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- PDB-3sqb: Structure of the major type 1 pilus subunit FimA bound to the Fim... -

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Basic information

Entry
Database: PDB / ID: 3sqb
TitleStructure of the major type 1 pilus subunit FimA bound to the FimC chaperone
Components
  • Chaperone protein fimC
  • Type-1 fimbrial protein, A chain
KeywordsSTRUCTURAL PROTEIN/CHAPERONE / immunoglobin-like fold / involved in type 1 pilus assembly / STRUCTURAL PROTEIN-CHAPERONE complex
Function / homology
Function and homology information


cell adhesion involved in single-species biofilm formation / pilus / chaperone-mediated protein folding / protein folding chaperone / cell wall organization / outer membrane-bounded periplasmic space / cell adhesion / identical protein binding
Similarity search - Function
Pili assembly chaperone, C-terminal / Pili assembly chaperone PapD, C-terminal domain / Pili assembly chaperone, bacterial / Pili assembly chaperone, conserved site / Pili assembly chaperone, C-terminal domain superfamily / Gram-negative pili assembly chaperone signature. / Pili assembly chaperone, N-terminal / Pili and flagellar-assembly chaperone, PapD N-terminal domain / PapD-like superfamily / Fimbrial-type adhesion domain ...Pili assembly chaperone, C-terminal / Pili assembly chaperone PapD, C-terminal domain / Pili assembly chaperone, bacterial / Pili assembly chaperone, conserved site / Pili assembly chaperone, C-terminal domain superfamily / Gram-negative pili assembly chaperone signature. / Pili assembly chaperone, N-terminal / Pili and flagellar-assembly chaperone, PapD N-terminal domain / PapD-like superfamily / Fimbrial-type adhesion domain / Fimbrial-type adhesion domain / Fimbrial protein / Fimbrial-type adhesion domain superfamily / Adhesion domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
DI(HYDROXYETHYL)ETHER / Type-1 fimbrial protein, A chain / Chaperone protein FimC
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.2 Å
AuthorsScharer, M.A. / Eidam, O. / Grutter, M.G. / Glockshuber, R. / Capitani, G.
CitationJournal: Nat.Chem.Biol. / Year: 2012
Title: Quality control of disulfide bond formation in pilus subunits by the chaperone FimC.
Authors: Crespo, M.D. / Puorger, C. / Scharer, M.A. / Eidam, O. / Grutter, M.G. / Capitani, G. / Glockshuber, R.
History
DepositionJul 5, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 30, 2012Provider: repository / Type: Initial release
Revision 1.1Aug 1, 2012Group: Database references
Revision 1.2Oct 17, 2012Group: Database references
Revision 1.3Sep 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_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_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

Downloads & links

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Assembly

Deposited unit
A: Chaperone protein fimC
B: Type-1 fimbrial protein, A chain
C: Chaperone protein fimC
D: Type-1 fimbrial protein, A chain
E: Chaperone protein fimC
F: Type-1 fimbrial protein, A chain
G: Chaperone protein fimC
H: Type-1 fimbrial protein, A chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)156,52915
Polymers155,8428
Non-polymers6877
Water86548
1
A: Chaperone protein fimC
B: Type-1 fimbrial protein, A chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,2795
Polymers38,9612
Non-polymers3183
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4030 Å2
ΔGint-7 kcal/mol
Surface area15760 Å2
MethodPISA
2
C: Chaperone protein fimC
D: Type-1 fimbrial protein, A chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,3296
Polymers38,9612
Non-polymers3684
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3720 Å2
ΔGint-9 kcal/mol
Surface area15750 Å2
MethodPISA
3
E: Chaperone protein fimC
F: Type-1 fimbrial protein, A chain


Theoretical massNumber of molelcules
Total (without water)38,9612
Polymers38,9612
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2630 Å2
ΔGint-13 kcal/mol
Surface area13500 Å2
MethodPISA
4
G: Chaperone protein fimC
H: Type-1 fimbrial protein, A chain


