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

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Basic information

Entry
Database: PDB / ID: 4gki
TitleCrystal structure of the aminoglycoside phosphotransferase APH(3')-Ia, with substrate kanamycin and small molecule inhibitor 1-NM-PP1
ComponentsAminoglycoside 3'-phosphotransferase AphA1-IAB
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / PYRAZOLOPYRIMIDINE / 1-NM-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 3'-phosphotransferase; Chain: A, domain 2 / Aminoglycoside phosphotransferase (APH), C-terminal lobe / Aminoglycoside phosphotransferase / Phosphotransferase enzyme family / 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-0JN / ACETATE ION / KANAMYCIN A / DI(HYDROXYETHYL)ETHER / Aminoglycoside 3'-phosphotransferase
Similarity search - Component
Biological speciesAcinetobacter baumannii (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.88 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

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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)388,64385
Polymers376,20512
Non-polymers12,43873
Water59,5943308
1
A: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,53110
Polymers31,3501
Non-polymers1,1819
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3315
Polymers31,3501
Non-polymers9814
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,4489
Polymers31,3501
Non-polymers1,0988
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3076
Polymers31,3501
Non-polymers9575
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,4859
Polymers31,3501
Non-polymers1,1348
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,2485
Polymers31,3501
Non-polymers8984
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3307
Polymers31,3501
Non-polymers9806
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
H: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3667
Polymers31,3501
Non-polymers1,0166
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
9
I: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3315
Polymers31,3501
Non-polymers9814
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
10
J: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,64910
Polymers31,3501
Non-polymers1,2989
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
11
K: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,2485
Polymers31,3501
Non-polymers8984
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
12
L: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,3667
Polymers31,3501
Non-polymers1,0166
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)64,86215
Polymers62,7012
Non-polymers2,16213
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7570 Å2
ΔGint-38 kcal/mol
Surface area23560 Å2
MethodPISA
14
C: Aminoglycoside 3'-phosphotransferase AphA1-IAB
D: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,75615
Polymers62,7012
Non-polymers2,05513
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7400 Å2
ΔGint-50 kcal/mol
Surface area23910 Å2
MethodPISA
15
E: Aminoglycoside 3'-phosphotransferase AphA1-IAB
F: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,73314
Polymers62,7012
Non-polymers2,03212
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7360 Å2
ΔGint-37 kcal/mol
Surface area23910 Å2
MethodPISA
16
G: Aminoglycoside 3'-phosphotransferase AphA1-IAB
H: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,69714
Polymers62,7012
Non-polymers1,99612
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7040 Å2
ΔGint-46 kcal/mol
Surface area23700 Å2
MethodPISA
17
I: Aminoglycoside 3'-phosphotransferase AphA1-IAB
J: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,98015
Polymers62,7012
Non-polymers2,27913
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7390 Å2
ΔGint-25 kcal/mol
Surface area23530 Å2
MethodPISA
18
K: Aminoglycoside 3'-phosphotransferase AphA1-IAB
L: Aminoglycoside 3'-phosphotransferase AphA1-IAB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,61512
Polymers62,7012
Non-polymers1,91410
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7480 Å2
ΔGint-36 kcal/mol
Surface area23620 Å2
MethodPISA
Unit cell
Length a, b, c (Å)96.843, 97.103, 112.128
Angle α, β, γ (deg.)103.24, 106.18, 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, 3381 molecules

#2: Chemical
ChemComp-KAN / KANAMYCIN A / Kanamycin A


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


Mass: 331.414 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C20H21N5
#4: Chemical
ChemComp-NA / SODIUM ION


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


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Chemical...
ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 28 / Source method: obtained synthetically / Formula: C2H3O2
#7: Chemical
ChemComp-PEG / DI(HYDROXYETHYL)ETHER / Diethylene glycol


