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- PDB-6dps: Crystal Structure of Neisseria meningitidis DsbD n-terminal domai... -

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Basic information

Entry
Database: PDB / ID: 6dps
TitleCrystal Structure of Neisseria meningitidis DsbD n-terminal domain in the oxidised form
ComponentsThiol:disulfide interchange protein DsbD
KeywordsOXIDOREDUCTASE / disulphide reductase / Dsb proteins
Function / homology
Function and homology information


protein-disulfide reductase / protein-disulfide reductase [NAD(P)H] activity / cytochrome complex assembly / cell redox homeostasis / electron transfer activity / metal ion binding / plasma membrane
Similarity search - Function
Thiol:disulfide interchange protein DsbD, N-terminal domain / Thiol:disulphide interchange protein DsbD / Thiol:disulfide interchange protein DsbD, N-terminal domain superfamily / DsbD gamma / Thiol:disulfide interchange protein DsbD, N-terminal domain / Thiol:disulfide interchange protein DsbD, N-terminal / Cytochrome C biogenesis protein, transmembrane domain / Cytochrome C biogenesis protein transmembrane domain / Thioredoxin-like domain / Thioredoxin-like fold ...Thiol:disulfide interchange protein DsbD, N-terminal domain / Thiol:disulphide interchange protein DsbD / Thiol:disulfide interchange protein DsbD, N-terminal domain superfamily / DsbD gamma / Thiol:disulfide interchange protein DsbD, N-terminal domain / Thiol:disulfide interchange protein DsbD, N-terminal / Cytochrome C biogenesis protein, transmembrane domain / Cytochrome C biogenesis protein transmembrane domain / Thioredoxin-like domain / Thioredoxin-like fold / Thioredoxin domain profile. / Thioredoxin domain / Thioredoxin-like superfamily / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Thiol:disulfide interchange protein DsbD
Similarity search - Component
Biological speciesNeisseria meningitidis (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.556 Å
AuthorsHeras, B. / Smith, R.P. / Paxman, J.J.
Citation
Journal: J. Biol. Chem. / Year: 2018
Title: Structural and biochemical insights into the disulfide reductase mechanism of DsbD, an essential enzyme for neisserial pathogens.
Authors: Smith, R.P. / Mohanty, B. / Mowlaboccus, S. / Paxman, J.J. / Williams, M.L. / Headey, S.J. / Wang, G. / Subedi, P. / Doak, B.C. / Kahler, C.M. / Scanlon, M.J. / Heras, B.
#1: Journal: Acta Crystallogr F Struct Biol Commun / Year: 2018
Title: Production, biophysical characterization and initial crystallization studies of the N- and C-terminal domains of DsbD, an essential enzyme in Neisseria meningitidis.
Authors: Smith, R.P. / Whitten, A.E. / Paxman, J.J. / Kahler, C.M. / Scanlon, M.J. / Heras, B.
History
DepositionJun 9, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 12, 2018Provider: repository / Type: Initial release
Revision 1.1Sep 19, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.2Nov 7, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Nov 20, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn
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_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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.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_label_seq_id / _struct_conn.ptnr2_symmetry

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Thiol:disulfide interchange protein DsbD
B: Thiol:disulfide interchange protein DsbD
C: Thiol:disulfide interchange protein DsbD
D: Thiol:disulfide interchange protein DsbD
E: Thiol:disulfide interchange protein DsbD
F: Thiol:disulfide interchange protein DsbD
hetero molecules


Theoretical massNumber of molelcules
Total (without water)85,64038
Polymers83,5466
Non-polymers2,09332
Water3,351186
1
A: Thiol:disulfide interchange protein DsbD
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,1214
Polymers13,9241
Non-polymers1963
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Thiol:disulfide interchange protein DsbD
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,4489
Polymers13,9241
Non-polymers5238
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Thiol:disulfide interchange protein DsbD
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,3177
Polymers13,9241
Non-polymers3926
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Thiol:disulfide interchange protein DsbD
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,3828
Polymers13,9241
Non-polymers4587
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Thiol:disulfide interchange protein DsbD
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,0553
Polymers13,9241
Non-polymers1312
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Thiol:disulfide interchange protein DsbD
hetero molecules