Theoretical massNumber of molelcules
Total (without water)38,9612
Polymers38,9612
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1400 Å2
ΔGint-7 kcal/mol
Surface area10150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)79.620, 142.180, 171.750
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11C
21A
12D
22B
13C
23E
33G
14D
24F
15D
25H

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111chain C and (resseq 5:23 or resseq 31:93 or resseq...C5 - 23
121chain C and (resseq 5:23 or resseq 31:93 or resseq...C31 - 93
131chain C and (resseq 5:23 or resseq 31:93 or resseq...C110 - 122
141chain C and (resseq 5:23 or resseq 31:93 or resseq...C130 - 175
151chain C and (resseq 5:23 or resseq 31:93 or resseq...C185 - 203
211chain A and (resseq 5:23 or resseq 31:93 or resseq...A5 - 23
221chain A and (resseq 5:23 or resseq 31:93 or resseq...A31 - 93
231chain A and (resseq 5:23 or resseq 31:93 or resseq...A110 - 122
241chain A and (resseq 5:23 or resseq 31:93 or resseq...A130 - 175
251chain A and (resseq 5:23 or resseq 31:93 or resseq...A185 - 203
112chain D and (resseq 17:24 or resseq 29:123 or resseq...D17 - 24
122chain D and (resseq 17:24 or resseq 29:123 or resseq...D29 - 123
132chain D and (resseq 17:24 or resseq 29:123 or resseq...D129 - 139
212chain B and (resseq 17:24 or resseq 29:123 or resseq...B17 - 24
222chain B and (resseq 17:24 or resseq 29:123 or resseq...B29 - 123
232chain B and (resseq 17:24 or resseq 29:123 or resseq...B129 - 139
113chain C and (resseq 1:73 or resseq 83:92 or resseq 101:136 )C1 - 73
123chain C and (resseq 1:73 or resseq 83:92 or resseq 101:136 )C83 - 92
133chain C and (resseq 1:73 or resseq 83:92 or resseq 101:136 )C101 - 136
213chain E and (resseq 1:70 or resseq 83:92 or resseq 101:136 )E1 - 70
223chain E and (resseq 1:70 or resseq 83:92 or resseq 101:136 )E83 - 92
233chain E and (resseq 1:70 or resseq 83:92 or resseq 101:136 )E101 - 136
313chain G and (resseq 1:73 or resseq 83:92 or resseq 102:117 )G1 - 73
323chain G and (resseq 1:73 or resseq 83:92 or resseq 102:117 )G83 - 92
333chain G and (resseq 1:73 or resseq 83:92 or resseq 102:117 )G102 - 117
114chain D and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )D18 - 25
124chain D and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )D29 - 37
134chain D and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )D48 - 119
144chain D and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )D129 - 137
154chain D and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )D149 - 158
214chain F and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )F18 - 25
224chain F and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )F29 - 37
234chain F and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )F48 - 119
244chain F and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )F129 - 137
254chain F and (resseq 18:25 or resseq 29:37 or resseq 48:119 or resseq 129:137 or resseq 149:158 )F149 - 158
115chain D and (resseq 18:25 or resseq 29:37 or resseq...D18 - 25
125chain D and (resseq 18:25 or resseq 29:37 or resseq...D29 - 37
135chain D and (resseq 18:25 or resseq 29:37 or resseq...D48 - 119
145chain D and (resseq 18:25 or resseq 29:37 or resseq...D123 - 124
155chain D and (resseq 18:25 or resseq 29:37 or resseq...D129 - 137
165chain D and (resseq 18:25 or resseq 29:37 or resseq...D149 - 159
215chain H and (resseq 18:25 or resseq 29:37 or resseq...H18 - 25
225chain H and (resseq 18:25 or resseq 29:37 or resseq...H29 - 37
235chain H and (resseq 18:25 or resseq 29:37 or resseq...H48 - 119
245chain H and (resseq 18:25 or resseq 29:37 or resseq...H123 - 124
255chain H and (resseq 18:25 or resseq 29:37 or resseq...H129 - 137
265chain H and (resseq 18:25 or resseq 29:37 or resseq...H149 - 159

