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- PDB-7kc9: Ricin bound to VHH antibody V5G1 -

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Basic information

Entry
Database: PDB / ID: 7kc9
TitleRicin bound to VHH antibody V5G1
Components
  • Ricin chain A
  • Ricin chain B
  • VHH antibody V5G1
KeywordsTOXIN / Glycosidase / VHH antibody
Function / homology
Function and homology information


rRNA N-glycosylase / rRNA N-glycosylase activity / AMP binding / defense response / toxin activity / carbohydrate binding / killing of cells of another organism / negative regulation of translation
Similarity search - Function
Ricin-type beta-trefoil lectin domain / Ribosome-inactivating protein conserved site / Shiga/ricin ribosomal inactivating toxins active site signature. / Ribosome-inactivating protein type 1/2 / Ribosome-inactivating protein / Ribosome-inactivating protein, subdomain 1 / Ribosome-inactivating protein, subdomain 2 / Ribosome-inactivating protein superfamily / Ribosome inactivating protein / Ricin-type beta-trefoil ...Ricin-type beta-trefoil lectin domain / Ribosome-inactivating protein conserved site / Shiga/ricin ribosomal inactivating toxins active site signature. / Ribosome-inactivating protein type 1/2 / Ribosome-inactivating protein / Ribosome-inactivating protein, subdomain 1 / Ribosome-inactivating protein, subdomain 2 / Ribosome-inactivating protein superfamily / Ribosome inactivating protein / Ricin-type beta-trefoil / Lectin domain of ricin B chain profile. / Ricin B, lectin domain / Ricin B-like lectins
Similarity search - Domain/homology
Biological speciesVicugna pacos (alpaca)
Ricinus communis (castor bean)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.301 Å
AuthorsRudolph, M.J.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)HHSN272201400021C United States
CitationJournal: J.Mol.Biol. / Year: 2021
Title: Structural Analysis of Toxin-Neutralizing, Single-Domain Antibodies that Bridge Ricin's A-B Subunit Interface.
Authors: Rudolph, M.J. / Poon, A.Y. / Kavaliauskiene, S. / Myrann, A.G. / Reynolds-Peterson, C. / Davis, S.A. / Sandvig, K. / Vance, D.J. / Mantis, N.J.
History
DepositionOct 5, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 4, 2021Provider: repository / Type: Initial release
Revision 1.1Oct 18, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ricin chain A
B: Ricin chain B
C: VHH antibody V5G1
D: Ricin chain A
E: Ricin chain B
F: VHH antibody V5G1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)149,06924
Polymers145,6176
Non-polymers3,45218
Water10,917606
1
A: Ricin chain A
B: Ricin chain B
C: VHH antibody V5G1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,48411
Polymers72,8093
Non-polymers1,6758
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7550 Å2
ΔGint-119 kcal/mol
Surface area24890 Å2
MethodPISA
2
D: Ricin chain A
E: Ricin chain B
F: VHH antibody V5G1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)74,58513
Polymers72,8093
Non-polymers1,77610
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7790 Å2
ΔGint-99 kcal/mol
Surface area25090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)44.345, 77.438, 101.577
Angle α, β, γ (deg.)89.970, 90.180, 89.980
Int Tables number1
Space group name H-MP1
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 5 through 205 or resid 207 through 261))
21(chain D and (resid 5 through 205 or resid 207 through 261))
12(chain B and (resid 3 through 19 or resid 21 through 262))
22(chain E and (resid 3 through 19 or resid 21 through 262))
13(chain C and (resid 3 through 20 or resid 22 through 25 or resid 30 through 120))
23(chain F and (resid 3 through 9 or resid 11 through 20 or resid 22 through 120))

