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- PDB-9hva: Crystal structure of Fab34 complexed with a 18-mer peptide of FMDV VP1 -

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Basic information

Entry
Database: PDB / ID: 9hva
TitleCrystal structure of Fab34 complexed with a 18-mer peptide of FMDV VP1
Components
  • Capsid protein VP1
  • heavy chain
  • light chain
KeywordsIMMUNE SYSTEM / foot-and-mouth disease virus / cattle antibody / cross-reactive / linear epitope / antibody structure
Function / homology
Function and homology information


L-peptidase / symbiont-mediated perturbation of host chromatin organization / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / clathrin-dependent endocytosis of virus by host cell ...L-peptidase / symbiont-mediated perturbation of host chromatin organization / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / ribonucleoside triphosphate phosphatase activity / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / clathrin-dependent endocytosis of virus by host cell / molecular adaptor activity / RNA helicase activity / viral protein processing / host cell endoplasmic reticulum membrane / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / virion attachment to host cell / host cell nucleus / structural molecule activity / proteolysis / RNA binding / ATP binding
Similarity search - Function
Peptidase C28, foot-and-mouth virus L-proteinase / Foot-and-mouth virus L-proteinase / Aphthovirus leader protease (L(pro)) domain profile. / Foot-and-mouth disease virus VP1 coat / Capsid protein VP4 superfamily, Picornavirus / Helicase/polymerase/peptidase polyprotein, Calicivirus-type / Papain-like cysteine peptidase superfamily / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirales 3C/3C-like protease domain ...Peptidase C28, foot-and-mouth virus L-proteinase / Foot-and-mouth virus L-proteinase / Aphthovirus leader protease (L(pro)) domain profile. / Foot-and-mouth disease virus VP1 coat / Capsid protein VP4 superfamily, Picornavirus / Helicase/polymerase/peptidase polyprotein, Calicivirus-type / Papain-like cysteine peptidase superfamily / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Picornavirus capsid / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / Reverse transcriptase/Diguanylate cyclase domain / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biological speciesBos taurus (domestic cattle)
Foot-and-mouth disease virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.89 Å
AuthorsRen, J. / Duyvesteyn, H.M.E. / Stuart, D.I.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Medical Research Council (MRC, United Kingdom)MR/N00065X/ 1 United Kingdom
Wellcome Trust060208/Z/00/Z United Kingdom
CitationJournal: NPJ Vaccines / Year: 2026
Title: Cattle antibodies identify a cross-serotype broadly neutralising foot-and-mouth disease virus epitope.
Authors: Marie Bonnet-Di Placido / Helen M E Duyvesteyn / Angela W Steyn / Abigail L Hay / Claudine Porta / Kristel Ramirez Valdez / Elena Lokhman / Sylvia Crossley / Kevan Hanson / William N Mwangi ...Authors: Marie Bonnet-Di Placido / Helen M E Duyvesteyn / Angela W Steyn / Abigail L Hay / Claudine Porta / Kristel Ramirez Valdez / Elena Lokhman / Sylvia Crossley / Kevan Hanson / William N Mwangi / Danish Munir / Eva Perez-Martin / Nick J Knowles / Alison Burman / Abdelaziz A Yassin / Amin Asfor / Cristina Faralla / Katherine J Lam / Róisín McComb / Carina Leifeld / Kimberly Pietersz / Donald P King / Erwin van den Born / Sherie K Duncan / Bryan Charleston / Elizabeth E Fry / Jingshan Ren / David I Stuart / John A Hammond /
Abstract: Foot-and-mouth disease virus (FMDV) causes a devastating disease that threatens global food security. Vaccination is hindered by antigenic diversity across serotypes. To identify cross-serotype ...Foot-and-mouth disease virus (FMDV) causes a devastating disease that threatens global food security. Vaccination is hindered by antigenic diversity across serotypes. To identify cross-serotype neutralising epitopes, we isolated 24 FMDV-specific antibodies from cattle sequentially vaccinated with antigens from four serotypes, of which three neutralised three vaccine strains. These three antibodies neutralised 21 and bound 59 additional topotypes across O, A, Asia 1, and C serotypes. Cryo-EM complexes of Fabs with FMD virus-like particles indicated all three recognise a common flexible epitope at the VP1 C-terminus, confirmed by binding competition. Crystallography and structural modelling revealed that a normally inaccessible surface of the hydrophobic VP1 C-terminal peptides inserts into a similar groove in all three antibodies. Comparison of neutralisation activity and integrin receptor blocking by whole antibodies, F(ab')s, and Fabs suggests neutralisation is mediated by Fc steric hindrance of receptor binding. This cryptic, linear, and cross-serotype neutralising epitope may inform improved FMD vaccines.
History
DepositionDec 25, 2024Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 14, 2026Provider: repository / Type: Initial release
Revision 1.1Apr 8, 2026Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.year
Revision 1.2Apr 15, 2026Group: Database references / Category: citation / citation_author / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.3Jun 3, 2026Group: Database references / Category: citation / Item: _citation.journal_volume

