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- PDB-6zfh: Structure of human galactokinase in complex with galactose and 2'... -

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Basic information

Entry
Database: PDB / ID: 6zfh
TitleStructure of human galactokinase in complex with galactose and 2'-(benzo[d]oxazol-2-ylamino)-7',8'-dihydro-1'H-spiro[cyclopentane-1,4'-quinazolin]-5'(6'H)-one
ComponentsGalactokinase
KeywordsTRANSFERASE / GHMP Kinase / Galactose metabolism / Inhibitor / Structural Genomics / Structural Genomics Consortium / SGC
Function / homology
Function and homology information


glycolytic process from galactose / Defective GALK1 causes GALCT2 / galactitol metabolic process / galactokinase / galactokinase activity / galactose catabolic process / Galactose catabolism / galactose catabolic process via UDP-galactose / galactose binding / galactose metabolic process ...glycolytic process from galactose / Defective GALK1 causes GALCT2 / galactitol metabolic process / galactokinase / galactokinase activity / galactose catabolic process / Galactose catabolism / galactose catabolic process via UDP-galactose / galactose binding / galactose metabolic process / extracellular exosome / ATP binding / membrane / cytosol / cytoplasm
Similarity search - Function
Galactokinase, N-terminal domain / Galactokinase, conserved site / Galactokinase galactose-binding signature / Galactokinase signature. / Galactokinase / Mevalonate/galactokinase / GHMP kinase, ATP-binding, conserved site / GHMP kinases putative ATP-binding domain. / GHMP kinase, C-terminal domain / GHMP kinases C terminal ...Galactokinase, N-terminal domain / Galactokinase, conserved site / Galactokinase galactose-binding signature / Galactokinase signature. / Galactokinase / Mevalonate/galactokinase / GHMP kinase, ATP-binding, conserved site / GHMP kinases putative ATP-binding domain. / GHMP kinase, C-terminal domain / GHMP kinases C terminal / GHMP kinase N-terminal domain / GHMP kinases N terminal domain / GHMP kinase, C-terminal domain superfamily / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold
Similarity search - Domain/homology
beta-D-galactopyranose / Chem-QV2 / Galactokinase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.439 Å
AuthorsBezerra, G.A. / Mackinnon, S. / Zhang, M. / Foster, W. / Bailey, H. / Arrowsmith, C. / Edwards, A. / Bountra, C. / Lai, K. / Yue, W.W. / Structural Genomics Consortium (SGC)
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Wellcome Trust106169/ZZ14/Z United Kingdom
CitationJournal: Acs Chem.Biol. / Year: 2021
Title: Fragment Screening Reveals Starting Points for Rational Design of Galactokinase 1 Inhibitors to Treat Classic Galactosemia.
Authors: Mackinnon, S.R. / Krojer, T. / Foster, W.R. / Diaz-Saez, L. / Tang, M. / Huber, K.V.M. / von Delft, F. / Lai, K. / Brennan, P.E. / Arruda Bezerra, G. / Yue, W.W.
History
DepositionJun 17, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 30, 2021Provider: repository / Type: Initial release
Revision 1.1Jul 28, 2021Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Galactokinase
B: Galactokinase
C: Galactokinase
D: Galactokinase
E: Galactokinase
F: Galactokinase
G: Galactokinase
H: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)348,62023
Polymers344,8248
Non-polymers3,79615
Water5,981332
1
A: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,6203
Polymers43,1031
Non-polymers5172
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,6203
Polymers43,1031
Non-polymers5172
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,6203
Polymers43,1031
Non-polymers5172
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,6203
Polymers43,1031
Non-polymers5172
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,6203
