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- PDB-6esz: Crystal structure of PqsBC from Pseudomonas aeruginosa (crystal f... -

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Basic information

Entry
Database: PDB / ID: 6esz
TitleCrystal structure of PqsBC from Pseudomonas aeruginosa (crystal form 1)
Components
  • PqsB
  • PqsC
KeywordsTRANSFERASE / Pseudomonas Quinolone Signal / FabH / HHQ
Function / homology
Function and homology information


2-heptyl-4(1H)-quinolone synthase / secondary metabolite biosynthetic process / acyltransferase activity / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / cytoplasm
Similarity search - Function
3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III / 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III / 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III, C-terminal / 3-Oxoacyl-[acyl-carrier-protein (ACP)] synthase III C terminal / Thiolase/Chalcone synthase / Peroxisomal Thiolase; Chain A, domain 1 / Thiolase-like / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / 2-heptyl-4(1H)-quinolone synthase subunit PqsC / 2-heptyl-4(1H)-quinolone synthase subunit PqsB
Similarity search - Component
Biological speciesPseudomonas aeruginosa PAO1 (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.84 Å
AuthorsWitzgall, F. / Blankenfeldt, W.
CitationJournal: Chembiochem / Year: 2018
Title: The Alkylquinolone Repertoire of Pseudomonas aeruginosa is Linked to Structural Flexibility of the FabH-like 2-Heptyl-3-hydroxy-4(1H)-quinolone (PQS) Biosynthesis Enzyme PqsBC.
Authors: Witzgall, F. / Depke, T. / Hoffmann, M. / Empting, M. / Bronstrup, M. / Muller, R. / Blankenfeldt, W.
History
DepositionOct 25, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 4, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 24, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_id_ISSN / _citation.journal_volume ..._citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Jan 17, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / 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
Revision 1.3Nov 13, 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: PqsC
B: PqsB
C: PqsC
D: PqsB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,58921
Polymers141,8354
Non-polymers1,75417
Water21,8341212
1
A: PqsC
B: PqsB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,93312
Polymers70,9182
Non-polymers1,01510
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6770 Å2
ΔGint-133 kcal/mol
Surface area23460 Å2
MethodPISA
2
C: PqsC
D: PqsB
hetero molecules


Theoretical massNumber of molelcules
Total (without water)71,6569
Polymers70,9182
Non-polymers7397
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6050 Å2
ΔGint-94 kcal/mol
Surface area22990 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.989, 142.384, 171.121
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and ((resid -5 and (name N or name...
21(chain C and (resid -5 through -3 or resid -1...
12(chain B and (resid 1 through 15 or resid 17...
22(chain D and (resid 1 through 15 or resid 17...