Theoretical massNumber of molelcules
Total (without water)14,3177
Polymers13,9241
Non-polymers3926
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
7
A: Thiol:disulfide interchange protein DsbD
B: Thiol:disulfide interchange protein DsbD
C: Thiol:disulfide interchange protein DsbD
D: Thiol:disulfide interchange protein DsbD
E: Thiol:disulfide interchange protein DsbD
F: Thiol:disulfide interchange protein DsbD
hetero molecules

A: Thiol:disulfide interchange protein DsbD
B: Thiol:disulfide interchange protein DsbD
C: Thiol:disulfide interchange protein DsbD
D: Thiol:disulfide interchange protein DsbD
E: Thiol:disulfide interchange protein DsbD
F: Thiol:disulfide interchange protein DsbD
hetero molecules

A: Thiol:disulfide interchange protein DsbD
B: Thiol:disulfide interchange protein DsbD
C: Thiol:disulfide interchange protein DsbD
D: Thiol:disulfide interchange protein DsbD
E: Thiol:disulfide interchange protein DsbD
F: Thiol:disulfide interchange protein DsbD
hetero molecules


Theoretical massNumber of molelcules
Total (without water)256,919114
Polymers250,63918
Non-polymers6,27996
Water32418
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation7_665-z+3/2,-x+1,y+1/21
crystal symmetry operation10_646-y+1,z-1/2,-x+3/21
Buried area42930 Å2
ΔGint-3117 kcal/mol
Surface area94530 Å2
MethodPISA
Unit cell
Length a, b, c (Å)147.643, 147.643, 147.643
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number198
Space group name H-MP213
Components on special symmetry positions
IDModelComponents
11C-206-

ZN

21D-206-

ZN

31F-205-

ZN

41F-206-

ZN

51C-318-

HOH

61E-315-

HOH

71F-317-

HOH

81F-318-

HOH

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Components

#1: Protein
Thiol:disulfide interchange protein DsbD / Protein-disulfide reductase / Disulfide reductase


Mass: 13924.407 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Neisseria meningitidis (strain alpha14) (bacteria)
Strain: alpha14 / Gene: dsbD, NMO_1340 / Plasmid: pMCSG7
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: C6S7X6, protein-disulfide reductase
#2: Chemical...
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 32 / Source method: obtained synthetically / Formula: Zn
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 186 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.26 Å3/Da / Density % sol: 62.24 %
Crystal growTemperature: 293 K / Method: vapor diffusion / Details: 8-20% w/v PEG 6000, 100 mM MES pH 6.4, 20 mM ZnCl2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 210r / Detector: CCD / Date: May 4, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2.55→50 Å / Num. obs: 34928 / % possible obs: 99.9 % / Redundancy: 13.1 % / Biso Wilson estimate: 57.94 Å2 / Rmerge(I) obs: 0.136 / Χ2: 1.147 / Net I/σ(I): 12.5
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsΧ2Diffraction-ID% possible all
2.55-2.6412.50.86134341.2781100
2.64-2.7512.50.6134611.2791100
2.75-2.8712.60.43834551.241100
2.87-3.0212.70.29734771.2421100
3.02-3.2113.10.21834751.1711100
3.21-3.4613.50.16534671.1431100
3.46-3.8113.80.14134891.0231100
3.81-4.3613.60.13135141.043199.9
4.36-5.4913.30.12235301.093199.5
5.49-5013.10.09336261.002199.3

