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- PDB-3rg2: Structure of a two-domain NRPS fusion protein containing the EntE... -

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Basic information

Entry
Database: PDB / ID: 3rg2
TitleStructure of a two-domain NRPS fusion protein containing the EntE adenylation domain and EntB aryl-carrier protein from enterobactin biosynthesis
ComponentsEnterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
KeywordsLIGASE / Adenylate-forming enzymes / ANL Superfamily / Non-ribosomal peptide synthetase carrier protein Function / NRPS adenylation domain acyl carrier protein / 4'phosphopantetheinylation 4'PP cofactor
Function / homology
Function and homology information


isochorismatase / 2,3-dihydroxybenzoate-[aryl-carrier protein] ligase / enterobactin synthase / isochorismatase activity / 2,3-dihydroxybenzoate--[aryl-carrier protein] ligase / 2,3-dihydroxybenzoate-serine ligase activity / enterobactin biosynthetic process / acyltransferase activity / ATP binding / membrane / cytosol
Similarity search - Function
Isochorismatase / 2,3-dihydroxybenzoate-AMP ligase / : / Isochorismatase-like / Isochorismatase-like superfamily / Isochorismatase domain / : / ANL, N-terminal domain / ANL, C-terminal domain / ACP-like ...Isochorismatase / 2,3-dihydroxybenzoate-AMP ligase / : / Isochorismatase-like / Isochorismatase-like superfamily / Isochorismatase domain / : / ANL, N-terminal domain / ANL, C-terminal domain / ACP-like / ANL, N-terminal domain / AMP-binding enzyme C-terminal domain / AMP-binding enzyme, C-terminal domain / AMP-binding, conserved site / Putative AMP-binding domain signature. / Non-ribosomal Peptide Synthetase Peptidyl Carrier Protein; Chain A / AMP-dependent synthetase/ligase / AMP-binding enzyme / GMP Synthetase; Chain A, domain 3 / AMP-binding enzyme, C-terminal domain superfamily / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
IODIDE ION / 4'-PHOSPHOPANTETHEINE / Chem-SVS / Enterobactin synthase component E / Enterobactin synthase component B
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsSundlov, J.A. / Gulick, A.M.
CitationJournal: Chem.Biol. / Year: 2012
Title: Structural and Functional Investigation of the Intermolecular Interaction between NRPS Adenylation and Carrier Protein Domains.
Authors: Sundlov, J.A. / Shi, C. / Wilson, D.J. / Aldrich, C.C. / Gulick, A.M.
History
DepositionApr 7, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 7, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 28, 2012Group: Database references
Revision 1.2Aug 9, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software
Revision 1.3Jul 17, 2019Group: Data collection / Derived calculations / Refinement description
Category: software / struct_conn
Item: _software.classification / _software.name ..._software.classification / _software.name / _software.version / _struct_conn.pdbx_leaving_atom_flag
Revision 1.4Aug 14, 2019Group: Data collection / Category: computing
Revision 1.5Sep 13, 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 / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
B: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
C: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
D: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
E: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
F: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
G: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
H: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
I: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
J: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)694,55555
Polymers683,29410
Non-polymers11,26145
Water00
1
A: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
B: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,41915
Polymers136,6592
Non-polymers2,76013
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6720 Å2
ΔGint-36 kcal/mol
Surface area45950 Å2
MethodPISA
2
C: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
H: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)138,5308
Polymers136,6592
Non-polymers1,8716
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6200 Å2
ΔGint-39 kcal/mol
Surface area45780 Å2
MethodPISA
3
D: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
E: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,16513
Polymers136,6592
Non-polymers2,50611
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6570 Å2
ΔGint-40 kcal/mol
Surface area45850 Å2
MethodPISA
4
F: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
I: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)138,78410
Polymers136,6592
Non-polymers2,1258
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6660 Å2
ΔGint-42 kcal/mol
Surface area45970 Å2
MethodPISA
5
G: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
J: Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb)
hetero molecules


Theoretical massNumber of molelcules
Total (without water)138,6579
Polymers136,6592
Non-polymers1,9987
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5670 Å2
ΔGint-39 kcal/mol
Surface area48320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)160.575, 101.771, 240.678
Angle α, β, γ (deg.)90.00, 107.06, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
31
41
51
61
71
81
91
101
12
22
32
42
52
62
72
82
92
102
13
23
33
43
53
63
73
83
93
103

