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- PDB-6lpi: Crystal Structure of AHAS holo-enzyme -

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Basic information

Entry
Database: PDB / ID: 6lpi
TitleCrystal Structure of AHAS holo-enzyme
Components(Acetolactate synthase isozyme 1 ...) x 2
KeywordsRECOMBINATION / AHAS / allosteric regulation
Function / homology
Function and homology information


acetolactate synthase regulator activity / acetolactate synthase / acetolactate synthase complex / branched-chain amino acid biosynthetic process / acetolactate synthase activity / valine biosynthetic process / isoleucine biosynthetic process / thiamine pyrophosphate binding / amino acid biosynthetic process / flavin adenine dinucleotide binding ...acetolactate synthase regulator activity / acetolactate synthase / acetolactate synthase complex / branched-chain amino acid biosynthetic process / acetolactate synthase activity / valine biosynthetic process / isoleucine biosynthetic process / thiamine pyrophosphate binding / amino acid biosynthetic process / flavin adenine dinucleotide binding / magnesium ion binding / cytosol
Similarity search - Function
Acetolactate synthase, small subunit / AHAS, ACT domain / Acetolactate synthase, large subunit, biosynthetic / Acetolactate synthase large subunit, TPP binding domain / ACT domain / TPP-binding enzyme, conserved site / Thiamine pyrophosphate enzymes signature. / ACT domain profile. / ACT domain / Thiamine pyrophosphate enzyme, central domain ...Acetolactate synthase, small subunit / AHAS, ACT domain / Acetolactate synthase, large subunit, biosynthetic / Acetolactate synthase large subunit, TPP binding domain / ACT domain / TPP-binding enzyme, conserved site / Thiamine pyrophosphate enzymes signature. / ACT domain profile. / ACT domain / Thiamine pyrophosphate enzyme, central domain / Thiamine pyrophosphate enzyme, central domain / ACT-like domain / Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain / Thiamine pyrophosphate enzyme, N-terminal TPP binding domain / Thiamine pyrophosphate enzyme, C-terminal TPP-binding / Thiamine pyrophosphate enzyme, C-terminal TPP binding domain / Thiamin diphosphate-binding fold / DHS-like NAD/FAD-binding domain superfamily
Similarity search - Domain/homology
FLAVIN-ADENINE DINUCLEOTIDE / THIAMINE DIPHOSPHATE / Acetolactate synthase isozyme 1 large subunit / Acetolactate synthase isozyme 1 small subunit
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.849 Å
AuthorsZhang, Y. / Yang, X. / Xi, Z. / Shen, Y.
CitationJournal: Biochem.J. / Year: 2020
Title: Molecular architecture of the acetohydroxyacid synthase holoenzyme.
Authors: Zhang, Y. / Li, Y. / Liu, X. / Sun, J. / Li, X. / Lin, J. / Yang, X. / Xi, Z. / Shen, Y.
History
DepositionJan 10, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 18, 2020Provider: repository / Type: Initial release
Revision 1.1Nov 29, 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
E: Acetolactate synthase isozyme 1 small subunit
A: Acetolactate synthase isozyme 1 large subunit
F: Acetolactate synthase isozyme 1 small subunit
B: Acetolactate synthase isozyme 1 large subunit
G: Acetolactate synthase isozyme 1 small subunit
C: Acetolactate synthase isozyme 1 large subunit
H: Acetolactate synthase isozyme 1 small subunit
D: Acetolactate synthase isozyme 1 large subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)301,48720
Polymers296,5478
Non-polymers4,94112
Water905
1
E: Acetolactate synthase isozyme 1 small subunit
A: Acetolactate synthase isozyme 1 large subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,3725
Polymers74,1372
Non-polymers1,2353
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
F: Acetolactate synthase isozyme 1 small subunit
B: Acetolactate synthase isozyme 1 large subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,3725
Polymers74,1372
Non-polymers1,2353
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
G: Acetolactate synthase isozyme 1 small subunit
C: Acetolactate synthase isozyme 1 large subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,3725
Polymers74,1372
Non-polymers1,2353
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
H: Acetolactate synthase isozyme 1 small subunit
D: Acetolactate synthase isozyme 1 large subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,3725
Polymers74,1372
Non-polymers1,2353
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)111.173, 104.577, 118.535
Angle α, β, γ (deg.)90.000, 105.680, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and ((resid 11 through 12 and (name N...
21(chain B and (resid 11 through 28 or resid 30...
31(chain C and (resid 11 through 28 or resid 30...
41(chain D and (resid 11 through 28 or resid 30...

