April, The energy functions include:

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REDUX A collection of Python scripts for torsion angle Monte Carlo protein molecular simulations and analysis The program is based on unified residue peptide model and is designed for more efficient exploration of conformational space compared to all atom peptide models Creation of REDUX was partially motivated by the publication of an efficient Cα-only local move algorithm in Python by Wouter Boomsma and Thomas Hamelryck, BMC Bioinformatics 2005, 6:159 The REDUX moveset includes a pivot move (around a single residue ϕ, ψ) and for each successful pivot move a user defined number of local fragment moves The local move needs 10 sequential residues to work with: first 3 are static anchor, middle 4 change, and last 3 move en bloc to defined rmsd with their pre-move positions This was designed to allow some flexibility in the pivoting arm to avoid VDW clash as the long arm moves The model includes a Cα atom, a single pseudo atom side chain with radius proportional to side chain size, and a backbone psuedo hydrogen bond site (of zero radius) between each pair of Cα atoms (See Model below) The pivot moveset is based on single residue ϕ, ψ distributions in a PDB-derived coil library converted to α, τ values REDUX includes a mapping of binned α, τ angle ranges into labeled mesostates for internal use (See Movesets below) The ability to use a probability mesostate file as a moveset was also included in order to use probability mesostates derived from NMR data (Here the mesostates are in α, τ space) The energy functions include: 1 soft debump (V = Eps,i,j[(Sigma,i,j/ri,j)**12], see soft_debump_score in Functionspy) 2 residue specific pairwise contact (PDB derived, see below and contact_score in Functionspy) 3 confinement (Rg target, see rg_confinement_score in Functionspy) 4 hydrogen bond (distance and angle criteria These were developed by converting a list of native PDB structures to the Ca reduced model and obtaining statistics on the distances and angle between respective backbone pseudo h-bond sites See Functionspy hbond_score for details) 5 backbone mesostate distributions (agreement with PDB derived, see meso_state_score in Functionspy) Current version is 21 available as a tarball, REDUX_2_1targz To install, tar xzf REDUX_2_1targz and then cd redux/redux_2_1 python setuppy install (using python version 2x with appropriate write privileges) REDUX requires Numeric and Biopython to be installed in the python distribution 1

Model Below is an image of the model of all 20 residue types in alphabetical order, from ALA in the lower left, to VAL in the upper right The white atoms are the hydrogen bonding sites which have a defined radius of zero in the program (Here all atoms are default pymol size for carbon or hydrogen The Cα Csidechain bond length is variable depending on the defined size of the side chain pseudo atom [see below]) The defined side chain pseudo atom radii are (this is cut from vdwradpy explained later): cmdalter('resn ala and name cb','vdw=20') cmdalter('resn arg and name cb','vdw=36') cmdalter('resn asn and name cb','vdw=27') cmdalter('resn asp and name cb','vdw=27') cmdalter('resn cys and name cb','vdw=26') cmdalter('resn gln and name cb','vdw=34') cmdalter('resn glu and name cb','vdw=34') cmdalter('resn his and name cb','vdw=32') cmdalter('resn ile and name cb','vdw=33') cmdalter('resn leu and name cb','vdw=33') cmdalter('resn lys and name cb','vdw=36') cmdalter('resn met and name cb','vdw=33') cmdalter('resn phe and name cb','vdw=35') cmdalter('resn pro and name cb','vdw=28') cmdalter('resn ser and name cb','vdw=24') cmdalter('resn thr and name cb','vdw=28') cmdalter('resn trp and name cb','vdw=42') cmdalter('resn tyr and name cb','vdw=37') cmdalter('resn val and name cb','vdw=30') cmdalter('name ca', 'vdw = 28') cmdalter('name hb', 'vdw = 00') These radii were chosen by trial and error to make the pseudo atom representing the sidechain approximately cover the actual all atom side chain when it was in its most ususal rotamer, ie the pseudo atom would accupy approximately the same volume as the actual side chain Here is an example of the REDUX model in surface rendering over the all heavy atom representation: 2