Mass: 106.120 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C4H10O3
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 3308 / 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: 2.3 Å3/Da / Density % sol: 46.48 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.5
Details: 0.1 M SODIUM ACETATE, 8% PEG3350, 3% DMSO, 2 MM KANAMYCIN, 3 mM 1-NM-PP1, pH 4.5, 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 22, 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: 1.88→99.63 Å / Num. obs: 265977 / % possible obs: 97.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -2 / Redundancy: 2.3 % / Rmerge(I) obs: 0.062 / Net I/σ(I): 7.6
Reflection shellResolution: 1.88→1.98 Å / Redundancy: 2.3 % / Rmerge(I) obs: 0.372 / Mean I/σ(I) obs: 2.1 / % 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: 1.88→54.384 Å / SU ML: 0.21 / σ(F): 1.96 / Phase error: 26.19 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2158 12522 5.02 %
Rwork0.1655 --
obs0.1681 248673 94.43 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.88→54.384 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms25493 0 865 3308 29666
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00827553
X-RAY DIFFRACTIONf_angle_d1.15937443
X-RAY DIFFRACTIONf_dihedral_angle_d13.24910239
X-RAY DIFFRACTIONf_chiral_restr0.0764045
X-RAY DIFFRACTIONf_plane_restr0.0054866
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.88-1.90140.33498380.285315901X-RAY DIFFRACTION92
1.9014-1.92370.31748310.272915661X-RAY DIFFRACTION92
1.9237-1.94720.30098400.263616058X-RAY DIFFRACTION92
1.9472-1.97180.30088410.25415889X-RAY DIFFRACTION92
1.9718-1.99780.2887640.242515956X-RAY DIFFRACTION93
1.9978-2.02520.2689520.217716004X-RAY DIFFRACTION93
2.0252-2.05410.27358300.217915886X-RAY DIFFRACTION93
2.0541-2.08480.26648250.205916171X-RAY DIFFRACTION93
2.0848-2.11730.26128480.200616282X-RAY DIFFRACTION93
2.1173-2.1520.24148600.190916137X-RAY DIFFRACTION94
2.152-2.18920.24898700.197416049X-RAY DIFFRACTION94
2.1892-2.2290.25298630.18416220X-RAY DIFFRACTION94
2.229-2.27180.2488370.1816189X-RAY DIFFRACTION94
2.2718-2.31820.24289200.178216361X-RAY DIFFRACTION94
2.3182-2.36860.22068520.169416438X-RAY DIFFRACTION95
2.3686-2.42370.23478270.166416432X-RAY DIFFRACTION95
2.4237-2.48430.22728720.160116417X-RAY DIFFRACTION95
2.4843-2.55150.22758730.164216405X-RAY DIFFRACTION95
2.5515-2.62660.24048810.166416521X-RAY DIFFRACTION95
2.6266-2.71140.22518600.169616383X-RAY DIFFRACTION96
2.7114-2.80830.20948860.165616530X-RAY DIFFRACTION96
2.8083-2.92070.21238490.158316545X-RAY DIFFRACTION96
2.9207-3.05360.21578810.153516532X-RAY DIFFRACTION96
3.0536-3.21460.20828590.155516549X-RAY DIFFRACTION96
3.2146-3.4160.20988970.152416529X-RAY DIFFRACTION96
3.416-3.67960.19338710.141816570X-RAY DIFFRACTION96
3.6796-4.04980.17278950.129416704X-RAY DIFFRACTION97
4.0498-4.63560.15798780.119816745X-RAY DIFFRACTION97
4.6356-5.83930.18548810.142416729X-RAY DIFFRACTION97
5.8393-54.40660.1758490.160416045X-RAY DIFFRACTION93
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)
13.4551-0.3992-1.47423.16860.64451.91520.15140.530.445-0.3706-0.00890.4851-0.0774-0.3714-0.12920.2423-0.0259-0.08640.31060.07050.239244.95912.57814.3403
21.6704-0.40340.14031.2933-0.46771.1129-0.0192-0.10560.02310.09690.0008-0.052-0.02030.00350.01930.1752-0.0005-0.00630.1403-0.02880.193348.196725.058929.3366
32.80630.8196-0.1822.43390.22510.5862-0.07970.35-0.0523-0.27760.06710.06360.0937-0.05270.02820.2385-0.0068-0.03210.22580.0280.101156.6256-8.309814.1721