Polymers43,1031
Non-polymers5172
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,6203
Polymers43,1031
Non-polymers5172
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
G: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,6203
Polymers43,1031
Non-polymers5172
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
8
H: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,2832
Polymers43,1031
Non-polymers1801
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)119.872, 97.204, 144.812
Angle α, β, γ (deg.)90.000, 98.510, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 7 or (resid 8 and (name...
21(chain B and (resid 7 or (resid 8 and (name...
31(chain C and (resid 7 or (resid 8 and (name...
41(chain D and (resid 7 or (resid 8 and (name...
51(chain E and (resid 7 or (resid 8 and (name...
61(chain F and (resid 7 through 22 or (resid 23...
71(chain G and (resid 7 through 14 or (resid 15...
81(chain H and (resid 7 or (resid 8 and (name...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 7 or (resid 8 and (name...A7
121(chain A and (resid 7 or (resid 8 and (name...A8
131(chain A and (resid 7 or (resid 8 and (name...A3 - 393
141(chain A and (resid 7 or (resid 8 and (name...A3 - 393
151(chain A and (resid 7 or (resid 8 and (name...A3 - 393
161(chain A and (resid 7 or (resid 8 and (name...A3 - 393
211(chain B and (resid 7 or (resid 8 and (name...B7
221(chain B and (resid 7 or (resid 8 and (name...B8
231(chain B and (resid 7 or (resid 8 and (name...B4 - 393
241(chain B and (resid 7 or (resid 8 and (name...B4 - 393
251(chain B and (resid 7 or (resid 8 and (name...B4 - 393
261(chain B and (resid 7 or (resid 8 and (name...B4 - 393
311(chain C and (resid 7 or (resid 8 and (name...C7
321(chain C and (resid 7 or (resid 8 and (name...C8
331(chain C and (resid 7 or (resid 8 and (name...C1 - 393
341(chain C and (resid 7 or (resid 8 and (name...C1 - 393
351(chain C and (resid 7 or (resid 8 and (name...C1 - 393
361(chain C and (resid 7 or (resid 8 and (name...C1 - 393
411(chain D and (resid 7 or (resid 8 and (name...D7
421(chain D and (resid 7 or (resid 8 and (name...D8
431(chain D and (resid 7 or (resid 8 and (name...D4 - 393
441(chain D and (resid 7 or (resid 8 and (name...D4 - 393
451(chain D and (resid 7 or (resid 8 and (name...D4 - 393
461(chain D and (resid 7 or (resid 8 and (name...D4 - 393
511(chain E and (resid 7 or (resid 8 and (name...E7
521(chain E and (resid 7 or (resid 8 and (name...E8
531(chain E and (resid 7 or (resid 8 and (name...E3 - 393
541(chain E and (resid 7 or (resid 8 and (name...E3 - 393
551(chain E and (resid 7 or (resid 8 and (name...E3 - 393
561(chain E and (resid 7 or (resid 8 and (name...E3 - 393
611(chain F and (resid 7 through 22 or (resid 23...F7 - 22
621(chain F and (resid 7 through 22 or (resid 23...F23 - 24
631(chain F and (resid 7 through 22 or (resid 23...F3 - 393
641(chain F and (resid 7 through 22 or (resid 23...F3 - 393
651(chain F and (resid 7 through 22 or (resid 23...F3 - 393
661(chain F and (resid 7 through 22 or (resid 23...F3 - 393
711(chain G and (resid 7 through 14 or (resid 15...G7 - 14
721(chain G and (resid 7 through 14 or (resid 15...G15 - 19
731(chain G and (resid 7 through 14 or (resid 15...G6 - 393
741(chain G and (resid 7 through 14 or (resid 15...G6 - 393
751(chain G and (resid 7 through 14 or (resid 15...G6 - 393
761(chain G and (resid 7 through 14 or (resid 15...G6 - 393
811(chain H and (resid 7 or (resid 8 and (name...H7
821(chain H and (resid 7 or (resid 8 and (name...H8
831(chain H and (resid 7 or (resid 8 and (name...H7 - 393
841(chain H and (resid 7 or (resid 8 and (name...H7 - 393
851(chain H and (resid 7 or (resid 8 and (name...H7 - 393
861(chain H and (resid 7 or (resid 8 and (name...H7 - 393