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
111LEULEULEULEU(chain A and ((resid -5 and (name N or name...AA-512
121HISHISCYSCYS(chain A and ((resid -5 and (name N or name...AA-10 - 3487 - 365
131HISHISCYSCYS(chain A and ((resid -5 and (name N or name...AA-10 - 3487 - 365
141HISHISCYSCYS(chain A and ((resid -5 and (name N or name...AA-10 - 3487 - 365
151HISHISCYSCYS(chain A and ((resid -5 and (name N or name...AA-10 - 3487 - 365
161HISHISCYSCYS(chain A and ((resid -5 and (name N or name...AA-10 - 3487 - 365
211LEULEUPHEPHE(chain C and (resid -5 through -3 or resid -1...CC-5 - -312 - 14
221GLYGLYPROPRO(chain C and (resid -5 through -3 or resid -1...CC-1 - 2316 - 40
231PHEPHEARGARG(chain C and (resid -5 through -3 or resid -1...CC25 - 6842 - 85
241SERSERTHRTHR(chain C and (resid -5 through -3 or resid -1...CC70 - 9087 - 107
251ALAALAASNASN(chain C and (resid -5 through -3 or resid -1...CC92 - 109109 - 126
261LEULEUSERSER(chain C and (resid -5 through -3 or resid -1...CC111 - 112128 - 129
271GLNGLNSERSER(chain C and (resid -5 through -3 or resid -1...CC114 - 125131 - 142
281METMETGLUGLU(chain C and (resid -5 through -3 or resid -1...CC127 - 128144 - 145
291ALAALASERSER(chain C and (resid -5 through -3 or resid -1...CC130 - 141147 - 158
2101ILEILEGLYGLY(chain C and (resid -5 through -3 or resid -1...CC143 - 176160 - 193
2111ALAALASERSER(chain C and (resid -5 through -3 or resid -1...CC178 - 228195 - 245
2121PHEPHESERSER(chain C and (resid -5 through -3 or resid -1...CC230 - 231247 - 248
2131LYSLYSPROPRO(chain C and (resid -5 through -3 or resid -1...CC236 - 242253 - 259
2141ASNASNALAALA(chain C and (resid -5 through -3 or resid -1...CC244 - 248261 - 265
2151ARGARGGLUGLU(chain C and (resid -5 through -3 or resid -1...CC250 - 254267 - 271
2161ALAALAVALVAL(chain C and (resid -5 through -3 or resid -1...CC256 - 276273 - 293
2171ALAALAPROPRO(chain C and (resid -5 through -3 or resid -1...CC278 - 287295 - 304
2181GLNGLNMETMET(chain C and (resid -5 through -3 or resid -1...CC289 - 310306 - 327
2191GLYGLYLEULEU(chain C and (resid -5 through -3 or resid -1...CC312 - 313329 - 330
2201GLUGLUASPASP(chain C and (resid -5 through -3 or resid -1...CC315 - 322332 - 339
2211ILEILECYSCYS(chain C and (resid -5 through -3 or resid -1...CC324 - 348341 - 365
112METMETVALVAL(chain B and (resid 1 through 15 or resid 17...BB1 - 151 - 15
122LEULEULEULEU(chain B and (resid 1 through 15 or resid 17...BB1717
132GLYGLYASPASP(chain B and (resid 1 through 15 or resid 17...BB19 - 3119 - 31
142METMETLEULEU(chain B and (resid 1 through 15 or resid 17...BB33 - 4633 - 46
152GLUGLUVALVAL(chain B and (resid 1 through 15 or resid 17...BB48 - 5148 - 51
162PROPROPROPRO(chain B and (resid 1 through 15 or resid 17...BB5353
172GLUGLUGLUGLU(chain B and (resid 1 through 15 or resid 17...BB5555