This is also illustrated in the following sequence of images: April, 2015 Movesets The movesets are attempts to sample a single α, τ angle pair The α, τ angles are defined below (note that each α, τ pair describes the relationship of 4 Cα atoms and the respective Cβ atoms of the central pair of Cα atoms): The α, τ space was split into bins and each bin is labeled as a specific mesostate for use within REDUX, 3

The overall coil library distribution of α, τ angles, as fractional incidence, is illustrated below as a mesostate plot Also indicated are the regions that correspond to helix (H), PII (P), strand (E), and turn type 1 (O) 4

Each attempted pivot move is chosen from the specific residue type α, τ probability mesostate distributions illustrated next: 5

Components of REDUX April, 2015 AlfTau2Mesopy Utility to convert list of α, τ angles to new mesotates Build_peptpy Build model from sequence file ContactEnergiespy Dictionary of Residue contact energies from the PDB Functionspy Common functions used in REDUX MesoDictpy Dictionary of α, τ mesostate definitions MesoTypespy Dictionary of mesostate indices Mk_camatrix_filelistpy Makes a data list of Cα distance vectors for input to Pycluster Mk_resi_pmeso_wtpy Makes a residue probability mesostate file from a native PDB file Residue mesostate probabilities will be 10 for the mesostate of the native structure This pmeso file can be used to set the choice of mesostates during simulation to the same as the native PDB file Mk_resi_pmeso_wt_GLYpy As above but if residue is GLY the probabilities are set to the PDB distribution of GLY alf-tau values PDB2seqpy Makes a sequence file in format for input to Build_peptpy PDBiopy, PDBio_PDBpy Functions for reading PDB files The first is to read REDUX files, the second is to read native PDB files These are imported by the approriate scripts as needed Pmeso_Weightspy Contains data for residue specific alf-tau mesotate probabilities Reduxpy Main command or run file for REDUX Redux_energiespy, Redux_energies_PDBpy 6

Calculates REDUX energies for structures First is for REDUX PDB files, second if for native PDB files Redux_from_PDBpy Convert a native PDB structure to a REDUX reduced model structure with same Capha postions Redux_from_Seq_Angpy Build model from list of residues and phi, psi angles Redux_meso_run1py, Redux_meso_run2py Command or run files to run a REDUX simulation using a probability mesostate file These are the same file with different parameters and options Torsionpy Calculates torsion angles α, τ for Cα model of protein Zmatrixdat Description of REDUX reduced model new_clusterpy Cluster by structure using Pycluster vdwradpy List of atom radii to read into Pymol for display of REDUX models 7

Running a simulation with REDUX April, 2015 Note: For the following commands you must have set an environmental value to define the path where REDUX_2_1 resides Eg setenv REDUX '/usr/local/lib/python24/site-packages/redux_2_1' You may start with the sequence of the polypeptide in a special format This can be created with an editor or obtained from a standard PDB file with the following type of command, python $REDUX/PDB2seqpy pdb1pgbcln > b1seq (the suffix cln just indicates that this PDB file contains only ATOM records, only one chain, only one of any alternate conformations, etc) and where the sequence file has the following format, % head b1seq DEFAULT ALF 1270 DEFAULT TAU -1650 RES END RES MET RES THR RES TYR RES LYS RES LEU RES ILE RES LEU % tail b1seq RES ALA RES THR RES LYS RES THR RES PHE RES THR RES VAL RES THR RES GLU RES END The first two lines define the default α, τ angles for the model; these can be edited to your choice The capping residues called END are necessary Then create the REDUX model, python $REDUX/Build_peptpy b1seq > b1_reduxpdb where b1_reduxpdb is now of the form, 8