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Phasing

PhasingMethod: SAD

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Processing

Software
NameVersionClassification
HKL-2000data scaling
SOLVEphasing
PHENIX1.13_2998refinement
PDB_EXTRACT3.24data extraction
HKL-2000data reduction
RefinementMethod to determine structure: SAD / Resolution: 2.556→35.809 Å / SU ML: 0.42 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 27.23
RfactorNum. reflection% reflection
Rfree0.2351 1763 5.05 %
Rwork0.1781 --
obs0.181 34893 99.88 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 273.28 Å2 / Biso mean: 71.5906 Å2 / Biso min: 25.47 Å2
Refinement stepCycle: final / Resolution: 2.556→35.809 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5734 0 32 188 5954
Biso mean--118.89 60.2 -
Num. residues----732
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 13 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2.5558-2.62490.42991160.304725192635
2.6249-2.70210.32671430.261325242667
2.7021-2.78930.35981280.244425432671
2.7893-2.8890.32581360.236825052641
2.889-3.00460.29761400.223325172657
3.0046-3.14130.30711450.212325592704
3.1413-3.30680.30381250.220525402665
3.3068-3.51380.24451500.182825292679
3.5138-3.78480.26521350.164925432678
3.7848-4.16520.20891290.155525482677
4.1652-4.76670.15691340.130125702704
4.7667-6.00090.18981400.140125602700
6.0009-35.81220.21151420.181626732815
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)
10.33370.2996-0.30990.115-0.49020.257-0.15760.4294-0.6226-0.18530.20960.62550.31020.1450.00120.4629-0.02180.03580.31840.01450.42315.2619143.8568187.7265
20.81310.1305-1.34890.4030.14382.54940.4817-0.1869-0.29390.48050.19230.9605-0.3210.10810.84690.46810.06930.15390.23530.18220.6107-3.7513153.2439186.4293
30.34710.0478-0.21160.68770.44930.495-0.0448-0.0729-0.19790.28560.19890.2916-0.42270.016600.38410.0355-0.01550.37890.00090.37888.0926153.254183.7543
40.4143-0.8230.56860.699-0.65820.3915-0.09420.0817-0.19480.12370.42230.0119-0.35670.0676-0.00110.5680.0745-0.00170.3547-0.05810.40474.9581160.4505183.1601
50.13720.1837-0.0670.13120.04240.2630.39770.35270.0054-0.1685-0.1066-0.5151-0.41390.2294-0.00020.62810.0270.13480.41990.00940.449218.3876159.2067186.6904
60.5865-0.693-0.1560.63110.31150.03120.4006-0.0043-0.74970.00320.15410.63770.18720.00390.00120.41990.0103-0.06110.32880.05760.554-3.6244156.2993181.8476
70.8358-0.4917-0.59260.45310.09330.6164-0.12090.3330.06980.2746-0.10430.0863-0.12640.4107-0.00030.4049-0.0099-0.02880.3295-0.00140.42279.7087149.096182.128
80.50110.154-0.08660.06170.13551.1070.35120.3169-1.2479-0.08550.05320.37430.336-0.3383-0.00010.39160.0089-0.05950.41310.14420.7592-4.4278145.1018178.9524
90.47180.36320.4572-0.0317-0.01640.57310.1352-0.9080.54680.256-0.19420.0793-0.18180.31820.00030.3552-0.047-0.00910.50560.01720.314835.6328142.6946187.9038
