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- PDB-6kj8: E. coli ATCase holoenzyme mutant - G166P (catalytic chain) -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6kj8
TitleE. coli ATCase holoenzyme mutant - G166P (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 / glutamine metabolic process / amino acid binding / 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 / glutamine metabolic process / amino acid binding / 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/ornithine 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 / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) 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: 3.011 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 / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
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)154,7599
Polymers154,5626
Non-polymers1963
Water50428
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)309,51718
Polymers309,12512
Non-polymers3926
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555y,x,-z1
Buried area26900 Å2
ΔGint-97 kcal/mol
Surface area100680 Å2
MethodPISA
Unit cell
Length a, b, c (Å)126.592, 126.592, 196.490
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 1 through 5 or (resid 6...
21(chain C and (resid 1 through 6 or (resid 7...
31(chain E and (resid 1 through 5 or (resid 6...
12(chain B and (resid 16 or (resid 17 and (name...
22(chain D and (resid 16 through 58 or (resid 59...
32(chain F and (resid 16 or (resid 17 and (name...

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
111ALAALATYRTYR(chain A and (resid 1 through 5 or (resid 6...AA1 - 51 - 5
121GLNGLNLYSLYS(chain A and (resid 1 through 5 or (resid 6...AA6 - 76 - 7
131ALAALAVALVAL(chain A and (resid 1 through 5 or (resid 6...AA1 - 3091 - 309
141ALAALAVALVAL(chain A and (resid 1 through 5 or (resid 6...AA1 - 3091 - 309
151ALAALAVALVAL(chain A and (resid 1 through 5 or (resid 6...AA1 - 3091 - 309
161ALAALAVALVAL(chain A and (resid 1 through 5 or (resid 6...AA1 - 3091 - 309
211ALAALAGLNGLN(chain C and (resid 1 through 6 or (resid 7...CC1 - 61 - 6
221LYSLYSLYSLYS(chain C and (resid 1 through 6 or (resid 7...CC77
231ALAALAVALVAL(chain C and (resid 1 through 6 or (resid 7...CC1 - 3091 - 309
241ALAALAVALVAL(chain C and (resid 1 through 6 or (resid 7...CC1 - 3091 - 309
251ALAALAVALVAL(chain C and (resid 1 through 6 or (resid 7...CC1 - 3091 - 309
261ALAALAVALVAL(chain C and (resid 1 through 6 or (resid 7...CC1 - 3091 - 309
311ALAALATYRTYR(chain E and (resid 1 through 5 or (resid 6...EE1 - 51 - 5
321GLNGLNLYSLYS(chain E and (resid 1 through 5 or (resid 6...EE6 - 76 - 7
331ALAALALEULEU(chain E and (resid 1 through 5 or (resid 6...EE1 - 3101 - 310
341ALAALALEULEU(chain E and (resid 1 through 5 or (resid 6...EE1 - 3101 - 310
351ALAALALEULEU(chain E and (resid 1 through 5 or (resid 6...EE1 - 3101 - 310
361ALAALALEULEU(chain E and (resid 1 through 5 or (resid 6...EE1 - 3101 - 310
112THRTHRTHRTHR(chain B and (resid 16 or (resid 17 and (name...BB1616
122VALVALVALVAL(chain B and (resid 16 or (resid 17 and (name...BB1717
132LYSLYSASNASN(chain B and (resid 16 or (resid 17 and (name...BB13 - 15313 - 153
