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- PDB-6kja: E. coli ATCase holoenzyme mutant - G128/130A (catalytic chain) -

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Basic information

Entry
Database: PDB / ID: 6kja
TitleE. coli ATCase holoenzyme mutant - G128/130A (catalytic chain)
Components
  • Aspartate carbamoyltransferase catalytic subunit
  • Aspartate carbamoyltransferase regulatory chain
KeywordsTRANSFERASE / aspartate transcarbamoylase holoenzyme / de novo pyrimidine biosynthesis
Function / homology
Function and homology information


aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / zinc ion binding ...aspartate carbamoyltransferase complex / pyrimidine nucleotide biosynthetic process / aspartate carbamoyltransferase / aspartate carbamoyltransferase activity / amino acid binding / glutamine metabolic process / protein homotrimerization / 'de novo' UMP biosynthetic process / 'de novo' pyrimidine nucleobase biosynthetic process / zinc ion binding / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Aspartate transcarbamylase regulatory subunit / Aspartate carbamoyltransferase regulatory subunit, C-terminal / Aspartate carbamoyltransferase regulatory subunit, N-terminal / Aspartate carbamoyltransferase regulatory subunit, C-terminal domain superfamily / Aspartate carbamoyltransferase regulatory subunit, N-terminal domain superfamily / Aspartate carbamoyltransferase regulatory chain, allosteric domain / Aspartate carbamoyltransferase regulatory chain, metal binding domain / Aspartate carbamoyltransferase regulatory subunit, N-terminal domain / Aspartate carbamoyltransferase regulatory subunit, C-terminal domain / Aspartate carbamoyltransferase ...Aspartate transcarbamylase regulatory subunit / Aspartate carbamoyltransferase regulatory subunit, C-terminal / Aspartate carbamoyltransferase regulatory subunit, N-terminal / Aspartate carbamoyltransferase regulatory subunit, C-terminal domain superfamily / Aspartate carbamoyltransferase regulatory subunit, N-terminal domain superfamily / Aspartate carbamoyltransferase regulatory chain, allosteric domain / Aspartate carbamoyltransferase regulatory chain, metal binding domain / Aspartate carbamoyltransferase regulatory subunit, N-terminal domain / Aspartate carbamoyltransferase regulatory subunit, C-terminal domain / Aspartate carbamoyltransferase / Aspartate and ornithine carbamoyltransferases signature. / Aspartate/ornithine carbamoyltransferase / Aspartate/ornithine carbamoyltransferase, Asp/Orn-binding domain / Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding / Aspartate/ornithine carbamoyltransferase superfamily / Aspartate/ornithine carbamoyltransferase, Asp/Orn binding domain / Aspartate/ornithine carbamoyltransferase, carbamoyl-P binding domain / SH3 type barrels. / Roll / Alpha-Beta Plaits / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Aspartate carbamoyltransferase catalytic subunit / Aspartate carbamoyltransferase regulatory chain
Similarity search - Component
Biological speciesEscherichia coli K-12 (bacteria)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.064 Å
AuthorsLei, Z. / Zheng, J. / Jia, Z.C.
Funding support China, Canada, 2items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)21773014 China
Natural Sciences and Engineering Research Council (NSERC, Canada)RGPIN-2018-04427 Canada
CitationJournal: Febs J. / Year: 2020
Title: New regulatory mechanism-based inhibitors of aspartate transcarbamoylase for potential anticancer drug development.
Authors: Lei, Z. / Wang, B. / Lu, Z. / Wang, N. / Tan, H. / Zheng, J. / Jia, Z.
History
DepositionJul 22, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 11, 2020Provider: repository / Type: Initial release
Revision 1.1Aug 26, 2020Group: Database references / Derived calculations / Category: citation / struct_conn
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _struct_conn.pdbx_dist_value / _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
Revision 1.2Nov 22, 2023Group: 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 / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Aspartate carbamoyltransferase catalytic subunit
B: Aspartate carbamoyltransferase regulatory chain
C: Aspartate carbamoyltransferase catalytic subunit
D: Aspartate carbamoyltransferase regulatory chain
E: Aspartate carbamoyltransferase catalytic subunit
F: Aspartate carbamoyltransferase regulatory chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)154,7239
Polymers154,5266
Non-polymers1963
Water19811
1
A: Aspartate carbamoyltransferase catalytic subunit
B: Aspartate carbamoyltransferase regulatory chain
C: Aspartate carbamoyltransferase catalytic subunit
D: Aspartate carbamoyltransferase regulatory chain
E: Aspartate carbamoyltransferase catalytic subunit
F: Aspartate carbamoyltransferase regulatory chain
hetero molecules