42.4216-0.3898-0.51381.06510.11631.263-0.0038-0.24760.06170.033-0.0063-0.21430.00860.17150.00990.1486-0.001-0.02780.14730.00240.157270.025-5.735934.1286
51.98880.67761.23112.4702-0.19891.1758-0.13880.7389-0.2598-0.41260.1015-0.50950.0260.52450.07020.28510.04110.08850.5098-0.03950.264610.9752-24.782928.5387
62.17150.5872-0.7531.4644-0.54091.2411-0.0159-0.15820.11640.16020.0670.1333-0.0648-0.0096-0.05210.17890.03520.02640.1896-0.01730.155231.0604-19.804246.7321
74.07470.06312.1131.0563-0.5052.5503-0.08860.29020.0314-0.04170.08220.05220.05290.18190.00630.13680.01980.01760.2019-0.04180.15-3.4516-28.700434.59
82.53920.7198-0.77912.0827-0.35171.845-0.01720.13460.22440.08940.05210.1607-0.124-0.1984-0.01870.17790.08250.02010.2290.01440.1982-5.5501-20.579456.6465
91.9468-0.5437-0.35082.2859-0.3521.8650.02820.4483-0.1569-0.5718-0.05810.17110.3802-0.154-0.00020.3327-0.0316-0.02710.2456-0.03480.1658.3454-31.119967.811
101.0404-0.62910.24511.887-0.23130.9126-0.0329-0.02540.19930.02540.0416-0.13930.02240.0208-0.00960.15420.00640.02650.1658-0.00510.197666.6318-11.331782.6341
112.6895-1.11740.43661.8559-0.13282.6554-0.05860.2618-0.4703-0.3870.06110.16150.4662-0.1399-0.00210.4193-0.08110.07310.2227-0.04570.258459.1677-43.726474.6882
122.67530.7447-0.89942.4366-0.91681.3143-0.058-0.1462-0.21170.17430.0090.02630.1048-0.05110.03160.2615-0.01360.03820.18180.01810.162355.6442-42.7914101.0776
131.95541.06450.83972.6086-0.16351.3967-0.06520.8362-0.2309-0.40690.1181-0.44490.03450.4558-0.02350.24910.04230.06540.5093-0.01530.276324.84670.031478.5545
142.0010.18-0.73971.3279-0.29661.26130.0436-0.10380.06260.0156-0.0113-0.041-0.01320.0655-0.03540.1027-0.00410.00360.176-0.0110.159944.73625.073996.8092
154.84630.62012.4822.0463-0.96762.7674-0.0180.45460.153-0.23130.07440.04830.06160.0808-0.05160.15770.03410.05420.2443-0.01580.184110.1307-4.207784.4198
162.53910.3966-0.63581.1203-0.41461.73450.0550.19980.40390.05390.02410.2155-0.1332-0.1969-0.05950.11880.00870.00150.15910.02270.22818.16443.3488106.9204
173.70860.79190.01244.85981.17420.6556-0.03920.3572-0.0728-0.33690.0570.1917-0.1228-0.0484-0.00530.20170.02980.00310.21590.06830.151942.3619-32.1209-34.5782
181.8965-0.496-0.29631.36470.14641.5473-0.0939-0.1841-0.13660.11670.0394-0.14080.0570.17170.05340.14130.0212-0.00060.15950.04260.203655.3241-29.5691-15.054
192.9829-0.553-1.02352.4231.20931.54670.14780.4470.2295-0.4843-0.20230.5239-0.3239-0.27340.00810.26040.0201-0.0940.260.05150.29930.1542-20.9776-35.2318
202.5036-0.92640.24121.5439-0.1870.7243-0.0278-0.08750.08270.08490.0422-0.0708-0.0819-0.0421-0.01310.23140.04850.02480.1710.00340.189133.83551.1501-20.3247
211.6563-0.53510.54352.3117-0.22773.4689-0.16480.1112-0.4019-0.15290.08240.34770.6116-0.25340.03980.3128-0.10820.1180.2838-0.07890.3977.753421.52625.5672
222.97421.4284-1.38592.9475-1.26672.5684-0.1886-0.2488-0.42380.26310.0862-0.07220.211-0.07020.08620.2950.03270.07290.29230.05640.26663.975422.455551.8711
231.173-0.45810.23270.9441-0.75732.3012-0.16710.4046-0.2994-0.18940.13410.19870.316-0.0674-0.01280.2073-0.11860.00670.2863-0.08340.24837.381633.534218.2894
241.5238-0.40250.0012.1638-0.29020.6514-0.1052-0.00310.1096-0.0590.0887-0.0732-0.0009-0.04770.01480.1726-0.01870.00660.1888-0.03740.160315.355753.268232.7537
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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