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
11LYSLYSARGARG(chain A and ((resid 11 through 12 and (name N...AB11 - 1211 - 12
12LYSLYSTPPTPP(chain A and ((resid 11 through 12 and (name N...AB - J11 - 60211
13LYSLYSTPPTPP(chain A and ((resid 11 through 12 and (name N...AB - J11 - 60211
14LYSLYSTPPTPP(chain A and ((resid 11 through 12 and (name N...AB - J11 - 60211
15LYSLYSTPPTPP(chain A and ((resid 11 through 12 and (name N...AB - J11 - 60211
21LYSLYSILEILE(chain B and (resid 11 through 28 or resid 30...BD11 - 2811 - 28
22ILEILESERSER(chain B and (resid 11 through 28 or resid 30...BD30 - 4730 - 47
23SERSERILEILE(chain B and (resid 11 through 28 or resid 30...BD49 - 5249 - 52
24SERSERTPPTPP(chain B and (resid 11 through 28 or resid 30...BD - M8 - 6028
25SERSERTPPTPP(chain B and (resid 11 through 28 or resid 30...BD - M8 - 6028
26SERSERTPPTPP(chain B and (resid 11 through 28 or resid 30...BD - M8 - 6028
27SERSERTPPTPP(chain B and (resid 11 through 28 or resid 30...BD - M8 - 6028
28SERSERTPPTPP(chain B and (resid 11 through 28 or resid 30...BD - M8 - 6028
29SERSERTPPTPP(chain B and (resid 11 through 28 or resid 30...BD - M8 - 6028
31LYSLYSILEILE(chain C and (resid 11 through 28 or resid 30...CF11 - 2811 - 28
32ILEILESERSER(chain C and (resid 11 through 28 or resid 30...CF30 - 4730 - 47
33SERSERILEILE(chain C and (resid 11 through 28 or resid 30...CF49 - 5249 - 52
34HISHISSERSER(chain C and (resid 11 through 28 or resid 30...CF54 - 11554 - 115
35GLUGLUGLUGLU(chain C and (resid 11 through 28 or resid 30...CF124124
36LYSLYSTPPTPP(chain C and (resid 11 through 28 or resid 30...CF - P11 - 60211
37LYSLYSTPPTPP(chain C and (resid 11 through 28 or resid 30...CF - P11 - 60211
38LYSLYSTPPTPP(chain C and (resid 11 through 28 or resid 30...CF - P11 - 60211
39LYSLYSTPPTPP(chain C and (resid 11 through 28 or resid 30...CF - P11 - 60211
41LYSLYSILEILE(chain D and (resid 11 through 28 or resid 30...DH11 - 2811 - 28
42ILEILESERSER(chain D and (resid 11 through 28 or resid 30...DH30 - 4730 - 47
43SERSERILEILE(chain D and (resid 11 through 28 or resid 30...DH49 - 5249 - 52
44HISHISSERSER(chain D and (resid 11 through 28 or resid 30...DH54 - 11554 - 115
45GLUGLUGLUGLU(chain D and (resid 11 through 28 or resid 30...DH124124
46LYSLYSTPPTPP(chain D and (resid 11 through 28 or resid 30...DH - S11 - 60211
47LYSLYSTPPTPP(chain D and (resid 11 through 28 or resid 30...DH - S11 - 60211
48LYSLYSTPPTPP(chain D and (resid 11 through 28 or resid 30...DH - S11 - 60211
49LYSLYSTPPTPP(chain D and (resid 11 through 28 or resid 30...DH - S11 - 60211