A: Aspartate carbamoyltransferase catalytic subunit
B: Aspartate carbamoyltransferase regulatory chain
C: Aspartate carbamoyltransferase catalytic subunit
D: Aspartate carbamoyltransferase regulatory chain
E: Aspartate carbamoyltransferase catalytic subunit
F: Aspartate carbamoyltransferase regulatory chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)309,44518
Polymers309,05312
Non-polymers3926
Water18010
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation6_554-x,-x+y,-z-1/31
Buried area26510 Å2
ΔGint-83 kcal/mol
Surface area102290 Å2
MethodPISA
Unit cell
Length a, b, c (Å)127.408, 127.408, 197.523
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221
Symmetry operation#1: x,y,z
#2: -y,x-y,z+2/3
#3: -x+y,-x,z+1/3
#4: x-y,-y,-z+1/3
#5: -x,-x+y,-z+2/3
#6: y,x,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 2 through 6 or (resid 7...
21(chain C and (resid 2 through 77 or resid 86...
31(chain E and (resid 2 through 6 or (resid 7...
12(chain B and (resid 16 through 45 or (resid 46...
22(chain D and (resid 16 through 18 or (resid 19...
32(chain F and (resid 16 through 18 or (resid 19...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ASNASNGLNGLN(chain A and (resid 2 through 6 or (resid 7...AA2 - 62 - 6
121LYSLYSLYSLYS(chain A and (resid 2 through 6 or (resid 7...AA77
131ASNASNVALVAL(chain A and (resid 2 through 6 or (resid 7...AA2 - 3092 - 309
141ASNASNVALVAL(chain A and (resid 2 through 6 or (resid 7...AA2 - 3092 - 309
151ASNASNVALVAL(chain A and (resid 2 through 6 or (resid 7...AA2 - 3092 - 309
161ASNASNVALVAL(chain A and (resid 2 through 6 or (resid 7...AA2 - 3092 - 309
211ASNASNALAALA(chain C and (resid 2 through 77 or resid 86...CC2 - 772 - 77
221GLUGLUTHRTHR(chain C and (resid 2 through 77 or resid 86...CC86 - 22886 - 228
231ARGARGARGARG(chain C and (resid 2 through 77 or resid 86...CC229229
241ALAALALEULEU(chain C and (resid 2 through 77 or resid 86...CC1 - 3101 - 310
251ALAALALEULEU(chain C and (resid 2 through 77 or resid 86...CC1 - 3101 - 310
261ALAALALEULEU(chain C and (resid 2 through 77 or resid 86...CC1 - 3101 - 310
271ALAALALEULEU(chain C and (resid 2 through 77 or resid 86...CC1 - 3101 - 310
311ASNASNGLNGLN(chain E and (resid 2 through 6 or (resid 7...EE2 - 62 - 6
321LYSLYSLYSLYS(chain E and (resid 2 through 6 or (resid 7...EE77
331ALAALALEULEU(chain E and (resid 2 through 6 or (resid 7...EE1 - 3101 - 310
341ALAALALEULEU(chain E and (resid 2 through 6 or (resid 7...EE1 - 3101 - 310
351ALAALALEULEU(chain E and (resid 2 through 6 or (resid 7...EE1 - 3101 - 310
361ALAALALEULEU(chain E and (resid 2 through 6 or (resid 7...EE1 - 3101 - 310
112THRTHRGLYGLY(chain B and (resid 16 through 45 or (resid 46...BB16 - 4516 - 45
122LEULEULEULEU(chain B and (resid 16 through 45 or (resid 46...BB4646
132THRTHRASNASN(chain B and (resid 16 through 45 or (resid 46...BB16 - 15316 - 153
142THRTHRASNASN(chain B and (resid 16 through 45 or (resid 46...BB16 - 15316 - 153
152THRTHRASNASN(chain B and (resid 16 through 45 or (resid 46...BB16 - 15316 - 153
162THRTHRASNASN(chain B and (resid 16 through 45 or (resid 46...BB16 - 15316 - 153
212THRTHRILEILE(chain D and (resid 16 through 18 or (resid 19...DD16 - 1816 - 18
222ASPASPHISHIS(chain D and (resid 16 through 18 or (resid 19...DD19 - 2019 - 20
232THRTHRASNASN(chain D and (resid 16 through 18 or (resid 19...DD16 - 15316 - 153
242THRTHRASNASN(chain D and (resid 16 through 18 or (resid 19...DD16 - 15316 - 153
252THRTHRASNASN(chain D and (resid 16 through 18 or (resid 19...DD16 - 15316 - 153
262THRTHRASNASN(chain D and (resid 16 through 18 or (resid 19...DD16 - 15316 - 153
312THRTHRILEILE(chain F and (resid 16 through 18 or (resid 19...FF16 - 1816 - 18
322ASPASPHISHIS(chain F and (resid 16 through 18 or (resid 19...FF19 - 2019 - 20
332THRTHRASNASN(chain F and (resid 16 through 18 or (resid 19...FF16 - 15316 - 153
342THRTHRASNASN(chain F and (resid 16 through 18 or (resid 19...FF16 - 15316 - 153
352THRTHRASNASN(chain F and (resid 16 through 18 or (resid 19...FF16 - 15316 - 153
362THRTHRASNASN(chain F and (resid 16 through 18 or (resid 19...FF16 - 15316 - 153

