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- PDB-3glg: Crystal Structure of a Mutant (gammaT157A) E. coli Clamp Loader B... -

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Basic information

Entry
Database: PDB / ID: 3glg
TitleCrystal Structure of a Mutant (gammaT157A) E. coli Clamp Loader Bound to Primer-Template DNA
Components
  • (DNA polymerase III subunit ...) x 3
  • DNA (5'-D(*CP*TP*GP*GP*CP*CP*TP*AP*TP*A)-3')
  • DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*AP*TP*AP*GP*GP*CP*CP*AP*G)-3')
KeywordsTransferase/DNA / AAA+ ATPase / Clamp Loader / Gamma Complex / Replication / DNA replication / DNA-directed DNA polymerase / Nucleotidyltransferase / Transferase / ATP-binding / Nucleotide-binding / Transferase-DNA COMPLEX
Function / homology
Function and homology information


DNA polymerase III, clamp loader complex / DNA polymerase III complex / replisome / DNA polymerase processivity factor activity / 3'-5' exonuclease activity / ribonucleoside triphosphate phosphatase activity / DNA-templated DNA replication / DNA-directed DNA polymerase / DNA replication / DNA-directed DNA polymerase activity ...DNA polymerase III, clamp loader complex / DNA polymerase III complex / replisome / DNA polymerase processivity factor activity / 3'-5' exonuclease activity / ribonucleoside triphosphate phosphatase activity / DNA-templated DNA replication / DNA-directed DNA polymerase / DNA replication / DNA-directed DNA polymerase activity / viral translational frameshifting / DNA clamp loader activity / ATP hydrolysis activity / DNA binding / ATP binding / identical protein binding / metal ion binding
Similarity search - Function
DNA polymerase III, delta prime subunit / DNA polymerase III, delta subunit, C-terminal / : / DNA polymerase III, delta subunit, C terminal / DNA polymerase III subunit delta', AAA+ ATPase lid domain / DNA polymerase III subunit delta, C-terminal / Processivity clamp loader gamma complex DNA pol III C-term / DNA polymerase III, delta subunit / DNA polymerase III delta, N-terminal / : ...DNA polymerase III, delta prime subunit / DNA polymerase III, delta subunit, C-terminal / : / DNA polymerase III, delta subunit, C terminal / DNA polymerase III subunit delta', AAA+ ATPase lid domain / DNA polymerase III subunit delta, C-terminal / Processivity clamp loader gamma complex DNA pol III C-term / DNA polymerase III, delta subunit / DNA polymerase III delta, N-terminal / : / DNA polymerase III, delta subunit / DNA polymerase III, tau subunit, domain V / DNA polymerase III subunit tau, DnaB-binding domain IV / DNA polymerase III, tau subunit, domain V superfamily / DNA polymerase III subunits tau domain IV DnaB-binding / DNA polymerase III tau subunit V interacting with alpha / DNA polymerase III, subunit gamma/tau, helical lid domain / DNA polymerase III clamp loader subunit, ATPase lid domain / DNA polymerase III, subunit gamma/ tau, N-terminal / DNA polymerase III, gamma subunit, domain III / DNA polymerase III subunits gamma and tau domain III / Zinc Finger, Delta Prime; domain 3 - #10 / Zinc Finger, Delta Prime; domain 3 / DNA polymerase III, delta subunit / : / Ubiquitin-associated (UBA) domain / DNA polymerase III, clamp loader complex, gamma/delta/delta subunit, C-terminal / ClpA/B family / Helicase, Ruva Protein; domain 3 - #60 / Helicase, Ruva Protein; domain 3 / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / Up-down Bundle / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ADENOSINE-5'-DIPHOSPHATE / BERYLLIUM TRIFLUORIDE ION / DNA / DNA (> 10) / DNA polymerase III subunit tau / DNA polymerase III subunit delta / DNA polymerase III subunit delta'
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.25 Å
AuthorsSimonetta, K.R. / Seyedin, S.N. / Kuriyan, J.
CitationJournal: Cell(Cambridge,Mass.) / Year: 2009
Title: The mechanism of ATP-dependent primer-template recognition by a clamp loader complex.
Authors: Simonetta, K.R. / Kazmirski, S.L. / Goedken, E.R. / Cantor, A.J. / Kelch, B.A. / McNally, R. / Seyedin, S.N. / Makino, D.L. / O'Donnell, M. / Kuriyan, J.
History
DepositionMar 12, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 26, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 10, 2012Group: Database references
Revision 1.3Oct 20, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_conn_angle ...database_2 / pdbx_struct_conn_angle / 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 / _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_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _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_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _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.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
Revision 1.4Feb 21, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA polymerase III subunit delta
B: DNA polymerase III subunit tau
C: DNA polymerase III subunit tau
D: DNA polymerase III subunit tau
E: DNA polymerase III subunit delta'
F: DNA polymerase III subunit delta
G: DNA polymerase III subunit tau
H: DNA polymerase III subunit tau
I: DNA polymerase III subunit tau
J: DNA polymerase III subunit delta'
K: DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*AP*TP*AP*GP*GP*CP*CP*AP*G)-3')
L: DNA (5'-D(*CP*TP*GP*GP*CP*CP*TP*AP*TP*A)-3')
M: DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*AP*TP*AP*GP*GP*CP*CP*AP*G)-3')
N: DNA (5'-D(*CP*TP*GP*GP*CP*CP*TP*AP*TP*A)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)436,89540
Polymers433,26714
Non-polymers3,62826
Water00
1
A: DNA polymerase III subunit delta
B: DNA polymerase III subunit tau
C: DNA polymerase III subunit tau
D: DNA polymerase III subunit tau
E: DNA polymerase III subunit delta'
K: DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*AP*TP*AP*GP*GP*CP*CP*AP*G)-3')
L: DNA (5'-D(*CP*TP*GP*GP*CP*CP*TP*AP*TP*A)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)218,44820
Polymers216,6337
Non-polymers1,81413
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area26280 Å2
ΔGint-142 kcal/mol
Surface area74580 Å2
MethodPISA
2
F: DNA polymerase III subunit delta
G: DNA polymerase III subunit tau
H: DNA polymerase III subunit tau
I: DNA polymerase III subunit tau
J: DNA polymerase III subunit delta'
M: DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*AP*TP*AP*GP*GP*CP*CP*AP*G)-3')
N: DNA (5'-D(*CP*TP*GP*GP*CP*CP*TP*AP*TP*A)-3')
hetero molecules


