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- PDB-2aq1: Crystal structure of T-cell receptor V beta domain variant comple... -

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Basic information

Entry
Database: PDB / ID: 2aq1
TitleCrystal structure of T-cell receptor V beta domain variant complexed with superantigen SEC3 mutant
Components
  • Enterotoxin type C-3
  • T-cell receptor beta chain V
KeywordsIMMUNE SYSTEM / T-CELL RECEPTOR / STAPHYLOCOCCAL ENTEROTOXIN C3 / SUPERANTIGEN / COMPLEX (TOXIN-RECEPTOR)
Function / homology
Function and homology information


T cell receptor complex / toxin activity / adaptive immune response / cell surface receptor signaling pathway / extracellular region / metal ion binding / plasma membrane
Similarity search - Function
Staphylococcal enterotoxin/Streptococcal pyrogenic exotoxin signature 1. / Staphylococcal/streptococcal toxin, bacterial / Staphylococcal/Streptococcal toxin, OB-fold / Staphylococcal/Streptococcal toxin, OB-fold domain / Staphylococcal/Streptococcal toxin, beta-grasp domain / Staphylococcal/Streptococcal toxin, beta-grasp domain / Staphylococcal enterotoxin/Streptococcal pyrogenic exotoxin, conserved site / Staphyloccocal enterotoxin/Streptococcal pyrogenic exotoxin signature 2. / Superantigen, staphylococcal/streptococcal toxin, bacterial / Ubiquitin-like (UB roll) - #120 ...Staphylococcal enterotoxin/Streptococcal pyrogenic exotoxin signature 1. / Staphylococcal/streptococcal toxin, bacterial / Staphylococcal/Streptococcal toxin, OB-fold / Staphylococcal/Streptococcal toxin, OB-fold domain / Staphylococcal/Streptococcal toxin, beta-grasp domain / Staphylococcal/Streptococcal toxin, beta-grasp domain / Staphylococcal enterotoxin/Streptococcal pyrogenic exotoxin, conserved site / Staphyloccocal enterotoxin/Streptococcal pyrogenic exotoxin signature 2. / Superantigen, staphylococcal/streptococcal toxin, bacterial / Ubiquitin-like (UB roll) - #120 / Superantigen toxin, C-terminal / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #110 / Enterotoxin / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Ubiquitin-like (UB roll) / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Roll / Immunoglobulin-like fold / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
T-cell receptor beta chain V region C5 / Enterotoxin type C-3
Similarity search - Component
Biological speciesMus musculus (house mouse)
Staphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsCho, S. / Swaminathan, C.P. / Yang, J. / Kerzic, M.C. / Guan, R. / Kieke, M.C. / Kranz, D.M. / Mariuzza, R.A. / Sundberg, E.J.
CitationJournal: Structure / Year: 2005
Title: Structural basis of affinity maturation and intramolecular cooperativity in a protein-protein interaction.
Authors: Cho, S. / Swaminathan, C.P. / Yang, J. / Kerzic, M.C. / Guan, R. / Kieke, M.C. / Kranz, D.M. / Mariuzza, R.A. / Sundberg, E.J.
History
DepositionAug 17, 2005Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 21, 2006Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software
Remark 600HETEROGEN PORTIONS OF THE DENSITY WAS COMPRISED OF PEG BUT THE COMPLETE MOLECULE COULD NOT BE TRACED.
Remark 999SEQUENCE NO SUITABLE SEQUENCE DATABASE REFERENCE WAS AVAILABLE FOR THE CHAINS A, C, E and G AT THE ...SEQUENCE NO SUITABLE SEQUENCE DATABASE REFERENCE WAS AVAILABLE FOR THE CHAINS A, C, E and G AT THE TIME OF PROCESSING THIS ENTRY. THE FIVE SEC3 WILD TYPE RESIDUES AT POSITIONS 102-106 (GKVTG) IN CHAINS B, D, F AND H ARE REPLACED BY THREE RESIDUES (WWH).