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and (resseq 3:133 or resseq 140:144 or resseq...
211chain B and (resseq 3:133 or resseq 140:144 or resseq...
311chain C and (resseq 3:133 or resseq 140:144 or resseq...
411chain D and (resseq 3:133 or resseq 140:144 or resseq...
511chain E and (resseq 3:133 or resseq 140:144 or resseq...
611chain F and (resseq 3:133 or resseq 140:144 or resseq...
711chain G and (resseq 3:133 or resseq 140:144 or resseq...
811chain H and (resseq 3:133 or resseq 140:144 or resseq...
911chain I and (resseq 3:133 or resseq 140:144 or resseq...
1011chain J and (resseq 3:133 or resseq 140:144 or resseq...
112chain A and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
212chain B and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
312chain C and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
412chain D and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
512chain E and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
612chain F and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
712chain G and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
812chain H and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
912chain I and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
1012chain J and (resseq 434:482 or resseq 484:510 or resseq 512:515 )
113chain A and (resseq 545:610 )
213chain B and (resseq 545:610 )
313chain C and (resseq 545:610 )
413chain D and (resseq 545:610 )
513chain E and (resseq 545:610 )
613chain F and (resseq 545:610 )
713chain G and (resseq 545:610 )
813chain H and (resseq 545:610 )
913chain I and (resseq 545:610 )
1013chain J and (resseq 545:610 )

NCS ensembles :
ID
1
2
3
DetailsThe asymmetric unit contains five domain-swapped dimers that each represent two functional interactions between the EntE adenylation and EntB carrier protein domains.

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Components

#1: Protein
Enterobactin synthase component E (entE), 2,3-dihydro-2,3-dihydroxybenzoate synthetase, isochroismatase (Entb) / Enterochelin synthase E / 2 / 3-dihydroxybenzoate-AMP ligase / Dihydroxybenzoic acid-activating ...Enterochelin synthase E / 2 / 3-dihydroxybenzoate-AMP ligase / Dihydroxybenzoic acid-activating enzyme / S-dihydroxybenzoyltransferase


Mass: 68329.438 Da / Num. of mol.: 10
Fragment: Fusion between EntE (unp residues 1-536) and EntB (unp residues 211-285)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: JM109 / Gene: b0594, entE, entE and entB, JW0586 / Plasmid: pET15bTEV, pSP55 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: P10378, UniProt: Q1REW7, (2,3-dihydroxybenzoyl)adenylate synthase, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups
#2: Chemical
ChemComp-SVS / 5'-deoxy-5'-({[2-(2-hydroxyphenyl)ethyl]sulfonyl}amino)adenosine


Mass: 450.469 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C18H22N6O6S
#3: Chemical
ChemComp-PNS / 4'-PHOSPHOPANTETHEINE


Mass: 358.348 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: C11H23N2O7PS
#4: Chemical...
ChemComp-IOD / IODIDE ION


Mass: 126.904 Da / Num. of mol.: 25 / Source method: obtained synthetically / Formula: I
Nonpolymer detailsTHE SVS LIGAND IS ATTACHED TO PHOSPHOPANTETHEINE (PNS) THIOL (S44) TO FORM A COVALENT LINKAGE. THE ...THE SVS LIGAND IS ATTACHED TO PHOSPHOPANTETHEINE (PNS) THIOL (S44) TO FORM A COVALENT LINKAGE. THE LIGAND SVS REPRESENTS THE FINAL BOUND PRODUCT. THE STARTING MATERIAL FOR SVS LIGAND ((E)-5'-AMINO-5'-DEOXY-5'-N-{[2-(2-HYDROXYPHENYL)ETHENYL]SULFONYL}ADENOSINE) HAS A DOUBLE BOND BETWEEN C21 AND C22 ATOM GROUPS.
Sequence detailsTHE STRUCTURE IS REPRESENTATIVE OF A CHIMERIC PROTEIN BETWEEN ENTEROBACTIN SYNTHETASE COMPONENT E ...THE STRUCTURE IS REPRESENTATIVE OF A CHIMERIC PROTEIN BETWEEN ENTEROBACTIN SYNTHETASE COMPONENT E (ENTE) AND THE CARRIER PROTEIN DOMAIN OF 2,3-DIHYDRO-2,3-DIHYDROXYBENZOATE SYNTHETASE, ISOCHROISMATASE (ENTB)

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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: 2.75 Å3/Da / Density % sol: 55.3 %
Crystal growTemperature: 293 K / Method: microbatch under oil / pH: 6
Details: 1:1 mixture of protein and 20-30% PEG 3350, 100 mM NH4I, 50 mM MES , pH 6.0, microbatch under oil, temperature 293K