182ASPASPILEILE(chain B and (resid 1 through 15 or resid 17...BB57 - 7057 - 70
192ASNASNALAALA(chain B and (resid 1 through 15 or resid 17...BB72 - 7772 - 77
1102LYSLYSSERSER(chain B and (resid 1 through 15 or resid 17...BB79 - 10279 - 102
1112ALAALAASPASP(chain B and (resid 1 through 15 or resid 17...BB104 - 116104 - 116
1122GLYGLYASNASN(chain B and (resid 1 through 15 or resid 17...BB118 - 121118 - 121
1132VALVALVALVAL(chain B and (resid 1 through 15 or resid 17...BB124 - 125124 - 125
1142GLYGLYASPASP(chain B and (resid 1 through 15 or resid 17...BB127 - 136127 - 136
1152SERSERGLYGLY(chain B and (resid 1 through 15 or resid 17...BB139 - 156139 - 156
1162ALAALAILEILE(chain B and (resid 1 through 15 or resid 17...BB158 - 184158 - 184
1172GLNGLNPROPRO(chain B and (resid 1 through 15 or resid 17...BB186 - 203186 - 203
1182ALAALAVALVAL(chain B and (resid 1 through 15 or resid 17...BB205 - 206205 - 206
1192ALAALAVALVAL(chain B and (resid 1 through 15 or resid 17...BB208 - 223208 - 223
1202GLUGLUGLUGLU(chain B and (resid 1 through 15 or resid 17...BB225225
1212TRPTRPGLYGLY(chain B and (resid 1 through 15 or resid 17...BB227 - 239227 - 239
1222PHEPHEALAALA(chain B and (resid 1 through 15 or resid 17...BB241 - 250241 - 250
1232ARGARGGLYGLY(chain B and (resid 1 through 15 or resid 17...BB252 - 279252 - 279
212METMETVALVAL(chain D and (resid 1 through 15 or resid 17...DD1 - 151 - 15
222LEULEULEULEU(chain D and (resid 1 through 15 or resid 17...DD1717
232GLYGLYASPASP(chain D and (resid 1 through 15 or resid 17...DD19 - 3119 - 31
242METMETLEULEU(chain D and (resid 1 through 15 or resid 17...DD33 - 4633 - 46
252GLUGLUVALVAL(chain D and (resid 1 through 15 or resid 17...DD48 - 5148 - 51
262PROPROPROPRO(chain D and (resid 1 through 15 or resid 17...DD5353
272GLUGLUGLUGLU(chain D and (resid 1 through 15 or resid 17...DD5555
282ASPASPILEILE(chain D and (resid 1 through 15 or resid 17...DD57 - 7057 - 70
292ASNASNALAALA(chain D and (resid 1 through 15 or resid 17...DD72 - 7772 - 77
2102LYSLYSSERSER(chain D and (resid 1 through 15 or resid 17...DD79 - 10279 - 102
2112ALAALAASPASP(chain D and (resid 1 through 15 or resid 17...DD104 - 116104 - 116
2122GLYGLYTYRTYR(chain D and (resid 1 through 15 or resid 17...DD118 - 119118 - 119
2132ARGARGARGARG(chain D and (resid 1 through 15 or resid 17...DD120120
2142METMETALAALA(chain D and (resid 1 through 15 or resid 17...DD1 - 2831 - 283
2152METMETALAALA(chain D and (resid 1 through 15 or resid 17...DD1 - 2831 - 283
2162METMETALAALA(chain D and (resid 1 through 15 or resid 17...DD1 - 2831 - 283
2172METMETALAALA(chain D and (resid 1 through 15 or resid 17...DD1 - 2831 - 283
2182METMETALAALA(chain D and (resid 1 through 15 or resid 17...DD1 - 2831 - 283
2192METMETALAALA(chain D and (resid 1 through 15 or resid 17...DD1 - 2831 - 283

