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- PDB-6gr2: Structure of human galactokinase in complex with galactose and ADP -

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Basic information

Entry
Database: PDB / ID: 6gr2
TitleStructure of human galactokinase in complex with galactose and ADP
ComponentsGalactokinase
KeywordsTRANSFERASE / Leloir pathway / GHMP kinase / galactose / ADP / 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 catabolism / galactose catabolic process via UDP-galactose, Leloir pathway / galactose binding / galactose metabolic process / extracellular exosome ...glycolytic process from galactose / Defective GALK1 causes GALCT2 / galactitol metabolic process / galactokinase / galactokinase activity / Galactose catabolism / galactose catabolic process via UDP-galactose, Leloir pathway / 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, C-terminal domain / GHMP kinase N-terminal domain / GHMP kinases N terminal domain / GHMP kinase, C-terminal domain superfamily / Ribosomal Protein S5; domain 2 - #10 / Ribosomal Protein S5; domain 2 / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / beta-D-galactopyranose / Galactokinase
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.49 Å
AuthorsBezerra, G.A. / Mackinnon, S. / Williams, E. / Zhang, M. / 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: To Be Published
Title: Structure of human galactokinase in complex with galactose and ADP
Authors: Bezerra, G.A. / Mackinnon, S. / Williams, E. / Zhang, M. / Arrowsmith, C. / Edwards, A. / Bountra, C. / Lai, K. / Yue, W.W.
History
DepositionJun 8, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 19, 2019Provider: repository / Type: Initial release
Revision 1.1Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_symmetry
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.2Jan 17, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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
Revision 1.3Nov 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: Galactokinase
B: Galactokinase
C: Galactokinase
D: Galactokinase
E: Galactokinase
F: Galactokinase
G: Galactokinase
H: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)350,16329
Polymers344,8248
Non-polymers5,33921
Water1,856103
1
A: Galactokinase
F: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,5177
Polymers86,2062
Non-polymers1,3115
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3720 Å2
ΔGint-19 kcal/mol
Surface area29130 Å2
MethodPISA
2
B: Galactokinase
hetero molecules