NCS ensembles :
ID
1
2
3
4
5

NCS oper:
IDCodeMatrixVector
1given(-0.613277, 0.507624, 0.605152), (-0.404084, 0.456663, -0.792575), (-0.678681, -0.7306, -0.074938)57.580898, -29.633699, 5.34699
2given(-0.560904, 0.514493, 0.648602), (-0.417791, 0.500459, -0.758282), (-0.714729, -0.696303, -0.065759)56.660702, -27.167101, 8.0676
3given(0.584875, 0.669279, -0.458244), (0.397537, 0.255923, 0.881174), (0.707026, -0.697545, -0.11638)10.0167, 29.8234, -19.8197
4given(-0.99998, -0.000225, -0.006376), (-0.002046, 0.957876, 0.287175), (0.006043, 0.287182, -0.957857)23.0611, 22.693899, -72.037804
5given(0.561011, 0.678382, -0.47441), (0.401726, 0.277976, 0.872551), (0.723798, -0.680093, -0.116576)8.82329, 29.993299, -18.8909
6given(-0.999935, 0.011444, 3.96102), (0.010942, 0.954976, 0.296482), (0.003355, 0.296463, -0.955038)24.318899, 23.1724, -71.3563

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Components

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Protein , 2 types, 8 molecules ACEGBDFH

#1: Protein
Chaperone protein fimC


Mass: 23582.914 Da / Num. of mol.: 4 / Fragment: UNP residues 37-241
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: b4316, fimC, JW4279 / Plasmid: pfimChis-cyt / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P31697
#2: Protein
Type-1 fimbrial protein, A chain / Type-1A pilin


Mass: 15377.686 Da / Num. of mol.: 4 / Fragment: UNP residues 37-182
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Gene: b4314, fimA, JW4277, pilA / Plasmid: pfimAt-cyt / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P04128

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Non-polymers , 4 types, 55 molecules

#3: Chemical ChemComp-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C4H10O3
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 48 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsFOR CHAINS B,D,F,H: THE FIRST 13 RESIDUES OF FIMA WERE REMOVED FROM THE CONSTRUCT AND REPLACED BY A ...FOR CHAINS B,D,F,H: THE FIRST 13 RESIDUES OF FIMA WERE REMOVED FROM THE CONSTRUCT AND REPLACED BY A (HIS)6-TAG DIRECTLY BEFORE RESIDUE 14.

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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: 3.12 Å3/Da / Density % sol: 60.56 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.5
Details: 0.1 M sodium acetate, 0.2 M magnesium chloride, 13% PEG 4000, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 90.6 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.071 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Sep 24, 2006 / Details: dynamically bendable mirror
RadiationMonochromator: LN2-cooled fixed-exit Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.071 Å / Relative weight: 1
ReflectionResolution: 3.2→60 Å / Num. obs: 32913 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 7 % / Rmerge(I) obs: 0.138 / Net I/σ(I): 10.89
Reflection shell

Diffraction-ID: 1

Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. unique obs% possible all
3.2-3.30.7692.3419430284099.9
3.3-3.80.4364.61745351022499.9
3.8-40.2777.719635274099.7
4-50.12613.82600358218100
5-60.09817.29259433662100
6-80.08418.63204112972100
8-100.06822.4668571084100
10-200.05823.346113103499.3
20-300.0592254410793
30-400.0616.29652365.7
40-500.05714.158440
500.07910.677527.8

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation3.2 Å29.61 Å
Translation3.2 Å29.61 Å

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Processing

Software
NameVersionClassificationNB
XSCALEdata scaling
PHASER2.1.4phasing
PHENIX1.7.1_743refinement
PDB_EXTRACT3.1data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3BWU