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Components

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Acetolactate synthase isozyme 1 ... , 2 types, 8 molecules EFGHABCD

#1: Protein
Acetolactate synthase isozyme 1 small subunit / Acetohydroxy-acid synthase I small subunit / ALS-I


Mass: 13640.341 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: ilvN, b3670, JW3645 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P0ADF8, acetolactate synthase
#2: Protein
Acetolactate synthase isozyme 1 large subunit / AHAS-I / Acetohydroxy-acid synthase I large subunit / ALS-I


Mass: 60496.316 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (strain K12) (bacteria)
Strain: K12 / Gene: ilvB, b3671, JW3646 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P08142, acetolactate synthase

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Non-polymers , 4 types, 17 molecules

#3: Chemical
ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: FAD*YM
#4: Chemical
ChemComp-TPP / THIAMINE DIPHOSPHATE


Mass: 425.314 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C12H19N4O7P2S / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg / Feature type: SUBJECT OF INVESTIGATION
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.38 Å3/Da / Density % sol: 48.39 %
Crystal growTemperature: 293 K / Method: evaporation / Details: Tris-HCl, MgCl2, PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.9791 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: May 28, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionResolution: 2.849→50 Å / Num. obs: 60768 / % possible obs: 96.11 % / Redundancy: 6.2 % / Rsym value: 0.157 / Net I/σ(I): 17.9
Reflection shellResolution: 2.85→2.96 Å / Num. unique obs: 5694 / Rsym value: 0.75

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Processing

Software
NameVersionClassification
PHENIXdev_2666refinement
PDB_EXTRACT3.25data extraction
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1JSC, 2LVW

