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- PDB-3ngb: Crystal structure of broadly and potently neutralizing antibody V... -

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Basic information

Entry
Database: PDB / ID: 3ngb
TitleCrystal structure of broadly and potently neutralizing antibody VRC01 in complex with HIV-1 gp120
Components
  • (Antigen binding fragment of ...) x 2
  • Envelope glycoprotein gp160
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / HIV / gp120 / antibody / VRC01 / neutralization / vaccine / envelope glycoprotein / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope ...positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / plasma membrane
Similarity search - Function
HIV Envelope Protein Gp120; Chain G / Human immunodeficiency virus 1, Gp160, envelope glycoprotein / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Beta Complex / Immunoglobulins ...HIV Envelope Protein Gp120; Chain G / Human immunodeficiency virus 1, Gp160, envelope glycoprotein / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Beta Complex / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
beta-D-glucopyranose / Envelope glycoprotein gp160
Similarity search - Component
Biological speciesHuman immunodeficiency virus 1
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.68 Å
AuthorsZhou, T. / Kwong, P.D.
CitationJournal: Science / Year: 2010
Title: Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01.
Authors: Zhou, T. / Georgiev, I. / Wu, X. / Yang, Z.Y. / Dai, K. / Finzi, A. / Do Kwon, Y. / Scheid, J.F. / Shi, W. / Xu, L. / Yang, Y. / Zhu, J. / Nussenzweig, M.C. / Sodroski, J. / Shapiro, L. / ...Authors: Zhou, T. / Georgiev, I. / Wu, X. / Yang, Z.Y. / Dai, K. / Finzi, A. / Do Kwon, Y. / Scheid, J.F. / Shi, W. / Xu, L. / Yang, Y. / Zhu, J. / Nussenzweig, M.C. / Sodroski, J. / Shapiro, L. / Nabel, G.J. / Mascola, J.R. / Kwong, P.D.
History
DepositionJun 11, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 7, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 23, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / 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 / pdbx_validate_close_contact / struct_asym / struct_conn / struct_ref_seq_dif / 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 / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 3.0Oct 14, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Refinement description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / pdbx_distant_solvent_atoms / pdbx_nonpoly_scheme / pdbx_refine_tls_group / pdbx_validate_close_contact / struct_conn
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_seq_id / _atom_site.label_asym_id / _chem_comp.pdbx_synonyms / _pdbx_nonpoly_scheme.asym_id / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.ndb_seq_num / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.ptnr2_auth_seq_id
Revision 3.1Mar 31, 2021Group: Source and taxonomy / Category: entity_src_gen
Item: _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strain
Revision 3.2Sep 6, 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
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
G: Envelope glycoprotein gp160
H: Antigen binding fragment of heavy chain: Antibody VRC01
L: Antigen binding fragment of light chain: Antibody VRC01
A: Envelope glycoprotein gp160
B: Antigen binding fragment of heavy chain: Antibody VRC01
C: Antigen binding fragment of light chain: Antibody VRC01
D: Envelope glycoprotein gp160
E: Antigen binding fragment of heavy chain: Antibody VRC01
F: Antigen binding fragment of light chain: Antibody VRC01
I: Envelope glycoprotein gp160
J: Antigen binding fragment of heavy chain: Antibody VRC01
K: Antigen binding fragment of light chain: Antibody VRC01
hetero molecules


Theoretical massNumber of molelcules
Total (without water)363,53682
Polymers347,00712
Non-polymers16,52970
Water9,422523
1
G: Envelope glycoprotein gp160
H: Antigen binding fragment of heavy chain: Antibody VRC01
L: Antigen binding fragment of light chain: Antibody VRC01
hetero molecules


Theoretical massNumber of molelcules
Total (without water)90,27616
Polymers86,7523
Non-polymers3,52413
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Envelope glycoprotein gp160
B: Antigen binding fragment of heavy chain: Antibody VRC01
C: Antigen binding fragment of light chain: Antibody VRC01
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,82225
Polymers86,7523
Non-polymers5,07122
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
D: Envelope glycoprotein gp160
E: Antigen binding fragment of heavy chain: Antibody VRC01
F: Antigen binding fragment of light chain: Antibody VRC01
hetero molecules


Theoretical massNumber of molelcules
Total (without water)90,43520
Polymers86,7523
Non-polymers3,68317
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
I: Envelope glycoprotein gp160
J: Antigen binding fragment of heavy chain: Antibody VRC01
K: Antigen binding fragment of light chain: Antibody VRC01
hetero molecules


Theoretical massNumber of molelcules
Total (without water)91,00321
Polymers86,7523
Non-polymers4,25118
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)108.630, 98.275, 205.256
Angle α, β, γ (deg.)90.00, 99.68, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 1 types, 4 molecules GADI