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
H: heavy chain
L: light chain
B: heavy chain
C: light chain
E: heavy chain
F: light chain
I: heavy chain
J: light chain
M: heavy chain
N: light chain
P: heavy chain
Q: light chain
A: Capsid protein VP1
D: Capsid protein VP1
G: Capsid protein VP1
K: Capsid protein VP1
O: Capsid protein VP1
R: Capsid protein VP1


Theoretical massNumber of molelcules
Total (without water)299,29418
Polymers299,29418
Non-polymers00
Water00
1
H: heavy chain
L: light chain
A: Capsid protein VP1


Theoretical massNumber of molelcules
Total (without water)49,8823
Polymers49,8823
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: heavy chain
C: light chain
D: Capsid protein VP1


Theoretical massNumber of molelcules
Total (without water)49,8823
Polymers49,8823
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: heavy chain
F: light chain
G: Capsid protein VP1


Theoretical massNumber of molelcules
Total (without water)49,8823
Polymers49,8823
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
I: heavy chain
J: light chain
K: Capsid protein VP1


Theoretical massNumber of molelcules
Total (without water)49,8823
Polymers49,8823
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
M: heavy chain
N: light chain
O: Capsid protein VP1


Theoretical massNumber of molelcules
Total (without water)49,8823
Polymers49,8823
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
P: heavy chain
Q: light chain
R: Capsid protein VP1


Theoretical massNumber of molelcules
Total (without water)49,8823
Polymers49,8823
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)302.540, 111.906, 140.575
Angle α, β, γ (deg.)90.000, 115.990, 90.000
Int Tables number5
Space group name H-MC121
Space group name HallC2y
Symmetry operation#1: x,y,z
#2: -x,y,-z
#3: x+1/2,y+1/2,z
#4: -x+1/2,y+1/2,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails (eV)
d_1ens_1chain "A"
d_2ens_1chain "D"
d_3ens_1chain "G"
d_4ens_1chain "K"
d_5ens_1chain "O"
d_6ens_1chain "R"
d_1ens_2(chain "B" and (resid 1 through 69 or resid 71...
d_2ens_2(chain "E" and (resid 1 through 69 or resid 71...
d_3ens_2(chain "H" and (resid 1 through 69 or resid 71...
d_4ens_2(chain "I" and (resid 1 through 69 or resid 71...
d_5ens_2(chain "M" and (resid 1 through 69 or resid 71...
d_6ens_2(chain "P" and (resid 1 through 69 or resid 71...
d_1ens_3chain "C"
d_2ens_3chain "F"
d_3ens_3chain "J"
d_4ens_3chain "L"
d_5ens_3chain "N"
d_6ens_3chain "Q"