142LYSLYSASNASN(chain B and (resid 16 or (resid 17 and (name...BB13 - 15313 - 153
152LYSLYSASNASN(chain B and (resid 16 or (resid 17 and (name...BB13 - 15313 - 153
162LYSLYSASNASN(chain B and (resid 16 or (resid 17 and (name...BB13 - 15313 - 153
212THRTHRLEULEU(chain D and (resid 16 through 58 or (resid 59...DD16 - 5816 - 58
222ILEILEASNASN(chain D and (resid 16 through 58 or (resid 59...DD59 - 6359 - 63
232THRTHRASNASN(chain D and (resid 16 through 58 or (resid 59...DD16 - 15316 - 153
242THRTHRASNASN(chain D and (resid 16 through 58 or (resid 59...DD16 - 15316 - 153
252THRTHRASNASN(chain D and (resid 16 through 58 or (resid 59...DD16 - 15316 - 153
262THRTHRASNASN(chain D and (resid 16 through 58 or (resid 59...DD16 - 15316 - 153
312THRTHRTHRTHR(chain F and (resid 16 or (resid 17 and (name...FF1616
322VALVALVALVAL(chain F and (resid 16 or (resid 17 and (name...FF1717
332ALAALAASNASN(chain F and (resid 16 or (resid 17 and (name...FF11 - 15311 - 153
342ALAALAASNASN(chain F and (resid 16 or (resid 17 and (name...FF11 - 15311 - 153
352ALAALAASNASN(chain F and (resid 16 or (resid 17 and (name...FF11 - 15311 - 153
362ALAALAASNASN(chain F and (resid 16 or (resid 17 and (name...FF11 - 15311 - 153

NCS ensembles :
ID
1
2

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Components

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


Mass: 34377.172 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: 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, b4244, JW4203 / 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


Mass: 18.015 Da / Num. of mol.: 28 / 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: 2.94 Å3/Da / Density % sol: 58.17 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.1M 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: Jan 12, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 37126 / % possible obs: 100 % / Redundancy: 8.8 % / CC1/2: 0.996 / Net I/σ(I): 16.1
Reflection shellResolution: 3→3.05 Å / Num. unique obs: 1823 / CC1/2: 0.811

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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: 3.011→47.869 Å / SU ML: 0.41 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 26.49 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2474 1988 5.44 %
Rwork0.2106 34587 -
obs0.2126 36575 99.63 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 186.42 Å2 / Biso mean: 60.697 Å2 / Biso min: 22.56 Å2
Refinement stepCycle: final / Resolution: 3.011→47.869 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10027 0 3 28 10058
Biso mean--47.66 48.33 -
Num. residues----1312
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A2721X-RAY DIFFRACTION10.31TORSIONAL
12C2721X-RAY DIFFRACTION10.31TORSIONAL
13E2721X-RAY DIFFRACTION10.31TORSIONAL
21B1149X-RAY DIFFRACTION10.31TORSIONAL
22D1149X-RAY DIFFRACTION10.31TORSIONAL
23F1149X-RAY DIFFRACTION10.31TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.011-3.0860.36861410.3023243599
3.086-3.16940.39691430.29052439100
3.1694-3.26260.35261340.28042420100
3.2626-3.36790.3141410.28462451100
3.3679-3.48830.29011420.26282458100
3.4883-3.62790.31121420.22592448100
