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- PDB-5ts2: Crystal structure of a phosphopantetheine adenylyltransferase (Co... -

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Basic information

Entry
Database: PDB / ID: 5ts2
TitleCrystal structure of a phosphopantetheine adenylyltransferase (CoaD, PPAT) from Pseudomonas aeruginosa bound to dephospho coenzyme A
ComponentsPhosphopantetheine adenylyltransferase
KeywordsTRANSFERASE / structural genomics / coenzyme A biosynthesis / PPAT / CoaD / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


[citrate (pro-3S)-lyase] ligase activity / pantetheine-phosphate adenylyltransferase / pantetheine-phosphate adenylyltransferase activity / coenzyme A biosynthetic process / ATP binding / cytoplasm
Similarity search - Function
Citrate lyase ligase, C-terminal / Citrate lyase ligase C-terminal domain / Phosphopantetheine adenylyltransferase / Cytidylyltransferase-like / Cytidyltransferase-like domain / HUPs / Rossmann-like alpha/beta/alpha sandwich fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
DEPHOSPHO COENZYME A / Phosphopantetheine adenylyltransferase / Phosphopantetheine adenylyltransferase
Similarity search - Component
Biological speciesPseudomonas aeruginosa (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.3 Å
AuthorsSeattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: To Be Published
Title: Crystal structure of a phosphopantetheine adenylyltransferase (CoaD, PPAT) from Pseudomonas aeruginosa bound to dephospho coenzyme A
Authors: Edwards, T.E. / Davies, D.R. / Fairman, J.W. / Lorimer, D. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
History
DepositionOct 27, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 9, 2016Provider: repository / Type: Initial release
Revision 1.1Nov 22, 2017Group: Derived calculations / Refinement description / Category: pdbx_struct_oper_list / software / Item: _pdbx_struct_oper_list.symmetry_operation
Revision 1.2Oct 4, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _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.ptnr1_symmetry / _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 / _struct_conn.ptnr2_symmetry / _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: Phosphopantetheine adenylyltransferase
B: Phosphopantetheine adenylyltransferase
C: Phosphopantetheine adenylyltransferase
D: Phosphopantetheine adenylyltransferase
E: Phosphopantetheine adenylyltransferase
F: Phosphopantetheine adenylyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,55525
Polymers112,9606
Non-polymers4,59519
Water3,405189
1
A: Phosphopantetheine adenylyltransferase
D: Phosphopantetheine adenylyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,1758
Polymers37,6532
Non-polymers1,5226
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5160 Å2
ΔGint-58 kcal/mol
Surface area15110 Å2
2
B: Phosphopantetheine adenylyltransferase
E: Phosphopantetheine adenylyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,1758
Polymers37,6532
Non-polymers1,5226
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5130 Å2
ΔGint-65 kcal/mol
Surface area15040 Å2
3
C: Phosphopantetheine adenylyltransferase
F: Phosphopantetheine adenylyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,2069
Polymers37,6532
Non-polymers1,5527
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5710 Å2
ΔGint-79 kcal/mol
Surface area15040 Å2
4


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area25250 Å2
ΔGint-307 kcal/mol
Surface area35950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)98.380, 101.350, 105.710
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 1 and (name N or name...
21(chain B and ((resid 1 and (name N or name...
31(chain C and ((resid 1 and (name N or name...
41(chain D and ((resid 1 and (name N or name...
51(chain E and ((resid 1 and (name N or name...
61(chain F and (resid 1 through 29 or resid 31...