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ens_1HISHISGLNGLNAM201 - 2118 - 18
d_21ens_1HISHISGLNGLNDN201 - 2118 - 18
d_31ens_1HISHISGLNGLNGO201 - 2118 - 18
d_41ens_1HISHISGLNGLNKP201 - 2118 - 18
d_51ens_1HISHISGLNGLNOQ201 - 2118 - 18
d_61ens_1HISHISGLNGLNRR201 - 2118 - 18
d_11ens_2GLNGLNILEILEBC1 - 691 - 69
d_12ens_2GLUGLUGLYGLYBC71 - 11971 - 119
d_13ens_2GLYGLYGLYGLYBC121 - 201121 - 201
d_14ens_2GLNGLNARGARGBC207 - 229207 - 229
d_21ens_2GLNGLNILEILEEE1 - 691 - 69
d_22ens_2GLUGLUGLYGLYEE71 - 11971 - 119
d_23ens_2GLYGLYGLYGLYEE121 - 201121 - 201
d_24ens_2GLNGLNARGARGEE207 - 229207 - 229
d_31ens_2GLNGLNILEILEHA1 - 691 - 69
d_32ens_2GLUGLUGLYGLYHA71 - 11971 - 119
d_33ens_2GLYGLYGLYGLYHA121 - 201121 - 201
d_34ens_2GLNGLNARGARGHA207 - 229207 - 229
d_41ens_2GLNGLNILEILEIG1 - 691 - 69
d_42ens_2GLUGLUGLYGLYIG71 - 11971 - 119
d_43ens_2GLYGLYGLYGLYIG121 - 201121 - 201
d_44ens_2GLNGLNARGARGIG207 - 229207 - 229
d_51ens_2GLNGLNILEILEMI1 - 691 - 69
d_52ens_2GLUGLUGLYGLYMI71 - 11971 - 119
d_53ens_2GLYGLYGLYGLYMI121 - 201121 - 201
d_54ens_2GLNGLNARGARGMI207 - 229207 - 229
d_61ens_2GLNGLNILEILEPK1 - 691 - 69
d_62ens_2GLUGLUGLYGLYPK71 - 11971 - 119
d_63ens_2GLYGLYGLYGLYPK121 - 201121 - 201
d_64ens_2GLNGLNARGARGPK207 - 229207 - 229
d_11ens_3TYRTYRCYSCYSCD3 - 2132 - 212
d_21ens_3TYRTYRCYSCYSFF3 - 2132 - 212
d_31ens_3TYRTYRCYSCYSJH3 - 2132 - 212
d_41ens_3TYRTYRCYSCYSLB3 - 2132 - 212
d_51ens_3TYRTYRCYSCYSNJ3 - 2132 - 212
d_61ens_3TYRTYRCYSCYSQL3 - 2132 - 212

NCS ensembles :
ID
ens_1
ens_2
ens_3

NCS oper:
IDCodeMatrixVector
1given(-0.794636978723, 0.606023046568, 0.0358906544059), (0.160623007502, 0.266890793394, -0.950247101475), (-0.585450528659, -0.749336620905, -0.309422538067)69.6886474031, -39.4276098144, -4.98632390032
2given(-0.978662671761, 0.145529863964, 0.145053209536), (0.204775509352, 0.748938596877, 0.630204703947), (-0.0169223423872, 0.646461164187, -0.762759200224)110.331414591, -25.2832180939, 50.5933125658
3given(0.592258465928, -0.62755632485, 0.505374087857), (-0.268864210384, -0.745183944555, -0.610256442123), (0.7595669463, 0.225552539154, -0.610068935588)-14.3181149288, -22.3439974796, 66.5221110592
4given(0.654723150086, 0.111130203089, 0.747654783107), (0.10314652288, -0.993015817763, 0.0572746059889), (0.748797964447, 0.0396189807391, -0.661613138326)-0.104503548348, -116.01515131, 8.639937471
5given(-0.934795603556, -0.28345823491, -0.2140294574), (-0.133988683888, -0.276639065798, 0.951587021698), (-0.328944086682, 0.918216889594, 0.220620786647)37.1075790853, -71.2884644102, 62.2106085789
6given(0.913361929931, -0.235209115497, 0.332335157545), (0.25483501925, -0.306339500558, -0.917177858085), (0.317535978934, 0.922405974821, -0.219859317969)41.0296834722, -63.2834281296, 60.2710872855
7given(-0.744019239807, 0.249646674015, -0.619767624961), (0.664764247457, 0.369952704153, -0.64901732796), (0.0672596914974, -0.894880737776, -0.441208113091)63.8160501072, -25.1165118567, -40.4075777136
8given(-0.808343420581, -0.587046651385, -0.0442396146173), (-0.265151598724, 0.29594994369, 0.917664568633), (-0.525619200655, 0.753518320897, -0.394885547944)19.0429345155, 11.3618111392, 128.151984081
9given(-0.391938318862, -0.60058173695, -0.696911709939), (-0.662622271647, -0.341219599916, 0.666709014302), (-0.638213192691, 0.723098030612, -0.264221798493)0.821675424008, -79.7062967381, 75.1655672808
10given(0.567539838933, 0.0218125447324, 0.823056950713), (-0.0122370927834, -0.999315125631, 0.0349218161902), (0.823254993781, -0.0298913462077, -0.56688422331)3.82337640188, -107.121080921, 0.621258771899
11given(0.894704535987, -0.248311827541, 0.371274870666), (0.273107739208, -0.353608196721, -0.894635906946), (0.353434514541, 0.901832844553, -0.24855897573)40.5289221945, -66.3032671353, 57.1077852681
12given(-0.827989373989, -0.55866516381, -0.0482372398266), (-0.284832387795, 0.344922556876, 0.894370695305), (-0.483015638902, 0.754268960321, -0.444718144529)22.0823792336, 14.4437933958, 126.64049391
13given(-0.717927175139, 0.243907332623, -0.65198909829), (0.693359138752, 0.333858885445, -0.638585428364), (0.0619166851936, -0.910520432337, -0.408801744605)63.0261773842, -28.5751079874, -40.4142982809
14given(-0.3843004831, -0.593759366358, -0.706939144164), (-0.705168800366, -0.305439963482, 0.639877638067), (-0.595860807303, 0.744416713656, -0.301319854557)2.7499201755, -76.634045917, 76.2598928882
15given(0.547938202226, 0.0256928315782, 0.836124156419), (-0.0148375976163, -0.999072461934, 0.0404235265812), (0.836387214296, -0.0345556682728, -0.547048748789)4.95555927263, -106.873598304, 0.312515735378