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Data collection

DiffractionMean temperature: 113 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 0.97945 Å
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Dec 11, 2007 / Details: SSRL 11-1
RadiationMonochromator: SSRL 11-1 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97945 Å / Relative weight: 1
ReflectionResolution: 3.1→40 Å / Num. all: 135141 / Num. obs: 134330 / % possible obs: 99.4 % / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Biso Wilson estimate: 90 Å2 / Rmerge(I) obs: 0.068 / Net I/σ(I): 13
Reflection shellResolution: 3.1→3.2 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.474 / Mean I/σ(I) obs: 1.8 / Num. unique all: 12070 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.7_637)refinement
PHASERphasing
BALBESphasing
REFMACrefinement
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: Mutated DhbE (pdb code 1MD9) with C-terminal domain rotated and pdb entry code 2FQ1

1md9

2fq1


Resolution: 3.1→39.269 Å / SU ML: 0.4 / σ(F): 1.34 / Stereochemistry target values: ML / Details: TLS Refinement
RfactorNum. reflection% reflectionSelection details
Rfree0.2639 6385 4.75 %Rfree chosen in thin shells with SHELX
Rwork0.2179 ---
obs0.2203 134306 98.96 %-
all-135717 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 38.433 Å2 / ksol: 0.254 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-1.4217 Å20 Å2-0.6087 Å2
2--3.9582 Å20 Å2
3----5.3798 Å2
Refinement stepCycle: LAST / Resolution: 3.1→39.269 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms44567 0 545 0 45112
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0146127
X-RAY DIFFRACTIONf_angle_d1.35663201
X-RAY DIFFRACTIONf_dihedral_angle_d15.75315854
X-RAY DIFFRACTIONf_chiral_restr0.0847265
X-RAY DIFFRACTIONf_plane_restr0.0068299
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2826X-RAY DIFFRACTIONPOSITIONAL
12B2826X-RAY DIFFRACTIONPOSITIONAL0.08
13C2803X-RAY DIFFRACTIONPOSITIONAL0.07
14D2821X-RAY DIFFRACTIONPOSITIONAL0.071
15E2746X-RAY DIFFRACTIONPOSITIONAL0.073
16F2810X-RAY DIFFRACTIONPOSITIONAL0.081
17G2691X-RAY DIFFRACTIONPOSITIONAL0.075
18H2741X-RAY DIFFRACTIONPOSITIONAL0.075
19I2709X-RAY DIFFRACTIONPOSITIONAL0.069
110J2555X-RAY DIFFRACTIONPOSITIONAL0.061
21A597X-RAY DIFFRACTIONPOSITIONAL
22B597X-RAY DIFFRACTIONPOSITIONAL0.083
23C594X-RAY DIFFRACTIONPOSITIONAL0.082
24D599X-RAY DIFFRACTIONPOSITIONAL0.092
25E587X-RAY DIFFRACTIONPOSITIONAL0.086
26F593X-RAY DIFFRACTIONPOSITIONAL0.079
27G591X-RAY DIFFRACTIONPOSITIONAL0.081
28H578X-RAY DIFFRACTIONPOSITIONAL0.079
29I572X-RAY DIFFRACTIONPOSITIONAL0.065
210J544X-RAY DIFFRACTIONPOSITIONAL0.059
31A494X-RAY DIFFRACTIONPOSITIONAL
32B494X-RAY DIFFRACTIONPOSITIONAL0.051
33C486X-RAY DIFFRACTIONPOSITIONAL0.052
34D478X-RAY DIFFRACTIONPOSITIONAL0.053
35E502X-RAY DIFFRACTIONPOSITIONAL0.059
36F492X-RAY DIFFRACTIONPOSITIONAL0.058
37G426X-RAY DIFFRACTIONPOSITIONAL0.05
38H502X-RAY DIFFRACTIONPOSITIONAL0.057
39I499X-RAY DIFFRACTIONPOSITIONAL0.054
310J502X-RAY DIFFRACTIONPOSITIONAL0.06
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)
10.12210.0702-0.01380.123-0.03430.6186-0.02790.04830.1482-0.14620.05880.02330.28570.54260.04740.04930.2057-0.02450.06760.02250.1824-100.4054-105.345190.4707
20.08050.0423-0.03540.0284-0.03050.0587-0.0441-0.00640.0033-0.0154-0.0854-0.08940.03340.0697-0.00490.06980.1197-0.03410.1442-0.04440.2059-69.7125-67.3217112.2809
30.34450.0029-0.27030.12060.02050.35760.4157-0.00980.49970.06310.0804-0.1775-0.32630.24650.782-0.5056-0.52590.2775-0.26490.10920.188-90.6393-46.4229116.0287