101.4359-0.05040.4198-0.01140.45020.7681-0.03620.0693-0.0944-0.0484-0.08490.0274-0.03740.293-0.00280.3704-0.02950.00260.3620.07140.294938.2312146.0351178.7737
110.7253-0.3521-0.28130.16480.1637-0.0258-0.11660.15760.1543-0.2475-0.02880.6095-0.04210.5296-0.010.5263-0.13030.01340.49340.0910.453142.954152.1504171.9379
120.2114-0.17630.30220.0724-0.23650.3518-0.27280.11390.262-0.23670.1337-0.3489-0.275-0.2120.00040.5143-0.0218-0.03430.4801-0.03050.388123.5372143.5023171.4214
130.681-0.09570.22530.4057-0.03610.33260.11510.0647-0.5556-0.6176-0.1953-0.17740.14210.429-0.00630.6089-0.09680.02770.4150.04290.210739.019142.1399175.2751
140.0210.0042-0.07090.44630.61051.5294-0.15580.1404-0.8965-1.10361.3347-1.1181-0.50421.10780.26530.9867-0.47080.19691.0131-0.13580.666854.7908158.2827177.3261
150.50180.18560.3770.8135-0.61930.9708-0.09330.66410.12630.03590.19780.2371-0.23870.21510.0060.5121-0.0435-0.06070.4173-0.00460.32937.2343151.6783182.3089
160.5567-0.1066-0.54520.5136-0.46370.75850.1389-0.2905-0.11250.2059-0.1545-0.0094-0.0380.2219-00.4044-0.0651-0.01930.45460.04390.261438.8495148.8433186.3098
170.18890.71150.02570.42930.27640.2424-0.30040.0537-0.56840.0974-0.0391-0.46810.2090.2181-0.00310.4810.07150.02560.48260.01970.405323.7613149.8371205.8499
180.5987-0.53520.28780.4575-0.22790.592-0.18410.32720.0718-0.2348-0.0705-0.1035-0.1481-0.0519-0.00060.5794-0.09690.04660.43480.0370.460123.4041158.8313202.2467
191.2652-0.3959-0.54070.95220.30051.26180.0822-0.05410.73040.03790.15210.2921-0.4559-0.12730.01040.4307-0.02450.0150.3122-0.05160.543322.536164.9278205.6532
200.52030.4743-0.35040.4263-0.2870.2272-0.3614-0.5306-0.40470.60190.0437-1.3774-0.67752.23380.04480.5875-0.44160.11230.84980.47821.763344.0915166.6994197.6779
210.72550.51670.34281.404-0.1621.11920.4711-0.75650.30080.6736-0.2481-0.1946-0.45420.6049-0.03710.4571-0.0023-0.030.56740.03640.585130.0897158.6504208.3152
220.1979-0.0748-0.69630.8596-0.12730.52880.2327-0.39140.1573-0.0197-0.2032-0.1256-0.30040.4997-0.00020.5176-0.00460.00610.55710.00510.394430.5745153.9011205.9978
230.96090.76760.021.05940.74840.72370.08430.0854-0.05160.55-0.04690.49880.30330.14540.00070.52140.08010.08160.32120.07120.487517.1708125.1895180.179
240.1991-0.1657-0.25170.13270.22040.36080.3378-0.38680.40830.39360.09990.4012-0.27930.07530.02610.46780.06580.08260.30960.12360.414712.5745135.8835170.3991
250.3987-0.13630.29551.22210.01540.8265-0.22870.4808-0.0590.0770.08370.2484-0.08520.66290.00780.50720.0157-0.02950.36650.01440.422117.4427124.2246169.4726
260.6455-0.0102-0.02550.14240.13640.57370.14811.05850.13080.0267-0.08860.05010.0137-0.0605-0.00030.6043-0.0169-0.06110.51560.00620.406311.4121130.9097160.6729
270.4438-0.0404-0.10930.04130.03830.0678-0.02340.5725-1.79840.83440.2754-0.16980.166-0.4815-0.00250.8026-0.0005-0.05680.75580.06830.932929.7761118.4986166.9181