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Components

#1: Protein
Galactokinase / / Galactose kinase


Mass: 43102.977 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: GALK1, GALK / Production host: Escherichia coli (E. coli) / References: UniProt: P51570, galactokinase
#2: Sugar
ChemComp-GAL / beta-D-galactopyranose / beta-D-galactose / D-galactose / galactose / Galactose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DGalpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-galactopyranoseCOMMON NAMEGMML 1.0
b-D-GalpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GalSNFG CARBOHYDRATE SYMBOLGMML 1.0
#3: Chemical
ChemComp-QV2 / 2-(1,3-benzoxazol-2-ylamino)spiro[1,6,7,8-tetrahydroquinazoline-4,1'-cyclopentane]-5-one


Mass: 336.388 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C19H20N4O2
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 332 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 2.42 Å3/Da / Density % sol: 49.17 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: Morpheus condition: Buffer system 1: 0.1 M pH 6.5, Imidazole; MES monohydrate (acid) Amino acids: 0.02M L-Na-Glutamate; 0.02M Alanine (racemic); 0.02M Glycine; 0.02M Lysine HCl (racemic); 0. ...Details: Morpheus condition: Buffer system 1: 0.1 M pH 6.5, Imidazole; MES monohydrate (acid) Amino acids: 0.02M L-Na-Glutamate; 0.02M Alanine (racemic); 0.02M Glycine; 0.02M Lysine HCl (racemic); 0.02M Serine (racemic) Precipitant Mix 1: 20% v/v PEG 500 MME; 10 % w/v PEG 20000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 30, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 2.439→98.79 Å / Num. obs: 121943 / % possible obs: 99.3 % / Redundancy: 6.6 % / Biso Wilson estimate: 41.59 Å2 / Rpim(I) all: 0.126 / Rrim(I) all: 0.325 / Net I/σ(I): 6
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all% possible all
2.44-2.486.713958959331.3753.56196.9
6.62-98.876.416.24028663350.0290.073100

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Processing

Software
NameVersionClassification
xia2data scaling
PHENIX1.13_2998refinement
PDB_EXTRACT3.24data extraction
Aimlessdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1WUU