NCS ensembles :
ID
1
2

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Components

#1: Protein Aspartate carbamoyltransferase catalytic subunit / Aspartate transcarbamylase / ATCase


Mass: 34365.156 Da / Num. of mol.: 3 / Mutation: G128A, G130A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K-12 / Gene: pyrB, b4245, JW4204 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A786, aspartate carbamoyltransferase
#2: Protein Aspartate carbamoyltransferase regulatory chain


Mass: 17143.625 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K-12 / Gene: pyrI / Production host: Escherichia coli (E. coli) / References: UniProt: P0A7F3
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN

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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: 3 Å3/Da / Density % sol: 58.93 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.1 M HEPES pH 7.0, 30% Jeffamine M-600 pH 7.0, and 10% glycerol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU R-AXIS IV / Wavelength: 1.54 Å
DetectorType: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Oct 15, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 3.04→50 Å / Num. obs: 36586 / % possible obs: 99.8 % / Redundancy: 4.8 % / CC1/2: 0.999 / Net I/σ(I): 16
Reflection shellResolution: 3.04→3.09 Å / Num. unique obs: 1813 / CC1/2: 0.88

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Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
HKL-2000data reduction
HKL-2000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1ZA1

1za1


Resolution: 3.064→42.287 Å / SU ML: 0.47 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 31.6 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2834 1966 5.62 %
Rwork0.2488 33032 -
obs0.2507 34998 98.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 165.93 Å2 / Biso mean: 68.8878 Å2 / Biso min: 23.92 Å2
Refinement stepCycle: final / Resolution: 3.064→42.287 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10005 0 3 11 10019
Biso mean--57.83 56.69 -
Num. residues----1311
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A2712X-RAY DIFFRACTION4.25TORSIONAL
12C2712X-RAY DIFFRACTION4.25TORSIONAL
13E2712X-RAY DIFFRACTION4.25TORSIONAL
21B1182X-RAY DIFFRACTION4.25TORSIONAL
22D1182X-RAY DIFFRACTION4.25TORSIONAL
23F1182X-RAY DIFFRACTION4.25TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.0644-3.1410.39671380.33742360100
3.141-3.22590.39591390.32862338100
3.2259-3.32080.33931340.3163231699
3.3208-3.42790.38331440.30632390100
3.4279-3.55040.36311460.30042355100
3.5504-3.69250.3281410.2884232799
3.6925-3.86040.28921380.2681234899
3.8604-4.06380.32121410.2658231697
4.0638-4.31810.29661380.2355232198
4.3181-4.65120.2521370.2138232897