280.33250.0807-0.16280.79620.19890.8297-0.43890.51570.61240.03180.5049-0.68940.00250.17180.01850.3689-0.05190.00090.39980.10450.329321.864129.6062167.0475
29-0.00840.0260.01080.2410.07690.01280.06771.1265-0.0163-0.36980.11971.0901-0.4712-0.23620.00970.54230.14040.01210.92830.07770.6177-1.8361135.8703161.5529
300.59320.47650.68441.18510.0041.1665-0.34570.02060.05890.19950.21410.5137-0.02810.127-0.00030.5158-0.01610.01520.33870.06740.615510.1783125.5964173.7901
310.6053-0.2965-0.5611.8808-0.09420.06330.24830.2467-0.0505-0.5688-0.1061-0.0974-0.0356-0.13230.00220.57110.11770.03560.5466-0.06760.37146.6042119.1967169.0723
320.1230.0568-0.08210.0364-0.02530.0699-0.06570.1485-0.46330.14690.5862-0.7-0.28090.2347-0.00260.7980.15140.04570.6710.0090.641650.4965136.6087178.9004
332.41231.70931.53951.72871.62312.008-0.51240.74570.5599-2.235-0.2931-0.0657-0.4407-0.6171-0.62420.95260.05880.25290.64230.07920.341346.2881125.8375167.194
340.177-0.0078-0.0420.1815-0.02080.05211.09030.82150.7363-0.023-0.6683-0.14250.02760.0244-0.00021.71720.26230.3591.2983-0.51381.447156.7812106.6424156.9387
350.12160.0407-0.49850.1229-0.34890.680.1664-0.6442-0.0134-0.7730.1843-0.15950.14580.38130.01680.66980.141-0.02410.47420.00570.454147.0185119.5345176.7846
360.37440.3346-0.32370.2429-0.24420.26310.03030.2623-1.580.0590.6823-0.07340.47421.05020.09041.04420.238-0.0660.7341-0.41271.397647.8379108.788170.9601
370.06340.07190.05280.04820.04730.07710.6410.1599-0.6673-1.1561-1.12221.0149-0.0194-0.5757-0.00161.7843-0.07540.01760.8201-0.17941.058242.2056107.3958163.5096
380.3579-0.06460.41980.25550.06330.3804-0.1271-0.7329-0.01130.35450.26770.26550.0814-0.22230.00550.58880.05810.16840.6426-0.03950.44531.102155.6478213.9416
390.8424-0.0390.28270.30860.56050.574-0.73870.46860.35890.3210.15120.4050.04871.0295-0.20640.66270.0188-0.05270.23060.00970.5857-1.1222163.154210.9334
400.55770.1078-0.30390.0275-0.00950.09850.9370.66570.1987-0.1011-0.46780.7014-0.1438-0.82750.0070.72110.09430.08150.6209-0.20690.8529-11.8999160.2852209.6931
41-0.01970.01450.00930.05460.06080.08930.6384-0.19940.6966-0.96240.4286-0.07830.4519-0.10110.04491.53771.13880.42221.868-0.06321.4948-17.894167.7968219.2919
421.673-0.1689-0.19040.6788-0.02861.3186-0.09730.28470.19090.01610.6034-0.3508-1.0485-0.66520.18380.87020.32890.07610.41720.03730.7163-6.2457161.6145201.525
430.43080.1546-0.13630.1639-0.17350.11920.02911.4899-0.0132-0.7126-0.7677-0.1324-0.1805-0.67140.14621.640.39780.31080.681-0.19160.9215-14.8026173.779224.8018
440.3721-0.65390.27271.7669-0.68670.24410.0585-0.3453-0.02080.08910.422-0.3313-0.67070.07850.04870.51030.10490.18110.4218-0.08340.416-5.7672158.1601216.3006
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 3 through 17 )A3 - 17
2X-RAY DIFFRACTION2chain 'A' and (resid 18 through 28 )A18 - 28