Theoretical massNumber of molelcules
Total (without water)218,44820
Polymers216,6337
Non-polymers1,81413
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area26900 Å2
ΔGint-142 kcal/mol
Surface area75580 Å2
MethodPISA
Unit cell
Length a, b, c (Å)100.102, 219.104, 274.664
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain C and (resseq 4:368 or resseq 400:403)
21chain H and (resseq 4:368 or resseq 400:403)
12chain D and (resseq 2:363 or resseq 400:403)
22chain I and (resseq 2:363 or resseq 400:403)
13chain B and (resseq 5:368 or resseq 400:403)
23chain G and (resseq 5:368 or resseq 400:403)
14chain E and (resseq 1:334 or resseq 403)
24chain J and (resseq 1:334 or resseq 403)
15chain A and (resseq 1:333 )
25chain F and (resseq 1:333 )
16chain K or chain L
26chain M or chain N

NCS domain segments:
Dom-IDComponent-IDEns-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111CC4 - 3684 - 368
121CC400 - 403400 - 403
211HH4 - 3684 - 368
221HH400 - 403400 - 403
112DD2 - 3632 - 363
122DD400 - 403400 - 403
212II2 - 3632 - 363
222II400 - 403400 - 403
113BB5 - 3685 - 368
123BB400 - 403400 - 403
213GG5 - 3685 - 368
223GG400 - 403400 - 403
114EE1 - 3341 - 334
124EE403 - 0403 - 0
214JJ1 - 3341 - 334
224JJ403 - 0403 - 0
115AA1 - 3331 - 333
215FF1 - 3331 - 333
116KK7 - 207 - 20
216MM7 - 207 - 20

NCS ensembles :
ID
1
2
3
4
5
6

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Components

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DNA polymerase III subunit ... , 3 types, 10 molecules AFBCDGHIEJ

#1: Protein DNA polymerase III subunit delta


Mass: 38745.574 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K-12 / Gene: holA, b0640, JW0635 / Production host: Escherichia coli (E. coli) / References: UniProt: P28630, DNA-directed DNA polymerase
#2: Protein
DNA polymerase III subunit tau / DNA polymerase III subunit gamma


Mass: 43925.484 Da / Num. of mol.: 6 / Fragment: UNP residues 1-373 / Mutation: T157A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K-12 / Gene: dnaX, dnaZ, dnaZX, b0470, JW0459 / Production host: Escherichia coli (E. coli) / References: UniProt: P06710, DNA-directed DNA polymerase
#3: Protein DNA polymerase III subunit delta'