C: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,7099
Polymers86,2062
Non-polymers1,5037
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_455x-1,y,z1
Buried area4430 Å2
ΔGint-60 kcal/mol
Surface area28800 Å2
MethodPISA
3
D: Galactokinase
G: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,4216
Polymers86,2062
Non-polymers1,2154
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3810 Å2
ΔGint-11 kcal/mol
Surface area28690 Å2
MethodPISA
4
E: Galactokinase
H: Galactokinase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,5177
Polymers86,2062
Non-polymers1,3115
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3800 Å2
ΔGint-23 kcal/mol
Surface area28930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)78.217, 110.320, 118.234
Angle α, β, γ (deg.)113.850, 102.260, 101.290
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 6 through 7 or (resid 8...
21(chain B and (resid 6 through 7 or (resid 8...
31(chain C and ((resid 6 and (name N or name...
41(chain D and (resid 6 through 7 or (resid 8...
51(chain E and ((resid 6 and (name N or name...
61(chain F and ((resid 6 and (name N or name...
71(chain G and (resid 6 through 7 or (resid 8...
81(chain H and (resid 6 through 7 or (resid 8...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLNGLNPROPRO(chain A and (resid 6 through 7 or (resid 8...AA6 - 713 - 14
12GLNGLNALAALA(chain A and (resid 6 through 7 or (resid 8...AA8 - 1015 - 17
13LEULEUGALGAL(chain A and (resid 6 through 7 or (resid 8...AA - I4 - 40111
14LEULEUGALGAL(chain A and (resid 6 through 7 or (resid 8...AA - I4 - 40111
15LEULEUGALGAL(chain A and (resid 6 through 7 or (resid 8...AA - I4 - 40111
16LEULEUGALGAL(chain A and (resid 6 through 7 or (resid 8...AA - I4 - 40111
21GLNGLNPROPRO(chain B and (resid 6 through 7 or (resid 8...BB6 - 713 - 14
22GLNGLNALAALA(chain B and (resid 6 through 7 or (resid 8...BB8 - 1015 - 17
23GLNGLNGALGAL(chain B and (resid 6 through 7 or (resid 8...BB - K6 - 40113
31GLNGLNGLNGLN(chain C and ((resid 6 and (name N or name...CC613
32LEULEUGALGAL(chain C and ((resid 6 and (name N or name...CC - O4 - 40111
33LEULEUGALGAL(chain C and ((resid 6 and (name N or name...CC - O4 - 40111
34LEULEUGALGAL(chain C and ((resid 6 and (name N or name...CC - O4 - 40111
35LEULEUGALGAL(chain C and ((resid 6 and (name N or name...CC - O4 - 40111
41GLNGLNPROPRO(chain D and (resid 6 through 7 or (resid 8...DD6 - 713 - 14
42GLNGLNALAALA(chain D and (resid 6 through 7 or (resid 8...DD8 - 1015 - 17
43LEULEUGALGAL(chain D and (resid 6 through 7 or (resid 8...DD - R4 - 40111
51GLNGLNGLNGLN(chain E and ((resid 6 and (name N or name...EE613
52ARGARGGALGAL(chain E and ((resid 6 and (name N or name...EE - T5 - 40112
53ARGARGGALGAL(chain E and ((resid 6 and (name N or name...EE - T5 - 40112
54ARGARGGALGAL(chain E and ((resid 6 and (name N or name...EE - T5 - 40112
55ARGARGGALGAL(chain E and ((resid 6 and (name N or name...EE - T5 - 40112
61GLNGLNGLNGLN(chain F and ((resid 6 and (name N or name...FF613
62GLNGLNGALGAL(chain F and ((resid 6 and (name N or name...FF - V6 - 40113
63GLNGLNGALGAL(chain F and ((resid 6 and (name N or name...FF - V6 - 40113
64GLNGLNGALGAL(chain F and ((resid 6 and (name N or name...FF - V6 - 40113
65GLNGLNGALGAL(chain F and ((resid 6 and (name N or name...FF - V6 - 40113
71GLNGLNPROPRO(chain G and (resid 6 through 7 or (resid 8...GG6 - 713 - 14
72GLNGLNALAALA(chain G and (resid 6 through 7 or (resid 8...GG8 - 1015 - 17
73ARGARGGALGAL(chain G and (resid 6 through 7 or (resid 8...GG - Y5 - 40112
81GLNGLNPROPRO(chain H and (resid 6 through 7 or (resid 8...HH6 - 713 - 14
82GLNGLNALAALA(chain H and (resid 6 through 7 or (resid 8...HH8 - 1015 - 17
83GLNGLNGALGAL(chain H and (resid 6 through 7 or (resid 8...HH - AA6 - 40113
84GLNGLNGALGAL(chain H and (resid 6 through 7 or (resid 8...HH - AA6 - 40113
85GLNGLNGALGAL(chain H and (resid 6 through 7 or (resid 8...HH - AA6 - 40113
86GLNGLNGALGAL(chain H and (resid 6 through 7 or (resid 8...HH - AA6 - 40113

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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


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-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 103 / Source method: isolated from a natural source / Formula: H2O
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: 2.51 Å3/Da / Density % sol: 50.97 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop
Details: 0.1M cacodylate pH 6.3, 17.5% PEG8K -- 0.2M ammonium sulfate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97619 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 13, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97619 Å / Relative weight: 1
ReflectionResolution: 2.49→95.76 Å / Num. obs: 114333 / % possible obs: 97.5 % / Redundancy: 2.5 % / Biso Wilson estimate: 43.67 Å2 / CC1/2: 0.949 / Rmerge(I) obs: 0.125 / Rpim(I) all: 0.093 / Rrim(I) all: 0.156 / Net I/σ(I): 4.2 / Num. measured all: 281718 / Scaling rejects: 46
Reflection shell

Diffraction-ID: 1 / Redundancy: 2.5 %

Resolution (Å)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.49-2.550.692089284250.6030.5220.871.597.3
11.14-95.760.066325312940.9650.0510.0847.999.4

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Processing

Software
NameVersionClassification
Aimless0.6.2data scaling
PHENIX1.13_2998refinement
PDB_EXTRACT3.24data extraction
xia2data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1WUU