3bwu


Resolution: 3.2→58.386 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.96 / Isotropic thermal model: isotropic / σ(F): 1.99 / Phase error: 29.47 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.3004 1021 3.11 %random
Rwork0.2605 ---
obs0.2617 32880 99.84 %-
Solvent computationShrinkage radii: 0.83 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 86.253 Å2 / ksol: 0.296 e/Å3
Displacement parametersBiso max: 264.09 Å2 / Biso mean: 103.8051 Å2 / Biso min: 27.22 Å2
Baniso -1Baniso -2Baniso -3
1--0.6446 Å20 Å2-0 Å2
2--3.8113 Å2-0 Å2
3----3.1667 Å2
Refinement stepCycle: LAST / Resolution: 3.2→58.386 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7747 0 45 48 7840
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0057878
X-RAY DIFFRACTIONf_angle_d0.82710743
X-RAY DIFFRACTIONf_chiral_restr0.0711331
X-RAY DIFFRACTIONf_plane_restr0.0031407
X-RAY DIFFRACTIONf_dihedral_angle_d13.6612630
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11C1178X-RAY DIFFRACTIONPOSITIONAL0.046
12A1178X-RAY DIFFRACTIONPOSITIONAL0.046
21D778X-RAY DIFFRACTIONPOSITIONAL0.066
22B778X-RAY DIFFRACTIONPOSITIONAL0.066
31C748X-RAY DIFFRACTIONPOSITIONAL0.09
32E748X-RAY DIFFRACTIONPOSITIONAL0.09
33G480X-RAY DIFFRACTIONPOSITIONAL0.063
41D528X-RAY DIFFRACTIONPOSITIONAL0.033
42F528X-RAY DIFFRACTIONPOSITIONAL0.033
51D402X-RAY DIFFRACTIONPOSITIONAL0.024
52H402X-RAY DIFFRACTIONPOSITIONAL0.024
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 7