#1: Protein
Envelope glycoprotein gp160


Mass: 39211.434 Da / Num. of mol.: 4 / Fragment: UNP RESIDUES 43-122, 201-303, 325-486
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Strain: 93TH057 / Description: HIV-1 gp120 with leader sequence / Gene: Env, pol / Cell line (production host): HEK293F / Production host: Homo sapiens (human) / References: UniProt: Q0ED31

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Antibody , 2 types, 8 molecules HBEJLCFK

#2: Antibody
Antigen binding fragment of heavy chain: Antibody VRC01


Mass: 24367.631 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Description: Codon-optimized human antibody heavy chain of VRC01
Gene: Heavy chain / Cell line (production host): HEK293F / Production host: Homo sapiens (human)
#3: Antibody
Antigen binding fragment of light chain: Antibody VRC01


Mass: 23172.686 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Description: Codon-optimized human antibody light chain of VRC01
Gene: Light chain / Cell line (production host): HEK293F / Production host: Homo sapiens (human)

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Sugars , 4 types, 63 molecules

#4: 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.: 3
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
#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.: 1
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
#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.: 46
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
#7: Sugar
ChemComp-BGC / beta-D-glucopyranose / beta-D-glucose / D-glucose / glucose


Type: D-saccharide, beta linking / Mass: 180.156 Da / Num. of mol.: 13
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DGlcpbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
b-D-glucopyranoseCOMMON NAMEGMML 1.0
b-D-GlcpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 2 types, 530 molecules

#8: Chemical
ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 523 / 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: 3.11 Å3/Da / Density % sol: 60.48 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 10% PEG 4000, 9% Isopropanol, 0.1M Ammonium Sulfate, 0.1M Tris/Cl-, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 0.82656 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 31, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.82656 Å / Relative weight: 1
ReflectionResolution: 2.68→50 Å / Num. obs: 97150 / % possible obs: 94.8 % / Observed criterion σ(F): 1 / Redundancy: 3.4 % / Rsym value: 0.08 / Net I/σ(I): 18.6

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Processing

Software
NameVersionClassification
APSSER-CAT MARCCDdata collection
PHASERphasing
PHENIX(phenix.refine: 1.5_2)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3IDX