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
11METMETMETMET(chain A and ((resid 1 and (name N or name...AA19
12ALAALALYSLYS(chain A and ((resid 1 and (name N or name...AA-6 - 1582 - 166
13ALAALALYSLYS(chain A and ((resid 1 and (name N or name...AA-6 - 1582 - 166
14ALAALALYSLYS(chain A and ((resid 1 and (name N or name...AA-6 - 1582 - 166
15ALAALALYSLYS(chain A and ((resid 1 and (name N or name...AA-6 - 1582 - 166
21METMETMETMET(chain B and ((resid 1 and (name N or name...BB19
22METMETLYSLYS(chain B and ((resid 1 and (name N or name...BB1 - 1589 - 166
23METMETLYSLYS(chain B and ((resid 1 and (name N or name...BB1 - 1589 - 166
24METMETLYSLYS(chain B and ((resid 1 and (name N or name...BB1 - 1589 - 166
25METMETLYSLYS(chain B and ((resid 1 and (name N or name...BB1 - 1589 - 166
31METMETMETMET(chain C and ((resid 1 and (name N or name...CC19
32ALAALALYSLYS(chain C and ((resid 1 and (name N or name...CC-6 - 1582 - 166
33ALAALALYSLYS(chain C and ((resid 1 and (name N or name...CC-6 - 1582 - 166
34ALAALALYSLYS(chain C and ((resid 1 and (name N or name...CC-6 - 1582 - 166
35ALAALALYSLYS(chain C and ((resid 1 and (name N or name...CC-6 - 1582 - 166
41METMETMETMET(chain D and ((resid 1 and (name N or name...DD19
42HISHISPHEPHE(chain D and ((resid 1 and (name N or name...DD-1 - 1577 - 165
43HISHISPHEPHE(chain D and ((resid 1 and (name N or name...DD-1 - 1577 - 165
44HISHISPHEPHE(chain D and ((resid 1 and (name N or name...DD-1 - 1577 - 165
45HISHISPHEPHE(chain D and ((resid 1 and (name N or name...DD-1 - 1577 - 165
51METMETMETMET(chain E and ((resid 1 and (name N or name...EE19
52ALAALACODCOD(chain E and ((resid 1 and (name N or name...EE - T-6 - 2012
53ALAALACODCOD(chain E and ((resid 1 and (name N or name...EE - T-6 - 2012
54ALAALACODCOD(chain E and ((resid 1 and (name N or name...EE - T-6 - 2012
55ALAALACODCOD(chain E and ((resid 1 and (name N or name...EE - T-6 - 2012
61METMETASPASP(chain F and (resid 1 through 29 or resid 31...FF1 - 299 - 37
62VALVALILEILE(chain F and (resid 1 through 29 or resid 31...FF31 - 3239 - 40
63ALAALAPROPRO(chain F and (resid 1 through 29 or resid 31...FF34 - 3942 - 47
64LYSLYSASNASN(chain F and (resid 1 through 29 or resid 31...FF40 - 4248 - 50
65HISHISLYSLYS(chain F and (resid 1 through 29 or resid 31...FF0 - 1588 - 166
66HISHISLYSLYS(chain F and (resid 1 through 29 or resid 31...FF0 - 1588 - 166
67HISHISLYSLYS(chain F and (resid 1 through 29 or resid 31...FF0 - 1588 - 166
68HISHISLYSLYS(chain F and (resid 1 through 29 or resid 31...FF0 - 1588 - 166

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Components

#1: Protein
Phosphopantetheine adenylyltransferase / Dephospho-CoA pyrophosphorylase / Pantetheine-phosphate adenylyltransferase / PPAT


Mass: 18826.633 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudomonas aeruginosa (strain LESB58) (bacteria)
Strain: LESB58 / Gene: coaD, PLES_03601 / Production host: Escherichia coli (E. coli)
References: UniProt: B7V2S6, UniProt: Q9I6D1*PLUS, pantetheine-phosphate adenylyltransferase
#2: Chemical
ChemComp-COD / DEPHOSPHO COENZYME A


Mass: 687.554 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C21H35N7O13P2S
#3: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#4: Chemical
ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: Cl
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 189 / Source method: isolated from a natural source / Formula: H2O

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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: 2.33 Å3/Da / Density % sol: 47.27 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: PsaeA.00960.a.B1 batch PS02167 at 18.6 against MCSG1 screen condition E9 0.2 M CaCl2, 20% PEG 3350 supplemented with 20% ethylene glycol, 2 mM MgCl, and 2 mM ATP in the cryo-protectant, ...Details: PsaeA.00960.a.B1 batch PS02167 at 18.6 against MCSG1 screen condition E9 0.2 M CaCl2, 20% PEG 3350 supplemented with 20% ethylene glycol, 2 mM MgCl, and 2 mM ATP in the cryo-protectant, crystal tracking ID 259488e9, unique puck ID sls7-3