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein PqsC


Mass: 40385.840 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria) / Gene: pqsC, PA0998 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9I4X1
#2: Protein PqsB


Mass: 30531.760 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa PAO1 (bacteria) / Gene: pqsB, PA0997 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9I4X2

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Non-polymers , 4 types, 1229 molecules

#3: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: SO4
#4: Chemical
ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C6H14O2 / Comment: precipitant*YM
#5: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H10O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1212 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.69 Å3/Da / Density % sol: 54.28 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.6
Details: 0.1 M Bis-Tris (pH 6.6), 0.2 M Lithium sulfate, 16% PEG 3350, 5% MPD

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Nov 4, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.84→47.46 Å / Num. obs: 132059 / % possible obs: 100 % / Redundancy: 8.2 % / Biso Wilson estimate: 19.37 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.12 / Rpim(I) all: 0.044 / Rrim(I) all: 0.128 / Net I/σ(I): 14.1
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
1.84-1.877.91.06665390.8060.4041.142100
10.08-47.467.30.0279290.9990.0110.02999.2

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Processing

Software
NameVersionClassification
PHENIXdev_2875refinement
Aimless0.5.17data scaling
PDB_EXTRACT3.22data extraction
Cootmodel building
PHASERphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6ET1

6et1


Resolution: 1.84→47.343 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 19.34
RfactorNum. reflection% reflection
Rfree0.1786 6454 4.89 %
Rwork0.1495 --
obs0.151 131871 99.91 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 155.54 Å2 / Biso mean: 33.2446 Å2 / Biso min: 11.56 Å2
Refinement stepCycle: final / Resolution: 1.84→47.343 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9721 0 182 1212 11115
Biso mean--62.39 39.87 -
Num. residues----1271
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00710400
X-RAY DIFFRACTIONf_angle_d0.82914225
X-RAY DIFFRACTIONf_chiral_restr0.0541578
X-RAY DIFFRACTIONf_plane_restr0.0061875
X-RAY DIFFRACTIONf_dihedral_angle_d14.4526391
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3788X-RAY DIFFRACTION5.264TORSIONAL
12C3788X-RAY DIFFRACTION5.264TORSIONAL
21B2818X-RAY DIFFRACTION5.264TORSIONAL
22D2818X-RAY DIFFRACTION5.264TORSIONAL
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 (%)
1.84-1.86090.32332310.263541364367100
1.8609-1.88280.29412050.245741494354100
1.8828-1.90580.27662390.25674067430699
1.9058-1.92990.31542120.27574121433399
1.9299-1.95530.25761670.23441694336100
1.9553-1.98210.2481960.199641354331100
1.9821-2.01040.2282230.184941834406100
2.0104-2.04040.22462080.182941144322100
2.0404-2.07230.25092030.197941834386100
2.0723-2.10630.22292200.170240844304100
2.1063-2.14260.20831970.152641934390100
2.1426-2.18150.17222510.152140734324100
2.1815-2.22350.1742140.150142034417100
2.2235-2.26890.25512320.187740754307100
2.2689-2.31820.19422420.146341544396100
2.3182-2.37210.18152080.138241364344100
2.3721-2.43150.16662130.137841854398100
2.4315-2.49720.18722060.136541814387100
2.4972-2.57070.19652220.134641554377100
2.5707-2.65360.19431910.136341924383100
2.6536-2.74850.1552030.13341964399100
2.7485-2.85850.16312330.130341684401100
2.8585-2.98860.1432190.138341954414100
2.9886-3.14610.17381960.136342224418100
3.1461-3.34320.15662180.135941864404100
3.3432-3.60120.15831960.128642584454100
3.6012-3.96350.13862330.120542254458100
3.9635-4.53660.11952370.105142424479100
4.5366-5.71410.13452170.118543394556100
5.7141-47.35830.1922220.184444984720100
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)
10.80081.0653-0.58334.2978-2.36071.9303-0.04630.10520.022-0.06310.28550.33230.1689-0.1736-0.27860.1695-0.0334-0.01930.2305-0.02020.1517-32.9912-33.333315.3655
20.89310.09730.18290.86420.24010.9856-0.0230.0619-0.0552-0.01950.03150.03670.1080.0106-0.01280.1728-0.0260.00630.1697-0.02270.1454-29.4226-29.245517.6636
31.0127-0.80370.51621.4224-0.12392.422-0.1407-0.03570.11450.11390.086-0.0833-0.24110.19780.06850.1442-0.07860.01680.1733-0.02950.1564-15.9492-5.389939.2403
43.2789-3.31473.90133.7541-4.68056.323-0.154-0.15570.22190.26360.0462-0.0529-0.3396-0.15630.08690.2177-0.01490.0260.189-0.05630.1724-29.1175-5.991839.1899
50.76810.31220.67331.9862-1.48633.39710.0377-0.0980.07230.08180.10820.2614-0.0615-0.2178-0.15310.1771-0.01540.0230.2032-0.02450.1919-31.7527-14.0133.0734