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Components

#1: Antibody
heavy chain


Mass: 24988.916 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Production host: Homo sapiens (human)
#2: Antibody
light chain


Mass: 22793.988 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bos taurus (domestic cattle) / Production host: Homo sapiens (human)
#3: Protein/peptide
Capsid protein VP1 / P1D / Virion protein 1


Mass: 2099.479 Da / Num. of mol.: 6 / Source method: obtained synthetically / Source: (synth.) Foot-and-mouth disease virus / References: UniProt: P03305
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: 3.57 Å3/Da / Density % sol: 65.58 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1 M MES monohydrate pH 6.0, 14 % w/v PEG 4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97627 Å
DetectorType: DECTRIS EIGER2 XE 16M / Detector: PIXEL / Date: Jul 7, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97627 Å / Relative weight: 1
ReflectionResolution: 3.89→75.2 Å / Num. obs: 38889 / % possible obs: 99.7 % / Redundancy: 7.2 % / Biso Wilson estimate: 146.15 Å2 / CC1/2: 0.984 / Rmerge(I) obs: 0.387 / Rpim(I) all: 0.154 / Net I/σ(I): 4.5
Reflection shellResolution: 3.89→3.96 Å / Mean I/σ(I) obs: 0.5 / Num. unique obs: 1876 / CC1/2: 0.242 / % possible all: 99.3