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111GLNGLNILEILE(chain A and (resid 5 through 205 or resid 207 through 261))AA5 - 2055 - 205
121LEULEUPROPRO(chain A and (resid 5 through 205 or resid 207 through 261))AA207 - 261207 - 261
211GLNGLNILEILE(chain D and (resid 5 through 205 or resid 207 through 261))DD5 - 2055 - 205
221LEULEUPROPRO(chain D and (resid 5 through 205 or resid 207 through 261))DD207 - 261207 - 261
112VALVALLEULEU(chain B and (resid 3 through 19 or resid 21 through 262))BB3 - 193 - 19
122VALVALPHEPHE(chain B and (resid 3 through 19 or resid 21 through 262))BB21 - 26221 - 262
212VALVALLEULEU(chain E and (resid 3 through 19 or resid 21 through 262))EE3 - 193 - 19
222VALVALPHEPHE(chain E and (resid 3 through 19 or resid 21 through 262))EE21 - 26221 - 262
113GLNGLNLEULEU(chain C and (resid 3 through 20 or resid 22 through 25 or resid 30 through 120))CC3 - 203 - 20
123CYSCYSSERSER(chain C and (resid 3 through 20 or resid 22 through 25 or resid 30 through 120))CC22 - 2522 - 25
133SERSERVALVAL(chain C and (resid 3 through 20 or resid 22 through 25 or resid 30 through 120))CC30 - 12030 - 120
213GLNGLNGLYGLY(chain F and (resid 3 through 9 or resid 11 through 20 or resid 22 through 120))FF3 - 93 - 9
223LEULEULEULEU(chain F and (resid 3 through 9 or resid 11 through 20 or resid 22 through 120))FF11 - 2011 - 20
233CYSCYSVALVAL(chain F and (resid 3 through 9 or resid 11 through 20 or resid 22 through 120))FF22 - 12022 - 120

NCS ensembles :
ID
1
2
3

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Components

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Protein , 2 types, 4 molecules ADBE

#1: Protein Ricin chain A


Mass: 29936.758 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Catalytic subunit, glycosidase / Source: (natural) Ricinus communis (castor bean) / References: UniProt: P02879, rRNA N-glycosylase
#2: Protein Ricin chain B


Mass: 28989.580 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Lectin / Source: (natural) Ricinus communis (castor bean) / References: UniProt: P02879, rRNA N-glycosylase

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Antibody , 1 types, 2 molecules CF

#3: Antibody VHH antibody V5G1


Mass: 13882.364 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: VHH antibody / Source: (gene. exp.) Vicugna pacos (alpaca) / Production host: Escherichia coli (E. coli)

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Sugars , 3 types, 6 molecules

#4: Polysaccharide alpha-L-fucopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-3DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a3-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(3+1)][a-L-Fucp]{}}LINUCSPDB-CARE
#5: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#6: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}LINUCSPDB-CARE

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Non-polymers , 3 types, 618 molecules

#7: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: Zn
#8: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 606 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 2.4 Å3/Da / Density % sol: 48.65 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 7.5 / Details: 200 mM zinc acetate, 20% PEG 3,350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.54 Å
DetectorType: RIGAKU SATURN 944 / Detector: CCD / Date: Jan 12, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.3→50 Å / Num. obs: 57480 / % possible obs: 96 % / Redundancy: 2 % / Biso Wilson estimate: 27.4 Å2 / Rmerge(I) obs: 0.068 / Rpim(I) all: 0.068 / Rrim(I) all: 0.096 / Χ2: 0.886 / Net I/σ(I): 6.8 / Num. measured all: 112499
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
2.3-2.341.90.31127880.820.3110.440.92592.6
2.34-2.381.90.27427410.8660.2740.3870.90293.6
2.38-2.431.90.2828470.8690.280.3960.85794.4
2.43-2.481.90.26528800.8710.2650.3740.89694.7
2.48-2.5320.24627820.90.2460.3480.89394.5
2.53-2.5920.22128980.9120.2210.3130.90695.3
2.59-2.6620.2128190.9150.210.2970.89995.1
2.66-2.7320.18428740.9370.1840.260.88395.5
2.73-2.8120.16928760.9420.1690.2390.91595.8
2.81-2.920.1528400.9540.150.2120.90196
2.9-320.12829220.9680.1280.1810.86796.4
3-3.1220.10428950.9780.1040.1470.93396.5
3.12-3.2620.07728580.9830.0770.1080.87796.7
3.26-3.4420.05929270.9880.0590.0840.84697
3.44-3.6520.04829390.9910.0480.0670.89497.4
3.65-3.9320.0428980.9950.040.0560.87497.7
3.93-4.3320.03429450.9960.0340.0480.80998
4.33-4.9520.03129610.9960.0310.0440.81198.2
4.95-6.2420.03529390.9960.0350.0490.86798.7
6.24-501.90.02728510.9970.0270.0390.97895.4