61.9709-1.8758-2.20873.21591.58273.86270.0811-0.0341-0.02-0.0085-0.14750.257-0.1671-0.31330.07630.1511-0.02850.00180.1387-0.02650.1413-32.538-13.768727.1752
70.43270.31180.21971.0213-0.12372.2465-0.053-0.00330.0781-0.02150.02410.0036-0.15480.09960.02930.1521-0.0360.00570.1865-0.02020.1564-22.1798-11.606527.0226
84.74590.0412.19110.37781.11373.9594-0.2132-0.10230.06440.13230.09090.0193-0.4445-0.05260.17660.1266-0.07280.03390.1212-0.03120.1243-19.6969-7.888633.2121
91.93980.3847-0.3231.7249-0.89932.7616-0.08590.16610.0943-0.2496-0.03-0.36680.16320.57170.12860.2217-0.0480.0550.3121-0.08270.1801-6.9115-11.673621.3127
108.48283.387-3.09253.8084-0.6442.90660.0058-0.5461-0.26450.1686-0.1887-0.15180.36170.41270.18690.20670.0265-0.03690.241-0.00130.1215-13.4338-25.778341.8348
113.4258-3.54133.50399.0048-7.48356.3346-0.04580.19250.28630.0541-0.1398-0.38-0.35490.59040.2890.1781-0.12290.05230.402-0.05740.2251-3.146-4.98624.5825
121.8806-0.0210.20232.1134-2.25544.38730.0454-0.13740.17050.1233-0.0382-0.0297-0.47780.52480.03210.2225-0.10440.02550.29-0.04160.2018-8.283-1.71832.477
133.9288-2.3594-0.09819.4514-1.34294.75510.07870.02980.404-0.04930.08260.2232-0.6118-0.0804-0.16450.1983-0.0930.01070.2021-0.00920.1941-16.252.043827.632
146.3306-4.98513.15057.8065-5.37296.3524-0.10750.17360.3439-0.15310.0167-0.191-0.15010.11440.09340.1462-0.1057-0.01030.2142-0.050.1267-14.1151-6.702522.8018
152.69160.8525-2.1960.9363-0.74482.61740.2678-0.21520.08590.0892-0.2008-0.1349-0.26750.1583-0.03880.1696-0.0805-0.03520.28860.02520.22220.765615.7873-6.1305
162.8756-1.0981.71145.9147-1.85468.15990.1453-0.2807-0.6412-0.084-0.195-0.39420.09750.5070.09260.1182-0.0352-0.04540.24560.05920.333519.9009-0.6498-9.3354
172.18760.57860.02150.7144-0.06581.29040.1381-0.3901-0.09660.1059-0.1647-0.1134-0.04920.0690.0280.1356-0.0544-0.01190.2380.02410.18768.86548.3768-6.7586
184.17871.05910.38072.62260.79691.99620.17430.26930.9765-0.4991-0.1736-0.5203-0.8464-0.0354-0.0280.391-0.07350.04590.35970.09290.505613.649426.0173-23.6749
191.50480.36460.29440.82120.17081.86830.2336-0.76060.25190.2023-0.2042-0.1376-0.24040.12940.00510.2639-0.1684-0.01260.5217-0.08330.264716.72620.6925.038
201.67380.44630.1880.60910.16631.20820.0493-0.20190.30050.0185-0.05050.0761-0.2106-0.0780.00550.1534-0.0110.01410.1509-0.02660.1789-9.230816.9627-13.8239
211.85470.75460.75541.29960.16720.72830.0728-0.19270.17370.0216-0.03050.0433-0.0989-0.0597-0.01640.1054-0.01970.00170.15140.00920.1422-8.816611.5749-14.9721
222.27850.4618-0.81381.1408-0.26342.2609-0.04360.0137-0.1878-0.09030.0032-0.02660.21370.02990.04680.1098-0.0014-0.02770.11210.01850.1633-6.0767-1.7792-17.7669
231.24810.4724-1.52722.4268-1.5294.20580.0308-0.091-0.0403-0.1830.10360.18690.1471-0.5527-0.1430.1263-0.0643-0.02790.22770.04150.1957-19.8509-0.0442-15.8559
245.0229-1.7239-0.84782.8170.27391.48820.0038-0.43160.15270.09560.10240.1601-0.0568-0.1492-0.11010.1293-0.0341-0.00810.23650.00350.1623-21.0766.7392-8.061
252.798-0.0633-0.16253.8063-0.70863.5426-0.1215-0.50350.0530.4443-0.03030.4796-0.1992-0.27870.16010.1052-0.0605-0.04130.234-0.02760.1945-15.27014.99-4.0669
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid -10 through 45 )A-10 - 45
2X-RAY DIFFRACTION2chain 'A' and (resid 46 through 348 )A46 - 348
3X-RAY DIFFRACTION3chain 'B' and (resid 1 through 26 )B1 - 26
4X-RAY DIFFRACTION4chain 'B' and (resid 27 through 49 )B27 - 49
5X-RAY DIFFRACTION5chain 'B' and (resid 50 through 80 )B50 - 80
6X-RAY DIFFRACTION6chain 'B' and (resid 81 through 102 )B81 - 102
7X-RAY DIFFRACTION7chain 'B' and (resid 103 through 138 )B103 - 138
8X-RAY DIFFRACTION8chain 'B' and (resid 139 through 153 )B139 - 153
9X-RAY DIFFRACTION9chain 'B' and (resid 154 through 176 )B154 - 176
10X-RAY DIFFRACTION10chain 'B' and (resid 177 through 201 )B177 - 201
11X-RAY DIFFRACTION11chain 'B' and (resid 202 through 217 )B202 - 217
12X-RAY DIFFRACTION12chain 'B' and (resid 218 through 238 )B218 - 238
13X-RAY DIFFRACTION13chain 'B' and (resid 239 through 264 )B239 - 264
14X-RAY DIFFRACTION14chain 'B' and (resid 265 through 279 )B265 - 279
15X-RAY DIFFRACTION15chain 'C' and (resid -5 through 48 )C-5 - 48
16X-RAY DIFFRACTION16chain 'C' and (resid 49 through 69 )C49 - 69
17X-RAY DIFFRACTION17chain 'C' and (resid 70 through 212 )C70 - 212
18X-RAY DIFFRACTION18chain 'C' and (resid 213 through 239 )C213 - 239
19X-RAY DIFFRACTION19chain 'C' and (resid 240 through 348 )C240 - 348
20X-RAY DIFFRACTION20chain 'D' and (resid 1 through 116 )D1 - 116
21X-RAY DIFFRACTION21chain 'D' and (resid 117 through 153 )D117 - 153
22X-RAY DIFFRACTION22chain 'D' and (resid 154 through 217 )D154 - 217
23X-RAY DIFFRACTION23chain 'D' and (resid 218 through 238 )D218 - 238
24X-RAY DIFFRACTION24chain 'D' and (resid 239 through 264 )D239 - 264
25X-RAY DIFFRACTION25chain 'D' and (resid 265 through 283 )D265 - 283

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