1jsc

2lvw


Resolution: 2.849→35.929 Å / SU ML: 0.34 / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 24.56
RfactorNum. reflection% reflection
Rfree0.2433 1947 3.31 %
Rwork0.1673 --
obs0.1697 58894 96.17 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 170.2 Å2 / Biso mean: 63.9853 Å2 / Biso min: 17.96 Å2
Refinement stepCycle: final / Resolution: 2.849→35.929 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms18515 0 320 5 18840
Biso mean--55.75 41.45 -
Num. residues----2486
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00919215
X-RAY DIFFRACTIONf_angle_d1.30226221
X-RAY DIFFRACTIONf_chiral_restr0.073051
X-RAY DIFFRACTIONf_plane_restr0.0093387
X-RAY DIFFRACTIONf_dihedral_angle_d7.611456
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A9117X-RAY DIFFRACTION13.944TORSIONAL
12B9117X-RAY DIFFRACTION13.944TORSIONAL
13C9117X-RAY DIFFRACTION13.944TORSIONAL
14D9117X-RAY DIFFRACTION13.944TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.8494-2.92070.30511140.2293341081
2.9207-2.99960.32561260.2245386391
2.9996-3.08780.32931390.2116386392
3.0878-3.18740.29921310.1956394294
3.1874-3.30130.23811410.1877405496
3.3013-3.43330.25251310.181410797
3.4333-3.58950.29261560.1821415098
3.5895-3.77850.25761270.1617413999
3.7785-4.0150.22071520.1529419099
4.015-4.32450.21791400.14424207100
4.3245-4.75880.20671460.13514215100
4.7588-5.44530.21971480.14844263100
5.4453-6.85280.27661460.19064241100
6.8528-35.9290.20931500.1621430399
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)
15.6586-0.88993.92643.465-4.86568.75150.08890.46650.0406-0.3704-0.0856-0.31080.3815-0.3148-0.07240.3305-0.0750.01530.22160.00560.341913.001-12.99634.0674
26.75482.67614.24886.2592-0.64513.7869-0.4081-0.59660.03590.0962-0.08820.1293-0.3347-0.24290.54930.27520.010.10350.47560.00490.25069.6242-12.681514.0059
39.11840.9546-7.1882.1371.61588.6244-0.0453-1.0076-1.52010.4347-0.679-0.86870.32991.05860.54040.4098-0.00660.01840.72590.2040.359720.1431-13.934315.4966
42.11862.08611.93879.02794.26732.61270.0130.74820.9204-1.4066-0.44130.5043-0.0057-1.00350.47360.42080.0526-0.04860.89780.13780.355411.7095-6.3214-2.5313
56.30444.0585-4.62649.1813-1.04595.2015-0.03060.9381-0.36460.148-0.6937-1.14490.03890.51610.01650.30280.02020.06910.51780.05910.391118.6035-15.43436.6247
69.37096.5963-5.65998.2112-1.40015.9671-0.11880.3346-0.5419-0.0484-0.0393-0.16060.027-0.16980.32030.31780.0418-0.03980.3662-0.00650.402413.4137-20.2086.13
74.629-2.31223.55682.4284-3.35486.06160.3304-0.0623-0.2519-1.4655-0.89-0.5339-0.46770.04270.51270.4335-0.02370.08430.51720.04610.475327.981-3.99033.902
82.0758-1.0917-0.45741.6722-0.36771.6392-0.01320.1746-0.1726-0.36530.11120.7887-0.019-0.2978-0.05430.3339-0.033-0.14480.39680.14690.6989-17.2283-15.194315.9672
93.973-2.25390.92913.28130.12232.5737-0.00170.639-0.0893-0.42330.03420.3673-0.30270.1990.04540.2917-0.0985-0.11050.50220.1640.4739-8.3987-10.71398.6484
102.0353-3.21490.74754.9359-1.34790.08670.41720.9365-0.5901-0.8811-0.44780.6040.2130.07240.05130.53280.0671-0.1250.6296-0.17850.83920.9694-38.77865.1115