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Processing

Software
NameVersionClassification
PHENIX1.11.1_2575refinement
SCALEPACKdata scaling
PDB_EXTRACT3.25data extraction
CrystalCleardata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2AAI

2aai


Resolution: 2.301→19.653 Å / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 1.97 / Phase error: 25.38 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2377 2742 4.77 %
Rwork0.187 54721 -
obs0.1894 57463 95.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 147.07 Å2 / Biso mean: 40.9173 Å2 / Biso min: 12.51 Å2
Refinement stepCycle: final / Resolution: 2.301→19.653 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9737 0 194 606 10537
Biso mean--58.05 38.13 -
Num. residues----1252
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00510165
X-RAY DIFFRACTIONf_angle_d0.86413849
X-RAY DIFFRACTIONf_chiral_restr0.0651582
X-RAY DIFFRACTIONf_plane_restr0.0051777
X-RAY DIFFRACTIONf_dihedral_angle_d5.3477093
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A2440X-RAY DIFFRACTION8.294TORSIONAL
12D2440X-RAY DIFFRACTION8.294TORSIONAL
21B2432X-RAY DIFFRACTION8.294TORSIONAL
22E2432X-RAY DIFFRACTION8.294TORSIONAL
31C906X-RAY DIFFRACTION8.294TORSIONAL
32F906X-RAY DIFFRACTION8.294TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.301-2.34050.30081260.2316255790
2.3405-2.3830.30641110.2301264493
2.383-2.42870.28221090.2321273094
2.4287-2.47820.26541330.219275595
2.4782-2.5320.25771520.2175263294
2.532-2.59080.30351670.2093271695
2.5908-2.65540.30121440.218270095
2.6554-2.7270.27141650.2206267695
2.727-2.80710.28271350.205275996
2.8071-2.89740.26991700.2158269896
2.8974-3.00060.34481470.2193274596
3.0006-3.12030.29631390.2122274396
3.1203-3.26170.23811180.1896276797
3.2617-3.43280.23781440.178277397
3.4328-3.64660.18721320.1647280898
3.6466-3.92610.2019920.1617279397
3.9261-4.31740.20661240.1537281098
4.3174-4.93350.18251300.1523283098
4.9335-6.18340.23951490.1772280899
6.1834-19.6530.18471550.1847277798
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)
10.49981.50450.61447.23950.97542.3908-0.01120.0796-0.028-0.16510.03-0.5096-0.15190.3116-0.00870.1148-0.01130.01880.2289-0.00430.1836-40.01216.1019-73.3568
24.60510.92091.82915.1824-2.69483.317-0.03360.2378-0.0077-0.17120.02680.20410.05090.071-0.00890.1929-0.00510.00750.1708-0.02070.1136-51.78983.0828-81.0193
36.35260.7954-0.68473.3105-2.98434.9288-0.06550.6470.2724-0.40950.12240.3365-0.3239-0.0527-0.01870.38340.0126-0.09470.22470.00840.2058-55.996110.6338-85.8396
45.7017-1.7296-1.37635.83943.46058.44440.0269-0.0436-0.0658-0.3385-0.13170.60670.0117-0.52410.06680.1575-0.0744-0.01110.13340.02230.2343-60.8383-3.5543-73.5084
52.71071.51871.93192.39361.37663.4087-0.021-0.34420.0970.1654-0.11670.16490.0108-0.13020.13050.18320.01840.02930.1607-0.00990.1547-49.19725.46-60.1585
62.38930.5232-0.56383.85881.00641.5578-0.0095-0.06150.1794-0.1493-0.21750.4615-0.2169-0.33470.15740.23050.0161-0.03270.211-0.07130.2046-39.317420.7501-40.1214