40.0103-0.0151-0.02330.13040.02440.070.0996-0.10280.0224-0.0688-0.0264-0.2111-0.03470.1553-0.04520.4052-0.21810.09290.81440.20080.6823-81.2456-84.319781.4982
50.1987-0.0605-0.15930.15260.04850.1789-0.09570.3480.147-0.01740.0950.1792-0.0036-0.3351-0.03310.04360.0752-0.00970.41280.10240.5499-31.6603-60.4002101.0681
60.0714-0.00730.02460.021-0.0110.0152-0.0315-0.03620.03010.03170.01810.0072-0.00260.01330.00620.71760.248-0.09260.7785-0.12310.675612.4592-37.479287.5255
70.131-0.0471-0.01720.05040.04570.13070.030.26170.2107-0.0659-0.0752-0.0144-0.3489-0.1945-0.02910.31150.1145-0.11760.3706-0.0785-0.2159-69.2337-36.575345.8618
80.063-0.0215-0.02120.09830.04950.02880.0976-0.0225-0.0086-0.0665-0.05380.0173-0.0467-0.0154-0.03781.2678-0.0017-0.09720.560.06460.5725-109.7804-63.978669.7173
90.0282-0.05780.03460.3074-0.16720.1443-0.04590.18490.0972-0.289-0.0486-0.2257-0.08760.069-0.01380.75720.2902-0.00370.29030.20590.2423-108.061-80.882845.3822
100.03650.02170.03310.05140.00150.2089-0.055-0.00790.0463-0.0295-0.08440.07090.01340.0210.03810.49420.2386-0.08480.778-0.13920.428-98.1488-31.347750.2902
110.150.02520.03440.07980.05290.23850.20380.21230.1335-0.1474-0.002-0.1687-0.06080.27410.07150.76450.10490.02930.54510.07540.2116-93.9112-9.74456.6627
120.04950.0348-0.03630.20760.0630.1118-0.04530.0286-0.0205-0.0278-0.0314-0.03510.0634-0.01780.04251.1070.00930.00030.66890.04210.6443-135.2294-38.27821.8237
130.1424-0.07990.13480.661-0.00780.20770.43230.1257-0.2732-0.2143-0.42190.15350.1945-0.175-0.01710.3530.0463-0.11280.5977-0.02350.4661-43.3866-86.878257.8916
140.04220.03860.01550.10090.01980.05420.0750.005-0.0484-0.02120.0270.07230.02280.0703-0.041.084-0.0701-0.29991.22390.07721.2736-18.2274-61.631520.8721
150.0638-0.00020.08480.37980.16910.4006-0.081-0.01460.065-0.05540.30710.1616-0.37240.0463-0.08350.5760.05330.14780.38010.08210.4237-4.3536-19.14771.528
160.0155-0.00190.01530.10820.02270.0253-0.04460.04080.0112-0.0418-0.02640.01960.01990.0053-0.03710.1711-0.02390.09710.50870.00590.4153-9.4246-69.419783.0552
170.57230.1989-0.25360.3686-0.05470.12680.4473-0.3070.25650.0543-0.20360.3643-0.350.0862-0.02360.7392-0.126-0.00330.304-0.02950.441-146.9601-23.082823.8272
180.0301-0.02-0.00840.04230.00090.0052-0.03390.0353-0.0027-0.0113-0.02860.01550.01140.00320.00080.8423-0.061-0.29310.41960.08470.3904-99.6363-38.68911.8022
190.2013-0.0468-0.04740.1899-0.00360.06090.178-0.3238-0.5203-0.0378-0.06460.03950.029-0.0467-0.01260.6549-0.308-0.26670.48950.20070.73115.9551-76.977926.7328
200.1025-0.0233-0.16450.15230.07790.27490.02570.10720.0149-0.071-0.1514-0.0631-0.0415-0.12620.01010.42190.03010.00420.67920.16020.4068-34.3893-58.713155.1626
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A resid 1:510
2X-RAY DIFFRACTION2chain A resid 541:613
3X-RAY DIFFRACTION3chain B resid 1:510
4X-RAY DIFFRACTION4chain B resid 541:613
5X-RAY DIFFRACTION5chain C resid 1:510
6X-RAY DIFFRACTION6chain C resid 541:613
7X-RAY DIFFRACTION7chain D resid 1:510
8X-RAY DIFFRACTION8chain D resid 541:613
9X-RAY DIFFRACTION9chain E resid 1:510
10X-RAY DIFFRACTION10chain E resid 541:613
11X-RAY DIFFRACTION11chain F resid 1:510
12X-RAY DIFFRACTION12chain F resid 541:613
13X-RAY DIFFRACTION13chain G resid 1:510
14X-RAY DIFFRACTION14chain G resid 541:613
15X-RAY DIFFRACTION15chain H resid 1:510
16X-RAY DIFFRACTION16chain H resid 541:613
17X-RAY DIFFRACTION17chain I resid 1:510
18X-RAY DIFFRACTION18chain I resid 541:613
19X-RAY DIFFRACTION19chain J resid 1:510
20X-RAY DIFFRACTION20chain J resid 541:613

+
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