112.5948-0.6345-1.36152.8251-0.10672.4568-0.1506-0.054-0.72780.30370.07850.67470.1553-0.05120.08870.2448-0.01060.01930.34090.1310.67433.4781-43.138125.28
122.7635-0.6319-0.73122.17-0.77330.4739-0.1035-0.2284-0.98940.07440.1230.48960.2744-0.13050.02010.4307-0.0301-0.01050.4040.08430.72881.1744-44.882725.0124
132.9648-0.12420.6162.71850.86981.2482-0.0627-0.5732-0.42110.38860.1340.77910.1168-0.1192-0.07770.38210.06250.14890.47380.23640.6391-12.4963-27.163236.3603
141.0564-1.30420.39371.80510.74041.81120.0636-0.6077-0.24010.11430.20010.33730.0807-0.0523-0.26220.45090.06980.18790.72810.35010.8475-15.1785-30.77643.2105
156.7246-2.4209-3.41188.52145.4824.4848-0.11140.49410.13020.0212-0.14320.1172-0.3773-0.19860.40010.44920.05530.03550.54020.15580.275638.18684.4798-20.1043
166.59341.3912.27444.07620.33841.73230.16040.19550.2696-0.2185-0.01010.2132-0.60780.3402-0.03540.4505-0.07360.03210.45830.07130.206748.73764.9307-20.2951
176.2771.4997-2.0323.3371-1.97823.1692-0.9135-0.23980.1669-1.08060.5009-0.0403-1.40050.6930.24580.6614-0.16380.02360.72060.00820.256943.83366.466-13.7256
181.99522.34776.02127.87183.4959.80240.19290.0632-2.3994-0.51760.8335-0.10961.2127-3.2461-0.84940.4798-0.10920.04361.12040.28010.609929.8066-4.8876-24.1696
197.7093-1.14932.13557.08272.85318.1266-0.80840.7229-0.28690.20480.91490.6072-0.8707-1.2401-0.30550.4745-0.07790.03030.59770.15310.276536.82314.622-16.5457
205.7389-5.4165-2.91665.4223.91325.8492-0.22930.40172.20361.16381.6996-0.9324-3.70310.6417-1.10641.2458-0.11910.07390.5336-0.05431.15143.246620.036-11.1256
219.15720.0105-3.83295.61654.57925.7879-0.3836-0.03491.211-2.36330.45080.2881-1.60230.41760.11560.9941-0.0844-0.07860.43870.15830.430943.503813.6257-23.5819
228.8876-0.8405-6.55662.29750.05844.9490.21760.83880.53670.26120.31290.6427-0.0818-0.8541-0.43520.54440.07970.08590.61120.13930.482633.099910.9422-17.1999
231.8918-1.972-0.36242.44370.55920.1543-0.0371-0.29780.31570.59511.33850.5456-1.1346-0.3766-1.06750.68950.01010.21670.80610.12090.412435.6540.9104-2.2111
242.00310.71830.16072.0850.80461.2022-0.25670.51380.0088-0.41760.37930.17070.3202-0.3478-0.09440.4739-0.176-0.02280.62320.01250.207655.6351-2.5408-41.9016
252.19380.28070.30413.54590.33562.134-0.15020.15910.3502-0.03660.23090.7756-0.0239-0.95850.00710.3692-0.099-0.00160.8410.05110.413644.23177.6192-40.7969
263.7908-0.30260.51372.91581.26741.3804-0.34070.36031.408-0.47120.08750.1579-0.5276-0.24090.17170.5117-0.0215-0.13940.55420.17390.776162.493629.0442-40.2061
272.45410.07740.07672.74010.0163.216-0.16970.44150.5714-0.30910.28-0.5351-0.50890.4273-0.03790.4212-0.14150.06950.58050.06240.540581.383214.414-41.359
287.6712-4.66593.45918.6897-2.75915.2609-0.62620.53070.55960.105-0.233-0.7852-0.0675-0.61520.60320.3174-0.13280.13720.45480.07320.492317.93362.418514.0484
292.5632.16130.66946.0576-0.24628.50560.26520.66361.31350.7922-0.01680.5342-0.4572-0.2493-0.0880.3985-0.05220.08380.29910.11010.38637.6208-0.749314.8929
303.05550.4559-2.70334.16180.792.7449-0.27830.66810.8716-0.39070.0697-0.0306-0.5479-0.676-0.20260.47310.09290.0070.52140.16890.411113.35310.13767.0831