74.51690.5962-0.66536.8892-0.80843.61960.0308-0.65290.56781.0583-0.32670.61910.0533-0.34690.27210.35720.01020.05540.3171-0.13090.2584-39.660223.1994-29.667
84.38130.99751.94185.00250.8433.3842-0.2269-0.16320.45290.2625-0.0133-0.0329-0.5232-0.14730.23910.28190.0034-0.02170.1827-0.06180.204-31.615929.5677-38.2536
92.88320.90970.52487.07795.65996.62960.0273-0.04880.1805-1.0479-0.0356-0.1083-0.7569-0.0044-0.00380.2920.0098-0.02660.15710.03210.2049-27.458523.7329-46.0036
101.35661.66940.90774.79282.11051.35390.1812-0.2488-0.11320.5529-0.0997-0.11010.1379-0.0691-0.06980.27340.017-0.03090.20530.01560.1425-32.386311.8069-39.387
116.2351-0.35985.12936.77222.46187.57830.4902-0.3456-0.52290.675-0.1405-0.45071.5469-0.0657-0.33190.3386-0.0004-0.04330.20720.0640.2796-35.9499-12.7329-47.2372
122.7550.45091.73248.65014.32778.06220.2904-0.6342-0.1690.9626-0.6420.66220.5256-0.67660.32870.2235-0.03120.03320.30190.0030.2075-40.0037-3.9694-40.6723
139.9539-1.3732-4.55666.18455.29916.01140.101-0.00250.05560.49430.487-1.20070.17770.5458-0.56350.42020.0267-0.11850.3030.06490.4373-23.0161-4.5501-44.4382
140.84171.0060.27195.37540.68444.96360.1098-0.1825-0.18960.46710.1061-0.22540.14590.0327-0.21680.12550.0296-0.02260.24340.00660.2105-29.63591.4814-45.0129
152.03991.66861.1518.80551.8944.6198-0.23540.2291-0.3403-0.22020.2549-0.49930.16080.1066-0.04620.19-0.0130.03070.1870.0130.195-29.178-5.9983-53.41
164.0073-1.41674.35437.7085-1.80718.52140.770.9145-2.1679-0.8572-0.3378-1.00660.78050.6198-0.43110.61910.02920.2310.5671-0.11571.4393-16.14-29.8456-65.7653
176.3603-0.57193.32327.2162-3.69189.4883-0.09670.9586-1.1782-1.0929-0.453-0.39481.63571.14040.4710.54490.09010.1510.5843-0.06280.6705-26.9632-22.0926-63.1002
189.1082-3.1210.83358.4926-1.50737.8064-0.28660.1964-0.8865-0.1394-0.1257-0.50920.4238-0.01830.35980.4243-0.04680.18040.3392-0.00890.5983-20.1943-18.3173-60.8733
198.1871-3.2684-2.04426.5488-0.72323.3052-0.34710.2903-2.07-0.1461-0.2853-0.75230.67740.30790.65990.6185-0.01930.15540.4598-0.00170.9748-22.2386-24.9206-59.2461
209.4264-8.2745-0.55872.01620.05232.7175-0.98820.5915-2.13670.0953-0.2454-0.50710.21430.21351.26830.7472-0.08050.25280.47280.07671.4884-24.1633-31.0058-60.0395
213.7917-0.04350.14486.0063.48112.8496-0.01870.05970.06110.03670.01390.70850.0396-0.31520.07940.19310.0074-0.01340.23030.04880.173-55.2127-40.983811.6027
222.4158-2.70781.89585.8931-1.36743.2113-0.1664-0.1498-0.030.49330.13820.1796-0.3184-0.19430.0170.1809-0.00720.02630.1903-0.01550.1532-52.6237-30.627312.6776
239.0066-4.62426.31917.7330.13126.5729-0.0085-0.06350.17970.05320.1827-0.37260.10890.0898-0.28150.2495-0.01690.05570.14030.00050.1632-41.1656-31.036417.8472
249.0703-1.016-3.29942.83614.02356.4263-0.0397-0.53910.10590.3834-0.0197-0.4097-0.32140.2008-0.06030.3993-0.0474-0.08130.2192-0.01230.2001-39.8455-28.050222.7325