3idx


Resolution: 2.68→49.733 Å / SU ML: 0.36 / Isotropic thermal model: Overall / Cross valid method: THROUGHOUT / σ(F): 1.34 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2563 4867 5.01 %RANDOM
Rwork0.1967 ---
obs0.1997 97150 94.8 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 67.594 Å2 / ksol: 0.304 e/Å3
Displacement parametersBiso mean: 57.3 Å2
Baniso -1Baniso -2Baniso -3
1-2.981 Å2-0 Å25.7775 Å2
2--2.2145 Å20 Å2
3----5.1954 Å2
Refinement stepCycle: LAST / Resolution: 2.68→49.733 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24218 0 1067 523 25808
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00225953
X-RAY DIFFRACTIONf_angle_d0.53435243
X-RAY DIFFRACTIONf_dihedral_angle_d14.6539716
X-RAY DIFFRACTIONf_chiral_restr0.0344058
X-RAY DIFFRACTIONf_plane_restr0.0034423
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.68-2.71340.3373110.3116270X-RAY DIFFRACTION7
2.7134-2.74530.251190.3339530X-RAY DIFFRACTION14
2.7453-2.77880.4039400.3578803X-RAY DIFFRACTION21
2.7788-2.8140.4475630.34381127X-RAY DIFFRACTION30
2.814-2.8510.4184660.36061551X-RAY DIFFRACTION41
2.851-2.89010.3776960.33151957X-RAY DIFFRACTION52
2.8901-2.93130.4131980.33972367X-RAY DIFFRACTION62
2.9313-2.97510.36731570.32442655X-RAY DIFFRACTION72
2.9751-3.02160.37331590.30492937X-RAY DIFFRACTION78
3.0216-3.07110.34641710.29883246X-RAY DIFFRACTION85
3.0711-3.12410.35722070.28683422X-RAY DIFFRACTION92
3.1241-3.18090.36841840.28273579X-RAY DIFFRACTION95
3.1809-3.2420.33671970.27043642X-RAY DIFFRACTION98
3.242-3.30820.31751750.26013714X-RAY DIFFRACTION98
3.3082-3.38010.31941950.23853755X-RAY DIFFRACTION99
3.3801-3.45870.29611890.22453745X-RAY DIFFRACTION99
3.4587-3.54520.2561840.21133776X-RAY DIFFRACTION99
3.5452-3.6410.27511730.19413786X-RAY DIFFRACTION100
3.641-3.74810.26171940.18963795X-RAY DIFFRACTION100
3.7481-3.8690.23122110.18173745X-RAY DIFFRACTION100
3.869-4.00730.24922280.16933744X-RAY DIFFRACTION100
4.0073-4.16760.2452060.16063750X-RAY DIFFRACTION100
4.1676-4.35720.21621900.14533793X-RAY DIFFRACTION100
4.3572-4.58680.20371860.14353799X-RAY DIFFRACTION100
4.5868-4.87390.20532210.13723773X-RAY DIFFRACTION100
4.8739-5.24990.2142060.1313765X-RAY DIFFRACTION100
5.2499-5.77750.21131870.14643830X-RAY DIFFRACTION100
5.7775-6.61180.23362270.16093785X-RAY DIFFRACTION100
6.6118-8.32390.24092130.17153817X-RAY DIFFRACTION99
8.3239-49.74120.22262140.20823825X-RAY DIFFRACTION98
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)
13.08570.7872-1.1082.8459-1.20513.00460.0861-0.11160.58720.1304-0.1021-0.5005-0.30450.0621-0.15251.0422-0.02080.1817-0.12960.080.823-31.019351.4471-96.6077
23.4581-1.0457-1.18032.6738-0.6781.6460.08930.3448-0.1311-0.59610.009-0.24850.0833-0.340701.1008-0.01390.34460.175-0.02350.607-34.553929.5912-103.2689
30.8019-0.6043-0.99991.5489-1.83592.0410.1282-0.2490.22110.08160.22260.02680.0719-0.0171-00.6952-0.0420.05180.27190.04290.621-37.132619.4353-76.2948
40.3035-0.7547-0.00462.1680.89691.720.08720.0437-0.4516-0.23690.1648-0.20450.03460.1505-00.5321-0.1313-0.0810.61920.32030.563-24.1239-14.6427-56.7231
50.9312-0.66530.92890.5201-0.84451.09450.4163-0.42870.19930.4495-0.5212-1.1645-0.13560.5057-0.00010.7077-0.0973-0.12520.61610.17221.0884-17.256422.4751-66.0029
63.0572-1.60462.40932.3241-1.89581.9591-0.12550.84-0.0283-0.3489-0.137-1.0078-0.57491.07740.00010.6119-0.25610.17590.79730.16140.9515-11.0507-6.902-61.4243
71.45610.15990.37211.6957-0.98412.517-0.1317-0.02550.1788-0.01360.40970.2637-0.5838-0.611100.37930.0508-0.12330.48820.09820.3888-48.825866.4734-42.3619
82.98560.0822-1.21391.43780.64983.04050.1290.0582-0.3588-0.3058-0.01650.09450.3074-0.3201-00.5364-0.0903-0.19190.4720.05810.5483-41.184544.5264-43.7233
92.5718-0.84171.18090.8275-0.99241.67160.0315-0.6999-0.54560.04980.49340.0583-0.1362-0.2202-0.00010.37860.0184-0.06480.56170.14870.6365-17.521149.3102-27.4529
100.01890.19350.23241.17221.21521.0721-0.5089-0.34350.04530.37190.1864-0.14070.5604-0.3635-00.83510.2648-0.11660.98490.03860.896921.711937.1324-29.3911