4.6512-5.11850.19431410.2005236498
5.1185-5.85750.24111410.2224237098
5.8575-7.37350.31021470.2565243799
7.3735-42.2870.20941410.1999246296
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)
10.02250.0103-0.0055-0.02220.022-0.02460.43080.2288-0.5216-0.02510.30260.26360.2709-0.04-0-1.49520.79650.6440.6229-0.6809-0.0326-16.870220.4201-64.8139
20.0182-0.0005-0.0085-0.002-0.0169-0.00020.10670.2941-0.3630.32390.1104-0.0470.0368-0.06-0-0.93810.1437-0.08390.6765-0.22310.3297-26.72820.6722-53.5694
30.0147-0.0153-0.0352-0.0254-0.002-0.03010.27930.0185-0.43940.72040.0185-0.2113-0.2960.09750-1.70621.73020.5107-0.6119-0.87860.5322-0.31849.585-49.7173
40.02540.021-0.06630.05450.02090.0502-0.0230.20630.0183-0.01760.0508-0.387-0.0187-0.1134-0-0.34040.0948-0.47941.0217-0.52980.46010.139321.2332-58.3121
5-0.00090.00030.0038-0.00050.0004-0.0013-0.0044-0.0016-0.01040.02660.0186-0.00070.0036-0.0108-00.94210.0465-0.05010.8414-0.16680.9331-40.338-15.6297-35.2173
60.0034-0.0021-0.00290.0035-0.00140.00050.0340.0112-0.0076-0.04970.04370.035-0.0196-0.0596-00.624-0.1928-0.07480.6308-0.20370.8458-46.1989-5.6083-38.4311
7-0.00530.00110.00250.01020.00280.0006-0.01240.0812-0.03830.0461-0.04740.00620.04310.030900.9862-0.2964-0.20840.8934-0.3511.2238-43.7598-14.4909-39.2863
80.0036-0.00690.00340.00670.0025-0.0045-0.02550.01130.0234-0.008-0.0021-0.05510.0474-0.0311-00.9338-0.0166-0.12060.8456-0.17141.2917-40.1121-17.704-42.4114
90.0027-0.0075-0.00070.00460.0036-0.0039-0.0150.0210.0468-0.02-0.0452-0.06450.0329-0.0203-00.9943-0.08170.07180.8672-0.21851.1771-39.2084-20.6584-47.0346
100.0042-0.0019-0.01280.0016-0.0031-0.00010.01160.0251-0.08280.02960.00710.0181-0.0119-0.0213-00.31450.01750.0070.5109-0.10750.6661-30.22785.4825-43.8592
110.00080.00450.00430.00170.0011-0.0024-0.0527-0.0244-0.11990.0052-0.0246-0.0370.0401-0.0118-00.37710.1233-0.24970.5266-0.20080.9329-22.3583-1.5766-44.986
120.00150.00060.00160.0022-0.00090.0017-0.00450.00260.0324-0.0001-0.017-0.01690.02840.020900.85330.19450.07960.8248-0.08920.8937-24.2269-1.5586-36.3818
130.05820.033-0.00370.02930.0669-0.0440.69090.540.27330.8520.13750.27460.0971-0.1138-0-1.42530.09780.04230.97140.09720.3741-38.246443.1189-59.8305
140.06420.0164-0.01810.05190.00860.0350.13150.07450.04110.49670.31550.18480.0315-0.0067-00.2197-0.0097-0.030.69970.15610.3415-57.528731.963-46.674
150.0295-0.02530.03340.035-0.00790.0016-0.0020.2902-0.36730.12340.05920.15610.18210.10690-0.24150.0147-0.24250.79940.140.1921-46.725325.829-57.3378
160.0011-0.0018-0.0037-0.0004-0.00440.0001-0.0212-0.01860.0104-0.0234-0.0090.0209-0.0211-0.001500.9980.25380.0961.09650.10061.3139-58.218579.7221-36.2614
17-0.00080.0007-0.00150.0007-0.0013-0.0016-0.01220.0205-0.032-0.0144-0.00270.0407-0.01490.029500.75560.1534-0.03590.57930.10981.1933-46.201679.5149-39.6034
