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- PDB-9y6d: CRYSTAL STRUCTURE OF THE A149T VARIANT OF SERINE HYDROXYMETHYLTRA... -

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Basic information

Entry
Database: PDB / ID: 9y6d
TitleCRYSTAL STRUCTURE OF THE A149T VARIANT OF SERINE HYDROXYMETHYLTRANSFERASE 8 FROM SOYBEAN CULTIVAR FORREST IN COMPLEX WITH PLP-GLYCINE
ComponentsSerine hydroxymethyltransferase
KeywordsTRANSFERASE / enzyme / missense variant
Function / homology
Function and homology information


glycine hydroxymethyltransferase / glycine hydroxymethyltransferase activity / : / tetrahydrofolate interconversion / methyltransferase activity / pyridoxal phosphate binding / methylation
Similarity search - Function
Serine hydroxymethyltransferase, pyridoxal phosphate binding site / Serine hydroxymethyltransferase pyridoxal-phosphate attachment site. / : / Serine hydroxymethyltransferase / Serine hydroxymethyltransferase-like domain / Serine hydroxymethyltransferase / Pyridoxal phosphate-dependent transferase, small domain / Pyridoxal phosphate-dependent transferase, major domain / Pyridoxal phosphate-dependent transferase
Similarity search - Domain/homology
Chem-PLG / Serine hydroxymethyltransferase
Similarity search - Component
Biological speciesGlycine max (soybean)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsBeamer, L.J. / Samarakoon, V. / Owuocha, L.F.
Funding support United States, 1items
OrganizationGrant numberCountry
National Science Foundation (NSF, United States)IOS 2152548 United States
Citation
Journal: FEBS J / Year: 2026
Title: Oligomeric defects in soybean serine hydroxymethyltransferase 8: tetramer destabilization by A149T and other variants associated with soybean cyst nematode resistance.
Authors: Vindya Samarakoon / David P Buckley / Luckio F Owuocha / Clarissa L Durie / Melissa G Mitchum / Lesa J Beamer /
Abstract: Serine hydroxymethyltransferase (SHMT) is a conserved enzyme in folate-mediated one-carbon metabolism, where it contributes to nucleotide biosynthesis, methylation capacity, and cellular stress ...Serine hydroxymethyltransferase (SHMT) is a conserved enzyme in folate-mediated one-carbon metabolism, where it contributes to nucleotide biosynthesis, methylation capacity, and cellular stress responses. Amino acid polymorphisms of soybean SHMT8 are known to affect the resistance of soybean to its primary pathogen, the soybean cyst nematode (SCN). A set of SHMT8 variants from ethyl methanesulfonate (EMS)-mutagenized soybean populations has been identified with varying resistance phenotypes, but their biochemical consequences remain poorly understood. Here, we use biochemical and structural studies to assess the impacts of the A149T variant on soybean SHMT8. Despite the conservative nature of the substitution, A149T reduces folate binding, pyridoxal-5'-phosphate-dependent catalysis, and thermal stability. High-resolution crystal structures (1.9-2.3 Å resolution) reveal only very minor structural changes. However, while the usual tetrameric assembly of the enzyme is retained at the high protein concentration in crystals, multiple other methods including a 2.9 Å cryo-electron microscopy (cryo-EM) structure show that the A149T variant is predominantly a dimer. Significant structural changes in the dimer are consistent with the observed biochemical impacts of the variant and help explain the well-known reduction in activity associated with dimerization of SHMT in other systems. We also find destabilization of the tetrameric assembly in other SHMT8 variants associated with changes in SCN resistance, suggesting that weakened oligomerization may be a common consequence of such mutations. Together, these results highlight quaternary structure as a critical determinant of SHMT8 activity and stability and suggest a potential mechanistic link between enzyme biochemistry and soybean defense.
#1: Journal: Acta Crystallogr D Struct Biol / Year: 2019
Title: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix.
Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty ...Authors: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams /
Abstract: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks.
History
DepositionSep 8, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 8, 2026Provider: repository / Type: Initial release
Revision 2.0Apr 22, 2026Group: Advisory / Atomic model ...Advisory / Atomic model / Database references / Derived calculations / Polymer sequence / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / citation / citation_author / entity / entity_poly / entity_poly_seq / entity_src_gen / pdbx_poly_seq_scheme / pdbx_struct_sheet_hbond / pdbx_unobs_or_zero_occ_atoms / pdbx_unobs_or_zero_occ_residues / struct_conf / struct_mon_prot_cis / struct_ref_seq / struct_ref_seq_dif / struct_sheet_range
Item: _atom_site.label_seq_id / _atom_site_anisotrop.pdbx_label_seq_id ..._atom_site.label_seq_id / _atom_site_anisotrop.pdbx_label_seq_id / _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _entity.formula_weight / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_src_gen.pdbx_end_seq_num / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _pdbx_unobs_or_zero_occ_atoms.label_seq_id / _struct_conf.beg_label_seq_id / _struct_conf.end_label_seq_id / _struct_mon_prot_cis.label_seq_id / _struct_mon_prot_cis.pdbx_label_seq_id_2 / _struct_ref_seq.seq_align_beg / _struct_ref_seq.seq_align_end / _struct_sheet_range.beg_label_seq_id / _struct_sheet_range.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Serine hydroxymethyltransferase
B: Serine hydroxymethyltransferase
C: Serine hydroxymethyltransferase
D: Serine hydroxymethyltransferase
E: Serine hydroxymethyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)275,69210
Polymers274,1615
Non-polymers1,5315
Water10,953608
1
A: Serine hydroxymethyltransferase
B: Serine hydroxymethyltransferase
C: Serine hydroxymethyltransferase
D: Serine hydroxymethyltransferase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)220,5538
Polymers219,3284
Non-polymers1,2254
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)175.306, 175.306, 186.332
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121
Space group name HallP312"
Symmetry operation#1: x,y,z
#2: -y,x-y,z+1/3
#3: -x+y,-x,z+2/3
#4: x-y,-y,-z+2/3
#5: -x,-x+y,-z+1/3
#6: y,x,-z
DetailsThe ASU contains 6 chains (A,B,C,D,E,F), where the chains A, B, C and D forms the tetramer in the ASU while chains E and F forms tetramers with their symmetry operators, out of the ASU. This mutant datasets show sever tNCS and always have very poor density for chain F. Hence we have left it out and did not build in the chain.