3.6279-3.79290.25841400.2112445100
3.7929-3.99280.24011440.19912463100
3.9928-4.24280.22511460.19012477100
4.2428-4.57020.18821420.16642483100
4.5702-5.02970.16171380.16432468100
5.0297-5.75640.22381440.19052502100
5.7564-7.24840.24341450.21992520100
7.2484-47.8690.2431460.1921257897
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)
10.05670.01260.02090.01420.0117-0.02421.0729-0.2865-1.2667-0.0876-0.0963-0.10090.4043-0.3075-00.2620.33960.70040.0542-0.2194-0.7595-8.7936-24.7848-31.5181
2-0.01550.01290.01890.01090.0090.00070.15870.0456-0.2681-0.06430.1598-0.13850.1601-0.0518-00.41230.11720.09990.2187-0.02910.166-6.7786-39.6005-21.0259
3-0.0319-0.0828-0.141-0.0128-0.0688-0.06650.2759-0.02760.1186-0.03660.0036-0.18730.1780.093900.3120.08390.22440.29530.03440.3687-5.7303-18.9411-22.3876
40.0158-0.0699-0.15280.0597-0.0060.1276-0.1632-0.42710.8662-0.425-0.1725-0.2105-0.2267-0.2645-0-0.0688-0.2040.62630.11560.18830.3687-9.8943-3.2927-14.754
50.0215-0.03340.0174-0.0122-0.0094-0.0144-0.0361-0.06610.1408-0.04790.0214-0.02480.1556-0.0086-00.49020.01010.18790.26730.03480.2831-17.2248-14.901-26.6305
60.007-0.006-0.00230.00570.00190.00370.01710.0146-0.050.01280.0109-0.07050.00920.0371-00.86310.16780.12171.01420.22071.459139.9331-31.5748-9.1114
7-0.0065-0.0211-0.00460.0056-0.01250.01160.13240.1751-0.0627-0.0415-0.0661-0.01210.1835-0.001900.6032-0.00460.03950.67830.0750.644929.4143-33.8083-3.3859
8-0.00670.0018-0.00460.00110.006-0.0014-0.0323-0.06810.00330.00460.0448-0.0888-0.00710.0297-00.7056-0.0231-0.08190.87580.14251.056737.1127-30.4063.0235
90.00760.00250.00490.0057-0.0003-0.00280.00920.08270.1014-0.161-0.1114-0.03410.06840.0664-00.68680.07150.08650.91480.16511.009632.9724-28.3409-10.6379
100.00040.002-0.00150.00120.00130.00020.02490.0192-0.02240.04040.0425-0.05230.03520.0421-00.7453-0.1750.26361.15630.36131.10247.0892-31.1656-14.2904
11-0.0011-0.0049-0.0007-0.0055-0.0014-0.0011-0.0766-0.01950.0117-0.0574-0.0527-0.02790.01530.14700.62720.11330.16990.82390.391.398229.9797-20.6514-14.2219
120.00620.04380.06030.0002-0.03770.0474-0.01030.0271-0.17190.0298-0.04-0.2011-0.1018-0.176800.26990.02550.09810.20430.04510.463311.1093-24.0828-10.8964
130.00990.0046-0.00520.00730.00980.00310.0939-0.02280.0776-0.05710.0760.0744-0.030.0076-00.38420.00260.01250.5096-0.00790.504513.6899-19.9848-3.296
140.0041-0.016-0.00430.06070.02050.00180.4714-0.0918-0.181-0.14370.38830.51430.3734-0.137400.5970.3037-0.0896-0.092-0.551-0.011-13.7645-62.8903-33.0441
15-0.0004-0.0088-0.02790.0037-0.018-0.00470.0150.18480.0769-0.2444-0.17890.5746-0.00170.0876-00.50920.3417-0.2395-0.53550.4835-0.1223-19.0005-47.4907-31.5514
160.03080.0163-0.04290.0245-0.049-0.03450.0355-0.0286-0.2356-0.2081-0.05610.0504-0.05030.1468-00.41850.0937-0.06170.242-0.00740.2599-22.9975-48.0719-23.3101
170.0057-0.0090.00250.0251-0.00390.00220.1289-0.3285-0.2641-0.1539-0.0460.08750.00530.1531-00.35130.0605-0.12410.2747-0.06410.3272-15.6419-59.0684-22.8295
180.00020.02610.0020.034-0.00620.04620.2461-0.033-0.30820.06330.0657-0.2344-0.0879-0.112200.44460.1177-0.10430.3068-0.12440.3305-0.6635-67.0019-17.3802