180.0016-0.0024-0.00180.0037-0.0006-0.0017-0.0121-0.01070.0202-0.0114-0.0303-0.03220.0101-0.0226-01.19710.19330.03141.1248-0.0291.4795-57.040384.9927-32.1185
190.0005-0.00260.00010.0004-0.0009-0.0011-0.0231-0.0052-0.02880.02310.01760.0244-0.0004-0.004701.09150.13270.02841.02720.20571.2646-52.410184.9946-45.4837
200.00250.0004-0.0007-0.0003-0.0014-0.0005-0.0148-0.0222-0.0169-0.04390.0180.0205-0.0105-0.0034-00.69640.17820.11190.97010.07991.3055-57.691772.8594-44.5836
210.0007-0.0015-0.00230.00020.00060.0013-0.0051-0.01030.00630.0117-0.00390.01040.00520.001301.3936-0.00640.07141.35250.17891.4025-59.093688.434-47.9723
220.0053-0.0011-0.0030.0245-0.0043-0.0014-0.01940.0057-0.0336-0.012-0.0056-0.0007-0.05150.0068-01.11110.07260.01130.99930.07041.3775-63.000980.9662-47.7227
230.004-0.00470.00140.01-0.00740.00710.0616-0.01240.07930.04870.0356-0.0320.00880.023500.30260.02330.15090.68040.20180.9723-47.77559.7268-44.2431
240.00190.00080.0020.0063-0.00580.00230.0084-0.02630.03270.0197-0.07170.02180.0461-0.040400.28530.05080.33140.62660.30310.8251-53.636255.5487-44.4454
250.00180.0016-0.00380.00090.00060.00070.00350.00020.02590.02480.0122-0.0042-0.0093-0.0192-00.6859-0.01920.18960.8515-0.00830.9143-53.804658.6856-36.5973
260.0151-0.03410.00830.0630.06230.01380.10820.29140.01430.42490.4244-0.01730.10170.1681-0-0.0647-0.04360.20591.00780.14140.1753-10.801847.8339-63.3916
270.01680.0165-0.02990.0147-0.0214-0.02990.28240.47380.0290.32690.2558-0.17950.12110.0033-00.07630.07850.02310.77620.09590.2498-5.753547.5867-57.0922
280.0529-0.00650.00540.0247-0.00350.00860.18080.11940.35120.56210.26550.28410.28410.1701-00.3332-0.03340.21810.60250.3930.6046-10.384171.2743-49.1874
290.02790.01410.04370.0110.01240.00090.24130.28280.19120.03550.27910.3759-0.01490.1482-0-0.3021-0.14690.33710.97520.43590.3117-18.771659.6248-60.4576
300.0008-0.00030.001-0.00010.0043-0.0010.0320.0135-0.00010.04190.0074-0.03920.00590.0203-00.5514-0.1013-0.14620.6796-0.07370.713734.171147.8434-38.4557
310.0006-0.0096-0.00050.002-0.01220.0051-0.02740.0301-0.04480.0385-0.0878-0.11590.03840.054200.36570.0983-0.02910.8506-0.05030.627632.617740.2101-40.4145
320.0027-0.00080.00020.00110.0018-0.00130.01370.0089-0.0029-0.0123-0.0110.0312-0.0114-0.002900.5706-0.111-0.28350.8359-0.08870.671727.34250.5744-46.078
330.0068-0.0049-0.00390.0090.00390.0017-0.0003-00.01420.0032-0.00430.0131-0.0077-0.0057-00.89360.02790.21951.019-0.17471.024141.450344.1102-48.9124
340.00230.0010.0090.0026-0.00790.0102-0.01180.0072-0.0276-0.0405-0.0748-0.0048-0.0055-0.0085-00.3026-0.04330.04110.9066-0.0520.629825.682249.7288-48.6412