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Components

#1: Protein
Serine hydroxymethyltransferase


Mass: 54832.113 Da / Num. of mol.: 5 / Mutation: A149T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Glycine max (soybean) / Gene: SHMT / Production host: Escherichia coli (E. coli)
References: UniProt: K4FW35, glycine hydroxymethyltransferase
#2: Chemical
ChemComp-PLG / N-GLYCINE-[3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YL-METHANE] / N-PYRIDOXYL-GLYCINE-5-MONOPHOSPHATE


Mass: 306.209 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C10H15N2O7P / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 608 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationN

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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: 3.05 Å3/Da / Density % sol: 59.63 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 0.1 M Ammonium tartrate dibasic pH 7.0 12% w/v Polyethylene glycol 3,350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 1 Å
DetectorType: RDI CMOS_8M / Detector: CMOS / Date: Oct 17, 2024
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.25→48.86 Å / Num. obs: 156345 / % possible obs: 100 % / Redundancy: 20.3 % / Biso Wilson estimate: 30.05 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.175 / Rpim(I) all: 0.04 / Rrim(I) all: 0.179 / Net I/σ(I): 20.8
Reflection shellResolution: 2.25→2.33 Å / Redundancy: 17.5 % / Rmerge(I) obs: 1.379 / Mean I/σ(I) obs: 3 / Num. unique obs: 7641 / CC1/2: 0.868 / Rpim(I) all: 0.341 / Rrim(I) all: 1.421 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX1.21.2_5419refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.25→48.86 Å / SU ML: 0.3412 / Cross valid method: FREE R-VALUE / σ(F): 1.05 / Phase error: 34.9446
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.3109 7645 4.93 %
Rwork0.2648 147551 -
obs0.2671 155196 99.28 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 37.75 Å2
Refinement stepCycle: LAST / Resolution: 2.25→48.86 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17182 0 100 608 17890
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.007117672
X-RAY DIFFRACTIONf_angle_d0.862424018
X-RAY DIFFRACTIONf_chiral_restr0.0482633
X-RAY DIFFRACTIONf_plane_restr0.00683145
X-RAY DIFFRACTIONf_dihedral_angle_d14.84036154
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.25-2.280.39392440.37694877X-RAY DIFFRACTION99.55
2.28-2.30.36792870.29694871X-RAY DIFFRACTION99.69
2.3-2.330.36732590.29694885X-RAY DIFFRACTION99.81
2.33-2.360.3532650.28654899X-RAY DIFFRACTION99.85
2.36-2.390.35772690.2764934X-RAY DIFFRACTION99.83
2.39-2.420.32872530.27764842X-RAY DIFFRACTION99.67
2.42-2.460.34492430.27754913X-RAY DIFFRACTION99.58
2.46-2.50.31592690.27784896X-RAY DIFFRACTION99.85
2.5-2.530.33462670.27974880X-RAY DIFFRACTION99.71
2.53-2.580.3582630.27824937X-RAY DIFFRACTION99.67
2.58-2.620.3772480.28194887X-RAY DIFFRACTION99.21
2.62-2.670.35412080.28114940X-RAY DIFFRACTION99.61
2.67-2.720.34812410.2764904X-RAY DIFFRACTION99.44
2.72-2.770.30622540.26794896X-RAY DIFFRACTION99.59
2.77-2.830.33182340.27264933X-RAY DIFFRACTION99.42
2.83-2.90.3562580.27644882X-RAY DIFFRACTION99.09
2.9-2.970.35342510.28224910X-RAY DIFFRACTION99.04
2.97-3.050.32422320.27574853X-RAY DIFFRACTION98.45
3.05-3.140.35922210.27954935X-RAY DIFFRACTION99.02