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.97872 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Mar 12, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97872 Å / Relative weight: 1
ReflectionResolution: 2.3→46.865 Å / Num. obs: 46486 / % possible obs: 97.5 % / Observed criterion σ(I): -3 / Redundancy: 4.7 % / Biso Wilson estimate: 43.25 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.057 / Net I/σ(I): 16.63
Reflection shell
Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsCC1/2Diffraction-ID% possible all
2.3-2.360.5073.020.824199
2.36-2.420.4113.70.867198.8
2.42-2.490.364.30.9198.7
2.49-2.570.2795.380.927198.4
2.57-2.660.2276.550.951198
2.66-2.750.1877.80.969198.5
2.75-2.850.13910.250.984198.3
2.85-2.970.1112.60.989197.6
2.97-3.10.08315.90.993198
3.1-3.250.07217.970.995197.6
3.25-3.430.05622.340.997197.5
3.43-3.640.04626.080.998196.8
3.64-3.890.04229.340.998197.2
3.89-4.20.03732.660.998196.8
4.2-4.60.03535.170.998196.4
4.6-5.140.03436.760.998195.6
5.14-5.940.03634.970.998195.6
5.94-7.270.03236.170.999194.9
7.27-10.290.02941.560.999193.7
10.290.02740.410.998188.4

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
XSCALEdata scaling
MOLREPphasing
PHENIXrefinement
PDB_EXTRACT3.2data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3k9w

3k9w


Resolution: 2.3→46.865 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 25.4
RfactorNum. reflection% reflection
Rfree0.2444 2158 4.65 %
Rwork0.1804 --
obs0.1834 46437 97.53 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 127.28 Å2 / Biso mean: 51.2273 Å2 / Biso min: 20.98 Å2
Refinement stepCycle: final / Resolution: 2.3→46.865 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7501 0 277 189 7967
Biso mean--69.12 47.07 -
Num. residues----971
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0087988
X-RAY DIFFRACTIONf_angle_d1.01410896
X-RAY DIFFRACTIONf_chiral_restr0.0571231
X-RAY DIFFRACTIONf_plane_restr0.0071388
X-RAY DIFFRACTIONf_dihedral_angle_d14.394652
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A4085X-RAY DIFFRACTION11.1TORSIONAL
12B4085X-RAY DIFFRACTION11.1TORSIONAL
13C4085X-RAY DIFFRACTION11.1TORSIONAL
14D4085X-RAY DIFFRACTION11.1TORSIONAL
15E4085X-RAY DIFFRACTION11.1TORSIONAL
16F4085X-RAY DIFFRACTION11.1TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 15

