION24chain L and resi 103:271

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