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Processing

Software
NameVersionClassification
Coot1.20.1_4487model building
PHENIX1.20.1_4487refinement
GDA1.20.1_4487data collection
xia2data reduction
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.89→75.17 Å / SU ML: 0.6838 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 29.3013
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2792 2001 5.15 %
Rwork0.2327 36828 -
obs0.2351 38829 99.51 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 188.61 Å2
Refinement stepCycle: LAST / Resolution: 3.89→75.17 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19794 0 0 0 19794
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.002320232
X-RAY DIFFRACTIONf_angle_d0.567227586
X-RAY DIFFRACTIONf_chiral_restr0.04543263
X-RAY DIFFRACTIONf_plane_restr0.00463491
X-RAY DIFFRACTIONf_dihedral_angle_d10.56797174
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2MAX-RAY DIFFRACTIONTorsion NCS0.271421280044
ens_1d_3MAX-RAY DIFFRACTIONTorsion NCS0.168006945981
ens_1d_4MAX-RAY DIFFRACTIONTorsion NCS0.209693083367
ens_1d_5MAX-RAY DIFFRACTIONTorsion NCS0.189185873555
ens_1d_6MAX-RAY DIFFRACTIONTorsion NCS0.37952673154
ens_2d_2CBX-RAY DIFFRACTIONTorsion NCS1.04152639307
ens_2d_3CBX-RAY DIFFRACTIONTorsion NCS1.30651968229
ens_2d_4CBX-RAY DIFFRACTIONTorsion NCS0.956304363542
ens_2d_5CBX-RAY DIFFRACTIONTorsion NCS1.04094024498
ens_2d_6CBX-RAY DIFFRACTIONTorsion NCS0.424402982166
ens_3d_2DCX-RAY DIFFRACTIONTorsion NCS0.932281587568
ens_3d_3DCX-RAY DIFFRACTIONTorsion NCS0.863313637404
ens_3d_4DCX-RAY DIFFRACTIONTorsion NCS1.18460858089
ens_3d_5DCX-RAY DIFFRACTIONTorsion NCS1.43999340125
ens_3d_6DCX-RAY DIFFRACTIONTorsion NCS0.16876442164
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.89-3.990.42021440.3642566X-RAY DIFFRACTION98.65
3.99-4.10.35091490.33782600X-RAY DIFFRACTION99.31
4.1-4.220.35611400.31042585X-RAY DIFFRACTION99.53
4.22-4.350.31941420.28852633X-RAY DIFFRACTION99.5
4.35-4.510.28581390.26262622X-RAY DIFFRACTION99.6
4.51-4.690.28291570.22962614X-RAY DIFFRACTION99.53
4.69-4.90.26481360.21932634X-RAY DIFFRACTION99.5
4.9-5.160.26881450.22892610X-RAY DIFFRACTION99.71
5.16-5.480.24711330.23712619X-RAY DIFFRACTION99.67
5.48-5.910.32181490.24112659X-RAY DIFFRACTION99.75
5.91-6.50.28731070.23312670X-RAY DIFFRACTION99.78
6.5-7.440.26761590.23892643X-RAY DIFFRACTION99.64
7.44-9.370.22811500.17812665X-RAY DIFFRACTION99.89
9.37-75.170.25961510.19582708X-RAY DIFFRACTION99.24
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)
16.305084998730.8268846453321.047016611662.85420712808-3.969449657128.9366468519-0.369589495844-0.2048138969620.4801485961940.2748521469990.0726793397403-0.03276453874920.2134693951820.21425614658-0.03026854879151.62635188426-0.3187128661180.165967006891.58402378677-0.3085991504821.5787551756246.9491586753-24.722207283444.4129450129
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38.62349649923-0.9253669954571.376707568987.445437466960.8009750448141.76065858216-0.713036801272-0.176961189436-0.3068751304820.1490286094250.4072477033851.931312736320.6483716837220.00124080684422-0.01947942931381.55241835617-0.235367423043-0.02508219988771.743647747010.2319341165891.5704841854940.2139361787-24.685758491738.2107273293
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508.30543963610.284355364525-5.829296659735.07289798173-5.436392696739.476987125263.655816953792.654864661921.383875087972.193328407150.451687176254-1.22982055043-1.175459577131.003067784321.913949593461.626028462360.394958495325-0.4235664000742.95806334651-0.14058081391.1034999840167.9283584437-40.863304460884.2082041953