1wuu


Resolution: 2.439→98.787 Å / SU ML: 0.37 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 30.03 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2619 5980 4.92 %
Rwork0.2097 115647 -
obs0.2122 121627 99.06 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 140.95 Å2 / Biso mean: 58.6014 Å2 / Biso min: 18.36 Å2
Refinement stepCycle: final / Resolution: 2.439→98.787 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22210 0 271 332 22813
Biso mean--60.1 45.11 -
Num. residues----3074
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A9016X-RAY DIFFRACTION5.013TORSIONAL
12B9016X-RAY DIFFRACTION5.013TORSIONAL
13C9016X-RAY DIFFRACTION5.013TORSIONAL
14D9016X-RAY DIFFRACTION5.013TORSIONAL
15E9016X-RAY DIFFRACTION5.013TORSIONAL
16F9016X-RAY DIFFRACTION5.013TORSIONAL
17G9016X-RAY DIFFRACTION5.013TORSIONAL
18H9016X-RAY DIFFRACTION5.013TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.44-2.46630.39612110.3486365595
2.4663-2.49540.36142070.3271384898
2.4954-2.52580.34462020.3103377698
2.5258-2.55780.33132030.3093383299
2.5578-2.59140.38761920.3029378998
2.5914-2.62690.36661880.3042385999
2.6269-2.66450.32521940.2965380598
2.6645-2.70420.33532050.2921380899
2.7042-2.74650.35661850.2779381599
2.7465-2.79150.30851990.2731387699
2.7915-2.83970.33922020.2687382899
2.8397-2.89130.33511810.2572382799
2.8913-2.94690.29222010.2587387899
2.9469-3.00710.2961920.2494385399
3.0071-3.07250.28582100.2508382099
3.0725-3.14390.29712080.2443385499
3.1439-3.22260.27382080.2384385399
3.2226-3.30970.2921900.2293382099
3.3097-3.40710.31882130.2221384799
3.4071-3.51710.28552050.2077387299
3.5171-3.64280.251910.1946387299
3.6428-3.78860.23471890.1887389799
3.7886-3.96110.24282070.18943860100
3.9611-4.16990.2131920.16363901100
4.1699-4.43120.19661820.15773918100
4.4312-4.77330.21341800.14623914100
4.7733-5.25360.19381880.15923917100
5.2536-6.01380.23172060.18513949100
6.0138-7.57630.22962110.1873927100
7.5763-98.780.21632380.1705397799
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)
15.67625.999-0.5627.5418-0.52362.16380.16910.14750.828-0.2211-0.14580.8526-0.0624-0.39180.06960.19730.0946-0.04830.470.0160.4138-29.525811.4739-31.6642
25.90310.30130.83530.9585-0.23571.41820.00910.4995-0.532-0.25020.03360.24670.06-0.1189-0.04910.27560.0354-0.07150.4879-0.01810.3034-20.8576-0.7813-38.5659
36.60370.70630.52763.75980.06851.70410.1982-0.1448-0.8979-0.0647-0.02480.12480.32050.0395-0.17840.20440.0257-0.04670.5466-0.03370.3076-19.1836-4.4916-34.6582
47.76940.29990.18594.5371.55572.27010.0496-0.2394-0.43330.1276-0.0833-0.23110.32350.11310.0710.2538-0.0346-0.03750.36920.10050.266-4.9267-0.1912-29.1496
52.0205-2.3144-0.57815.9785-0.73950.78630.33190.5513-0.1801-0.6634-0.27920.18480.22030.2952-0.03340.23960.0377-0.02060.7632-0.02060.2148-1.22486.5725-41.296
61.7161-1.7253-0.33293.42192.05322.30030.62280.0309-0.6427-0.81-0.1501-0.59150.38880.9523-0.43010.43080.22020.0611.1939-0.00310.448615.9646-6.0001-41.6997
71.4-0.93950.19383.25430.2521.0750.26190.43790.1628-0.3704-0.3428-0.2967-0.07850.30410.04150.2669-0.00720.03610.6730.1830.29926.153611.9176-38.0746
84.56922.0852-0.66338.1313-0.15883.7321-0.0027-0.26510.8827-0.0939-0.17220.2878-0.36460.2380.16950.16460.0061-0.01030.44240.07240.3279-3.656125.7629-34.4383
93.83293.8583-0.60246.6727-1.80891.13950.1075-0.21360.6182-0.0116-0.20670.65380.0190.10850.02280.24720.1164-0.04150.4519-0.00940.3435-13.872114.6636-32.3727
