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- PDB-1bwm: A SINGLE-CHAIN T CELL RECEPTOR -

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Basic information

Entry
Database: PDB / ID: 1bwm
TitleA SINGLE-CHAIN T CELL RECEPTOR
ComponentsPROTEIN (ALPHA-BETA T CELL RECEPTOR (TCR) (D10))
KeywordsIMMUNE SYSTEM / IMMUNOGLOBULIN / IMMUNORECEPTOR
Function / homology
Function and homology information


Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
MethodSOLUTION NMR / molecular dynamics
AuthorsHare, B.J. / Wyss, D.F. / Reinherz, E.L. / Wagner, G.
Citation
Journal: Nat.Struct.Biol. / Year: 1999
Title: Structure, specificity and CDR mobility of a class II restricted single-chain T-cell receptor.
Authors: Hare, B.J. / Wyss, D.F. / Osburne, M.S. / Kern, P.S. / Reinherz, E.L. / Wagner, G.
#1: Journal: To be Published
Title: Application of Automated NOE Assignment to Three-dimensional Structure Refinement of a 28 kD Single-chain T Cell Receptor
Authors: Hare, B.J. / Wagner, G.
History
DepositionSep 23, 1998Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 22, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (ALPHA-BETA T CELL RECEPTOR (TCR) (D10))


Theoretical massNumber of molelcules
Total (without water)26,9711
Polymers26,9711
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)15 / 80NO NOE DISTANCE VIOLATION GREATER THAN 0.5 A, NO DIHEDRAL VIOLATION GREATER THAN 5 DEGREES
RepresentativeModel #7

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Components

#1: Protein PROTEIN (ALPHA-BETA T CELL RECEPTOR (TCR) (D10))


Mass: 26970.664 Da / Num. of mol.: 1 / Fragment: VARIABLE DOMAINS FROM ALPHA AND BETA CHAINS / Mutation: C415S
Source method: isolated from a genetically manipulated source
Details: 27-RESIDUE HYDROPHILIC LINKER CONNECTS C TERMINUS OF BETA DOMAIN WITH N TERMINUS OF ALPHA DOMAIN
Source: (gene. exp.) Mus musculus (house mouse) / Description: SYNTHETIC GENE CONNECTS ALPHA AND BETA DOMAINS / Plasmid: PET11A / Species (production host): Escherichia coli
Cellular location (production host): CYTOPLASMIC INCLUSION BODIES
Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3)
References: GenBank: U83243, GenBank: U83242, UniProt: Q5R1G1*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY (1H
12115N
13113C)
141HNCA
151HN(CO)CA
161HA(CA)(CO)NH
171TOCSY-HSQC (15N)
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE RESONANCE NMR SPECTROSCOPY ON UNIFORM 13C, 15N, AND FRACTIONALLY 2H-LABELED SINGLE-CHAIN TCR

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Sample preparation

Sample conditionsIonic strength: 20 mM SODIUM ACETATE / pH: 5.0 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian UNITYPLUSVarianUNITYPLUS5001
Varian UNITYPLUSVarianUNITYPLUS7502

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
X-PLORstructure solution
RefinementMethod: molecular dynamics / Software ordinal: 1
NMR ensembleConformer selection criteria: NO NOE DISTANCE VIOLATION GREATER THAN 0.5 A, NO DIHEDRAL VIOLATION GREATER THAN 5 DEGREES
Conformers calculated total number: 80 / Conformers submitted total number: 15

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