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection allNum. reflection obs% reflection obs (%)
3.2-3.36870.32621420.2822444245844584100
3.3687-3.57970.35741450.2839450946544654100
3.5797-3.85610.32271430.2946448646294629100
3.8561-4.2440.28441440.2414450446484648100
4.244-4.85790.25481460.208455547014703100
4.8579-6.11940.25471480.2395460947574757100
6.1194-58.39570.33991530.291547544907490799
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)
12.2099-0.786-0.95761.4734-1.37932.91940.00880.8356-0.5641-0.90030.39550.15160.4077-0.337-0.1770.7022-0.0840.03560.5624-0.25610.278332.8558-32.8936-33.0924
20.55510.9771-0.62533.0170.90893.6614-0.36450.3885-0.0998-0.78880.3168-0.0426-0.1468-0.10740.02910.5629-0.0198-0.00160.3566-0.03090.202237.118-25.7983-26.133
30.0938-0.0103-0.0750.00070.00880.062-0.19420.40340.2083-0.1591-0.05690.05860.07790.0294-0.04421.5922-0.4561-0.57091.33990.23750.760422.1994-23.3217-50.8583
42.6481.8998-1.74075.708-1.93014.6688-0.0911.23451.7761-0.2522-0.08230.10370.0472-0.15050.09481.03410.0498-0.47640.87780.47821.215921.9513-6.0207-44.2048
57.0748-5.33530.60874.44150.34331.63890.00721.51461.3362-2.2304-0.0776-0.4195-0.4443-0.32360.03611.1706-0.1866-0.27941.14010.36340.703730.9483-11.9734-47.2336
63.69210.78740.85213.31061.24595.03420.07170.3410.053-0.537-0.0453-0.7499-0.07880.58-0.0280.4545-0.05480.08870.26290.11160.429949.8809-10.6924-17.9016
74.62913.23634.43095.21415.68359.32310.1370.11050.0771-0.75190.0869-0.00820.2347-0.6253-0.3230.62940.01990.05490.46370.12950.405342.2525-14.1932-26.1497
81.2547-1.6841-1.4335.18160.52842.3184-0.0054-0.4575-0.0770.74080.1234-0.0695-0.2326-0.3433-0.09240.313-0.0686-0.0410.35240.06140.53280.5478-31.80459.6651
93.0848-0.4264-1.83690.941-1.47345.15850.0952-0.0333-0.1947-0.02990.09650.22180.40570.0956-0.17390.38690.0678-0.07670.20450.09650.56376.104-34.81271.6301
109.11084.9057-7.89996.6566-2.11238.29921.0889-0.83330.9281.8983-0.21650.6504-2.0025-0.9003-0.89480.8675-0.23760.25120.7383-0.08790.73810.994-8.719910.7081
112.06790.90850.21244.10980.13152.6115-0.08390.25440.5487-0.11660.1128-0.2104-0.59790.3637-0.09320.8235-0.32890.19520.2346-0.24331.020914.3916-6.0024-3.2602
121.77071.1251-1.35128.3527-3.97827.03210.34410.08031.4710.18770.36280.8826-0.5316-0.3064-0.6330.41550.04920.00230.45990.01661.1395.1501-8.8415-4.6972
139.0676-2.8842-4.11813.96142.25235.0187-0.01970.686-0.9327-0.6089-0.22150.69880.3494-0.42980.17080.666-0.179-0.1870.53650.03610.486411.3612-39.5599-18.5815
148.5341-5.3949-2.78925.53384.27574.408-0.1877-0.43750.651-0.77490.4314-0.4582-0.1141-0.3991-0.17790.6815-0.0499-0.02130.33770.13650.59428.9207-32.1226-10.7096
153.7532-2.9019-3.37583.13441.77823.8206-0.27610.8876-1.51310.21170.50520.1402-0.09480.4459-0.24310.82670.01430.04432.189-0.25650.8138-11.2467-41.9922-53.8106
161.9630.06982.91281.2552-0.19716.9721-0.0942-0.3131-0.0840.08210.1620.65130.2433-0.72190.35070.9572-0.14920.04672.6402-0.46240.1251-14.6484-33.714-58.8752
172.6912.3348-0.63046.1941-6.58188.8885-0.3963-0.1987-0.23640.17540.4855-0.25110.93482.22130.04570.8464-0.01920.10243.34370.2510.7851.4658-37.5339-34.3478
182.893-3.0516-0.18294.7315-0.00290.0342-0.1245-0.10840.68531.8368-0.9319-1.1218-0.90570.26111.01411.2353-0.155-0.30352.16910.08880.66121.3433-20.6258-36.0683