190.06920.05550.01860.0495-0.00750.0653-0.0007-0.08210.06320.07210.1621-0.11130.0767-0.028800.39060.0432-0.06790.2252-0.09890.46651.6663-66.6595-12.7112
200.00750.0210.00430.0297-0.00910.01820.0765-0.18540.0127-0.01990.1131-0.30790.0344-0.0355-00.31850.0495-0.05860.3258-0.1120.36849.1477-56.5632-11.2162
21-0.0290.08330.0827-0.0011-0.0144-0.08830.0895-0.18870.2135-0.32130.07680.0284-0.04880.1905-00.51670.2199-0.11820.0587-0.07660.1979-3.1629-51.909-25.8015
22-0.0044-0.00410.00190.00910.0044-0.0045-0.04620.13610.0002-0.1714-0.02860.06590.0569-0.0785-00.58050.05-0.11930.49140.29181.1748-40.3922-90.3155-3.1031
23-0.01240.01640.02250.0250.0171-0.00840.09890.08690.04650.1073-0.0014-0.12860.231-0.1719-00.0114-0.8821-0.6802-0.7957-0.29160.786-44.0118-84.1379-8.7911
240.0028-0.00330.00340.00130.0020.0007-0.00840.0220.0420.03920.007-0.0028-0.03920.015701.1425-0.179-0.20280.7140.13691.4614-35.0295-90.0662-7.4763
250.00220.001-0.0006-0.0008-0-0.0026-0.0198-0.00540.003-0.0229-0.02080.03150.0179-0.0068-01.328-0.3192-0.03241.484-0.08351.4657-49.9331-98.0065-16.0561
260.0582-0.0171-0.02030.003-0.0290.02980.06330.1086-0.37860.04010.06230.2939-0.0523-0.2409-00.3580.0241-0.2557-0.03170.16710.6188-30.1989-73.2888-11.2971
270.00460.0089-0.0209-0.00340.00770.0170.0426-0.0252-0.2775-0.31080.1631-0.0931-0.05360.192300.36630.0467-0.21230.40160.08480.5088-22.4057-75.5493-9.1463
280.08660.1315-0.10460.08310.22050.04780.0758-0.0455-0.0281-0.0934-0.0319-0.0372-0.00480.0147-00.43460.1092-0.05590.2865-0.01240.1795-36.0407-33.2984-30.7422
290.0128-0.06840.07040.11790.0374-0.06650.4393-0.44610.2244-0.0696-0.18110.1958-0.12570.3101-00.31410.1223-0.16710.11970.06520.2235-42.0328-31.7809-23.11
300.0713-0.04070.0224-0.0081-0.00550.07790.2487-0.1938-0.3178-0.0920.04070.2321-0.43450.2043-00.29040.1108-0.23420.29940.05370.5368-56.0835-44.6327-15.3424
310.01930.02770.0022-0.0096-0.026-0.03370.24190.1996-0.2755-0.1194-0.23870.0957-0.123-0.210100.39140.0504-0.13320.3113-0.04070.3383-42.0338-45.52-27.4017
320.0059-0.01330.0002-0.0003-0.00280.00240.0885-0.05460.00050.08350.23150.05730.1343-0.1793-00.7130.0193-0.0780.5452-0.01970.6574-54.65197.1965-7.4743
330.0138-0.00640.00870.01120.02440.0077-0.2434-0.01010.0213-0.2048-0.1479-0.11-0.17250.013400.568-0.0229-0.11370.48450.02180.6998-49.78719.8316-6.5215
340.0053-0.0028-0.00580.010.01580.001-0.0771-0.0261-0.01370.0083-0.02420.1132-0.1017-0.03900.95150.1373-0.13370.7501-0.16591.1596-58.569410.6875-5.3771
350.0089-0.0030.00670.0015-0.00570.0099-0.05190.07990.0338-0.095-0.05820.0283-0.0022-0.0115-00.7024-0.02760.03080.385-0.01170.5034-53.77283.6562-18.1544
360.0025-0.00330.00130.00610.00230.0030.0636-0.0024-0.0270.05060.0076-0.04820.03710.02200.34250.1540.01250.6039-0.01050.567-59.923-2.5681-8.5465
370.00370.0001-0.0020.0025-0.00030.0009-0.0510.05350.1089-0.0296-0.0329-0.0378-0.0587-0.0131-00.8899-0.0069-0.36510.92980.23511.2409-59.106613.9206-17.6312
380.0266-0.00240.0030.0005-0.00090.0014-0.13960.01770.1157-0.0207-0.10840.04860.0073-0.0927-00.48050.0636-0.10590.34470.06140.783-61.76942.9956-17.8225
390.01860.0114-0.01260.0076-0.00450.0043-0.2536-0.05970.0836-0.0388-0.0858-0.1033-0.00350.0181-00.27560.0273-0.03010.29470.08090.26-46.2678-14.4849-11.0528