% head b1_reduxpdb COMPND ATOM 0 CA END 0 1000 1000 1000 100 000 ATOM 1 CA MET 1 4800 1000 1000 100 000 ATOM 2 CB MET 1 6139-1661 1355 100 000 ATOM 3 HB MET 1 5943 2517 1000 100 000 ATOM 4 CA THR 2 7087 4035 1000 100 000 ATOM 5 CB THR 2 6471 5281 1161 100 000 ATOM 6 HB THR 2 8946 4066 0607 100 000 ATOM 7 CA TYR 3 10804 4097 0215 100 000 ATOM 8 CB TYR 3 12198 1118-0982 100 000 % tail b1_reduxpdb ATOM 157 CB VAL 54 163885 84377-10226 100 000 ATOM 158 HB VAL 54 166678 82665-9751 100 000 ATOM 159 CA THR 55 168576 82659-9818 100 000 ATOM 160 CB THR 55 169199 81406-9761 100 000 ATOM 161 HB THR 55 169728 84169-9752 100 000 ATOM 162 CA GLU 56 170879 85678-9686 100 000 ATOM 163 CB GLU 56 169544 88412-9089 100 000 ATOM 164 HB GLU 56 172724 85731-10140 100 000 ATOM 165 CA END 57 174568 85783-10595 100 000 END April, 2015 Note that both the N-terminus and C-terminus are capped with a residue called END which contains only a Cα atom To visualize the reduced residue structure in PyMOL get a copy of the atom radii, cp $REDUX/vdwradpy Then, after loading b1_reduxpdb into PyMOL run the radii script, PyMOL> @vdwradpy (and then show spheres) To run a torsion angle MC simulation get a copy of the command file, cp $REDUX/Reduxpy and edit the following section appropriately, ####### EDIT THESE IF DESIRED ######### # How large should the confinement cage be (28 is normal, 25 is small, 35 is big) # The cage will gradually shrink to the end size start_rg_prefac = 30 end_rg_prefac = 30 Rg_predict = start_rg_prefac * (mathpow(numres, 034)) # Scale the various scoring functions # Set to 00 to turn off that function # # Confinement rgscale = 01 # 01 default # # Soft Debump dbscale = 10 # 10 default # # Residue Specific Contact cnscale = 10 # 10 default # # Hydrogen bond hbscale = 10 # 10 default # # Backbone Mesostate Propensity msscale = 10 # 10 default 9

# How many cycles: where a cycle is numres attempts to get a successful pivot move? ncycles = 100 # Save a frame every how many cycles of pivot moves: save_int = 1 # How many local move attempts for each successful pivot move? l_trials = 1 ######## END EDIT ############ Then run the simulation with a command similar to the following, python Reduxpy b1_reduxpdb The output should be in a directory called sim/ % ls sim/ b1_reduxpdb minpdb trajpdb where b1_reduxpdb is the initial extended model, minpdb is the minimum energy conformation sampled during the simulation and trajpdb contains multiple conformations saved during the simulation The trajpdb is in the format of NMR multiple PDB files and can be loaded directly into PyMOL for viewing as a movie This allows one to see the difference between a pivot move and a local move To collect minimal energy conformers from multiple independent simulations the following lines can be inserted into Reduxpy instead of the simple run_sim(file) command, for i in range(400): run_sim(file) osrename('minpdb', 'emin_' + `i` + 'pdb') 10

Utility scripts April, 2015 To calculate the α, τ angles and associated mesostates from a PDB file: python $REDUX/Torsionpy pdb1pgbcln > pdb1pgbang where pdb1pgbang looks like the following, % head pdb1pgbang 3 TYR LYS 12628-17463 Ea 4 LYS LEU 13283-14626 Eb 5 LEU ILE 12241-15652 Da 6 ILE LEU 10970-15718 Ca 7 LEU ASN 11694-15574 Da 8 ASN GLY 10129 16870 Bl 9 GLY LYS 12778 14811 Ek 10 LYS THR 9001-10539 Ac 11 THR LEU 10897 1387 Cg 12 LEU LYS 11907 5523 Dh To calculate the REDUX energies of a conformation: From a REDUX model structure, % cp $REDUX/Redux_energiespy % python Redux_energiespy minpdb debump 0251166874474 confine 0764243831542 contact -397808618667 meso -23057013828 hbond -00 From a native PDB file, % cp $REDUX/ Redux_energies_PDBpy % python Redux_energies_PDBpy pdb1pgbcln debump 245157211148 confine 00 contact -746524261987 meso -157870798552 hbond -110 11