3X-RAY DIFFRACTION3chain 'A' and (resid 29 through 44 )A29 - 44
4X-RAY DIFFRACTION4chain 'A' and (resid 45 through 62 )A45 - 62
5X-RAY DIFFRACTION5chain 'A' and (resid 63 through 70 )A63 - 70
6X-RAY DIFFRACTION6chain 'A' and (resid 71 through 88 )A71 - 88
7X-RAY DIFFRACTION7chain 'A' and (resid 89 through 107 )A89 - 107
8X-RAY DIFFRACTION8chain 'A' and (resid 108 through 124 )A108 - 124
9X-RAY DIFFRACTION9chain 'B' and (resid 3 through 17 )B3 - 17
10X-RAY DIFFRACTION10chain 'B' and (resid 18 through 44 )B18 - 44
11X-RAY DIFFRACTION11chain 'B' and (resid 45 through 57 )B45 - 57
12X-RAY DIFFRACTION12chain 'B' and (resid 58 through 70 )B58 - 70
13X-RAY DIFFRACTION13chain 'B' and (resid 71 through 80 )B71 - 80
14X-RAY DIFFRACTION14chain 'B' and (resid 81 through 88 )B81 - 88
15X-RAY DIFFRACTION15chain 'B' and (resid 89 through 99 )B89 - 99
16X-RAY DIFFRACTION16chain 'B' and (resid 100 through 124 )B100 - 124
17X-RAY DIFFRACTION17chain 'C' and (resid 2 through 17 )C2 - 17
18X-RAY DIFFRACTION18chain 'C' and (resid 18 through 38 )C18 - 38
19X-RAY DIFFRACTION19chain 'C' and (resid 39 through 80 )C39 - 80
20X-RAY DIFFRACTION20chain 'C' and (resid 81 through 88 )C81 - 88
21X-RAY DIFFRACTION21chain 'C' and (resid 89 through 99 )C89 - 99
22X-RAY DIFFRACTION22chain 'C' and (resid 100 through 124 )C100 - 124
23X-RAY DIFFRACTION23chain 'D' and (resid 1 through 17 )D1 - 17
24X-RAY DIFFRACTION24chain 'D' and (resid 18 through 28 )D18 - 28
25X-RAY DIFFRACTION25chain 'D' and (resid 29 through 44 )D29 - 44
26X-RAY DIFFRACTION26chain 'D' and (resid 45 through 57 )D45 - 57
27X-RAY DIFFRACTION27chain 'D' and (resid 58 through 66 )D58 - 66
28X-RAY DIFFRACTION28chain 'D' and (resid 67 through 80 )D67 - 80
29X-RAY DIFFRACTION29chain 'D' and (resid 81 through 88 )D81 - 88
30X-RAY DIFFRACTION30chain 'D' and (resid 89 through 124 )D89 - 124
31X-RAY DIFFRACTION31chain 'E' and (resid 3 through 57 )E3 - 57
32X-RAY DIFFRACTION32chain 'E' and (resid 58 through 67 )E58 - 67
33X-RAY DIFFRACTION33chain 'E' and (resid 68 through 80 )E68 - 80
34X-RAY DIFFRACTION34chain 'E' and (resid 81 through 88 )E81 - 88
35X-RAY DIFFRACTION35chain 'E' and (resid 89 through 107 )E89 - 107
36X-RAY DIFFRACTION36chain 'E' and (resid 108 through 114 )E108 - 114
37X-RAY DIFFRACTION37chain 'E' and (resid 115 through 123 )E115 - 123
38X-RAY DIFFRACTION38chain 'F' and (resid 3 through 17 )F3 - 17
39X-RAY DIFFRACTION39chain 'F' and (resid 18 through 34 )F18 - 34
40X-RAY DIFFRACTION40chain 'F' and (resid 35 through 43 )F35 - 43
41X-RAY DIFFRACTION41chain 'F' and (resid 44 through 51 )F44 - 51
42X-RAY DIFFRACTION42chain 'F' and (resid 52 through 80 )F52 - 80
43X-RAY DIFFRACTION43chain 'F' and (resid 81 through 88 )F81 - 88
44X-RAY DIFFRACTION44chain 'F' and (resid 89 through 122 )F89 - 122

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