3O2V

Crystal structure of 1E9 PheL89Ser/LeuH47Trp/MetH100bPhe, an engineered Diels-Alderase Fab with modified specificity and catalytic activity

PDB DOI: https://doi.org/10.2210/pdb3O2V/pdb

Classification: IMMUNE SYSTEM
Organism(s): Mus musculus, Homo sapiens
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2010-07-22 Released: 2011-07-20
Deposition Author(s): Verdino, P., Wilson, I.A.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.219
R-Value Work: 0.192
R-Value Observed: 0.194

wwPDB Validation 3D Report Full Report

This is version 1.1 of the entry. See complete history.

Literature

Crystal structure of 1E9 PheL89Ser/LeuH47Trp/MetH100bPhe, an engineered Diels-Alderase Fab with modified specificity and catalytic activity

Verdino, P., Aldag, C., Jonsson, S., Hilvert, D., Wilson, I.A.

To be published.

Macromolecule Content

Total Structure Weight: 51.55 kDa
Atom Count: 3,765
Modelled Residue Count: 437
Deposited Residue Count: 446
Unique protein chains: 2

Macromolecules

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(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Chimeric antibody Fab 1E9, light chain	A [auth L]	219	Mus musculus, Homo sapiens This entity is chimeric	Mutation(s): 0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 2
Molecule	Chains	Sequence Length	Organism	Details	Image
Chimeric antibody Fab 1E9, heavy chain	B [auth H]	227	Mus musculus, Homo sapiens This entity is chimeric	Mutation(s): 0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 3 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
FLC Query on FLC Download Ideal Coordinates CCD File SDF format, chain I [auth L] SDF format, chain U [auth H] SDF format, chain V [auth H] MOL2 format, chain I [auth L] MOL2 format, chain U [auth H] MOL2 format, chain V [auth H]	I [auth L], U [auth H], V [auth H]	CITRATE ANION C₆ H₅ O₇ KRKNYBCHXYNGOX-UHFFFAOYSA-K		Interactions Focus chain I [auth L] Focus chain U [auth H] Focus chain V [auth H] Interactions & Density Focus chain I [auth L] Focus chain U [auth H] Focus chain V [auth H]
TRS Query on TRS Download Ideal Coordinates CCD File SDF format, chain D [auth L] SDF format, chain E [auth L] SDF format, chain F [auth L] SDF format, chain G [auth L] SDF format, chain H [auth L] SDF format, chain R [auth H] SDF format, chain S [auth H] SDF format, chain T [auth H] SDF format, chain C [auth L] SDF format, chain Q [auth H] MOL2 format, chain D [auth L] MOL2 format, chain E [auth L] MOL2 format, chain F [auth L] MOL2 format, chain G [auth L] MOL2 format, chain H [auth L] MOL2 format, chain R [auth H] MOL2 format, chain S [auth H] MOL2 format, chain T [auth H] MOL2 format, chain C [auth L] MOL2 format, chain Q [auth H]	C [auth L] D [auth L] E [auth L] F [auth L] G [auth L] C [auth L], D [auth L], E [auth L], F [auth L], G [auth L], H [auth L], Q [auth H], R [auth H], S [auth H], T [auth H]	2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL C₄ H₁₂ N O₃ LENZDBCJOHFCAS-UHFFFAOYSA-O		Interactions Focus chain C [auth L] Focus chain D [auth L] Focus chain E [auth L] Focus chain F [auth L] Focus chain G [auth L] Focus chain H [auth L] Focus chain Q [auth H] Focus chain R [auth H] Focus chain S [auth H] Focus chain T [auth H] Interactions & Density Focus chain C [auth L] Focus chain D [auth L] Focus chain E [auth L] Focus chain F [auth L] Focus chain G [auth L] Focus chain H [auth L] Focus chain Q [auth H] Focus chain R [auth H] Focus chain S [auth H] Focus chain T [auth H]
SO4 Query on SO4 Download Ideal Coordinates CCD File SDF format, chain AA [auth H] SDF format, chain BA [auth H] SDF format, chain J [auth L] SDF format, chain K [auth L] SDF format, chain M [auth L] SDF format, chain N [auth L] SDF format, chain P [auth L] SDF format, chain X [auth H] SDF format, chain Y [auth H] SDF format, chain Z [auth H] SDF format, chain L SDF format, chain O [auth L] SDF format, chain W [auth H] MOL2 format, chain AA [auth H] MOL2 format, chain BA [auth H] MOL2 format, chain J [auth L] MOL2 format, chain K [auth L] MOL2 format, chain M [auth L] MOL2 format, chain N [auth L] MOL2 format, chain P [auth L] MOL2 format, chain X [auth H] MOL2 format, chain Y [auth H] MOL2 format, chain Z [auth H] MOL2 format, chain L MOL2 format, chain O [auth L] MOL2 format, chain W [auth H]	AA [auth H] BA [auth H] J [auth L] K [auth L] L AA [auth H], BA [auth H], J [auth L], K [auth L], L, M [auth L], N [auth L], O [auth L], P [auth L], W [auth H], X [auth H], Y [auth H], Z [auth H]	SULFATE ION O₄ S QAOWNCQODCNURD-UHFFFAOYSA-L		Interactions Focus chain AA [auth H] Focus chain BA [auth H] Focus chain J [auth L] Focus chain K [auth L] Focus chain L Focus chain M [auth L] Focus chain N [auth L] Focus chain O [auth L] Focus chain P [auth L] Focus chain W [auth H] Focus chain X [auth H] Focus chain Y [auth H] Focus chain Z [auth H] Interactions & Density Focus chain AA [auth H] Focus chain BA [auth H] Focus chain J [auth L] Focus chain K [auth L] Focus chain L Focus chain M [auth L] Focus chain N [auth L] Focus chain O [auth L] Focus chain P [auth L] Focus chain W [auth H] Focus chain X [auth H] Focus chain Y [auth H] Focus chain Z [auth H]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.30 Å
R-Value Free: 0.219
R-Value Work: 0.192
R-Value Observed: 0.194
Space Group: P 3₁ 2 1

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 128.73	α = 90
b = 128.73	β = 90
c = 92.342	γ = 120

Software Package:

Software Name	Purpose
BOS	data collection
PHASER	phasing
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2011-07-20

Deposition Author(s):

Verdino, P.

Wilson, I.A.

Revision History (Full details and data files)

Version 1.0: 2011-07-20
Type: Initial release
Version 1.1: 2023-09-06
Changes: Data collection, Database references, Derived calculations, Refinement description