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- PDB-5vtz: Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza viru... -

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Basic information

Entry
Database: PDB / ID: 5vtz
TitleCrystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin G225Q/L226A mutant apo form
Components(Hemagglutinin ...) x 2
KeywordsVIRAL PROTEIN / Influenza A virus / hemagglutinin / mutant / receptor binding
Function / homology
Function and homology information


viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane
Similarity search - Function
Hemagglutinin Ectodomain; Chain B - #10 / Hemagglutinin Ectodomain; Chain B / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Biological speciesInfluenza A virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.15 Å
AuthorsWu, N.C. / Wilson, I.A.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R56 AI117675 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI114730 United States
CitationJournal: Cell Host Microbe / Year: 2017
Title: Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin.
Authors: Wu, N.C. / Xie, J. / Zheng, T. / Nycholat, C.M. / Grande, G. / Paulson, J.C. / Lerner, R.A. / Wilson, I.A.
History
DepositionMay 18, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 28, 2017Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2017Group: Author supporting evidence / Refinement description / Category: pdbx_audit_support / software / Item: _pdbx_audit_support.funding_organization
Revision 1.2Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 4, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag / _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: Hemagglutinin HA1 chain
B: Hemagglutinin HA2 chain
C: Hemagglutinin HA1 chain
D: Hemagglutinin HA2 chain
E: Hemagglutinin HA1 chain
F: Hemagglutinin HA2 chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)171,56017
Polymers166,7316
Non-polymers4,82811
Water15,763875
1
A: Hemagglutinin HA1 chain
B: Hemagglutinin HA2 chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,3966
Polymers55,5772
Non-polymers1,8194
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7510 Å2
ΔGint-9 kcal/mol
Surface area25220 Å2
MethodPISA
2
C: Hemagglutinin HA1 chain
D: Hemagglutinin HA2 chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,0306
Polymers55,5772
Non-polymers1,4534
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7190 Å2
ΔGint-11 kcal/mol
Surface area23850 Å2
MethodPISA
3
E: Hemagglutinin HA1 chain
F: Hemagglutinin HA2 chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,1345
Polymers55,5772
Non-polymers1,5563
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7510 Å2
ΔGint-9 kcal/mol
Surface area24030 Å2
MethodPISA
4


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area38220 Å2
ΔGint-59 kcal/mol
Surface area57080 Å2
MethodPISA
Unit cell
Length a, b, c (Å)209.735, 131.202, 72.439
Angle α, β, γ (deg.)90.00, 98.35, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12A
22E
13B
23D
14B
24F
15C
25E
16D
26F

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11PROPROPROPROAA9 - 3243 - 318
21PROPROPROPROCC9 - 3243 - 318
12PROPROPROPROAA9 - 3243 - 318
22PROPROPROPROEE9 - 3243 - 318
13GLYGLYARGARGBB1 - 1701 - 170
23GLYGLYARGARGDD1 - 1701 - 170
14GLYGLYARGARGBB1 - 1701 - 170
24GLYGLYARGARGFF1 - 1701 - 170
15PROPROGLUGLUCC9 - 3253 - 319
25PROPROGLUGLUEE9 - 3253 - 319
16GLYGLYPHEPHEDD1 - 1711 - 171
26GLYGLYPHEPHEFF1 - 1711 - 171

NCS ensembles :
ID
1
6
2
3
4
5

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Components

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Hemagglutinin ... , 2 types, 6 molecules ACEBDF

#1: Protein Hemagglutinin HA1 chain


Mass: 35535.945 Da / Num. of mol.: 3 / Mutation: G225Q/L226A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus (strain A/Hong Kong/1/1968 H3N2)
Strain: A/Hong Kong/1/1968 H3N2 / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q91MA7
#2: Protein Hemagglutinin HA2 chain


Mass: 20041.131 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus (strain A/Hong Kong/1/1968 H3N2)
Strain: A/Hong Kong/1/1968 H3N2 / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q91MA7

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Sugars , 4 types, 11 molecules

#3: 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.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam 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
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#4: 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.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam 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
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#6: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 1 types, 875 molecules

#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 875 / Source method: isolated from a natural source / Formula: H2O

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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: 2.96 Å3/Da / Density % sol: 58.41 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1 M sodium cacodylate pH 6.5, 5% PEG 8000, and 38% 2-methyl-2,4-pentanediol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0331 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 15, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0331 Å / Relative weight: 1
ReflectionResolution: 2.15→50 Å / Num. obs: 105027 / % possible obs: 99.6 % / Redundancy: 6.2 % / CC1/2: 1 / Rpim(I) all: 0.03 / Rsym value: 0.08 / Net I/σ(I): 20.1
Reflection shellResolution: 2.15→2.22 Å / Redundancy: 4.8 % / Mean I/σ(I) obs: 1.9 / Num. unique obs: 9304 / CC1/2: 0.82 / Rpim(I) all: 0.27 / Rsym value: 0.57 / % possible all: 97.5