192.4023-0.25941.0528.42845.33284.00050.6006-0.5743-0.16290.972-1.59890.5802-0.2554-0.13960.92691.17140.05950.00281.6753-0.15890.5091-7.5685-25.4529-33.8441
202.2047-0.89330.13212.9846-0.49135.3478-0.6817-0.0357-0.14470.50670.69380.4479-1.793-0.04250.04261.24890.0954-0.03981.703-0.20470.6201-27.3189-21.3466-55.0779
214.3042-2.72665.14027.8232-6.01188.44930.2949-0.01310.04941.1039-0.1079-0.3826-1.68520.5157-0.20011.2148-0.22450.08351.7436-0.18870.5635-18.5071-23.4651-53.7921
221.598-0.0953-0.75410.26420.97883.64640.3226-0.9219-0.04380.0997-0.2424-0.3524-0.2431.8629-0.09730.7840.03280.10213.2181-0.61850.816424.3821-31.8901-93.1697
233.43851.6837-3.61590.9568-1.74319.784-0.5012-1.2615-0.05650.37970.0134-0.51220.70472.04540.1320.9484-0.1310.09572.3776-0.77690.833217.6498-36.8122-86.1883
242.237-0.4619-1.35123.97570.13330.8452-0.462-0.3258-1.12520.39120.0027-0.7030.05571.68940.57130.78940.0890.12142.7698-0.07020.8659.8987-45.5553-68.6758
251.30550.2293-0.76921.52540.99842.2628-0.6524-0.7413-0.60490.16670.3956-0.30160.07970.93390.24460.9163-0.13690.46362.2682-0.36140.82413.0822-39.0277-75.2463
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and (resid 1: 25 or resid 46: 52 or resid 60: 75))A1 - 25
2X-RAY DIFFRACTION1(chain A and (resid 1: 25 or resid 46: 52 or resid 60: 75))A46 - 52
3X-RAY DIFFRACTION1(chain A and (resid 1: 25 or resid 46: 52 or resid 60: 75))A60 - 75
4X-RAY DIFFRACTION2(chain A and (resid 53: 59 or resid 26: 45 or resid 76:116))A53 - 59
5X-RAY DIFFRACTION2(chain A and (resid 53: 59 or resid 26: 45 or resid 76:116))A26 - 45
6X-RAY DIFFRACTION2(chain A and (resid 53: 59 or resid 26: 45 or resid 76:116))A76 - 116
7X-RAY DIFFRACTION3(chain A and (resid 117:130))A117 - 130
8X-RAY DIFFRACTION4(chain A and (resid 131:147 or resid 168:182))A131 - 147
9X-RAY DIFFRACTION4(chain A and (resid 131:147 or resid 168:182))A168 - 182
10X-RAY DIFFRACTION5(chain A and (resid 148:167 or resid 183:206))A148 - 167
11X-RAY DIFFRACTION5(chain A and (resid 148:167 or resid 183:206))A183 - 206
12X-RAY DIFFRACTION6(chain B and (resid 1: 59 or resid 79:110 or resid 121:144))B1 - 59
13X-RAY DIFFRACTION6(chain B and (resid 1: 59 or resid 79:110 or resid 121:144))B79 - 110
14X-RAY DIFFRACTION6(chain B and (resid 1: 59 or resid 79:110 or resid 121:144))B121 - 144
15X-RAY DIFFRACTION7(chain B and (resid 60: 76 or resid 111:120 or resid 145:159))B60 - 76
16X-RAY DIFFRACTION7(chain B and (resid 60: 76 or resid 111:120 or resid 145:159))B111 - 120
17X-RAY DIFFRACTION7(chain B and (resid 60: 76 or resid 111:120 or resid 145:159))B145 - 159
18X-RAY DIFFRACTION8(chain C and (resid 1: 25 or resid 46: 52 or resid 60: 75))C1 - 25
19X-RAY DIFFRACTION8(chain C and (resid 1: 25 or resid 46: 52 or resid 60: 75))C46 - 52
20X-RAY DIFFRACTION8(chain C and (resid 1: 25 or resid 46: 52 or resid 60: 75))C60 - 75
21X-RAY DIFFRACTION9(chain C and (resid 53: 59 or resid 26: 45 or resid 76:116))C53 - 59
22X-RAY DIFFRACTION9(chain C and (resid 53: 59 or resid 26: 45 or resid 76:116))C26 - 45
23X-RAY DIFFRACTION9(chain C and (resid 53: 59 or resid 26: 45 or resid 76:116))C76 - 116
24X-RAY DIFFRACTION10(chain C and (resid 117:130))C117 - 130
25X-RAY DIFFRACTION11(chain C and (resid 131:147 or resid 168:182))C131 - 147
26X-RAY DIFFRACTION11(chain C and (resid 131:147 or resid 168:182))C168 - 182