400.00140.02720.0238-0.00040.03180.04530.0393-0.1055-0.0471-0.04620.07130.1676-0.0751-0.0162-00.39250.0098-0.02250.32320.04460.3461-50.0531-16.925-13.4818
410.0035-0.01380.00890.0098-0.00630.00020.06350.0772-0.1083-0.077-0.02590.18470.0515-0.032900.34540.0124-0.00720.38380.04950.3492-53.9745-15.7074-5.3307
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 66 )A1 - 66
2X-RAY DIFFRACTION2chain 'A' and (resid 67 through 98 )A67 - 98
3X-RAY DIFFRACTION3chain 'A' and (resid 99 through 166 )A99 - 166
4X-RAY DIFFRACTION4chain 'A' and (resid 167 through 265 )A167 - 265
5X-RAY DIFFRACTION5chain 'A' and (resid 266 through 309 )A266 - 309
6X-RAY DIFFRACTION6chain 'B' and (resid 13 through 19 )B13 - 19
7X-RAY DIFFRACTION7chain 'B' and (resid 20 through 41 )B20 - 41
8X-RAY DIFFRACTION8chain 'B' and (resid 42 through 57 )B42 - 57
9X-RAY DIFFRACTION9chain 'B' and (resid 58 through 85 )B58 - 85
10X-RAY DIFFRACTION10chain 'B' and (resid 86 through 92 )B86 - 92
11X-RAY DIFFRACTION11chain 'B' and (resid 93 through 101 )B93 - 101
12X-RAY DIFFRACTION12chain 'B' and (resid 102 through 143 )B102 - 143
13X-RAY DIFFRACTION13chain 'B' and (resid 144 through 153 )B144 - 153
14X-RAY DIFFRACTION14chain 'C' and (resid 1 through 32 )C1 - 32
15X-RAY DIFFRACTION15chain 'C' and (resid 33 through 52 )C33 - 52
16X-RAY DIFFRACTION16chain 'C' and (resid 53 through 106 )C53 - 106
17X-RAY DIFFRACTION17chain 'C' and (resid 107 through 149 )C107 - 149
18X-RAY DIFFRACTION18chain 'C' and (resid 150 through 195 )C150 - 195
19X-RAY DIFFRACTION19chain 'C' and (resid 196 through 236 )C196 - 236
20X-RAY DIFFRACTION20chain 'C' and (resid 237 through 265 )C237 - 265
21X-RAY DIFFRACTION21chain 'C' and (resid 266 through 309 )C266 - 309
22X-RAY DIFFRACTION22chain 'D' and (resid 16 through 26 )D16 - 26
23X-RAY DIFFRACTION23chain 'D' and (resid 27 through 74 )D27 - 74
24X-RAY DIFFRACTION24chain 'D' and (resid 75 through 84 )D75 - 84
25X-RAY DIFFRACTION25chain 'D' and (resid 85 through 93 )D85 - 93
26X-RAY DIFFRACTION26chain 'D' and (resid 94 through 123 )D94 - 123
27X-RAY DIFFRACTION27chain 'D' and (resid 124 through 153 )D124 - 153
28X-RAY DIFFRACTION28chain 'E' and (resid 1 through 87 )E1 - 87
29X-RAY DIFFRACTION29chain 'E' and (resid 88 through 166 )E88 - 166
30X-RAY DIFFRACTION30chain 'E' and (resid 167 through 265 )E167 - 265
31X-RAY DIFFRACTION31chain 'E' and (resid 266 through 310 )E266 - 310
32X-RAY DIFFRACTION32chain 'F' and (resid 11 through 32 )F11 - 32
33X-RAY DIFFRACTION33chain 'F' and (resid 33 through 50 )F33 - 50
34X-RAY DIFFRACTION34chain 'F' and (resid 51 through 62 )F51 - 62
35X-RAY DIFFRACTION35chain 'F' and (resid 63 through 74 )F63 - 74
36X-RAY DIFFRACTION36chain 'F' and (resid 75 through 81 )F75 - 81
37X-RAY DIFFRACTION37chain 'F' and (resid 82 through 89 )F82 - 89
38X-RAY DIFFRACTION38chain 'F' and (resid 90 through 101 )F90 - 101
39X-RAY DIFFRACTION39chain 'F' and (resid 102 through 114 )F102 - 114
40X-RAY DIFFRACTION40chain 'F' and (resid 115 through 143 )F115 - 143
41X-RAY DIFFRACTION41chain 'F' and (resid 144 through 153 )F144 - 153

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