1wuu


Resolution: 2.49→54.092 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 30.32
RfactorNum. reflection% reflection
Rfree0.2556 5727 5.01 %
Rwork0.2213 --
obs0.223 114213 97.27 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 165.92 Å2 / Biso mean: 58.7349 Å2 / Biso min: 20.95 Å2
Refinement stepCycle: final / Resolution: 2.49→54.092 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22465 0 433 103 23001
Biso mean--62.01 44.23 -
Num. residues----3066
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A12906X-RAY DIFFRACTION10.18TORSIONAL
12B12906X-RAY DIFFRACTION10.18TORSIONAL
13C12906X-RAY DIFFRACTION10.18TORSIONAL
14D12906X-RAY DIFFRACTION10.18TORSIONAL
15E12906X-RAY DIFFRACTION10.18TORSIONAL
16F12906X-RAY DIFFRACTION10.18TORSIONAL
17G12906X-RAY DIFFRACTION10.18TORSIONAL
18H12906X-RAY DIFFRACTION10.18TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4898-2.51810.32811850.31753479366494
2.5181-2.54770.3611780.31343638381697
2.5477-2.57880.33381900.30233564375497
2.5788-2.61140.3781930.31243661385497
2.6114-2.64580.31111870.30323562374997
2.6458-2.6820.35291970.30723606380397
2.682-2.72030.36021840.29643643382797
2.7203-2.76090.33771800.29513622380297
2.7609-2.80410.33572080.30043591379997
2.8041-2.850.33191980.28873600379897
2.85-2.89920.34941810.28613680386197
2.8992-2.95190.29661820.27263571375397
2.9519-3.00870.30131880.26413650383897
3.0087-3.07010.29781900.24833602379297
3.0701-3.13680.29012310.25763588381997
3.1368-3.20980.27092090.25633590379997
3.2098-3.290.29711950.25953590378597
3.29-3.3790.30891800.25563644382497
3.379-3.47840.27712210.2433584380597
3.4784-3.59060.24381920.23023612380497
3.5906-3.71890.26621980.20833594379297
3.7189-3.86780.26771710.20883608377997
3.8678-4.04380.21711470.20233678382598
4.0438-4.25690.2322060.18563669387598
4.2569-4.52350.19692290.17283626385599
4.5235-4.87250.21062450.16553617386298
4.8725-5.36250.19131770.17433643382098
5.3625-6.13750.21911740.18993695386998
6.1375-7.7290.21371450.18543671381697
7.729-54.1050.18261660.16953608377497
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)
12.62090.71850.94622.02062.00843.22840.05990.1022-0.6105-0.3670.0421-0.4664-0.2080.0138-0.02920.3506-0.02930.10630.23560.11990.465-50.75670.809634.2504
21.01181.29740.60552.13030.99520.85490.2755-0.3753-0.50850.0921-0.2977-0.45410.268-0.1336-0.00720.3345-0.00740.03210.38540.20520.5988-50.50530.860945.514
30.9433-0.74591.69812.6473-0.62422.2903-0.2901-0.31310.29930.7969-0.0701-1.0469-0.33770.03460.08490.2884-0.1525-0.07290.64030.18980.645-39.583116.686661.5015
41.12181.20630.27632.73360.29121.58410.0094-0.1402-0.343-0.4849-0.1972-0.895-0.20640.44320.04310.338-0.03250.15530.40350.19150.6243-38.020818.347740.4561
53.39321.40071.60143.0571.11782.26520.2246-0.0692-0.4909-0.102-0.0342-0.20350.4225-0.2102-0.12630.385-0.08310.03340.24030.0390.3513-80.8124-57.111438.0666
62.57180.2390.87792.10530.1543.104-0.0511-0.03360.14210.02010.0283-0.09940.07150.09610.00630.2504-0.02080.06830.1691-0.00610.284-67.1231-39.278447.9426
71.9345-0.27050.40070.66540.50252.64590.0732-0.1089-0.12690.04810.00950.25630.3071-0.2095-0.0730.33370.0564-0.06770.29410.00990.3052-27.5055-39.090637.8302
83.1155-0.24232.22641.35071.07515.185-0.26250.07590.1642-0.2404-0.01790.1556-0.3691-0.39010.24710.28740.0174-0.01510.2755-0.03180.2904-29.4731-31.772528.3826