27X-RAY DIFFRACTION12(chain C and (resid 148:167 or resid 183:206))C148 - 167
28X-RAY DIFFRACTION12(chain C and (resid 148:167 or resid 183:206))C183 - 206
29X-RAY DIFFRACTION13(chain D and (resid 1: 59 or resid 79:110 or resid 121:144))D1 - 59
30X-RAY DIFFRACTION13(chain D and (resid 1: 59 or resid 79:110 or resid 121:144))D79 - 110
31X-RAY DIFFRACTION13(chain D and (resid 1: 59 or resid 79:110 or resid 121:144))D121 - 144
32X-RAY DIFFRACTION14(chain D and (resid 60: 76 or resid 111:120 or resid 145:159))D60 - 76
33X-RAY DIFFRACTION14(chain D and (resid 60: 76 or resid 111:120 or resid 145:159))D111 - 120
34X-RAY DIFFRACTION14(chain D and (resid 60: 76 or resid 111:120 or resid 145:159))D145 - 159
35X-RAY DIFFRACTION15(chain E and (resid 1: 25 or resid 46: 52 or resid 60: 75))E1 - 25
36X-RAY DIFFRACTION15(chain E and (resid 1: 25 or resid 46: 52 or resid 60: 75))E46 - 52
37X-RAY DIFFRACTION15(chain E and (resid 1: 25 or resid 46: 52 or resid 60: 75))E60 - 75
38X-RAY DIFFRACTION16(chain E and (resid 53: 59 or resid 26: 45 or resid 76:116))E53 - 59
39X-RAY DIFFRACTION16(chain E and (resid 53: 59 or resid 26: 45 or resid 76:116))E26 - 45
40X-RAY DIFFRACTION16(chain E and (resid 53: 59 or resid 26: 45 or resid 76:116))E76 - 116
41X-RAY DIFFRACTION17(chain E and (resid 117:130))E117 - 130
42X-RAY DIFFRACTION18(chain E and (resid 131:147 or resid 168:182))E131 - 147
43X-RAY DIFFRACTION18(chain E and (resid 131:147 or resid 168:182))E168 - 182
44X-RAY DIFFRACTION19(chain E and (resid 148:167 or resid 183:206))E148 - 167
45X-RAY DIFFRACTION19(chain E and (resid 148:167 or resid 183:206))E183 - 206
46X-RAY DIFFRACTION20(chain F and (resid 1: 59 or resid 79:110 or resid 121:144))F1 - 59
47X-RAY DIFFRACTION20(chain F and (resid 1: 59 or resid 79:110 or resid 121:144))F79 - 110
48X-RAY DIFFRACTION20(chain F and (resid 1: 59 or resid 79:110 or resid 121:144))F121 - 144
49X-RAY DIFFRACTION21(chain F and (resid 60: 76 or resid 111:120 or resid 145:159))F60 - 76
50X-RAY DIFFRACTION21(chain F and (resid 60: 76 or resid 111:120 or resid 145:159))F111 - 120
51X-RAY DIFFRACTION21(chain F and (resid 60: 76 or resid 111:120 or resid 145:159))F145 - 159
52X-RAY DIFFRACTION22(chain G and (resid 1: 25 or resid 46: 52 or resid 60: 75))G1 - 25
53X-RAY DIFFRACTION22(chain G and (resid 1: 25 or resid 46: 52 or resid 60: 75))G46 - 52
54X-RAY DIFFRACTION22(chain G and (resid 1: 25 or resid 46: 52 or resid 60: 75))G60 - 75
55X-RAY DIFFRACTION23(chain G and (resid 53: 59 or resid 26: 45 or resid 76:116))G53 - 59
56X-RAY DIFFRACTION23(chain G and (resid 53: 59 or resid 26: 45 or resid 76:116))G26 - 45
57X-RAY DIFFRACTION23(chain G and (resid 53: 59 or resid 26: 45 or resid 76:116))G76 - 116
58X-RAY DIFFRACTION24(chain H and (resid 1: 59 or resid 79:110 or resid 121:144))H1 - 59
59X-RAY DIFFRACTION24(chain H and (resid 1: 59 or resid 79:110 or resid 121:144))H79 - 110
60X-RAY DIFFRACTION24(chain H and (resid 1: 59 or resid 79:110 or resid 121:144))H121 - 144
61X-RAY DIFFRACTION25(chain H and (resid 60: 76 or resid 111:120 or resid 145:159))H60 - 76
62X-RAY DIFFRACTION25(chain H and (resid 60: 76 or resid 111:120 or resid 145:159))H111 - 120
63X-RAY DIFFRACTION25(chain H and (resid 60: 76 or resid 111:120 or resid 145:159))H145 - 159

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