257.2482-0.2990.13033.3071-3.58958.5448-0.1124-0.04270.1987-0.2056-0.0679-0.8283-0.360.68910.20710.11730.00750.03550.2437-0.00010.311-32.94-38.13383.5869
266.00930.56971.17095.7669-3.23168.327-0.0935-0.362-0.28050.7324-0.108-0.5098-0.08260.34250.09060.28040.0278-0.06080.14060.02170.2469-37.1592-46.315817.0351
274.79270.03533.36052.4294-0.43045.13080.1080.1912-0.225-0.13980.0653-0.11220.3685-0.0846-0.17050.2062-0.01190.03290.13410.00420.1466-44.645-41.15963.8426
283.1876-2.21792.39055.2886-3.47057.53440.02850.4388-0.3335-0.2845-0.01240.0460.43060.16890.05040.20330.06120.03770.2841-0.00780.2099-41.8174-40.4708-3.1025
295.982-1.75760.16355.05010.12815.3082-0.03980.51170.2806-0.3171-0.2453-0.31-0.46610.38030.29370.2516-0.0512-0.01710.2220.08940.2274-48.1308-25.7139-10.4158
303.24871.7958-0.00156.63576.43177.31440.11080.2886-0.0015-0.1172-0.27710.0836-0.1067-0.54190.10410.33830.0141-0.07430.24020.00540.1416-54.3894-23.5016-0.7591
312.8045-0.5025-0.64952.8144-1.68691.5347-0.061-0.02260.24060.2109-0.1142-0.4161-0.41090.270.1560.3574-0.0049-0.03650.22750.0710.2027-56.4746-17.8298-22.1912
324.3651-0.9311-0.18695.99390.21393.44680.09340.60190.4275-1.0021-0.491-0.73630.12350.35180.36420.42310.01530.04420.34250.15180.2737-56.1893-15.5736-33.478
332.9912-0.3860.67355.0139-1.26383.3275-0.02140.13510.2724-0.1908-0.06030.1904-0.27530.0670.06940.2098-0.0142-0.02790.15990.02990.1598-66.1139-13.2205-23.5103
340.1782-0.99820.42725.7316-2.43871.03430.11210.1614-0.0373-0.263-0.2117-0.0628-0.04670.18010.10150.2881-0.0147-0.02150.2031-0.01890.1206-61.3981-28.7762-20.9845
352.0033-1.29032.1335.713-2.5326.30220.21630.3849-0.202-0.919-0.3363-0.14380.70930.30510.11020.27610.01570.01840.2517-0.04550.1944-58.1094-45.7052-20.2722
360.4732-1.0270.55525.5839-0.4125.60160.1112-0.0924-0.2758-0.37320.05720.82570.3358-0.7486-0.13030.2206-0.0798-0.04340.3083-0.0230.2964-69.2503-39.2149-17.554
373.6815-1.35271.90158.4134-1.31613.5818-0.1273-0.017-0.56430.14810.22810.44520.1484-0.0607-0.07440.2176-0.0040.02030.1779-0.02840.1946-66.712-44.694-9.7411
383.4571.1149-3.96143.8819-2.56745.01170.1884-0.3213-1.83070.23960.01150.92920.329-0.608-0.20850.49130.01310.20540.48410.07411.369-79.73-68.63452.5829
396.04822.28983.78517.89996.24182.0073-0.6988-0.3873-1.13910.4892-0.35520.29210.9755-0.59631.05890.609-0.17610.22830.73260.08210.7736-69.1399-60.7486-0.5599
406.79713.17572.39174.8008-3.20716.6158-0.28640.4492-0.98350.09860.50520.24810.2463-0.2349-0.16380.432-0.03850.21010.4548-0.04680.6461-73.5262-56.8707-5.6351
417.13823.4144-1.01889.64761.53511.3028-0.306-0.2864-0.14650.215-0.65760.69330.4558-0.2840.95560.46680.0140.14640.4338-0.02970.675-77.871-57.2680.6315
429.85082.9383-0.08787.43491.69684.2797-0.61260.0807-2.0922-0.3819-0.43721.27730.3901-0.2831.02480.6687-0.11430.19890.586-0.0591.2307-79.0238-65.0429-3.2767
438.51846.9876-2.88089.5031-1.7773.6526-0.3659-0.4362-1.16670.0156-0.19860.09450.49760.16340.53370.6210.101-0.01710.3931-0.08380.7773-65.5387-65.6346-4.2841