91.93241.39451.11851.10131.23543.6462-0.0337-0.07480.0255-0.01510.1040.00660.01280.3411-0.07010.28380.0601-0.02080.3095-0.01740.3213-19.7715-31.607937.173
102.50011.9421-1.00052.68360.40552.15840.1786-0.26770.6042-0.097-0.07740.724-0.3329-0.4446-0.05560.49350.12170.03120.5046-0.05490.3478-27.1376-22.55751.1897
111.1514-0.3473-0.18125.23662.05160.8986-0.0958-0.3780.11430.44810.2503-0.20380.1009-0.1282-0.09580.45450.1051-0.03540.6165-0.10490.3059-18.6831-18.867160.7415
123.32820.5625-1.04891.11130.95281.72770.0812-0.35960.1230.3676-0.18390.68940.0159-0.80580.13260.49970.01910.07560.7485-0.07920.408-33.0969-26.12159.5053
132.4295-0.1932-0.43311.81110.61473.4751-0.1195-0.583-0.30280.6136-0.07460.46780.6316-0.62060.19750.4607-0.12080.03470.57910.06670.4835-32.7398-39.401554.2505
142.28140.3961.43421.49561.09743.7883-0.1892-0.2630.12410.0367-0.10030.0704-0.2526-0.38630.26980.29950.06180.00060.3358-0.05060.2748-48.6196-38.79261.3711
154.24920.2672-1.89951.77120.6294.75490.0571-0.2477-0.5955-0.0159-0.29540.35860.53240.04830.17930.361-0.0312-0.00210.3489-0.05790.4688-57.0001-56.3606-17.3066
161.71450.21740.57671.1013-0.01441.560.0905-0.8223-0.53960.5125-0.3050.42610.6228-0.81220.22070.554-0.19480.16140.80120.1130.5718-63.7066-56.4381-0.7898
171.4869-0.51240.60022.43780.20662.8526-0.1095-0.46670.12130.25420.00460.117-0.0573-0.43510.1340.39110.0393-0.10690.4229-0.08170.4142-24.547314.84445.428
182.6661-1.36791.58532.15650.81685.9847-0.0613-0.1740.01950.1233-0.1717-0.3893-0.1890.35810.09880.410.0324-0.14870.4272-0.02760.434-9.466814.05637.4072
191.35151.25211.06442.19470.33372.3356-0.2397-0.10020.2602-0.5059-0.07510.3208-0.5195-0.19040.2730.5060.0542-0.17340.3257-0.00960.4654-22.823216.596-4.2264
202.3590.7094-1.35431.98351.36984.4561-0.130.0491-0.3758-0.5462-0.0392-0.2229-0.45320.2690.07650.54180.0359-0.14790.26430.01260.5424-18.73550.3014-20.5892
210.8830.1420.19342.70430.88922.96160.1459-0.2355-0.3884-0.1503-0.20050.45010.3662-0.5060.08380.5353-0.0981-0.26360.42780.06090.6799-32.9661-2.5369-10.5481
221.49510.87020.49170.52720.83543.5908-0.1130.19750.0679-0.24760.0020.239-0.16470.06460.11680.36980.1045-0.09510.3286-0.06770.3789-76.978718.832636.4275
230.67930.2407-0.31512.35060.78030.7930.0021-0.01270.11070.1828-0.2080.57890.0281-0.20520.1590.29770.05980.00260.4476-0.1160.4131-80.549423.011559.958
241.784-1.7429-1.42852.9002-0.77816.8315-0.81050.10580.5302-0.11880.54870.1326-0.83921.08070.09990.7904-0.214-0.37510.7834-0.00420.9268-59.3455-8.3693.0832
252.40010.8852.17032.07611.19074.6125-0.6560.04130.744-0.160.12070.4306-1.10160.00920.43990.506-0.0239-0.17820.4682-0.01960.7256-70.1327-15.1363-4.1598
262.51680.34092.19552.67470.28354.5933-0.5249-0.48791.02850.09810.07110.5899-0.4932-0.89320.30070.39230.1264-0.10760.638-0.12950.6935-75.9251-18.8806-0.2039
271.71260.99761.51251.88980.94013.1634-0.53480.63660.5377-0.13440.33970.0363-0.87250.6410.12190.4551-0.1336-0.12490.6420.10340.5884-71.6262-23.5168-18.7597
287.91250.5784-0.10964.9562.2023.0064-0.08760.6404-0.0448-1.226-0.2156-0.40240.1983-0.92120.14930.6927-0.1646-0.03860.70020.01170.3588-86.8078-31.5048-33.0303
290.7818-0.34660.52321.2030.72291.0971-0.06670.7083-0.0929-0.6527-0.02810.0986-0.93190.97810.02780.6976-0.4234-0.12170.95430.33340.6431-70.7788-24.2356-32.2144