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.3002-2.35370.30231830.22852921310499
2.3537-2.41260.3251470.23582931307899
2.4126-2.47780.30131380.2252953309199
2.4778-2.55070.30281340.22312925305999
2.5507-2.6330.2971340.22992971310599
2.633-2.72710.31081440.23722950309498
2.7271-2.83630.31881170.22352965308298
2.8363-2.96530.29291240.222953307798
2.9653-3.12170.30541360.21252955309198
3.1217-3.31720.26571060.21692988309498
3.3172-3.57320.25331490.1932929307897
3.5732-3.93270.22611920.16482913310597
3.9327-4.50130.18291620.14222940310297
4.5013-5.66960.19751700.13572936310696
5.6696-46.87460.23321220.14993049317194
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)
19.26254.18624.10741.75431.12052.98220.07070.4236-0.24540.03180.1986-0.10490.1647-0.054-0.28540.3868-0.04140.05660.4032-0.0940.4234-1.824435.3518-22.3685
23.55552.06334.14812.39811.6435.29980.01580.3093-0.15380.26470.0865-0.26690.98810.5347-0.18380.3928-0.01190.15610.407-0.12010.54547.260831.9384-14.4447
36.85441.80742.00316.90683.16855.671-0.39960.08850.678-1.18260.23270.2021-0.84310.21850.13490.5116-0.08440.15670.3761-0.07360.47478.722544.4644-21.6425
45.0594-0.21430.04254.527-1.34511.66610.00040.6752-0.1651-0.67830.1312-0.7616-0.31590.4158-0.14750.4623-0.09610.14510.4399-0.16540.37178.792841.4847-25.2597
56.2106-0.52714.75457.5004-3.29626.7544-0.5061-0.47040.44860.1324-0.107-0.8416-0.88990.30640.5980.35260.02280.07210.513-0.03970.4608-0.116241.5098-14.9697
64.62540.00214.47716.5940.30154.44690.3863-0.79480.0208-0.1453-0.1981-0.6897-0.087-1.0178-0.20140.52550.0142-0.0050.4242-0.04030.5258-6.11249.5697-12.4775
74.8705-1.98683.77825.9054-4.53844.61580.142-0.1214-0.4641-0.59940.06850.36840.3532-0.2874-0.16560.4740.0382-0.03640.4027-0.04970.334-7.304740.6856-17.42
83.18072.30882.11293.158-1.18326.57930.3496-0.37340.8043-0.3172-0.3081-0.6917-0.3334-0.4567-0.19230.5409-0.04170.01360.4091-0.0470.630710.090136.2255-4.8767
96.1549-4.32143.23233.2726-1.1868.8961-0.47450.2454-0.16990.03560.7278-0.2309-0.7465-0.4491-0.10360.4458-0.04870.11690.253-0.03260.581419.404348.2323-7.7518
104.3096-2.32442.81163.03662.11489.19980.03650.5436-0.7823-0.35320.4672-0.75910.10960.2814-0.51810.3599-0.08130.0980.4748-0.07870.713124.691942.2516-12.3432
117.03142.0489-2.97623.2912.83516.4311-0.4716-0.25940.6793-0.29610.0061-0.5502-0.2021-0.13120.36810.42120.1187-0.01480.2808-0.11530.4382-22.884557.722217.1733
126.035-2.28392.02052.67931.13752.6936-0.0802-0.22010.61770.62550.0545-0.8154-0.55870.48520.05420.47490.1441-0.04260.4636-0.06850.3327-15.494464.1319.1757
134.1219-0.64291.80576.65-4.37095.4745-0.1552-0.4924-0.52780.04240.16560.42980.1923-0.1717-0.04790.4280.16330.09820.4256-0.03820.4211-24.985352.929322.7203
144.87320.4681.83052.52331.13363.5216-0.1841-0.0094-0.10280.1913-0.00540.0937-0.00740.02980.25910.34680.13650.02040.3554-0.01280.3907-24.891157.252313.7128
156.63221.58463.70854.43922.87165.7169-0.23660.0321-0.2792-0.12410.2579-0.1359-0.10840.2233-0.04880.41890.05090.08050.39240.00370.3832-16.593754.4447.037