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Processing

Software
NameVersionClassification
REFMAC5.8.0155refinement
HKL-2000712data scaling
PHASER2.5.6phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4FNK

4fnk


Resolution: 2.15→50 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.952 / SU B: 8.935 / SU ML: 0.122 / Cross valid method: THROUGHOUT / ESU R: 0.196 / ESU R Free: 0.155 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19857 5341 5.1 %RANDOM
Rwork0.1757 ---
obs0.17686 99672 99.42 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 52.338 Å2
Baniso -1Baniso -2Baniso -3
1-0.67 Å20 Å2-0.8 Å2
2--0.02 Å2-0 Å2
3----0.44 Å2
Refinement stepCycle: 1 / Resolution: 2.15→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11526 0 318 875 12719
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01912129
X-RAY DIFFRACTIONr_bond_other_d0.0020.0211128
X-RAY DIFFRACTIONr_angle_refined_deg1.3491.96616485
X-RAY DIFFRACTIONr_angle_other_deg0.914325672
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.93851463
X-RAY DIFFRACTIONr_dihedral_angle_2_deg34.87924.784579
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.86151974
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.1281570
X-RAY DIFFRACTIONr_chiral_restr0.080.21855
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213729
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022801
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.692.5915870
X-RAY DIFFRACTIONr_mcbond_other0.6892.595869
X-RAY DIFFRACTIONr_mcangle_it1.1653.8817327
X-RAY DIFFRACTIONr_mcangle_other1.1653.8827328
X-RAY DIFFRACTIONr_scbond_it1.2482.9126258
X-RAY DIFFRACTIONr_scbond_other1.2482.9126259
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.0674.3269159
X-RAY DIFFRACTIONr_long_range_B_refined5.0651.19449676
X-RAY DIFFRACTIONr_long_range_B_other4.90850.70748992
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A202800.05
12C202800.05
21A201260.06
22E201260.06
31B108180.04
32D108180.04
41B107480.05
42F107480.05
51C201560.06
52E201560.06
61D109160.04
62F109160.04
LS refinement shellResolution: 2.147→2.203 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.249 356 -
Rwork0.24 7051 -
obs--95.51 %
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)
10.79160.21620.01973.6924-0.19870.0305-0.0913-0.40870.35470.47880.051-0.41980.0019-0.07740.04030.21870.0324-0.10560.4687-0.18610.2597-16.6287-26.113638.997
22.4924-0.3589-0.65061.37450.54661.4222-0.0450.0237-0.6169-0.0114-0.13450.13820.2967-0.29170.17960.2673-0.09090.03590.3110.08160.1965-31.0725-78.223218.9793
30.78610.14720.11072.1307-0.05090.4033-0.0482-0.34430.16520.1722-0.0351-0.03590.0147-0.1520.08330.15970.003-0.00490.4256-0.02560.0623-22.3099-44.897633.1533
421.6563-8.05150.01812.50778.55467.71410.2291-0.8751.0898-0.4569-0.72460.2427-0.2901-0.91050.49550.65630.0084-0.13510.6821-0.15310.9657-0.1956-8.276641.6227
52.59220.45051.21451.65921.30285.3138-0.0595-0.48480.40120.47710.1797-0.3958-0.27260.1713-0.12020.30840.084-0.17690.4149-0.35930.3786-17.2417-6.603948.693
65.61433.01951.13348.22845.93168.2253-0.0831-0.21920.05260.69490.07990.17310.3503-0.10690.00330.19680.11-0.04840.3795-0.09560.0768-29.2346-24.102442.3455
73.2462-0.1372-0.8321.3888-0.79044.9202-0.0501-0.2564-0.03010.15260.02670.01460.0518-0.04030.02340.134-0.0252-0.010.21580.02290.0371-25.5502-52.845618.9314