314.75871.7799-1.2226.09840.55426.91890.15450.28871.1367-0.04570.0153-0.0411-0.3576-0.619-0.16970.3446-0.04790.08190.43570.10210.524816.15366.844212.8364
326.1740.5529-5.43067.72552.66366.0584-0.63680.3936-0.3965-0.47451.0772-0.1464-0.8491-1.2021-0.27240.55260.1056-0.02210.79390.05290.339721.7798-1.3627-3.0216
332.3764-0.43940.52952.2482-0.80542.2015-0.0066-0.56590.14240.30590.0740.0920.03660.164-0.0740.30690.02390.01810.53050.03040.23075.8573-6.312237.1017
341.3941-0.1623-0.40761.87210.17890.6784-0.0896-0.1250.8374-0.02710.24640.303-0.20860.0235-0.14350.4789-0.00140.07060.44820.0420.9089-10.593216.104732.8512
351.9709-1.01940.70032.2199-0.7245.5591-0.1473-0.0930.32820.13530.08240.6118-0.5007-0.45360.03070.45230.04120.06720.48640.09820.9713-27.92330.538632.751
365.93414.3921-1.0363.8275-0.68285.87980.43930.0547-0.02121.04720.22710.3488-0.16540.2145-0.53930.4665-0.00610.10650.47340.04750.406948.883-5.3571-7.632
373.8547-0.67783.12346.95465.18167.366-0.65920.490.2307-0.04860.1977-0.12440.2072-0.44920.31540.4858-0.06980.18410.49270.19960.352151.6505-4.8174-17.1996
387.8407-5.3921-7.65657.94685.54917.4795-0.5260.2497-0.2851-0.73480.71250.02120.23070.6118-0.27070.6956-0.18060.09020.52-0.00210.246844.1593-7.1691-14.672
395.70116.05746.07476.56046.41316.5060.6718-0.7915-0.30321.6978-0.6172-0.04771.1424-0.16850.25780.6486-0.11530.080.5041-0.00060.378945.6073-5.6676-5.8103
404.36353.7578-1.84424.2567-0.37776.8079-0.93620.1663-0.8296-0.98660.27090.5517-0.21670.22550.50070.6533-0.00090.08440.47970.01330.439751.4994-17.2546-13.7384
414.41215.6932-4.67668.4186-5.10435.7898-0.3362-0.9234-0.7552-0.1593-0.2157-0.22070.66620.22030.45190.57960.00470.02950.43950.07210.400448.6688-10.9045-5.3455
424.903-4.29882.10424.2903-3.07183.7147-0.2230.9212-0.66580.4056-0.02460.93770.1621-0.58250.18960.3657-0.02990.10980.57920.03420.520330.8094-4.4558-9.0945
431.91430.6552-0.15023.13481.24853.22480.0048-0.4246-0.0150.27370.0821-0.51540.250.1707-0.08450.23960.0121-0.05370.3369-0.01380.302178.56251.5411-19.7032
443.19672.21851.20954.9601-0.35722.0690.0836-0.41120.28660.4912-0.170.1157-0.1717-0.25910.05870.3160.03880.04680.4146-0.03710.195567.99242.9473-13.9799
451.5508-0.5526-0.38054.41681.6743.1064-0.1625-0.1305-0.7662-0.07130.0239-0.13590.9381-0.01320.16640.71990.00330.11130.38320.09670.636771.7407-31.6448-19.0682
465.2343-0.29442.110.11550.58215.8338-0.1474-0.1151-0.0915-0.1068-0.0156-0.14720.3967-0.370.14180.8388-0.10070.02860.35010.10610.481762.7848-29.7993-17.5002
471.6329-0.2383-0.73052.4965-0.17581.3679-0.29930.5777-0.6476-0.61460.1046-0.70770.70260.0540.04930.7234-0.05220.2010.4184-0.15750.487578.443-19.2805-36.525
480.21191.2540.69155.03852.53822.0368-0.21250.6156-0.3819-0.25080.1837-0.190.1395-0.12120.01840.7192-0.01330.2020.7205-0.22840.670282.8623-17.735-43.889
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'E' and (resid 7 through 20 )E7 - 20
2X-RAY DIFFRACTION2chain 'E' and (resid 21 through 32 )E21 - 32
3X-RAY DIFFRACTION3chain 'E' and (resid 33 through 38 )E33 - 38