350.00190.00110.0091-0.0007-0.01290.0197-0.01690.0248-0.01950.064-0.00580.0209-0.13470.038-00.4009-0.0105-0.00190.7313-0.04710.45649.37551.4331-45.7124
360.00090.0007-0.00140.00090.00120.0013-0.00440.0083-0.01390.0123-0.00010.025500.0035-00.4632-0.1083-0.07560.6591-0.12850.51213.265954.7192-38.4349
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 66 )A2 - 66
2X-RAY DIFFRACTION2chain 'A' and (resid 67 through 134 )A67 - 134
3X-RAY DIFFRACTION3chain 'A' and (resid 135 through 247 )A135 - 247
4X-RAY DIFFRACTION4chain 'A' and (resid 248 through 309 )A248 - 309
5X-RAY DIFFRACTION5chain 'B' and (resid 16 through 25 )B16 - 25
6X-RAY DIFFRACTION6chain 'B' and (resid 26 through 41 )B26 - 41
7X-RAY DIFFRACTION7chain 'B' and (resid 42 through 74 )B42 - 74
8X-RAY DIFFRACTION8chain 'B' and (resid 75 through 89 )B75 - 89
9X-RAY DIFFRACTION9chain 'B' and (resid 90 through 99 )B90 - 99
10X-RAY DIFFRACTION10chain 'B' and (resid 100 through 123 )B100 - 123
11X-RAY DIFFRACTION11chain 'B' and (resid 124 through 143 )B124 - 143
12X-RAY DIFFRACTION12chain 'B' and (resid 144 through 153 )B144 - 153
13X-RAY DIFFRACTION13chain 'C' and (resid 1 through 149 )C1 - 149
14X-RAY DIFFRACTION14chain 'C' and (resid 150 through 247 )C150 - 247
15X-RAY DIFFRACTION15chain 'C' and (resid 248 through 310 )C248 - 310
16X-RAY DIFFRACTION16chain 'D' and (resid 16 through 25 )D16 - 25
17X-RAY DIFFRACTION17chain 'D' and (resid 26 through 41 )D26 - 41
18X-RAY DIFFRACTION18chain 'D' and (resid 42 through 57 )D42 - 57
19X-RAY DIFFRACTION19chain 'D' and (resid 58 through 67 )D58 - 67
20X-RAY DIFFRACTION20chain 'D' and (resid 68 through 81 )D68 - 81
21X-RAY DIFFRACTION21chain 'D' and (resid 82 through 89 )D82 - 89
22X-RAY DIFFRACTION22chain 'D' and (resid 90 through 99 )D90 - 99
23X-RAY DIFFRACTION23chain 'D' and (resid 100 through 130 )D100 - 130
24X-RAY DIFFRACTION24chain 'D' and (resid 131 through 143 )D131 - 143
25X-RAY DIFFRACTION25chain 'D' and (resid 144 through 153 )D144 - 153
26X-RAY DIFFRACTION26chain 'E' and (resid 1 through 87 )E1 - 87
27X-RAY DIFFRACTION27chain 'E' and (resid 88 through 149 )E88 - 149
28X-RAY DIFFRACTION28chain 'E' and (resid 150 through 265 )E150 - 265
29X-RAY DIFFRACTION29chain 'E' and (resid 266 through 310 )E266 - 310
30X-RAY DIFFRACTION30chain 'F' and (resid 16 through 25 )F16 - 25
31X-RAY DIFFRACTION31chain 'F' and (resid 26 through 67 )F26 - 67
32X-RAY DIFFRACTION32chain 'F' and (resid 68 through 81 )F68 - 81
33X-RAY DIFFRACTION33chain 'F' and (resid 82 through 89 )F82 - 89
34X-RAY DIFFRACTION34chain 'F' and (resid 90 through 109 )F90 - 109
35X-RAY DIFFRACTION35chain 'F' and (resid 110 through 143 )F110 - 143
36X-RAY DIFFRACTION36chain 'F' and (resid 144 through 153 )F144 - 153

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