3.14-3.240.32772820.28054909X-RAY DIFFRACTION99.14
3.24-3.360.34312710.27314873X-RAY DIFFRACTION98.9
3.36-3.50.30772330.26944888X-RAY DIFFRACTION98.54
3.5-3.650.27242640.25614882X-RAY DIFFRACTION98.36
3.65-3.850.26482460.23914851X-RAY DIFFRACTION98.28
3.85-4.090.2562630.23624917X-RAY DIFFRACTION98.69
4.09-4.40.25122520.22694957X-RAY DIFFRACTION99.07
4.4-4.850.27272470.22434974X-RAY DIFFRACTION99.13
4.85-5.550.28072750.23754981X-RAY DIFFRACTION99.55
5.55-6.980.29152760.26355060X-RAY DIFFRACTION99.85
6.99-48.860.33992700.29235185X-RAY DIFFRACTION99.09
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)
10.305635411658-0.04595568281810.02668009923340.2651240016670.03055228528190.00451786485078-0.060578060964-0.05960744256960.1105968324770.0162089496149-0.0522490443077-0.008208409870530.05464588545920.000303519652245-0.1037449127450.168104309362-0.03807012212870.05255144288990.213899282050.02616623679830.0929046720662-1.13225328244-81.047090414833.4782597703
20.2791512239890.0692550392256-0.03167067202230.108214493720.02016597452290.0415479757268-0.102328240163-0.08801172862120.2555841070910.06145258733250.06622233816070.1458393480050.0617017609514-0.048516229608-0.01189828011520.19832175307-0.08054494510080.006844017442220.2689494581950.04569103833680.150670761931-6.7641953993-75.655111756234.9813585241
30.0570433723541-0.0542550732778-0.009429395554960.04487413644440.01335902294720.00456790593752-0.1534652125160.07164946588040.22278763974-0.1060808106160.137263138402-0.00554531452770.0888379407031-0.07110844915010.02577345037540.31474974402-0.154669833143-0.03331854736260.3271227002360.1489461990610.194971518793-10.47171429-65.074316590714.7562883011
40.0270400262813-0.0547958601867-0.01694244464010.08474429502450.03088422988010.0111910457758-0.06226309679550.0008997916917120.0602826647396-0.08401428389830.0584574545815-0.1092501278940.06969312615010.03462195748250.08790111880770.288124644421-0.06464118271540.02414624106920.267196001080.2105175075380.3004462079320.920051059622-59.734507252911.7863996113
50.09837468440030.0464308443746-0.0274353924860.0435720712307-0.02594410011250.0176984287669-0.0220205629755-0.014142316910.262224560051-0.0290573358644-0.0758973322657-0.129148738878-0.0430940724293-0.0339712537643-0.007902489796190.213917850493-0.04876151103950.02599690763280.2753113344890.03294748373390.27355048711414.8834956007-73.223367974128.1376163427
60.01594259663150.002936199295054.06126556086E-50.03175434806650.01901621431130.003601640635350.000450094687710.0559429170693-0.165027686423-0.0321520828553-0.0515291713773-0.02230765986730.087021134810.007323476611320.00300059706310.187645486456-0.01123197887490.08567216259160.1931616229330.01284952790680.1895355668412.2783567236-97.248996681821.9460226914
70.041397763766-0.05189909554410.06118037395330.0726460678673-0.07832448552930.09458610757580.00415695692967-0.0505704815688-0.05546666914220.0595771995071-0.000431791577906-0.207781653907-0.0340862763735-0.0569255588724-0.01401858840020.14259959318-0.01718612612240.05309163499070.2405537784920.04432587037830.45202785747216.1732932575-108.79280919131.504312314
80.110831140238-0.01339302249030.08883536721610.10371902120.01822714135440.0882604760966-0.0629810974220.152968196377-0.0987786163305-0.115033534072-0.0482564803893-0.2075238600530.143526376648-0.0552094608938-0.170279692850.227025130799-0.01825011219510.120945183290.262292992127-0.01658970963770.27498491269420.5387531516-99.658508565418.466669948