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 5 through 56 )A5 - 56
2X-RAY DIFFRACTION2chain 'A' and (resid 57 through 97 )A57 - 97
3X-RAY DIFFRACTION3chain 'A' and (resid 98 through 122 )A98 - 122
4X-RAY DIFFRACTION4chain 'A' and (resid 123 through 160 )A123 - 160
5X-RAY DIFFRACTION5chain 'A' and (resid 161 through 261 )A161 - 261
6X-RAY DIFFRACTION6chain 'B' and (resid 3 through 26 )B3 - 26
7X-RAY DIFFRACTION7chain 'B' and (resid 27 through 47 )B27 - 47
8X-RAY DIFFRACTION8chain 'B' and (resid 48 through 84 )B48 - 84
9X-RAY DIFFRACTION9chain 'B' and (resid 85 through 103 )B85 - 103
10X-RAY DIFFRACTION10chain 'B' and (resid 104 through 145 )B104 - 145
11X-RAY DIFFRACTION11chain 'B' and (resid 146 through 162 )B146 - 162
12X-RAY DIFFRACTION12chain 'B' and (resid 163 through 188 )B163 - 188
13X-RAY DIFFRACTION13chain 'B' and (resid 189 through 201 )B189 - 201
14X-RAY DIFFRACTION14chain 'B' and (resid 202 through 223 )B202 - 223
15X-RAY DIFFRACTION15chain 'B' and (resid 224 through 262 )B224 - 262
16X-RAY DIFFRACTION16chain 'C' and (resid 3 through 24 )C3 - 24
17X-RAY DIFFRACTION17chain 'C' and (resid 25 through 38 )C25 - 38
18X-RAY DIFFRACTION18chain 'C' and (resid 44 through 77 )C44 - 77
19X-RAY DIFFRACTION19chain 'C' and (resid 78 through 108 )C78 - 108
20X-RAY DIFFRACTION20chain 'C' and (resid 109 through 120 )C109 - 120
21X-RAY DIFFRACTION21chain 'D' and (resid 5 through 32 )D5 - 32
22X-RAY DIFFRACTION22chain 'D' and (resid 33 through 75 )D33 - 75
23X-RAY DIFFRACTION23chain 'D' and (resid 76 through 97 )D76 - 97
24X-RAY DIFFRACTION24chain 'D' and (resid 98 through 122 )D98 - 122
25X-RAY DIFFRACTION25chain 'D' and (resid 123 through 140 )D123 - 140
26X-RAY DIFFRACTION26chain 'D' and (resid 141 through 160 )D141 - 160
27X-RAY DIFFRACTION27chain 'D' and (resid 161 through 194 )D161 - 194
28X-RAY DIFFRACTION28chain 'D' and (resid 195 through 210 )D195 - 210
29X-RAY DIFFRACTION29chain 'D' and (resid 211 through 247 )D211 - 247
30X-RAY DIFFRACTION30chain 'D' and (resid 248 through 262 )D248 - 262
31X-RAY DIFFRACTION31chain 'E' and (resid 2 through 26 )E2 - 26
32X-RAY DIFFRACTION32chain 'E' and (resid 27 through 47 )E27 - 47
33X-RAY DIFFRACTION33chain 'E' and (resid 48 through 118 )E48 - 118
34X-RAY DIFFRACTION34chain 'E' and (resid 119 through 145 )E119 - 145
35X-RAY DIFFRACTION35chain 'E' and (resid 146 through 192 )E146 - 192
36X-RAY DIFFRACTION36chain 'E' and (resid 193 through 223 )E193 - 223
37X-RAY DIFFRACTION37chain 'E' and (resid 224 through 262 )E224 - 262
38X-RAY DIFFRACTION38chain 'F' and (resid 3 through 24 )F3 - 24
39X-RAY DIFFRACTION39chain 'F' and (resid 25 through 38 )F25 - 38
40X-RAY DIFFRACTION40chain 'F' and (resid 44 through 60 )F44 - 60
41X-RAY DIFFRACTION41chain 'F' and (resid 61 through 77 )F61 - 77
42X-RAY DIFFRACTION42chain 'F' and (resid 78 through 100 )F78 - 100
43X-RAY DIFFRACTION43chain 'F' and (resid 101 through 120 )F101 - 120

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