Mass: 36980.484 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K-12 / Gene: holB, b1099, JW1085 / Production host: Escherichia coli (E. coli) / References: UniProt: P28631, DNA-directed DNA polymerase

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DNA chain , 2 types, 4 molecules KMLN

#4: DNA chain DNA (5'-D(*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*TP*AP*TP*AP*GP*GP*CP*CP*AP*G)-3')


Mass: 6110.958 Da / Num. of mol.: 2 / Source method: obtained synthetically
#5: DNA chain DNA (5'-D(*CP*TP*GP*GP*CP*CP*TP*AP*TP*A)-3')


Mass: 3019.991 Da / Num. of mol.: 2 / Source method: obtained synthetically

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Non-polymers , 4 types, 26 molecules

#6: Chemical
ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#7: Chemical
ChemComp-BEF / BERYLLIUM TRIFLUORIDE ION


Mass: 66.007 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: BeF3
#8: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#9: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn

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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: 3.48 Å3/Da / Density % sol: 64.61 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 9% PEG 400, 150 mM MgCl2, 100 mM HEPES, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 8.2.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Mar 27, 2008
RadiationMonochromator: KOHZU / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.25→50 Å / Num. all: 95863 / Num. obs: 94904 / % possible obs: 99 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1
Reflection shellResolution: 3.25→3.37 Å / % possible all: 92.3