90.0482494165158-0.0160312531795-0.04285377980390.1078897579250.1084621319160.140035039077-0.01616960140980.0459954062592-0.0700888119748-0.122138019268-0.104246846215-0.1633996869030.09466715416920.0362387111408-0.155358295050.157216007279-0.01080695724160.1143066540510.269516242710.08769067416580.22940943419922.894664997-87.231914866323.3421015274
100.0256671564446-0.01297534208130.01458068236060.00693196304795-0.00710416263960.0122114329178-0.0902895281901-0.000993939869271-0.02613381307660.0567019680645-0.0251076612261-0.1498094154880.1170699492230.0271553527036-8.75550405251E-50.26236678734-0.0186263282122-0.0009528744258660.2957498745620.1013499200130.29739679471831.9956556975-96.15991594842.088071798
110.0139582860138-0.008071064490.004864648133540.00615510602793-0.0004028105827240.001388693908680.03218301709680.006409469450290.06921077943940.0762458946806-0.0382770695985-0.1061547106360.0398616593480.06087969994671.95831618254E-50.272910112616-0.0412356578512-0.06510332086820.3884393229070.1530422620210.30165786114936.4837953985-92.9303516852.7947964828
120.002382497372850.002530818832150.00510128274830.002217312680790.0005642211125910.001992402065950.013281486368-0.03450798525660.0247310836898-0.0133591242631-0.0233346092078-0.06157044445890.0007994858895130.00894691323545-1.65273665187E-50.247639246368-0.0654801785807-0.08246626322080.3981143665990.04516326160030.32409568498134.9283775929-75.279186791943.9862514239
130.2945151967780.09254214693760.05827910045270.167192727734-0.03314141664770.215243915579-0.004716962323750.0133199371884-0.0221902549201-0.150403177580.03849287997490.2070973585770.0118522894345-0.03032897340380.00141027011570.29125344448-0.0493980182140.02629855457940.254597556864-0.01874643113420.15822642796-24.833503039-123.14451602623.7358149973
140.03302629869840.0117924221460.007723447542110.284370087938-0.0741364980450.05153360581030.0551996649540.06943178135090.00443954329099-0.139555089121-0.004286303355340.3522225816580.01050380055580.01531784117330.03331969058050.247169733058-0.03419083589580.03657341019750.240534142393-0.02097280894630.280019144025-32.9055133984-123.02719008624.3394839901
150.0107173869412-0.0231838923216-0.0007609889627720.125719009880.02235399014340.01882169067520.0235618299672-0.241612336115-0.170989332740.002436928598010.03560644632460.268199936069-0.0334042757240.08393839744460.007404045307960.182098397672-0.06296769020210.09222085241040.2435611160240.01987945171960.378452103515-44.8664064895-126.13061417241.0917243777
160.121008899467-0.1565796159960.07266849040420.368889975154-0.09082849621140.08812181675740.0166736611973-0.0612657756653-0.1535109596210.0102535214967-0.0368478153756-0.09846834356520.03230835409660.0263856205524.68496577186E-50.209962320383-0.04578051065570.01483764050860.2145197125150.01467565921520.155992336233-8.25662686477-133.02757163734.0613555065
170.06599336967210.0331938228218-0.006930449955060.0314703805223-0.04931316441660.09259626791550.0247953621967-0.150964307223-0.1501319073070.0982844091457-0.076620919047-0.112458088056-0.02919973465530.07183203482193.85103449882E-50.254306826447-0.03145212875390.0077880221660.2692370091250.03557411596890.201575171777-8.06094360488-137.55639501639.5306273281
