4MTM

Crystal structure of the tail fiber gp53 from Acinetobacter baumannii bacteriophage AP22

PDB DOI: https://doi.org/10.2210/pdb4MTM/pdb

Classification: STRUCTURAL PROTEIN
Organism(s): Acinetobacter phage AP22
Expression System: Escherichia coli
Mutation(s): No

Deposited: 2013-09-19 Released: 2014-10-01
Deposition Author(s): Sycheva, L.V., Shneider, M.M., Leiman, P.G.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 1.37 Å
R-Value Free: 0.132
R-Value Work: 0.099
R-Value Observed: 0.101

wwPDB Validation 3D Report Full Report

This is version 1.3 of the entry. See complete history.

Literature

Crystal Structure of the putative tail fiber protein gp53 from the Acinetobacter baumannii bacteriophage AP22

Sycheva, L.V., Shneider, M.M., Popova, A.V., Ziganshin, R.K., Volozhantsev, N., Miroshnikov, K.A., Leiman, P.G.

(2019) Biorxiv

DOI: https://doi.org/10.1101/518761

Macromolecule Content

Total Structure Weight: 19.07 kDa
Atom Count: 1,241
Modelled Residue Count: 137
Deposited Residue Count: 164
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
Putative tail fiber protein	A	164	Acinetobacter phage AP22	Mutation(s): 0 Gene Names: ORF53
UniProt
Find proteins for I2GUG0 (Acinetobacter phage AP22) Explore I2GUG0 Go to UniProtKB: I2GUG0
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	I2GUG0
Sequence Annotations Expand
Reference Sequence

Small Molecules

Ligands 5 Unique
ID	Chains	Name / Formula / InChI Key	2D Diagram	3D Interactions
GOL Query on GOL Download Ideal Coordinates CCD File SDF format, chain B [auth A] MOL2 format, chain B [auth A]	B [auth A]	GLYCEROL C₃ H₈ O₃ PEDCQBHIVMGVHV-UHFFFAOYSA-N		Interactions Focus chain B [auth A] Interactions & Density Focus chain B [auth A]
SO3 Query on SO3 Download Ideal Coordinates CCD File SDF format, chain BA [auth A] MOL2 format, chain BA [auth A]	BA [auth A]	SULFITE ION O₃ S LSNNMFCWUKXFEE-UHFFFAOYSA-L		Interactions Focus chain BA [auth A] Interactions & Density Focus chain BA [auth A]
BR Query on BR Download Ideal Coordinates CCD File SDF format, chain C [auth A] SDF format, chain D [auth A] SDF format, chain E [auth A] SDF format, chain F [auth A] SDF format, chain G [auth A] SDF format, chain H [auth A] SDF format, chain I [auth A] SDF format, chain J [auth A] SDF format, chain K [auth A] SDF format, chain L [auth A] SDF format, chain M [auth A] SDF format, chain N [auth A] SDF format, chain O [auth A] SDF format, chain P [auth A] SDF format, chain Q [auth A] SDF format, chain R [auth A] SDF format, chain S [auth A] SDF format, chain T [auth A] SDF format, chain U [auth A] SDF format, chain V [auth A] MOL2 format, chain C [auth A] MOL2 format, chain D [auth A] MOL2 format, chain E [auth A] MOL2 format, chain F [auth A] MOL2 format, chain G [auth A] MOL2 format, chain H [auth A] MOL2 format, chain I [auth A] MOL2 format, chain J [auth A] MOL2 format, chain K [auth A] MOL2 format, chain L [auth A] MOL2 format, chain M [auth A] MOL2 format, chain N [auth A] MOL2 format, chain O [auth A] MOL2 format, chain P [auth A] MOL2 format, chain Q [auth A] MOL2 format, chain R [auth A] MOL2 format, chain S [auth A] MOL2 format, chain T [auth A] MOL2 format, chain U [auth A] MOL2 format, chain V [auth A]	C [auth A] D [auth A] E [auth A] F [auth A] G [auth A] C [auth A], D [auth A], E [auth A], F [auth A], G [auth A], H [auth A], I [auth A], J [auth A], K [auth A], L [auth A], M [auth A], N [auth A], O [auth A], P [auth A], Q [auth A], R [auth A], S [auth A], T [auth A], U [auth A], V [auth A]	BROMIDE ION Br CPELXLSAUQHCOX-UHFFFAOYSA-M		Interactions Focus chain C [auth A] Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain G [auth A] Focus chain H [auth A] Focus chain I [auth A] Focus chain J [auth A] Focus chain K [auth A] Focus chain L [auth A] Focus chain M [auth A] Focus chain N [auth A] Focus chain O [auth A] Focus chain P [auth A] Focus chain Q [auth A] Focus chain R [auth A] Focus chain S [auth A] Focus chain T [auth A] Focus chain U [auth A] Focus chain V [auth A] Interactions & Density Focus chain C [auth A] Focus chain D [auth A] Focus chain E [auth A] Focus chain F [auth A] Focus chain G [auth A] Focus chain H [auth A] Focus chain I [auth A] Focus chain J [auth A] Focus chain K [auth A] Focus chain L [auth A] Focus chain M [auth A] Focus chain N [auth A] Focus chain O [auth A] Focus chain P [auth A] Focus chain Q [auth A] Focus chain R [auth A] Focus chain S [auth A] Focus chain T [auth A] Focus chain U [auth A] Focus chain V [auth A]
EDO Query on EDO Download Ideal Coordinates CCD File SDF format, chain AA [auth A] SDF format, chain Z [auth A] MOL2 format, chain AA [auth A] MOL2 format, chain Z [auth A]	AA [auth A], Z [auth A]	1,2-ETHANEDIOL C₂ H₆ O₂ LYCAIKOWRPUZTN-UHFFFAOYSA-N		Interactions Focus chain AA [auth A] Focus chain Z [auth A] Interactions & Density Focus chain AA [auth A] Focus chain Z [auth A]
NA Query on NA Download Ideal Coordinates CCD File SDF format, chain W [auth A] SDF format, chain X [auth A] SDF format, chain Y [auth A] MOL2 format, chain W [auth A] MOL2 format, chain X [auth A] MOL2 format, chain Y [auth A]	W [auth A], X [auth A], Y [auth A]	SODIUM ION Na FKNQFGJONOIPTF-UHFFFAOYSA-N		Interactions Focus chain W [auth A] Focus chain X [auth A] Focus chain Y [auth A] Interactions & Density Focus chain W [auth A] Focus chain X [auth A] Focus chain Y [auth A]

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 1.37 Å
R-Value Free: 0.132
R-Value Work: 0.099
R-Value Observed: 0.101
Space Group: H 3 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 51.2	α = 90
b = 51.2	β = 90
c = 302.03	γ = 120

Software Package:

Software Name	Purpose
MAR345	data collection
SHELX	model building
PHENIX	refinement
XDS	data reduction
XDS	data scaling
SHELX	phasing

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2014-10-01

Deposition Author(s):

Sycheva, L.V.

Shneider, M.M.

Leiman, P.G.

Revision History (Full details and data files)

Version 1.0: 2014-10-01
Type: Initial release
Version 1.1: 2017-11-15
Changes: Refinement description
Version 1.2: 2019-02-06
Changes: Data collection, Database references
Version 1.3: 2024-02-28
Changes: Data collection, Database references, Derived calculations