300.4489-0.2470.160.90780.15320.5119-0.2440.72230.5031-0.9670.2551-0.2269-1.34091.04330.10281.1412-1.2821-0.44341.1380.44451.0513-64.7108-11.503-29.547
310.62480.2165-1.32620.4065-1.10354.1869-0.35010.39190.70420.13810.2451-0.1609-1.42071.40570.19260.7716-0.41-0.22180.9120.0210.8579-60.1824-13.0846-13.5255
320.9902-0.02120.80071.4103-0.07232.8723-0.1453-0.6820.36910.5314-0.09530.1608-0.72560.00170.15320.90820.1032-0.08590.9073-0.17820.5006-38.898738.3375-1.7566
332.60540.2791-0.00211.57320.20374.4717-0.0572-0.57090.35520.1943-0.08330.7708-0.4212-0.88690.14290.89990.252-0.05360.9268-0.24990.6339-48.916235.62020.0375
341.57440.39360.03282.07860.33322.952-0.3574-0.8220.53640.84350.23670.0403-0.3498-0.02790.09520.81380.1028-0.09390.5103-0.14710.5429-42.578332.5035-18.8896
352.35290.11810.34541.3752-0.14292.2919-0.204-0.01770.49280.18380.0292-0.3547-0.7680.16580.12740.77030.0065-0.18350.3537-0.12080.5974-38.768938.0489-27.5609
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 4 through 91 )A4 - 91
2X-RAY DIFFRACTION2chain 'A' and (resid 92 through 249 )A92 - 249
3X-RAY DIFFRACTION3chain 'A' and (resid 250 through 316 )A250 - 316
4X-RAY DIFFRACTION4chain 'A' and (resid 317 through 392 )A317 - 392
5X-RAY DIFFRACTION5chain 'B' and (resid 6 through 178 )B6 - 178
6X-RAY DIFFRACTION6chain 'B' and (resid 179 through 392 )B179 - 392
7X-RAY DIFFRACTION7chain 'C' and (resid 4 through 50 )C4 - 50
8X-RAY DIFFRACTION8chain 'C' and (resid 51 through 116 )C51 - 116
9X-RAY DIFFRACTION9chain 'C' and (resid 117 through 212 )C117 - 212
10X-RAY DIFFRACTION10chain 'C' and (resid 213 through 249 )C213 - 249
11X-RAY DIFFRACTION11chain 'C' and (resid 250 through 316 )C250 - 316
12X-RAY DIFFRACTION12chain 'C' and (resid 317 through 350 )C317 - 350
13X-RAY DIFFRACTION13chain 'C' and (resid 351 through 392 )C351 - 392
14X-RAY DIFFRACTION14chain 'D' and (resid 4 through 212 )D4 - 212
15X-RAY DIFFRACTION15chain 'D' and (resid 213 through 316 )D213 - 316
16X-RAY DIFFRACTION16chain 'D' and (resid 317 through 392 )D317 - 392
17X-RAY DIFFRACTION17chain 'E' and (resid 5 through 77 )E5 - 77
18X-RAY DIFFRACTION18chain 'E' and (resid 78 through 116 )E78 - 116
19X-RAY DIFFRACTION19chain 'E' and (resid 117 through 217 )E117 - 217
20X-RAY DIFFRACTION20chain 'E' and (resid 218 through 271 )E218 - 271
21X-RAY DIFFRACTION21chain 'E' and (resid 272 through 392 )E272 - 392
22X-RAY DIFFRACTION22chain 'F' and (resid 6 through 212 )F6 - 212
23X-RAY DIFFRACTION23chain 'F' and (resid 213 through 392 )F213 - 392
24X-RAY DIFFRACTION24chain 'G' and (resid 5 through 24 )G5 - 24
25X-RAY DIFFRACTION25chain 'G' and (resid 25 through 91 )G25 - 91
26X-RAY DIFFRACTION26chain 'G' and (resid 92 through 178 )G92 - 178
27X-RAY DIFFRACTION27chain 'G' and (resid 179 through 249 )G179 - 249
28X-RAY DIFFRACTION28chain 'G' and (resid 250 through 271 )G250 - 271
29X-RAY DIFFRACTION29chain 'G' and (resid 272 through 316 )G272 - 316
30X-RAY DIFFRACTION30chain 'G' and (resid 317 through 370 )G317 - 370
31X-RAY DIFFRACTION31chain 'G' and (resid 371 through 392 )G371 - 392
32X-RAY DIFFRACTION32chain 'H' and (resid 6 through 77 )H6 - 77
33X-RAY DIFFRACTION33chain 'H' and (resid 78 through 178 )H78 - 178
34X-RAY DIFFRACTION34chain 'H' and (resid 179 through 249 )H179 - 249
35X-RAY DIFFRACTION35chain 'H' and (resid 250 through 392 )H250 - 392

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