80.5198-0.2107-0.19154.12892.29072.1017-0.048-0.3390.40340.34440.1269-0.2049-0.2162-0.0154-0.0790.30230.0951-0.09220.4093-0.25040.3383-25.2444-7.10241.9744
93.3721-1.3616-0.57957.23560.70941.5565-0.0442-0.34210.02490.4299-0.02320.4311-0.0361-0.27190.06730.20890.12570.03010.49-0.11640.0884-44.8574-12.391538.9104
100.24650.43150.13631.861.15471.4701-0.1169-0.03680.0409-0.0952-0.13180.34780.0679-0.32020.24870.0908-0.0694-0.03210.43140.01670.1841-55.0668-56.8963-0.0084
111.27110.3270.41152.5087-0.49323.205-0.02340.0694-0.0181-0.1228-0.3131-0.25840.29540.31640.33650.0597-0.05630.03010.35970.08110.0917-44.41-69.097-8.8938
120.50620.57030.44992.23351.45121.4801-0.067-0.14170.1291-0.0686-0.09850.4308-0.1502-0.30050.16550.06440.0362-0.00850.3765-0.01330.1359-49.9276-35.230717.4272
131.9189-0.4688-0.3312.71471.41953.1086-0.1038-0.33640.43910.1478-0.06310.1292-0.4343-0.32410.16690.25110.21020.00830.4033-0.16560.2341-46.7281-3.47533.9282
140.66453.53232.612718.896913.964310.3221-0.2137-0.03180.0487-1.3242-0.00750.2727-0.9735-0.04740.22120.3820.0430.01490.55980.00660.3659-44.1279-26.848612.8488
150.5428-0.2536-0.00332.66460.90640.917-0.0783-0.2240.20610.16520.080.1402-0.1504-0.21-0.00170.14910.09410.02210.3893-0.07510.1444-38.3828-20.238427.5135
165.13733.46421.19766.21682.00283.9928-0.152-0.16970.7367-0.2597-0.0520.1947-0.8572-0.26470.2040.67810.31750.00380.2824-0.26810.6623-42.43918.362537.411
170.7396-0.5028-0.39891.72010.97561.14040.00880.10560.1004-0.1420.0572-0.1116-0.0175-0.0597-0.06590.0609-0.03470.00780.22820.05010.0272-17.0189-45.02-4.7015
181.7540.02380.34040.91630.03081.8118-0.06850.0317-0.26850.03190.0410.08930.3325-0.14610.02750.1923-0.06010.05540.19620.00920.0628-18.1295-70.8036-4.4203
190.6845-0.4846-0.37842.49341.13391.03770.05350.01940.2651-0.09020.0915-0.1027-0.208-0.0739-0.1450.11110.01020.02590.21680.03570.1194-21.1809-27.59753.1742
200.96560.0744-0.16713.2295-0.39941.67690.1236-0.14690.6136-0.26320.1175-0.429-0.5505-0.0042-0.24110.3663-0.00510.09370.1722-0.13590.5498-20.64132.257220.0253
210.688-4.7341-1.844832.626312.71694.9649-0.1564-0.09020.12261.03850.575-1.00770.41950.2932-0.41860.39930.1432-0.00930.71490.00030.6005-16.187-26.818614.5816
220.6755-0.0366-0.04281.63520.71740.92280.0224-0.08790.3887-0.05080.0801-0.0641-0.2775-0.1159-0.10250.18840.05420.03290.2466-0.03240.2521-26.4637-15.352118.9263
233.9724-1.041-0.65175.97883.44398.49320.2031-0.35780.6243-0.25650.3395-0.5155-0.78270.2939-0.54260.5563-0.08670.02570.1515-0.33330.8098-16.901518.562136.2207
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A9 - 56
2X-RAY DIFFRACTION2A57 - 258
3X-RAY DIFFRACTION3A259 - 324
4X-RAY DIFFRACTION4A325 - 329
5X-RAY DIFFRACTION5B1 - 38
6X-RAY DIFFRACTION6B39 - 58
7X-RAY DIFFRACTION7B59 - 79
8X-RAY DIFFRACTION8B80 - 172
9X-RAY DIFFRACTION9C9 - 37
10X-RAY DIFFRACTION10C38 - 159
11X-RAY DIFFRACTION11C160 - 258
12X-RAY DIFFRACTION12C259 - 325
13X-RAY DIFFRACTION13D1 - 54
14X-RAY DIFFRACTION14D55 - 61
15X-RAY DIFFRACTION15D62 - 145
16X-RAY DIFFRACTION16D146 - 171
17X-RAY DIFFRACTION17E9 - 160
18X-RAY DIFFRACTION18E161 - 263
19X-RAY DIFFRACTION19E264 - 325
20X-RAY DIFFRACTION20F1 - 54
21X-RAY DIFFRACTION21F55 - 60
22X-RAY DIFFRACTION22F61 - 149
23X-RAY DIFFRACTION23F150 - 171

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