6csn : EncoMPASS

6csn
General information about the complete biological unit of each membrane protein structure.

The orientation in the lipid bilayer is either taken directly from OPM or generated using the related routine PPM; the title is taken from the OPM database. However, the structure shown may be modified from the coordinate file retrievable from OPM or the PDB, because of inconsistencies with the definition of the biological unit. The coordinate file is downloadable, as is a PyMOL script for visualizing the structure.

Light-gated anion channel iC++

Number of Chains: 2
Number of TM Chains: 2
Amino Acids: 562
Method: X-RAY DIFFRACTION
Resolution: 2.9 Å
Uniprot:
Links: PDB      OPM      PDBTM 
Coordinates The structure shown may be modified from the coordinate file retrievable from OPM or from the PDB because of inconsistencies with the definition of the biological unit.

Structure Relationships
A list of chains contained in the biological unit and their relationships to other structures in the database.

Details include: (i) the predominant secondary structure (alpha or beta), (ii) the number of transmembrane regions according to our algorithm, and (iii-v) the number of neighbors according to comparisons using sequence (iii), structure (iv), or both (v).

Two chains are designated sequence neighbors when the sequence identity in the MUSCLE alignment is ≥0.85. Two chains are assigned as structural neighbors when the Fr-TM-Align structure alignment led to a TM-score of ≥0.6.

Member Class TM Domains Seq Neighbors Struct Neighbors All Neighbors Symmetry
6csn_A alpha 7 19 740 740 na
6csn_B alpha 7 19 740 740 C3
    Symmetry analysis has been carried out for this structure, using two different strategies named "Standard Symmetry Detection" and "Multi-step Symmetry Detection". See section titles for details.

Standard Symmetry Detection
Raw output from two symmetry detection programs: CE-Symm and SymD.

Structures were processed using CE-Symm and SymD with default options. For CE-Symm, if no symmetry was detected (reported as Order = C1), no image is provided. When symmetry is detected, different colors are used to represent the repeated elements with respect to a given symmetry axis and the PyMOL script for generating the representations is provided. [Note that CE-Symm calculations were carried out with a random seed of 3, 5, or 10, from which the result with the highest number of repeats and/or highest number of aligned residues is reported.]

For SymD, which does not report repeats information, the aligned residues (capital letters in the FASTA files) are colored blue and the accompanying PyMOL script generates this representation. [Note that SymD does not report symmetry order and so here, the order has been predicted based on the unit angle provided by the program.]

To interpret the repeat definitions, see the FAQ.

CE-Symm   2.2

Order: C2
Angle: 180.00
Translation: 0.00
RMSD: 0.0
TM-Score: 1.0
Coverage: 1.0
See additional CE-Symm data
View alignment(s)

SymD   1.6

Order: 2
Angle: 180.0
Translation: 0.0
RMSD: 0.002
TM-Score: 1.0
Coverage: 1.0
See additional SymD data
View alignment(s)

Multi-step Symmetry Detection
Consensus results from processing with SymD, CE-Symm and QuatSymm with default and customized parameters

These results were filtered using rules that take into account the restraints imposed by the membrane environment (e.g., an alpha-helical repeat should contain at least two transmembrane spans to be functionally relevant) and that consider coverage and symmetry levels. Only symmetries between repeats that are at least partially located in the membrane are considered. Note that for multi-chain complexes the order of the chains is important for symmetry detection and is therefore also reported.

Chain Order: A;B;
Order: C2
Angle: 180.0
Translation: 0.0
RMSD: 0.0
TM-Score: 1.0
Coverage: 1.0
Aligned Residues: 562
Number of Repeats: 2
Repeat Length: 281
Levels: 1
Topology: Parallel
Angle with Membrane Normal: -89.97999999999999
Repeats:
View alignment(s)