180.01931317925190.002257980669790.01704119821320.0402921919-0.019183794770.0224686074713-0.004702441031330.108633334584-0.270721212827-0.244210579708-0.0899851941513-0.1138540253140.1254529523940.0246935270281.74532093988E-50.3453217282240.01088344941250.09984314335150.275220093496-0.0581371521370.4148794176042.08007384736-150.43439936317.5212314625
190.052387466020.03010231340050.03164313395880.02963774456610.003219837946360.0156128926635-0.093083851762-0.0505002153607-0.174486164173-0.01589218096240.00469713363126-0.1205459375610.07114356665140.050297886527-0.07302200930680.0168841780236-0.1550712020650.08415935405960.1477168746080.05850797326650.8483214528316.0467034751-26.156766242129.3960137638
200.06976841684460.03117899020580.008625174584760.0673041820270.03062310425140.0329825686872-0.09353862547970.06301860612710.212003291394-0.01485136894820.06314468244470.2266251019220.0360572259971-0.0400598314784-0.05453426131490.0292287765829-0.140431913415-0.1013070677520.2208455922030.002348334692811.12386106465-11.5779981023-13.564631610425.9512996342
210.0997478073460.07230058277130.03787913389840.165010858513-0.0002602045852140.0353887665143-0.2041104536790.0542673195224-0.0601860210868-0.1704894412440.0717995105955-0.01953846661660.00382886835857-0.0913768245752-0.1137870350520.0572772370257-0.09764608885430.04518880046130.183352990243-0.0111182164460.765489313524-5.75013205874-27.202428327330.6500109431
220.01181274850570.0217062715758-0.01561928553610.0333466634943-0.01545121356680.003839388560630.0158129928684-0.142804251174-0.09273465721650.04947075142920.00343810220257-0.09531361069750.00389723517853-0.122462321483-0.02576523477110.0793548648254-0.03855550524810.1218738128280.33240087040.12370373240.67466609441-4.81521281981-40.026033210547.8575066314
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid -1 through 257 )AA-1 - 2571 - 259
22chain 'A' and (resid 258 through 356 )AA258 - 356260 - 358
33chain 'A' and (resid 357 through 426 )AA357 - 426359 - 423
44chain 'A' and (resid 427 through 470 )AA427 - 470424 - 467
55chain 'B' and (resid -1 through 90 )BC-1 - 901 - 92
66chain 'B' and (resid 91 through 131 )BC91 - 13193 - 133
77chain 'B' and (resid 132 through 180 )BC132 - 180134 - 182
88chain 'B' and (resid 181 through 274 )BC181 - 274183 - 274
99chain 'B' and (resid 275 through 331 )BC275 - 331275 - 331
1010chain 'B' and (resid 332 through 401 )BC332 - 401332 - 399
1111chain 'B' and (resid 402 through 440 )BC402 - 440400 - 438
1212chain 'B' and (resid 441 through 469 )BC441 - 469439 - 467
1313chain 'C' and (resid -1 through 241 )CE-1 - 2411 - 243
1414chain 'C' and (resid 242 through 367 )CE242 - 367244 - 363
1515chain 'C' and (resid 368 through 470 )CE368 - 470364 - 466
1616chain 'D' and (resid -1 through 230 )DG-1 - 2301 - 232
1717chain 'D' and (resid 231 through 332 )DG231 - 332233 - 324
1818chain 'D' and (resid 333 through 470 )DG333 - 470325 - 462
1919chain 'E' and (resid -1 through 89 )EI-1 - 891 - 91
2020chain 'E' and (resid 90 through 230 )EI90 - 23092 - 232
2121chain 'E' and (resid 231 through 401 )EI231 - 401233 - 380
2222chain 'E' and (resid 402 through 470 )EI402 - 470381 - 449

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