4X-RAY DIFFRACTION4chain 'E' and (resid 39 through 48 )E39 - 48
5X-RAY DIFFRACTION5chain 'E' and (resid 49 through 61 )E49 - 61
6X-RAY DIFFRACTION6chain 'E' and (resid 62 through 84 )E62 - 84
7X-RAY DIFFRACTION7chain 'E' and (resid 85 through 95 )E85 - 95
8X-RAY DIFFRACTION8chain 'A' and (resid 11 through 111 )A11 - 111
9X-RAY DIFFRACTION9chain 'A' and (resid 112 through 180 )A112 - 180
10X-RAY DIFFRACTION10chain 'A' and (resid 181 through 209 )A181 - 209
11X-RAY DIFFRACTION11chain 'A' and (resid 210 through 307 )A210 - 307
12X-RAY DIFFRACTION12chain 'A' and (resid 308 through 380 )A308 - 380
13X-RAY DIFFRACTION13chain 'A' and (resid 381 through 499 )A381 - 499
14X-RAY DIFFRACTION14chain 'A' and (resid 500 through 560 )A500 - 560
15X-RAY DIFFRACTION15chain 'F' and (resid 8 through 20 )F8 - 20
16X-RAY DIFFRACTION16chain 'F' and (resid 21 through 31 )F21 - 31
17X-RAY DIFFRACTION17chain 'F' and (resid 32 through 43 )F32 - 43
18X-RAY DIFFRACTION18chain 'F' and (resid 44 through 48 )F44 - 48
19X-RAY DIFFRACTION19chain 'F' and (resid 49 through 56 )F49 - 56
20X-RAY DIFFRACTION20chain 'F' and (resid 57 through 61 )F57 - 61
21X-RAY DIFFRACTION21chain 'F' and (resid 62 through 74 )F62 - 74
22X-RAY DIFFRACTION22chain 'F' and (resid 75 through 84 )F75 - 84
23X-RAY DIFFRACTION23chain 'F' and (resid 85 through 96 )F85 - 96
24X-RAY DIFFRACTION24chain 'B' and (resid 8 through 143 )B8 - 143
25X-RAY DIFFRACTION25chain 'B' and (resid 144 through 209 )B144 - 209
26X-RAY DIFFRACTION26chain 'B' and (resid 210 through 437 )B210 - 437
27X-RAY DIFFRACTION27chain 'B' and (resid 438 through 560 )B438 - 560
28X-RAY DIFFRACTION28chain 'G' and (resid 8 through 20 )G8 - 20
29X-RAY DIFFRACTION29chain 'G' and (resid 21 through 32 )G21 - 32
30X-RAY DIFFRACTION30chain 'G' and (resid 33 through 43 )G33 - 43
31X-RAY DIFFRACTION31chain 'G' and (resid 44 through 84 )G44 - 84
32X-RAY DIFFRACTION32chain 'G' and (resid 85 through 95 )G85 - 95
33X-RAY DIFFRACTION33chain 'C' and (resid 11 through 176 )C11 - 176
34X-RAY DIFFRACTION34chain 'C' and (resid 177 through 470 )C177 - 470
35X-RAY DIFFRACTION35chain 'C' and (resid 471 through 560 )C471 - 560
36X-RAY DIFFRACTION36chain 'H' and (resid 8 through 20 )H8 - 20
37X-RAY DIFFRACTION37chain 'H' and (resid 21 through 31 )H21 - 31
38X-RAY DIFFRACTION38chain 'H' and (resid 32 through 43 )H32 - 43
39X-RAY DIFFRACTION39chain 'H' and (resid 44 through 59 )H44 - 59
40X-RAY DIFFRACTION40chain 'H' and (resid 60 through 71 )H60 - 71
41X-RAY DIFFRACTION41chain 'H' and (resid 72 through 84 )H72 - 84
42X-RAY DIFFRACTION42chain 'H' and (resid 85 through 95 )H85 - 95
43X-RAY DIFFRACTION43chain 'D' and (resid 11 through 101 )D11 - 101
44X-RAY DIFFRACTION44chain 'D' and (resid 102 through 180 )D102 - 180
45X-RAY DIFFRACTION45chain 'D' and (resid 181 through 275 )D181 - 275
46X-RAY DIFFRACTION46chain 'D' and (resid 276 through 337 )D276 - 337
47X-RAY DIFFRACTION47chain 'D' and (resid 338 through 499 )D338 - 499
48X-RAY DIFFRACTION48chain 'D' and (resid 500 through 560 )D500 - 560

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