518.68047217991-5.47294027505-4.019759386283.550521063282.75593665936.954116351210.72267758737-0.4522737572421.2734928873-1.949104374152.031807480961.12488777639-0.6557458434851.76946713366-0.0156563501282.528473974280.06030187349490.2413007703961.95547460615-0.08020223828691.5635299148771.5431437779-73.092363659429.723126238
529.39517270381.21762431187-5.415597554085.85423427638-3.34373896293.88657140437-1.10864229379-1.81607165167-1.492105944130.364518764297-4.23250297485-0.907446756412-2.730568716371.25117407001-3.178046777632.244746450660.256237242829-0.9120700446482.161658079320.2979335564052.5268554441-25.0584953577-30.884649623918.3526732598
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'H' and (resid 1 through 90 )HA1 - 901 - 90
22chain 'H' and (resid 91 through 110 )HA91 - 11091 - 110
33chain 'H' and (resid 111 through 134 )HA111 - 134111 - 134
44chain 'H' and (resid 135 through 229 )HA135 - 229135 - 222
55chain 'L' and (resid 3 through 75 )LB3 - 751 - 73
66chain 'L' and (resid 76 through 115 )LB76 - 11574 - 113
77chain 'L' and (resid 116 through 188 )LB116 - 188114 - 186
88chain 'L' and (resid 189 through 213 )LB189 - 213187 - 211
99chain 'B' and (resid 1 through 90 )BC1 - 901 - 90
1010chain 'B' and (resid 91 through 110 )BC91 - 11091 - 110
1111chain 'B' and (resid 111 through 134 )BC111 - 134111 - 134
1212chain 'B' and (resid 135 through 229 )BC135 - 229135 - 221
1313chain 'C' and (resid 3 through 75 )CD3 - 751 - 73
1414chain 'C' and (resid 76 through 130 )CD76 - 13074 - 128
1515chain 'C' and (resid 131 through 213 )CD131 - 213129 - 211
1616chain 'E' and (resid 1 through 90 )EE1 - 901 - 90
1717chain 'E' and (resid 91 through 110 )EE91 - 11091 - 110
1818chain 'E' and (resid 111 through 134 )EE111 - 134111 - 134
1919chain 'E' and (resid 135 through 229 )EE135 - 229135 - 222
2020chain 'F' and (resid 3 through 75 )FF3 - 751 - 73
2121chain 'F' and (resid 76 through 115 )FF76 - 11574 - 113
2222chain 'F' and (resid 116 through 188 )FF116 - 188114 - 186
2323chain 'F' and (resid 189 through 213 )FF189 - 213187 - 211
2424chain 'I' and (resid 1 through 90 )IG1 - 901 - 90
2525chain 'I' and (resid 91 through 110 )IG91 - 11091 - 110
2626chain 'I' and (resid 111 through 134 )IG111 - 134111 - 134
2727chain 'I' and (resid 135 through 229 )IG135 - 229135 - 222
2828chain 'J' and (resid 3 through 75 )JH3 - 751 - 73
2929chain 'J' and (resid 76 through 115 )JH76 - 11574 - 113
3030chain 'J' and (resid 116 through 188 )JH116 - 188114 - 186
3131chain 'J' and (resid 189 through 213 )JH189 - 213187 - 211
3232chain 'M' and (resid 1 through 90 )MI1 - 901 - 90
3333chain 'M' and (resid 91 through 110 )MI91 - 11091 - 110
3434chain 'M' and (resid 111 through 134 )MI111 - 134111 - 134
3535chain 'M' and (resid 135 through 229 )MI135 - 229135 - 222
3636chain 'N' and (resid 3 through 75 )NJ3 - 751 - 73
3737chain 'N' and (resid 76 through 115 )NJ76 - 11574 - 113
3838chain 'N' and (resid 116 through 188 )NJ116 - 188114 - 186
3939chain 'N' and (resid 189 through 213 )NJ189 - 213187 - 211
4040chain 'P' and (resid 1 through 90 )PK1 - 901 - 90
4141chain 'P' and (resid 91 through 110 )PK91 - 11091 - 110
4242chain 'P' and (resid 111 through 134 )PK111 - 134111 - 134
4343chain 'P' and (resid 135 through 229 )PK135 - 229135 - 222
4444chain 'Q' and (resid 3 through 75 )QL3 - 751 - 73
4545chain 'Q' and (resid 76 through 130 )QL76 - 13074 - 128
4646chain 'Q' and (resid 131 through 213 )QL131 - 213129 - 211
4747chain 'A' and (resid 201 through 211 )AM201 - 2111 - 11
4848chain 'D' and (resid 201 through 211 )DN201 - 2111 - 11
4949chain 'G' and (resid 201 through 211 )GO201 - 2111 - 11
5050chain 'K' and (resid 201 through 211 )KP201 - 2111 - 11
5151chain 'O' and (resid 201 through 211 )OQ201 - 2111 - 11
5252chain 'R' and (resid 201 through 211 )RR201 - 2111 - 11

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