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASESphasing
PHENIX(phenix.refine)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.25→49.24 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.35 / σ(F): 1.33 / Phase error: 27.76 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.263 4742 5.02 %Copied from a lower resolution data set of a wildtype complex in the same crystal form (which had been chosen at random) and extended to the higher resolution at random using the ImportScaled program of the CCP4 program suite.
Rwork0.224 ---
obs0.226 94510 98.62 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 61.396 Å2 / ksol: 0.31 e/Å3
Displacement parametersBiso max: 260.28 Å2 / Biso mean: 119.381 Å2 / Biso min: 61.28 Å2
Baniso -1Baniso -2Baniso -3
1-9.968 Å2-0 Å2-0 Å2
2---0.712 Å20 Å2
3----9.256 Å2
Refinement stepCycle: LAST / Resolution: 3.25→49.24 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27572 974 200 0 28746
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01629406
X-RAY DIFFRACTIONf_angle_d1.75140173
X-RAY DIFFRACTIONf_dihedral_angle_d19.51111045
X-RAY DIFFRACTIONf_chiral_restr0.14619
X-RAY DIFFRACTIONf_plane_restr0.0075013
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11C2869X-RAY DIFFRACTIONPOSITIONAL
12H2869X-RAY DIFFRACTIONPOSITIONAL0.078
21D2849X-RAY DIFFRACTIONPOSITIONAL
22I2849X-RAY DIFFRACTIONPOSITIONAL0.098
31B2860X-RAY DIFFRACTIONPOSITIONAL
32G2860X-RAY DIFFRACTIONPOSITIONAL0.071
41E2602X-RAY DIFFRACTIONPOSITIONAL
42J2602X-RAY DIFFRACTIONPOSITIONAL0.091
51A2650X-RAY DIFFRACTIONPOSITIONAL
52F2650X-RAY DIFFRACTIONPOSITIONAL0.065
61K487X-RAY DIFFRACTIONPOSITIONAL
62M487X-RAY DIFFRACTIONPOSITIONAL0.087
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.25-3.28740.35971400.32042594X-RAY DIFFRACTION87
3.2874-3.32610.34511360.32252777X-RAY DIFFRACTION93
3.3261-3.36660.36281560.31562859X-RAY DIFFRACTION96
3.3666-3.40920.31431400.30132970X-RAY DIFFRACTION98
3.4092-3.45410.29171450.29612951X-RAY DIFFRACTION98
3.4541-3.50140.28551540.28632953X-RAY DIFFRACTION99
3.5014-3.55140.33421530.28593008X-RAY DIFFRACTION99
3.5514-3.60440.33491550.27032981X-RAY DIFFRACTION99
3.6044-3.66070.27971620.26582995X-RAY DIFFRACTION100
3.6607-3.72070.29291790.25652980X-RAY DIFFRACTION100
3.7207-3.78480.27041580.24782963X-RAY DIFFRACTION100
3.7848-3.85360.29451490.25353056X-RAY DIFFRACTION100
3.8536-3.92770.33931450.24022959X-RAY DIFFRACTION99
3.9277-4.00780.30571720.23073022X-RAY DIFFRACTION100
4.0078-4.09490.26141470.22482984X-RAY DIFFRACTION100
4.0949-4.19010.25341540.23353014X-RAY DIFFRACTION99
4.1901-4.29490.27831820.21752970X-RAY DIFFRACTION99
4.2949-4.41090.2451550.20042983X-RAY DIFFRACTION99
4.4109-4.54060.25571530.19583037X-RAY DIFFRACTION99
4.5406-4.68710.24221640.19352963X-RAY DIFFRACTION99
4.6871-4.85450.23971660.19783013X-RAY DIFFRACTION99
4.8545-5.04860.25761450.19133047X-RAY DIFFRACTION100
5.0486-5.27820.27151290.20073078X-RAY DIFFRACTION100
5.2782-5.55610.24771680.20733019X-RAY DIFFRACTION100
5.5561-5.90370.25381690.19943052X-RAY DIFFRACTION100
5.9037-6.35860.26121730.2053029X-RAY DIFFRACTION100
6.3586-6.99690.25551750.19973062X-RAY DIFFRACTION100
6.9969-8.00560.21341770.16743089X-RAY DIFFRACTION100
8.0056-10.0720.16611690.13393139X-RAY DIFFRACTION100
10.072-49.24580.21161720.20543221X-RAY DIFFRACTION99
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)
13.6490.8319-0.17172.56642.57522.64850.1863-0.5412-0.47360.8421-0.59020.49360.61-0.830701.21210.0966-0.25611.3541-0.30761.52157.487920.288550.7535
23.79191.10140.2623.2648-0.08321.9503-0.1405-0.10940.7178-0.3309-0.1750.2246-0.7355-0.1919-00.96410.1296-0.19110.6204-0.21831.083735.951539.374450.3365
34.0233-1.5893-0.01721.14990.63511.3504-0.0893-0.02320.2666-0.31540.0114-0.645-0.48270.6477-00.5974-0.2440.08210.9983-0.17341.026366.979725.61648.3568
41.08160.01520.03023.65290.06332.5022-0.0937-0.1388-0.26940.35210.3585-0.81310.51620.768500.52880.2566-0.10431.0458-0.36641.023772.3106-8.190148.8575
51.6331.49781.34742.13831.3812.05750.0611-0.216-0.07990.75830.112-0.03760.88220.046601.26540.1004-0.01090.6416-0.06230.67849.6467-27.586547.3323
61.14411.22561.85771.1977-0.54882.5428-0.02520.7890.775-0.1229-0.0329-0.4289-0.72350.888401.487-0.00690.00441.09970.13991.794511.926122.7226-44.1117
72.61281.8091-0.52292.4406-0.9622.5017-0.18660.12370.6312-0.16810.04160.7684-0.363-0.508500.80120.17540.00370.72750.05651.2148-16.2543-0.223-45.0557
81.4089-0.45490.38275.8085-0.681.6895-0.17490.0303-0.0215-0.12940.16720.56650.0033-0.383500.4981-0.08330.09250.61250.08730.5212-11.9308-32.7179-43.4286