166.5213-2.74393.57685.2826-0.77136.643-0.7071-0.9074-0.00771.05120.5518-0.09840.106-0.080.14840.51490.1850.03350.55990.02510.3614-12.695248.515231.5559
170.4165-1.23250.60845.2872-6.7417.1644-0.1683-0.00620.14440.262-0.2396-1.1917-0.50290.36360.44090.5506-0.0152-0.10120.30640.02510.507222.787947.374416.9719
183.5228-0.9882-0.95857.6387-1.76692.0075-0.0749-0.01180.0095-0.0209-0.041-0.3932-0.686-0.14920.16650.5454-0.0485-0.12610.2916-0.04310.362419.425357.806912.5167
191.19360.4272-0.56223.18571.40573.87610.0147-0.1034-0.0999-0.15590.0812-0.4418-0.5920.2182-0.13380.5109-0.0838-0.09050.3589-0.00330.603126.450357.974811.46
208.787-1.4048-0.79023.36483.08587.9271-0.13820.24170.04560.0245-0.02430.1076-0.2274-0.53190.15060.3239-0.0664-0.01710.26750.1040.417215.518645.48977.7439
213.7065-1.01421.83218.1325-2.92883.614-0.4059-0.22020.29610.00240.2157-0.3378-0.4928-0.14240.19320.68020.04330.02120.3547-0.04480.357310.672269.702410.3962
224.056-0.4399-2.00644.9045-0.58958.5862-0.2906-0.0049-0.5758-0.0961-0.0864-0.00650.48810.63960.34740.19210.0207-0.03190.2949-0.06890.3644-15.153427.3895-9.2135
235.8198-0.6586-4.60135.53651.2313.76770.1541-0.0340.1169-0.2526-0.12810.1372-0.9763-0.26170.00460.31250.0288-0.07950.3339-0.04570.3364-17.332335.7746-14.0217
244.3865-0.3573-2.55624.79340.35732.8106-0.13710.0343-0.21420.3814-0.10650.68860.3598-0.23760.29020.2847-0.01920.01080.273-0.07480.3479-21.592426.2893-3.7956
253.0715-1.90812.17471.5614-1.17463.61750.0348-0.0961-0.3842-0.1654-0.08630.15690.2608-0.4697-0.02840.2857-0.0569-0.01230.2938-0.03490.3783-15.356921.5213-7.7863
261.80190.72260.9612.3038-0.26642.7637-0.1658-0.06540.35140.93310.35570.118-0.06010.17650.02030.31980.0297-0.0150.3409-0.0040.3966-8.841731.628-6.4853
274.2101-0.76881.40967.4532-2.48054.036-0.1490.02520.11840.4306-0.0287-0.4921-0.22460.03760.1980.2262-0.0564-0.05330.40980.01170.4188-1.932230.4547-2.6049
287.9272-1.1532-0.11364.15150.68144.27470.1141-0.024-0.1216-0.0241-0.46620.4045-0.4209-0.37530.3560.30380.0201-0.03480.313-0.1040.4342-26.905440.1245-1.1332
291.3494-0.0856-1.36491.58711.1454.78470.1490.0393-0.1038-0.4474-0.08560.0582-0.6236-0.2033-0.12930.52240.08380.00380.2748-0.01310.3487-13.42571.4616-1.5723
302.47690.09890.35160.5497-0.32653.01830.06120.18920.0916-0.25-0.0554-0.0556-0.3348-0.0190.01020.7730.0894-0.00850.2936-0.00680.3824-9.673173.5296-3.4978
317.7722.31954.27893.5925-1.07083.94420.03090.0592-0.37770.2446-0.2058-0.0137-0.1160.2170.01230.48880.07990.01510.36920.01960.3496-5.040265.08518.2539
325.3318-1.8923-3.03492.0929-0.48727.74760.07660.00230.1066-0.0711-0.44280.2244-0.71310.27140.39710.7192-0.0613-0.08570.3663-0.0160.3126-8.104361.9908-18.5305
336.03982.9099-0.15744.97460.57685.63770.2511-0.1052-0.02730.2021-0.1639-0.01480.077-0.4203-0.09680.25710.0822-0.04890.36420.01940.26996.947630.892522.505
346.4104-1.57641.74443.5762-2.06013.86490.109-0.5172-0.43950.6270.1038-0.0746-0.1636-0.0301-0.19740.4170.0333-0.10920.55320.08440.32227.333334.03530.0085
354.3162-0.86934.22462.8061-0.95394.30050.74410.7409-0.6216-0.6841-0.21970.23970.597-0.6549-0.47820.5530.0857-0.09530.5933-0.00570.46456.308340.821919.3677