106.85570.85831.83121.578-0.02122.26720.00560.16480.1777-0.0789-0.03170.310.0782-0.24570.01330.2111-0.0258-0.00780.44550.01820.2978-55.8459-46.7278-20.4157
112.9734-0.3704-0.13711.61380.06581.8245-0.08570.44050.3857-0.2679-0.0482-0.039-0.12580.19050.10940.2382-0.0609-0.04980.45190.09270.3809-33.4534-36.8292-19.9843
124.9817-0.56620.70281.6922-0.06621.8155-0.1548-0.36560.18990.09750.05290.0691-0.1246-0.34520.0730.24180.0251-0.00620.29770.01920.2597-17.41350.1006-4.2899
133.72050.65551.02552.64210.91851.87210.1823-0.2733-0.4650.186-0.0331-0.16550.27250.0971-0.12890.21290.0248-0.00760.25730.08040.31714.8772-12.3612-1.3818
143.4215-3.21990.288.0859-2.50994.11870.1315-0.2782-0.404-0.1796-0.38460.18950.3987-0.39620.01370.1379-0.26460.04190.38320.11760.2674-14.2878-15.2845-7.2856
155.5283-0.3910.4831.1881-0.04310.99310.0595-0.72810.36250.18330.04570.22970.0109-0.3456-0.07860.2909-0.04530.01380.659-0.02690.3859-52.1803-48.415412.2718
165.0150.20562.16762.21441.36933.70110.2758-0.7763-0.13010.13230.0244-0.19360.4166-0.0518-0.24690.2833-0.0352-0.05360.31790.00940.3399-26.9381-56.745213.7358
172.9796-1.7289-0.42744.013-0.52391.27670.2936-0.4424-0.78960.0426-0.09640.44780.5088-0.1808-0.21950.4512-0.2119-0.14590.47150.14370.4993-39.8552-68.501410.5881
184.4186-0.37360.37391.01150.35612.2181-0.20070.36580.8507-0.00690.1762-0.1024-0.38140.38660.0590.2933-0.0535-0.06720.43210.0970.397928.0545-41.704-40.6775
195.99131.14931.73723.3993-0.40343.8997-0.0607-0.09190.04160.21860.2194-0.42590.16490.1098-0.04910.237-0.0266-0.08210.5017-0.01680.357438.9461-50.7058-30.7014
204.21630.84711.49821.76350.72521.6401-0.0450.5061-0.0396-0.10080.088-0.0426-0.02120.2584-0.08950.2478-0.0326-0.03420.45540.06050.286325.6617-51.5199-40.0893
214.36241.17090.79774.7286-0.52662.5382-0.0302-0.25980.40660.14060.17790.3612-0.033-0.357-0.05920.26190.0283-0.06780.388-0.02110.255312.014-44.4088-31.4707
223.37331.6236-0.00884.1104-0.62142.9169-0.0634-0.05190.72740.33280.10290.2463-0.4977-0.422-0.08880.28620.1142-0.04430.3698-0.00120.4364.3718-39.6973-34.7198
234.5657-3.6205-1.43748.19313.48685.7167-0.46550.2350.6875-0.25970.0344-0.3365-0.9870.22040.11080.4424-0.2418-0.16030.440.25580.590123.7117-33.9955-41.0173
241.19490.64560.75180.63650.01880.79040.184-0.4882-0.47470.05640.15690.50830.008-0.7168-0.18990.33880.0861-0.12710.89120.12080.8132-43.5617-55.9141-60.1947
257.2284-1.36170.8673.2598-0.48412.84380.1502-0.7076-0.24150.77780.05411.115-0.5976-0.8662-0.07110.45280.20010.06120.84410.04250.7147-45.8755-46.1277-53.8013
263.017-0.5370.03212.2052-0.25352.42170.0410.15690.3963-0.0471-0.04630.3632-0.2836-0.35450.01180.31910.0928-0.09460.6150.04010.5943-36.2117-49.0158-61.6245
273.04711.66541.54553.36480.90943.08480.2011-0.0038-0.38970.0221-0.0278-0.24170.08470.1857-0.14240.20780.0277-0.02670.4980.11640.4137-17.4396-61.1315-55.4214
280.42380.36860.06341.16390.48181.6719-0.1042-0.03470.22170.2437-0.11760.45840.4167-0.20910.05410.3409-0.1461-0.06580.86270.17710.6385-32.4013-71.3174-54.8334
294.58040.20721.43820.82920.10391.2207-0.39950.40870.07230.08330.2896-0.1145-0.1051-0.38830.09350.3730.0271-0.14380.9692-0.21820.4773-55.5685-3.6247-53.0892
303.3010.8289-0.34462.6538-0.99710.8467-0.2455-0.5911-0.05880.18110.0724-0.13550.20530.26870.21160.45590.27980.01830.9251-0.08270.3513-79.9713-4.9357-46.9407