93.936-1.02281.05561.65210.15853.09970.14060.1767-0.4516-0.0852-0.1191-0.21530.54770.242-00.7404-0.00560.15090.4130.09490.473918.2925-48.5835-43.2876
103.42391.43381.05911.57310.38882.7573-0.02810.33870.0966-0.3660.1155-0.47280.34720.7977-00.58810.0590.2220.89350.07750.670943.7628-33.7347-40.5657
112.08510.0626-0.20062.66810.53392.0387-0.03120.19550.4201-0.42750.1256-0.4716-0.44230.6279-00.839-0.0267-0.00120.8854-0.08450.686148.641-2.547717.8309
121.75540.08070.59492.5627-0.09921.0531-0.0265-0.310.03260.27380.09460.3561-0.0629-0.2675-00.71640.01520.10740.74030.02690.525119.5827-24.8787-11.9919
130.391-0.8445-0.57352.11740.50570.20760.68260.32820.0682-0.22630.04130.50510.5104-1.110300.8520.0159-0.0631.0577-0.19320.719337.33856.029652.1728
142.1227-1.77720.50760.1477-1.25470.06340.00770.11310.57150.21490.5332-0.3634-0.97320.97340.00181.1162-0.1215-0.0680.80520.14120.632516.1223-10.8996-46.2895
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resseq 1:211A1 - 211
2X-RAY DIFFRACTION2(chain B and resseq 5:246) or (chain B and (resseq 400:403))B5 - 246
3X-RAY DIFFRACTION2(chain B and resseq 5:246) or (chain B and (resseq 400:403))B400 - 403
4X-RAY DIFFRACTION3(chain C and resseq 4:246) or (chain C and (resseq 400:403))C4 - 246
5X-RAY DIFFRACTION3(chain C and resseq 4:246) or (chain C and (resseq 400:403))C400 - 403
6X-RAY DIFFRACTION4(chain D and resseq 2:246) or (chain D and (resseq 400:403))D2 - 246
7X-RAY DIFFRACTION4(chain D and resseq 2:246) or (chain D and (resseq 400:403))D400 - 403
8X-RAY DIFFRACTION5(chain E and resseq 1:207) or (chain E and resseq 403)E1 - 207
9X-RAY DIFFRACTION5(chain E and resseq 1:207) or (chain E and resseq 403)E403
10X-RAY DIFFRACTION6chain F and resseq 1:211F1 - 211
11X-RAY DIFFRACTION7(chain G and resseq -9:246) or (chain G and (resseq 400:403))G-9 - 246
12X-RAY DIFFRACTION7(chain G and resseq -9:246) or (chain G and (resseq 400:403))G400 - 403
13X-RAY DIFFRACTION8(chain H and resseq 4:246) or (chain H and (resseq 400:403))H4 - 246
14X-RAY DIFFRACTION8(chain H and resseq 4:246) or (chain H and (resseq 400:403))H400 - 403
15X-RAY DIFFRACTION9(chain I and resseq 2:246) or (chain I and (resseq 400:403))I2 - 246
16X-RAY DIFFRACTION9(chain I and resseq 2:246) or (chain I and (resseq 400:403))I400 - 403
17X-RAY DIFFRACTION10(chain J and resseq 1:207) or (chain J and resseq 403)J1 - 207
18X-RAY DIFFRACTION10(chain J and resseq 1:207) or (chain J and resseq 403)J403
19X-RAY DIFFRACTION11(chain A and resseq 212:333) or (chain B and resseq 247:368) or (chain C and resseq 247:368) or (chain D and resseq 247:363) or (chain E and resseq 208:334)A212 - 333
20X-RAY DIFFRACTION11(chain A and resseq 212:333) or (chain B and resseq 247:368) or (chain C and resseq 247:368) or (chain D and resseq 247:363) or (chain E and resseq 208:334)B247 - 368
21X-RAY DIFFRACTION11(chain A and resseq 212:333) or (chain B and resseq 247:368) or (chain C and resseq 247:368) or (chain D and resseq 247:363) or (chain E and resseq 208:334)C247 - 368
22X-RAY DIFFRACTION11(chain A and resseq 212:333) or (chain B and resseq 247:368) or (chain C and resseq 247:368) or (chain D and resseq 247:363) or (chain E and resseq 208:334)D247 - 363
23X-RAY DIFFRACTION11(chain A and resseq 212:333) or (chain B and resseq 247:368) or (chain C and resseq 247:368) or (chain D and resseq 247:363) or (chain E and resseq 208:334)E208 - 334
24X-RAY DIFFRACTION12(chain F and resseq 212:333) or (chain G and resseq 247:368) or (chain H and resseq 247:368) or (chain I and resseq 247:363) or (chain J and resseq 208:334)F212 - 333
25X-RAY DIFFRACTION12(chain F and resseq 212:333) or (chain G and resseq 247:368) or (chain H and resseq 247:368) or (chain I and resseq 247:363) or (chain J and resseq 208:334)G247 - 368
26X-RAY DIFFRACTION12(chain F and resseq 212:333) or (chain G and resseq 247:368) or (chain H and resseq 247:368) or (chain I and resseq 247:363) or (chain J and resseq 208:334)H247 - 368
27X-RAY DIFFRACTION12(chain F and resseq 212:333) or (chain G and resseq 247:368) or (chain H and resseq 247:368) or (chain I and resseq 247:363) or (chain J and resseq 208:334)I247 - 363
28X-RAY DIFFRACTION12(chain F and resseq 212:333) or (chain G and resseq 247:368) or (chain H and resseq 247:368) or (chain I and resseq 247:363) or (chain J and resseq 208:334)J208 - 334
29X-RAY DIFFRACTION13chain K or chain LK7 - 20
30X-RAY DIFFRACTION13chain K or chain LL1 - 10
31X-RAY DIFFRACTION14chain M or chain NM7 - 20
32X-RAY DIFFRACTION14chain M or chain NN1 - 10

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