113.01790.4642-1.42512.0594-0.0681.31770.14430.55940.2799-0.0453-0.0777-0.8662-0.37070.1337-00.3899-0.0306-0.13060.6480.03910.7359-4.446463.5072-38.7127
122.5281-1.14890.21620.552-0.37761.31640.17680.78130.6497-0.5948-0.4449-0.5740.64090.62-0.00010.83770.24870.02911.00140.01810.789819.422246.0887-42.2084
131.36021.3743-0.05841.8912-1.24082.37290.143-0.54710.23050.4930.13630.3668-0.4447-0.0501-00.90350.19610.10370.78380.19430.5029-67.48086.0249-44.3832
142.41440.31850.15222.3944-0.95531.27890.00740.0749-0.1707-0.28820.27390.23110.2929-0.24800.7374-0.0593-0.02830.62010.21920.4609-70.422-0.1361-66.6403
152.9003-0.6019-0.54734.9863-2.67191.9333-0.2604-0.33540.142-0.29160.19560.426-0.19430.0294-0.00050.57820.20390.15970.37690.15160.2482-64.595926.2924-77.1733
16-0.02420.11740.09381.04220.64230.27731.10070.3978-0.1933-0.9388-0.29870.82810.28990.134801.77950.3785-0.29792.14110.5811.3968-83.361348.7572-107.0718
171.5097-0.65190.88042.32630.58530.84270.0709-0.75050.18330.21910.35811.5148-0.8738-0.706701.04590.51750.36471.02890.34141.1922-80.380440.5358-69.7038
180.6052-0.34610.56230.0783-0.09090.17170.00320.6290.21640.01180.29420.0164-1.0749-1.00401.0940.2939-0.23061.97850.20241.1698-93.164246.3386-94.7239
192.9328-1.08511.01132.3159-1.30882.28690.1097-1.0013-0.21550.14180.018-0.4025-0.38060.042200.259-0.1685-0.19341.24790.23490.7139-0.119643.577814.9745
201.20061.2794-0.46951.1441-0.54681.74450.326-0.5924-0.6787-0.2593-0.1502-0.33440.20740.0718-0.00010.41370.0159-0.2590.99630.50041.1358-12.381626.64834.6902
214.3798-0.5291-0.68440.8593-0.72841.8990.2336-0.2432-0.16310.03-0.33670.4047-0.31430.2533-00.39370.0869-0.01870.88390.0230.3929-33.075944.7173-4.8552
220.61430.7575-0.13192.8066-0.04880.60620.4442-0.78960.0626-0.5604-0.2349-0.04090.3894-0.15250.00010.66820.1241-0.07481.350.2760.8794-73.657440.1733-5.3249
232.36550.0218-2.28631.4968-0.09022.01090.6862-0.88950.04850.4634-0.92450.3877-0.52040.3390.00010.5479-0.22610.11511.2229-0.14420.3592-43.427253.588313.005
241.03320.683-0.65330.7557-0.11880.24020.1958-1.0107-0.04350.2337-0.2118-0.25120.34040.254800.76490.0207-0.14991.13220.14210.6736-68.749940.74789.7178
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN G AND ( RESID 44:253 OR RESID 476:492 ) )G44 - 253
2X-RAY DIFFRACTION1( CHAIN G AND ( RESID 44:253 OR RESID 476:492 ) )G476 - 492
3X-RAY DIFFRACTION2( CHAIN G AND RESID 254:475 )G254 - 475
4X-RAY DIFFRACTION3( CHAIN H AND RESID 1:121 )H1 - 121
5X-RAY DIFFRACTION4( CHAIN H AND RESID 122:216 )H122 - 216
6X-RAY DIFFRACTION5( CHAIN L AND RESID 3:103 )L3 - 103
7X-RAY DIFFRACTION6( CHAIN L AND RESID 104:208 )L104 - 208
8X-RAY DIFFRACTION7( CHAIN A AND ( RESID 44:253 OR RESID 476:492 ) )A44 - 253
9X-RAY DIFFRACTION7( CHAIN A AND ( RESID 44:253 OR RESID 476:492 ) )A476 - 492
10X-RAY DIFFRACTION8( CHAIN A AND RESID 254:475 )A254 - 475
11X-RAY DIFFRACTION9( CHAIN B AND RESID 1:121 )B1 - 121
12X-RAY DIFFRACTION10( CHAIN B AND RESID 122:216 )B122 - 216
13X-RAY DIFFRACTION11( CHAIN C AND RESID 1:103 )C1 - 103
14X-RAY DIFFRACTION12( CHAIN C AND RESID 104:208 )C104 - 208
15X-RAY DIFFRACTION13( CHAIN D AND ( RESID 44:253 OR RESID 476:492 ) )D44 - 253
16X-RAY DIFFRACTION13( CHAIN D AND ( RESID 44:253 OR RESID 476:492 ) )D476 - 492
17X-RAY DIFFRACTION14( CHAIN D AND RESID 254:475 )D254 - 475
18X-RAY DIFFRACTION15( CHAIN E AND RESID 1:121 )E1 - 121
19X-RAY DIFFRACTION16( CHAIN E AND RESID 122:216 )E122 - 216
20X-RAY DIFFRACTION17( CHAIN F AND RESID 3:103 )F3 - 103
21X-RAY DIFFRACTION18( CHAIN F AND RESID 104:208 )F104 - 208
22X-RAY DIFFRACTION19( CHAIN I AND ( RESID 44:253 OR RESID 476:492 ) )I44 - 253
23X-RAY DIFFRACTION19( CHAIN I AND ( RESID 44:253 OR RESID 476:492 ) )I476 - 492
24X-RAY DIFFRACTION20( CHAIN I AND RESID 254:475 )I254 - 475
25X-RAY DIFFRACTION21( CHAIN J AND RESID 1:121 )J1 - 121
26X-RAY DIFFRACTION22( CHAIN J AND RESID 122:216 )J122 - 216
27X-RAY DIFFRACTION23( CHAIN K AND RESID 1:103 )K1 - 103
28X-RAY DIFFRACTION24( CHAIN K AND RESID 104:208 )K104 - 208

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