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: T-cell receptor beta chain V
B: Enterotoxin type C-3
C: T-cell receptor beta chain V
D: Enterotoxin type C-3
E: T-cell receptor beta chain V
F: Enterotoxin type C-3
G: T-cell receptor beta chain V
H: Enterotoxin type C-3


Theoretical massNumber of molelcules
Total (without water)159,4588
Polymers159,4588
Non-polymers00
Water10,521584
1
A: T-cell receptor beta chain V
B: Enterotoxin type C-3


Theoretical massNumber of molelcules
Total (without water)39,8642
Polymers39,8642
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: T-cell receptor beta chain V
D: Enterotoxin type C-3


Theoretical massNumber of molelcules
Total (without water)39,8642
Polymers39,8642
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: T-cell receptor beta chain V
F: Enterotoxin type C-3


Theoretical massNumber of molelcules
Total (without water)39,8642
Polymers39,8642
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
G: T-cell receptor beta chain V
H: Enterotoxin type C-3


Theoretical massNumber of molelcules
Total (without water)39,8642
Polymers39,8642
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)63.200, 70.186, 98.403
Angle α, β, γ (deg.)74.79, 75.05, 88.54
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
T-cell receptor beta chain V


Mass: 12174.466 Da / Num. of mol.: 4 / Mutation: G17E,A52V,S54N,K66E,E80V,L81S,T87S,G96V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pT7-7 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P04213
#2: Protein
Enterotoxin type C-3 / SEC3


Mass: 27690.033 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: entC3 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A0L5
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 584 / 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: 2.8 Å3/Da / Density % sol: 55.2 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7
Details: 20% PEG 3350, 0.2M tri-ammonium citrate, 0.3% dioxane, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X25 / Wavelength: 1.0722 Å
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0722 Å / Relative weight: 1
ReflectionRedundancy: 2.5 % / Number: 81743 / Rmerge(I) obs: 0.034 / Χ2: 1.48 / D res high: 2.1 Å / D res low: 40 Å / % possible obs: 89.8
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
4.524097.410.0262.0732.6
3.594.529710.0241.7542.6
3.143.5997.610.0311.7832.6
2.853.1497.510.0441.5562.6
2.652.8597.310.0651.3882.6
2.492.6596.710.0931.2742.6
2.372.4992.310.1231.2022.4
2.262.3782.610.1431.1222.3
2.182.2673.810.1721.1072.3
2.12.186610.2221.0542.2
ReflectionResolution: 2.1→40 Å / Num. obs: 81743 / % possible obs: 89.8 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 4 / Redundancy: 2.5 % / Rmerge(I) obs: 0.034 / Χ2: 1.48
Reflection shellResolution: 2.1→2.18 Å / % possible obs: 66 % / Redundancy: 2.2 % / Rmerge(I) obs: 0.222 / Num. measured obs: 5983 / Χ2: 1.054 / % possible all: 79.9

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMAC5.2.0005refinement
PDB_EXTRACT1.7data extraction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→35 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.938 / SU B: 5.553 / SU ML: 0.147 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.227 / ESU R Free: 0.197 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.243 4468 5.1 %RANDOM
Rwork0.185 ---
all0.188 91912 --
obs0.187 81743 95.98 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 45.303 Å2
Baniso -1Baniso -2Baniso -3
1-2.36 Å2-0.62 Å20.88 Å2
2---0.95 Å20.35 Å2
3----2.01 Å2
Refinement stepCycle: LAST / Resolution: 2.1→35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11089 0 0 584 11673
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0240.02211442
X-RAY DIFFRACTIONr_angle_refined_deg2.0161.95315426
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.84151364
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.94925.186565
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.68151967
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.41532
X-RAY DIFFRACTIONr_chiral_restr0.1450.21621
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.028672
X-RAY DIFFRACTIONr_nbd_refined0.2440.25002
X-RAY DIFFRACTIONr_nbtor_refined0.3110.27554
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1820.2835
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1780.255
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2120.29
X-RAY DIFFRACTIONr_mcbond_it1.4011.57070
X-RAY DIFFRACTIONr_mcangle_it2.322211035
X-RAY DIFFRACTIONr_scbond_it3.12735152
X-RAY DIFFRACTIONr_scangle_it4.454.54391
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.337 291 -
Rwork0.249 5084 -
all-5375 -
obs--79.96 %

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