364.81984.30594.65494.12294.35094.8327-0.69260.44380.3454-0.70360.43440.024-1.731-0.49130.37970.71390.1694-0.06840.6072-0.02630.5202-0.524848.298920.4685
374.6614-0.4636-2.12987.03545.77925.908-0.22910.46230.2369-0.42030.40190.0417-0.21380.2772-0.13260.39490.0528-0.02870.40210.13050.28978.286239.631615.1251
388.7755-1.9835.06696.5419-1.45375.72930.4694-0.2651-0.86220.27910.11570.34530.6679-0.2587-0.5530.4463-0.1139-0.01290.40170.00410.3911-1.076519.345412.1541
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid -6 through 14 )A-6 - 14
2X-RAY DIFFRACTION2chain 'A' and (resid 15 through 27 )A15 - 27
3X-RAY DIFFRACTION3chain 'A' and (resid 28 through 46 )A28 - 46
4X-RAY DIFFRACTION4chain 'A' and (resid 47 through 79 )A47 - 79
5X-RAY DIFFRACTION5chain 'A' and (resid 80 through 94 )A80 - 94
6X-RAY DIFFRACTION6chain 'A' and (resid 95 through 108 )A95 - 108
7X-RAY DIFFRACTION7chain 'A' and (resid 109 through 117 )A109 - 117
8X-RAY DIFFRACTION8chain 'A' and (resid 118 through 127 )A118 - 127
9X-RAY DIFFRACTION9chain 'A' and (resid 128 through 136 )A128 - 136
10X-RAY DIFFRACTION10chain 'A' and (resid 137 through 158 )A137 - 158
11X-RAY DIFFRACTION11chain 'B' and (resid 1 through 14 )B1 - 14
12X-RAY DIFFRACTION12chain 'B' and (resid 15 through 27 )B15 - 27
13X-RAY DIFFRACTION13chain 'B' and (resid 28 through 58 )B28 - 58
14X-RAY DIFFRACTION14chain 'B' and (resid 59 through 94 )B59 - 94
15X-RAY DIFFRACTION15chain 'B' and (resid 95 through 127 )B95 - 127
16X-RAY DIFFRACTION16chain 'B' and (resid 128 through 158 )B128 - 158
17X-RAY DIFFRACTION17chain 'C' and (resid -6 through 14 )C-6 - 14
18X-RAY DIFFRACTION18chain 'C' and (resid 15 through 46 )C15 - 46
19X-RAY DIFFRACTION19chain 'C' and (resid 47 through 79 )C47 - 79
20X-RAY DIFFRACTION20chain 'C' and (resid 80 through 117 )C80 - 117
21X-RAY DIFFRACTION21chain 'C' and (resid 118 through 158 )C118 - 158
22X-RAY DIFFRACTION22chain 'D' and (resid -1 through 14 )D-1 - 14
23X-RAY DIFFRACTION23chain 'D' and (resid 15 through 27 )D15 - 27
24X-RAY DIFFRACTION24chain 'D' and (resid 28 through 58 )D28 - 58
25X-RAY DIFFRACTION25chain 'D' and (resid 59 through 79 )D59 - 79
26X-RAY DIFFRACTION26chain 'D' and (resid 80 through 94 )D80 - 94
27X-RAY DIFFRACTION27chain 'D' and (resid 95 through 117 )D95 - 117
28X-RAY DIFFRACTION28chain 'D' and (resid 118 through 157 )D118 - 157
29X-RAY DIFFRACTION29chain 'E' and (resid -6 through 46 )E-6 - 46
30X-RAY DIFFRACTION30chain 'E' and (resid 47 through 94 )E47 - 94
31X-RAY DIFFRACTION31chain 'E' and (resid 95 through 118 )E95 - 118
32X-RAY DIFFRACTION32chain 'E' and (resid 119 through 158 )E119 - 158
33X-RAY DIFFRACTION33chain 'F' and (resid 0 through 58 )F0 - 58
34X-RAY DIFFRACTION34chain 'F' and (resid 59 through 79 )F59 - 79
35X-RAY DIFFRACTION35chain 'F' and (resid 80 through 94 )F80 - 94
36X-RAY DIFFRACTION36chain 'F' and (resid 95 through 108 )F95 - 108
37X-RAY DIFFRACTION37chain 'F' and (resid 109 through 127 )F109 - 127
38X-RAY DIFFRACTION38chain 'F' and (resid 128 through 158 )F128 - 158

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