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- PDB-1h8o: Three-dimensional structure of anti-ampicillin single chain Fv fr... -

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Basic information

Entry
Database: PDB / ID: 1h8o
TitleThree-dimensional structure of anti-ampicillin single chain Fv fragment.
ComponentsMUTANT AL2 6E7P9G
KeywordsANTIBODY / FV FRAGMENT / ANTI-AMPICILLIN
Function / homologyImmunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Function and homology information
Biological speciesMUS MUSCULUS (house mouse)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.75 Å
AuthorsBurmester, J. / Spinelli, S. / Pugliese, L. / Krebber, A. / Honegger, A. / Jung, S. / Schimmele, B. / Cambillau, C. / Pluckthun, A.
CitationJournal: J.Mol.Biol. / Year: 2001
Title: Selection, Characterization and X-Ray Structure of Anti-Ampicillin Single-Chain Fv Fragments from Phage-Displayed Murine Antibody Libraries
Authors: Burmester, J. / Spinelli, S. / Pugliese, L. / Krebber, A. / Honegger, A. / Jung, S. / Schimmele, B. / Cambillau, C. / Pluckthun, A.
History
DepositionFeb 14, 2001Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 2, 2001Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MUTANT AL2 6E7P9G
B: MUTANT AL2 6E7P9G
hetero molecules


Theoretical massNumber of molelcules
Total (without water)54,2064
Polymers54,0132
Non-polymers1922
Water1,982110
1
A: MUTANT AL2 6E7P9G
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,1993
Polymers27,0071
Non-polymers1922
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
2
B: MUTANT AL2 6E7P9G


Theoretical massNumber of molelcules
Total (without water)27,0071
Polymers27,0071
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
Length a, b, c (Å)59.690, 89.850, 97.260
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Antibody MUTANT AL2 6E7P9G


Mass: 27006.734 Da / Num. of mol.: 2 / Fragment: FV FRAGMENT
Source method: isolated from a genetically manipulated source
Details: SINGLE CHAIN FV ANTIBODY IN WHICH THE VL AND VH FRAGMENTS ARE JOINED BY A GGGGSGGGGSGGGGSGGGGS LINKER
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PAK3000 / Production host: ESCHERICHIA COLI K-12 (bacteria) / Variant (production host): RV308
#2: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 110 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.4 Å3/Da / Density % sol: 49.05 %
Crystal growpH: 5 / Details: pH 5.00
Crystal grow
*PLUS
Temperature: 20 ℃ / Method: vapor diffusion, hanging drop / pH: 5
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
13 mg/mlprotein1drop
226 %(w/v)PEG2000 MME1reservoir
3200 mMammonium sulfate1reservoir
4100 mMsodium acetate1reservoirpH5.0

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.54178
DetectorDetector: IMAGE PLATE
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54178 Å / Relative weight: 1
ReflectionResolution: 2.75→12 Å / Num. obs: 14189 / % possible obs: 98.8 % / Redundancy: 3.5 % / Rsym value: 0.11 / Net I/σ(I): 8
Reflection shellResolution: 2.75→2.8 Å / Redundancy: 3 % / Mean I/σ(I) obs: 2 / Rsym value: 0.4 / % possible all: 90.7
Reflection
*PLUS
Num. measured all: 81293 / Rmerge(I) obs: 0.11
Reflection shell
*PLUS
% possible obs: 90.7 % / Rmerge(I) obs: 0.4

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Processing

Software
NameVersionClassification
CNS1refinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.75→11.94 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 1342809.82 / Cross valid method: THROUGHOUT / σ(F): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.258 1070 7.9 %RANDOM
Rwork0.178 ---
obs0.178 13604 97.5 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 31.0488 Å2 / ksol: 0.31283 e/Å3
Refine analyzeLuzzati coordinate error obs: 0.27 Å
Refinement stepCycle: LAST / Resolution: 2.75→11.94 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3400 0 10 110 3520
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.011
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg1.6
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d26.7
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d0.96
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_scangle_it
LS refinement shellResolution: 2.75→2.92 Å / Rfactor Rfree error: 0.031 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.404 175 8 %
Rwork0.314 2014 -
obs--95.6 %
Xplor fileSerial no: 1 / Param file: PROTEIN_REP.PARAM / Topol file: PROTEIN.TOP
Software
*PLUS
Name: CNS / Version: 1 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg26.7
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg0.96

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