312.26190.70330.25261.9009-0.42091.0504-0.26180.15230.8390.36110.38140.3583-0.5356-0.5070.0070.46160.2162-0.20871.137-0.11110.6791-77.12687.8837-52.2433
322.8319-1.7207-1.04832.47860.16181.2173-0.3849-0.7386-0.02850.71920.31410.5906-0.2217-0.774-0.06780.56250.18240.13331.5789-0.03210.5915-10.0202-2.1715-72.638
332.6516-1.9527-1.23894.47541.55351.81180.2541-0.9390.5260.69040.25540.1233-0.6447-0.4726-0.30240.5690.26920.18521.46-0.16550.5183-6.71882.8796-74.6854
342.2236-1.2457-0.77613.0875-1.89582.47790.1175-1.09140.02120.6504-0.11890.2911-0.3593-0.863-0.23660.4629-0.0307-0.02971.1267-0.00980.37087.6315-8.2543-76.9117
352.69350.36114.6072.78150.99257.87370.0517-1.06360.03440.2495-0.2278-0.53380.27910.38430.1950.3165-0.0359-0.00811.15150.00470.458123.8912-10.3473-72.6865
362.5944-0.86840.19873.8585-0.2293.90750.2119-1.0649-0.96910.3873-0.19630.47680.8762-0.5651-0.05340.5184-0.23980.00091.04140.21140.64445.4456-22.9978-76.4061
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 24 )A3 - 24
2X-RAY DIFFRACTION2chain 'A' and (resid 25 through 116 )A25 - 116
3X-RAY DIFFRACTION3chain 'A' and (resid 117 through 178 )A117 - 178
4X-RAY DIFFRACTION4chain 'A' and (resid 179 through 212 )A179 - 212
5X-RAY DIFFRACTION5chain 'A' and (resid 213 through 249 )A213 - 249
6X-RAY DIFFRACTION6chain 'A' and (resid 250 through 271 )A250 - 271
7X-RAY DIFFRACTION7chain 'A' and (resid 272 through 350 )A272 - 350
8X-RAY DIFFRACTION8chain 'A' and (resid 351 through 370 )A351 - 370
9X-RAY DIFFRACTION9chain 'A' and (resid 371 through 392 )A371 - 392
10X-RAY DIFFRACTION10chain 'B' and (resid 4 through 177 )B4 - 177
11X-RAY DIFFRACTION11chain 'B' and (resid 178 through 392 )B178 - 392
12X-RAY DIFFRACTION12chain 'C' and (resid 1 through 212 )C1 - 212
13X-RAY DIFFRACTION13chain 'C' and (resid 213 through 370 )C213 - 370
14X-RAY DIFFRACTION14chain 'C' and (resid 371 through 392 )C371 - 392
15X-RAY DIFFRACTION15chain 'D' and (resid 4 through 212 )D4 - 212
16X-RAY DIFFRACTION16chain 'D' and (resid 213 through 316 )D213 - 316
17X-RAY DIFFRACTION17chain 'D' and (resid 317 through 392 )D317 - 392
18X-RAY DIFFRACTION18chain 'E' and (resid 3 through 59 )E3 - 59
19X-RAY DIFFRACTION19chain 'E' and (resid 60 through 116 )E60 - 116
20X-RAY DIFFRACTION20chain 'E' and (resid 117 through 212 )E117 - 212
21X-RAY DIFFRACTION21chain 'E' and (resid 213 through 249 )E213 - 249
22X-RAY DIFFRACTION22chain 'E' and (resid 250 through 370 )E250 - 370
23X-RAY DIFFRACTION23chain 'E' and (resid 371 through 392 )E371 - 392
24X-RAY DIFFRACTION24chain 'F' and (resid 3 through 50 )F3 - 50
25X-RAY DIFFRACTION25chain 'F' and (resid 51 through 116 )F51 - 116
26X-RAY DIFFRACTION26chain 'F' and (resid 117 through 212 )F117 - 212
27X-RAY DIFFRACTION27chain 'F' and (resid 213 through 316 )F213 - 316
28X-RAY DIFFRACTION28chain 'F' and (resid 317 through 392 )F317 - 392
29X-RAY DIFFRACTION29chain 'G' and (resid 6 through 212 )G6 - 212
30X-RAY DIFFRACTION30chain 'G' and (resid 213 through 271 )G213 - 271
31X-RAY DIFFRACTION31chain 'G' and (resid 272 through 392 )G272 - 392
32X-RAY DIFFRACTION32chain 'H' and (resid 7 through 116 )H7 - 116
33X-RAY DIFFRACTION33chain 'H' and (resid 117 through 178 )H117 - 178
34X-RAY DIFFRACTION34chain 'H' and (resid 179 through 249 )H179 - 249
35X-RAY DIFFRACTION35chain 'H' and (resid 250 through 296 )H250 - 296
36X-RAY DIFFRACTION36chain 'H' and (resid 297 through 391 )H297 - 391

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